HEADER    MEMBRANE PROTEIN                        04-AUG-20   7JNI              
TITLE     CRYSTAL STRUCTURE OF THE ANGIOTENSIN II TYPE 2 RECEPTOROR (AT2R) IN   
TITLE    2 COMPLEX WITH EMA401                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOLUBLE CYTOCHROME B562,TYPE-2 ANGIOTENSIN II RECEPTOR;    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYTOCHROME B-562,ANGIOTENSIN II TYPE-2 RECEPTOR,AT2;        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 562, 9606;                                           
SOURCE   5 GENE: CYBC, AGTR2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    ANGIOTENSIN II TYPE 2 RECEPTOR, AT2R, EMA401, PD-126055, G PROTEIN-   
KEYWDS   2 COUPLED RECEPTOR, GPCR, BRIL FUSION, GLIOBLASTOMA, GBM, MEMBRANE     
KEYWDS   3 PROTEIN, LCP                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.CHEREZOV,H.SHAYE,G.W.HAN                                            
REVDAT   2   24-AUG-22 7JNI    1       JRNL                                     
REVDAT   1   09-FEB-22 7JNI    0                                                
JRNL        AUTH   R.PERRYMAN,A.RENZIEHAUSEN,H.SHAYE,A.D.KOSTAGIANNI,           
JRNL        AUTH 2 A.D.TSIAILANIS,T.THORNE,M.V.CHATZIATHANASIADOU,              
JRNL        AUTH 3 G.B.SIVOLAPENKO,M.A.EL MUBARAK,G.W.HAN,B.ZARZYCKA,           
JRNL        AUTH 4 V.KATRITCH,G.LEBON,C.LO NIGRO,L.LATTANZIO,S.V.MORSE,         
JRNL        AUTH 5 J.J.CHOI,K.O'NEILL,Z.KANAKI,A.KLINAKIS,T.CROOK,V.CHEREZOV,   
JRNL        AUTH 6 A.G.TZAKOS,N.SYED                                            
JRNL        TITL   INHIBITION OF THE ANGIOTENSIN II TYPE 2 RECEPTOR AT 2 R IS A 
JRNL        TITL 2 NOVEL THERAPEUTIC STRATEGY FOR GLIOBLASTOMA.                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 119 89119 2022              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   35917342                                                     
JRNL        DOI    10.1073/PNAS.2116289119                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18.2_3874                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 17830                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.830                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 862                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 32.7200 -  5.4300    0.97     2894   143  0.2113 0.2601        
REMARK   3     2  5.4300 -  4.3100    0.98     2863   134  0.2129 0.2303        
REMARK   3     3  4.3100 -  3.7700    0.98     2868   149  0.2265 0.2499        
REMARK   3     4  3.7700 -  3.4300    0.98     2836   141  0.2536 0.3152        
REMARK   3     5  3.4300 -  3.1800    0.99     2868   152  0.2900 0.3496        
REMARK   3     6  3.1800 -  3.0000    0.92     2639   143  0.3315 0.3498        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.170           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 96.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           6728                                  
REMARK   3   ANGLE     :  0.551           9106                                  
REMARK   3   CHIRALITY :  0.038           1023                                  
REMARK   3   PLANARITY :  0.003           1127                                  
REMARK   3   DIHEDRAL  : 17.581           2403                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 147 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8781 -12.2747   8.9229              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5666 T22:   0.3930                                     
REMARK   3      T33:   0.5366 T12:   0.0320                                     
REMARK   3      T13:   0.0158 T23:  -0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1016 L22:   2.3927                                     
REMARK   3      L33:   3.1963 L12:  -0.2763                                     
REMARK   3      L13:  -0.3025 L23:  -0.2775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1656 S12:  -0.3661 S13:   0.0094                       
REMARK   3      S21:   0.1598 S22:  -0.0797 S23:  -0.0149                       
REMARK   3      S31:   0.2376 S32:   0.0704 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 174 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  49.2338  -0.9940  21.2639              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7497 T22:   1.2529                                     
REMARK   3      T33:   1.1567 T12:  -0.0358                                     
REMARK   3      T13:  -0.0671 T23:  -0.3314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5092 L22:   0.9180                                     
REMARK   3      L33:   0.5578 L12:  -0.1671                                     
REMARK   3      L13:   0.1819 L23:   0.7154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5271 S12:  -1.2794 S13:   2.3592                       
REMARK   3      S21:   0.1538 S22:   0.4556 S23:  -1.3375                       
REMARK   3      S31:  -0.4612 S32:   0.8598 S33:  -0.0187                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 220 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0542   1.8735   8.2723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6011 T22:   0.5878                                     
REMARK   3      T33:   0.7275 T12:   0.0336                                     
REMARK   3      T13:  -0.0308 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0497 L22:   2.3179                                     
REMARK   3      L33:   2.0420 L12:   0.4106                                     
REMARK   3      L13:  -0.4261 L23:  -0.1143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0950 S12:   0.0149 S13:  -0.0081                       
REMARK   3      S21:   0.2132 S22:   0.3369 S23:   0.3358                       
REMARK   3      S31:   0.1713 S32:  -0.3603 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 221 THROUGH 318 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  42.9846  -1.2611  -1.2850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5908 T22:   0.3881                                     
REMARK   3      T33:   0.5986 T12:   0.0298                                     
REMARK   3      T13:   0.0406 T23:   0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8987 L22:   2.3653                                     
REMARK   3      L33:   1.9230 L12:   0.2957                                     
REMARK   3      L13:   0.3733 L23:  -0.4699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1753 S12:   0.2356 S13:   0.1182                       
REMARK   3      S21:  -0.2920 S22:  -0.1301 S23:  -0.4421                       
REMARK   3      S31:   0.0185 S32:   0.2521 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 334 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  61.6364 -10.9523   7.8396              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8732 T22:   1.2018                                     
REMARK   3      T33:   1.2343 T12:  -0.0454                                     
REMARK   3      T13:  -0.1003 T23:   0.1512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1488 L22:   0.1607                                     
REMARK   3      L33:   0.0178 L12:   0.0665                                     
REMARK   3      L13:  -0.0077 L23:   0.0859                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3691 S12:  -0.8530 S13:   0.9214                       
REMARK   3      S21:   0.5842 S22:  -0.0280 S23:  -0.9465                       
REMARK   3      S31:  -0.2207 S32:   1.5353 S33:   0.0093                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 42 THROUGH 147 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4746 -27.9117  33.7194              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8157 T22:   1.1299                                     
REMARK   3      T33:   0.8358 T12:   0.1733                                     
REMARK   3      T13:   0.1117 T23:   0.3622                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1910 L22:   1.4299                                     
REMARK   3      L33:   3.0267 L12:  -0.3289                                     
REMARK   3      L13:  -1.6041 L23:   0.0351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3189 S12:  -1.1418 S13:  -0.5382                       
REMARK   3      S21:   0.3830 S22:   0.5718 S23:   0.3720                       
REMARK   3      S31:   0.5331 S32:   0.0052 S33:  -0.0013                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 148 THROUGH 174 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3626 -20.1688  17.4394              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7310 T22:   0.8103                                     
REMARK   3      T33:   0.9517 T12:   0.0307                                     
REMARK   3      T13:  -0.0464 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2255 L22:   1.5505                                     
REMARK   3      L33:   1.3839 L12:   0.2364                                     
REMARK   3      L13:  -0.5673 L23:  -0.5341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8369 S12:  -0.5045 S13:   0.5245                       
REMARK   3      S21:  -0.5983 S22:   0.1028 S23:   0.8374                       
REMARK   3      S31:  -0.3545 S32:  -0.4309 S33:  -0.0008                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 175 THROUGH 220 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.8784 -16.9868  32.0881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7550 T22:   1.6640                                     
REMARK   3      T33:   0.6780 T12:   0.1203                                     
REMARK   3      T13:  -0.0689 T23:   0.1328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1742 L22:   0.6969                                     
REMARK   3      L33:   1.1560 L12:   0.1330                                     
REMARK   3      L13:   0.6046 L23:   0.0392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1958 S12:  -1.2759 S13:  -0.1872                       
REMARK   3      S21:   0.5799 S22:   0.0012 S23:   0.0412                       
REMARK   3      S31:   0.8319 S32:  -0.1419 S33:  -0.0041                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 221 THROUGH 318 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1182 -12.3308  38.5052              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7710 T22:   1.5894                                     
REMARK   3      T33:   0.5200 T12:   0.3086                                     
REMARK   3      T13:   0.1025 T23:   0.0873                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5877 L22:   3.8126                                     
REMARK   3      L33:   2.4569 L12:  -0.2278                                     
REMARK   3      L13:  -1.1122 L23:   0.2859                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4406 S12:  -1.4582 S13:  -0.4962                       
REMARK   3      S21:   0.5245 S22:   0.5585 S23:   0.3875                       
REMARK   3      S31:   0.1066 S32:   0.4765 S33:  -0.0218                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 319 THROUGH 333 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5718 -21.1946  31.7792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0438 T22:   1.2319                                     
REMARK   3      T33:   1.4726 T12:  -0.0431                                     
REMARK   3      T13:   0.1842 T23:   0.1167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0889 L22:   0.0558                                     
REMARK   3      L33:   0.0249 L12:  -0.0735                                     
REMARK   3      L13:   0.0532 L23:  -0.0250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2584 S12:  -0.3817 S13:   0.0006                       
REMARK   3      S21:  -0.7332 S22:  -0.5812 S23:   0.6245                       
REMARK   3      S31:   0.2732 S32:   0.7443 S33:  -0.0001                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1048 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2885  18.3611   6.2067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7473 T22:   0.7136                                     
REMARK   3      T33:   0.9842 T12:  -0.0037                                     
REMARK   3      T13:   0.0024 T23:   0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3947 L22:   3.3817                                     
REMARK   3      L33:   1.2222 L12:   1.2986                                     
REMARK   3      L13:   0.0611 L23:  -1.3207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1176 S12:   0.0402 S13:   0.4370                       
REMARK   3      S21:  -0.1910 S22:  -0.0723 S23:  -0.7067                       
REMARK   3      S31:  -0.2611 S32:   0.3050 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1049 THROUGH 1080 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1130  10.9933  -2.5340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7557 T22:   0.8903                                     
REMARK   3      T33:   0.8337 T12:   0.0983                                     
REMARK   3      T13:  -0.0810 T23:  -0.0984                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5330 L22:   2.2875                                     
REMARK   3      L33:   1.1524 L12:   0.8486                                     
REMARK   3      L13:   0.9502 L23:  -0.4369                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2408 S12:   0.7398 S13:  -0.8797                       
REMARK   3      S21:  -0.3187 S22:   0.0495 S23:   0.2360                       
REMARK   3      S31:   0.4544 S32:  -0.4250 S33:   0.0001                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1081 THROUGH 1106 AND RESID 900   
REMARK   3               THROUGH 903 AND RESID 35)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0939   8.3700   8.2597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7693 T22:   0.8757                                     
REMARK   3      T33:   0.9218 T12:   0.1580                                     
REMARK   3      T13:   0.1115 T23:   0.0801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6438 L22:   1.6575                                     
REMARK   3      L33:   0.7300 L12:   0.1431                                     
REMARK   3      L13:   0.6603 L23:   0.0392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0806 S12:  -0.3376 S13:   0.2905                       
REMARK   3      S21:   0.0577 S22:   0.0740 S23:  -0.7971                       
REMARK   3      S31:  -0.0571 S32:   0.2182 S33:   0.0001                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1001 THROUGH 1048 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  62.8759   7.1148  42.8845              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1019 T22:   1.4210                                     
REMARK   3      T33:   0.8476 T12:   0.0422                                     
REMARK   3      T13:   0.0992 T23:   0.1645                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5090 L22:   1.3427                                     
REMARK   3      L33:   0.6872 L12:  -0.0116                                     
REMARK   3      L13:   0.3864 L23:   0.7426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3545 S12:  -1.1439 S13:  -0.1816                       
REMARK   3      S21:   0.5630 S22:   0.2390 S23:   0.6726                       
REMARK   3      S31:  -0.8004 S32:  -1.4406 S33:  -0.0012                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1049 THROUGH 1080 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  68.5940  -3.3093  46.4174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1186 T22:   1.0712                                     
REMARK   3      T33:   1.2775 T12:  -0.0037                                     
REMARK   3      T13:  -0.0537 T23:   0.2276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4860 L22:   0.4060                                     
REMARK   3      L33:   0.4777 L12:  -0.0963                                     
REMARK   3      L13:   0.1170 L23:   0.4272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6428 S12:  -0.6725 S13:  -0.7878                       
REMARK   3      S21:  -0.0834 S22:  -0.3577 S23:  -0.5331                       
REMARK   3      S31:   1.4287 S32:   0.7772 S33:   0.0001                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1081 THROUGH 1106 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  61.1228  -0.6600  35.9140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9927 T22:   1.5072                                     
REMARK   3      T33:   0.8943 T12:  -0.1678                                     
REMARK   3      T13:  -0.0864 T23:   0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3129 L22:   1.6508                                     
REMARK   3      L33:   0.0464 L12:  -0.6176                                     
REMARK   3      L13:  -0.0749 L23:   0.2744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0938 S12:  -0.2621 S13:  -0.2228                       
REMARK   3      S21:   0.9618 S22:  -0.4611 S23:   0.2106                       
REMARK   3      S31:  -0.0475 S32:   0.0091 S33:   0.0073                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND ((RESID 42 THROUGH 43 AND      
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 44 OR (RESID 45         
REMARK   3                          THROUGH 46 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 47       
REMARK   3                          THROUGH 48 OR (RESID 49 AND (NAME N OR      
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 50 THROUGH 75 OR (RESID 76 AND     
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 77 THROUGH 152 OR       
REMARK   3                          (RESID 153 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 154 OR   
REMARK   3                          (RESID 155 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 156      
REMARK   3                          THROUGH 187 OR (RESID 188 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 189 THROUGH 240 OR (RESID 241      
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB )) OR RESID 242 THROUGH 243    
REMARK   3                          OR (RESID 244 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID     
REMARK   3                          245 OR (RESID 246 THROUGH 247 AND (NAME N   
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 248 OR (RESID 249 AND (NAME N   
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 250 THROUGH 266 OR (RESID 267   
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB OR NAME CG1 OR NAME CG2)) OR   
REMARK   3                          RESID 268 THROUGH 286 OR (RESID 287 AND     
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 288 THROUGH 297 OR      
REMARK   3                          (RESID 298 THROUGH 299 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 300 THROUGH 333))                  
REMARK   3     SELECTION          : (CHAIN B AND (RESID 42 THROUGH 246 OR       
REMARK   3                          (RESID 247 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 248      
REMARK   3                          THROUGH 255 OR (RESID 256 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB OR   
REMARK   3                          NAME CG )) OR RESID 257 THROUGH 333))       
REMARK   3     ATOM PAIRS NUMBER  : 2646                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN C AND (RESID 1001 THROUGH 1014 OR    
REMARK   3                          (RESID 1015 AND (NAME N OR NAME CA OR       
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID     
REMARK   3                          1016 THROUGH 1018 OR (RESID 1019 THROUGH    
REMARK   3                          1020 AND (NAME N OR NAME CA OR NAME C OR    
REMARK   3                          NAME O OR NAME CB )) OR RESID 1021          
REMARK   3                          THROUGH 1056 OR (RESID 1057 AND (NAME N     
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 1058 THROUGH 1091 OR (RESID     
REMARK   3                          1092 AND (NAME N OR NAME CA OR NAME C OR    
REMARK   3                          NAME O OR NAME CB )) OR RESID 1093          
REMARK   3                          THROUGH 1100 OR (RESID 1101 AND (NAME N     
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 1102 OR (RESID 1103 THROUGH     
REMARK   3                          1105 AND (NAME N OR NAME CA OR NAME C OR    
REMARK   3                          NAME O OR NAME CB )) OR RESID 1106))        
REMARK   3     SELECTION          : (CHAIN D AND (RESID 1001 THROUGH 1103 OR    
REMARK   3                          (RESID 1104 THROUGH 1105 AND (NAME N OR     
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 1106))                             
REMARK   3     ATOM PAIRS NUMBER  : 956                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7JNI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000250963.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17858                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.19000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.18000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB 5UNH                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL PH 8.0, POTASSIUM FORMATE,      
REMARK 280  PEG400, AND 1,6-HEXANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.04500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN        
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  1000                                                      
REMARK 465     SER A    36                                                      
REMARK 465     GLN A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     VAL A   335                                                      
REMARK 465     GLY B  1000                                                      
REMARK 465     GLY B   900                                                      
REMARK 465     SER B   901                                                      
REMARK 465     GLY B   902                                                      
REMARK 465     SER B   903                                                      
REMARK 465     CYS B    35                                                      
REMARK 465     SER B    36                                                      
REMARK 465     GLN B    37                                                      
REMARK 465     LYS B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     ARG B   334                                                      
REMARK 465     VAL B   335                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A1104    CG   CD   CE   NZ                                   
REMARK 470     ASN A 247    CG   OD1  ND2                                       
REMARK 470     LYS A 256    CD   CE   NZ                                        
REMARK 470     LYS B1015    CG   CD   CE   NZ                                   
REMARK 470     LYS B1019    CG   CD   CE   NZ                                   
REMARK 470     GLU B1057    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1092    CG   CD   OE1  OE2                                  
REMARK 470     TYR B1101    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B1103    CG   CD   OE1  NE2                                  
REMARK 470     TYR B1105    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B  42    CG   CD   CE   NZ                                   
REMARK 470     HIS B  43    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B  45    CG   OD1  OD2                                       
REMARK 470     ILE B  49    CG1  CG2  CD1                                       
REMARK 470     LYS B  76    CG   CD   CE   NZ                                   
REMARK 470     GLN B 153    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 188    CG   CD   OE1  OE2                                  
REMARK 470     THR B 241    OG1  CG2                                            
REMARK 470     TYR B 244    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 246    CG   CD   CE   NZ                                   
REMARK 470     ILE B 249    CG1  CG2  CD1                                       
REMARK 470     ILE B 267    CD1                                                 
REMARK 470     ILE B 287    CG1  CG2  CD1                                       
REMARK 470     LEU B 298    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A1042       32.91    -99.68                                   
REMARK 500    ASP A  41       34.21    -83.72                                   
REMARK 500    VAL A 119      -72.31    -70.97                                   
REMARK 500    PHE A 150       49.70    -83.87                                   
REMARK 500    PHE A 220      -61.20   -144.26                                   
REMARK 500    SER A 243       19.14   -141.43                                   
REMARK 500    TYR A 318      -67.74   -124.02                                   
REMARK 500    LYS B1019       74.37   -107.46                                   
REMARK 500    THR B1044       64.38     28.46                                   
REMARK 500    LYS B1083       74.67   -100.35                                   
REMARK 500    TYR B1105      -31.79   -130.88                                   
REMARK 500    PHE B  69      -73.71    -64.11                                   
REMARK 500    VAL B 119      -73.28    -70.52                                   
REMARK 500    ARG B 154      -12.47     77.92                                   
REMARK 500    ARG B 155     -158.99     58.86                                   
REMARK 500    PHE B 220      -63.39   -144.48                                   
REMARK 500    SER B 243       16.49   -150.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A 1201                                                       
REMARK 610     OLA A 1202                                                       
REMARK 610     OLA A 1203                                                       
DBREF  7JNI A 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  7JNI A   35   335  UNP    P50052   AGTR2_HUMAN     35    335             
DBREF  7JNI B 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  7JNI B  112   335  UNP    P50052   AGTR2_HUMAN     35    335             
SEQADV 7JNI GLY A 1000  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 7JNI TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 7JNI ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 7JNI LEU A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 7JNI GLY A  900  UNP  P0ABE7              LINKER                         
SEQADV 7JNI SER A  901  UNP  P0ABE7              LINKER                         
SEQADV 7JNI GLY A  902  UNP  P0ABE7              LINKER                         
SEQADV 7JNI SER A  903  UNP  P0ABE7              LINKER                         
SEQADV 7JNI GLY B 1000  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 7JNI TRP B 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 7JNI ILE B 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 7JNI LEU B 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 7JNI GLY B  108  UNP  P0ABE7              LINKER                         
SEQADV 7JNI SER B  109  UNP  P0ABE7              LINKER                         
SEQADV 7JNI GLY B  110  UNP  P0ABE7              LINKER                         
SEQADV 7JNI SER B  111  UNP  P0ABE7              LINKER                         
SEQRES   1 A  412  GLY ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP          
SEQRES   2 A  412  ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN          
SEQRES   3 A  412  VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU          
SEQRES   4 A  412  ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS          
SEQRES   5 A  412  SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY          
SEQRES   6 A  412  PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS          
SEQRES   7 A  412  LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA          
SEQRES   8 A  412  ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN          
SEQRES   9 A  412  LYS TYR LEU GLY SER GLY SER CYS SER GLN LYS PRO SER          
SEQRES  10 A  412  ASP LYS HIS LEU ASP ALA ILE PRO ILE LEU TYR TYR ILE          
SEQRES  11 A  412  ILE PHE VAL ILE GLY PHE LEU VAL ASN ILE VAL VAL VAL          
SEQRES  12 A  412  THR LEU PHE YCM CYS GLN LYS GLY PRO LYS LYS VAL SER          
SEQRES  13 A  412  SER ILE TYR ILE PHE ASN LEU ALA VAL ALA ASP LEU LEU          
SEQRES  14 A  412  LEU LEU ALA THR LEU PRO LEU TRP ALA THR TYR TYR SER          
SEQRES  15 A  412  TYR ARG TYR ASP TRP LEU PHE GLY PRO VAL MET CYS LYS          
SEQRES  16 A  412  VAL PHE GLY SER PHE LEU THR LEU ASN MET PHE ALA SER          
SEQRES  17 A  412  ILE PHE PHE ILE THR CYS MET SER VAL ASP ARG TYR GLN          
SEQRES  18 A  412  SER VAL ILE TYR PRO PHE LEU SER GLN ARG ARG ASN PRO          
SEQRES  19 A  412  TRP GLN ALA SER TYR ILE VAL PRO LEU VAL TRP CYS MET          
SEQRES  20 A  412  ALA CYS LEU SER SER LEU PRO THR PHE TYR PHE ARG ASP          
SEQRES  21 A  412  VAL ARG THR ILE GLU TYR LEU GLY VAL ASN ALA CYS ILE          
SEQRES  22 A  412  MET ALA PHE PRO PRO GLU LYS TYR ALA GLN TRP SER ALA          
SEQRES  23 A  412  GLY ILE ALA LEU MET LYS ASN ILE LEU GLY PHE ILE ILE          
SEQRES  24 A  412  PRO LEU ILE PHE ILE ALA THR CYS TYR PHE GLY ILE ARG          
SEQRES  25 A  412  LYS HIS LEU LEU LYS THR ASN SER TYR GLY LYS ASN ARG          
SEQRES  26 A  412  ILE THR ARG ASP GLN VAL LEU LYS MET ALA ALA ALA VAL          
SEQRES  27 A  412  VAL LEU ALA PHE ILE ILE CYS TRP LEU PRO PHE HIS VAL          
SEQRES  28 A  412  LEU THR PHE LEU ASP ALA LEU ALA TRP MET GLY VAL ILE          
SEQRES  29 A  412  ASN SER CYS GLU VAL ILE ALA VAL ILE ASP LEU ALA LEU          
SEQRES  30 A  412  PRO PHE ALA ILE LEU LEU GLY PHE THR ASN SER CYS VAL          
SEQRES  31 A  412  ASN PRO PHE LEU TYR YCM PHE VAL GLY ASN ARG PHE GLN          
SEQRES  32 A  412  GLN LYS LEU ARG SER VAL PHE ARG VAL                          
SEQRES   1 B  412  GLY ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP          
SEQRES   2 B  412  ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN          
SEQRES   3 B  412  VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU          
SEQRES   4 B  412  ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS          
SEQRES   5 B  412  SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY          
SEQRES   6 B  412  PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS          
SEQRES   7 B  412  LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA          
SEQRES   8 B  412  ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN          
SEQRES   9 B  412  LYS TYR LEU GLY SER GLY SER CYS SER GLN LYS PRO SER          
SEQRES  10 B  412  ASP LYS HIS LEU ASP ALA ILE PRO ILE LEU TYR TYR ILE          
SEQRES  11 B  412  ILE PHE VAL ILE GLY PHE LEU VAL ASN ILE VAL VAL VAL          
SEQRES  12 B  412  THR LEU PHE YCM CYS GLN LYS GLY PRO LYS LYS VAL SER          
SEQRES  13 B  412  SER ILE TYR ILE PHE ASN LEU ALA VAL ALA ASP LEU LEU          
SEQRES  14 B  412  LEU LEU ALA THR LEU PRO LEU TRP ALA THR TYR TYR SER          
SEQRES  15 B  412  TYR ARG TYR ASP TRP LEU PHE GLY PRO VAL MET CYS LYS          
SEQRES  16 B  412  VAL PHE GLY SER PHE LEU THR LEU ASN MET PHE ALA SER          
SEQRES  17 B  412  ILE PHE PHE ILE THR CYS MET SER VAL ASP ARG TYR GLN          
SEQRES  18 B  412  SER VAL ILE TYR PRO PHE LEU SER GLN ARG ARG ASN PRO          
SEQRES  19 B  412  TRP GLN ALA SER TYR ILE VAL PRO LEU VAL TRP CYS MET          
SEQRES  20 B  412  ALA CYS LEU SER SER LEU PRO THR PHE TYR PHE ARG ASP          
SEQRES  21 B  412  VAL ARG THR ILE GLU TYR LEU GLY VAL ASN ALA CYS ILE          
SEQRES  22 B  412  MET ALA PHE PRO PRO GLU LYS TYR ALA GLN TRP SER ALA          
SEQRES  23 B  412  GLY ILE ALA LEU MET LYS ASN ILE LEU GLY PHE ILE ILE          
SEQRES  24 B  412  PRO LEU ILE PHE ILE ALA THR CYS TYR PHE GLY ILE ARG          
SEQRES  25 B  412  LYS HIS LEU LEU LYS THR ASN SER TYR GLY LYS ASN ARG          
SEQRES  26 B  412  ILE THR ARG ASP GLN VAL LEU LYS MET ALA ALA ALA VAL          
SEQRES  27 B  412  VAL LEU ALA PHE ILE ILE CYS TRP LEU PRO PHE HIS VAL          
SEQRES  28 B  412  LEU THR PHE LEU ASP ALA LEU ALA TRP MET GLY VAL ILE          
SEQRES  29 B  412  ASN SER CYS GLU VAL ILE ALA VAL ILE ASP LEU ALA LEU          
SEQRES  30 B  412  PRO PHE ALA ILE LEU LEU GLY PHE THR ASN SER CYS VAL          
SEQRES  31 B  412  ASN PRO PHE LEU TYR YCM PHE VAL GLY ASN ARG PHE GLN          
SEQRES  32 B  412  GLN LYS LEU ARG SER VAL PHE ARG VAL                          
MODRES 7JNI YCM A   70  CYS  MODIFIED RESIDUE                                   
MODRES 7JNI YCM A  319  CYS  MODIFIED RESIDUE                                   
MODRES 7JNI YCM B   70  CYS  MODIFIED RESIDUE                                   
MODRES 7JNI YCM B  319  CYS  MODIFIED RESIDUE                                   
HET    YCM  A  70      10                                                       
HET    YCM  A 319      10                                                       
HET    YCM  B  70      10                                                       
HET    YCM  B 319      10                                                       
HET    VFD  A1900      38                                                       
HET    OLC  A1201      18                                                       
HET    OLA  A1202      16                                                       
HET    OLA  A1203      15                                                       
HET    OLC  A1204      25                                                       
HET    OLC  A1205      25                                                       
HET    OLA  A1206      20                                                       
HET    FMT  A1207       3                                                       
HET    HEZ  A1208       8                                                       
HET    VFD  B1900      38                                                       
HET    OLA  B1201      20                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     VFD OLODANRIGAN                                                      
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     OLA OLEIC ACID                                                       
HETNAM     FMT FORMIC ACID                                                      
HETNAM     HEZ HEXANE-1,6-DIOL                                                  
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     VFD EMA401; (3S)-5-(BENZYLOXY)-2-(DIPHENYLACETYL)-6-                 
HETSYN   2 VFD  METHOXY-1,2,3,4-TETRAHYDROISOQUINOLINE-3-CARBOXYLIC             
HETSYN   3 VFD  ACID                                                            
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   1  YCM    4(C5 H10 N2 O3 S)                                            
FORMUL   3  VFD    2(C32 H29 N O5)                                              
FORMUL   4  OLC    3(C21 H40 O4)                                                
FORMUL   5  OLA    4(C18 H34 O2)                                                
FORMUL  10  FMT    C H2 O2                                                      
FORMUL  11  HEZ    C6 H14 O2                                                    
FORMUL  14  HOH   *4(H2 O)                                                      
HELIX    1 AA1 ASP A 1002  LYS A 1019  1                                  18    
HELIX    2 AA2 ASN A 1022  LYS A 1042  1                                  21    
HELIX    3 AA3 PRO A 1045  GLU A 1049  5                                   5    
HELIX    4 AA4 SER A 1055  GLU A 1081  1                                  27    
HELIX    5 AA5 LYS A 1083  TYR A 1105  1                                  23    
HELIX    6 AA6 GLY A  900  CYS A   35  5                                   5    
HELIX    7 AA7 ASP A   45  GLN A   72  1                                  28    
HELIX    8 AA8 LYS A   77  ALA A   95  1                                  19    
HELIX    9 AA9 THR A   96  TYR A  106  1                                  11    
HELIX   10 AB1 GLY A  113  TYR A  148  1                                  36    
HELIX   11 AB2 PHE A  150  ARG A  155  1                                   6    
HELIX   12 AB3 TRP A  158  SER A  175  1                                  18    
HELIX   13 AB4 SER A  175  PHE A  181  1                                   7    
HELIX   14 AB5 PRO A  200  GLU A  202  5                                   3    
HELIX   15 AB6 LYS A  203  PHE A  220  1                                  18    
HELIX   16 AB7 PHE A  220  ASN A  242  1                                  23    
HELIX   17 AB8 TYR A  244  MET A  284  1                                  41    
HELIX   18 AB9 SER A  289  TYR A  318  1                                  30    
HELIX   19 AC1 VAL A  321  PHE A  333  1                                  13    
HELIX   20 AC2 ASP B 1002  LYS B 1019  1                                  18    
HELIX   21 AC3 ASN B 1022  GLN B 1041  1                                  20    
HELIX   22 AC4 PRO B 1045  GLU B 1049  5                                   5    
HELIX   23 AC5 SER B 1055  GLU B 1081  1                                  27    
HELIX   24 AC6 LYS B 1083  TYR B 1105  1                                  23    
HELIX   25 AC7 ASP B   45  GLN B   72  1                                  28    
HELIX   26 AC8 LYS B   77  ALA B   95  1                                  19    
HELIX   27 AC9 THR B   96  TYR B  106  1                                  11    
HELIX   28 AD1 GLY B  113  TYR B  148  1                                  36    
HELIX   29 AD2 ASN B  156  SER B  175  1                                  20    
HELIX   30 AD3 SER B  175  PHE B  181  1                                   7    
HELIX   31 AD4 PRO B  200  GLU B  202  5                                   3    
HELIX   32 AD5 LYS B  203  PHE B  220  1                                  18    
HELIX   33 AD6 PHE B  220  ASN B  242  1                                  23    
HELIX   34 AD7 LYS B  246  MET B  284  1                                  39    
HELIX   35 AD8 SER B  289  YCM B  319  1                                  31    
HELIX   36 AD9 VAL B  321  PHE B  333  1                                  13    
SHEET    1 AA1 2 ARG A 182  ILE A 187  0                                        
SHEET    2 AA1 2 VAL A 192  MET A 197 -1  O  VAL A 192   N  ILE A 187           
SHEET    1 AA2 2 ARG B 182  ILE B 187  0                                        
SHEET    2 AA2 2 VAL B 192  MET B 197 -1  O  VAL B 192   N  ILE B 187           
SSBOND   1 CYS A   35    CYS A  290                          1555   1555  2.04  
SSBOND   2 CYS A  117    CYS A  195                          1555   1555  2.03  
SSBOND   3 CYS B  117    CYS B  195                          1555   1555  2.03  
LINK         C   PHE A  69                 N   YCM A  70     1555   1555  1.33  
LINK         C   YCM A  70                 N   CYS A  71     1555   1555  1.33  
LINK         C   TYR A 318                 N   YCM A 319     1555   1555  1.33  
LINK         C   YCM A 319                 N   PHE A 320     1555   1555  1.33  
LINK         C   PHE B  69                 N   YCM B  70     1555   1555  1.33  
LINK         C   YCM B  70                 N   CYS B  71     1555   1555  1.33  
LINK         C   TYR B 318                 N   YCM B 319     1555   1555  1.33  
LINK         C   YCM B 319                 N   PHE B 320     1555   1555  1.33  
CRYST1   77.658   68.090   89.171  90.00 104.65  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012877  0.000000  0.003365        0.00000                         
SCALE2      0.000000  0.014686  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011591        0.00000                         
ATOM      1  N   ALA A1001       7.001  24.144  -1.224  1.00111.51           N  
ANISOU    1  N   ALA A1001    13313  12542  16512   -805    863   1166       N  
ATOM      2  CA  ALA A1001       6.127  23.971  -2.378  1.00113.17           C  
ANISOU    2  CA  ALA A1001    13762  12761  16476   -826    967   1212       C  
ATOM      3  C   ALA A1001       6.643  22.837  -3.261  1.00106.47           C  
ANISOU    3  C   ALA A1001    12957  11986  15512   -818   1272   1255       C  
ATOM      4  O   ALA A1001       6.334  22.770  -4.451  1.00108.05           O  
ANISOU    4  O   ALA A1001    13352  12177  15524   -891   1420   1332       O  
ATOM      5  CB  ALA A1001       6.031  25.267  -3.169  1.00124.85           C  
ANISOU    5  CB  ALA A1001    15318  14132  17989   -964    927   1337       C  
ATOM      6  N   ASP A1002       7.422  21.940  -2.660  1.00 99.62           N  
ANISOU    6  N   ASP A1002    11915  11178  14757   -734   1364   1205       N  
ATOM      7  CA  ASP A1002       8.042  20.823  -3.359  1.00 97.35           C  
ANISOU    7  CA  ASP A1002    11635  10939  14415   -703   1680   1233       C  
ATOM      8  C   ASP A1002       7.708  19.535  -2.620  1.00 94.51           C  
ANISOU    8  C   ASP A1002    11262  10664  13985   -558   1657   1109       C  
ATOM      9  O   ASP A1002       7.395  19.547  -1.427  1.00 94.18           O  
ANISOU    9  O   ASP A1002    11126  10648  14012   -491   1414   1020       O  
ATOM     10  CB  ASP A1002       9.566  21.001  -3.460  1.00 97.39           C  
ANISOU   10  CB  ASP A1002    11386  10911  14708   -748   1863   1341       C  
ATOM     11  CG  ASP A1002      10.241  19.868  -4.215  1.00 98.39           C  
ANISOU   11  CG  ASP A1002    11513  11063  14807   -706   2237   1370       C  
ATOM     12  OD1 ASP A1002      10.043  19.767  -5.445  1.00103.30           O  
ANISOU   12  OD1 ASP A1002    12362  11669  15220   -774   2466   1414       O  
ATOM     13  OD2 ASP A1002      10.970  19.078  -3.579  1.00 91.93           O  
ANISOU   13  OD2 ASP A1002    10479  10272  14178   -610   2305   1352       O  
ATOM     14  N   LEU A1003       7.796  18.413  -3.338  1.00 98.29           N  
ANISOU   14  N   LEU A1003    11850  11177  14320   -516   1921   1102       N  
ATOM     15  CA  LEU A1003       7.454  17.127  -2.738  1.00 99.00           C  
ANISOU   15  CA  LEU A1003    11947  11339  14331   -382   1911    991       C  
ATOM     16  C   LEU A1003       8.282  16.874  -1.484  1.00 97.75           C  
ANISOU   16  C   LEU A1003    11477  11201  14461   -305   1808    967       C  
ATOM     17  O   LEU A1003       7.744  16.496  -0.437  1.00 96.21           O  
ANISOU   17  O   LEU A1003    11252  11060  14244   -227   1588    870       O  
ATOM     18  CB  LEU A1003       7.654  16.000  -3.752  1.00100.84           C  
ANISOU   18  CB  LEU A1003    12334  11575  14406   -360   2252    996       C  
ATOM     19  CG  LEU A1003       7.185  14.620  -3.281  1.00 99.48           C  
ANISOU   19  CG  LEU A1003    12216  11465  14116   -230   2249    885       C  
ATOM     20  CD1 LEU A1003       6.579  13.837  -4.437  1.00105.31           C  
ANISOU   20  CD1 LEU A1003    13288  12196  14527   -259   2458    867       C  
ATOM     21  CD2 LEU A1003       8.315  13.829  -2.636  1.00101.71           C  
ANISOU   21  CD2 LEU A1003    12216  11751  14677   -126   2373    883       C  
ATOM     22  N   GLU A1004       9.598  17.077  -1.569  1.00 94.05           N  
ANISOU   22  N   GLU A1004    10774  10690  14271   -337   1958   1069       N  
ATOM     23  CA  GLU A1004      10.437  16.895  -0.390  1.00 91.69           C  
ANISOU   23  CA  GLU A1004    10168  10402  14270   -292   1828   1082       C  
ATOM     24  C   GLU A1004      10.086  17.910   0.687  1.00 90.38           C  
ANISOU   24  C   GLU A1004     9947  10228  14164   -346   1457   1043       C  
ATOM     25  O   GLU A1004      10.065  17.584   1.879  1.00 82.20           O  
ANISOU   25  O   GLU A1004     8801   9229  13203   -300   1243    980       O  
ATOM     26  CB  GLU A1004      11.909  17.028  -0.778  1.00 79.77           C  
ANISOU   26  CB  GLU A1004     8401   8835  13074   -333   2058   1233       C  
ATOM     27  CG  GLU A1004      12.892  16.702   0.333  1.00 80.55           C  
ANISOU   27  CG  GLU A1004     8158   8935  13514   -297   1942   1288       C  
ATOM     28  CD  GLU A1004      14.338  16.771  -0.134  1.00 96.60           C  
ANISOU   28  CD  GLU A1004     9913  10905  15887   -330   2197   1464       C  
ATOM     29  OE1 GLU A1004      14.572  17.197  -1.285  1.00101.64           O  
ANISOU   29  OE1 GLU A1004    10636  11499  16483   -391   2460   1533       O  
ATOM     30  OE2 GLU A1004      15.241  16.400   0.647  1.00 97.78           O  
ANISOU   30  OE2 GLU A1004     9754  11044  16352   -303   2134   1547       O  
ATOM     31  N   ASP A1005       9.804  19.149   0.281  1.00 98.14           N  
ANISOU   31  N   ASP A1005    11025  11153  15112   -451   1380   1078       N  
ATOM     32  CA  ASP A1005       9.400  20.179   1.229  1.00101.62           C  
ANISOU   32  CA  ASP A1005    11456  11560  15596   -503   1054   1027       C  
ATOM     33  C   ASP A1005       7.977  19.978   1.733  1.00 98.44           C  
ANISOU   33  C   ASP A1005    11257  11200  14944   -430    875    880       C  
ATOM     34  O   ASP A1005       7.678  20.321   2.883  1.00 91.78           O  
ANISOU   34  O   ASP A1005    10384  10352  14137   -425    625    794       O  
ATOM     35  CB  ASP A1005       9.550  21.554   0.583  1.00109.39           C  
ANISOU   35  CB  ASP A1005    12474  12449  16639   -633   1043   1120       C  
ATOM     36  CG  ASP A1005      10.990  21.878   0.257  1.00108.15           C  
ANISOU   36  CG  ASP A1005    12081  12246  16764   -717   1185   1276       C  
ATOM     37  OD1 ASP A1005      11.883  21.373   0.969  1.00 94.71           O  
ANISOU   37  OD1 ASP A1005    10141  10563  15281   -693   1166   1309       O  
ATOM     38  OD2 ASP A1005      11.228  22.623  -0.715  1.00110.48           O  
ANISOU   38  OD2 ASP A1005    12422  12484  17071   -814   1312   1381       O  
ATOM     39  N   ASN A1006       7.088  19.431   0.900  1.00107.21           N  
ANISOU   39  N   ASN A1006    12585  12348  15802   -384   1001    854       N  
ATOM     40  CA  ASN A1006       5.737  19.155   1.373  1.00103.40           C  
ANISOU   40  CA  ASN A1006    12270  11911  15108   -311    838    736       C  
ATOM     41  C   ASN A1006       5.723  18.060   2.429  1.00 86.30           C  
ANISOU   41  C   ASN A1006    10021   9830  12940   -207    763    639       C  
ATOM     42  O   ASN A1006       4.900  18.101   3.350  1.00 91.20           O  
ANISOU   42  O   ASN A1006    10691  10477  13483   -164    560    535       O  
ATOM     43  CB  ASN A1006       4.839  18.738   0.204  1.00106.40           C  
ANISOU   43  CB  ASN A1006    12896  12309  15223   -306    975    758       C  
ATOM     44  CG  ASN A1006       4.589  19.862  -0.785  1.00105.12           C  
ANISOU   44  CG  ASN A1006    12853  12061  15025   -420    993    857       C  
ATOM     45  OD1 ASN A1006       4.963  19.771  -1.953  1.00108.53           O  
ANISOU   45  OD1 ASN A1006    13369  12475  15391   -490   1208    952       O  
ATOM     46  ND2 ASN A1006       3.931  20.916  -0.328  1.00106.71           N  
ANISOU   46  ND2 ASN A1006    13077  12203  15264   -444    775    837       N  
ATOM     47  N   TRP A1007       6.620  17.080   2.319  1.00 85.78           N  
ANISOU   47  N   TRP A1007     9825   9799  12967   -167    932    677       N  
ATOM     48  CA  TRP A1007       6.694  16.030   3.327  1.00 81.13           C  
ANISOU   48  CA  TRP A1007     9139   9283  12403    -79    849    607       C  
ATOM     49  C   TRP A1007       7.351  16.507   4.614  1.00 80.24           C  
ANISOU   49  C   TRP A1007     8822   9155  12510   -124    621    602       C  
ATOM     50  O   TRP A1007       7.037  15.989   5.691  1.00 80.19           O  
ANISOU   50  O   TRP A1007     8795   9205  12467    -80    448    519       O  
ATOM     51  CB  TRP A1007       7.429  14.814   2.766  1.00 90.51           C  
ANISOU   51  CB  TRP A1007    10252  10492  13644    -15   1112    659       C  
ATOM     52  CG  TRP A1007       6.496  13.868   2.079  1.00 90.73           C  
ANISOU   52  CG  TRP A1007    10517  10564  13390     54   1239    601       C  
ATOM     53  CD1 TRP A1007       6.419  13.612   0.741  1.00 94.34           C  
ANISOU   53  CD1 TRP A1007    11147  10993  13705     35   1501    643       C  
ATOM     54  CD2 TRP A1007       5.484  13.068   2.701  1.00 92.72           C  
ANISOU   54  CD2 TRP A1007    10880  10894  13456    134   1099    496       C  
ATOM     55  NE1 TRP A1007       5.427  12.693   0.493  1.00 93.74           N  
ANISOU   55  NE1 TRP A1007    11288  10966  13364     92   1516    572       N  
ATOM     56  CE2 TRP A1007       4.838  12.344   1.679  1.00 90.33           C  
ANISOU   56  CE2 TRP A1007    10808  10603  12912    159   1272    487       C  
ATOM     57  CE3 TRP A1007       5.065  12.890   4.023  1.00 92.50           C  
ANISOU   57  CE3 TRP A1007    10789  10925  13431    175    845    414       C  
ATOM     58  CZ2 TRP A1007       3.796  11.455   1.939  1.00 90.61           C  
ANISOU   58  CZ2 TRP A1007    10992  10706  12730    226   1188    408       C  
ATOM     59  CZ3 TRP A1007       4.031  12.007   4.279  1.00 89.53           C  
ANISOU   59  CZ3 TRP A1007    10555  10622  12839    249    781    332       C  
ATOM     60  CH2 TRP A1007       3.408  11.301   3.242  1.00 90.97           C  
ANISOU   60  CH2 TRP A1007    10946  10814  12803    276    946    334       C  
ATOM     61  N   GLU A1008       8.253  17.488   4.532  1.00 76.74           N  
ANISOU   61  N   GLU A1008     8241   8634  12283   -227    606    696       N  
ATOM     62  CA  GLU A1008       8.826  18.047   5.751  1.00 81.44           C  
ANISOU   62  CA  GLU A1008     8679   9200  13064   -303    355    696       C  
ATOM     63  C   GLU A1008       7.802  18.886   6.502  1.00 87.05           C  
ANISOU   63  C   GLU A1008     9560   9887  13629   -331    116    567       C  
ATOM     64  O   GLU A1008       7.792  18.901   7.738  1.00 83.21           O  
ANISOU   64  O   GLU A1008     9043   9410  13162   -358   -106    496       O  
ATOM     65  CB  GLU A1008      10.055  18.892   5.414  1.00 84.83           C  
ANISOU   65  CB  GLU A1008     8919   9543  13769   -419    398    845       C  
ATOM     66  CG  GLU A1008      11.238  18.098   4.881  1.00 97.55           C  
ANISOU   66  CG  GLU A1008    10303  11162  15598   -392    633    987       C  
ATOM     67  CD  GLU A1008      12.418  18.981   4.508  1.00 91.94           C  
ANISOU   67  CD  GLU A1008     9394  10367  15172   -511    686   1153       C  
ATOM     68  OE1 GLU A1008      12.308  20.217   4.650  1.00 94.97           O  
ANISOU   68  OE1 GLU A1008     9831  10685  15569   -621    525   1153       O  
ATOM     69  OE2 GLU A1008      13.456  18.438   4.072  1.00 82.89           O  
ANISOU   69  OE2 GLU A1008     8032   9211  14250   -492    897   1287       O  
ATOM     70  N   THR A1009       6.934  19.590   5.774  1.00 98.24           N  
ANISOU   70  N   THR A1009    11162  11263  14903   -331    162    541       N  
ATOM     71  CA  THR A1009       5.852  20.322   6.422  1.00 84.05           C  
ANISOU   71  CA  THR A1009     9526   9429  12982   -331    -24    419       C  
ATOM     72  C   THR A1009       4.888  19.365   7.115  1.00 81.06           C  
ANISOU   72  C   THR A1009     9244   9147  12409   -224    -86    295       C  
ATOM     73  O   THR A1009       4.391  19.652   8.210  1.00 80.51           O  
ANISOU   73  O   THR A1009     9229   9067  12292   -228   -266    181       O  
ATOM     74  CB  THR A1009       5.113  21.180   5.396  1.00102.76           C  
ANISOU   74  CB  THR A1009    12049  11728  15268   -346     48    450       C  
ATOM     75  OG1 THR A1009       6.023  22.121   4.814  1.00113.42           O  
ANISOU   75  OG1 THR A1009    13310  12986  16800   -458     93    569       O  
ATOM     76  CG2 THR A1009       3.988  21.959   6.064  1.00 99.60           C  
ANISOU   76  CG2 THR A1009    11792  11267  14784   -329   -121    333       C  
ATOM     77  N   LEU A1010       4.610  18.221   6.486  1.00 79.76           N  
ANISOU   77  N   LEU A1010     9113   9070  12122   -135     69    313       N  
ATOM     78  CA  LEU A1010       3.718  17.230   7.080  1.00 73.58           C  
ANISOU   78  CA  LEU A1010     8415   8384  11159    -37     15    213       C  
ATOM     79  C   LEU A1010       4.325  16.618   8.336  1.00 77.67           C  
ANISOU   79  C   LEU A1010     8798   8953  11759    -43   -122    172       C  
ATOM     80  O   LEU A1010       3.714  16.643   9.412  1.00 75.29           O  
ANISOU   80  O   LEU A1010     8560   8677  11369    -36   -291     63       O  
ATOM     81  CB  LEU A1010       3.400  16.141   6.053  1.00 67.50           C  
ANISOU   81  CB  LEU A1010     7720   7678  10248     39    212    254       C  
ATOM     82  CG  LEU A1010       2.336  16.481   5.010  1.00 67.44           C  
ANISOU   82  CG  LEU A1010     7911   7647  10066     47    284    275       C  
ATOM     83  CD1 LEU A1010       2.419  15.532   3.826  1.00 68.22           C  
ANISOU   83  CD1 LEU A1010     8089   7779  10052     70    504    343       C  
ATOM     84  CD2 LEU A1010       0.951  16.429   5.635  1.00 71.43           C  
ANISOU   84  CD2 LEU A1010     8542   8189  10411    109    139    180       C  
ATOM     85  N   ASN A1011       5.531  16.057   8.220  1.00 80.70           N  
ANISOU   85  N   ASN A1011     8994   9347  12321    -61    -49    270       N  
ATOM     86  CA  ASN A1011       6.150  15.393   9.360  1.00 80.81           C  
ANISOU   86  CA  ASN A1011     8863   9407  12434    -77   -194    266       C  
ATOM     87  C   ASN A1011       6.517  16.368  10.469  1.00 79.14           C  
ANISOU   87  C   ASN A1011     8613   9135  12321   -204   -439    237       C  
ATOM     88  O   ASN A1011       6.669  15.948  11.621  1.00 83.80           O  
ANISOU   88  O   ASN A1011     9163   9766  12913   -240   -622    200       O  
ATOM     89  CB  ASN A1011       7.392  14.622   8.912  1.00 86.74           C  
ANISOU   89  CB  ASN A1011     9394  10160  13405    -64    -47    405       C  
ATOM     90  CG  ASN A1011       7.056  13.458   8.001  1.00 84.82           C  
ANISOU   90  CG  ASN A1011     9213   9968  13046     59    192    410       C  
ATOM     91  OD1 ASN A1011       6.672  12.382   8.463  1.00 80.08           O  
ANISOU   91  OD1 ASN A1011     8637   9442  12350    135    157    360       O  
ATOM     92  ND2 ASN A1011       7.202  13.666   6.698  1.00 87.44           N  
ANISOU   92  ND2 ASN A1011     9593  10256  13377     68    434    472       N  
ATOM     93  N   ASP A1012       6.662  17.655  10.153  1.00 88.06           N  
ANISOU   93  N   ASP A1012     9772  10163  13523   -287   -455    256       N  
ATOM     94  CA  ASP A1012       6.874  18.651  11.196  1.00 87.75           C  
ANISOU   94  CA  ASP A1012     9752  10046  13541   -417   -689    205       C  
ATOM     95  C   ASP A1012       5.578  18.964  11.933  1.00 87.66           C  
ANISOU   95  C   ASP A1012     9971  10036  13301   -386   -793     27       C  
ATOM     96  O   ASP A1012       5.585  19.147  13.155  1.00 87.84           O  
ANISOU   96  O   ASP A1012    10043  10044  13287   -466   -990    -57       O  
ATOM     97  CB  ASP A1012       7.469  19.923  10.596  1.00 89.26           C  
ANISOU   97  CB  ASP A1012     9902  10116  13898   -518   -668    288       C  
ATOM     98  CG  ASP A1012       8.930  19.767  10.245  1.00 97.72           C  
ANISOU   98  CG  ASP A1012    10714  11170  15244   -589   -619    472       C  
ATOM     99  OD1 ASP A1012       9.487  18.678  10.500  1.00 98.34           O  
ANISOU   99  OD1 ASP A1012    10639  11323  15404   -553   -604    534       O  
ATOM    100  OD2 ASP A1012       9.521  20.732   9.716  1.00112.61           O  
ANISOU  100  OD2 ASP A1012    12540  12964  17284   -678   -593    563       O  
ATOM    101  N   ASN A1013       4.459  19.028  11.208  1.00 88.22           N  
ANISOU  101  N   ASN A1013    10186  10115  13217   -279   -660    -25       N  
ATOM    102  CA  ASN A1013       3.168  19.217  11.856  1.00 80.46           C  
ANISOU  102  CA  ASN A1013     9394   9135  12043   -226   -724   -177       C  
ATOM    103  C   ASN A1013       2.703  17.960  12.577  1.00 77.05           C  
ANISOU  103  C   ASN A1013     8982   8835  11459   -155   -762   -243       C  
ATOM    104  O   ASN A1013       1.883  18.054  13.497  1.00 72.39           O  
ANISOU  104  O   ASN A1013     8523   8252  10730   -144   -851   -373       O  
ATOM    105  CB  ASN A1013       2.118  19.650  10.831  1.00 81.96           C  
ANISOU  105  CB  ASN A1013     9701   9288  12150   -141   -588   -175       C  
ATOM    106  CG  ASN A1013       2.309  21.083  10.371  1.00 70.34           C  
ANISOU  106  CG  ASN A1013     8254   7666  10806   -217   -592   -140       C  
ATOM    107  OD1 ASN A1013       2.004  22.026  11.101  1.00 67.00           O  
ANISOU  107  OD1 ASN A1013     7922   7139  10397   -262   -698   -237       O  
ATOM    108  ND2 ASN A1013       2.809  21.254   9.153  1.00 66.73           N  
ANISOU  108  ND2 ASN A1013     7730   7187  10438   -236   -466     -4       N  
ATOM    109  N   LEU A1014       3.202  16.787  12.181  1.00 78.96           N  
ANISOU  109  N   LEU A1014     9103   9172  11728   -107   -686   -155       N  
ATOM    110  CA  LEU A1014       2.911  15.575  12.938  1.00 79.06           C  
ANISOU  110  CA  LEU A1014     9116   9300  11622    -57   -747   -202       C  
ATOM    111  C   LEU A1014       3.482  15.667  14.347  1.00 80.84           C  
ANISOU  111  C   LEU A1014     9308   9521  11886   -177   -970   -243       C  
ATOM    112  O   LEU A1014       2.877  15.173  15.305  1.00 83.70           O  
ANISOU  112  O   LEU A1014     9762   9950  12091   -169  -1071   -339       O  
ATOM    113  CB  LEU A1014       3.476  14.353  12.214  1.00 75.10           C  
ANISOU  113  CB  LEU A1014     8483   8871  11182     12   -614    -92       C  
ATOM    114  CG  LEU A1014       2.518  13.600  11.291  1.00 75.13           C  
ANISOU  114  CG  LEU A1014     8595   8937  11016    139   -447    -98       C  
ATOM    115  CD1 LEU A1014       3.278  12.600  10.435  1.00 74.75           C  
ANISOU  115  CD1 LEU A1014     8432   8913  11057    187   -278     10       C  
ATOM    116  CD2 LEU A1014       1.439  12.897  12.099  1.00 77.86           C  
ANISOU  116  CD2 LEU A1014     9052   9374  11156    199   -537   -201       C  
ATOM    117  N   LYS A1015       4.649  16.298  14.492  1.00 83.32           N  
ANISOU  117  N   LYS A1015     9499   9756  12404   -304  -1058   -162       N  
ATOM    118  CA  LYS A1015       5.241  16.458  15.815  1.00 87.71           C  
ANISOU  118  CA  LYS A1015    10040  10293  12993   -456  -1303   -182       C  
ATOM    119  C   LYS A1015       4.457  17.460  16.653  1.00 89.01           C  
ANISOU  119  C   LYS A1015    10437  10384  12998   -522  -1406   -351       C  
ATOM    120  O   LYS A1015       4.315  17.282  17.868  1.00 92.51           O  
ANISOU  120  O   LYS A1015    10979  10850  13320   -607  -1573   -436       O  
ATOM    121  CB  LYS A1015       6.702  16.891  15.686  1.00 91.02           C  
ANISOU  121  CB  LYS A1015    10254  10636  13692   -587  -1379    -25       C  
ATOM    122  CG  LYS A1015       7.604  15.843  15.054  1.00 93.39           C  
ANISOU  122  CG  LYS A1015    10300  10993  14188   -528  -1274    147       C  
ATOM    123  CD  LYS A1015       9.055  16.296  15.044  1.00 89.97           C  
ANISOU  123  CD  LYS A1015     9638  10481  14065   -666  -1362    322       C  
ATOM    124  CE  LYS A1015       9.964  15.236  14.440  1.00 95.61           C  
ANISOU  124  CE  LYS A1015    10081  11235  15010   -593  -1226    498       C  
ATOM    125  NZ  LYS A1015       9.723  15.048  12.982  1.00 93.20           N  
ANISOU  125  NZ  LYS A1015     9774  10936  14703   -442   -896    517       N  
ATOM    126  N   VAL A1016       3.931  18.515  16.024  1.00 88.75           N  
ANISOU  126  N   VAL A1016    10504  10253  12963   -489  -1301   -399       N  
ATOM    127  CA  VAL A1016       3.167  19.513  16.767  1.00 87.77           C  
ANISOU  127  CA  VAL A1016    10602  10030  12716   -535  -1362   -564       C  
ATOM    128  C   VAL A1016       1.932  18.878  17.389  1.00 92.90           C  
ANISOU  128  C   VAL A1016    11403  10766  13129   -436  -1330   -700       C  
ATOM    129  O   VAL A1016       1.528  19.225  18.505  1.00 96.68           O  
ANISOU  129  O   VAL A1016    12053  11205  13475   -507  -1423   -842       O  
ATOM    130  CB  VAL A1016       2.789  20.689  15.846  1.00 78.54           C  
ANISOU  130  CB  VAL A1016     9487   8733  11623   -495  -1239   -566       C  
ATOM    131  CG1 VAL A1016       1.914  21.690  16.588  1.00 69.06           C  
ANISOU  131  CG1 VAL A1016     8514   7410  10316   -515  -1267   -742       C  
ATOM    132  CG2 VAL A1016       4.040  21.362  15.298  1.00 81.50           C  
ANISOU  132  CG2 VAL A1016     9715   9021  12230   -610  -1278   -427       C  
ATOM    133  N   ILE A1017       1.315  17.935  16.676  1.00 96.77           N  
ANISOU  133  N   ILE A1017    11842  11370  13556   -282  -1191   -659       N  
ATOM    134  CA  ILE A1017       0.111  17.284  17.179  1.00 92.48           C  
ANISOU  134  CA  ILE A1017    11420  10915  12803   -185  -1154   -764       C  
ATOM    135  C   ILE A1017       0.443  16.401  18.375  1.00101.30           C  
ANISOU  135  C   ILE A1017    12541  12128  13820   -266  -1311   -794       C  
ATOM    136  O   ILE A1017      -0.311  16.347  19.354  1.00 99.78           O  
ANISOU  136  O   ILE A1017    12506  11957  13449   -278  -1350   -925       O  
ATOM    137  CB  ILE A1017      -0.571  16.486  16.053  1.00 91.19           C  
ANISOU  137  CB  ILE A1017    11204  10841  12602    -22   -990   -689       C  
ATOM    138  CG1 ILE A1017      -1.071  17.437  14.963  1.00 81.15           C  
ANISOU  138  CG1 ILE A1017     9966   9467  11401     37   -860   -659       C  
ATOM    139  CG2 ILE A1017      -1.723  15.661  16.608  1.00100.04           C  
ANISOU  139  CG2 ILE A1017    12420  12068  13522     66   -973   -770       C  
ATOM    140  CD1 ILE A1017      -1.479  16.748  13.680  1.00 77.77           C  
ANISOU  140  CD1 ILE A1017     9492   9106  10952    147   -719   -551       C  
ATOM    141  N   GLU A1018       1.576  15.696  18.317  1.00 92.34           N  
ANISOU  141  N   GLU A1018    11229  11046  12808   -325  -1398   -665       N  
ATOM    142  CA  GLU A1018       1.924  14.765  19.384  1.00 92.20           C  
ANISOU  142  CA  GLU A1018    11192  11122  12719   -406  -1566   -659       C  
ATOM    143  C   GLU A1018       2.186  15.479  20.704  1.00 92.39           C  
ANISOU  143  C   GLU A1018    11362  11073  12668   -598  -1765   -754       C  
ATOM    144  O   GLU A1018       1.939  14.908  21.772  1.00 92.36           O  
ANISOU  144  O   GLU A1018    11455  11138  12498   -665  -1885   -815       O  
ATOM    145  CB  GLU A1018       3.162  13.963  18.976  1.00 92.59           C  
ANISOU  145  CB  GLU A1018    10992  11211  12977   -428  -1611   -475       C  
ATOM    146  CG  GLU A1018       2.931  12.968  17.848  1.00 93.30           C  
ANISOU  146  CG  GLU A1018    10971  11381  13099   -252  -1417   -394       C  
ATOM    147  CD  GLU A1018       4.196  12.210  17.467  1.00105.96           C  
ANISOU  147  CD  GLU A1018    12325  12998  14938   -264  -1426   -218       C  
ATOM    148  OE1 GLU A1018       5.269  12.514  18.032  1.00108.36           O  
ANISOU  148  OE1 GLU A1018    12512  13250  15409   -411  -1594   -136       O  
ATOM    149  OE2 GLU A1018       4.121  11.318  16.595  1.00102.43           O  
ANISOU  149  OE2 GLU A1018    11799  12601  14519   -132  -1261   -156       O  
ATOM    150  N   LYS A1019       2.680  16.715  20.657  1.00104.19           N  
ANISOU  150  N   LYS A1019    12894  12425  14270   -704  -1807   -767       N  
ATOM    151  CA  LYS A1019       2.895  17.537  21.848  1.00104.20           C  
ANISOU  151  CA  LYS A1019    13082  12326  14185   -903  -1987   -872       C  
ATOM    152  C   LYS A1019       1.927  18.719  21.798  1.00104.59           C  
ANISOU  152  C   LYS A1019    13350  12247  14144   -854  -1849  -1044       C  
ATOM    153  O   LYS A1019       2.289  19.834  21.422  1.00105.07           O  
ANISOU  153  O   LYS A1019    13424  12163  14334   -907  -1843  -1040       O  
ATOM    154  CB  LYS A1019       4.373  17.994  21.964  1.00105.86           C  
ANISOU  154  CB  LYS A1019    13159  12453  14609  -1100  -2188   -732       C  
ATOM    155  CG  LYS A1019       4.932  18.735  20.759  1.00106.00           C  
ANISOU  155  CG  LYS A1019    13021  12382  14874  -1057  -2081   -624       C  
ATOM    156  CD  LYS A1019       6.380  19.158  20.996  1.00108.27           C  
ANISOU  156  CD  LYS A1019    13168  12591  15380  -1267  -2296   -473       C  
ATOM    157  CE  LYS A1019       7.326  17.963  21.011  1.00112.45           C  
ANISOU  157  CE  LYS A1019    13427  13229  16068  -1289  -2396   -275       C  
ATOM    158  NZ  LYS A1019       8.739  18.369  21.259  1.00110.89           N  
ANISOU  158  NZ  LYS A1019    13063  12950  16120  -1499  -2617    -97       N  
ATOM    159  N   ALA A1020       0.678  18.465  22.182  1.00107.85           N  
ANISOU  159  N   ALA A1020    13923  12706  14351   -748  -1733  -1185       N  
ATOM    160  CA  ALA A1020      -0.344  19.501  22.172  1.00107.13           C  
ANISOU  160  CA  ALA A1020    14020  12486  14197   -676  -1577  -1341       C  
ATOM    161  C   ALA A1020      -1.361  19.209  23.264  1.00105.94           C  
ANISOU  161  C   ALA A1020    14086  12373  13792   -667  -1536  -1512       C  
ATOM    162  O   ALA A1020      -1.612  18.050  23.606  1.00106.85           O  
ANISOU  162  O   ALA A1020    14164  12649  13784   -635  -1562  -1487       O  
ATOM    163  CB  ALA A1020      -1.040  19.590  20.808  1.00104.11           C  
ANISOU  163  CB  ALA A1020    13523  12106  13926   -464  -1365  -1277       C  
ATOM    164  N   ASP A1021      -1.940  20.276  23.812  1.00 97.94           N  
ANISOU  164  N   ASP A1021    13304  11201  12707   -697  -1459  -1685       N  
ATOM    165  CA  ASP A1021      -2.880  20.178  24.922  1.00 99.49           C  
ANISOU  165  CA  ASP A1021    13740  11401  12662   -705  -1386  -1868       C  
ATOM    166  C   ASP A1021      -4.310  20.538  24.552  1.00100.23           C  
ANISOU  166  C   ASP A1021    13884  11442  12758   -490  -1113  -1957       C  
ATOM    167  O   ASP A1021      -5.242  19.893  25.036  1.00 98.87           O  
ANISOU  167  O   ASP A1021    13775  11364  12428   -410  -1010  -2022       O  
ATOM    168  CB  ASP A1021      -2.419  21.079  26.076  1.00109.38           C  
ANISOU  168  CB  ASP A1021    15267  12492  13799   -938  -1502  -2019       C  
ATOM    169  CG  ASP A1021      -2.305  22.538  25.669  1.00102.58           C  
ANISOU  169  CG  ASP A1021    14482  11399  13094   -948  -1437  -2078       C  
ATOM    170  OD1 ASP A1021      -2.495  22.843  24.472  1.00101.88           O  
ANISOU  170  OD1 ASP A1021    14213  11284  13215   -786  -1322  -1981       O  
ATOM    171  OD2 ASP A1021      -2.024  23.380  26.549  1.00112.14           O  
ANISOU  171  OD2 ASP A1021    15949  12447  14210  -1131  -1508  -2219       O  
ATOM    172  N   ASN A1022      -4.514  21.547  23.709  1.00106.26           N  
ANISOU  172  N   ASN A1022    14609  12054  13712   -400  -1000  -1945       N  
ATOM    173  CA  ASN A1022      -5.844  21.948  23.277  1.00107.50           C  
ANISOU  173  CA  ASN A1022    14780  12141  13925   -196   -757  -1993       C  
ATOM    174  C   ASN A1022      -6.066  21.542  21.825  1.00102.54           C  
ANISOU  174  C   ASN A1022    13898  11597  13464    -34   -705  -1798       C  
ATOM    175  O   ASN A1022      -5.120  21.324  21.064  1.00100.19           O  
ANISOU  175  O   ASN A1022    13443  11351  13272    -80   -819  -1652       O  
ATOM    176  CB  ASN A1022      -6.054  23.460  23.434  1.00118.44           C  
ANISOU  176  CB  ASN A1022    16333  13262  15408   -213   -658  -2125       C  
ATOM    177  CG  ASN A1022      -5.090  24.279  22.595  1.00115.01           C  
ANISOU  177  CG  ASN A1022    15802  12713  15184   -281   -762  -2021       C  
ATOM    178  OD1 ASN A1022      -5.123  24.228  21.366  1.00111.66           O  
ANISOU  178  OD1 ASN A1022    15174  12322  14930   -170   -729  -1859       O  
ATOM    179  ND2 ASN A1022      -4.241  25.057  23.257  1.00118.06           N  
ANISOU  179  ND2 ASN A1022    16349  12958  15550   -479   -889  -2109       N  
ATOM    180  N   ALA A1023      -7.343  21.446  21.449  1.00 94.24           N  
ANISOU  180  N   ALA A1023    12816  10554  12438    149   -526  -1789       N  
ATOM    181  CA  ALA A1023      -7.689  21.044  20.092  1.00 90.30           C  
ANISOU  181  CA  ALA A1023    12114  10129  12067    286   -484  -1602       C  
ATOM    182  C   ALA A1023      -7.398  22.138  19.074  1.00 87.94           C  
ANISOU  182  C   ALA A1023    11755   9668  11991    297   -467  -1522       C  
ATOM    183  O   ALA A1023      -7.296  21.844  17.878  1.00 85.97           O  
ANISOU  183  O   ALA A1023    11352   9478  11835    350   -476  -1351       O  
ATOM    184  CB  ALA A1023      -9.166  20.652  20.020  1.00 87.07           C  
ANISOU  184  CB  ALA A1023    11686   9765  11633    458   -324  -1594       C  
ATOM    185  N   ALA A1024      -7.268  23.390  19.517  1.00103.40           N  
ANISOU  185  N   ALA A1024    13846  11415  14024    238   -442  -1641       N  
ATOM    186  CA  ALA A1024      -6.936  24.467  18.592  1.00104.56           C  
ANISOU  186  CA  ALA A1024    13941  11400  14388    233   -442  -1560       C  
ATOM    187  C   ALA A1024      -5.532  24.293  18.027  1.00 99.04           C  
ANISOU  187  C   ALA A1024    13131  10763  13735    102   -603  -1439       C  
ATOM    188  O   ALA A1024      -5.285  24.601  16.855  1.00 96.58           O  
ANISOU  188  O   ALA A1024    12699  10424  13575    125   -600  -1289       O  
ATOM    189  CB  ALA A1024      -7.073  25.815  19.292  1.00118.81           C  
ANISOU  189  CB  ALA A1024    15932  12951  16257    190   -383  -1728       C  
ATOM    190  N   GLN A1025      -4.600  23.799  18.845  1.00 93.67           N  
ANISOU  190  N   GLN A1025    12487  10165  12936    -42   -742  -1488       N  
ATOM    191  CA  GLN A1025      -3.259  23.516  18.346  1.00 93.29           C  
ANISOU  191  CA  GLN A1025    12300  10186  12962   -156   -883  -1352       C  
ATOM    192  C   GLN A1025      -3.293  22.395  17.317  1.00 87.51           C  
ANISOU  192  C   GLN A1025    11379   9635  12235    -56   -845  -1184       C  
ATOM    193  O   GLN A1025      -2.621  22.470  16.282  1.00 83.16           O  
ANISOU  193  O   GLN A1025    10695   9088  11814    -72   -851  -1038       O  
ATOM    194  CB  GLN A1025      -2.331  23.144  19.501  1.00 96.37           C  
ANISOU  194  CB  GLN A1025    12754  10625  13238   -334  -1057  -1418       C  
ATOM    195  CG  GLN A1025      -2.009  24.287  20.446  1.00 98.77           C  
ANISOU  195  CG  GLN A1025    13265  10734  13530   -489  -1133  -1567       C  
ATOM    196  CD  GLN A1025      -1.185  23.838  21.638  1.00101.42           C  
ANISOU  196  CD  GLN A1025    13688  11125  13722   -688  -1331  -1619       C  
ATOM    197  OE1 GLN A1025      -1.189  22.662  22.003  1.00100.52           O  
ANISOU  197  OE1 GLN A1025    13519  11190  13483   -680  -1379  -1589       O  
ATOM    198  NE2 GLN A1025      -0.471  24.775  22.250  1.00 99.53           N  
ANISOU  198  NE2 GLN A1025    13590  10724  13502   -881  -1464  -1685       N  
ATOM    199  N   VAL A1026      -4.070  21.346  17.590  1.00 94.40           N  
ANISOU  199  N   VAL A1026    12254  10653  12959     40   -797  -1205       N  
ATOM    200  CA  VAL A1026      -4.198  20.244  16.642  1.00 90.30           C  
ANISOU  200  CA  VAL A1026    11592  10293  12424    132   -756  -1059       C  
ATOM    201  C   VAL A1026      -4.864  20.728  15.362  1.00 87.40           C  
ANISOU  201  C   VAL A1026    11181   9860  12167    234   -643   -952       C  
ATOM    202  O   VAL A1026      -4.408  20.432  14.251  1.00 83.53           O  
ANISOU  202  O   VAL A1026    10585   9414  11738    237   -626   -806       O  
ATOM    203  CB  VAL A1026      -4.985  19.083  17.277  1.00 90.79           C  
ANISOU  203  CB  VAL A1026    11686  10509  12303    204   -740  -1108       C  
ATOM    204  CG1 VAL A1026      -5.078  17.912  16.311  1.00 92.70           C  
ANISOU  204  CG1 VAL A1026    11803  10901  12518    285   -708   -962       C  
ATOM    205  CG2 VAL A1026      -4.343  18.656  18.589  1.00 96.38           C  
ANISOU  205  CG2 VAL A1026    12455  11273  12892     79   -871  -1204       C  
ATOM    206  N   LYS A1027      -5.961  21.476  15.500  1.00 83.77           N  
ANISOU  206  N   LYS A1027    10806   9285  11737    315   -558  -1017       N  
ATOM    207  CA  LYS A1027      -6.649  22.001  14.327  1.00 83.19           C  
ANISOU  207  CA  LYS A1027    10688   9132  11787    399   -477   -895       C  
ATOM    208  C   LYS A1027      -5.708  22.827  13.459  1.00 82.45           C  
ANISOU  208  C   LYS A1027    10544   8937  11848    311   -511   -799       C  
ATOM    209  O   LYS A1027      -5.721  22.710  12.227  1.00 81.66           O  
ANISOU  209  O   LYS A1027    10372   8858  11796    329   -481   -640       O  
ATOM    210  CB  LYS A1027      -7.839  22.856  14.756  1.00 83.51           C  
ANISOU  210  CB  LYS A1027    10812   9024  11894    489   -385   -980       C  
ATOM    211  CG  LYS A1027      -8.714  23.284  13.601  1.00 86.36           C  
ANISOU  211  CG  LYS A1027    11111   9309  12393    580   -323   -827       C  
ATOM    212  CD  LYS A1027     -10.010  23.907  14.082  1.00 89.89           C  
ANISOU  212  CD  LYS A1027    11603   9623  12928    697   -215   -892       C  
ATOM    213  CE  LYS A1027     -10.652  24.711  12.971  1.00106.84           C  
ANISOU  213  CE  LYS A1027    13684  11629  15281    753   -187   -729       C  
ATOM    214  NZ  LYS A1027     -10.932  23.811  11.817  1.00 96.48           N  
ANISOU  214  NZ  LYS A1027    12281  10465  13913    768   -231   -523       N  
ATOM    215  N   ASP A1028      -4.877  23.665  14.084  1.00 82.58           N  
ANISOU  215  N   ASP A1028    10610   8836  11931    201   -576   -888       N  
ATOM    216  CA  ASP A1028      -3.957  24.498  13.318  1.00 82.13           C  
ANISOU  216  CA  ASP A1028    10499   8676  12031    107   -613   -791       C  
ATOM    217  C   ASP A1028      -2.944  23.649  12.562  1.00 80.97           C  
ANISOU  217  C   ASP A1028    10219   8672  11874     54   -636   -651       C  
ATOM    218  O   ASP A1028      -2.669  23.901  11.383  1.00 80.51           O  
ANISOU  218  O   ASP A1028    10095   8591  11906     40   -594   -507       O  
ATOM    219  CB  ASP A1028      -3.247  25.481  14.250  1.00 85.34           C  
ANISOU  219  CB  ASP A1028    10995   8932  12498    -19   -700   -915       C  
ATOM    220  CG  ASP A1028      -2.313  26.418  13.508  1.00 97.25           C  
ANISOU  220  CG  ASP A1028    12445  10321  14183   -125   -746   -810       C  
ATOM    221  OD1 ASP A1028      -2.813  27.300  12.776  1.00100.46           O  
ANISOU  221  OD1 ASP A1028    12863  10592  14714    -84   -689   -753       O  
ATOM    222  OD2 ASP A1028      -1.081  26.273  13.657  1.00 94.74           O  
ANISOU  222  OD2 ASP A1028    12060  10042  13894   -254   -844   -771       O  
ATOM    223  N   ALA A1029      -2.376  22.637  13.222  1.00 81.71           N  
ANISOU  223  N   ALA A1029    10274   8905  11866     20   -693   -687       N  
ATOM    224  CA  ALA A1029      -1.392  21.791  12.557  1.00 74.76           C  
ANISOU  224  CA  ALA A1029     9256   8144  11006    -16   -690   -557       C  
ATOM    225  C   ALA A1029      -2.028  20.985  11.432  1.00 68.90           C  
ANISOU  225  C   ALA A1029     8485   7500  10192     89   -574   -447       C  
ATOM    226  O   ALA A1029      -1.459  20.879  10.339  1.00 67.63           O  
ANISOU  226  O   ALA A1029     8254   7353  10091     64   -508   -315       O  
ATOM    227  CB  ALA A1029      -0.730  20.861  13.574  1.00 76.28           C  
ANISOU  227  CB  ALA A1029     9407   8450  11125    -68   -788   -608       C  
ATOM    228  N   LEU A1030      -3.210  20.415  11.677  1.00 72.43           N  
ANISOU  228  N   LEU A1030     8999   8014  10507    194   -545   -497       N  
ATOM    229  CA  LEU A1030      -3.883  19.638  10.642  1.00 73.40           C  
ANISOU  229  CA  LEU A1030     9118   8222  10546    274   -461   -387       C  
ATOM    230  C   LEU A1030      -4.235  20.495   9.434  1.00 72.78           C  
ANISOU  230  C   LEU A1030     9062   8036  10555    269   -406   -269       C  
ATOM    231  O   LEU A1030      -4.221  20.004   8.299  1.00 66.31           O  
ANISOU  231  O   LEU A1030     8238   7266   9691    267   -342   -141       O  
ATOM    232  CB  LEU A1030      -5.142  18.987  11.211  1.00 70.73           C  
ANISOU  232  CB  LEU A1030     8841   7960  10072    376   -460   -451       C  
ATOM    233  CG  LEU A1030      -4.914  17.828  12.180  1.00 72.93           C  
ANISOU  233  CG  LEU A1030     9105   8381  10225    384   -509   -531       C  
ATOM    234  CD1 LEU A1030      -6.189  17.501  12.935  1.00 74.02           C  
ANISOU  234  CD1 LEU A1030     9313   8564  10249    471   -507   -613       C  
ATOM    235  CD2 LEU A1030      -4.407  16.601  11.434  1.00 70.39           C  
ANISOU  235  CD2 LEU A1030     8721   8183   9842    390   -473   -429       C  
ATOM    236  N   THR A1031      -4.559  21.771   9.654  1.00 76.76           N  
ANISOU  236  N   THR A1031     9603   8381  11179    258   -430   -306       N  
ATOM    237  CA  THR A1031      -4.874  22.653   8.536  1.00 70.59           C  
ANISOU  237  CA  THR A1031     8836   7483  10502    241   -400   -178       C  
ATOM    238  C   THR A1031      -3.677  22.799   7.606  1.00 67.71           C  
ANISOU  238  C   THR A1031     8416   7113  10196    135   -372    -65       C  
ATOM    239  O   THR A1031      -3.821  22.745   6.379  1.00 67.65           O  
ANISOU  239  O   THR A1031     8426   7109  10169    113   -318     81       O  
ATOM    240  CB  THR A1031      -5.316  24.021   9.057  1.00 75.73           C  
ANISOU  240  CB  THR A1031     9531   7943  11301    249   -430   -250       C  
ATOM    241  OG1 THR A1031      -6.342  23.850  10.042  1.00 75.74           O  
ANISOU  241  OG1 THR A1031     9581   7945  11251    350   -422   -373       O  
ATOM    242  CG2 THR A1031      -5.849  24.878   7.918  1.00 91.79           C  
ANISOU  242  CG2 THR A1031    11573   9851  13453    244   -415    -98       C  
ATOM    243  N   LYS A1032      -2.484  22.990   8.176  1.00 67.81           N  
ANISOU  243  N   LYS A1032     8368   7116  10282     56   -408   -119       N  
ATOM    244  CA  LYS A1032      -1.278  23.072   7.361  1.00 65.27           C  
ANISOU  244  CA  LYS A1032     7966   6794  10039    -41   -362     -4       C  
ATOM    245  C   LYS A1032      -1.029  21.765   6.620  1.00 64.29           C  
ANISOU  245  C   LYS A1032     7812   6819   9795    -17   -257     76       C  
ATOM    246  O   LYS A1032      -0.622  21.770   5.452  1.00 69.35           O  
ANISOU  246  O   LYS A1032     8449   7456  10446    -66   -157    205       O  
ATOM    247  CB  LYS A1032      -0.078  23.418   8.241  1.00 71.89           C  
ANISOU  247  CB  LYS A1032     8722   7598  10993   -133   -443    -65       C  
ATOM    248  CG  LYS A1032      -0.159  24.776   8.920  1.00 67.68           C  
ANISOU  248  CG  LYS A1032     8246   6893  10578   -186   -543   -148       C  
ATOM    249  CD  LYS A1032       1.111  25.064   9.707  1.00 76.10           C  
ANISOU  249  CD  LYS A1032     9240   7927  11749   -310   -647   -181       C  
ATOM    250  CE  LYS A1032       1.103  26.460  10.306  1.00 84.44           C  
ANISOU  250  CE  LYS A1032    10382   8789  12913   -387   -747   -261       C  
ATOM    251  NZ  LYS A1032       0.093  26.602  11.390  1.00 91.21           N  
ANISOU  251  NZ  LYS A1032    11385   9599  13672   -320   -784   -443       N  
ATOM    252  N   MET A1033      -1.275  20.632   7.281  1.00 63.11           N  
ANISOU  252  N   MET A1033     7659   6795   9526     55   -268      0       N  
ATOM    253  CA  MET A1033      -1.004  19.340   6.662  1.00 62.33           C  
ANISOU  253  CA  MET A1033     7541   6820   9320     82   -164     62       C  
ATOM    254  C   MET A1033      -1.885  19.112   5.441  1.00 66.16           C  
ANISOU  254  C   MET A1033     8143   7315   9680    104    -83    162       C  
ATOM    255  O   MET A1033      -1.423  18.581   4.424  1.00 67.43           O  
ANISOU  255  O   MET A1033     8322   7508   9789     70     42    256       O  
ATOM    256  CB  MET A1033      -1.207  18.223   7.684  1.00 67.84           C  
ANISOU  256  CB  MET A1033     8221   7637   9918    152   -216    -39       C  
ATOM    257  CG  MET A1033      -0.234  18.278   8.853  1.00 71.72           C  
ANISOU  257  CG  MET A1033     8604   8131  10516    102   -314   -113       C  
ATOM    258  SD  MET A1033      -0.499  16.972  10.068  1.00 69.48           S  
ANISOU  258  SD  MET A1033     8311   7985  10104    164   -396   -215       S  
ATOM    259  CE  MET A1033      -0.066  15.526   9.102  1.00 69.43           C  
ANISOU  259  CE  MET A1033     8251   8082  10046    212   -250   -112       C  
ATOM    260  N   ARG A1034      -3.159  19.504   5.520  1.00 70.67           N  
ANISOU  260  N   ARG A1034     8799   7849  10205    151   -151    153       N  
ATOM    261  CA  ARG A1034      -4.060  19.299   4.392  1.00 63.88           C  
ANISOU  261  CA  ARG A1034     8050   6991   9231    151   -115    273       C  
ATOM    262  C   ARG A1034      -3.597  20.080   3.168  1.00 71.65           C  
ANISOU  262  C   ARG A1034     9068   7884  10273     44    -54    410       C  
ATOM    263  O   ARG A1034      -3.685  19.588   2.037  1.00 74.04           O  
ANISOU  263  O   ARG A1034     9467   8216  10448     -6     26    521       O  
ATOM    264  CB  ARG A1034      -5.482  19.704   4.776  1.00 66.74           C  
ANISOU  264  CB  ARG A1034     8455   7310   9594    220   -211    261       C  
ATOM    265  CG  ARG A1034      -6.560  18.879   4.096  1.00 67.93           C  
ANISOU  265  CG  ARG A1034     8700   7527   9583    246   -216    357       C  
ATOM    266  CD  ARG A1034      -7.941  19.496   4.274  1.00 63.46           C  
ANISOU  266  CD  ARG A1034     8145   6885   9081    302   -305    399       C  
ATOM    267  NE  ARG A1034      -8.969  18.745   3.556  1.00 59.69           N  
ANISOU  267  NE  ARG A1034     7750   6465   8464    303   -339    526       N  
ATOM    268  CZ  ARG A1034      -9.460  19.077   2.364  1.00 61.17           C  
ANISOU  268  CZ  ARG A1034     8017   6589   8634    221   -374    710       C  
ATOM    269  NH1 ARG A1034      -9.027  20.160   1.728  1.00 68.89           N  
ANISOU  269  NH1 ARG A1034     9000   7447   9729    139   -370    788       N  
ATOM    270  NH2 ARG A1034     -10.391  18.320   1.803  1.00 60.09           N  
ANISOU  270  NH2 ARG A1034     7964   6507   8360    205   -429    828       N  
ATOM    271  N   ALA A1035      -3.097  21.300   3.374  1.00 74.26           N  
ANISOU  271  N   ALA A1035     9336   8097  10781     -6    -91    405       N  
ATOM    272  CA  ALA A1035      -2.582  22.081   2.255  1.00 77.40           C  
ANISOU  272  CA  ALA A1035     9758   8408  11243   -119    -36    540       C  
ATOM    273  C   ALA A1035      -1.341  21.433   1.654  1.00 84.12           C  
ANISOU  273  C   ALA A1035    10575   9326  12061   -181    118    584       C  
ATOM    274  O   ALA A1035      -1.187  21.392   0.427  1.00 84.52           O  
ANISOU  274  O   ALA A1035    10713   9367  12035   -263    223    709       O  
ATOM    275  CB  ALA A1035      -2.271  23.507   2.710  1.00 81.21           C  
ANISOU  275  CB  ALA A1035    10176   8744  11936   -159   -118    518       C  
ATOM    276  N   ALA A1036      -0.446  20.919   2.501  1.00 89.74           N  
ANISOU  276  N   ALA A1036    11162  10098  12837   -149    138    490       N  
ATOM    277  CA  ALA A1036       0.771  20.292   1.996  1.00 96.26           C  
ANISOU  277  CA  ALA A1036    11919  10972  13683   -190    303    539       C  
ATOM    278  C   ALA A1036       0.457  19.012   1.234  1.00 89.01           C  
ANISOU  278  C   ALA A1036    11117  10147  12557   -158    440    568       C  
ATOM    279  O   ALA A1036       1.052  18.747   0.183  1.00 93.58           O  
ANISOU  279  O   ALA A1036    11741  10721  13092   -221    621    656       O  
ATOM    280  CB  ALA A1036       1.733  20.009   3.150  1.00 92.08           C  
ANISOU  280  CB  ALA A1036    11211  10478  13296   -165    260    453       C  
ATOM    281  N   ALA A1037      -0.471  18.203   1.747  1.00 84.54           N  
ANISOU  281  N   ALA A1037    10610   9656  11856    -68    365    494       N  
ATOM    282  CA  ALA A1037      -0.839  16.973   1.054  1.00 81.97           C  
ANISOU  282  CA  ALA A1037    10416   9406  11321    -46    475    519       C  
ATOM    283  C   ALA A1037      -1.406  17.278  -0.326  1.00 89.05           C  
ANISOU  283  C   ALA A1037    11507  10253  12075   -142    528    648       C  
ATOM    284  O   ALA A1037      -1.008  16.667  -1.324  1.00 93.89           O  
ANISOU  284  O   ALA A1037    12233  10877  12565   -199    706    706       O  
ATOM    285  CB  ALA A1037      -1.843  16.181   1.889  1.00 69.16           C  
ANISOU  285  CB  ALA A1037     8823   7867   9590     56    353    431       C  
ATOM    286  N   LEU A1038      -2.346  18.224  -0.402  1.00 88.77           N  
ANISOU  286  N   LEU A1038    11521  10152  12057   -169    378    700       N  
ATOM    287  CA  LEU A1038      -2.908  18.591  -1.697  1.00 90.22           C  
ANISOU  287  CA  LEU A1038    11884  10278  12117   -283    388    850       C  
ATOM    288  C   LEU A1038      -1.837  19.159  -2.619  1.00 95.49           C  
ANISOU  288  C   LEU A1038    12566  10884  12833   -405    543    937       C  
ATOM    289  O   LEU A1038      -1.824  18.868  -3.821  1.00 95.76           O  
ANISOU  289  O   LEU A1038    12781  10910  12693   -513    660   1038       O  
ATOM    290  CB  LEU A1038      -4.040  19.600  -1.507  1.00 88.13           C  
ANISOU  290  CB  LEU A1038    11621   9933  11930   -280    189    906       C  
ATOM    291  CG  LEU A1038      -5.281  19.082  -0.778  1.00 85.55           C  
ANISOU  291  CG  LEU A1038    11298   9658  11550   -172     52    857       C  
ATOM    292  CD1 LEU A1038      -6.142  20.238  -0.294  1.00 81.98           C  
ANISOU  292  CD1 LEU A1038    10776   9101  11269   -135   -105    880       C  
ATOM    293  CD2 LEU A1038      -6.083  18.158  -1.679  1.00 86.27           C  
ANISOU  293  CD2 LEU A1038    11579   9800  11400   -225     48    959       C  
ATOM    294  N   ASP A1039      -0.924  19.971  -2.075  1.00 83.94           N  
ANISOU  294  N   ASP A1039    10924   9373  11596   -403    546    904       N  
ATOM    295  CA  ASP A1039       0.143  20.526  -2.901  1.00 85.70           C  
ANISOU  295  CA  ASP A1039    11133   9539  11889   -520    699    995       C  
ATOM    296  C   ASP A1039       1.105  19.437  -3.354  1.00 87.13           C  
ANISOU  296  C   ASP A1039    11324   9785  11995   -520    954    982       C  
ATOM    297  O   ASP A1039       1.526  19.417  -4.517  1.00 94.11           O  
ANISOU  297  O   ASP A1039    12332  10642  12782   -630   1139   1078       O  
ATOM    298  CB  ASP A1039       0.893  21.617  -2.136  1.00 92.16           C  
ANISOU  298  CB  ASP A1039    11748  10287  12980   -523    621    969       C  
ATOM    299  CG  ASP A1039       1.890  22.360  -3.009  1.00100.66           C  
ANISOU  299  CG  ASP A1039    12803  11295  14149   -656    753   1089       C  
ATOM    300  OD1 ASP A1039       1.806  22.233  -4.250  1.00104.73           O  
ANISOU  300  OD1 ASP A1039    13487  11802  14502   -757    883   1200       O  
ATOM    301  OD2 ASP A1039       2.760  23.067  -2.456  1.00 99.29           O  
ANISOU  301  OD2 ASP A1039    12453  11074  14201   -674    724   1079       O  
ATOM    302  N   ALA A1040       1.464  18.518  -2.452  1.00100.75           N  
ANISOU  302  N   ALA A1040    12925  11586  13769   -401    978    866       N  
ATOM    303  CA  ALA A1040       2.362  17.434  -2.830  1.00103.96           C  
ANISOU  303  CA  ALA A1040    13322  12037  14142   -381   1231    853       C  
ATOM    304  C   ALA A1040       1.731  16.556  -3.898  1.00101.01           C  
ANISOU  304  C   ALA A1040    13225  11683  13470   -422   1359    884       C  
ATOM    305  O   ALA A1040       2.439  15.972  -4.727  1.00102.15           O  
ANISOU  305  O   ALA A1040    13451  11817  13545   -463   1627    912       O  
ATOM    306  CB  ALA A1040       2.722  16.591  -1.608  1.00105.82           C  
ANISOU  306  CB  ALA A1040    13375  12343  14490   -247   1190    737       C  
ATOM    307  N   GLN A1041       0.403  16.452  -3.891  1.00 98.35           N  
ANISOU  307  N   GLN A1041    13042  11367  12960   -419   1174    884       N  
ATOM    308  CA  GLN A1041      -0.289  15.685  -4.915  1.00 96.01           C  
ANISOU  308  CA  GLN A1041    13035  11080  12366   -490   1247    932       C  
ATOM    309  C   GLN A1041      -0.007  16.237  -6.303  1.00 99.12           C  
ANISOU  309  C   GLN A1041    13615  11399  12646   -666   1394   1062       C  
ATOM    310  O   GLN A1041      -0.111  15.499  -7.289  1.00 97.16           O  
ANISOU  310  O   GLN A1041    13624  11147  12147   -751   1553   1093       O  
ATOM    311  CB  GLN A1041      -1.791  15.694  -4.632  1.00 93.24           C  
ANISOU  311  CB  GLN A1041    12777  10753  11899   -473    982    948       C  
ATOM    312  CG  GLN A1041      -2.540  14.491  -5.167  1.00 94.03           C  
ANISOU  312  CG  GLN A1041    13119  10895  11714   -495   1004    952       C  
ATOM    313  CD  GLN A1041      -4.013  14.529  -4.813  1.00 93.73           C  
ANISOU  313  CD  GLN A1041    13126  10879  11606   -475    731    990       C  
ATOM    314  OE1 GLN A1041      -4.634  15.592  -4.802  1.00100.65           O  
ANISOU  314  OE1 GLN A1041    13964  11705  12574   -513    557   1077       O  
ATOM    315  NE2 GLN A1041      -4.579  13.366  -4.512  1.00 86.91           N  
ANISOU  315  NE2 GLN A1041    12335  10086  10601   -411    696    933       N  
ATOM    316  N   LYS A1042       0.357  17.518  -6.399  1.00112.16           N  
ANISOU  316  N   LYS A1042    15162  12987  14466   -734   1345   1139       N  
ATOM    317  CA  LYS A1042       0.630  18.169  -7.672  1.00112.23           C  
ANISOU  317  CA  LYS A1042    15338  12925  14381   -916   1463   1277       C  
ATOM    318  C   LYS A1042       2.127  18.249  -7.952  1.00113.36           C  
ANISOU  318  C   LYS A1042    15363  13046  14663   -938   1754   1279       C  
ATOM    319  O   LYS A1042       2.593  19.207  -8.578  1.00115.34           O  
ANISOU  319  O   LYS A1042    15616  13232  14974  -1063   1808   1388       O  
ATOM    320  CB  LYS A1042       0.037  19.579  -7.664  1.00112.52           C  
ANISOU  320  CB  LYS A1042    15336  12890  14527   -989   1217   1384       C  
ATOM    321  CG  LYS A1042      -1.400  19.663  -7.168  1.00112.47           C  
ANISOU  321  CG  LYS A1042    15360  12891  14484   -935    923   1389       C  
ATOM    322  CD  LYS A1042      -2.348  18.724  -7.884  1.00112.22           C  
ANISOU  322  CD  LYS A1042    15604  12892  14143   -999    902   1437       C  
ATOM    323  CE  LYS A1042      -3.782  18.995  -7.452  1.00113.32           C  
ANISOU  323  CE  LYS A1042    15738  13023  14296   -961    600   1486       C  
ATOM    324  NZ  LYS A1042      -3.964  18.806  -5.980  1.00113.20           N  
ANISOU  324  NZ  LYS A1042    15485  13061  14465   -757    500   1333       N  
ATOM    325  N   ALA A1043       2.889  17.254  -7.499  1.00106.14           N  
ANISOU  325  N   ALA A1043    14331  12177  13818   -818   1941   1174       N  
ATOM    326  CA  ALA A1043       4.347  17.249  -7.607  1.00102.79           C  
ANISOU  326  CA  ALA A1043    13733  11731  13593   -810   2219   1184       C  
ATOM    327  C   ALA A1043       4.804  15.892  -8.131  1.00104.35           C  
ANISOU  327  C   ALA A1043    14055  11941  13652   -772   2545   1128       C  
ATOM    328  O   ALA A1043       4.855  14.919  -7.374  1.00104.55           O  
ANISOU  328  O   ALA A1043    13978  12014  13731   -626   2547   1023       O  
ATOM    329  CB  ALA A1043       4.993  17.564  -6.260  1.00101.94           C  
ANISOU  329  CB  ALA A1043    13261  11644  13828   -686   2090   1127       C  
ATOM    330  N   THR A1044       5.128  15.821  -9.413  1.00117.97           N  
ANISOU  330  N   THR A1044    16013  13614  15196   -907   2824   1196       N  
ATOM    331  CA  THR A1044       5.664  14.584  -9.962  1.00119.12           C  
ANISOU  331  CA  THR A1044    16292  13743  15225   -873   3186   1134       C  
ATOM    332  C   THR A1044       6.883  14.139  -9.150  1.00119.12           C  
ANISOU  332  C   THR A1044    15931  13749  15580   -708   3356   1084       C  
ATOM    333  O   THR A1044       7.742  14.967  -8.819  1.00121.76           O  
ANISOU  333  O   THR A1044    15984  14067  16211   -709   3360   1152       O  
ATOM    334  CB  THR A1044       6.038  14.777 -11.435  1.00121.71           C  
ANISOU  334  CB  THR A1044    16902  13998  15342  -1060   3501   1221       C  
ATOM    335  OG1 THR A1044       6.460  13.525 -11.993  1.00124.73           O  
ANISOU  335  OG1 THR A1044    17464  14347  15583  -1027   3875   1142       O  
ATOM    336  CG2 THR A1044       7.145  15.805 -11.582  1.00122.25           C  
ANISOU  336  CG2 THR A1044    16739  14029  15682  -1112   3636   1324       C  
ATOM    337  N   PRO A1045       6.993  12.856  -8.811  1.00112.12           N  
ANISOU  337  N   PRO A1045    15037  12877  14687   -573   3482    981       N  
ATOM    338  CA  PRO A1045       8.201  12.355  -8.134  1.00110.47           C  
ANISOU  338  CA  PRO A1045    14483  12657  14834   -424   3663    960       C  
ATOM    339  C   PRO A1045       9.434  12.519  -9.002  1.00113.65           C  
ANISOU  339  C   PRO A1045    14834  12977  15369   -478   4085   1041       C  
ATOM    340  O   PRO A1045       9.431  12.130 -10.180  1.00117.21           O  
ANISOU  340  O   PRO A1045    15599  13370  15565   -567   4399   1038       O  
ATOM    341  CB  PRO A1045       7.887  10.870  -7.887  1.00112.10           C  
ANISOU  341  CB  PRO A1045    14790  12875  14929   -297   3740    841       C  
ATOM    342  CG  PRO A1045       6.412  10.768  -7.969  1.00111.07           C  
ANISOU  342  CG  PRO A1045    14959  12794  14450   -356   3461    796       C  
ATOM    343  CD  PRO A1045       5.991  11.788  -8.982  1.00111.81           C  
ANISOU  343  CD  PRO A1045    15291  12858  14333   -553   3438    891       C  
ATOM    344  N   PRO A1046      10.512  13.090  -8.457  1.00116.14           N  
ANISOU  344  N   PRO A1046    14766  13282  16079   -437   4107   1121       N  
ATOM    345  CA  PRO A1046      11.663  13.424  -9.313  1.00123.17           C  
ANISOU  345  CA  PRO A1046    15587  14097  17117   -505   4499   1227       C  
ATOM    346  C   PRO A1046      12.319  12.213  -9.951  1.00125.64           C  
ANISOU  346  C   PRO A1046    15980  14335  17423   -427   4985   1183       C  
ATOM    347  O   PRO A1046      12.776  12.293 -11.099  1.00130.23           O  
ANISOU  347  O   PRO A1046    16741  14845  17896   -527   5368   1229       O  
ATOM    348  CB  PRO A1046      12.617  14.132  -8.339  1.00119.58           C  
ANISOU  348  CB  PRO A1046    14659  13652  17125   -456   4353   1323       C  
ATOM    349  CG  PRO A1046      12.299  13.528  -7.009  1.00121.50           C  
ANISOU  349  CG  PRO A1046    14718  13955  17492   -307   4053   1236       C  
ATOM    350  CD  PRO A1046      10.820  13.252  -7.023  1.00106.23           C  
ANISOU  350  CD  PRO A1046    13124  12077  15163   -322   3815   1120       C  
ATOM    351  N   LYS A1047      12.384  11.088  -9.238  1.00119.54           N  
ANISOU  351  N   LYS A1047    15087  13567  16767   -254   4992   1096       N  
ATOM    352  CA  LYS A1047      13.036   9.898  -9.773  1.00121.90           C  
ANISOU  352  CA  LYS A1047    15441  13772  17104   -158   5464   1050       C  
ATOM    353  C   LYS A1047      12.311   9.308 -10.978  1.00122.72           C  
ANISOU  353  C   LYS A1047    16081  13825  16723   -256   5703    956       C  
ATOM    354  O   LYS A1047      12.914   8.524 -11.719  1.00125.45           O  
ANISOU  354  O   LYS A1047    16550  14063  17052   -222   6179    921       O  
ATOM    355  CB  LYS A1047      13.159   8.849  -8.668  1.00120.68           C  
ANISOU  355  CB  LYS A1047    15041  13631  17180     43   5356    985       C  
ATOM    356  CG  LYS A1047      13.835   7.570  -9.101  1.00123.14           C  
ANISOU  356  CG  LYS A1047    15375  13826  17586    169   5830    937       C  
ATOM    357  CD  LYS A1047      14.178   6.708  -7.905  1.00122.27           C  
ANISOU  357  CD  LYS A1047    14921  13723  17815    364   5697    924       C  
ATOM    358  CE  LYS A1047      14.573   5.324  -8.354  1.00124.41           C  
ANISOU  358  CE  LYS A1047    15289  13866  18116    495   6136    849       C  
ATOM    359  NZ  LYS A1047      14.813   4.380  -7.232  1.00123.60           N  
ANISOU  359  NZ  LYS A1047    14884  13760  18319    680   5995    839       N  
ATOM    360  N   LEU A1048      11.047   9.661 -11.194  1.00122.85           N  
ANISOU  360  N   LEU A1048    16423  13904  16353   -383   5391    920       N  
ATOM    361  CA  LEU A1048      10.264   9.169 -12.325  1.00127.03           C  
ANISOU  361  CA  LEU A1048    17485  14387  16393   -517   5545    853       C  
ATOM    362  C   LEU A1048       9.642  10.333 -13.083  1.00134.23           C  
ANISOU  362  C   LEU A1048    18648  15325  17030   -750   5379    944       C  
ATOM    363  O   LEU A1048       8.506  10.257 -13.563  1.00133.56           O  
ANISOU  363  O   LEU A1048    18944  15257  16547   -879   5196    920       O  
ATOM    364  CB  LEU A1048       9.199   8.173 -11.874  1.00122.87           C  
ANISOU  364  CB  LEU A1048    17146  13898  15642   -447   5311    731       C  
ATOM    365  CG  LEU A1048       8.119   8.656 -10.910  1.00119.44           C  
ANISOU  365  CG  LEU A1048    16617  13587  15179   -437   4746    735       C  
ATOM    366  CD1 LEU A1048       6.743   8.525 -11.542  1.00122.21           C  
ANISOU  366  CD1 LEU A1048    17424  13955  15057   -589   4553    711       C  
ATOM    367  CD2 LEU A1048       8.189   7.869  -9.613  1.00116.71           C  
ANISOU  367  CD2 LEU A1048    15969  13288  15087   -225   4582    662       C  
ATOM    368  N   GLU A1049      10.386  11.438 -13.189  1.00134.81           N  
ANISOU  368  N   GLU A1049    16714  18917  15591   1410    449  -2318       N  
ATOM    369  CA  GLU A1049       9.957  12.558 -14.020  1.00134.96           C  
ANISOU  369  CA  GLU A1049    16774  19322  15183   1289    291  -2239       C  
ATOM    370  C   GLU A1049       9.642  12.111 -15.443  1.00135.85           C  
ANISOU  370  C   GLU A1049    16949  19653  15016   1120    371  -2606       C  
ATOM    371  O   GLU A1049       8.783  12.703 -16.106  1.00135.44           O  
ANISOU  371  O   GLU A1049    16951  19858  14651    966    193  -2614       O  
ATOM    372  CB  GLU A1049      11.059  13.624 -14.044  1.00132.66           C  
ANISOU  372  CB  GLU A1049    16446  19200  14760   1375    294  -1965       C  
ATOM    373  CG  GLU A1049      10.711  14.912 -14.781  1.00132.31           C  
ANISOU  373  CG  GLU A1049    16441  19538  14291   1258     98  -1818       C  
ATOM    374  CD  GLU A1049       9.773  15.799 -13.987  1.00137.38           C  
ANISOU  374  CD  GLU A1049    17096  20178  14924   1262   -191  -1527       C  
ATOM    375  OE1 GLU A1049       9.692  15.614 -12.756  1.00132.98           O  
ANISOU  375  OE1 GLU A1049    16513  19339  14675   1383   -218  -1368       O  
ATOM    376  OE2 GLU A1049       9.124  16.681 -14.589  1.00139.12           O  
ANISOU  376  OE2 GLU A1049    17354  20673  14832   1143   -391  -1457       O  
ATOM    377  N   ASP A1050      10.324  11.069 -15.926  1.00145.93           N  
ANISOU  377  N   ASP A1050    18223  20822  16402   1145    630  -2914       N  
ATOM    378  CA  ASP A1050      10.106  10.600 -17.291  1.00145.26           C  
ANISOU  378  CA  ASP A1050    18218  20936  16039    987    728  -3287       C  
ATOM    379  C   ASP A1050       8.698  10.048 -17.489  1.00146.07           C  
ANISOU  379  C   ASP A1050    18394  20993  16113    829    581  -3479       C  
ATOM    380  O   ASP A1050       8.093  10.251 -18.549  1.00147.82           O  
ANISOU  380  O   ASP A1050    18701  21477  15987    645    500  -3637       O  
ATOM    381  CB  ASP A1050      11.146   9.536 -17.647  1.00148.07           C  
ANISOU  381  CB  ASP A1050    18551  21142  16568   1073   1050  -3589       C  
ATOM    382  CG  ASP A1050      11.168   8.387 -16.659  1.00147.86           C  
ANISOU  382  CG  ASP A1050    18478  20671  17031   1197   1129  -3665       C  
ATOM    383  OD1 ASP A1050      10.283   8.338 -15.778  1.00145.79           O  
ANISOU  383  OD1 ASP A1050    18216  20236  16940   1187    944  -3515       O  
ATOM    384  OD2 ASP A1050      12.074   7.534 -16.760  1.00149.90           O  
ANISOU  384  OD2 ASP A1050    18696  20753  17508   1302   1377  -3872       O  
ATOM    385  N   LYS A1051       8.157   9.353 -16.490  1.00139.40           N  
ANISOU  385  N   LYS A1051    17518  19822  15627    885    537  -3457       N  
ATOM    386  CA  LYS A1051       6.868   8.696 -16.667  1.00138.72           C  
ANISOU  386  CA  LYS A1051    17486  19667  15554    734    418  -3653       C  
ATOM    387  C   LYS A1051       5.779   9.733 -16.915  1.00143.11           C  
ANISOU  387  C   LYS A1051    18063  20493  15820    594    135  -3477       C  
ATOM    388  O   LYS A1051       5.788  10.824 -16.338  1.00147.75           O  
ANISOU  388  O   LYS A1051    18601  21174  16364    660     -7  -3132       O  
ATOM    389  CB  LYS A1051       6.533   7.842 -15.442  1.00134.54           C  
ANISOU  389  CB  LYS A1051    16907  18740  15472    820    417  -3609       C  
ATOM    390  CG  LYS A1051       6.481   6.335 -15.719  1.00133.80           C  
ANISOU  390  CG  LYS A1051    16854  18392  15592    784    568  -3993       C  
ATOM    391  CD  LYS A1051       7.358   5.537 -14.753  1.00128.76           C  
ANISOU  391  CD  LYS A1051    16152  17375  15397    968    734  -3966       C  
ATOM    392  CE  LYS A1051       8.743   5.258 -15.331  1.00139.34           C  
ANISOU  392  CE  LYS A1051    17479  18721  16743   1080    997  -4140       C  
ATOM    393  NZ  LYS A1051       9.841   5.742 -14.445  1.00140.28           N  
ANISOU  393  NZ  LYS A1051    17499  18734  17065   1276   1063  -3834       N  
ATOM    394  N   SER A1052       4.830   9.379 -17.779  1.00157.82           N  
ANISOU  394  N   SER A1052    20001  22467  17495    398     42  -3717       N  
ATOM    395  CA  SER A1052       3.759  10.290 -18.135  1.00161.26           C  
ANISOU  395  CA  SER A1052    20452  23156  17665    248   -237  -3579       C  
ATOM    396  C   SER A1052       2.767  10.475 -16.991  1.00158.50           C  
ANISOU  396  C   SER A1052    20017  22645  17562    284   -425  -3342       C  
ATOM    397  O   SER A1052       2.752   9.703 -16.030  1.00158.11           O  
ANISOU  397  O   SER A1052    19920  22283  17872    380   -341  -3339       O  
ATOM    398  CB  SER A1052       3.024   9.767 -19.367  1.00172.12           C  
ANISOU  398  CB  SER A1052    21935  24670  18794     17   -291  -3910       C  
ATOM    399  OG  SER A1052       2.355   8.550 -19.076  1.00166.91           O  
ANISOU  399  OG  SER A1052    21282  23733  18405    -26   -268  -4125       O  
ATOM    400  N   PRO A1053       1.925  11.511 -17.078  1.00130.20           N  
ANISOU  400  N   PRO A1053    16408  19273  13789    204   -681  -3138       N  
ATOM    401  CA  PRO A1053       0.967  11.772 -15.989  1.00130.75           C  
ANISOU  401  CA  PRO A1053    16383  19212  14082    246   -847  -2910       C  
ATOM    402  C   PRO A1053       0.056  10.596 -15.689  1.00130.12           C  
ANISOU  402  C   PRO A1053    16285  18896  14257    166   -841  -3099       C  
ATOM    403  O   PRO A1053      -0.215  10.304 -14.517  1.00129.52           O  
ANISOU  403  O   PRO A1053    16136  18581  14494    261   -826  -2964       O  
ATOM    404  CB  PRO A1053       0.179  12.986 -16.503  1.00131.23           C  
ANISOU  404  CB  PRO A1053    16433  19576  13853    138  -1125  -2745       C  
ATOM    405  CG  PRO A1053       1.109  13.668 -17.447  1.00129.07           C  
ANISOU  405  CG  PRO A1053    16233  19566  13241    115  -1092  -2744       C  
ATOM    406  CD  PRO A1053       1.891  12.567 -18.108  1.00128.06           C  
ANISOU  406  CD  PRO A1053    16187  19368  13101     86   -830  -3079       C  
ATOM    407  N   ASP A1054      -0.424   9.910 -16.723  1.00140.30           N  
ANISOU  407  N   ASP A1054    17648  20247  15412    -18   -858  -3405       N  
ATOM    408  CA  ASP A1054      -1.450   8.886 -16.585  1.00139.61           C  
ANISOU  408  CA  ASP A1054    17545  19973  15527   -134   -907  -3577       C  
ATOM    409  C   ASP A1054      -0.885   7.479 -16.446  1.00136.53           C  
ANISOU  409  C   ASP A1054    17204  19286  15386    -96   -678  -3843       C  
ATOM    410  O   ASP A1054      -1.662   6.519 -16.393  1.00129.56           O  
ANISOU  410  O   ASP A1054    16323  18228  14675   -203   -712  -4011       O  
ATOM    411  CB  ASP A1054      -2.389   8.946 -17.798  1.00141.46           C  
ANISOU  411  CB  ASP A1054    17841  20431  15478   -376  -1097  -3752       C  
ATOM    412  CG  ASP A1054      -3.593   8.038 -17.655  1.00135.40           C  
ANISOU  412  CG  ASP A1054    17041  19496  14909   -516  -1199  -3884       C  
ATOM    413  OD1 ASP A1054      -4.480   8.351 -16.835  1.00134.18           O  
ANISOU  413  OD1 ASP A1054    16760  19290  14931   -504  -1340  -3667       O  
ATOM    414  OD2 ASP A1054      -3.651   7.013 -18.367  1.00139.47           O  
ANISOU  414  OD2 ASP A1054    17657  19931  15406   -641  -1137  -4208       O  
ATOM    415  N   SER A1055       0.433   7.327 -16.371  1.00120.40           N  
ANISOU  415  N   SER A1055    15192  17170  13386     54   -455  -3878       N  
ATOM    416  CA  SER A1055       1.000   6.020 -16.087  1.00118.72           C  
ANISOU  416  CA  SER A1055    15003  16636  13468    120   -246  -4100       C  
ATOM    417  C   SER A1055       0.432   5.493 -14.769  1.00118.03           C  
ANISOU  417  C   SER A1055    14829  16242  13775    170   -288  -3951       C  
ATOM    418  O   SER A1055       0.149   6.271 -13.852  1.00118.56           O  
ANISOU  418  O   SER A1055    14811  16324  13910    245   -388  -3626       O  
ATOM    419  CB  SER A1055       2.522   6.099 -16.009  1.00123.31           C  
ANISOU  419  CB  SER A1055    15589  17178  14084    304    -16  -4087       C  
ATOM    420  OG  SER A1055       2.937   6.888 -14.908  1.00123.27           O  
ANISOU  420  OG  SER A1055    15496  17128  14213    470    -37  -3718       O  
ATOM    421  N   PRO A1056       0.254   4.176 -14.643  1.00124.46           N  
ANISOU  421  N   PRO A1056    15669  16771  14848    126   -214  -4182       N  
ATOM    422  CA  PRO A1056      -0.355   3.640 -13.414  1.00123.34           C  
ANISOU  422  CA  PRO A1056    15451  16346  15068    142   -264  -4035       C  
ATOM    423  C   PRO A1056       0.441   3.956 -12.163  1.00120.86           C  
ANISOU  423  C   PRO A1056    15073  15866  14983    345   -175  -3743       C  
ATOM    424  O   PRO A1056      -0.129   3.944 -11.064  1.00121.19           O  
ANISOU  424  O   PRO A1056    15046  15762  15239    358   -247  -3525       O  
ATOM    425  CB  PRO A1056      -0.416   2.128 -13.678  1.00125.73           C  
ANISOU  425  CB  PRO A1056    15815  16368  15587     64   -182  -4371       C  
ATOM    426  CG  PRO A1056       0.646   1.875 -14.693  1.00127.61           C  
ANISOU  426  CG  PRO A1056    16150  16667  15669    109     -4  -4651       C  
ATOM    427  CD  PRO A1056       0.687   3.104 -15.559  1.00127.09           C  
ANISOU  427  CD  PRO A1056    16109  17010  15171     70    -70  -4583       C  
ATOM    428  N   GLU A1057       1.739   4.238 -12.289  1.00128.79           N  
ANISOU  428  N   GLU A1057    16099  16890  15946    496    -21  -3727       N  
ATOM    429  CA  GLU A1057       2.534   4.581 -11.115  1.00127.38           C  
ANISOU  429  CA  GLU A1057    15868  16553  15978    681     43  -3434       C  
ATOM    430  C   GLU A1057       2.189   5.975 -10.605  1.00124.86           C  
ANISOU  430  C   GLU A1057    15500  16450  15492    722   -104  -3079       C  
ATOM    431  O   GLU A1057       2.137   6.201  -9.390  1.00124.38           O  
ANISOU  431  O   GLU A1057    15395  16239  15626    807   -137  -2808       O  
ATOM    432  CB  GLU A1057       4.024   4.482 -11.443  1.00130.10           C  
ANISOU  432  CB  GLU A1057    16234  16859  16339    825    243  -3517       C  
ATOM    433  CG  GLU A1057       4.472   3.105 -11.919  1.00128.65           C  
ANISOU  433  CG  GLU A1057    16094  16439  16349    816    407  -3882       C  
ATOM    434  CD  GLU A1057       4.144   2.846 -13.378  1.00126.17           C  
ANISOU  434  CD  GLU A1057    15862  16335  15743    669    424  -4238       C  
ATOM    435  OE1 GLU A1057       4.056   3.823 -14.152  1.00121.93           O  
ANISOU  435  OE1 GLU A1057    15348  16151  14831    615    366  -4200       O  
ATOM    436  OE2 GLU A1057       3.968   1.667 -13.749  1.00139.51           O  
ANISOU  436  OE2 GLU A1057    17602  17830  17574    600    485  -4553       O  
ATOM    437  N   MET A1058       1.947   6.925 -11.513  1.00127.74           N  
ANISOU  437  N   MET A1058    15879  17162  15493    658   -201  -3076       N  
ATOM    438  CA  MET A1058       1.514   8.250 -11.088  1.00124.83           C  
ANISOU  438  CA  MET A1058    15465  16994  14971    689   -367  -2757       C  
ATOM    439  C   MET A1058       0.071   8.244 -10.606  1.00120.89           C  
ANISOU  439  C   MET A1058    14906  16479  14546    584   -532  -2681       C  
ATOM    440  O   MET A1058      -0.353   9.188  -9.931  1.00116.83           O  
ANISOU  440  O   MET A1058    14339  16049  14003    635   -651  -2404       O  
ATOM    441  CB  MET A1058       1.666   9.248 -12.237  1.00127.21           C  
ANISOU  441  CB  MET A1058    15800  17663  14871    638   -443  -2773       C  
ATOM    442  CG  MET A1058       3.103   9.588 -12.577  1.00128.23           C  
ANISOU  442  CG  MET A1058    15963  17861  14899    757   -295  -2754       C  
ATOM    443  SD  MET A1058       3.971  10.351 -11.196  1.00118.71           S  
ANISOU  443  SD  MET A1058    14710  16520  13875    978   -278  -2352       S  
ATOM    444  CE  MET A1058       3.143  11.934 -11.079  1.00124.26           C  
ANISOU  444  CE  MET A1058    15387  17508  14318    955   -544  -2051       C  
ATOM    445  N   LYS A1059      -0.687   7.198 -10.940  1.00110.72           N  
ANISOU  445  N   LYS A1059    13624  15084  13361    437   -540  -2925       N  
ATOM    446  CA  LYS A1059      -2.033   7.049 -10.402  1.00109.82           C  
ANISOU  446  CA  LYS A1059    13433  14923  13369    334   -677  -2852       C  
ATOM    447  C   LYS A1059      -1.995   6.606  -8.945  1.00108.08           C  
ANISOU  447  C   LYS A1059    13169  14405  13491    424   -608  -2669       C  
ATOM    448  O   LYS A1059      -2.750   7.120  -8.112  1.00106.05           O  
ANISOU  448  O   LYS A1059    12837  14165  13293    432   -699  -2441       O  
ATOM    449  CB  LYS A1059      -2.801   6.040 -11.254  1.00112.73           C  
ANISOU  449  CB  LYS A1059    13827  15263  13740    136   -717  -3167       C  
ATOM    450  CG  LYS A1059      -3.213   6.578 -12.612  1.00114.36           C  
ANISOU  450  CG  LYS A1059    14073  15789  13590      0   -847  -3308       C  
ATOM    451  CD  LYS A1059      -4.037   5.566 -13.391  1.00117.68           C  
ANISOU  451  CD  LYS A1059    14530  16162  14021   -208   -909  -3608       C  
ATOM    452  CE  LYS A1059      -4.956   6.247 -14.385  1.00117.71           C  
ANISOU  452  CE  LYS A1059    14529  16472  13724   -375  -1127  -3638       C  
ATOM    453  NZ  LYS A1059      -5.407   5.326 -15.464  1.00130.03           N  
ANISOU  453  NZ  LYS A1059    16181  18023  15200   -579  -1171  -3978       N  
ATOM    454  N   ASP A1060      -1.111   5.660  -8.620  1.00109.54           N  
ANISOU  454  N   ASP A1060    13402  14313  13904    490   -447  -2766       N  
ATOM    455  CA  ASP A1060      -0.921   5.263  -7.230  1.00104.33           C  
ANISOU  455  CA  ASP A1060    12720  13361  13559    573   -387  -2572       C  
ATOM    456  C   ASP A1060      -0.228   6.350  -6.419  1.00102.79           C  
ANISOU  456  C   ASP A1060    12523  13211  13322    746   -380  -2249       C  
ATOM    457  O   ASP A1060      -0.420   6.429  -5.201  1.00 97.45           O  
ANISOU  457  O   ASP A1060    11824  12384  12820    793   -389  -2017       O  
ATOM    458  CB  ASP A1060      -0.118   3.962  -7.176  1.00104.11           C  
ANISOU  458  CB  ASP A1060    12744  13015  13797    595   -239  -2767       C  
ATOM    459  CG  ASP A1060      -0.063   3.364  -5.786  1.00103.55           C  
ANISOU  459  CG  ASP A1060    12657  12614  14071    634   -204  -2589       C  
ATOM    460  OD1 ASP A1060      -0.753   3.882  -4.883  1.00103.72           O  
ANISOU  460  OD1 ASP A1060    12632  12662  14114    624   -282  -2337       O  
ATOM    461  OD2 ASP A1060       0.671   2.370  -5.598  1.00109.77           O  
ANISOU  461  OD2 ASP A1060    13483  13115  15111    671    -98  -2702       O  
ATOM    462  N   PHE A1061       0.573   7.196  -7.070  1.00116.86           N  
ANISOU  462  N   PHE A1061    14335  15199  14866    832   -368  -2225       N  
ATOM    463  CA  PHE A1061       1.226   8.294  -6.364  1.00116.39           C  
ANISOU  463  CA  PHE A1061    14281  15194  14749    988   -386  -1913       C  
ATOM    464  C   PHE A1061       0.208   9.315  -5.869  1.00107.24           C  
ANISOU  464  C   PHE A1061    13071  14201  13473    975   -546  -1686       C  
ATOM    465  O   PHE A1061       0.133   9.607  -4.669  1.00 93.84           O  
ANISOU  465  O   PHE A1061    11368  12378  11908   1051   -557  -1441       O  
ATOM    466  CB  PHE A1061       2.262   8.960  -7.275  1.00117.01           C  
ANISOU  466  CB  PHE A1061    14395  15476  14588   1061   -348  -1945       C  
ATOM    467  CG  PHE A1061       2.666  10.334  -6.825  1.00114.89           C  
ANISOU  467  CG  PHE A1061    14129  15353  14171   1182   -432  -1628       C  
ATOM    468  CD1 PHE A1061       3.620  10.501  -5.835  1.00116.49           C  
ANISOU  468  CD1 PHE A1061    14355  15367  14540   1331   -372  -1402       C  
ATOM    469  CD2 PHE A1061       2.097  11.460  -7.396  1.00114.75           C  
ANISOU  469  CD2 PHE A1061    14095  15649  13854   1142   -589  -1552       C  
ATOM    470  CE1 PHE A1061       3.991  11.764  -5.416  1.00110.71           C  
ANISOU  470  CE1 PHE A1061    13638  14757  13670   1438   -464  -1110       C  
ATOM    471  CE2 PHE A1061       2.466  12.726  -6.983  1.00112.77           C  
ANISOU  471  CE2 PHE A1061    13854  15518  13476   1254   -683  -1264       C  
ATOM    472  CZ  PHE A1061       3.414  12.876  -5.991  1.00111.23           C  
ANISOU  472  CZ  PHE A1061    13690  15133  13441   1403   -618  -1045       C  
ATOM    473  N   ARG A1062      -0.588   9.872  -6.784  1.00102.09           N  
ANISOU  473  N   ARG A1062    12386  13830  12574    876   -673  -1768       N  
ATOM    474  CA  ARG A1062      -1.609  10.834  -6.385  1.00 94.47           C  
ANISOU  474  CA  ARG A1062    11353  13023  11518    868   -831  -1574       C  
ATOM    475  C   ARG A1062      -2.645  10.204  -5.464  1.00 90.59           C  
ANISOU  475  C   ARG A1062    10795  12358  11267    801   -831  -1539       C  
ATOM    476  O   ARG A1062      -3.219  10.894  -4.613  1.00 86.04           O  
ANISOU  476  O   ARG A1062    10169  11809  10711    851   -896  -1318       O  
ATOM    477  CB  ARG A1062      -2.282  11.430  -7.621  1.00 91.09           C  
ANISOU  477  CB  ARG A1062    10895  12908  10805    755   -984  -1686       C  
ATOM    478  CG  ARG A1062      -1.468  12.527  -8.293  1.00 90.52           C  
ANISOU  478  CG  ARG A1062    10874  13069  10452    828  -1039  -1601       C  
ATOM    479  CD  ARG A1062      -2.141  13.016  -9.565  1.00 95.17           C  
ANISOU  479  CD  ARG A1062    11446  13955  10758    687  -1202  -1722       C  
ATOM    480  NE  ARG A1062      -2.298  11.939 -10.539  1.00105.82           N  
ANISOU  480  NE  ARG A1062    12829  15290  12086    531  -1144  -2049       N  
ATOM    481  CZ  ARG A1062      -1.418  11.645 -11.492  1.00101.61           C  
ANISOU  481  CZ  ARG A1062    12382  14824  11401    504  -1046  -2238       C  
ATOM    482  NH1 ARG A1062      -0.297  12.344 -11.620  1.00103.12           N  
ANISOU  482  NH1 ARG A1062    12619  15110  11451    618   -994  -2122       N  
ATOM    483  NH2 ARG A1062      -1.661  10.641 -12.323  1.00107.56           N  
ANISOU  483  NH2 ARG A1062    13176  15550  12141    359   -998  -2548       N  
ATOM    484  N   HIS A1063      -2.902   8.903  -5.615  1.00 92.56           N  
ANISOU  484  N   HIS A1063    11043  12429  11698    685   -759  -1754       N  
ATOM    485  CA  HIS A1063      -3.871   8.247  -4.746  1.00 89.10           C  
ANISOU  485  CA  HIS A1063    10537  11824  11494    603   -757  -1714       C  
ATOM    486  C   HIS A1063      -3.383   8.188  -3.305  1.00 85.66           C  
ANISOU  486  C   HIS A1063    10133  11152  11263    716   -665  -1478       C  
ATOM    487  O   HIS A1063      -4.193   8.277  -2.375  1.00 82.92           O  
ANISOU  487  O   HIS A1063     9727  10759  11020    693   -684  -1325       O  
ATOM    488  CB  HIS A1063      -4.169   6.837  -5.255  1.00 91.86           C  
ANISOU  488  CB  HIS A1063    10891  12015  11997    448   -714  -1995       C  
ATOM    489  CG  HIS A1063      -5.132   6.078  -4.397  1.00 94.90           C  
ANISOU  489  CG  HIS A1063    11205  12221  12631    342   -714  -1953       C  
ATOM    490  ND1 HIS A1063      -6.498   6.180  -4.542  1.00 99.85           N  
ANISOU  490  ND1 HIS A1063    11718  12982  13237    207   -830  -1962       N  
ATOM    491  CD2 HIS A1063      -4.925   5.207  -3.382  1.00 99.80           C  
ANISOU  491  CD2 HIS A1063    11848  12540  13532    341   -619  -1890       C  
ATOM    492  CE1 HIS A1063      -7.092   5.403  -3.653  1.00100.68           C  
ANISOU  492  CE1 HIS A1063    11773  12888  13593    127   -791  -1908       C  
ATOM    493  NE2 HIS A1063      -6.160   4.801  -2.937  1.00107.04           N  
ANISOU  493  NE2 HIS A1063    12667  13426  14577    201   -668  -1862       N  
ATOM    494  N   GLY A1064      -2.075   8.037  -3.097  1.00 88.22           N  
ANISOU  494  N   GLY A1064    10548  11325  11646    833   -566  -1443       N  
ATOM    495  CA  GLY A1064      -1.554   7.999  -1.743  1.00 75.87           C  
ANISOU  495  CA  GLY A1064     9030   9528  10268    931   -500  -1206       C  
ATOM    496  C   GLY A1064      -1.915   9.230  -0.938  1.00 65.31           C  
ANISOU  496  C   GLY A1064     7680   8319   8816   1018   -572   -923       C  
ATOM    497  O   GLY A1064      -2.106   9.148   0.278  1.00 64.47           O  
ANISOU  497  O   GLY A1064     7590   8051   8854   1036   -540   -738       O  
ATOM    498  N   PHE A1065      -2.018  10.384  -1.598  1.00 64.49           N  
ANISOU  498  N   PHE A1065     7555   8501   8448   1069   -674   -886       N  
ATOM    499  CA  PHE A1065      -2.383  11.615  -0.909  1.00 67.96           C  
ANISOU  499  CA  PHE A1065     7983   9065   8772   1163   -757   -635       C  
ATOM    500  C   PHE A1065      -3.887  11.774  -0.738  1.00 75.81           C  
ANISOU  500  C   PHE A1065     8859  10176   9769   1070   -826   -637       C  
ATOM    501  O   PHE A1065      -4.317  12.587   0.087  1.00 73.64           O  
ANISOU  501  O   PHE A1065     8568   9947   9466   1144   -862   -436       O  
ATOM    502  CB  PHE A1065      -1.797  12.818  -1.648  1.00 79.83           C  
ANISOU  502  CB  PHE A1065     9515  10807  10009   1261   -855   -575       C  
ATOM    503  CG  PHE A1065      -0.296  12.805  -1.714  1.00 92.59           C  
ANISOU  503  CG  PHE A1065    11231  12324  11626   1364   -785   -530       C  
ATOM    504  CD1 PHE A1065       0.454  13.362  -0.693  1.00 86.57           C  
ANISOU  504  CD1 PHE A1065    10548  11438  10905   1501   -777   -269       C  
ATOM    505  CD2 PHE A1065       0.364  12.222  -2.781  1.00 96.01           C  
ANISOU  505  CD2 PHE A1065    11675  12779  12024   1323   -725   -749       C  
ATOM    506  CE1 PHE A1065       1.831  13.349  -0.740  1.00 92.48           C  
ANISOU  506  CE1 PHE A1065    11371  12090  11677   1592   -722   -212       C  
ATOM    507  CE2 PHE A1065       1.744  12.207  -2.831  1.00 99.01           C  
ANISOU  507  CE2 PHE A1065    12122  13070  12425   1423   -647   -706       C  
ATOM    508  CZ  PHE A1065       2.477  12.771  -1.809  1.00 95.74           C  
ANISOU  508  CZ  PHE A1065    11772  12535  12072   1557   -651   -430       C  
ATOM    509  N   ASP A1066      -4.697  11.024  -1.488  1.00 70.78           N  
ANISOU  509  N   ASP A1066     8138   9586   9171    913   -846   -859       N  
ATOM    510  CA  ASP A1066      -6.128  11.018  -1.210  1.00 66.14           C  
ANISOU  510  CA  ASP A1066     7418   9072   8642    814   -898   -850       C  
ATOM    511  C   ASP A1066      -6.414  10.253   0.075  1.00 66.24           C  
ANISOU  511  C   ASP A1066     7428   8839   8902    778   -781   -752       C  
ATOM    512  O   ASP A1066      -7.241  10.679   0.890  1.00 65.85           O  
ANISOU  512  O   ASP A1066     7305   8827   8886    787   -782   -606       O  
ATOM    513  CB  ASP A1066      -6.904  10.412  -2.380  1.00 82.31           C  
ANISOU  513  CB  ASP A1066     9381  11228  10667    640   -971  -1104       C  
ATOM    514  CG  ASP A1066      -6.820  11.256  -3.640  1.00 83.08           C  
ANISOU  514  CG  ASP A1066     9476  11598  10493    647  -1110  -1184       C  
ATOM    515  OD1 ASP A1066      -6.645  12.488  -3.523  1.00 78.89           O  
ANISOU  515  OD1 ASP A1066     8950  11220   9804    771  -1188  -1013       O  
ATOM    516  OD2 ASP A1066      -6.940  10.690  -4.748  1.00 83.89           O  
ANISOU  516  OD2 ASP A1066     9580  11760  10535    519  -1151  -1416       O  
ATOM    517  N   ILE A1067      -5.738   9.119   0.273  1.00 66.94           N  
ANISOU  517  N   ILE A1067     7595   8671   9168    735   -678   -831       N  
ATOM    518  CA  ILE A1067      -5.824   8.417   1.549  1.00 66.95           C  
ANISOU  518  CA  ILE A1067     7622   8418   9398    701   -577   -706       C  
ATOM    519  C   ILE A1067      -5.345   9.323   2.676  1.00 64.69           C  
ANISOU  519  C   ILE A1067     7418   8100   9062    853   -549   -426       C  
ATOM    520  O   ILE A1067      -5.899   9.313   3.783  1.00 64.50           O  
ANISOU  520  O   ILE A1067     7380   8000   9126    831   -498   -272       O  
ATOM    521  CB  ILE A1067      -5.011   7.108   1.499  1.00 68.08           C  
ANISOU  521  CB  ILE A1067     7849   8276   9744    646   -498   -833       C  
ATOM    522  CG1 ILE A1067      -5.532   6.191   0.388  1.00 79.14           C  
ANISOU  522  CG1 ILE A1067     9185   9697  11188    489   -532  -1126       C  
ATOM    523  CG2 ILE A1067      -5.061   6.399   2.850  1.00 69.00           C  
ANISOU  523  CG2 ILE A1067     8004   8118  10095    597   -414   -679       C  
ATOM    524  CD1 ILE A1067      -4.622   5.012   0.088  1.00 92.87           C  
ANISOU  524  CD1 ILE A1067    11010  11177  13099    463   -464  -1298       C  
ATOM    525  N   LEU A1068      -4.308  10.120   2.414  1.00 63.10           N  
ANISOU  525  N   LEU A1068     7306   7956   8712   1003   -581   -356       N  
ATOM    526  CA  LEU A1068      -3.766  10.997   3.445  1.00 61.01           C  
ANISOU  526  CA  LEU A1068     7140   7647   8393   1148   -573    -91       C  
ATOM    527  C   LEU A1068      -4.761  12.089   3.821  1.00 60.31           C  
ANISOU  527  C   LEU A1068     6980   7765   8171   1192   -633     32       C  
ATOM    528  O   LEU A1068      -5.043  12.303   5.005  1.00 59.70           O  
ANISOU  528  O   LEU A1068     6938   7605   8141   1219   -581    209       O  
ATOM    529  CB  LEU A1068      -2.449  11.610   2.969  1.00 59.66           C  
ANISOU  529  CB  LEU A1068     7068   7505   8096   1286   -612    -47       C  
ATOM    530  CG  LEU A1068      -1.514  12.079   4.083  1.00 57.83           C  
ANISOU  530  CG  LEU A1068     6977   7109   7886   1413   -592    215       C  
ATOM    531  CD1 LEU A1068      -0.874  10.886   4.773  1.00 58.45           C  
ANISOU  531  CD1 LEU A1068     7131   6856   8222   1362   -493    232       C  
ATOM    532  CD2 LEU A1068      -0.454  13.023   3.541  1.00 63.91           C  
ANISOU  532  CD2 LEU A1068     7810   7990   8482   1552   -665    286       C  
ATOM    533  N   VAL A1069      -5.308  12.789   2.824  1.00 60.57           N  
ANISOU  533  N   VAL A1069     6913   8064   8036   1197   -745    -64       N  
ATOM    534  CA  VAL A1069      -6.264  13.856   3.111  1.00 65.38           C  
ANISOU  534  CA  VAL A1069     7435   8866   8539   1251   -815     40       C  
ATOM    535  C   VAL A1069      -7.489  13.295   3.821  1.00 61.96           C  
ANISOU  535  C   VAL A1069     6887   8391   8264   1139   -736     37       C  
ATOM    536  O   VAL A1069      -8.042  13.927   4.731  1.00 60.96           O  
ANISOU  536  O   VAL A1069     6738   8297   8127   1202   -708    187       O  
ATOM    537  CB  VAL A1069      -6.650  14.594   1.815  1.00 61.19           C  
ANISOU  537  CB  VAL A1069     6809   8614   7825   1252   -973    -71       C  
ATOM    538  CG1 VAL A1069      -7.791  15.569   2.080  1.00 60.48           C  
ANISOU  538  CG1 VAL A1069     6596   8707   7678   1295  -1053     13       C  
ATOM    539  CG2 VAL A1069      -5.446  15.327   1.243  1.00 59.07           C  
ANISOU  539  CG2 VAL A1069     6658   8411   7377   1369  -1049    -23       C  
ATOM    540  N   GLY A1070      -7.938  12.107   3.415  1.00 63.35           N  
ANISOU  540  N   GLY A1070     6987   8496   8589    969   -697   -135       N  
ATOM    541  CA  GLY A1070      -9.062  11.485   4.093  1.00 64.82           C  
ANISOU  541  CA  GLY A1070     7057   8632   8939    842   -619   -128       C  
ATOM    542  C   GLY A1070      -8.811  11.300   5.577  1.00 64.12           C  
ANISOU  542  C   GLY A1070     7071   8342   8948    870   -486     67       C  
ATOM    543  O   GLY A1070      -9.710  11.495   6.398  1.00 64.59           O  
ANISOU  543  O   GLY A1070     7052   8441   9048    847   -421    165       O  
ATOM    544  N   GLN A1071      -7.582  10.924   5.940  1.00 66.26           N  
ANISOU  544  N   GLN A1071     7519   8397   9259    915   -443    130       N  
ATOM    545  CA  GLN A1071      -7.242  10.775   7.351  1.00 62.48           C  
ANISOU  545  CA  GLN A1071     7167   7715   8859    933   -339    334       C  
ATOM    546  C   GLN A1071      -7.077  12.132   8.022  1.00 63.64           C  
ANISOU  546  C   GLN A1071     7392   7960   8830   1107   -357    530       C  
ATOM    547  O   GLN A1071      -7.419  12.294   9.200  1.00 65.24           O  
ANISOU  547  O   GLN A1071     7639   8101   9047   1108   -271    686       O  
ATOM    548  CB  GLN A1071      -5.966   9.948   7.499  1.00 63.99           C  
ANISOU  548  CB  GLN A1071     7514   7630   9170    925   -312    346       C  
ATOM    549  CG  GLN A1071      -6.077   8.527   6.966  1.00 74.46           C  
ANISOU  549  CG  GLN A1071     8785   8811  10697    757   -290    153       C  
ATOM    550  CD  GLN A1071      -4.765   7.768   7.047  1.00 73.96           C  
ANISOU  550  CD  GLN A1071     8862   8470  10770    774   -271    153       C  
ATOM    551  OE1 GLN A1071      -4.473   7.118   8.050  1.00 77.85           O  
ANISOU  551  OE1 GLN A1071     9445   8711  11422    716   -214    280       O  
ATOM    552  NE2 GLN A1071      -3.968   7.846   5.988  1.00 67.05           N  
ANISOU  552  NE2 GLN A1071     8002   7638   9837    849   -320     13       N  
ATOM    553  N   ILE A1072      -6.545  13.118   7.295  1.00 64.46           N  
ANISOU  553  N   ILE A1072     7521   8212   8759   1248   -471    525       N  
ATOM    554  CA  ILE A1072      -6.424  14.460   7.853  1.00 63.56           C  
ANISOU  554  CA  ILE A1072     7481   8193   8477   1416   -515    701       C  
ATOM    555  C   ILE A1072      -7.798  15.065   8.116  1.00 64.77           C  
ANISOU  555  C   ILE A1072     7481   8534   8593   1419   -502    704       C  
ATOM    556  O   ILE A1072      -7.976  15.823   9.077  1.00 65.42           O  
ANISOU  556  O   ILE A1072     7626   8623   8607   1516   -465    858       O  
ATOM    557  CB  ILE A1072      -5.591  15.351   6.914  1.00 66.30           C  
ANISOU  557  CB  ILE A1072     7873   8666   8651   1546   -659    693       C  
ATOM    558  CG1 ILE A1072      -4.151  14.838   6.835  1.00 63.91           C  
ANISOU  558  CG1 ILE A1072     7721   8165   8397   1565   -649    722       C  
ATOM    559  CG2 ILE A1072      -5.615  16.798   7.398  1.00 70.60           C  
ANISOU  559  CG2 ILE A1072     8477   9323   9024   1715   -734    862       C  
ATOM    560  CD1 ILE A1072      -3.316  15.504   5.758  1.00 63.78           C  
ANISOU  560  CD1 ILE A1072     7727   8281   8227   1658   -770    685       C  
ATOM    561  N   ASP A1073      -8.788  14.748   7.277  1.00 61.59           N  
ANISOU  561  N   ASP A1073     6876   8285   8241   1315   -534    532       N  
ATOM    562  CA  ASP A1073     -10.136  15.263   7.500  1.00 61.15           C  
ANISOU  562  CA  ASP A1073     6643   8405   8189   1314   -521    531       C  
ATOM    563  C   ASP A1073     -10.813  14.558   8.669  1.00 62.40           C  
ANISOU  563  C   ASP A1073     6770   8446   8491   1207   -342    596       C  
ATOM    564  O   ASP A1073     -11.510  15.198   9.467  1.00 64.59           O  
ANISOU  564  O   ASP A1073     7001   8799   8740   1269   -272    690       O  
ATOM    565  CB  ASP A1073     -10.975  15.116   6.230  1.00 62.63           C  
ANISOU  565  CB  ASP A1073     6619   8781   8396   1221   -630    341       C  
ATOM    566  CG  ASP A1073     -10.594  16.121   5.158  1.00 61.64           C  
ANISOU  566  CG  ASP A1073     6497   8832   8090   1332   -819    305       C  
ATOM    567  OD1 ASP A1073     -10.016  17.172   5.505  1.00 59.95           O  
ANISOU  567  OD1 ASP A1073     6399   8641   7739   1502   -868    442       O  
ATOM    568  OD2 ASP A1073     -10.885  15.865   3.969  1.00 62.67           O  
ANISOU  568  OD2 ASP A1073     6523   9079   8209   1240   -927    144       O  
ATOM    569  N   ASP A1074     -10.630  13.241   8.785  1.00 64.03           N  
ANISOU  569  N   ASP A1074     7004   8469   8856   1042   -265    546       N  
ATOM    570  CA  ASP A1074     -11.202  12.520   9.917  1.00 65.90           C  
ANISOU  570  CA  ASP A1074     7229   8585   9226    918   -102    627       C  
ATOM    571  C   ASP A1074     -10.685  13.076  11.237  1.00 66.67           C  
ANISOU  571  C   ASP A1074     7520   8574   9236   1022    -12    840       C  
ATOM    572  O   ASP A1074     -11.435  13.172  12.216  1.00 68.04           O  
ANISOU  572  O   ASP A1074     7660   8770   9424    990    119    929       O  
ATOM    573  CB  ASP A1074     -10.886  11.030   9.804  1.00 67.35           C  
ANISOU  573  CB  ASP A1074     7444   8552   9593    731    -68    553       C  
ATOM    574  CG  ASP A1074     -11.642  10.358   8.674  1.00 77.62           C  
ANISOU  574  CG  ASP A1074     8547   9949  10995    590   -136    343       C  
ATOM    575  OD1 ASP A1074     -12.581  10.978   8.130  1.00 92.71           O  
ANISOU  575  OD1 ASP A1074    10275  12094  12856    611   -194    277       O  
ATOM    576  OD2 ASP A1074     -11.292   9.210   8.325  1.00 78.64           O  
ANISOU  576  OD2 ASP A1074     8710   9909  11262    459   -143    243       O  
ATOM    577  N   ALA A1075      -9.402  13.447  11.284  1.00 71.91           N  
ANISOU  577  N   ALA A1075     8393   9122   9806   1141    -80    924       N  
ATOM    578  CA  ALA A1075      -8.845  14.036  12.497  1.00 60.29           C  
ANISOU  578  CA  ALA A1075     7130   7541   8237   1240    -25   1132       C  
ATOM    579  C   ALA A1075      -9.361  15.455  12.709  1.00 64.57           C  
ANISOU  579  C   ALA A1075     7640   8284   8608   1412    -48   1186       C  
ATOM    580  O   ALA A1075      -9.662  15.848  13.842  1.00 67.54           O  
ANISOU  580  O   ALA A1075     8097   8639   8928   1445     61   1312       O  
ATOM    581  CB  ALA A1075      -7.319  14.025  12.429  1.00 64.21           C  
ANISOU  581  CB  ALA A1075     7842   7853   8703   1314   -111   1213       C  
ATOM    582  N   LEU A1076      -9.473  16.238  11.632  1.00 67.39           N  
ANISOU  582  N   LEU A1076     7888   8836   8881   1519   -192   1089       N  
ATOM    583  CA  LEU A1076      -9.997  17.594  11.756  1.00 70.47           C  
ANISOU  583  CA  LEU A1076     8234   9410   9133   1686   -239   1129       C  
ATOM    584  C   LEU A1076     -11.407  17.593  12.329  1.00 70.64           C  
ANISOU  584  C   LEU A1076     8072   9545   9222   1637    -98   1102       C  
ATOM    585  O   LEU A1076     -11.783  18.520  13.056  1.00 74.04           O  
ANISOU  585  O   LEU A1076     8530  10041   9562   1764    -50   1181       O  
ATOM    586  CB  LEU A1076      -9.985  18.290  10.396  1.00 74.27           C  
ANISOU  586  CB  LEU A1076     8600  10081   9536   1770   -435   1021       C  
ATOM    587  CG  LEU A1076      -8.719  19.062  10.031  1.00 77.20           C  
ANISOU  587  CG  LEU A1076     9154  10422   9755   1912   -589   1104       C  
ATOM    588  CD1 LEU A1076      -8.665  19.321   8.535  1.00 76.41           C  
ANISOU  588  CD1 LEU A1076     8936  10494   9604   1916   -764    972       C  
ATOM    589  CD2 LEU A1076      -8.659  20.372  10.802  1.00 81.63           C  
ANISOU  589  CD2 LEU A1076     9830  11013  10172   2098   -624   1253       C  
ATOM    590  N   LYS A1077     -12.199  16.567  12.014  1.00 64.43           N  
ANISOU  590  N   LYS A1077     7098   8782   8601   1454    -29    988       N  
ATOM    591  CA  LYS A1077     -13.545  16.472  12.568  1.00 71.32           C  
ANISOU  591  CA  LYS A1077     7775   9762   9561   1388    119    970       C  
ATOM    592  C   LYS A1077     -13.496  16.342  14.084  1.00 71.10           C  
ANISOU  592  C   LYS A1077     7906   9604   9507   1367    316   1123       C  
ATOM    593  O   LYS A1077     -14.216  17.041  14.806  1.00 70.30           O  
ANISOU  593  O   LYS A1077     7752   9605   9353   1448    426   1167       O  
ATOM    594  CB  LYS A1077     -14.269  15.276  11.947  1.00 72.42           C  
ANISOU  594  CB  LYS A1077     7706   9920   9891   1170    139    837       C  
ATOM    595  CG  LYS A1077     -15.755  15.187  12.269  1.00 78.64           C  
ANISOU  595  CG  LYS A1077     8231  10856  10793   1090    264    804       C  
ATOM    596  CD  LYS A1077     -16.624  15.550  11.062  1.00 80.53           C  
ANISOU  596  CD  LYS A1077     8197  11314  11088   1101    116    659       C  
ATOM    597  CE  LYS A1077     -17.780  14.568  10.874  1.00 91.03           C  
ANISOU  597  CE  LYS A1077     9268  12695  12623    884    183    576       C  
ATOM    598  NZ  LYS A1077     -19.114  15.232  10.981  1.00 86.66           N  
ANISOU  598  NZ  LYS A1077     8434  12355  12137    933    230    561       N  
ATOM    599  N   LEU A1078     -12.642  15.446  14.583  1.00 74.66           N  
ANISOU  599  N   LEU A1078     8554   9822   9993   1254    361   1204       N  
ATOM    600  CA  LEU A1078     -12.489  15.284  16.024  1.00 73.76           C  
ANISOU  600  CA  LEU A1078     8626   9564   9837   1211    527   1367       C  
ATOM    601  C   LEU A1078     -11.949  16.554  16.670  1.00 74.79           C  
ANISOU  601  C   LEU A1078     8962   9695   9761   1422    504   1489       C  
ATOM    602  O   LEU A1078     -12.400  16.949  17.751  1.00 78.29           O  
ANISOU  602  O   LEU A1078     9467  10155  10124   1447    655   1574       O  
ATOM    603  CB  LEU A1078     -11.568  14.098  16.310  1.00 66.69           C  
ANISOU  603  CB  LEU A1078     7907   8398   9034   1053    530   1436       C  
ATOM    604  CG  LEU A1078     -12.079  12.748  15.804  1.00 66.25           C  
ANISOU  604  CG  LEU A1078     7678   8302   9193    829    555   1323       C  
ATOM    605  CD1 LEU A1078     -10.956  11.728  15.743  1.00 65.65           C  
ANISOU  605  CD1 LEU A1078     7772   7952   9219    728    490   1356       C  
ATOM    606  CD2 LEU A1078     -13.210  12.245  16.688  1.00 68.63           C  
ANISOU  606  CD2 LEU A1078     7864   8644   9568    666    752   1365       C  
ATOM    607  N   ALA A1079     -10.985  17.211  16.018  1.00 71.62           N  
ANISOU  607  N   ALA A1079     8672   9275   9267   1571    316   1498       N  
ATOM    608  CA  ALA A1079     -10.414  18.431  16.581  1.00 72.64           C  
ANISOU  608  CA  ALA A1079     9006   9389   9203   1768    262   1620       C  
ATOM    609  C   ALA A1079     -11.444  19.552  16.634  1.00 78.37           C  
ANISOU  609  C   ALA A1079     9586  10338   9855   1917    290   1566       C  
ATOM    610  O   ALA A1079     -11.454  20.347  17.581  1.00 80.96           O  
ANISOU  610  O   ALA A1079    10061  10650  10048   2031    355   1661       O  
ATOM    611  CB  ALA A1079      -9.195  18.863  15.766  1.00 78.16           C  
ANISOU  611  CB  ALA A1079     9826  10037   9835   1879     44   1642       C  
ATOM    612  N   ASN A1080     -12.315  19.637  15.627  1.00 85.60           N  
ANISOU  612  N   ASN A1080    10213  11453  10860   1918    234   1411       N  
ATOM    613  CA  ASN A1080     -13.353  20.661  15.646  1.00 84.61           C  
ANISOU  613  CA  ASN A1080     9913  11531  10705   2059    252   1354       C  
ATOM    614  C   ASN A1080     -14.377  20.394  16.740  1.00 85.48           C  
ANISOU  614  C   ASN A1080     9943  11674  10863   1989    514   1366       C  
ATOM    615  O   ASN A1080     -15.004  21.333  17.243  1.00 84.31           O  
ANISOU  615  O   ASN A1080     9750  11633  10651   2135    584   1363       O  
ATOM    616  CB  ASN A1080     -14.043  20.744  14.285  1.00 83.97           C  
ANISOU  616  CB  ASN A1080     9536  11642  10727   2054    110   1197       C  
ATOM    617  CG  ASN A1080     -13.256  21.565  13.284  1.00 81.43           C  
ANISOU  617  CG  ASN A1080     9280  11361  10299   2192   -151   1190       C  
ATOM    618  OD1 ASN A1080     -13.392  22.787  13.226  1.00 81.82           O  
ANISOU  618  OD1 ASN A1080     9326  11507  10255   2378   -255   1208       O  
ATOM    619  ND2 ASN A1080     -12.431  20.897  12.487  1.00 80.95           N  
ANISOU  619  ND2 ASN A1080     9277  11225  10254   2098   -258   1163       N  
ATOM    620  N   GLU A1081     -14.559  19.131  17.118  1.00 80.37           N  
ANISOU  620  N   GLU A1081    10180  11328   9028   1832    970   -274       N  
ATOM    621  CA  GLU A1081     -15.454  18.762  18.205  1.00 80.93           C  
ANISOU  621  CA  GLU A1081    10278  11597   8875   1866    963   -309       C  
ATOM    622  C   GLU A1081     -14.799  18.880  19.575  1.00 82.38           C  
ANISOU  622  C   GLU A1081    10457  11879   8963   1859    850   -436       C  
ATOM    623  O   GLU A1081     -15.415  18.494  20.574  1.00 92.30           O  
ANISOU  623  O   GLU A1081    11745  13310  10013   1877    838   -464       O  
ATOM    624  CB  GLU A1081     -15.966  17.334  17.999  1.00 81.88           C  
ANISOU  624  CB  GLU A1081    10424  11826   8860   1852    997   -127       C  
ATOM    625  CG  GLU A1081     -16.875  17.176  16.792  1.00 83.51           C  
ANISOU  625  CG  GLU A1081    10651  11960   9120   1867   1102     -5       C  
ATOM    626  CD  GLU A1081     -17.294  15.738  16.555  1.00 89.89           C  
ANISOU  626  CD  GLU A1081    11487  12861   9807   1850   1120    180       C  
ATOM    627  OE1 GLU A1081     -16.695  14.829  17.167  1.00 80.12           O  
ANISOU  627  OE1 GLU A1081    10251  11718   8473   1819   1047    227       O  
ATOM    628  OE2 GLU A1081     -18.226  15.518  15.753  1.00119.20           O  
ANISOU  628  OE2 GLU A1081    15223  16543  13525   1865   1195    280       O  
ATOM    629  N   GLY A1082     -13.573  19.393  19.647  1.00 80.80           N  
ANISOU  629  N   GLY A1082    10223  11572   8907   1829    765   -511       N  
ATOM    630  CA  GLY A1082     -12.883  19.490  20.917  1.00 76.00           C  
ANISOU  630  CA  GLY A1082     9617  11041   8219   1819    638   -628       C  
ATOM    631  C   GLY A1082     -12.349  18.182  21.447  1.00 72.77           C  
ANISOU  631  C   GLY A1082     9216  10743   7689   1782    560   -528       C  
ATOM    632  O   GLY A1082     -12.087  18.072  22.647  1.00 86.58           O  
ANISOU  632  O   GLY A1082    10993  12599   9304   1778    458   -609       O  
ATOM    633  N   LYS A1083     -12.177  17.181  20.585  1.00 71.43           N  
ANISOU  633  N   LYS A1083     9031  10546   7563   1756    598   -355       N  
ATOM    634  CA  LYS A1083     -11.675  15.869  20.992  1.00 80.90           C  
ANISOU  634  CA  LYS A1083    10239  11839   8662   1722    518   -248       C  
ATOM    635  C   LYS A1083     -10.189  15.806  20.650  1.00 71.91           C  
ANISOU  635  C   LYS A1083     9032  10569   7722   1684    435   -241       C  
ATOM    636  O   LYS A1083      -9.765  15.187  19.675  1.00 70.69           O  
ANISOU  636  O   LYS A1083     8843  10333   7681   1665    473   -116       O  
ATOM    637  CB  LYS A1083     -12.474  14.759  20.318  1.00 87.00           C  
ANISOU  637  CB  LYS A1083    11041  12669   9348   1723    603    -65       C  
ATOM    638  CG  LYS A1083     -13.973  14.856  20.566  1.00 86.75           C  
ANISOU  638  CG  LYS A1083    11058  12756   9147   1759    695    -66       C  
ATOM    639  CD  LYS A1083     -14.741  13.760  19.845  1.00 92.33           C  
ANISOU  639  CD  LYS A1083    11790  13504   9786   1755    769    123       C  
ATOM    640  CE  LYS A1083     -16.226  13.833  20.164  1.00 97.98           C  
ANISOU  640  CE  LYS A1083    12540  14348  10341   1786    855    122       C  
ATOM    641  NZ  LYS A1083     -17.043  12.984  19.253  1.00 96.86           N  
ANISOU  641  NZ  LYS A1083    12416  14206  10180   1784    933    301       N  
ATOM    642  N   VAL A1084      -9.391  16.475  21.486  1.00 72.82           N  
ANISOU  642  N   VAL A1084     9125  10663   7881   1673    318   -384       N  
ATOM    643  CA  VAL A1084      -7.962  16.615  21.216  1.00 73.21           C  
ANISOU  643  CA  VAL A1084     9092  10578   8147   1635    235   -402       C  
ATOM    644  C   VAL A1084      -7.270  15.257  21.217  1.00 72.84           C  
ANISOU  644  C   VAL A1084     9023  10568   8086   1608    163   -275       C  
ATOM    645  O   VAL A1084      -6.454  14.961  20.335  1.00 72.29           O  
ANISOU  645  O   VAL A1084     8882  10384   8203   1587    183   -202       O  
ATOM    646  CB  VAL A1084      -7.324  17.576  22.239  1.00 76.81           C  
ANISOU  646  CB  VAL A1084     9537  11011   8635   1629    103   -583       C  
ATOM    647  CG1 VAL A1084      -7.472  17.037  23.660  1.00 80.13           C  
ANISOU  647  CG1 VAL A1084    10029  11599   8817   1632    -21   -627       C  
ATOM    648  CG2 VAL A1084      -5.857  17.814  21.905  1.00 84.46           C  
ANISOU  648  CG2 VAL A1084    10404  11830   9858   1587     22   -602       C  
ATOM    649  N   LYS A1085      -7.580  14.407  22.199  1.00 73.23           N  
ANISOU  649  N   LYS A1085     9136  10774   7914   1607     78   -248       N  
ATOM    650  CA  LYS A1085      -6.892  13.123  22.290  1.00 73.05           C  
ANISOU  650  CA  LYS A1085     9099  10781   7878   1582    -17   -136       C  
ATOM    651  C   LYS A1085      -7.322  12.185  21.170  1.00 71.40           C  
ANISOU  651  C   LYS A1085     8891  10559   7678   1589     97     40       C  
ATOM    652  O   LYS A1085      -6.500  11.433  20.634  1.00 71.00           O  
ANISOU  652  O   LYS A1085     8788  10443   7746   1575     65    127       O  
ATOM    653  CB  LYS A1085      -7.139  12.486  23.656  1.00 74.29           C  
ANISOU  653  CB  LYS A1085     9339  11104   7784   1572   -146   -150       C  
ATOM    654  CG  LYS A1085      -6.544  13.280  24.811  1.00 89.73           C  
ANISOU  654  CG  LYS A1085    11304  13063   9728   1563   -289   -320       C  
ATOM    655  CD  LYS A1085      -6.668  12.546  26.140  1.00 93.01           C  
ANISOU  655  CD  LYS A1085    11814  13635   9891   1544   -429   -322       C  
ATOM    656  CE  LYS A1085      -5.670  11.401  26.254  1.00 92.87           C  
ANISOU  656  CE  LYS A1085    11767  13598   9920   1511   -579   -227       C  
ATOM    657  NZ  LYS A1085      -4.256  11.877  26.237  1.00 89.78           N  
ANISOU  657  NZ  LYS A1085    11276  13059   9777   1495   -702   -311       N  
ATOM    658  N   GLU A1086      -8.604  12.211  20.800  1.00 76.41           N  
ANISOU  658  N   GLU A1086     9586  11251   8194   1613    226     92       N  
ATOM    659  CA  GLU A1086      -9.057  11.387  19.684  1.00 76.22           C  
ANISOU  659  CA  GLU A1086     9574  11201   8184   1620    330    256       C  
ATOM    660  C   GLU A1086      -8.404  11.830  18.381  1.00 73.78           C  
ANISOU  660  C   GLU A1086     9196  10709   8129   1619    417    275       C  
ATOM    661  O   GLU A1086      -8.075  10.999  17.527  1.00 72.76           O  
ANISOU  661  O   GLU A1086     9051  10524   8069   1616    449    398       O  
ATOM    662  CB  GLU A1086     -10.580  11.447  19.561  1.00 76.97           C  
ANISOU  662  CB  GLU A1086     9740  11384   8120   1645    444    298       C  
ATOM    663  CG  GLU A1086     -11.324  10.718  20.666  1.00 80.33           C  
ANISOU  663  CG  GLU A1086    10237  12003   8281   1638    386    327       C  
ATOM    664  CD  GLU A1086     -11.579  11.588  21.879  1.00 81.99           C  
ANISOU  664  CD  GLU A1086    10472  12304   8377   1646    345    164       C  
ATOM    665  OE1 GLU A1086     -12.599  11.359  22.560  1.00 85.17           O  
ANISOU  665  OE1 GLU A1086    10936  12859   8565   1651    370    172       O  
ATOM    666  OE2 GLU A1086     -10.769  12.500  22.148  1.00 80.45           O  
ANISOU  666  OE2 GLU A1086    10235  12026   8305   1646    288     27       O  
ATOM    667  N   ALA A1087      -8.210  13.139  18.210  1.00 68.80           N  
ANISOU  667  N   ALA A1087     8528   9980   7634   1620    457    153       N  
ATOM    668  CA  ALA A1087      -7.539  13.632  17.014  1.00 68.38           C  
ANISOU  668  CA  ALA A1087     8412   9751   7820   1607    540    167       C  
ATOM    669  C   ALA A1087      -6.079  13.198  16.986  1.00 69.98           C  
ANISOU  669  C   ALA A1087     8524   9887   8180   1579    454    174       C  
ATOM    670  O   ALA A1087      -5.554  12.833  15.928  1.00 73.25           O  
ANISOU  670  O   ALA A1087     8896  10200   8736   1571    527    260       O  
ATOM    671  CB  ALA A1087      -7.648  15.154  16.943  1.00 68.99           C  
ANISOU  671  CB  ALA A1087     8472   9738   8002   1608    583     32       C  
ATOM    672  N   GLN A1088      -5.404  13.240  18.138  1.00 70.23           N  
ANISOU  672  N   GLN A1088     8523   9970   8192   1565    299     81       N  
ATOM    673  CA  GLN A1088      -4.015  12.797  18.192  1.00 70.91           C  
ANISOU  673  CA  GLN A1088     8513   9994   8436   1541    199     83       C  
ATOM    674  C   GLN A1088      -3.891  11.325  17.823  1.00 70.10           C  
ANISOU  674  C   GLN A1088     8419   9931   8286   1550    189    232       C  
ATOM    675  O   GLN A1088      -2.973  10.936  17.092  1.00 70.01           O  
ANISOU  675  O   GLN A1088     8325   9822   8452   1543    209    281       O  
ATOM    676  CB  GLN A1088      -3.438  13.053  19.584  1.00 72.50           C  
ANISOU  676  CB  GLN A1088     8698  10250   8597   1526     13    -40       C  
ATOM    677  CG  GLN A1088      -3.254  14.523  19.913  1.00 73.53           C  
ANISOU  677  CG  GLN A1088     8803  10311   8826   1514     -2   -198       C  
ATOM    678  CD  GLN A1088      -2.845  14.755  21.353  1.00 85.22           C  
ANISOU  678  CD  GLN A1088    10298  11856  10228   1504   -193   -321       C  
ATOM    679  OE1 GLN A1088      -3.095  13.922  22.225  1.00 86.04           O  
ANISOU  679  OE1 GLN A1088    10468  12089  10134   1510   -294   -294       O  
ATOM    680  NE2 GLN A1088      -2.202  15.888  21.609  1.00 99.14           N  
ANISOU  680  NE2 GLN A1088    12005  13522  12143   1485   -251   -455       N  
ATOM    681  N   ALA A1089      -4.811  10.491  18.312  1.00 69.60           N  
ANISOU  681  N   ALA A1089     8453  10006   7986   1566    161    304       N  
ATOM    682  CA  ALA A1089      -4.792   9.080  17.944  1.00 68.82           C  
ANISOU  682  CA  ALA A1089     8375   9940   7832   1576    145    452       C  
ATOM    683  C   ALA A1089      -4.979   8.904  16.443  1.00 69.19           C  
ANISOU  683  C   ALA A1089     8419   9885   7985   1592    311    555       C  
ATOM    684  O   ALA A1089      -4.309   8.073  15.819  1.00 68.99           O  
ANISOU  684  O   ALA A1089     8353   9802   8056   1599    311    637       O  
ATOM    685  CB  ALA A1089      -5.876   8.325  18.712  1.00 68.55           C  
ANISOU  685  CB  ALA A1089     8454  10073   7519   1581     97    515       C  
ATOM    686  N   ALA A1090      -5.888   9.679  15.847  1.00 80.72           N  
ANISOU  686  N   ALA A1090     9926  11316   9428   1600    451    550       N  
ATOM    687  CA  ALA A1090      -6.092   9.608  14.404  1.00 79.70           C  
ANISOU  687  CA  ALA A1090     9811  11078   9393   1611    605    644       C  
ATOM    688  C   ALA A1090      -4.836  10.001  13.637  1.00 72.18           C  
ANISOU  688  C   ALA A1090     8755   9973   8696   1594    652    614       C  
ATOM    689  O   ALA A1090      -4.566   9.447  12.566  1.00 81.29           O  
ANISOU  689  O   ALA A1090     9906  11049   9932   1603    739    709       O  
ATOM    690  CB  ALA A1090      -7.262  10.502  13.995  1.00 84.06           C  
ANISOU  690  CB  ALA A1090    10431  11616   9893   1620    724    628       C  
ATOM    691  N   ALA A1091      -4.059  10.952  14.163  1.00 70.79           N  
ANISOU  691  N   ALA A1091     8495   9754   8649   1568    596    481       N  
ATOM    692  CA  ALA A1091      -2.806  11.334  13.522  1.00 67.91           C  
ANISOU  692  CA  ALA A1091     8014   9251   8538   1543    635    450       C  
ATOM    693  C   ALA A1091      -1.792  10.199  13.521  1.00 79.10           C  
ANISOU  693  C   ALA A1091     9357  10668  10031   1550    560    504       C  
ATOM    694  O   ALA A1091      -0.888  10.190  12.678  1.00 79.46           O  
ANISOU  694  O   ALA A1091     9315  10602  10274   1540    635    521       O  
ATOM    695  CB  ALA A1091      -2.212  12.561  14.214  1.00 73.33           C  
ANISOU  695  CB  ALA A1091     8624   9896   9341   1510    565    297       C  
ATOM    696  N   GLU A1092      -1.915   9.244  14.446  1.00 78.92           N  
ANISOU  696  N   GLU A1092     9365  10763   9856   1568    415    530       N  
ATOM    697  CA  GLU A1092      -1.053   8.068  14.402  1.00 79.55           C  
ANISOU  697  CA  GLU A1092     9387  10840   9999   1583    335    591       C  
ATOM    698  C   GLU A1092      -1.274   7.285  13.116  1.00 78.15           C  
ANISOU  698  C   GLU A1092     9249  10611   9835   1612    472    722       C  
ATOM    699  O   GLU A1092      -0.335   6.687  12.580  1.00 78.08           O  
ANISOU  699  O   GLU A1092     9160  10534   9975   1625    482    754       O  
ATOM    700  CB  GLU A1092      -1.307   7.175  15.616  1.00 84.23           C  
ANISOU  700  CB  GLU A1092    10035  11570  10398   1591    149    608       C  
ATOM    701  CG  GLU A1092      -0.944   7.822  16.940  1.00 82.44           C  
ANISOU  701  CG  GLU A1092     9778  11391  10155   1564     -8    477       C  
ATOM    702  CD  GLU A1092       0.528   8.163  17.032  1.00 94.62           C  
ANISOU  702  CD  GLU A1092    11167  12831  11954   1546    -84    392       C  
ATOM    703  OE1 GLU A1092       1.359   7.331  16.607  1.00100.24           O  
ANISOU  703  OE1 GLU A1092    11801  13493  12793   1561   -109    445       O  
ATOM    704  OE2 GLU A1092       0.854   9.267  17.517  1.00103.10           O  
ANISOU  704  OE2 GLU A1092    12195  13871  13109   1517   -121    270       O  
ATOM    705  N   GLN A1093      -2.508   7.278  12.611  1.00 90.90           N  
ANISOU  705  N   GLN A1093    10987  12253  11298   1624    576    797       N  
ATOM    706  CA  GLN A1093      -2.803   6.601  11.358  1.00 90.57           C  
ANISOU  706  CA  GLN A1093    11003  12152  11257   1651    703    921       C  
ATOM    707  C   GLN A1093      -2.098   7.259  10.178  1.00 89.19           C  
ANISOU  707  C   GLN A1093    10763  11826  11300   1638    862    904       C  
ATOM    708  O   GLN A1093      -1.889   6.603   9.152  1.00 89.25           O  
ANISOU  708  O   GLN A1093    10788  11768  11357   1661    955    990       O  
ATOM    709  CB  GLN A1093      -4.316   6.609  11.127  1.00 91.75           C  
ANISOU  709  CB  GLN A1093    11295  12356  11209   1661    769    994       C  
ATOM    710  CG  GLN A1093      -5.136   6.110  12.316  1.00 93.09           C  
ANISOU  710  CG  GLN A1093    11531  12685  11154   1664    635   1007       C  
ATOM    711  CD  GLN A1093      -6.637   6.234  12.092  1.00108.13           C  
ANISOU  711  CD  GLN A1093    13554  14641  12887   1671    711   1070       C  
ATOM    712  OE1 GLN A1093      -7.089   7.005  11.243  1.00102.49           O  
ANISOU  712  OE1 GLN A1093    12870  13844  12229   1671    845   1068       O  
ATOM    713  NE2 GLN A1093      -7.417   5.491  12.871  1.00108.73           N  
ANISOU  713  NE2 GLN A1093    13699  14855  12761   1674    619   1125       N  
ATOM    714  N   LEU A1094      -1.722   8.535  10.304  1.00 80.05           N  
ANISOU  714  N   LEU A1094     9536  10610  10270   1599    894    794       N  
ATOM    715  CA  LEU A1094      -0.979   9.204   9.240  1.00 71.93           C  
ANISOU  715  CA  LEU A1094     8439   9438   9454   1573   1042    778       C  
ATOM    716  C   LEU A1094       0.434   8.650   9.114  1.00 72.44           C  
ANISOU  716  C   LEU A1094     8361   9454   9707   1576   1017    766       C  
ATOM    717  O   LEU A1094       0.956   8.524   8.000  1.00 68.83           O  
ANISOU  717  O   LEU A1094     7875   8900   9379   1576   1158    810       O  
ATOM    718  CB  LEU A1094      -0.956  10.711   9.486  1.00 74.43           C  
ANISOU  718  CB  LEU A1094     8719   9703   9857   1526   1063    665       C  
ATOM    719  CG  LEU A1094      -2.288  11.430   9.282  1.00 72.44           C  
ANISOU  719  CG  LEU A1094     8597   9458   9470   1525   1131    673       C  
ATOM    720  CD1 LEU A1094      -2.200  12.877   9.707  1.00 78.84           C  
ANISOU  720  CD1 LEU A1094     9365  10223  10366   1484   1116    547       C  
ATOM    721  CD2 LEU A1094      -2.675  11.355   7.808  1.00 75.90           C  
ANISOU  721  CD2 LEU A1094     9118   9796   9925   1527   1310    777       C  
ATOM    722  N   LYS A1095       1.076   8.316  10.238  1.00 78.93           N  
ANISOU  722  N   LYS A1095     9096  10341  10552   1578    838    704       N  
ATOM    723  CA  LYS A1095       2.414   7.742  10.148  1.00 74.59           C  
ANISOU  723  CA  LYS A1095     8401   9744  10196   1587    799    691       C  
ATOM    724  C   LYS A1095       2.388   6.422   9.390  1.00 70.45           C  
ANISOU  724  C   LYS A1095     7921   9218   9628   1641    848    806       C  
ATOM    725  O   LYS A1095       3.385   6.044   8.764  1.00 69.96           O  
ANISOU  725  O   LYS A1095     7754   9082   9745   1655    908    812       O  
ATOM    726  CB  LYS A1095       3.038   7.549  11.532  1.00 70.51           C  
ANISOU  726  CB  LYS A1095     7799   9294   9698   1583    571    610       C  
ATOM    727  CG  LYS A1095       3.330   8.845  12.281  1.00 80.15           C  
ANISOU  727  CG  LYS A1095     8954  10497  11002   1531    507    481       C  
ATOM    728  CD  LYS A1095       4.284   8.596  13.451  1.00 84.12           C  
ANISOU  728  CD  LYS A1095     9345  11028  11587   1525    286    402       C  
ATOM    729  CE  LYS A1095       3.612   7.986  14.666  1.00 90.74           C  
ANISOU  729  CE  LYS A1095    10292  12003  12182   1544     99    407       C  
ATOM    730  NZ  LYS A1095       3.111   9.046  15.583  1.00 91.44           N  
ANISOU  730  NZ  LYS A1095    10432  12136  12176   1511     30    308       N  
ATOM    731  N   THR A1096       1.260   5.711   9.430  1.00 72.04           N  
ANISOU  731  N   THR A1096     8276   9499   9598   1673    824    897       N  
ATOM    732  CA  THR A1096       1.158   4.458   8.693  1.00 68.32           C  
ANISOU  732  CA  THR A1096     7865   9019   9076   1725    861   1009       C  
ATOM    733  C   THR A1096       1.182   4.712   7.191  1.00 71.80           C  
ANISOU  733  C   THR A1096     8336   9343   9601   1728   1087   1058       C  
ATOM    734  O   THR A1096       1.844   3.984   6.443  1.00 70.67           O  
ANISOU  734  O   THR A1096     8155   9142   9554   1764   1151   1098       O  
ATOM    735  CB  THR A1096      -0.118   3.715   9.090  1.00 74.92           C  
ANISOU  735  CB  THR A1096     8860   9962   9644   1748    781   1099       C  
ATOM    736  OG1 THR A1096      -0.103   3.445  10.497  1.00 66.09           O  
ANISOU  736  OG1 THR A1096     7722   8953   8435   1739    574   1057       O  
ATOM    737  CG2 THR A1096      -0.240   2.405   8.322  1.00 81.19           C  
ANISOU  737  CG2 THR A1096     9726  10738  10385   1802    804   1219       C  
ATOM    738  N   THR A1097       0.462   5.739   6.730  1.00 77.59           N  
ANISOU  738  N   THR A1097     9144  10038  10298   1692   1209   1054       N  
ATOM    739  CA  THR A1097       0.480   6.058   5.307  1.00 73.66           C  
ANISOU  739  CA  THR A1097     8692   9423   9874   1685   1420   1101       C  
ATOM    740  C   THR A1097       1.800   6.704   4.900  1.00 79.00           C  
ANISOU  740  C   THR A1097     9207  10001  10808   1649   1515   1026       C  
ATOM    741  O   THR A1097       2.293   6.471   3.790  1.00 80.80           O  
ANISOU  741  O   THR A1097     9428  10142  11132   1658   1670   1068       O  
ATOM    742  CB  THR A1097      -0.688   6.987   4.969  1.00 65.80           C  
ANISOU  742  CB  THR A1097     7826   8407   8769   1654   1502   1118       C  
ATOM    743  OG1 THR A1097      -1.914   6.409   5.436  1.00 71.51           O  
ANISOU  743  OG1 THR A1097     8678   9230   9264   1684   1410   1183       O  
ATOM    744  CG2 THR A1097      -0.775   7.222   3.466  1.00 66.60           C  
ANISOU  744  CG2 THR A1097     8007   8383   8916   1645   1708   1183       C  
ATOM    745  N   ARG A1098       2.389   7.519   5.780  1.00 81.13           N  
ANISOU  745  N   ARG A1098     9349  10282  11193   1606   1427    917       N  
ATOM    746  CA  ARG A1098       3.702   8.085   5.483  1.00 80.05           C  
ANISOU  746  CA  ARG A1098     9039  10056  11319   1567   1500    847       C  
ATOM    747  C   ARG A1098       4.756   6.994   5.330  1.00 75.15           C  
ANISOU  747  C   ARG A1098     8302   9430  10823   1614   1480    860       C  
ATOM    748  O   ARG A1098       5.635   7.090   4.465  1.00 79.59           O  
ANISOU  748  O   ARG A1098     8770   9903  11568   1602   1629    856       O  
ATOM    749  CB  ARG A1098       4.086   9.103   6.561  1.00 80.02           C  
ANISOU  749  CB  ARG A1098     8928  10069  11408   1515   1375    728       C  
ATOM    750  CG  ARG A1098       5.516   9.616   6.468  1.00 71.95           C  
ANISOU  750  CG  ARG A1098     7702   8964  10672   1472   1407    651       C  
ATOM    751  CD  ARG A1098       6.367   9.071   7.601  1.00 73.03           C  
ANISOU  751  CD  ARG A1098     7697   9157  10894   1492   1199    586       C  
ATOM    752  NE  ARG A1098       6.123   9.820   8.834  1.00 73.38           N  
ANISOU  752  NE  ARG A1098     7740   9253  10890   1460   1026    497       N  
ATOM    753  CZ  ARG A1098       6.302   9.349  10.065  1.00 73.86           C  
ANISOU  753  CZ  ARG A1098     7767   9395  10901   1481    803    451       C  
ATOM    754  NH1 ARG A1098       6.063  10.134  11.106  1.00 74.27           N  
ANISOU  754  NH1 ARG A1098     7832   9485  10903   1449    667    365       N  
ATOM    755  NH2 ARG A1098       6.699   8.100  10.265  1.00 73.99           N  
ANISOU  755  NH2 ARG A1098     7749   9453  10910   1534    711    490       N  
ATOM    756  N   ASN A1099       4.688   5.948   6.157  1.00 74.25           N  
ANISOU  756  N   ASN A1099     8192   9406  10613   1666   1299    874       N  
ATOM    757  CA  ASN A1099       5.605   4.825   5.989  1.00 76.84           C  
ANISOU  757  CA  ASN A1099     8422   9723  11049   1721   1268    890       C  
ATOM    758  C   ASN A1099       5.422   4.149   4.636  1.00 82.71           C  
ANISOU  758  C   ASN A1099     9257  10409  11759   1766   1450    985       C  
ATOM    759  O   ASN A1099       6.395   3.665   4.047  1.00 87.43           O  
ANISOU  759  O   ASN A1099     9748  10951  12523   1796   1528    978       O  
ATOM    760  CB  ASN A1099       5.416   3.812   7.116  1.00 75.49           C  
ANISOU  760  CB  ASN A1099     8273   9657  10753   1765   1026    900       C  
ATOM    761  CG  ASN A1099       5.758   4.385   8.476  1.00 75.80           C  
ANISOU  761  CG  ASN A1099     8219   9747  10834   1725    834    800       C  
ATOM    762  OD1 ASN A1099       6.070   5.570   8.603  1.00 72.00           O  
ANISOU  762  OD1 ASN A1099     7662   9225  10471   1666    875    721       O  
ATOM    763  ND2 ASN A1099       5.708   3.545   9.502  1.00 84.18           N  
ANISOU  763  ND2 ASN A1099     9295  10894  11797   1754    616    805       N  
ATOM    764  N   ALA A1100       4.188   4.106   4.129  1.00 89.76           N  
ANISOU  764  N   ALA A1100    10348  11313  12443   1772   1517   1070       N  
ATOM    765  CA  ALA A1100       3.948   3.494   2.827  1.00 90.71           C  
ANISOU  765  CA  ALA A1100    10580  11370  12515   1813   1682   1162       C  
ATOM    766  C   ALA A1100       4.577   4.309   1.706  1.00 95.45           C  
ANISOU  766  C   ALA A1100    11129  11855  13283   1771   1917   1141       C  
ATOM    767  O   ALA A1100       4.979   3.747   0.681  1.00 96.69           O  
ANISOU  767  O   ALA A1100    11302  11949  13489   1808   2059   1183       O  
ATOM    768  CB  ALA A1100       2.446   3.338   2.589  1.00 95.64           C  
ANISOU  768  CB  ALA A1100    11427  12026  12885   1822   1683   1257       C  
ATOM    769  N   TYR A1101       4.670   5.628   1.883  1.00 93.07           N  
ANISOU  769  N   TYR A1101    10773  11523  13068   1693   1960   1077       N  
ATOM    770  CA  TYR A1101       5.229   6.478   0.839  1.00 93.67           C  
ANISOU  770  CA  TYR A1101    10808  11486  13297   1638   2181   1065       C  
ATOM    771  C   TYR A1101       6.732   6.265   0.704  1.00101.15           C  
ANISOU  771  C   TYR A1101    11539  12395  14499   1641   2234   1005       C  
ATOM    772  O   TYR A1101       7.254   6.151  -0.411  1.00100.31           O  
ANISOU  772  O   TYR A1101    11421  12212  14481   1643   2434   1032       O  
ATOM    773  CB  TYR A1101       4.916   7.946   1.138  1.00 94.00           C  
ANISOU  773  CB  TYR A1101    10849  11502  13366   1551   2188   1011       C  
ATOM    774  CG  TYR A1101       5.965   8.915   0.638  1.00 94.81           C  
ANISOU  774  CG  TYR A1101    10807  11508  13709   1476   2334    955       C  
ATOM    775  CD1 TYR A1101       5.955   9.368  -0.675  1.00 94.94           C  
ANISOU  775  CD1 TYR A1101    10902  11419  13750   1435   2564   1006       C  
ATOM    776  CD2 TYR A1101       6.966   9.379   1.483  1.00 98.80           C  
ANISOU  776  CD2 TYR A1101    11102  12022  14415   1439   2236    854       C  
ATOM    777  CE1 TYR A1101       6.915  10.255  -1.134  1.00 95.01           C  
ANISOU  777  CE1 TYR A1101    10780  11342  13978   1356   2703    962       C  
ATOM    778  CE2 TYR A1101       7.930  10.264   1.035  1.00 99.64           C  
ANISOU  778  CE2 TYR A1101    11068  12039  14752   1363   2366    808       C  
ATOM    779  CZ  TYR A1101       7.901  10.699  -0.274  1.00100.35           C  
ANISOU  779  CZ  TYR A1101    11235  12032  14862   1320   2604    864       C  
ATOM    780  OH  TYR A1101       8.861  11.580  -0.720  1.00 97.73           O  
ANISOU  780  OH  TYR A1101    10763  11613  14758   1234   2739    826       O  
ATOM    781  N   ILE A1102       7.449   6.216   1.829  1.00116.06           N  
ANISOU  781  N   ILE A1102    13253  14335  16509   1642   2058    923       N  
ATOM    782  CA  ILE A1102       8.902   6.137   1.744  1.00117.89           C  
ANISOU  782  CA  ILE A1102    13256  14524  17014   1638   2102    858       C  
ATOM    783  C   ILE A1102       9.352   4.793   1.180  1.00118.14           C  
ANISOU  783  C   ILE A1102    13271  14553  17065   1730   2146    898       C  
ATOM    784  O   ILE A1102      10.437   4.693   0.593  1.00119.59           O  
ANISOU  784  O   ILE A1102    13302  14679  17459   1735   2279    867       O  
ATOM    785  CB  ILE A1102       9.535   6.389   3.125  1.00118.87           C  
ANISOU  785  CB  ILE A1102    13206  14696  17264   1618   1876    760       C  
ATOM    786  CG1 ILE A1102       9.035   5.362   4.146  1.00118.08           C  
ANISOU  786  CG1 ILE A1102    13169  14698  16996   1687   1633    775       C  
ATOM    787  CG2 ILE A1102       9.198   7.794   3.608  1.00118.87           C  
ANISOU  787  CG2 ILE A1102    13214  14682  17267   1529   1847    708       C  
ATOM    788  CD1 ILE A1102       9.749   5.430   5.486  1.00119.22           C  
ANISOU  788  CD1 ILE A1102    13151  14884  17262   1676   1397    683       C  
ATOM    789  N   GLN A1103       8.541   3.742   1.338  1.00106.63           N  
ANISOU  789  N   GLN A1103    11965  13155  15395   1804   2039    966       N  
ATOM    790  CA  GLN A1103       8.884   2.460   0.730  1.00102.88           C  
ANISOU  790  CA  GLN A1103    11499  12668  14924   1896   2081   1007       C  
ATOM    791  C   GLN A1103       8.648   2.479  -0.774  1.00106.00           C  
ANISOU  791  C   GLN A1103    12023  12982  15271   1902   2346   1074       C  
ATOM    792  O   GLN A1103       9.481   1.995  -1.550  1.00105.04           O  
ANISOU  792  O   GLN A1103    11822  12808  15279   1943   2488   1065       O  
ATOM    793  CB  GLN A1103       8.070   1.335   1.372  1.00 93.96           C  
ANISOU  793  CB  GLN A1103    10500  11619  13580   1967   1872   1066       C  
ATOM    794  CG  GLN A1103       8.528   0.948   2.765  1.00 90.33           C  
ANISOU  794  CG  GLN A1103     9910  11233  13180   1982   1606   1005       C  
ATOM    795  CD  GLN A1103       7.909  -0.352   3.269  1.00 93.90           C  
ANISOU  795  CD  GLN A1103    10480  11754  13443   2055   1413   1070       C  
ATOM    796  OE1 GLN A1103       8.434  -0.979   4.190  1.00 90.44           O  
ANISOU  796  OE1 GLN A1103     9942  11358  13064   2086   1206   1033       O  
ATOM    797  NE2 GLN A1103       6.794  -0.759   2.670  1.00 95.60           N  
ANISOU  797  NE2 GLN A1103    10912  11977  13434   2078   1469   1172       N  
ATOM    798  N   LYS A1104       7.519   3.045  -1.199  1.00109.39           N  
ANISOU  798  N   LYS A1104    12653  13397  15514   1861   2415   1139       N  
ATOM    799  CA  LYS A1104       7.109   2.950  -2.595  1.00111.78           C  
ANISOU  799  CA  LYS A1104    13126  13623  15724   1871   2634   1217       C  
ATOM    800  C   LYS A1104       7.933   3.866  -3.490  1.00111.07           C  
ANISOU  800  C   LYS A1104    12945  13440  15816   1802   2880   1183       C  
ATOM    801  O   LYS A1104       8.308   3.478  -4.603  1.00116.25           O  
ANISOU  801  O   LYS A1104    13639  14033  16499   1831   3074   1212       O  
ATOM    802  CB  LYS A1104       5.620   3.270  -2.721  1.00118.20           C  
ANISOU  802  CB  LYS A1104    14178  14444  16289   1847   2608   1297       C  
ATOM    803  N   TYR A1105       8.229   5.081  -3.025  1.00109.65           N  
ANISOU  803  N   TYR A1105    12651  13250  15762   1709   2876   1121       N  
ATOM    804  CA  TYR A1105       8.714   6.127  -3.915  1.00110.25           C  
ANISOU  804  CA  TYR A1105    12693  13232  15966   1621   3108   1111       C  
ATOM    805  C   TYR A1105      10.033   6.752  -3.480  1.00109.54           C  
ANISOU  805  C   TYR A1105    12326  13128  16167   1564   3123   1013       C  
ATOM    806  O   TYR A1105      10.802   7.212  -4.330  1.00105.81           O  
ANISOU  806  O   TYR A1105    11774  12582  15848   1513   3340   1004       O  
ATOM    807  CB  TYR A1105       7.644   7.221  -4.039  1.00105.63           C  
ANISOU  807  CB  TYR A1105    12278  12615  15243   1542   3122   1147       C  
ATOM    808  CG  TYR A1105       6.386   6.754  -4.733  1.00109.76           C  
ANISOU  808  CG  TYR A1105    13076  13123  15505   1583   3152   1252       C  
ATOM    809  CD1 TYR A1105       5.385   6.096  -4.032  1.00112.85           C  
ANISOU  809  CD1 TYR A1105    13579  13596  15704   1644   2955   1287       C  
ATOM    810  CD2 TYR A1105       6.203   6.963  -6.092  1.00115.29           C  
ANISOU  810  CD2 TYR A1105    13929  13725  16153   1557   3376   1318       C  
ATOM    811  CE1 TYR A1105       4.236   5.659  -4.665  1.00114.22           C  
ANISOU  811  CE1 TYR A1105    13995  13751  15654   1679   2974   1386       C  
ATOM    812  CE2 TYR A1105       5.057   6.531  -6.734  1.00119.20           C  
ANISOU  812  CE2 TYR A1105    14679  14196  16416   1595   3389   1415       C  
ATOM    813  CZ  TYR A1105       4.077   5.880  -6.016  1.00114.86           C  
ANISOU  813  CZ  TYR A1105    14223  13725  15692   1656   3185   1448       C  
ATOM    814  OH  TYR A1105       2.934   5.449  -6.651  1.00112.94           O  
ANISOU  814  OH  TYR A1105    14225  13454  15233   1690   3190   1547       O  
ATOM    815  N   LEU A1106      10.317   6.784  -2.182  1.00123.19           N  
ANISOU  815  N   LEU A1106    13907  14923  17975   1567   2896    942       N  
ATOM    816  CA  LEU A1106      11.506   7.467  -1.681  1.00128.07           C  
ANISOU  816  CA  LEU A1106    14265  15522  18873   1506   2879    848       C  
ATOM    817  C   LEU A1106      12.676   6.491  -1.711  1.00129.50           C  
ANISOU  817  C   LEU A1106    14249  15711  19243   1577   2889    808       C  
ATOM    818  O   LEU A1106      12.715   5.532  -0.931  1.00124.66           O  
ANISOU  818  O   LEU A1106    13600  15165  18601   1659   2690    790       O  
ATOM    819  CB  LEU A1106      11.280   8.006  -0.272  1.00126.16           C  
ANISOU  819  CB  LEU A1106    13968  15337  18629   1475   2623    784       C  
ATOM    820  CG  LEU A1106      12.423   8.866   0.273  1.00100.46           C  
ANISOU  820  CG  LEU A1106    10462  12049  15661   1398   2587    689       C  
ATOM    821  CD1 LEU A1106      12.473  10.197  -0.467  1.00 81.39           C  
ANISOU  821  CD1 LEU A1106     8060   9543  13323   1284   2779    696       C  
ATOM    822  CD2 LEU A1106      12.286   9.092   1.769  1.00 95.27           C  
ANISOU  822  CD2 LEU A1106     9750  11456  14991   1394   2299    619       C  
ATOM    823  N   GLY A 900      13.625   6.732  -2.613  1.00112.90           N  
ANISOU  823  N   GLY A 900    12021  13541  17336   1544   3121    794       N  
ATOM    824  CA  GLY A 900      14.820   5.918  -2.698  1.00114.57           C  
ANISOU  824  CA  GLY A 900    12018  13752  17763   1608   3155    745       C  
ATOM    825  C   GLY A 900      14.785   4.884  -3.805  1.00114.51           C  
ANISOU  825  C   GLY A 900    12114  13726  17668   1698   3334    799       C  
ATOM    826  O   GLY A 900      14.167   5.096  -4.852  1.00113.83           O  
ANISOU  826  O   GLY A 900    12227  13596  17427   1676   3530    871       O  
ATOM    827  N   SER A 901      15.449   3.749  -3.572  1.00105.21           N  
ANISOU  827  N   SER A 901    10809  12577  16589   1803   3257    761       N  
ATOM    828  CA  SER A 901      15.578   2.723  -4.599  1.00106.14           C  
ANISOU  828  CA  SER A 901    10998  12673  16656   1899   3424    794       C  
ATOM    829  C   SER A 901      14.242   2.102  -4.991  1.00114.06           C  
ANISOU  829  C   SER A 901    12320  13691  17327   1956   3395    892       C  
ATOM    830  O   SER A 901      14.154   1.468  -6.048  1.00110.31           O  
ANISOU  830  O   SER A 901    11965  13179  16767   2017   3570    935       O  
ATOM    831  CB  SER A 901      16.529   1.628  -4.110  1.00105.48           C  
ANISOU  831  CB  SER A 901    10707  12616  16756   2007   3300    725       C  
ATOM    832  OG  SER A 901      16.165   1.185  -2.812  1.00107.95           O  
ANISOU  832  OG  SER A 901    11019  12994  17003   2044   2969    710       O  
ATOM    833  N   GLY A 902      13.201   2.275  -4.175  1.00109.23           N  
ANISOU  833  N   GLY A 902    11847  13129  16526   1937   3182    927       N  
ATOM    834  CA  GLY A 902      11.959   1.554  -4.395  1.00111.46           C  
ANISOU  834  CA  GLY A 902    12404  13433  16512   1998   3115   1018       C  
ATOM    835  C   GLY A 902      11.152   2.024  -5.588  1.00112.64           C  
ANISOU  835  C   GLY A 902    12792  13520  16486   1956   3332   1102       C  
ATOM    836  O   GLY A 902      10.287   1.282  -6.065  1.00108.36           O  
ANISOU  836  O   GLY A 902    12472  12975  15725   2019   3324   1180       O  
ATOM    837  N   SER A 903      11.415   3.232  -6.087  1.00107.43           N  
ANISOU  837  N   SER A 903    12096  12802  15919   1848   3516   1091       N  
ATOM    838  CA  SER A 903      10.546   3.807  -7.108  1.00108.45           C  
ANISOU  838  CA  SER A 903    12469  12867  15870   1794   3687   1173       C  
ATOM    839  C   SER A 903      10.761   3.192  -8.486  1.00111.93           C  
ANISOU  839  C   SER A 903    13021  13242  16264   1844   3930   1217       C  
ATOM    840  O   SER A 903       9.831   3.185  -9.301  1.00113.89           O  
ANISOU  840  O   SER A 903    13529  13443  16299   1842   4012   1302       O  
ATOM    841  CB  SER A 903      10.755   5.321  -7.179  1.00111.83           C  
ANISOU  841  CB  SER A 903    12833  13247  16411   1656   3791   1150       C  
ATOM    842  OG  SER A 903       9.874   5.914  -8.116  1.00125.21           O  
ANISOU  842  OG  SER A 903    14771  14871  17931   1600   3932   1231       O  
ATOM    843  N   CYS A  35      11.955   2.683  -8.777  1.00111.05           N  
ANISOU  843  N   CYS A  35    12722  13124  16348   1892   4046   1157       N  
ATOM    844  CA  CYS A  35      12.220   2.103 -10.093  1.00110.34           C  
ANISOU  844  CA  CYS A  35    12734  12974  16216   1944   4292   1187       C  
ATOM    845  C   CYS A  35      11.235   0.978 -10.399  1.00108.77           C  
ANISOU  845  C   CYS A  35    12791  12778  15757   2052   4201   1262       C  
ATOM    846  O   CYS A  35      11.467  -0.178 -10.046  1.00108.82           O  
ANISOU  846  O   CYS A  35    12746  12825  15777   2167   4075   1238       O  
ATOM    847  CB  CYS A  35      13.653   1.574 -10.189  1.00112.58           C  
ANISOU  847  CB  CYS A  35    12752  13265  16760   2001   4397   1098       C  
ATOM    848  SG  CYS A  35      14.931   2.852 -10.130  1.00127.47           S  
ANISOU  848  SG  CYS A  35    14334  15127  18972   1870   4565   1020       S  
ATOM    849  N   PRO A  39      13.131  -5.228  -7.716  1.00108.60           N  
ANISOU  849  N   PRO A  39    13090  13088  15083   1571  -1247   -438       N  
ATOM    850  CA  PRO A  39      12.515  -6.210  -6.821  1.00103.58           C  
ANISOU  850  CA  PRO A  39    12150  12671  14537   1311  -1249   -355       C  
ATOM    851  C   PRO A  39      13.490  -7.317  -6.442  1.00108.64           C  
ANISOU  851  C   PRO A  39    12963  13161  15153   1053  -1207   -323       C  
ATOM    852  O   PRO A  39      14.539  -7.438  -7.077  1.00108.62           O  
ANISOU  852  O   PRO A  39    13297  12895  15080   1072  -1223   -357       O  
ATOM    853  CB  PRO A  39      11.365  -6.757  -7.663  1.00104.75           C  
ANISOU  853  CB  PRO A  39    12116  12935  14749   1237  -1529   -309       C  
ATOM    854  CG  PRO A  39      11.921  -6.742  -9.056  1.00105.31           C  
ANISOU  854  CG  PRO A  39    12550  12720  14743   1321  -1701   -354       C  
ATOM    855  CD  PRO A  39      12.859  -5.545  -9.131  1.00118.27           C  
ANISOU  855  CD  PRO A  39    14461  14182  16292   1590  -1514   -442       C  
ATOM    856  N   SER A  40      13.143  -8.122  -5.431  1.00114.88           N  
ANISOU  856  N   SER A  40    13534  14117  15997    826  -1148   -256       N  
ATOM    857  CA  SER A  40      13.957  -9.276  -5.063  1.00115.53           C  
ANISOU  857  CA  SER A  40    13779  14068  16048    581  -1127   -217       C  
ATOM    858  C   SER A  40      13.946 -10.326  -6.160  1.00113.61           C  
ANISOU  858  C   SER A  40    13710  13667  15789    423  -1372   -183       C  
ATOM    859  O   SER A  40      14.644 -11.342  -6.061  1.00113.14           O  
ANISOU  859  O   SER A  40    13842  13461  15684    240  -1380   -148       O  
ATOM    860  CB  SER A  40      13.460  -9.877  -3.742  1.00115.99           C  
ANISOU  860  CB  SER A  40    13574  14341  16157    378  -1010   -151       C  
ATOM    861  OG  SER A  40      13.189  -8.866  -2.786  1.00117.00           O  
ANISOU  861  OG  SER A  40    13510  14642  16301    537   -802   -175       O  
ATOM    862  N   ASP A  41      13.167 -10.092  -7.217  1.00105.31           N  
ANISOU  862  N   ASP A  41    12617  12635  14761    501  -1579   -192       N  
ATOM    863  CA  ASP A  41      13.112 -11.000  -8.355  1.00100.09           C  
ANISOU  863  CA  ASP A  41    12156  11806  14068    365  -1832   -166       C  
ATOM    864  C   ASP A  41      14.246 -10.730  -9.339  1.00 99.18           C  
ANISOU  864  C   ASP A  41    12466  11365  13853    526  -1845   -222       C  
ATOM    865  O   ASP A  41      14.072 -10.861 -10.556  1.00 98.90           O  
ANISOU  865  O   ASP A  41    12612  11185  13779    562  -2053   -232       O  
ATOM    866  CB  ASP A  41      11.759 -10.883  -9.058  1.00106.44           C  
ANISOU  866  CB  ASP A  41    12726  12780  14937    371  -2070   -150       C  
ATOM    867  CG  ASP A  41      10.594 -11.107  -8.117  1.00112.65           C  
ANISOU  867  CG  ASP A  41    13055  13911  15834    217  -2044    -89       C  
ATOM    868  OD1 ASP A  41      10.850 -11.387  -6.926  1.00108.73           O  
ANISOU  868  OD1 ASP A  41    12460  13497  15353    101  -1837    -61       O  
ATOM    869  OD2 ASP A  41       9.430 -10.997  -8.563  1.00106.44           O  
ANISOU  869  OD2 ASP A  41    12007  13316  15118    216  -2227    -69       O  
ATOM    870  N   LYS A  42      15.401 -10.333  -8.816  1.00 96.79           N  
ANISOU  870  N   LYS A  42    12320  10950  13504    621  -1622   -259       N  
ATOM    871  CA  LYS A  42      16.666 -10.315  -9.543  1.00 89.04           C  
ANISOU  871  CA  LYS A  42    11734   9665  12433    715  -1588   -295       C  
ATOM    872  C   LYS A  42      17.618 -11.324  -8.910  1.00 79.08           C  
ANISOU  872  C   LYS A  42    10603   8309  11136    539  -1487   -249       C  
ATOM    873  O   LYS A  42      18.800 -11.049  -8.695  1.00 67.84           O  
ANISOU  873  O   LYS A  42     9352   6756   9667    626  -1323   -280       O  
ATOM    874  CB  LYS A  42      17.275  -8.917  -9.546  1.00 93.44           C  
ANISOU  874  CB  LYS A  42    12371  10170  12963    984  -1413   -381       C  
ATOM    875  CG  LYS A  42      17.501  -8.344  -8.155  1.00 99.63           C  
ANISOU  875  CG  LYS A  42    12956  11123  13775   1004  -1175   -396       C  
ATOM    876  CD  LYS A  42      17.947  -6.891  -8.208  1.00 99.27           C  
ANISOU  876  CD  LYS A  42    12998  11028  13691   1259  -1022   -483       C  
ATOM    877  CE  LYS A  42      18.147  -6.325  -6.808  1.00 98.09           C  
ANISOU  877  CE  LYS A  42    12679  11036  13554   1268   -796   -498       C  
ATOM    878  NZ  LYS A  42      16.867  -6.239  -6.045  1.00 89.32           N  
ANISOU  878  NZ  LYS A  42    11215  10210  12512   1242   -800   -461       N  
ATOM    879  N   HIS A  43      17.094 -12.509  -8.613  1.00 69.75           N  
ANISOU  879  N   HIS A  43     9339   7194   9968    287  -1591   -174       N  
ATOM    880  CA  HIS A  43      17.781 -13.492  -7.790  1.00 61.08           C  
ANISOU  880  CA  HIS A  43     8316   6057   8835    113  -1492   -122       C  
ATOM    881  C   HIS A  43      18.676 -14.386  -8.634  1.00 57.05           C  
ANISOU  881  C   HIS A  43     8196   5254   8226     77  -1567    -95       C  
ATOM    882  O   HIS A  43      18.227 -14.981  -9.618  1.00 62.66           O  
ANISOU  882  O   HIS A  43     9055   5850   8902      0  -1772    -69       O  
ATOM    883  CB  HIS A  43      16.747 -14.335  -7.039  1.00 54.21           C  
ANISOU  883  CB  HIS A  43     7191   5391   8014   -147  -1550    -52       C  
ATOM    884  CG  HIS A  43      17.339 -15.342  -6.107  1.00 51.52           C  
ANISOU  884  CG  HIS A  43     6929   5020   7625   -325  -1446      3       C  
ATOM    885  ND1 HIS A  43      17.751 -16.589  -6.522  1.00 58.22           N  
ANISOU  885  ND1 HIS A  43     8062   5672   8386   -480  -1543     58       N  
ATOM    886  CD2 HIS A  43      17.573 -15.292  -4.774  1.00 53.27           C  
ANISOU  886  CD2 HIS A  43     7004   5375   7860   -363  -1255     13       C  
ATOM    887  CE1 HIS A  43      18.224 -17.262  -5.488  1.00 57.79           C  
ANISOU  887  CE1 HIS A  43     8030   5634   8293   -596  -1416     99       C  
ATOM    888  NE2 HIS A  43      18.126 -16.497  -4.415  1.00 55.42           N  
ANISOU  888  NE2 HIS A  43     7468   5534   8055   -532  -1245     72       N  
ATOM    889  N   LEU A  44      19.943 -14.473  -8.243  1.00 58.37           N  
ANISOU  889  N   LEU A  44     8531   5304   8342    139  -1401   -100       N  
ATOM    890  CA  LEU A  44      20.911 -15.363  -8.864  1.00 60.88           C  
ANISOU  890  CA  LEU A  44     9208   5360   8562    126  -1427    -64       C  
ATOM    891  C   LEU A  44      21.194 -16.526  -7.924  1.00 55.42           C  
ANISOU  891  C   LEU A  44     8535   4692   7829    -62  -1377      8       C  
ATOM    892  O   LEU A  44      21.343 -16.332  -6.713  1.00 51.98           O  
ANISOU  892  O   LEU A  44     7903   4420   7428    -88  -1230      6       O  
ATOM    893  CB  LEU A  44      22.212 -14.626  -9.187  1.00 54.92           C  
ANISOU  893  CB  LEU A  44     8634   4455   7778    352  -1273   -117       C  
ATOM    894  CG  LEU A  44      22.063 -13.339  -9.999  1.00 55.84           C  
ANISOU  894  CG  LEU A  44     8759   4538   7921    557  -1277   -198       C  
ATOM    895  CD1 LEU A  44      23.426 -12.746 -10.316  1.00 55.39           C  
ANISOU  895  CD1 LEU A  44     8904   4315   7827    739  -1112   -242       C  
ATOM    896  CD2 LEU A  44      21.272 -13.594 -11.276  1.00 55.67           C  
ANISOU  896  CD2 LEU A  44     8885   4398   7871    548  -1507   -190       C  
ATOM    897  N   ASP A  45      21.258 -17.736  -8.480  1.00 61.91           N  
ANISOU  897  N   ASP A  45     9624   5338   8563   -190  -1500     71       N  
ATOM    898  CA  ASP A  45      21.631 -18.886  -7.668  1.00 62.33           C  
ANISOU  898  CA  ASP A  45     9765   5372   8547   -346  -1448    141       C  
ATOM    899  C   ASP A  45      23.097 -18.842  -7.262  1.00 61.32           C  
ANISOU  899  C   ASP A  45     9775   5152   8370   -187  -1265    138       C  
ATOM    900  O   ASP A  45      23.492 -19.560  -6.341  1.00 62.46           O  
ANISOU  900  O   ASP A  45     9938   5327   8468   -270  -1187    185       O  
ATOM    901  CB  ASP A  45      21.349 -20.186  -8.422  1.00 67.08           C  
ANISOU  901  CB  ASP A  45    10666   5780   9042   -515  -1626    211       C  
ATOM    902  CG  ASP A  45      19.868 -20.472  -8.556  1.00 76.57           C  
ANISOU  902  CG  ASP A  45    11694   7110  10289   -748  -1813    230       C  
ATOM    903  OD1 ASP A  45      19.064 -19.733  -7.951  1.00 80.49           O  
ANISOU  903  OD1 ASP A  45    11814   7865  10904   -772  -1784    199       O  
ATOM    904  OD2 ASP A  45      19.507 -21.432  -9.270  1.00 78.88           O  
ANISOU  904  OD2 ASP A  45    12228   7248  10496   -908  -1989    279       O  
ATOM    905  N   ALA A  46      23.905 -18.002  -7.910  1.00 52.91           N  
ANISOU  905  N   ALA A  46     8802   3987   7316     37  -1194     85       N  
ATOM    906  CA  ALA A  46      25.338 -17.998  -7.640  1.00 50.39           C  
ANISOU  906  CA  ALA A  46     8608   3584   6955    182  -1032     87       C  
ATOM    907  C   ALA A  46      25.641 -17.416  -6.265  1.00 49.41           C  
ANISOU  907  C   ALA A  46     8211   3675   6890    191   -875     59       C  
ATOM    908  O   ALA A  46      26.421 -17.991  -5.496  1.00 49.50           O  
ANISOU  908  O   ALA A  46     8264   3692   6852    182   -789     98       O  
ATOM    909  CB  ALA A  46      26.069 -17.213  -8.729  1.00 54.45           C  
ANISOU  909  CB  ALA A  46     9281   3937   7469    398   -989     37       C  
ATOM    910  N   ILE A  47      25.032 -16.273  -5.937  1.00 49.81           N  
ANISOU  910  N   ILE A  47     7996   3896   7032    221   -840     -8       N  
ATOM    911  CA  ILE A  47      25.387 -15.567  -4.705  1.00 46.43           C  
ANISOU  911  CA  ILE A  47     7348   3647   6645    252   -684    -44       C  
ATOM    912  C   ILE A  47      25.367 -16.491  -3.492  1.00 46.04           C  
ANISOU  912  C   ILE A  47     7242   3694   6558    100   -652     17       C  
ATOM    913  O   ILE A  47      26.377 -16.557  -2.779  1.00 46.81           O  
ANISOU  913  O   ILE A  47     7361   3802   6622    151   -544     22       O  
ATOM    914  CB  ILE A  47      24.488 -14.331  -4.528  1.00 43.73           C  
ANISOU  914  CB  ILE A  47     6755   3470   6389    291   -664   -112       C  
ATOM    915  CG1 ILE A  47      25.035 -13.157  -5.345  1.00 45.23           C  
ANISOU  915  CG1 ILE A  47     7020   3568   6597    490   -610   -189       C  
ATOM    916  CG2 ILE A  47      24.371 -13.950  -3.057  1.00 44.25           C  
ANISOU  916  CG2 ILE A  47     6586   3746   6482    242   -538   -124       C  
ATOM    917  CD1 ILE A  47      24.026 -12.554  -6.290  1.00 59.32           C  
ANISOU  917  CD1 ILE A  47     8780   5343   8417    546   -722   -225       C  
ATOM    918  N   PRO A  48      24.283 -17.214  -3.197  1.00 47.77           N  
ANISOU  918  N   PRO A  48     7390   3986   6775    -90   -740     65       N  
ATOM    919  CA  PRO A  48      24.338 -18.151  -2.062  1.00 47.50           C  
ANISOU  919  CA  PRO A  48     7353   4013   6683   -234   -697    125       C  
ATOM    920  C   PRO A  48      25.464 -19.165  -2.185  1.00 48.24           C  
ANISOU  920  C   PRO A  48     7738   3926   6664   -197   -691    180       C  
ATOM    921  O   PRO A  48      26.078 -19.528  -1.173  1.00 48.26           O  
ANISOU  921  O   PRO A  48     7747   3974   6616   -202   -604    205       O  
ATOM    922  CB  PRO A  48      22.954 -18.815  -2.089  1.00 45.75           C  
ANISOU  922  CB  PRO A  48     7054   3856   6475   -457   -813    170       C  
ATOM    923  CG  PRO A  48      22.075 -17.820  -2.767  1.00 48.12           C  
ANISOU  923  CG  PRO A  48     7167   4240   6875   -405   -876    115       C  
ATOM    924  CD  PRO A  48      22.938 -17.147  -3.796  1.00 45.81           C  
ANISOU  924  CD  PRO A  48     7036   3790   6578   -187   -877     64       C  
ATOM    925  N   ILE A  49      25.762 -19.625  -3.402  1.00 49.89           N  
ANISOU  925  N   ILE A  49     8202   3928   6824   -143   -781    203       N  
ATOM    926  CA  ILE A  49      26.869 -20.557  -3.590  1.00 53.45           C  
ANISOU  926  CA  ILE A  49     8946   4202   7162    -69   -761    260       C  
ATOM    927  C   ILE A  49      28.191 -19.874  -3.266  1.00 53.02           C  
ANISOU  927  C   ILE A  49     8844   4174   7126    134   -620    225       C  
ATOM    928  O   ILE A  49      29.027 -20.412  -2.530  1.00 50.91           O  
ANISOU  928  O   ILE A  49     8636   3914   6794    172   -553    263       O  
ATOM    929  CB  ILE A  49      26.874 -21.107  -5.029  1.00 54.19           C  
ANISOU  929  CB  ILE A  49     9342   4055   7192    -39   -876    290       C  
ATOM    930  CG1 ILE A  49      25.503 -21.668  -5.421  1.00 55.93           C  
ANISOU  930  CG1 ILE A  49     9587   4262   7403   -262  -1043    316       C  
ATOM    931  CG2 ILE A  49      27.960 -22.165  -5.191  1.00 51.69           C  
ANISOU  931  CG2 ILE A  49     9348   3550   6741     49   -844    362       C  
ATOM    932  CD1 ILE A  49      25.026 -22.829  -4.589  1.00 59.59           C  
ANISOU  932  CD1 ILE A  49    10102   4753   7786   -483  -1071    386       C  
ATOM    933  N   LEU A  50      28.396 -18.671  -3.809  1.00 46.82           N  
ANISOU  933  N   LEU A  50     7955   3407   6427    263   -577    151       N  
ATOM    934  CA  LEU A  50      29.646 -17.955  -3.582  1.00 41.93           C  
ANISOU  934  CA  LEU A  50     7286   2815   5832    430   -445    113       C  
ATOM    935  C   LEU A  50      29.828 -17.604  -2.111  1.00 44.53           C  
ANISOU  935  C   LEU A  50     7393   3346   6182    387   -359     93       C  
ATOM    936  O   LEU A  50      30.930 -17.731  -1.567  1.00 50.00           O  
ANISOU  936  O   LEU A  50     8096   4060   6842    467   -285    107       O  
ATOM    937  CB  LEU A  50      29.686 -16.693  -4.443  1.00 45.63           C  
ANISOU  937  CB  LEU A  50     7704   3255   6379    545   -414     32       C  
ATOM    938  CG  LEU A  50      30.131 -16.865  -5.897  1.00 46.86           C  
ANISOU  938  CG  LEU A  50     8122   3182   6502    664   -442     44       C  
ATOM    939  CD1 LEU A  50      29.259 -17.858  -6.649  1.00 50.29           C  
ANISOU  939  CD1 LEU A  50     8759   3476   6873    567   -599    100       C  
ATOM    940  CD2 LEU A  50      30.123 -15.516  -6.602  1.00 45.84           C  
ANISOU  940  CD2 LEU A  50     7938   3036   6444    771   -395    -43       C  
ATOM    941  N   TYR A  51      28.760 -17.152  -1.451  1.00 44.85           N  
ANISOU  941  N   TYR A  51     7230   3539   6271    270   -367     63       N  
ATOM    942  CA  TYR A  51      28.872 -16.782  -0.047  1.00 44.16           C  
ANISOU  942  CA  TYR A  51     6960   3630   6190    231   -280     43       C  
ATOM    943  C   TYR A  51      29.361 -17.950   0.802  1.00 46.19           C  
ANISOU  943  C   TYR A  51     7321   3881   6349    179   -279    116       C  
ATOM    944  O   TYR A  51      30.220 -17.775   1.675  1.00 51.00           O  
ANISOU  944  O   TYR A  51     7880   4564   6933    234   -208    108       O  
ATOM    945  CB  TYR A  51      27.533 -16.261   0.476  1.00 43.73           C  
ANISOU  945  CB  TYR A  51     6696   3727   6192    117   -281     14       C  
ATOM    946  CG  TYR A  51      27.319 -14.785   0.228  1.00 40.14           C  
ANISOU  946  CG  TYR A  51     6093   3341   5819    213   -227    -74       C  
ATOM    947  CD1 TYR A  51      27.485 -14.236  -1.034  1.00 39.27           C  
ANISOU  947  CD1 TYR A  51     6066   3113   5743    326   -258   -112       C  
ATOM    948  CD2 TYR A  51      26.994 -13.932   1.275  1.00 44.04           C  
ANISOU  948  CD2 TYR A  51     6395   4001   6338    200   -134   -118       C  
ATOM    949  CE1 TYR A  51      27.308 -12.885  -1.254  1.00 38.90           C  
ANISOU  949  CE1 TYR A  51     5918   3111   5750    420   -202   -194       C  
ATOM    950  CE2 TYR A  51      26.816 -12.578   1.065  1.00 40.95           C  
ANISOU  950  CE2 TYR A  51     5905   3655   5998    298    -76   -198       C  
ATOM    951  CZ  TYR A  51      26.974 -12.060  -0.202  1.00 42.38           C  
ANISOU  951  CZ  TYR A  51     6175   3717   6210    407   -111   -236       C  
ATOM    952  OH  TYR A  51      26.799 -10.711  -0.420  1.00 47.81           O  
ANISOU  952  OH  TYR A  51     6799   4434   6932    512    -49   -316       O  
ATOM    953  N   TYR A  52      28.828 -19.150   0.565  1.00 43.33           N  
ANISOU  953  N   TYR A  52     7121   3425   5918     69   -362    188       N  
ATOM    954  CA  TYR A  52      29.268 -20.310   1.333  1.00 45.17           C  
ANISOU  954  CA  TYR A  52     7500   3629   6035     28   -359    261       C  
ATOM    955  C   TYR A  52      30.694 -20.711   0.972  1.00 47.70           C  
ANISOU  955  C   TYR A  52     7999   3833   6291    210   -339    293       C  
ATOM    956  O   TYR A  52      31.457 -21.154   1.838  1.00 44.69           O  
ANISOU  956  O   TYR A  52     7654   3490   5838    258   -301    325       O  
ATOM    957  CB  TYR A  52      28.305 -21.476   1.120  1.00 52.38           C  
ANISOU  957  CB  TYR A  52     8569   4454   6878   -153   -450    329       C  
ATOM    958  CG  TYR A  52      27.140 -21.462   2.083  1.00 60.45           C  
ANISOU  958  CG  TYR A  52     9414   5631   7925   -351   -433    328       C  
ATOM    959  CD1 TYR A  52      27.313 -21.825   3.413  1.00 54.30           C  
ANISOU  959  CD1 TYR A  52     8620   4936   7077   -402   -362    351       C  
ATOM    960  CD2 TYR A  52      25.870 -21.077   1.669  1.00 60.77           C  
ANISOU  960  CD2 TYR A  52     9299   5738   8054   -477   -484    305       C  
ATOM    961  CE1 TYR A  52      26.255 -21.811   4.300  1.00 60.06           C  
ANISOU  961  CE1 TYR A  52     9196   5800   7824   -580   -322    354       C  
ATOM    962  CE2 TYR A  52      24.807 -21.059   2.551  1.00 57.70           C  
ANISOU  962  CE2 TYR A  52     8724   5505   7693   -650   -449    311       C  
ATOM    963  CZ  TYR A  52      25.006 -21.427   3.865  1.00 57.87           C  
ANISOU  963  CZ  TYR A  52     8746   5597   7644   -704   -358    336       C  
ATOM    964  OH  TYR A  52      23.953 -21.412   4.748  1.00 61.47           O  
ANISOU  964  OH  TYR A  52     9029   6203   8125   -873   -300    346       O  
ATOM    965  N   ILE A  53      31.072 -20.567  -0.300  1.00 51.76           N  
ANISOU  965  N   ILE A  53     8629   4209   6828    323   -360    287       N  
ATOM    966  CA  ILE A  53      32.440 -20.876  -0.709  1.00 48.14           C  
ANISOU  966  CA  ILE A  53     8319   3652   6321    514   -317    321       C  
ATOM    967  C   ILE A  53      33.433 -20.030   0.079  1.00 46.99           C  
ANISOU  967  C   ILE A  53     7966   3663   6227    616   -224    274       C  
ATOM    968  O   ILE A  53      34.383 -20.548   0.678  1.00 41.89           O  
ANISOU  968  O   ILE A  53     7359   3043   5514    705   -198    318       O  
ATOM    969  CB  ILE A  53      32.605 -20.675  -2.227  1.00 49.31           C  
ANISOU  969  CB  ILE A  53     8612   3628   6495    617   -333    313       C  
ATOM    970  CG1 ILE A  53      31.852 -21.770  -2.988  1.00 46.89           C  
ANISOU  970  CG1 ILE A  53     8583   3136   6097    526   -443    376       C  
ATOM    971  CG2 ILE A  53      34.082 -20.664  -2.605  1.00 47.72           C  
ANISOU  971  CG2 ILE A  53     8486   3369   6278    833   -248    333       C  
ATOM    972  CD1 ILE A  53      31.756 -21.539  -4.484  1.00 41.35           C  
ANISOU  972  CD1 ILE A  53     8042   2256   5412    598   -482    363       C  
ATOM    973  N   ILE A  54      33.226 -18.711   0.090  1.00 48.55           N  
ANISOU  973  N   ILE A  54     7948   3963   6535    606   -181    186       N  
ATOM    974  CA  ILE A  54      34.114 -17.824   0.836  1.00 43.77           C  
ANISOU  974  CA  ILE A  54     7155   3503   5974    670   -102    135       C  
ATOM    975  C   ILE A  54      34.090 -18.169   2.318  1.00 45.93           C  
ANISOU  975  C   ILE A  54     7351   3912   6187    593   -105    153       C  
ATOM    976  O   ILE A  54      35.107 -18.065   3.013  1.00 43.43           O  
ANISOU  976  O   ILE A  54     6970   3682   5851    665    -75    153       O  
ATOM    977  CB  ILE A  54      33.723 -16.353   0.597  1.00 45.60           C  
ANISOU  977  CB  ILE A  54     7216   3799   6311    651    -55     36       C  
ATOM    978  CG1 ILE A  54      34.006 -15.947  -0.854  1.00 49.76           C  
ANISOU  978  CG1 ILE A  54     7841   4180   6884    756    -37     14       C  
ATOM    979  CG2 ILE A  54      34.451 -15.442   1.575  1.00 38.54           C  
ANISOU  979  CG2 ILE A  54     6139   3061   5444    664     15    -21       C  
ATOM    980  CD1 ILE A  54      35.471 -15.990  -1.245  1.00 48.12           C  
ANISOU  980  CD1 ILE A  54     7682   3929   6675    904     31     33       C  
ATOM    981  N   PHE A  55      32.928 -18.581   2.827  1.00 46.41           N  
ANISOU  981  N   PHE A  55     7419   3998   6218    443   -142    170       N  
ATOM    982  CA  PHE A  55      32.797 -18.876   4.250  1.00 45.23           C  
ANISOU  982  CA  PHE A  55     7217   3964   6004    363   -130    185       C  
ATOM    983  C   PHE A  55      33.781 -19.959   4.679  1.00 45.49           C  
ANISOU  983  C   PHE A  55     7409   3956   5921    449   -152    259       C  
ATOM    984  O   PHE A  55      34.604 -19.746   5.576  1.00 41.02           O  
ANISOU  984  O   PHE A  55     6766   3494   5327    509   -132    249       O  
ATOM    985  CB  PHE A  55      31.350 -19.276   4.559  1.00 44.61           C  
ANISOU  985  CB  PHE A  55     7140   3899   5911    181   -154    203       C  
ATOM    986  CG  PHE A  55      31.181 -20.010   5.861  1.00 44.30           C  
ANISOU  986  CG  PHE A  55     7146   3917   5769     91   -142    247       C  
ATOM    987  CD1 PHE A  55      31.382 -19.366   7.069  1.00 42.91           C  
ANISOU  987  CD1 PHE A  55     6833   3883   5586     85    -84    207       C  
ATOM    988  CD2 PHE A  55      30.787 -21.339   5.873  1.00 42.79           C  
ANISOU  988  CD2 PHE A  55     7162   3623   5474      3   -188    328       C  
ATOM    989  CE1 PHE A  55      31.219 -20.042   8.264  1.00 43.66           C  
ANISOU  989  CE1 PHE A  55     6998   4016   5574      8    -70    247       C  
ATOM    990  CE2 PHE A  55      30.620 -22.018   7.066  1.00 43.72           C  
ANISOU  990  CE2 PHE A  55     7350   3778   5484    -82   -167    367       C  
ATOM    991  CZ  PHE A  55      30.834 -21.370   8.261  1.00 43.64           C  
ANISOU  991  CZ  PHE A  55     7202   3910   5471    -73   -107    327       C  
ATOM    992  N   VAL A  56      33.712 -21.133   4.048  1.00 45.81           N  
ANISOU  992  N   VAL A  56     7684   3840   5880    464   -200    336       N  
ATOM    993  CA  VAL A  56      34.566 -22.241   4.466  1.00 43.83           C  
ANISOU  993  CA  VAL A  56     7619   3539   5495    564   -218    415       C  
ATOM    994  C   VAL A  56      36.026 -21.961   4.122  1.00 44.64           C  
ANISOU  994  C   VAL A  56     7680   3659   5621    781   -190    417       C  
ATOM    995  O   VAL A  56      36.926 -22.223   4.929  1.00 46.49           O  
ANISOU  995  O   VAL A  56     7898   3974   5793    880   -191    442       O  
ATOM    996  CB  VAL A  56      34.078 -23.565   3.849  1.00 47.95           C  
ANISOU  996  CB  VAL A  56     8446   3869   5906    520   -271    498       C  
ATOM    997  CG1 VAL A  56      32.674 -23.893   4.343  1.00 49.66           C  
ANISOU  997  CG1 VAL A  56     8675   4094   6097    278   -295    502       C  
ATOM    998  CG2 VAL A  56      34.110 -23.505   2.334  1.00 56.21           C  
ANISOU  998  CG2 VAL A  56     9594   4765   7000    588   -287    501       C  
ATOM    999  N   ILE A  57      36.290 -21.436   2.922  1.00 45.99           N  
ANISOU  999  N   ILE A  57     7834   3761   5881    861   -165    392       N  
ATOM   1000  CA  ILE A  57      37.664 -21.102   2.551  1.00 45.72           C  
ANISOU 1000  CA  ILE A  57     7732   3755   5883   1053   -116    394       C  
ATOM   1001  C   ILE A  57      38.260 -20.144   3.574  1.00 46.10           C  
ANISOU 1001  C   ILE A  57     7515   4011   5989   1045    -92    331       C  
ATOM   1002  O   ILE A  57      39.369 -20.356   4.079  1.00 49.75           O  
ANISOU 1002  O   ILE A  57     7927   4559   6417   1168    -93    361       O  
ATOM   1003  CB  ILE A  57      37.715 -20.508   1.132  1.00 46.11           C  
ANISOU 1003  CB  ILE A  57     7798   3696   6025   1110    -73    363       C  
ATOM   1004  CG1 ILE A  57      37.403 -21.576   0.080  1.00 47.82           C  
ANISOU 1004  CG1 ILE A  57     8324   3688   6158   1155   -105    438       C  
ATOM   1005  CG2 ILE A  57      39.077 -19.877   0.868  1.00 44.53           C  
ANISOU 1005  CG2 ILE A  57     7459   3566   5893   1270      3    347       C  
ATOM   1006  CD1 ILE A  57      38.479 -22.636  -0.072  1.00 55.19           C  
ANISOU 1006  CD1 ILE A  57     9447   4541   6980   1354    -86    535       C  
ATOM   1007  N   GLY A  58      37.523 -19.082   3.903  1.00 47.25           N  
ANISOU 1007  N   GLY A  58     7495   4242   6216    904    -76    246       N  
ATOM   1008  CA  GLY A  58      38.015 -18.133   4.886  1.00 47.32           C  
ANISOU 1008  CA  GLY A  58     7289   4428   6263    876    -57    182       C  
ATOM   1009  C   GLY A  58      38.115 -18.730   6.276  1.00 41.28           C  
ANISOU 1009  C   GLY A  58     6539   3755   5390    847   -105    215       C  
ATOM   1010  O   GLY A  58      39.072 -18.464   7.007  1.00 48.22           O  
ANISOU 1010  O   GLY A  58     7307   4759   6255    903   -120    204       O  
ATOM   1011  N   PHE A  59      37.130 -19.543   6.662  1.00 41.59           N  
ANISOU 1011  N   PHE A  59     6722   3735   5347    752   -133    255       N  
ATOM   1012  CA  PHE A  59      37.159 -20.143   7.990  1.00 46.04           C  
ANISOU 1012  CA  PHE A  59     7339   4364   5792    721   -167    288       C  
ATOM   1013  C   PHE A  59      38.293 -21.148   8.132  1.00 47.98           C  
ANISOU 1013  C   PHE A  59     7709   4590   5933    896   -213    368       C  
ATOM   1014  O   PHE A  59      38.765 -21.388   9.248  1.00 45.49           O  
ANISOU 1014  O   PHE A  59     7392   4365   5529    926   -252    382       O  
ATOM   1015  CB  PHE A  59      35.823 -20.818   8.294  1.00 46.24           C  
ANISOU 1015  CB  PHE A  59     7500   4318   5751    565   -168    317       C  
ATOM   1016  CG  PHE A  59      35.391 -20.677   9.719  1.00 43.29           C  
ANISOU 1016  CG  PHE A  59     7088   4047   5314    458   -156    298       C  
ATOM   1017  CD1 PHE A  59      35.792 -21.595  10.674  1.00 50.32           C  
ANISOU 1017  CD1 PHE A  59     8127   4937   6056    496   -192    355       C  
ATOM   1018  CD2 PHE A  59      34.588 -19.618  10.108  1.00 44.85           C  
ANISOU 1018  CD2 PHE A  59     7120   4333   5587    336   -102    224       C  
ATOM   1019  CE1 PHE A  59      35.398 -21.461  11.991  1.00 51.77           C  
ANISOU 1019  CE1 PHE A  59     8302   5199   6168    402   -174    337       C  
ATOM   1020  CE2 PHE A  59      34.191 -19.479  11.421  1.00 49.47           C  
ANISOU 1020  CE2 PHE A  59     7692   5001   6103    248    -75    210       C  
ATOM   1021  CZ  PHE A  59      34.597 -20.401  12.365  1.00 48.54           C  
ANISOU 1021  CZ  PHE A  59     7730   4874   5838    275   -111    265       C  
ATOM   1022  N   LEU A  60      38.741 -21.746   7.026  1.00 51.39           N  
ANISOU 1022  N   LEU A  60     8263   4901   6362   1026   -209    423       N  
ATOM   1023  CA  LEU A  60      39.849 -22.692   7.097  1.00 50.07           C  
ANISOU 1023  CA  LEU A  60     8216   4716   6092   1229   -240    506       C  
ATOM   1024  C   LEU A  60      41.191 -21.975   7.184  1.00 49.44           C  
ANISOU 1024  C   LEU A  60     7904   4794   6089   1368   -235    481       C  
ATOM   1025  O   LEU A  60      42.018 -22.297   8.043  1.00 50.06           O  
ANISOU 1025  O   LEU A  60     7949   4980   6093   1471   -288    512       O  
ATOM   1026  CB  LEU A  60      39.822 -23.637   5.894  1.00 49.64           C  
ANISOU 1026  CB  LEU A  60     8411   4462   5988   1330   -225    582       C  
ATOM   1027  CG  LEU A  60      39.213 -25.007   6.206  1.00 54.43           C  
ANISOU 1027  CG  LEU A  60     9337   4925   6417   1294   -262    662       C  
ATOM   1028  CD1 LEU A  60      37.799 -24.861   6.761  1.00 54.71           C  
ANISOU 1028  CD1 LEU A  60     9374   4958   6454   1030   -271    620       C  
ATOM   1029  CD2 LEU A  60      39.223 -25.903   4.978  1.00 63.65           C  
ANISOU 1029  CD2 LEU A  60    10785   5877   7521   1391   -251    735       C  
ATOM   1030  N   VAL A  61      41.432 -21.001   6.304  1.00 58.90           N  
ANISOU 1030  N   VAL A  61     8940   6007   7431   1367   -177    426       N  
ATOM   1031  CA  VAL A  61      42.709 -20.295   6.350  1.00 58.55           C  
ANISOU 1031  CA  VAL A  61     8662   6116   7467   1468   -164    402       C  
ATOM   1032  C   VAL A  61      42.850 -19.542   7.665  1.00 58.73           C  
ANISOU 1032  C   VAL A  61     8499   6324   7492   1359   -217    337       C  
ATOM   1033  O   VAL A  61      43.960 -19.399   8.191  1.00 59.61           O  
ANISOU 1033  O   VAL A  61     8460   6587   7603   1446   -261    344       O  
ATOM   1034  CB  VAL A  61      42.856 -19.350   5.141  1.00 58.82           C  
ANISOU 1034  CB  VAL A  61     8588   6113   7648   1462    -74    350       C  
ATOM   1035  CG1 VAL A  61      42.940 -20.154   3.854  1.00 61.01           C  
ANISOU 1035  CG1 VAL A  61     9071   6205   7905   1606    -25    424       C  
ATOM   1036  CG2 VAL A  61      41.704 -18.352   5.087  1.00 59.68           C  
ANISOU 1036  CG2 VAL A  61     8650   6197   7828   1259    -49    255       C  
ATOM   1037  N   ASN A  62      41.739 -19.055   8.220  1.00 45.79           N  
ANISOU 1037  N   ASN A  62     6869   4679   5851   1171   -217    276       N  
ATOM   1038  CA  ASN A  62      41.803 -18.313   9.473  1.00 44.33           C  
ANISOU 1038  CA  ASN A  62     6549   4644   5650   1065   -258    213       C  
ATOM   1039  C   ASN A  62      41.879 -19.236  10.682  1.00 47.21           C  
ANISOU 1039  C   ASN A  62     7034   5045   5859   1098   -341    267       C  
ATOM   1040  O   ASN A  62      42.477 -18.865  11.698  1.00 47.02           O  
ANISOU 1040  O   ASN A  62     6907   5162   5799   1090   -407    241       O  
ATOM   1041  CB  ASN A  62      40.596 -17.384   9.600  1.00 43.22           C  
ANISOU 1041  CB  ASN A  62     6379   4482   5560    875   -204    130       C  
ATOM   1042  CG  ASN A  62      40.754 -16.112   8.791  1.00 48.54           C  
ANISOU 1042  CG  ASN A  62     6899   5171   6372    836   -136     51       C  
ATOM   1043  OD1 ASN A  62      41.348 -15.137   9.254  1.00 47.79           O  
ANISOU 1043  OD1 ASN A  62     6651   5193   6312    788   -141    -13       O  
ATOM   1044  ND2 ASN A  62      40.222 -16.115   7.574  1.00 53.43           N  
ANISOU 1044  ND2 ASN A  62     7582   5660   7057    849    -77     53       N  
ATOM   1045  N   ILE A  63      41.278 -20.427  10.610  1.00 50.84           N  
ANISOU 1045  N   ILE A  63     7731   5371   6213   1127   -345    342       N  
ATOM   1046  CA  ILE A  63      41.448 -21.383  11.697  1.00 50.07           C  
ANISOU 1046  CA  ILE A  63     7788   5288   5949   1182   -417    400       C  
ATOM   1047  C   ILE A  63      42.863 -21.947  11.670  1.00 48.32           C  
ANISOU 1047  C   ILE A  63     7542   5136   5681   1416   -483    464       C  
ATOM   1048  O   ILE A  63      43.334 -22.493  12.674  1.00 52.84           O  
ANISOU 1048  O   ILE A  63     8181   5772   6125   1497   -566    500       O  
ATOM   1049  CB  ILE A  63      40.397 -22.504  11.616  1.00 48.33           C  
ANISOU 1049  CB  ILE A  63     7852   4894   5618   1127   -393    461       C  
ATOM   1050  CG1 ILE A  63      40.126 -23.099  12.999  1.00 57.82           C  
ANISOU 1050  CG1 ILE A  63     9205   6109   6654   1085   -437    484       C  
ATOM   1051  CG2 ILE A  63      40.865 -23.630  10.716  1.00 51.33           C  
ANISOU 1051  CG2 ILE A  63     8422   5144   5937   1305   -397    555       C  
ATOM   1052  CD1 ILE A  63      39.352 -22.164  13.916  1.00 66.63           C  
ANISOU 1052  CD1 ILE A  63    10214   7306   7797    891   -408    403       C  
ATOM   1053  N   VAL A  64      43.554 -21.822  10.534  1.00 50.62           N  
ANISOU 1053  N   VAL A  64     7740   5420   6073   1539   -443    482       N  
ATOM   1054  CA  VAL A  64      44.963 -22.191  10.455  1.00 51.16           C  
ANISOU 1054  CA  VAL A  64     7721   5590   6127   1771   -488    542       C  
ATOM   1055  C   VAL A  64      45.832 -21.125  11.109  1.00 55.78           C  
ANISOU 1055  C   VAL A  64     7999   6402   6793   1734   -546    476       C  
ATOM   1056  O   VAL A  64      46.843 -21.438  11.748  1.00 56.15           O  
ANISOU 1056  O   VAL A  64     7964   6588   6780   1877   -640    514       O  
ATOM   1057  CB  VAL A  64      45.364 -22.422   8.986  1.00 51.81           C  
ANISOU 1057  CB  VAL A  64     7822   5578   6288   1912   -400    588       C  
ATOM   1058  CG1 VAL A  64      46.872 -22.348   8.825  1.00 50.81           C  
ANISOU 1058  CG1 VAL A  64     7485   5611   6209   2121   -415    626       C  
ATOM   1059  CG2 VAL A  64      44.846 -23.765   8.500  1.00 59.70           C  
ANISOU 1059  CG2 VAL A  64     9170   6361   7151   2007   -379    680       C  
ATOM   1060  N   VAL A  65      45.458 -19.854  10.955  1.00 49.04           N  
ANISOU 1060  N   VAL A  65     6979   5586   6067   1545   -498    376       N  
ATOM   1061  CA  VAL A  65      46.245 -18.770  11.535  1.00 49.59           C  
ANISOU 1061  CA  VAL A  65     6782   5854   6208   1474   -552    306       C  
ATOM   1062  C   VAL A  65      46.298 -18.906  13.052  1.00 57.11           C  
ANISOU 1062  C   VAL A  65     7767   6905   7028   1435   -679    297       C  
ATOM   1063  O   VAL A  65      47.363 -18.786  13.668  1.00 69.24           O  
ANISOU 1063  O   VAL A  65     9146   8614   8547   1503   -787    303       O  
ATOM   1064  CB  VAL A  65      45.664 -17.409  11.110  1.00 50.48           C  
ANISOU 1064  CB  VAL A  65     6784   5947   6449   1270   -466    200       C  
ATOM   1065  CG1 VAL A  65      46.321 -16.278  11.883  1.00 61.40           C  
ANISOU 1065  CG1 VAL A  65     7949   7511   7871   1152   -528    120       C  
ATOM   1066  CG2 VAL A  65      45.843 -17.202   9.616  1.00 49.22           C  
ANISOU 1066  CG2 VAL A  65     6579   5704   6416   1328   -351    207       C  
ATOM   1067  N   VAL A  66      45.146 -19.153  13.678  1.00 58.06           N  
ANISOU 1067  N   VAL A  66     8091   6919   7051   1322   -668    284       N  
ATOM   1068  CA  VAL A  66      45.110 -19.255  15.134  1.00 57.05           C  
ANISOU 1068  CA  VAL A  66     8033   6859   6783   1278   -772    273       C  
ATOM   1069  C   VAL A  66      45.769 -20.549  15.599  1.00 58.39           C  
ANISOU 1069  C   VAL A  66     8339   7042   6803   1491   -871    372       C  
ATOM   1070  O   VAL A  66      46.463 -20.574  16.622  1.00 62.63           O  
ANISOU 1070  O   VAL A  66     8835   7709   7251   1542  -1001    373       O  
ATOM   1071  CB  VAL A  66      43.661 -19.141  15.645  1.00 51.46           C  
ANISOU 1071  CB  VAL A  66     7503   6033   6018   1098   -703    236       C  
ATOM   1072  CG1 VAL A  66      43.073 -17.792  15.263  1.00 48.64           C  
ANISOU 1072  CG1 VAL A  66     7007   5679   5794    918   -613    138       C  
ATOM   1073  CG2 VAL A  66      42.802 -20.284  15.110  1.00 50.55           C  
ANISOU 1073  CG2 VAL A  66     7626   5736   5843   1136   -634    309       C  
ATOM   1074  N   THR A  67      45.568 -21.642  14.857  1.00 57.96           N  
ANISOU 1074  N   THR A  67     8469   6848   6706   1626   -817    456       N  
ATOM   1075  CA  THR A  67      46.123 -22.928  15.271  1.00 63.50           C  
ANISOU 1075  CA  THR A  67     9354   7534   7240   1847   -898    555       C  
ATOM   1076  C   THR A  67      47.634 -22.975  15.088  1.00 64.71           C  
ANISOU 1076  C   THR A  67     9292   7864   7433   2071   -981    597       C  
ATOM   1077  O   THR A  67      48.327 -23.643  15.863  1.00 67.76           O  
ANISOU 1077  O   THR A  67     9735   8329   7683   2243  -1100    652       O  
ATOM   1078  CB  THR A  67      45.464 -24.074  14.503  1.00 59.90           C  
ANISOU 1078  CB  THR A  67     9191   6858   6710   1918   -811    634       C  
ATOM   1079  OG1 THR A  67      45.511 -23.806  13.098  1.00 68.71           O  
ANISOU 1079  OG1 THR A  67    10212   7919   7977   1939   -713    636       O  
ATOM   1080  CG2 THR A  67      44.021 -24.254  14.943  1.00 63.48           C  
ANISOU 1080  CG2 THR A  67     9869   7163   7089   1705   -755    610       C  
ATOM   1081  N   LEU A  68      48.160 -22.290  14.071  1.00 68.45           N  
ANISOU 1081  N   LEU A  68     9519   8403   8086   2080   -916    576       N  
ATOM   1082  CA  LEU A  68      49.608 -22.226  13.903  1.00 71.37           C  
ANISOU 1082  CA  LEU A  68     9631   8970   8515   2271   -981    614       C  
ATOM   1083  C   LEU A  68      50.286 -21.764  15.186  1.00 73.63           C  
ANISOU 1083  C   LEU A  68     9748   9471   8756   2237  -1152    576       C  
ATOM   1084  O   LEU A  68      51.357 -22.265  15.543  1.00 81.48           O  
ANISOU 1084  O   LEU A  68    10647  10616   9694   2451  -1266    640       O  
ATOM   1085  CB  LEU A  68      49.972 -21.298  12.743  1.00 70.06           C  
ANISOU 1085  CB  LEU A  68     9208   8849   8561   2214   -870    574       C  
ATOM   1086  CG  LEU A  68      50.000 -21.934  11.350  1.00 69.90           C  
ANISOU 1086  CG  LEU A  68     9292   8683   8583   2379   -733    648       C  
ATOM   1087  CD1 LEU A  68      50.049 -20.868  10.267  1.00 67.75           C  
ANISOU 1087  CD1 LEU A  68     8823   8410   8509   2261   -607    585       C  
ATOM   1088  CD2 LEU A  68      51.187 -22.878  11.217  1.00 64.98           C  
ANISOU 1088  CD2 LEU A  68     8637   8153   7900   2707   -771    762       C  
ATOM   1089  N   PHE A  69      49.661 -20.836  15.910  1.00 75.93           N  
ANISOU 1089  N   PHE A  69    10019   9775   9057   1980  -1177    477       N  
ATOM   1090  CA  PHE A  69      50.247 -20.297  17.135  1.00 74.13           C  
ANISOU 1090  CA  PHE A  69     9658   9731   8776   1915  -1345    430       C  
ATOM   1091  C   PHE A  69      50.536 -21.385  18.170  1.00 72.54           C  
ANISOU 1091  C   PHE A  69     9650   9548   8363   2101  -1490    502       C  
ATOM   1092  O   PHE A  69      51.347 -21.182  19.073  1.00 79.08           O  
ANISOU 1092  O   PHE A  69    10350  10558   9137   2134  -1664    491       O  
ATOM   1093  CB  PHE A  69      49.322 -19.238  17.748  1.00 70.82           C  
ANISOU 1093  CB  PHE A  69     9280   9264   8364   1620  -1321    318       C  
ATOM   1094  CG  PHE A  69      49.291 -17.945  16.983  1.00 71.43           C  
ANISOU 1094  CG  PHE A  69     9136   9372   8630   1436  -1224    233       C  
ATOM   1095  CD1 PHE A  69      50.451 -17.212  16.793  1.00 74.94           C  
ANISOU 1095  CD1 PHE A  69     9266  10016   9191   1422  -1287    207       C  
ATOM   1096  CD2 PHE A  69      48.104 -17.458  16.462  1.00 74.95           C  
ANISOU 1096  CD2 PHE A  69     9690   9653   9134   1276  -1070    181       C  
ATOM   1097  CE1 PHE A  69      50.430 -16.022  16.091  1.00 73.45           C  
ANISOU 1097  CE1 PHE A  69     8908   9838   9161   1245  -1187    128       C  
ATOM   1098  CE2 PHE A  69      48.076 -16.267  15.759  1.00 70.37           C  
ANISOU 1098  CE2 PHE A  69     8940   9088   8709   1124   -979    102       C  
ATOM   1099  CZ  PHE A  69      49.241 -15.548  15.574  1.00 71.66           C  
ANISOU 1099  CZ  PHE A  69     8823   9429   8976   1105  -1032     74       C  
HETATM 1100  N   YCM A  70      49.889 -22.539  18.035  1.00 69.64           N  
ANISOU 1100  N   YCM A  70     9603   8989   7866   2219  -1426    574       N  
HETATM 1101  CA  YCM A  70      50.110 -23.634  18.952  1.00 71.61           C  
ANISOU 1101  CA  YCM A  70    10091   9222   7895   2406  -1544    646       C  
HETATM 1102  CB  YCM A  70      48.932 -24.618  18.966  1.00 71.99           C  
ANISOU 1102  CB  YCM A  70    10553   9005   7793   2393  -1440    688       C  
HETATM 1103  SG  YCM A  70      47.384 -23.951  19.495  1.00 78.09           S  
ANISOU 1103  SG  YCM A  70    11473   9636   8560   2047  -1342    593       S  
HETATM 1104  CD  YCM A  70      46.166 -24.699  18.448  1.00 81.48           C  
ANISOU 1104  CD  YCM A  70    12159   9803   8996   1992  -1151    637       C  
HETATM 1105  CE  YCM A  70      45.734 -26.076  18.889  1.00 84.99           C  
ANISOU 1105  CE  YCM A  70    13002  10077   9215   2090  -1148    719       C  
HETATM 1106  OZ1 YCM A  70      46.456 -27.078  18.694  1.00 90.40           O  
ANISOU 1106  OZ1 YCM A  70    13816  10740   9791   2350  -1196    809       O  
HETATM 1107  NZ2 YCM A  70      44.514 -26.202  19.501  1.00 86.18           N  
ANISOU 1107  NZ2 YCM A  70    13379  10089   9275   1888  -1077    694       N  
HETATM 1108  C   YCM A  70      51.395 -24.386  18.621  1.00 86.49           C  
ANISOU 1108  C   YCM A  70    11866  11238   9759   2738  -1624    745       C  
HETATM 1109  O   YCM A  70      52.140 -24.889  19.467  1.00 93.24           O  
ANISOU 1109  O   YCM A  70    12740  12210  10476   2921  -1789    789       O  
ATOM   1110  N   CYS A  71      51.657 -24.451  17.319  1.00 91.16           N  
ANISOU 1110  N   CYS A  71    12341  11807  10488   2829  -1498    783       N  
ATOM   1111  CA  CYS A  71      52.819 -25.151  16.784  1.00 90.71           C  
ANISOU 1111  CA  CYS A  71    12174  11859  10431   3160  -1523    886       C  
ATOM   1112  C   CYS A  71      54.031 -24.229  16.629  1.00101.00           C  
ANISOU 1112  C   CYS A  71    13002  13457  11917   3170  -1594    860       C  
ATOM   1113  O   CYS A  71      55.085 -24.661  16.163  1.00112.14           O  
ANISOU 1113  O   CYS A  71    14244  15004  13361   3440  -1606    944       O  
ATOM   1114  CB  CYS A  71      52.472 -25.786  15.435  1.00 85.69           C  
ANISOU 1114  CB  CYS A  71    11705  11024   9831   3271  -1335    952       C  
ATOM   1115  SG  CYS A  71      51.306 -27.157  15.551  1.00 86.02           S  
ANISOU 1115  SG  CYS A  71    12319  10735   9629   3316  -1271   1014       S  
ATOM   1116  N   GLN A  72      53.882 -22.965  17.021  1.00101.02           N  
ANISOU 1116  N   GLN A  72    12794  13557  12030   2875  -1634    746       N  
ATOM   1117  CA  GLN A  72      54.968 -22.004  16.870  1.00102.30           C  
ANISOU 1117  CA  GLN A  72    12513  13989  12368   2824  -1696    711       C  
ATOM   1118  C   GLN A  72      56.168 -22.373  17.728  1.00123.78           C  
ANISOU 1118  C   GLN A  72    15056  16967  15008   3031  -1918    765       C  
ATOM   1119  O   GLN A  72      56.045 -22.994  18.788  1.00124.62           O  
ANISOU 1119  O   GLN A  72    15380  17054  14915   3119  -2064    786       O  
ATOM   1120  CB  GLN A  72      54.500 -20.592  17.213  1.00102.80           C  
ANISOU 1120  CB  GLN A  72    12453  14077  12529   2453  -1702    575       C  
ATOM   1121  CG  GLN A  72      53.518 -20.029  16.215  1.00107.21           C  
ANISOU 1121  CG  GLN A  72    13092  14436  13207   2265  -1487    519       C  
ATOM   1122  CD  GLN A  72      54.107 -19.937  14.819  1.00105.23           C  
ANISOU 1122  CD  GLN A  72    12639  14215  13130   2368  -1340    559       C  
ATOM   1123  OE1 GLN A  72      55.177 -19.359  14.625  1.00121.83           O  
ANISOU 1123  OE1 GLN A  72    14394  16538  15359   2371  -1376    553       O  
ATOM   1124  NE2 GLN A  72      53.423 -20.523  13.845  1.00 97.62           N  
ANISOU 1124  NE2 GLN A  72    11898  13027  12167   2449  -1174    602       N  
ATOM   1125  N   LYS A  73      57.343 -21.974  17.241  1.00144.42           N  
ANISOU 1125  N   LYS A  73    17265  19829  17780   3110  -1939    788       N  
ATOM   1126  CA  LYS A  73      58.620 -22.328  17.838  1.00147.88           C  
ANISOU 1126  CA  LYS A  73    17456  20554  18179   3340  -2141    854       C  
ATOM   1127  C   LYS A  73      59.486 -21.121  18.175  1.00149.49           C  
ANISOU 1127  C   LYS A  73    17210  21053  18535   3127  -2275    780       C  
ATOM   1128  O   LYS A  73      60.683 -21.295  18.433  1.00152.61           O  
ANISOU 1128  O   LYS A  73    17297  21735  18954   3307  -2427    838       O  
ATOM   1129  CB  LYS A  73      59.392 -23.260  16.890  1.00149.34           C  
ANISOU 1129  CB  LYS A  73    17558  20789  18394   3721  -2040    988       C  
ATOM   1130  CG  LYS A  73      59.451 -22.772  15.427  1.00147.98           C  
ANISOU 1130  CG  LYS A  73    17212  20573  18439   3664  -1793    987       C  
ATOM   1131  CD  LYS A  73      58.168 -23.140  14.682  1.00144.79           C  
ANISOU 1131  CD  LYS A  73    17220  19804  17990   3608  -1586    980       C  
ATOM   1132  CE  LYS A  73      57.695 -22.023  13.760  1.00142.43           C  
ANISOU 1132  CE  LYS A  73    16807  19421  17890   3314  -1408    889       C  
ATOM   1133  NZ  LYS A  73      56.338 -22.311  13.201  1.00139.44           N  
ANISOU 1133  NZ  LYS A  73    16825  18699  17455   3224  -1251    869       N  
ATOM   1134  N   GLY A  74      58.932 -19.906  18.186  1.00148.08           N  
ANISOU 1134  N   GLY A  74    16987  20821  18455   2751  -2228    656       N  
ATOM   1135  CA  GLY A  74      59.747 -18.739  18.433  1.00149.69           C  
ANISOU 1135  CA  GLY A  74    16793  21284  18797   2521  -2342    584       C  
ATOM   1136  C   GLY A  74      59.107 -17.664  19.291  1.00149.89           C  
ANISOU 1136  C   GLY A  74    16919  21253  18781   2147  -2428    450       C  
ATOM   1137  O   GLY A  74      57.936 -17.740  19.676  1.00150.42           O  
ANISOU 1137  O   GLY A  74    17356  21072  18725   2051  -2377    406       O  
ATOM   1138  N   PRO A  75      59.890 -16.627  19.599  1.00156.30           N  
ANISOU 1138  N   PRO A  75    17398  22297  19692   1926  -2556    385       N  
ATOM   1139  CA  PRO A  75      59.401 -15.504  20.421  1.00154.71           C  
ANISOU 1139  CA  PRO A  75    17290  22050  19443   1562  -2645    255       C  
ATOM   1140  C   PRO A  75      58.432 -14.623  19.646  1.00148.93           C  
ANISOU 1140  C   PRO A  75    16687  21090  18809   1311  -2398    168       C  
ATOM   1141  O   PRO A  75      58.790 -14.051  18.614  1.00153.91           O  
ANISOU 1141  O   PRO A  75    17086  21768  19626   1230  -2248    155       O  
ATOM   1142  CB  PRO A  75      60.686 -14.750  20.789  1.00180.81           C  
ANISOU 1142  CB  PRO A  75    20171  25689  22839   1421  -2849    227       C  
ATOM   1143  CG  PRO A  75      61.644 -15.082  19.689  1.00171.24           C  
ANISOU 1143  CG  PRO A  75    18593  24658  21812   1616  -2744    317       C  
ATOM   1144  CD  PRO A  75      61.317 -16.485  19.253  1.00168.66           C  
ANISOU 1144  CD  PRO A  75    18483  24191  21407   2008  -2635    435       C  
ATOM   1145  N   LYS A  76      57.203 -14.509  20.148  1.00129.97           N  
ANISOU 1145  N   LYS A  76    14658  18445  16278   1195  -2351    110       N  
ATOM   1146  CA  LYS A  76      56.183 -13.732  19.458  1.00129.61           C  
ANISOU 1146  CA  LYS A  76    14758  18180  16308    990  -2123     32       C  
ATOM   1147  C   LYS A  76      56.312 -12.247  19.788  1.00129.59           C  
ANISOU 1147  C   LYS A  76    14654  18235  16351    639  -2165    -90       C  
ATOM   1148  O   LYS A  76      56.324 -11.861  20.961  1.00130.55           O  
ANISOU 1148  O   LYS A  76    14864  18399  16341    501  -2347   -143       O  
ATOM   1149  CB  LYS A  76      54.788 -14.220  19.856  1.00129.20           C  
ANISOU 1149  CB  LYS A  76    15127  17858  16104   1014  -2044     27       C  
ATOM   1150  CG  LYS A  76      54.579 -15.733  19.823  1.00129.23           C  
ANISOU 1150  CG  LYS A  76    15315  17781  16004   1329  -2037    141       C  
ATOM   1151  CD  LYS A  76      54.092 -16.215  18.465  1.00126.11           C  
ANISOU 1151  CD  LYS A  76    14977  17227  15713   1450  -1802    192       C  
ATOM   1152  CE  LYS A  76      55.246 -16.534  17.533  1.00126.12           C  
ANISOU 1152  CE  LYS A  76    14677  17393  15852   1640  -1777    269       C  
ATOM   1153  NZ  LYS A  76      54.823 -16.491  16.104  1.00121.43           N  
ANISOU 1153  NZ  LYS A  76    14099  16644  15394   1660  -1533    281       N  
ATOM   1154  N   LYS A  77      56.418 -11.421  18.750  1.00114.71           N  
ANISOU 1154  N   LYS A  77    12611  16336  14636    497  -1996   -133       N  
ATOM   1155  CA  LYS A  77      56.357  -9.971  18.878  1.00110.23           C  
ANISOU 1155  CA  LYS A  77    12018  15761  14105    155  -1981   -254       C  
ATOM   1156  C   LYS A  77      54.903  -9.506  18.968  1.00105.72           C  
ANISOU 1156  C   LYS A  77    11811  14907  13451     35  -1835   -327       C  
ATOM   1157  O   LYS A  77      53.965 -10.245  18.657  1.00 98.45           O  
ANISOU 1157  O   LYS A  77    11107  13806  12494    196  -1711   -283       O  
ATOM   1158  CB  LYS A  77      57.095  -9.282  17.729  1.00112.51           C  
ANISOU 1158  CB  LYS A  77    12007  16145  14599     55  -1850   -269       C  
ATOM   1159  CG  LYS A  77      58.605  -9.521  17.784  1.00115.28           C  
ANISOU 1159  CG  LYS A  77    11946  16817  15037    120  -2007   -209       C  
ATOM   1160  CD  LYS A  77      59.365  -8.906  16.614  1.00127.71           C  
ANISOU 1160  CD  LYS A  77    13211  18492  16821     28  -1851   -213       C  
ATOM   1161  CE  LYS A  77      59.295  -7.384  16.630  1.00137.58           C  
ANISOU 1161  CE  LYS A  77    14472  19701  18101   -365  -1811   -343       C  
ATOM   1162  NZ  LYS A  77      60.157  -6.770  15.577  1.00113.88           N  
ANISOU 1162  NZ  LYS A  77    11157  16816  15295   -478  -1669   -347       N  
ATOM   1163  N   VAL A  78      54.726  -8.260  19.410  1.00110.37           N  
ANISOU 1163  N   VAL A  78    12468  15464  14003   -254  -1852   -437       N  
ATOM   1164  CA  VAL A  78      53.408  -7.645  19.560  1.00110.89           C  
ANISOU 1164  CA  VAL A  78    12861  15285  13987   -376  -1714   -512       C  
ATOM   1165  C   VAL A  78      52.612  -7.764  18.265  1.00106.81           C  
ANISOU 1165  C   VAL A  78    12408  14590  13584   -285  -1455   -496       C  
ATOM   1166  O   VAL A  78      51.377  -7.711  18.281  1.00 99.59           O  
ANISOU 1166  O   VAL A  78    11758  13475  12607   -282  -1332   -520       O  
ATOM   1167  CB  VAL A  78      53.536  -6.171  19.998  1.00120.04           C  
ANISOU 1167  CB  VAL A  78    14057  16445  15109   -699  -1748   -631       C  
ATOM   1168  CG1 VAL A  78      52.528  -5.275  19.272  1.00121.48           C  
ANISOU 1168  CG1 VAL A  78    14424  16405  15326   -812  -1506   -704       C  
ATOM   1169  CG2 VAL A  78      53.352  -6.052  21.504  1.00127.38           C  
ANISOU 1169  CG2 VAL A  78    15194  17373  15831   -784  -1938   -666       C  
ATOM   1170  N   SER A  79      53.305  -7.926  17.137  1.00 99.74           N  
ANISOU 1170  N   SER A  79    11273  13771  12854   -206  -1370   -453       N  
ATOM   1171  CA  SER A  79      52.606  -8.115  15.870  1.00 91.13           C  
ANISOU 1171  CA  SER A  79    10258  12506  11862   -102  -1140   -432       C  
ATOM   1172  C   SER A  79      51.662  -9.309  15.940  1.00 78.09           C  
ANISOU 1172  C   SER A  79     8823  10717  10130    117  -1108   -359       C  
ATOM   1173  O   SER A  79      50.526  -9.240  15.459  1.00 70.91           O  
ANISOU 1173  O   SER A  79     8113   9609   9219    120   -956   -377       O  
ATOM   1174  CB  SER A  79      53.612  -8.300  14.735  1.00101.28           C  
ANISOU 1174  CB  SER A  79    11262  13903  13317    -11  -1067   -379       C  
ATOM   1175  OG  SER A  79      54.455  -7.169  14.614  1.00 99.97           O  
ANISOU 1175  OG  SER A  79    10893  13860  13232   -242  -1076   -449       O  
ATOM   1176  N   SER A  80      52.114 -10.414  16.538  1.00 84.13           N  
ANISOU 1176  N   SER A  80     9558  11585  10822    298  -1254   -274       N  
ATOM   1177  CA  SER A  80      51.262 -11.594  16.644  1.00 78.20           C  
ANISOU 1177  CA  SER A  80     9037  10697   9978    490  -1225   -201       C  
ATOM   1178  C   SER A  80      49.962 -11.283  17.374  1.00 70.77           C  
ANISOU 1178  C   SER A  80     8383   9593   8915    370  -1189   -259       C  
ATOM   1179  O   SER A  80      48.936 -11.922  17.110  1.00 67.62           O  
ANISOU 1179  O   SER A  80     8180   9030   8481    456  -1086   -224       O  
ATOM   1180  CB  SER A  80      52.010 -12.719  17.360  1.00 86.40           C  
ANISOU 1180  CB  SER A  80    10031  11875  10923    689  -1405   -111       C  
ATOM   1181  OG  SER A  80      53.124 -13.153  16.602  1.00 93.16           O  
ANISOU 1181  OG  SER A  80    10628  12876  11892    852  -1411    -39       O  
ATOM   1182  N   ILE A  81      49.981 -10.317  18.295  1.00 67.93           N  
ANISOU 1182  N   ILE A  81     8055   9274   8482    170  -1271   -344       N  
ATOM   1183  CA  ILE A  81      48.754  -9.941  18.992  1.00 69.08           C  
ANISOU 1183  CA  ILE A  81     8473   9266   8509     65  -1214   -397       C  
ATOM   1184  C   ILE A  81      47.733  -9.393  18.003  1.00 66.64           C  
ANISOU 1184  C   ILE A  81     8243   8788   8290     14   -994   -437       C  
ATOM   1185  O   ILE A  81      46.535  -9.686  18.096  1.00 66.05           O  
ANISOU 1185  O   ILE A  81     8367   8569   8160     43   -896   -428       O  
ATOM   1186  CB  ILE A  81      49.060  -8.917  20.102  1.00 72.56           C  
ANISOU 1186  CB  ILE A  81     8949   9773   8847   -139  -1336   -483       C  
ATOM   1187  CG1 ILE A  81      50.109  -9.463  21.074  1.00 73.01           C  
ANISOU 1187  CG1 ILE A  81     8919  10009   8813    -84  -1582   -444       C  
ATOM   1188  CG2 ILE A  81      47.784  -8.547  20.851  1.00 68.74           C  
ANISOU 1188  CG2 ILE A  81     8763   9127   8230   -222  -1257   -530       C  
ATOM   1189  CD1 ILE A  81      49.733 -10.773  21.727  1.00 69.67           C  
ANISOU 1189  CD1 ILE A  81     8669   9544   8258    111  -1643   -360       C  
ATOM   1190  N   TYR A  82      48.191  -8.590  17.041  1.00 67.94           N  
ANISOU 1190  N   TYR A  82     8250   8973   8592    -62   -915   -479       N  
ATOM   1191  CA  TYR A  82      47.290  -8.071  16.020  1.00 55.73           C  
ANISOU 1191  CA  TYR A  82     6781   7267   7128    -89   -717   -515       C  
ATOM   1192  C   TYR A  82      46.880  -9.157  15.033  1.00 50.92           C  
ANISOU 1192  C   TYR A  82     6187   6572   6589    105   -629   -430       C  
ATOM   1193  O   TYR A  82      45.756  -9.134  14.520  1.00 51.82           O  
ANISOU 1193  O   TYR A  82     6439   6534   6717    118   -501   -438       O  
ATOM   1194  CB  TYR A  82      47.956  -6.905  15.290  1.00 62.04           C  
ANISOU 1194  CB  TYR A  82     7438   8100   8036   -228   -656   -586       C  
ATOM   1195  CG  TYR A  82      48.334  -5.750  16.193  1.00 67.90           C  
ANISOU 1195  CG  TYR A  82     8197   8903   8698   -451   -738   -678       C  
ATOM   1196  CD1 TYR A  82      47.606  -5.471  17.345  1.00 69.99           C  
ANISOU 1196  CD1 TYR A  82     8675   9111   8806   -524   -781   -717       C  
ATOM   1197  CD2 TYR A  82      49.425  -4.943  15.899  1.00 73.05           C  
ANISOU 1197  CD2 TYR A  82     8666   9666   9425   -597   -768   -724       C  
ATOM   1198  CE1 TYR A  82      47.950  -4.417  18.172  1.00 71.35           C  
ANISOU 1198  CE1 TYR A  82     8904   9320   8885   -728   -858   -800       C  
ATOM   1199  CE2 TYR A  82      49.777  -3.887  16.721  1.00 76.52           C  
ANISOU 1199  CE2 TYR A  82     9145  10151   9779   -824   -853   -809       C  
ATOM   1200  CZ  TYR A  82      49.036  -3.629  17.856  1.00 77.37           C  
ANISOU 1200  CZ  TYR A  82     9493  10186   9718   -885   -902   -847       C  
ATOM   1201  OH  TYR A  82      49.383  -2.581  18.676  1.00 80.58           O  
ANISOU 1201  OH  TYR A  82     9980  10618  10020  -1112   -990   -932       O  
ATOM   1202  N   ILE A  83      47.768 -10.114  14.760  1.00 54.23           N  
ANISOU 1202  N   ILE A  83     6475   7086   7044    260   -700   -345       N  
ATOM   1203  CA  ILE A  83      47.413 -11.225  13.882  1.00 50.51           C  
ANISOU 1203  CA  ILE A  83     6063   6517   6610    449   -626   -258       C  
ATOM   1204  C   ILE A  83      46.274 -12.030  14.493  1.00 50.24           C  
ANISOU 1204  C   ILE A  83     6262   6371   6455    495   -630   -222       C  
ATOM   1205  O   ILE A  83      45.309 -12.396  13.811  1.00 54.21           O  
ANISOU 1205  O   ILE A  83     6891   6726   6980    534   -521   -201       O  
ATOM   1206  CB  ILE A  83      48.642 -12.113  13.614  1.00 55.09           C  
ANISOU 1206  CB  ILE A  83     6479   7228   7226    629   -704   -168       C  
ATOM   1207  CG1 ILE A  83      49.795 -11.294  13.029  1.00 53.01           C  
ANISOU 1207  CG1 ILE A  83     5952   7096   7093    566   -687   -200       C  
ATOM   1208  CG2 ILE A  83      48.277 -13.248  12.674  1.00 55.22           C  
ANISOU 1208  CG2 ILE A  83     6604   7117   7261    826   -620    -77       C  
ATOM   1209  CD1 ILE A  83      49.478 -10.630  11.715  1.00 62.44           C  
ANISOU 1209  CD1 ILE A  83     7148   8166   8412    519   -503   -239       C  
ATOM   1210  N   PHE A  84      46.375 -12.327  15.790  1.00 50.77           N  
ANISOU 1210  N   PHE A  84     6396   6508   6388    482   -758   -214       N  
ATOM   1211  CA  PHE A  84      45.337 -13.108  16.453  1.00 50.29           C  
ANISOU 1211  CA  PHE A  84     6564   6342   6200    513   -751   -177       C  
ATOM   1212  C   PHE A  84      44.001 -12.375  16.428  1.00 48.83           C  
ANISOU 1212  C   PHE A  84     6502   6032   6018    377   -618   -241       C  
ATOM   1213  O   PHE A  84      42.977 -12.940  16.027  1.00 48.55           O  
ANISOU 1213  O   PHE A  84     6589   5874   5983    410   -526   -206       O  
ATOM   1214  CB  PHE A  84      45.753 -13.416  17.892  1.00 51.98           C  
ANISOU 1214  CB  PHE A  84     6842   6650   6259    516   -910   -166       C  
ATOM   1215  CG  PHE A  84      44.745 -14.230  18.651  1.00 51.75           C  
ANISOU 1215  CG  PHE A  84     7065   6511   6087    540   -892   -127       C  
ATOM   1216  CD1 PHE A  84      44.720 -15.609  18.531  1.00 51.97           C  
ANISOU 1216  CD1 PHE A  84     7205   6489   6054    704   -912    -30       C  
ATOM   1217  CD2 PHE A  84      43.819 -13.616  19.478  1.00 51.47           C  
ANISOU 1217  CD2 PHE A  84     7171   6416   5970    399   -842   -186       C  
ATOM   1218  CE1 PHE A  84      43.794 -16.362  19.225  1.00 52.19           C  
ANISOU 1218  CE1 PHE A  84     7477   6409   5944    704   -885      6       C  
ATOM   1219  CE2 PHE A  84      42.890 -14.363  20.174  1.00 51.45           C  
ANISOU 1219  CE2 PHE A  84     7392   6317   5839    411   -806   -146       C  
ATOM   1220  CZ  PHE A  84      42.877 -15.738  20.048  1.00 51.68           C  
ANISOU 1220  CZ  PHE A  84     7527   6297   5812    552   -828    -52       C  
ATOM   1221  N   ASN A  85      43.993 -11.109  16.854  1.00 49.03           N  
ANISOU 1221  N   ASN A  85     6499   6090   6040    223   -608   -334       N  
ATOM   1222  CA  ASN A  85      42.749 -10.347  16.875  1.00 47.90           C  
ANISOU 1222  CA  ASN A  85     6472   5839   5889    120   -476   -393       C  
ATOM   1223  C   ASN A  85      42.176 -10.167  15.477  1.00 49.77           C  
ANISOU 1223  C   ASN A  85     6673   5977   6260    149   -340   -398       C  
ATOM   1224  O   ASN A  85      40.951 -10.137  15.310  1.00 46.94           O  
ANISOU 1224  O   ASN A  85     6416   5520   5900    134   -235   -402       O  
ATOM   1225  CB  ASN A  85      42.976  -8.985  17.531  1.00 48.63           C  
ANISOU 1225  CB  ASN A  85     6566   5973   5938    -36   -491   -491       C  
ATOM   1226  CG  ASN A  85      43.033  -9.069  19.042  1.00 50.01           C  
ANISOU 1226  CG  ASN A  85     6865   6191   5944    -83   -597   -497       C  
ATOM   1227  OD1 ASN A  85      42.047  -8.795  19.727  1.00 49.83           O  
ANISOU 1227  OD1 ASN A  85     7012   6094   5828   -133   -524   -520       O  
ATOM   1228  ND2 ASN A  85      44.187  -9.454  19.570  1.00 54.28           N  
ANISOU 1228  ND2 ASN A  85     7325   6856   6442    -57   -768   -472       N  
ATOM   1229  N   LEU A  86      43.035 -10.045  14.464  1.00 46.25           N  
ANISOU 1229  N   LEU A  86     6083   5560   5930    192   -337   -394       N  
ATOM   1230  CA  LEU A  86      42.539  -9.929  13.097  1.00 44.87           C  
ANISOU 1230  CA  LEU A  86     5901   5277   5870    233   -215   -395       C  
ATOM   1231  C   LEU A  86      41.855 -11.217  12.656  1.00 45.22           C  
ANISOU 1231  C   LEU A  86     6041   5232   5908    350   -199   -307       C  
ATOM   1232  O   LEU A  86      40.849 -11.178  11.938  1.00 49.05           O  
ANISOU 1232  O   LEU A  86     6593   5606   6438    350   -107   -311       O  
ATOM   1233  CB  LEU A  86      43.687  -9.573  12.154  1.00 45.20           C  
ANISOU 1233  CB  LEU A  86     5784   5364   6024    258   -206   -404       C  
ATOM   1234  CG  LEU A  86      43.316  -9.360  10.685  1.00 49.65           C  
ANISOU 1234  CG  LEU A  86     6359   5805   6700    304    -80   -411       C  
ATOM   1235  CD1 LEU A  86      42.306  -8.231  10.537  1.00 49.85           C  
ANISOU 1235  CD1 LEU A  86     6472   5740   6728    202     21   -497       C  
ATOM   1236  CD2 LEU A  86      44.560  -9.074   9.860  1.00 44.70           C  
ANISOU 1236  CD2 LEU A  86     5578   5231   6173    330    -60   -412       C  
ATOM   1237  N   ALA A  87      42.382 -12.366  13.083  1.00 45.39           N  
ANISOU 1237  N   ALA A  87     6082   5298   5866    449   -293   -226       N  
ATOM   1238  CA  ALA A  87      41.790 -13.640  12.691  1.00 44.94           C  
ANISOU 1238  CA  ALA A  87     6154   5142   5781    548   -281   -140       C  
ATOM   1239  C   ALA A  87      40.472 -13.886  13.416  1.00 46.54           C  
ANISOU 1239  C   ALA A  87     6505   5281   5897    469   -248   -138       C  
ATOM   1240  O   ALA A  87      39.514 -14.390  12.817  1.00 51.83           O  
ANISOU 1240  O   ALA A  87     7263   5844   6587    472   -187   -106       O  
ATOM   1241  CB  ALA A  87      42.771 -14.779  12.967  1.00 46.15           C  
ANISOU 1241  CB  ALA A  87     6314   5353   5869    693   -385    -53       C  
ATOM   1242  N   VAL A  88      40.403 -13.544  14.704  1.00 44.98           N  
ANISOU 1242  N   VAL A  88     6340   5150   5601    393   -286   -170       N  
ATOM   1243  CA  VAL A  88      39.161 -13.723  15.452  1.00 44.89           C  
ANISOU 1243  CA  VAL A  88     6465   5087   5506    317   -231   -167       C  
ATOM   1244  C   VAL A  88      38.052 -12.875  14.842  1.00 46.59           C  
ANISOU 1244  C   VAL A  88     6654   5242   5806    241   -105   -221       C  
ATOM   1245  O   VAL A  88      36.932 -13.350  14.618  1.00 43.94           O  
ANISOU 1245  O   VAL A  88     6385   4836   5475    219    -39   -188       O  
ATOM   1246  CB  VAL A  88      39.376 -13.386  16.939  1.00 47.92           C  
ANISOU 1246  CB  VAL A  88     6905   5544   5760    257   -287   -197       C  
ATOM   1247  CG1 VAL A  88      38.042 -13.268  17.662  1.00 47.53           C  
ANISOU 1247  CG1 VAL A  88     6979   5441   5638    168   -188   -208       C  
ATOM   1248  CG2 VAL A  88      40.244 -14.448  17.599  1.00 47.32           C  
ANISOU 1248  CG2 VAL A  88     6892   5513   5576    352   -419   -130       C  
ATOM   1249  N   ALA A  89      38.349 -11.606  14.560  1.00 45.75           N  
ANISOU 1249  N   ALA A  89     6453   5165   5764    198    -72   -302       N  
ATOM   1250  CA  ALA A  89      37.375 -10.752  13.890  1.00 42.55           C  
ANISOU 1250  CA  ALA A  89     6032   4702   5435    158     44   -354       C  
ATOM   1251  C   ALA A  89      36.983 -11.337  12.540  1.00 46.95           C  
ANISOU 1251  C   ALA A  89     6575   5173   6091    223     71   -311       C  
ATOM   1252  O   ALA A  89      35.797 -11.402  12.198  1.00 51.29           O  
ANISOU 1252  O   ALA A  89     7152   5667   6667    203    137   -303       O  
ATOM   1253  CB  ALA A  89      37.940  -9.341  13.725  1.00 49.26           C  
ANISOU 1253  CB  ALA A  89     6815   5579   6322    111     70   -446       C  
ATOM   1254  N   ASP A  90      37.972 -11.782  11.761  1.00 54.55           N  
ANISOU 1254  N   ASP A  90     7496   6125   7105    304     19   -279       N  
ATOM   1255  CA  ASP A  90      37.673 -12.393  10.470  1.00 54.40           C  
ANISOU 1255  CA  ASP A  90     7504   6005   7162    372     39   -234       C  
ATOM   1256  C   ASP A  90      36.808 -13.635  10.641  1.00 55.32           C  
ANISOU 1256  C   ASP A  90     7736   6065   7220    370     21   -155       C  
ATOM   1257  O   ASP A  90      35.871 -13.858   9.867  1.00 54.54           O  
ANISOU 1257  O   ASP A  90     7675   5883   7166    356     56   -139       O  
ATOM   1258  CB  ASP A  90      38.971 -12.740   9.739  1.00 57.65           C  
ANISOU 1258  CB  ASP A  90     7869   6417   7617    477     -1   -202       C  
ATOM   1259  CG  ASP A  90      39.692 -11.509   9.207  1.00 58.73           C  
ANISOU 1259  CG  ASP A  90     7894   6582   7838    460     44   -279       C  
ATOM   1260  OD1 ASP A  90      39.012 -10.505   8.904  1.00 59.65           O  
ANISOU 1260  OD1 ASP A  90     8012   6659   7992    399    117   -349       O  
ATOM   1261  OD2 ASP A  90      40.937 -11.547   9.085  1.00 53.86           O  
ANISOU 1261  OD2 ASP A  90     7191   6029   7246    511     10   -266       O  
ATOM   1262  N   LEU A  91      37.104 -14.453  11.652  1.00 45.04           N  
ANISOU 1262  N   LEU A  91     6501   4803   5809    376    -38   -105       N  
ATOM   1263  CA  LEU A  91      36.307 -15.653  11.883  1.00 47.80           C  
ANISOU 1263  CA  LEU A  91     6989   5088   6085    354    -46    -30       C  
ATOM   1264  C   LEU A  91      34.883 -15.300  12.294  1.00 50.16           C  
ANISOU 1264  C   LEU A  91     7288   5387   6382    232     33    -54       C  
ATOM   1265  O   LEU A  91      33.923 -15.926  11.829  1.00 48.97           O  
ANISOU 1265  O   LEU A  91     7192   5167   6246    186     55    -13       O  
ATOM   1266  CB  LEU A  91      36.965 -16.527  12.949  1.00 48.30           C  
ANISOU 1266  CB  LEU A  91     7149   5189   6015    395   -120     23       C  
ATOM   1267  CG  LEU A  91      38.178 -17.347  12.512  1.00 43.70           C  
ANISOU 1267  CG  LEU A  91     6600   4594   5410    546   -200     85       C  
ATOM   1268  CD1 LEU A  91      38.845 -17.988  13.721  1.00 45.01           C  
ANISOU 1268  CD1 LEU A  91     6846   4822   5434    598   -283    124       C  
ATOM   1269  CD2 LEU A  91      37.773 -18.407  11.498  1.00 43.45           C  
ANISOU 1269  CD2 LEU A  91     6706   4423   5380    591   -190    158       C  
ATOM   1270  N   LEU A  92      34.724 -14.306  13.171  1.00 47.26           N  
ANISOU 1270  N   LEU A  92     6864   5098   5994    177     77   -119       N  
ATOM   1271  CA  LEU A  92      33.393 -13.967  13.664  1.00 45.07           C  
ANISOU 1271  CA  LEU A  92     6583   4835   5707     84    171   -134       C  
ATOM   1272  C   LEU A  92      32.541 -13.318  12.577  1.00 47.60           C  
ANISOU 1272  C   LEU A  92     6812   5127   6148     77    232   -168       C  
ATOM   1273  O   LEU A  92      31.337 -13.587  12.486  1.00 49.81           O  
ANISOU 1273  O   LEU A  92     7080   5398   6447     17    283   -142       O  
ATOM   1274  CB  LEU A  92      33.504 -13.056  14.886  1.00 48.03           C  
ANISOU 1274  CB  LEU A  92     6957   5287   6008     48    209   -191       C  
ATOM   1275  CG  LEU A  92      34.101 -13.712  16.134  1.00 44.07           C  
ANISOU 1275  CG  LEU A  92     6569   4812   5363     43    148   -157       C  
ATOM   1276  CD1 LEU A  92      34.296 -12.692  17.243  1.00 44.69           C  
ANISOU 1276  CD1 LEU A  92     6665   4952   5364      7    172   -222       C  
ATOM   1277  CD2 LEU A  92      33.222 -14.860  16.610  1.00 44.75           C  
ANISOU 1277  CD2 LEU A  92     6771   4857   5374     -9    182    -82       C  
ATOM   1278  N   LEU A  93      33.137 -12.459  11.745  1.00 42.99           N  
ANISOU 1278  N   LEU A  93     6160   4530   5643    137    227   -224       N  
ATOM   1279  CA  LEU A  93      32.369 -11.863  10.656  1.00 47.60           C  
ANISOU 1279  CA  LEU A  93     6683   5072   6329    152    273   -255       C  
ATOM   1280  C   LEU A  93      32.116 -12.886   9.556  1.00 49.58           C  
ANISOU 1280  C   LEU A  93     6977   5233   6627    171    218   -192       C  
ATOM   1281  O   LEU A  93      31.045 -12.893   8.936  1.00 43.64           O  
ANISOU 1281  O   LEU A  93     6196   4455   5930    145    236   -185       O  
ATOM   1282  CB  LEU A  93      33.088 -10.634  10.100  1.00 47.59           C  
ANISOU 1282  CB  LEU A  93     6636   5064   6381    205    295   -336       C  
ATOM   1283  CG  LEU A  93      34.379 -10.840   9.304  1.00 55.95           C  
ANISOU 1283  CG  LEU A  93     7700   6079   7478    272    237   -330       C  
ATOM   1284  CD1 LEU A  93      34.096 -11.085   7.829  1.00 47.59           C  
ANISOU 1284  CD1 LEU A  93     6663   4915   6505    330    231   -312       C  
ATOM   1285  CD2 LEU A  93      35.299  -9.638   9.475  1.00 57.25           C  
ANISOU 1285  CD2 LEU A  93     7821   6283   7648    269    263   -410       C  
ATOM   1286  N   LEU A  94      33.088 -13.764   9.302  1.00 53.57           N  
ANISOU 1286  N   LEU A  94     7559   5691   7106    223    146   -142       N  
ATOM   1287  CA  LEU A  94      32.861 -14.848   8.355  1.00 50.14           C  
ANISOU 1287  CA  LEU A  94     7217   5150   6684    239     94    -73       C  
ATOM   1288  C   LEU A  94      31.790 -15.802   8.864  1.00 44.24           C  
ANISOU 1288  C   LEU A  94     6533   4396   5879    131     90    -12       C  
ATOM   1289  O   LEU A  94      31.119 -16.466   8.067  1.00 46.39           O  
ANISOU 1289  O   LEU A  94     6865   4588   6174     93     57     30       O  
ATOM   1290  CB  LEU A  94      34.164 -15.605   8.097  1.00 47.93           C  
ANISOU 1290  CB  LEU A  94     7023   4822   6365    341     35    -26       C  
ATOM   1291  CG  LEU A  94      35.193 -14.925   7.191  1.00 47.52           C  
ANISOU 1291  CG  LEU A  94     6920   4748   6389    446     44    -65       C  
ATOM   1292  CD1 LEU A  94      36.506 -15.699   7.199  1.00 45.97           C  
ANISOU 1292  CD1 LEU A  94     6776   4546   6146    557     -3     -8       C  
ATOM   1293  CD2 LEU A  94      34.665 -14.796   5.776  1.00 47.83           C  
ANISOU 1293  CD2 LEU A  94     6997   4671   6506    472     55    -71       C  
ATOM   1294  N   ALA A  95      31.615 -15.882  10.186  1.00 49.22           N  
ANISOU 1294  N   ALA A  95     7165   5106   6429     69    123     -7       N  
ATOM   1295  CA  ALA A  95      30.615 -16.772  10.761  1.00 48.02           C  
ANISOU 1295  CA  ALA A  95     7077   4950   6216    -50    141     52       C  
ATOM   1296  C   ALA A  95      29.193 -16.300  10.490  1.00 49.97           C  
ANISOU 1296  C   ALA A  95     7203   5239   6544   -141    201     33       C  
ATOM   1297  O   ALA A  95      28.254 -17.091  10.629  1.00 53.43           O  
ANISOU 1297  O   ALA A  95     7671   5669   6960   -260    210     88       O  
ATOM   1298  CB  ALA A  95      30.838 -16.904  12.268  1.00 46.50           C  
ANISOU 1298  CB  ALA A  95     6935   4823   5908    -81    174     59       C  
ATOM   1299  N   THR A  96      29.010 -15.036  10.111  1.00 52.61           N  
ANISOU 1299  N   THR A  96     7402   5621   6964    -88    244    -39       N  
ATOM   1300  CA  THR A  96      27.689 -14.518   9.784  1.00 42.30           C  
ANISOU 1300  CA  THR A  96     5965   4369   5738   -137    295    -56       C  
ATOM   1301  C   THR A  96      27.331 -14.699   8.315  1.00 41.81           C  
ANISOU 1301  C   THR A  96     5895   4230   5763   -121    218    -47       C  
ATOM   1302  O   THR A  96      26.194 -14.407   7.932  1.00 51.95           O  
ANISOU 1302  O   THR A  96     7064   5561   7115   -161    233    -52       O  
ATOM   1303  CB  THR A  96      27.594 -13.030  10.144  1.00 41.95           C  
ANISOU 1303  CB  THR A  96     5811   4407   5721    -69    386   -138       C  
ATOM   1304  OG1 THR A  96      28.558 -12.286   9.389  1.00 45.84           O  
ANISOU 1304  OG1 THR A  96     6322   4845   6252     40    354   -196       O  
ATOM   1305  CG2 THR A  96      27.843 -12.819  11.626  1.00 46.52           C  
ANISOU 1305  CG2 THR A  96     6422   5053   6201    -95    460   -147       C  
ATOM   1306  N   LEU A  97      28.265 -15.167   7.488  1.00 44.45           N  
ANISOU 1306  N   LEU A  97     6349   4447   6091    -54    138    -32       N  
ATOM   1307  CA  LEU A  97      27.956 -15.378   6.078  1.00 48.31           C  
ANISOU 1307  CA  LEU A  97     6874   4838   6644    -35     62    -22       C  
ATOM   1308  C   LEU A  97      26.783 -16.326   5.875  1.00 50.28           C  
ANISOU 1308  C   LEU A  97     7135   5077   6893   -179     11     42       C  
ATOM   1309  O   LEU A  97      25.919 -16.023   5.033  1.00 42.19           O  
ANISOU 1309  O   LEU A  97     6031   4054   5944   -196    -29     29       O  
ATOM   1310  CB  LEU A  97      29.202 -15.896   5.349  1.00 49.43           C  
ANISOU 1310  CB  LEU A  97     7176   4847   6757     63      2      0       C  
ATOM   1311  CG  LEU A  97      30.195 -14.841   4.860  1.00 48.50           C  
ANISOU 1311  CG  LEU A  97     7028   4713   6685    202     35    -69       C  
ATOM   1312  CD1 LEU A  97      31.517 -15.489   4.494  1.00 52.15           C  
ANISOU 1312  CD1 LEU A  97     7624   5084   7107    295      2    -31       C  
ATOM   1313  CD2 LEU A  97      29.630 -14.084   3.667  1.00 42.56           C  
ANISOU 1313  CD2 LEU A  97     6242   3910   6019    248     24   -115       C  
ATOM   1314  N   PRO A  98      26.685 -17.459   6.576  1.00 51.69           N  
ANISOU 1314  N   PRO A  98     7413   5241   6984   -292      3    110       N  
ATOM   1315  CA  PRO A  98      25.503 -18.319   6.401  1.00 49.35           C  
ANISOU 1315  CA  PRO A  98     7121   4941   6689   -467    -39    168       C  
ATOM   1316  C   PRO A  98      24.191 -17.596   6.647  1.00 44.89           C  
ANISOU 1316  C   PRO A  98     6314   4532   6212   -542     18    144       C  
ATOM   1317  O   PRO A  98      23.187 -17.922   6.001  1.00 50.61           O  
ANISOU 1317  O   PRO A  98     6977   5265   6989   -650    -46    170       O  
ATOM   1318  CB  PRO A  98      25.734 -19.442   7.423  1.00 46.08           C  
ANISOU 1318  CB  PRO A  98     6859   4500   6147   -565    -15    233       C  
ATOM   1319  CG  PRO A  98      27.215 -19.490   7.596  1.00 43.94           C  
ANISOU 1319  CG  PRO A  98     6726   4162   5807   -407    -23    225       C  
ATOM   1320  CD  PRO A  98      27.687 -18.068   7.470  1.00 42.79           C  
ANISOU 1320  CD  PRO A  98     6422   4090   5746   -266     20    140       C  
ATOM   1321  N   LEU A  99      24.163 -16.627   7.565  1.00 44.75           N  
ANISOU 1321  N   LEU A  99     6159   4637   6205   -483    136     96       N  
ATOM   1322  CA  LEU A  99      22.940 -15.862   7.787  1.00 47.31           C  
ANISOU 1322  CA  LEU A  99     6252   5114   6609   -514    209     76       C  
ATOM   1323  C   LEU A  99      22.538 -15.085   6.539  1.00 50.36           C  
ANISOU 1323  C   LEU A  99     6537   5499   7100   -419    142     32       C  
ATOM   1324  O   LEU A  99      21.359 -15.058   6.168  1.00 53.63           O  
ANISOU 1324  O   LEU A  99     6793   5997   7586   -487    117     49       O  
ATOM   1325  CB  LEU A  99      23.123 -14.906   8.965  1.00 45.53           C  
ANISOU 1325  CB  LEU A  99     5953   4991   6353   -438    354     30       C  
ATOM   1326  CG  LEU A  99      23.387 -15.529  10.335  1.00 49.96           C  
ANISOU 1326  CG  LEU A  99     6610   5568   6803   -522    432     68       C  
ATOM   1327  CD1 LEU A  99      23.608 -14.440  11.375  1.00 52.28           C  
ANISOU 1327  CD1 LEU A  99     6857   5945   7060   -430    560     14       C  
ATOM   1328  CD2 LEU A  99      22.240 -16.436  10.747  1.00 52.76           C  
ANISOU 1328  CD2 LEU A  99     6911   5983   7153   -714    468    141       C  
ATOM   1329  N   TRP A 100      23.507 -14.452   5.871  1.00 48.22           N  
ANISOU 1329  N   TRP A 100     6354   5133   6835   -263    112    -23       N  
ATOM   1330  CA  TRP A 100      23.192 -13.637   4.703  1.00 47.67           C  
ANISOU 1330  CA  TRP A 100     6225   5043   6846   -154     59    -72       C  
ATOM   1331  C   TRP A 100      22.934 -14.481   3.460  1.00 50.04           C  
ANISOU 1331  C   TRP A 100     6618   5227   7168   -212    -95    -31       C  
ATOM   1332  O   TRP A 100      22.178 -14.059   2.578  1.00 44.28           O  
ANISOU 1332  O   TRP A 100     5803   4513   6507   -179   -163    -50       O  
ATOM   1333  CB  TRP A 100      24.326 -12.646   4.430  1.00 49.08           C  
ANISOU 1333  CB  TRP A 100     6484   5149   7015     16     97   -145       C  
ATOM   1334  CG  TRP A 100      24.924 -12.054   5.671  1.00 51.47           C  
ANISOU 1334  CG  TRP A 100     6772   5520   7263     47    220   -179       C  
ATOM   1335  CD1 TRP A 100      26.252 -11.896   5.944  1.00 44.80           C  
ANISOU 1335  CD1 TRP A 100     6041   4615   6368    103    239   -205       C  
ATOM   1336  CD2 TRP A 100      24.217 -11.548   6.810  1.00 49.06           C  
ANISOU 1336  CD2 TRP A 100     6338   5360   6943     21    336   -187       C  
ATOM   1337  NE1 TRP A 100      26.415 -11.319   7.180  1.00 43.93           N  
ANISOU 1337  NE1 TRP A 100     5890   4595   6206    102    342   -233       N  
ATOM   1338  CE2 TRP A 100      25.181 -11.096   7.732  1.00 48.36           C  
ANISOU 1338  CE2 TRP A 100     6320   5272   6782     58    411   -222       C  
ATOM   1339  CE3 TRP A 100      22.864 -11.432   7.139  1.00 46.29           C  
ANISOU 1339  CE3 TRP A 100     5815   5141   6632    -28    388   -164       C  
ATOM   1340  CZ2 TRP A 100      24.834 -10.537   8.960  1.00 49.05           C  
ANISOU 1340  CZ2 TRP A 100     6349   5466   6821     50    534   -238       C  
ATOM   1341  CZ3 TRP A 100      22.522 -10.877   8.358  1.00 44.69           C  
ANISOU 1341  CZ3 TRP A 100     5538   5053   6389    -22    531   -175       C  
ATOM   1342  CH2 TRP A 100      23.502 -10.436   9.253  1.00 45.57           C  
ANISOU 1342  CH2 TRP A 100     5760   5139   6414     18    602   -213       C  
ATOM   1343  N   ALA A 101      23.544 -15.663   3.368  1.00 46.71           N  
ANISOU 1343  N   ALA A 101     6389   4682   6677   -289   -157     25       N  
ATOM   1344  CA  ALA A 101      23.248 -16.558   2.254  1.00 44.20           C  
ANISOU 1344  CA  ALA A 101     6200   4238   6355   -364   -303     70       C  
ATOM   1345  C   ALA A 101      21.814 -17.067   2.334  1.00 50.14           C  
ANISOU 1345  C   ALA A 101     6810   5095   7145   -556   -357    116       C  
ATOM   1346  O   ALA A 101      21.091 -17.082   1.331  1.00 49.68           O  
ANISOU 1346  O   ALA A 101     6719   5018   7139   -587   -478    118       O  
ATOM   1347  CB  ALA A 101      24.237 -17.724   2.241  1.00 47.60           C  
ANISOU 1347  CB  ALA A 101     6895   4509   6681   -389   -338    125       C  
ATOM   1348  N   THR A 102      21.385 -17.490   3.524  1.00 48.80           N  
ANISOU 1348  N   THR A 102     6555   5039   6949   -693   -270    154       N  
ATOM   1349  CA  THR A 102      19.997 -17.902   3.700  1.00 52.73           C  
ANISOU 1349  CA  THR A 102     6877   5666   7494   -890   -294    199       C  
ATOM   1350  C   THR A 102      19.057 -16.710   3.565  1.00 56.24           C  
ANISOU 1350  C   THR A 102     7024   6289   8054   -805   -261    153       C  
ATOM   1351  O   THR A 102      17.958 -16.835   3.012  1.00 55.02           O  
ANISOU 1351  O   THR A 102     6716   6219   7972   -904   -353    175       O  
ATOM   1352  CB  THR A 102      19.819 -18.576   5.060  1.00 59.91           C  
ANISOU 1352  CB  THR A 102     7779   6647   8337  -1045   -177    249       C  
ATOM   1353  OG1 THR A 102      20.764 -19.645   5.193  1.00 61.67           O  
ANISOU 1353  OG1 THR A 102     8302   6695   8435  -1086   -207    290       O  
ATOM   1354  CG2 THR A 102      18.406 -19.130   5.202  1.00 69.83           C  
ANISOU 1354  CG2 THR A 102     8859   8031   9641  -1283   -195    304       C  
ATOM   1355  N   TYR A 103      19.474 -15.547   4.070  1.00 60.36           N  
ANISOU 1355  N   TYR A 103     7472   6875   8589   -620   -135     91       N  
ATOM   1356  CA  TYR A 103      18.669 -14.338   3.937  1.00 53.80           C  
ANISOU 1356  CA  TYR A 103     6400   6195   7846   -496    -90     45       C  
ATOM   1357  C   TYR A 103      18.474 -13.955   2.475  1.00 51.50           C  
ANISOU 1357  C   TYR A 103     6124   5834   7611   -397   -243     13       C  
ATOM   1358  O   TYR A 103      17.416 -13.433   2.106  1.00 50.21           O  
ANISOU 1358  O   TYR A 103     5747   5803   7527   -364   -279      6       O  
ATOM   1359  CB  TYR A 103      19.334 -13.201   4.715  1.00 49.81           C  
ANISOU 1359  CB  TYR A 103     5894   5720   7310   -317     70    -19       C  
ATOM   1360  CG  TYR A 103      18.634 -11.867   4.625  1.00 53.09           C  
ANISOU 1360  CG  TYR A 103     6118   6266   7787   -152    138    -71       C  
ATOM   1361  CD1 TYR A 103      17.335 -11.708   5.090  1.00 64.17           C  
ANISOU 1361  CD1 TYR A 103     7259   7873   9251   -196    202    -38       C  
ATOM   1362  CD2 TYR A 103      19.281 -10.757   4.103  1.00 53.14           C  
ANISOU 1362  CD2 TYR A 103     6213   6193   7785     54    152   -149       C  
ATOM   1363  CE1 TYR A 103      16.696 -10.483   5.022  1.00 59.54           C  
ANISOU 1363  CE1 TYR A 103     6507   7406   8708    -13    273    -80       C  
ATOM   1364  CE2 TYR A 103      18.652  -9.531   4.031  1.00 54.55           C  
ANISOU 1364  CE2 TYR A 103     6256   6474   7998    221    221   -196       C  
ATOM   1365  CZ  TYR A 103      17.360  -9.399   4.492  1.00 54.98           C  
ANISOU 1365  CZ  TYR A 103     6054   6730   8106    201    279   -160       C  
ATOM   1366  OH  TYR A 103      16.730  -8.178   4.421  1.00 60.40           O  
ANISOU 1366  OH  TYR A 103     6614   7519   8815    398    354   -201       O  
ATOM   1367  N   TYR A 104      19.477 -14.206   1.632  1.00 47.99           N  
ANISOU 1367  N   TYR A 104     5930   5183   7121   -336   -331     -4       N  
ATOM   1368  CA  TYR A 104      19.342 -13.922   0.208  1.00 47.41           C  
ANISOU 1368  CA  TYR A 104     5920   5010   7081   -244   -477    -32       C  
ATOM   1369  C   TYR A 104      18.533 -15.001  -0.501  1.00 56.93           C  
ANISOU 1369  C   TYR A 104     7139   6191   8302   -434   -657     31       C  
ATOM   1370  O   TYR A 104      17.707 -14.692  -1.368  1.00 53.34           O  
ANISOU 1370  O   TYR A 104     6584   5777   7907   -409   -781     21       O  
ATOM   1371  CB  TYR A 104      20.725 -13.792  -0.431  1.00 45.51           C  
ANISOU 1371  CB  TYR A 104     5954   4554   6783   -108   -483    -69       C  
ATOM   1372  CG  TYR A 104      20.702 -13.473  -1.910  1.00 45.36           C  
ANISOU 1372  CG  TYR A 104     6052   4400   6781      2   -615   -100       C  
ATOM   1373  CD1 TYR A 104      20.622 -14.488  -2.858  1.00 45.88           C  
ANISOU 1373  CD1 TYR A 104     6295   4319   6817    -96   -780    -54       C  
ATOM   1374  CD2 TYR A 104      20.769 -12.162  -2.360  1.00 44.81           C  
ANISOU 1374  CD2 TYR A 104     5953   4333   6741    206   -572   -177       C  
ATOM   1375  CE1 TYR A 104      20.603 -14.204  -4.209  1.00 45.85           C  
ANISOU 1375  CE1 TYR A 104     6429   4177   6816      9   -902    -82       C  
ATOM   1376  CE2 TYR A 104      20.752 -11.868  -3.709  1.00 44.78           C  
ANISOU 1376  CE2 TYR A 104     6083   4191   6739    314   -689   -207       C  
ATOM   1377  CZ  TYR A 104      20.668 -12.893  -4.630  1.00 45.91           C  
ANISOU 1377  CZ  TYR A 104     6397   4192   6856    217   -856   -159       C  
ATOM   1378  OH  TYR A 104      20.650 -12.608  -5.978  1.00 53.08           O  
ANISOU 1378  OH  TYR A 104     7469   4948   7753    329   -975   -188       O  
ATOM   1379  N   SER A 105      18.754 -16.269  -0.145  1.00 56.93           N  
ANISOU 1379  N   SER A 105     7276   6119   8236   -626   -680     97       N  
ATOM   1380  CA  SER A 105      18.044 -17.354  -0.812  1.00 56.31           C  
ANISOU 1380  CA  SER A 105     7255   5990   8149   -836   -855    158       C  
ATOM   1381  C   SER A 105      16.543 -17.271  -0.571  1.00 55.77           C  
ANISOU 1381  C   SER A 105     6857   6158   8177   -980   -889    183       C  
ATOM   1382  O   SER A 105      15.755 -17.697  -1.422  1.00 59.70           O  
ANISOU 1382  O   SER A 105     7324   6655   8704  -1102  -1070    209       O  
ATOM   1383  CB  SER A 105      18.579 -18.703  -0.334  1.00 57.83           C  
ANISOU 1383  CB  SER A 105     7683   6057   8233  -1011   -846    224       C  
ATOM   1384  OG  SER A 105      18.297 -18.895   1.041  1.00 65.20           O  
ANISOU 1384  OG  SER A 105     8470   7141   9160  -1124   -699    252       O  
ATOM   1385  N   TYR A 106      16.129 -16.734   0.577  1.00 53.63           N  
ANISOU 1385  N   TYR A 106     6334   6092   7951   -968   -718    180       N  
ATOM   1386  CA  TYR A 106      14.720 -16.523   0.879  1.00 61.18           C  
ANISOU 1386  CA  TYR A 106     6935   7303   9008  -1067   -712    206       C  
ATOM   1387  C   TYR A 106      14.232 -15.141   0.451  1.00 58.57           C  
ANISOU 1387  C   TYR A 106     6387   7102   8765   -824   -708    146       C  
ATOM   1388  O   TYR A 106      13.240 -14.644   0.995  1.00 57.76           O  
ANISOU 1388  O   TYR A 106     5964   7240   8743   -817   -627    159       O  
ATOM   1389  CB  TYR A 106      14.461 -16.754   2.370  1.00 57.50           C  
ANISOU 1389  CB  TYR A 106     6330   6983   8532  -1186   -511    244       C  
ATOM   1390  CG  TYR A 106      14.429 -18.223   2.740  1.00 58.03           C  
ANISOU 1390  CG  TYR A 106     6545   6975   8527  -1483   -540    320       C  
ATOM   1391  CD1 TYR A 106      13.438 -19.060   2.243  1.00 68.15           C  
ANISOU 1391  CD1 TYR A 106     7739   8308   9846  -1742   -688    377       C  
ATOM   1392  CD2 TYR A 106      15.387 -18.773   3.579  1.00 66.48           C  
ANISOU 1392  CD2 TYR A 106     7856   7921   9483  -1509   -427    333       C  
ATOM   1393  CE1 TYR A 106      13.402 -20.403   2.571  1.00 76.27           C  
ANISOU 1393  CE1 TYR A 106     8939   9249  10791  -2027   -708    444       C  
ATOM   1394  CE2 TYR A 106      15.359 -20.115   3.914  1.00 74.20           C  
ANISOU 1394  CE2 TYR A 106     9005   8813  10375  -1767   -448    402       C  
ATOM   1395  CZ  TYR A 106      14.364 -20.925   3.407  1.00 78.24           C  
ANISOU 1395  CZ  TYR A 106     9451   9361  10918  -2030   -582    456       C  
ATOM   1396  OH  TYR A 106      14.331 -22.261   3.736  1.00 87.42           O  
ANISOU 1396  OH  TYR A 106    10819  10420  11978  -2300   -596    524       O  
ATOM   1397  N   ARG A 107      14.907 -14.520  -0.513  1.00 60.96           N  
ANISOU 1397  N   ARG A 107     6870   7246   9046   -617   -784     85       N  
ATOM   1398  CA  ARG A 107      14.505 -13.239  -1.087  1.00 55.99           C  
ANISOU 1398  CA  ARG A 107     6103   6696   8475   -373   -801     25       C  
ATOM   1399  C   ARG A 107      14.238 -12.197  -0.002  1.00 55.12           C  
ANISOU 1399  C   ARG A 107     5773   6777   8393   -227   -581     -1       C  
ATOM   1400  O   ARG A 107      13.154 -11.622   0.105  1.00 56.84           O  
ANISOU 1400  O   ARG A 107     5698   7210   8688   -165   -564      6       O  
ATOM   1401  CB  ARG A 107      13.281 -13.421  -1.987  1.00 58.48           C  
ANISOU 1401  CB  ARG A 107     6231   7121   8868   -446  -1010     52       C  
ATOM   1402  CG  ARG A 107      13.592 -14.026  -3.350  1.00 56.82           C  
ANISOU 1402  CG  ARG A 107     6290   6684   8614   -493  -1245     51       C  
ATOM   1403  CD  ARG A 107      13.956 -15.499  -3.253  1.00 56.83           C  
ANISOU 1403  CD  ARG A 107     6502   6545   8547   -770  -1306    115       C  
ATOM   1404  NE  ARG A 107      14.013 -16.132  -4.568  1.00 57.21           N  
ANISOU 1404  NE  ARG A 107     6793   6394   8549   -837  -1545    125       N  
ATOM   1405  CZ  ARG A 107      14.482 -17.356  -4.795  1.00 57.08           C  
ANISOU 1405  CZ  ARG A 107     7063   6183   8442  -1028  -1623    172       C  
ATOM   1406  NH1 ARG A 107      14.955 -18.090  -3.796  1.00 56.56           N  
ANISOU 1406  NH1 ARG A 107     7072   6096   8321  -1165  -1485    213       N  
ATOM   1407  NH2 ARG A 107      14.488 -17.845  -6.028  1.00 57.58           N  
ANISOU 1407  NH2 ARG A 107     7366   6059   8454  -1069  -1839    179       N  
ATOM   1408  N   TYR A 108      15.271 -11.951   0.801  1.00 61.49           N  
ANISOU 1408  N   TYR A 108     6736   7499   9129   -164   -413    -29       N  
ATOM   1409  CA  TYR A 108      15.253 -10.899   1.814  1.00 61.57           C  
ANISOU 1409  CA  TYR A 108     6629   7634   9133    -10   -200    -64       C  
ATOM   1410  C   TYR A 108      14.028 -11.021   2.717  1.00 55.84           C  
ANISOU 1410  C   TYR A 108     5582   7167   8469   -110   -103     -6       C  
ATOM   1411  O   TYR A 108      13.297 -10.058   2.958  1.00 56.34           O  
ANISOU 1411  O   TYR A 108     5434   7398   8573     52    -10    -22       O  
ATOM   1412  CB  TYR A 108      15.320  -9.520   1.156  1.00 54.93           C  
ANISOU 1412  CB  TYR A 108     5808   6769   8295    274   -192   -143       C  
ATOM   1413  CG  TYR A 108      16.534  -9.346   0.273  1.00 57.07           C  
ANISOU 1413  CG  TYR A 108     6393   6786   8507    369   -262   -200       C  
ATOM   1414  CD1 TYR A 108      17.756  -8.964   0.809  1.00 60.12           C  
ANISOU 1414  CD1 TYR A 108     6971   7054   8817    431   -130   -244       C  
ATOM   1415  CD2 TYR A 108      16.462  -9.573  -1.094  1.00 66.95           C  
ANISOU 1415  CD2 TYR A 108     7748   7917   9774    390   -457   -207       C  
ATOM   1416  CE1 TYR A 108      18.872  -8.810   0.008  1.00 64.11           C  
ANISOU 1416  CE1 TYR A 108     7738   7342   9277    510   -177   -291       C  
ATOM   1417  CE2 TYR A 108      17.573  -9.421  -1.904  1.00 64.54           C  
ANISOU 1417  CE2 TYR A 108     7736   7375   9412    480   -497   -254       C  
ATOM   1418  CZ  TYR A 108      18.775  -9.039  -1.347  1.00 59.64           C  
ANISOU 1418  CZ  TYR A 108     7276   6655   8729    539   -348   -294       C  
ATOM   1419  OH  TYR A 108      19.885  -8.884  -2.144  1.00 56.22           O  
ANISOU 1419  OH  TYR A 108     7109   6004   8249    623   -371   -336       O  
ATOM   1420  N   ASP A 109      13.814 -12.231   3.229  1.00 58.43           N  
ANISOU 1420  N   ASP A 109     5885   7520   8794   -375   -112     65       N  
ATOM   1421  CA  ASP A 109      12.754 -12.525   4.190  1.00 58.79           C  
ANISOU 1421  CA  ASP A 109     5652   7797   8890   -517      7    129       C  
ATOM   1422  C   ASP A 109      13.427 -13.125   5.420  1.00 60.39           C  
ANISOU 1422  C   ASP A 109     6008   7935   9002   -643    163    154       C  
ATOM   1423  O   ASP A 109      13.783 -14.308   5.425  1.00 60.18           O  
ANISOU 1423  O   ASP A 109     6145   7794   8928   -857     89    196       O  
ATOM   1424  CB  ASP A 109      11.713 -13.472   3.604  1.00 60.91           C  
ANISOU 1424  CB  ASP A 109     5739   8164   9239   -755   -161    197       C  
ATOM   1425  CG  ASP A 109      10.524 -13.679   4.529  1.00 65.31           C  
ANISOU 1425  CG  ASP A 109     5960   8988   9867   -898    -26    266       C  
ATOM   1426  OD1 ASP A 109      10.478 -13.036   5.599  1.00 64.76           O  
ANISOU 1426  OD1 ASP A 109     5807   9021   9780   -783    205    260       O  
ATOM   1427  OD2 ASP A 109       9.635 -14.487   4.185  1.00 69.47           O  
ANISOU 1427  OD2 ASP A 109     6313   9620  10463  -1133   -147    327       O  
ATOM   1428  N   TRP A 110      13.602 -12.310   6.456  1.00 61.01           N  
ANISOU 1428  N   TRP A 110     6061   8079   9041   -503    372    128       N  
ATOM   1429  CA  TRP A 110      14.307 -12.760   7.648  1.00 65.69           C  
ANISOU 1429  CA  TRP A 110     6824   8604   9533   -591    513    143       C  
ATOM   1430  C   TRP A 110      13.458 -13.774   8.405  1.00 62.60           C  
ANISOU 1430  C   TRP A 110     6295   8334   9156   -851    584    230       C  
ATOM   1431  O   TRP A 110      12.287 -13.521   8.707  1.00 63.87           O  
ANISOU 1431  O   TRP A 110     6159   8711   9397   -871    675    267       O  
ATOM   1432  CB  TRP A 110      14.642 -11.567   8.543  1.00 67.27           C  
ANISOU 1432  CB  TRP A 110     7045   8839   9677   -379    711     91       C  
ATOM   1433  CG  TRP A 110      15.617 -11.894   9.631  1.00 64.44           C  
ANISOU 1433  CG  TRP A 110     6917   8372   9197   -431    815     88       C  
ATOM   1434  CD1 TRP A 110      15.331 -12.156  10.938  1.00 64.49           C  
ANISOU 1434  CD1 TRP A 110     6900   8455   9147   -520    991    129       C  
ATOM   1435  CD2 TRP A 110      17.040 -11.998   9.501  1.00 63.95           C  
ANISOU 1435  CD2 TRP A 110     7142   8108   9049   -391    745     44       C  
ATOM   1436  NE1 TRP A 110      16.489 -12.415  11.632  1.00 70.32           N  
ANISOU 1436  NE1 TRP A 110     7906   9047   9764   -534   1018    110       N  
ATOM   1437  CE2 TRP A 110      17.552 -12.324  10.772  1.00 66.25           C  
ANISOU 1437  CE2 TRP A 110     7566   8371   9234   -456    867     60       C  
ATOM   1438  CE3 TRP A 110      17.930 -11.845   8.434  1.00 63.26           C  
ANISOU 1438  CE3 TRP A 110     7209   7866   8963   -303    596     -5       C  
ATOM   1439  CZ2 TRP A 110      18.914 -12.501  11.004  1.00 65.22           C  
ANISOU 1439  CZ2 TRP A 110     7692   8082   9006   -432    827     29       C  
ATOM   1440  CZ3 TRP A 110      19.280 -12.021   8.665  1.00 63.47           C  
ANISOU 1440  CZ3 TRP A 110     7478   7737   8899   -284    579    -32       C  
ATOM   1441  CH2 TRP A 110      19.760 -12.346   9.940  1.00 64.08           C  
ANISOU 1441  CH2 TRP A 110     7660   7810   8879   -346    685    -15       C  
ATOM   1442  N   LEU A 111      14.057 -14.925   8.716  1.00 67.47           N  
ANISOU 1442  N   LEU A 111     7135   8812   9691  -1044    550    265       N  
ATOM   1443  CA  LEU A 111      13.369 -16.012   9.395  1.00 75.41           C  
ANISOU 1443  CA  LEU A 111     8078   9888  10686  -1319    612    347       C  
ATOM   1444  C   LEU A 111      13.899 -16.282  10.795  1.00 75.87           C  
ANISOU 1444  C   LEU A 111     8305   9899  10622  -1357    798    362       C  
ATOM   1445  O   LEU A 111      13.247 -17.006  11.556  1.00 77.25           O  
ANISOU 1445  O   LEU A 111     8420  10151  10781  -1563    906    427       O  
ATOM   1446  CB  LEU A 111      13.483 -17.303   8.570  1.00 76.90           C  
ANISOU 1446  CB  LEU A 111     8422   9939  10857  -1546    410    388       C  
ATOM   1447  CG  LEU A 111      12.920 -17.260   7.149  1.00 71.96           C  
ANISOU 1447  CG  LEU A 111     7670   9338  10336  -1558    195    383       C  
ATOM   1448  CD1 LEU A 111      13.301 -18.527   6.397  1.00 74.28           C  
ANISOU 1448  CD1 LEU A 111     8223   9434  10568  -1759      3    416       C  
ATOM   1449  CD2 LEU A 111      11.412 -17.077   7.167  1.00 63.74           C  
ANISOU 1449  CD2 LEU A 111     6227   8565   9424  -1656    224    425       C  
ATOM   1450  N   PHE A 112      15.054 -15.727  11.152  1.00 76.09           N  
ANISOU 1450  N   PHE A 112     8548   9803  10560  -1173    835    303       N  
ATOM   1451  CA  PHE A 112      15.704 -16.048  12.415  1.00 77.50           C  
ANISOU 1451  CA  PHE A 112     8931   9910  10604  -1204    969    313       C  
ATOM   1452  C   PHE A 112      15.131 -15.281  13.600  1.00 72.27           C  
ANISOU 1452  C   PHE A 112     8135   9397   9928  -1131   1207    315       C  
ATOM   1453  O   PHE A 112      15.462 -15.612  14.744  1.00 76.78           O  
ANISOU 1453  O   PHE A 112     8866   9924  10384  -1183   1333    334       O  
ATOM   1454  CB  PHE A 112      17.205 -15.776  12.294  1.00 70.20           C  
ANISOU 1454  CB  PHE A 112     8277   8805   9590  -1046    891    252       C  
ATOM   1455  CG  PHE A 112      17.853 -16.486  11.139  1.00 71.05           C  
ANISOU 1455  CG  PHE A 112     8541   8755   9701  -1083    680    252       C  
ATOM   1456  CD1 PHE A 112      17.920 -15.888   9.891  1.00 69.69           C  
ANISOU 1456  CD1 PHE A 112     8302   8561   9616   -959    552    208       C  
ATOM   1457  CD2 PHE A 112      18.383 -17.755  11.297  1.00 82.16           C  
ANISOU 1457  CD2 PHE A 112    10185  10024  11009  -1229    618    301       C  
ATOM   1458  CE1 PHE A 112      18.510 -16.540   8.824  1.00 68.35           C  
ANISOU 1458  CE1 PHE A 112     8299   8233   9438   -984    373    212       C  
ATOM   1459  CE2 PHE A 112      18.975 -18.413  10.234  1.00 84.15           C  
ANISOU 1459  CE2 PHE A 112    10604  10120  11250  -1244    439    307       C  
ATOM   1460  CZ  PHE A 112      19.038 -17.804   8.995  1.00 73.71           C  
ANISOU 1460  CZ  PHE A 112     9211   8776  10018  -1124    319    263       C  
ATOM   1461  N   GLY A 113      14.288 -14.279  13.363  1.00 72.71           N  
ANISOU 1461  N   GLY A 113     7922   9619  10086   -999   1275    298       N  
ATOM   1462  CA  GLY A 113      13.688 -13.520  14.434  1.00 72.86           C  
ANISOU 1462  CA  GLY A 113     7819   9778  10086   -906   1516    306       C  
ATOM   1463  C   GLY A 113      14.164 -12.082  14.449  1.00 69.99           C  
ANISOU 1463  C   GLY A 113     7498   9399   9695   -618   1566    225       C  
ATOM   1464  O   GLY A 113      15.185 -11.735  13.849  1.00 68.36           O  
ANISOU 1464  O   GLY A 113     7464   9049   9458   -511   1432    160       O  
ATOM   1465  N   PRO A 114      13.428 -11.212  15.144  1.00 73.06           N  
ANISOU 1465  N   PRO A 114     7742   9933  10086   -488   1774    230       N  
ATOM   1466  CA  PRO A 114      13.812  -9.792  15.171  1.00 77.68           C  
ANISOU 1466  CA  PRO A 114     8396  10493  10626   -213   1834    154       C  
ATOM   1467  C   PRO A 114      15.026  -9.506  16.035  1.00 67.50           C  
ANISOU 1467  C   PRO A 114     7434   9037   9174   -163   1880    102       C  
ATOM   1468  O   PRO A 114      15.708  -8.500  15.801  1.00 57.25           O  
ANISOU 1468  O   PRO A 114     6264   7658   7831     16   1853     25       O  
ATOM   1469  CB  PRO A 114      12.559  -9.105  15.729  1.00 82.87           C  
ANISOU 1469  CB  PRO A 114     8806  11358  11320   -100   2060    192       C  
ATOM   1470  CG  PRO A 114      11.938 -10.143  16.602  1.00 79.30           C  
ANISOU 1470  CG  PRO A 114     8278  10988  10865   -327   2187    280       C  
ATOM   1471  CD  PRO A 114      12.223 -11.476  15.952  1.00 79.93           C  
ANISOU 1471  CD  PRO A 114     8395  10987  10988   -583   1978    309       C  
ATOM   1472  N   VAL A 115      15.315 -10.352  17.024  1.00 71.08           N  
ANISOU 1472  N   VAL A 115     8036   9436   9533   -321   1944    142       N  
ATOM   1473  CA  VAL A 115      16.468 -10.126  17.888  1.00 61.13           C  
ANISOU 1473  CA  VAL A 115     7085   8028   8114   -279   1966     96       C  
ATOM   1474  C   VAL A 115      17.763 -10.473  17.165  1.00 55.34           C  
ANISOU 1474  C   VAL A 115     6528   7133   7365   -302   1737     50       C  
ATOM   1475  O   VAL A 115      18.780  -9.791  17.332  1.00 57.90           O  
ANISOU 1475  O   VAL A 115     7036   7357   7607   -195   1702    -18       O  
ATOM   1476  CB  VAL A 115      16.311 -10.926  19.194  1.00 67.62           C  
ANISOU 1476  CB  VAL A 115     8021   8843   8828   -426   2109    157       C  
ATOM   1477  CG1 VAL A 115      17.533 -10.749  20.082  1.00 72.10           C  
ANISOU 1477  CG1 VAL A 115     8915   9258   9223   -386   2100    111       C  
ATOM   1478  CG2 VAL A 115      15.049 -10.496  19.930  1.00 73.14           C  
ANISOU 1478  CG2 VAL A 115     8545   9704   9541   -384   2367    205       C  
ATOM   1479  N   MET A 116      17.753 -11.529  16.349  1.00 59.38           N  
ANISOU 1479  N   MET A 116     6991   7619   7952   -445   1582     88       N  
ATOM   1480  CA  MET A 116      18.958 -11.912  15.623  1.00 58.56           C  
ANISOU 1480  CA  MET A 116     7053   7363   7833   -450   1380     54       C  
ATOM   1481  C   MET A 116      19.291 -10.951  14.487  1.00 57.33           C  
ANISOU 1481  C   MET A 116     6849   7182   7752   -288   1281    -16       C  
ATOM   1482  O   MET A 116      20.439 -10.928  14.032  1.00 55.76           O  
ANISOU 1482  O   MET A 116     6802   6858   7526   -247   1156    -60       O  
ATOM   1483  CB  MET A 116      18.815 -13.334  15.075  1.00 55.89           C  
ANISOU 1483  CB  MET A 116     6717   6984   7533   -641   1255    119       C  
ATOM   1484  CG  MET A 116      19.135 -14.418  16.099  1.00 60.70           C  
ANISOU 1484  CG  MET A 116     7517   7529   8019   -790   1296    172       C  
ATOM   1485  SD  MET A 116      19.220 -16.089  15.417  1.00 63.73           S  
ANISOU 1485  SD  MET A 116     8000   7810   8404   -998   1135    241       S  
ATOM   1486  CE  MET A 116      20.369 -15.876  14.058  1.00 64.19           C  
ANISOU 1486  CE  MET A 116     8145   7741   8504   -864    917    185       C  
ATOM   1487  N   CYS A 117      18.325 -10.159  14.018  1.00 63.36           N  
ANISOU 1487  N   CYS A 117     7408   8061   8606   -187   1338    -27       N  
ATOM   1488  CA  CYS A 117      18.629  -9.154  13.004  1.00 61.89           C  
ANISOU 1488  CA  CYS A 117     7213   7836   8468    -15   1261    -98       C  
ATOM   1489  C   CYS A 117      19.421  -7.999  13.605  1.00 57.80           C  
ANISOU 1489  C   CYS A 117     6863   7254   7843    130   1347   -173       C  
ATOM   1490  O   CYS A 117      20.447  -7.582  13.054  1.00 53.31           O  
ANISOU 1490  O   CYS A 117     6431   6568   7256    193   1251   -236       O  
ATOM   1491  CB  CYS A 117      17.337  -8.650  12.358  1.00 61.80           C  
ANISOU 1491  CB  CYS A 117     6943   7970   8569     69   1291    -84       C  
ATOM   1492  SG  CYS A 117      17.509  -7.118  11.402  1.00 58.09           S  
ANISOU 1492  SG  CYS A 117     6489   7463   8120    332   1265   -176       S  
ATOM   1493  N   LYS A 118      18.964  -7.475  14.745  1.00 55.47           N  
ANISOU 1493  N   LYS A 118     6574   7031   7473    176   1534   -167       N  
ATOM   1494  CA  LYS A 118      19.691  -6.394  15.401  1.00 57.86           C  
ANISOU 1494  CA  LYS A 118     7071   7261   7651    293   1615   -237       C  
ATOM   1495  C   LYS A 118      21.025  -6.883  15.954  1.00 56.30           C  
ANISOU 1495  C   LYS A 118     7096   6940   7354    194   1530   -255       C  
ATOM   1496  O   LYS A 118      22.028  -6.161  15.902  1.00 54.34           O  
ANISOU 1496  O   LYS A 118     7005   6599   7045    255   1485   -327       O  
ATOM   1497  CB  LYS A 118      18.837  -5.796  16.520  1.00 53.23           C  
ANISOU 1497  CB  LYS A 118     6465   6769   6991    368   1843   -217       C  
ATOM   1498  CG  LYS A 118      19.423  -4.542  17.152  1.00 55.97           C  
ANISOU 1498  CG  LYS A 118     7031   7036   7197    501   1936   -291       C  
ATOM   1499  CD  LYS A 118      18.532  -3.997  18.261  1.00 55.15           C  
ANISOU 1499  CD  LYS A 118     6933   7015   7007    589   2178   -263       C  
ATOM   1500  CE  LYS A 118      17.272  -3.340  17.719  1.00 69.30           C  
ANISOU 1500  CE  LYS A 118     8502   8942   8886    758   2287   -244       C  
ATOM   1501  NZ  LYS A 118      17.568  -2.102  16.944  1.00 72.16           N  
ANISOU 1501  NZ  LYS A 118     8949   9237   9231    944   2254   -326       N  
ATOM   1502  N   VAL A 119      21.058  -8.108  16.476  1.00 55.14           N  
ANISOU 1502  N   VAL A 119     6969   6795   7187     40   1505   -191       N  
ATOM   1503  CA  VAL A 119      22.264  -8.663  17.078  1.00 51.39           C  
ANISOU 1503  CA  VAL A 119     6699   6218   6608    -38   1422   -198       C  
ATOM   1504  C   VAL A 119      23.291  -8.967  15.996  1.00 52.15           C  
ANISOU 1504  C   VAL A 119     6831   6224   6762    -41   1228   -225       C  
ATOM   1505  O   VAL A 119      24.302  -8.268  15.872  1.00 50.49           O  
ANISOU 1505  O   VAL A 119     6726   5946   6512     24   1173   -291       O  
ATOM   1506  CB  VAL A 119      21.937  -9.923  17.902  1.00 51.91           C  
ANISOU 1506  CB  VAL A 119     6799   6301   6624   -187   1458   -116       C  
ATOM   1507  CG1 VAL A 119      23.206 -10.698  18.224  1.00 52.18           C  
ANISOU 1507  CG1 VAL A 119     7030   6228   6569   -252   1325   -115       C  
ATOM   1508  CG2 VAL A 119      21.207  -9.537  19.179  1.00 52.85           C  
ANISOU 1508  CG2 VAL A 119     6947   6483   6650   -175   1669    -97       C  
ATOM   1509  N   PHE A 120      23.040 -10.013  15.206  1.00 53.34           N  
ANISOU 1509  N   PHE A 120     6901   6368   6998   -124   1128   -171       N  
ATOM   1510  CA  PHE A 120      24.001 -10.437  14.195  1.00 47.83           C  
ANISOU 1510  CA  PHE A 120     6258   5573   6342   -122    958   -184       C  
ATOM   1511  C   PHE A 120      24.195  -9.406  13.092  1.00 45.29           C  
ANISOU 1511  C   PHE A 120     5887   5224   6098      2    919   -252       C  
ATOM   1512  O   PHE A 120      25.120  -9.555  12.287  1.00 45.55           O  
ANISOU 1512  O   PHE A 120     5983   5168   6157     25    801   -272       O  
ATOM   1513  CB  PHE A 120      23.568 -11.771  13.591  1.00 50.12           C  
ANISOU 1513  CB  PHE A 120     6507   5848   6689   -239    871   -108       C  
ATOM   1514  CG  PHE A 120      23.744 -12.936  14.521  1.00 54.61           C  
ANISOU 1514  CG  PHE A 120     7197   6392   7159   -363    876    -45       C  
ATOM   1515  CD1 PHE A 120      22.739 -13.295  15.403  1.00 61.24           C  
ANISOU 1515  CD1 PHE A 120     7991   7310   7968   -461   1004      6       C  
ATOM   1516  CD2 PHE A 120      24.921 -13.662  14.525  1.00 55.10           C  
ANISOU 1516  CD2 PHE A 120     7428   6354   7155   -370    763    -33       C  
ATOM   1517  CE1 PHE A 120      22.902 -14.365  16.264  1.00 55.71           C  
ANISOU 1517  CE1 PHE A 120     7437   6570   7162   -576   1017     63       C  
ATOM   1518  CE2 PHE A 120      25.088 -14.730  15.382  1.00 56.01           C  
ANISOU 1518  CE2 PHE A 120     7683   6436   7162   -464    765     25       C  
ATOM   1519  CZ  PHE A 120      24.076 -15.082  16.253  1.00 55.49           C  
ANISOU 1519  CZ  PHE A 120     7597   6430   7055   -572    892     71       C  
ATOM   1520  N   GLY A 121      23.353  -8.380  13.028  1.00 45.92           N  
ANISOU 1520  N   GLY A 121     5869   5372   6207     95   1023   -284       N  
ATOM   1521  CA  GLY A 121      23.568  -7.294  12.095  1.00 49.58           C  
ANISOU 1521  CA  GLY A 121     6331   5793   6713    226   1002   -355       C  
ATOM   1522  C   GLY A 121      24.660  -6.373  12.593  1.00 47.43           C  
ANISOU 1522  C   GLY A 121     6220   5456   6346    276   1030   -429       C  
ATOM   1523  O   GLY A 121      25.534  -5.952  11.829  1.00 44.00           O  
ANISOU 1523  O   GLY A 121     5852   4936   5930    318    957   -481       O  
ATOM   1524  N   SER A 122      24.616  -6.055  13.888  1.00 52.47           N  
ANISOU 1524  N   SER A 122     6929   6130   6875    262   1139   -433       N  
ATOM   1525  CA  SER A 122      25.667  -5.247  14.492  1.00 49.48           C  
ANISOU 1525  CA  SER A 122     6720   5690   6389    276   1150   -501       C  
ATOM   1526  C   SER A 122      26.933  -6.065  14.706  1.00 44.36           C  
ANISOU 1526  C   SER A 122     6153   4993   5710    180   1019   -488       C  
ATOM   1527  O   SER A 122      28.044  -5.547  14.552  1.00 43.73           O  
ANISOU 1527  O   SER A 122     6157   4855   5602    184    958   -545       O  
ATOM   1528  CB  SER A 122      25.182  -4.670  15.823  1.00 54.84           C  
ANISOU 1528  CB  SER A 122     7480   6412   6946    295   1303   -506       C  
ATOM   1529  OG  SER A 122      23.929  -4.027  15.676  1.00 57.90           O  
ANISOU 1529  OG  SER A 122     7772   6866   7362    404   1439   -501       O  
ATOM   1530  N   PHE A 123      26.779  -7.343  15.063  1.00 44.63           N  
ANISOU 1530  N   PHE A 123     6162   5051   5743     95    977   -412       N  
ATOM   1531  CA  PHE A 123      27.935  -8.214  15.244  1.00 44.12           C  
ANISOU 1531  CA  PHE A 123     6177   4943   5642     33    850   -390       C  
ATOM   1532  C   PHE A 123      28.790  -8.262  13.986  1.00 49.56           C  
ANISOU 1532  C   PHE A 123     6840   5570   6419     68    733   -411       C  
ATOM   1533  O   PHE A 123      30.019  -8.364  14.074  1.00 50.63           O  
ANISOU 1533  O   PHE A 123     7038   5677   6522     59    647   -427       O  
ATOM   1534  CB  PHE A 123      27.464  -9.614  15.635  1.00 44.70           C  
ANISOU 1534  CB  PHE A 123     6247   5035   5701    -52    835   -300       C  
ATOM   1535  CG  PHE A 123      28.564 -10.524  16.095  1.00 44.91           C  
ANISOU 1535  CG  PHE A 123     6389   5023   5653    -93    724   -270       C  
ATOM   1536  CD1 PHE A 123      29.208 -10.296  17.299  1.00 45.97           C  
ANISOU 1536  CD1 PHE A 123     6645   5164   5656   -105    726   -291       C  
ATOM   1537  CD2 PHE A 123      28.936 -11.623  15.340  1.00 46.37           C  
ANISOU 1537  CD2 PHE A 123     6576   5160   5883   -109    613   -218       C  
ATOM   1538  CE1 PHE A 123      30.216 -11.136  17.733  1.00 46.13           C  
ANISOU 1538  CE1 PHE A 123     6765   5160   5601   -123    611   -260       C  
ATOM   1539  CE2 PHE A 123      29.942 -12.468  15.772  1.00 44.13           C  
ANISOU 1539  CE2 PHE A 123     6404   4844   5519   -116    516   -185       C  
ATOM   1540  CZ  PHE A 123      30.581 -12.224  16.970  1.00 44.77           C  
ANISOU 1540  CZ  PHE A 123     6583   4949   5478   -118    511   -206       C  
ATOM   1541  N   LEU A 124      28.164  -8.194  12.810  1.00 46.27           N  
ANISOU 1541  N   LEU A 124     6333   5137   6112    112    729   -409       N  
ATOM   1542  CA  LEU A 124      28.924  -8.108  11.568  1.00 47.10           C  
ANISOU 1542  CA  LEU A 124     6437   5166   6291    159    642   -434       C  
ATOM   1543  C   LEU A 124      29.704  -6.801  11.504  1.00 43.90           C  
ANISOU 1543  C   LEU A 124     6086   4732   5861    207    672   -523       C  
ATOM   1544  O   LEU A 124      30.931  -6.799  11.357  1.00 47.03           O  
ANISOU 1544  O   LEU A 124     6524   5095   6251    196    606   -543       O  
ATOM   1545  CB  LEU A 124      27.980  -8.232  10.369  1.00 43.43           C  
ANISOU 1545  CB  LEU A 124     5888   4682   5931    198    630   -416       C  
ATOM   1546  CG  LEU A 124      28.597  -8.011   8.986  1.00 44.54           C  
ANISOU 1546  CG  LEU A 124     6053   4727   6144    265    562   -446       C  
ATOM   1547  CD1 LEU A 124      29.632  -9.079   8.680  1.00 43.07           C  
ANISOU 1547  CD1 LEU A 124     5926   4480   5958    236    460   -400       C  
ATOM   1548  CD2 LEU A 124      27.518  -7.981   7.913  1.00 50.79           C  
ANISOU 1548  CD2 LEU A 124     6776   5503   7020    311    547   -437       C  
ATOM   1549  N   THR A 125      29.001  -5.672  11.619  1.00 45.91           N  
ANISOU 1549  N   THR A 125     6344   5003   6098    260    778   -575       N  
ATOM   1550  CA  THR A 125      29.664  -4.374  11.550  1.00 46.05           C  
ANISOU 1550  CA  THR A 125     6450   4974   6074    293    818   -664       C  
ATOM   1551  C   THR A 125      30.752  -4.257  12.609  1.00 49.40           C  
ANISOU 1551  C   THR A 125     6961   5412   6399    211    788   -686       C  
ATOM   1552  O   THR A 125      31.798  -3.642  12.372  1.00 47.34           O  
ANISOU 1552  O   THR A 125     6751   5110   6126    189    757   -742       O  
ATOM   1553  CB  THR A 125      28.634  -3.255  11.715  1.00 49.71           C  
ANISOU 1553  CB  THR A 125     6937   5450   6500    377    949   -706       C  
ATOM   1554  OG1 THR A 125      27.514  -3.499  10.855  1.00 50.83           O  
ANISOU 1554  OG1 THR A 125     6967   5612   6735    452    958   -672       O  
ATOM   1555  CG2 THR A 125      29.247  -1.910  11.368  1.00 51.83           C  
ANISOU 1555  CG2 THR A 125     7328   5639   6724    416    991   -799       C  
ATOM   1556  N   LEU A 126      30.523  -4.846  13.784  1.00 50.01           N  
ANISOU 1556  N   LEU A 126     7056   5547   6399    159    795   -642       N  
ATOM   1557  CA  LEU A 126      31.505  -4.785  14.861  1.00 51.34           C  
ANISOU 1557  CA  LEU A 126     7317   5731   6459     85    747   -660       C  
ATOM   1558  C   LEU A 126      32.820  -5.433  14.441  1.00 47.24           C  
ANISOU 1558  C   LEU A 126     6760   5207   5983     51    607   -645       C  
ATOM   1559  O   LEU A 126      33.874  -4.787  14.433  1.00 46.14           O  
ANISOU 1559  O   LEU A 126     6649   5060   5823     15    564   -700       O  
ATOM   1560  CB  LEU A 126      30.938  -5.470  16.106  1.00 46.65           C  
ANISOU 1560  CB  LEU A 126     6765   5187   5775     48    778   -605       C  
ATOM   1561  CG  LEU A 126      31.874  -5.657  17.298  1.00 44.62           C  
ANISOU 1561  CG  LEU A 126     6615   4946   5391    -22    704   -608       C  
ATOM   1562  CD1 LEU A 126      32.414  -4.323  17.775  1.00 58.85           C  
ANISOU 1562  CD1 LEU A 126     8535   6724   7100    -49    727   -696       C  
ATOM   1563  CD2 LEU A 126      31.153  -6.383  18.422  1.00 45.56           C  
ANISOU 1563  CD2 LEU A 126     6797   5094   5419    -46    757   -548       C  
ATOM   1564  N   ASN A 127      32.773  -6.718  14.081  1.00 44.50           N  
ANISOU 1564  N   ASN A 127     6350   4867   5691     62    540   -568       N  
ATOM   1565  CA  ASN A 127      33.990  -7.437  13.725  1.00 43.64           C  
ANISOU 1565  CA  ASN A 127     6211   4758   5612     61    419   -540       C  
ATOM   1566  C   ASN A 127      34.603  -6.945  12.420  1.00 48.10           C  
ANISOU 1566  C   ASN A 127     6724   5273   6279    101    409   -577       C  
ATOM   1567  O   ASN A 127      35.809  -7.120  12.217  1.00 47.91           O  
ANISOU 1567  O   ASN A 127     6667   5263   6272     98    333   -576       O  
ATOM   1568  CB  ASN A 127      33.705  -8.938  13.629  1.00 44.20           C  
ANISOU 1568  CB  ASN A 127     6273   4824   5696     75    365   -444       C  
ATOM   1569  CG  ASN A 127      33.396  -9.561  14.977  1.00 42.58           C  
ANISOU 1569  CG  ASN A 127     6145   4661   5374     28    364   -403       C  
ATOM   1570  OD1 ASN A 127      34.292 -10.031  15.677  1.00 44.27           O  
ANISOU 1570  OD1 ASN A 127     6406   4903   5512     19    277   -383       O  
ATOM   1571  ND2 ASN A 127      32.123  -9.565  15.350  1.00 47.81           N  
ANISOU 1571  ND2 ASN A 127     6818   5329   6018      3    464   -386       N  
ATOM   1572  N   MET A 128      33.812  -6.340  11.531  1.00 52.05           N  
ANISOU 1572  N   MET A 128     7215   5718   6844    146    486   -607       N  
ATOM   1573  CA  MET A 128      34.371  -5.859  10.272  1.00 51.14           C  
ANISOU 1573  CA  MET A 128     7083   5536   6813    188    488   -644       C  
ATOM   1574  C   MET A 128      35.143  -4.559  10.467  1.00 51.54           C  
ANISOU 1574  C   MET A 128     7176   5581   6825    140    525   -733       C  
ATOM   1575  O   MET A 128      36.221  -4.385   9.888  1.00 51.37           O  
ANISOU 1575  O   MET A 128     7128   5542   6847    127    497   -753       O  
ATOM   1576  CB  MET A 128      33.262  -5.679   9.235  1.00 53.80           C  
ANISOU 1576  CB  MET A 128     7416   5807   7219    261    542   -646       C  
ATOM   1577  CG  MET A 128      33.767  -5.271   7.859  1.00 55.25           C  
ANISOU 1577  CG  MET A 128     7615   5897   7480    316    548   -679       C  
ATOM   1578  SD  MET A 128      35.066  -6.358   7.233  1.00 71.00           S  
ANISOU 1578  SD  MET A 128     9578   7870   9530    328    459   -618       S  
ATOM   1579  CE  MET A 128      34.123  -7.755   6.628  1.00 64.29           C  
ANISOU 1579  CE  MET A 128     8732   6975   8719    377    401   -524       C  
ATOM   1580  N   PHE A 129      34.616  -3.636  11.274  1.00 54.64           N  
ANISOU 1580  N   PHE A 129     7645   5985   7130    110    596   -786       N  
ATOM   1581  CA  PHE A 129      35.402  -2.462  11.640  1.00 53.90           C  
ANISOU 1581  CA  PHE A 129     7629   5882   6971     35    618   -869       C  
ATOM   1582  C   PHE A 129      36.663  -2.872  12.388  1.00 52.11           C  
ANISOU 1582  C   PHE A 129     7359   5732   6707    -59    506   -855       C  
ATOM   1583  O   PHE A 129      37.755  -2.359  12.114  1.00 47.59           O  
ANISOU 1583  O   PHE A 129     6767   5163   6152   -126    477   -898       O  
ATOM   1584  CB  PHE A 129      34.566  -1.501  12.486  1.00 50.81           C  
ANISOU 1584  CB  PHE A 129     7364   5478   6465     31    716   -917       C  
ATOM   1585  CG  PHE A 129      33.739  -0.545  11.678  1.00 50.13           C  
ANISOU 1585  CG  PHE A 129     7346   5309   6393    120    831   -966       C  
ATOM   1586  CD1 PHE A 129      34.345   0.414  10.883  1.00 48.68           C  
ANISOU 1586  CD1 PHE A 129     7234   5041   6220    105    865  -1037       C  
ATOM   1587  CD2 PHE A 129      32.357  -0.595  11.721  1.00 54.35           C  
ANISOU 1587  CD2 PHE A 129     7873   5852   6926    221    908   -939       C  
ATOM   1588  CE1 PHE A 129      33.589   1.297  10.139  1.00 50.35           C  
ANISOU 1588  CE1 PHE A 129     7538   5164   6427    205    968  -1083       C  
ATOM   1589  CE2 PHE A 129      31.594   0.288  10.981  1.00 52.63           C  
ANISOU 1589  CE2 PHE A 129     7714   5568   6715    328   1003   -981       C  
ATOM   1590  CZ  PHE A 129      32.211   1.235  10.189  1.00 54.61           C  
ANISOU 1590  CZ  PHE A 129     8065   5720   6963    328   1031  -1054       C  
ATOM   1591  N   ALA A 130      36.530  -3.796  13.342  1.00 48.84           N  
ANISOU 1591  N   ALA A 130     6931   5386   6240    -66    442   -795       N  
ATOM   1592  CA  ALA A 130      37.702  -4.316  14.036  1.00 54.12           C  
ANISOU 1592  CA  ALA A 130     7555   6137   6872   -127    315   -773       C  
ATOM   1593  C   ALA A 130      38.701  -4.903  13.047  1.00 50.20           C  
ANISOU 1593  C   ALA A 130     6929   5657   6487    -91    250   -738       C  
ATOM   1594  O   ALA A 130      39.910  -4.668  13.159  1.00 43.54           O  
ANISOU 1594  O   ALA A 130     6020   4875   5648   -152    179   -759       O  
ATOM   1595  CB  ALA A 130      37.280  -5.366  15.063  1.00 49.61           C  
ANISOU 1595  CB  ALA A 130     7013   5612   6223   -110    265   -703       C  
ATOM   1596  N   SER A 131      38.214  -5.665  12.065  1.00 52.20           N  
ANISOU 1596  N   SER A 131     7145   5858   6829      8    274   -683       N  
ATOM   1597  CA  SER A 131      39.104  -6.232  11.058  1.00 50.60           C  
ANISOU 1597  CA  SER A 131     6849   5651   6725     65    235   -645       C  
ATOM   1598  C   SER A 131      39.827  -5.137  10.284  1.00 45.71           C  
ANISOU 1598  C   SER A 131     6201   5002   6163     22    289   -717       C  
ATOM   1599  O   SER A 131      41.025  -5.254   9.999  1.00 51.33           O  
ANISOU 1599  O   SER A 131     6813   5766   6922     10    246   -707       O  
ATOM   1600  CB  SER A 131      38.307  -7.123  10.104  1.00 50.08           C  
ANISOU 1600  CB  SER A 131     6800   5503   6725    168    260   -582       C  
ATOM   1601  OG  SER A 131      39.130  -7.662   9.086  1.00 49.00           O  
ANISOU 1601  OG  SER A 131     6608   5340   6669    240    238   -542       O  
ATOM   1602  N   ILE A 132      39.117  -4.063   9.935  1.00 50.09           N  
ANISOU 1602  N   ILE A 132     6847   5474   6712      2    392   -788       N  
ATOM   1603  CA  ILE A 132      39.740  -2.976   9.186  1.00 45.48           C  
ANISOU 1603  CA  ILE A 132     6278   4838   6165    -48    460   -861       C  
ATOM   1604  C   ILE A 132      40.653  -2.159  10.091  1.00 45.09           C  
ANISOU 1604  C   ILE A 132     6223   4863   6044   -199    423   -921       C  
ATOM   1605  O   ILE A 132      41.716  -1.692   9.664  1.00 43.32           O  
ANISOU 1605  O   ILE A 132     5937   4657   5864   -274    428   -953       O  
ATOM   1606  CB  ILE A 132      38.660  -2.097   8.529  1.00 51.38           C  
ANISOU 1606  CB  ILE A 132     7155   5461   6908     -1    577   -916       C  
ATOM   1607  CG1 ILE A 132      37.861  -2.913   7.508  1.00 56.76           C  
ANISOU 1607  CG1 ILE A 132     7827   6071   7668    134    588   -857       C  
ATOM   1608  CG2 ILE A 132      39.295  -0.881   7.863  1.00 46.66           C  
ANISOU 1608  CG2 ILE A 132     6619   4790   6319    -66    659  -1000       C  
ATOM   1609  CD1 ILE A 132      36.590  -2.239   7.039  1.00 60.42           C  
ANISOU 1609  CD1 ILE A 132     8394   6444   8118    204    673   -896       C  
ATOM   1610  N   PHE A 133      40.254  -1.968  11.351  1.00 52.19           N  
ANISOU 1610  N   PHE A 133     7195   5805   6828   -257    389   -937       N  
ATOM   1611  CA  PHE A 133      41.085  -1.204  12.275  1.00 47.51           C  
ANISOU 1611  CA  PHE A 133     6627   5275   6148   -414    334   -995       C  
ATOM   1612  C   PHE A 133      42.364  -1.950  12.633  1.00 45.65           C  
ANISOU 1612  C   PHE A 133     6219   5181   5944   -455    191   -948       C  
ATOM   1613  O   PHE A 133      43.408  -1.320  12.831  1.00 49.90           O  
ANISOU 1613  O   PHE A 133     6705   5782   6474   -593    143   -994       O  
ATOM   1614  CB  PHE A 133      40.295  -0.871  13.541  1.00 46.77           C  
ANISOU 1614  CB  PHE A 133     6686   5177   5907   -447    336  -1018       C  
ATOM   1615  CG  PHE A 133      39.130   0.058  13.310  1.00 48.09           C  
ANISOU 1615  CG  PHE A 133     7023   5223   6025   -404    483  -1071       C  
ATOM   1616  CD1 PHE A 133      39.056   0.846  12.172  1.00 45.49           C  
ANISOU 1616  CD1 PHE A 133     6739   4794   5752   -383    586  -1121       C  
ATOM   1617  CD2 PHE A 133      38.107   0.142  14.240  1.00 57.19           C  
ANISOU 1617  CD2 PHE A 133     8300   6362   7068   -369    526  -1067       C  
ATOM   1618  CE1 PHE A 133      37.987   1.697  11.968  1.00 45.02           C  
ANISOU 1618  CE1 PHE A 133     6842   4629   5636   -316    715  -1167       C  
ATOM   1619  CE2 PHE A 133      37.035   0.990  14.040  1.00 48.35           C  
ANISOU 1619  CE2 PHE A 133     7322   5147   5901   -302    667  -1108       C  
ATOM   1620  CZ  PHE A 133      36.976   1.768  12.903  1.00 46.45           C  
ANISOU 1620  CZ  PHE A 133     7123   4813   5713   -268    754  -1158       C  
ATOM   1621  N   PHE A 134      42.311  -3.281  12.718  1.00 45.24           N  
ANISOU 1621  N   PHE A 134     6082   5183   5924   -339    119   -856       N  
ATOM   1622  CA  PHE A 134      43.522  -4.037  13.018  1.00 46.49           C  
ANISOU 1622  CA  PHE A 134     6077   5479   6107   -339    -16   -803       C  
ATOM   1623  C   PHE A 134      44.447  -4.130  11.811  1.00 48.33           C  
ANISOU 1623  C   PHE A 134     6155   5732   6478   -304     15   -785       C  
ATOM   1624  O   PHE A 134      45.671  -4.175  11.978  1.00 54.30           O  
ANISOU 1624  O   PHE A 134     6752   6616   7263   -357    -70   -775       O  
ATOM   1625  CB  PHE A 134      43.165  -5.434  13.532  1.00 46.03           C  
ANISOU 1625  CB  PHE A 134     6019   5455   6013   -214    -95   -709       C  
ATOM   1626  CG  PHE A 134      42.743  -5.451  14.976  1.00 46.74           C  
ANISOU 1626  CG  PHE A 134     6228   5575   5956   -267   -162   -718       C  
ATOM   1627  CD1 PHE A 134      43.607  -5.015  15.969  1.00 48.38           C  
ANISOU 1627  CD1 PHE A 134     6418   5885   6081   -384   -282   -754       C  
ATOM   1628  CD2 PHE A 134      41.489  -5.910  15.343  1.00 47.42           C  
ANISOU 1628  CD2 PHE A 134     6445   5589   5983   -208   -106   -688       C  
ATOM   1629  CE1 PHE A 134      43.225  -5.024  17.295  1.00 49.15           C  
ANISOU 1629  CE1 PHE A 134     6657   5991   6027   -427   -342   -762       C  
ATOM   1630  CE2 PHE A 134      41.102  -5.924  16.672  1.00 46.75           C  
ANISOU 1630  CE2 PHE A 134     6485   5521   5756   -253   -147   -693       C  
ATOM   1631  CZ  PHE A 134      41.973  -5.481  17.648  1.00 48.51           C  
ANISOU 1631  CZ  PHE A 134     6720   5826   5885   -356   -264   -731       C  
ATOM   1632  N   ILE A 135      43.891  -4.169  10.599  1.00 44.97           N  
ANISOU 1632  N   ILE A 135     5770   5183   6134   -212    135   -777       N  
ATOM   1633  CA  ILE A 135      44.723  -4.062   9.404  1.00 48.76           C  
ANISOU 1633  CA  ILE A 135     6142   5651   6732   -188    198   -771       C  
ATOM   1634  C   ILE A 135      45.533  -2.775   9.443  1.00 50.74           C  
ANISOU 1634  C   ILE A 135     6358   5936   6984   -372    229   -859       C  
ATOM   1635  O   ILE A 135      46.691  -2.734   9.008  1.00 47.36           O  
ANISOU 1635  O   ILE A 135     5767   5592   6637   -410    227   -848       O  
ATOM   1636  CB  ILE A 135      43.851  -4.144   8.136  1.00 51.34           C  
ANISOU 1636  CB  ILE A 135     6576   5812   7120    -73    322   -762       C  
ATOM   1637  CG1 ILE A 135      43.411  -5.588   7.896  1.00 49.54           C  
ANISOU 1637  CG1 ILE A 135     6349   5565   6909     94    278   -660       C  
ATOM   1638  CG2 ILE A 135      44.601  -3.586   6.930  1.00 45.68           C  
ANISOU 1638  CG2 ILE A 135     5814   5043   6498    -86    427   -788       C  
ATOM   1639  CD1 ILE A 135      42.281  -5.721   6.908  1.00 55.91           C  
ANISOU 1639  CD1 ILE A 135     7287   6211   7746    188    363   -652       C  
ATOM   1640  N   THR A 136      44.937  -1.702   9.966  1.00 47.71           N  
ANISOU 1640  N   THR A 136     6133   5486   6506   -491    266   -945       N  
ATOM   1641  CA  THR A 136      45.657  -0.440  10.081  1.00 47.69           C  
ANISOU 1641  CA  THR A 136     6145   5497   6479   -693    292  -1034       C  
ATOM   1642  C   THR A 136      46.754  -0.530  11.135  1.00 50.76           C  
ANISOU 1642  C   THR A 136     6384   6071   6833   -827    132  -1029       C  
ATOM   1643  O   THR A 136      47.871  -0.043  10.919  1.00 54.84           O  
ANISOU 1643  O   THR A 136     6766   6671   7402   -966    121  -1056       O  
ATOM   1644  CB  THR A 136      44.682   0.687  10.415  1.00 47.39           C  
ANISOU 1644  CB  THR A 136     6359   5324   6322   -763    374  -1122       C  
ATOM   1645  OG1 THR A 136      43.656   0.748   9.416  1.00 45.80           O  
ANISOU 1645  OG1 THR A 136     6277   4967   6156   -620    506  -1123       O  
ATOM   1646  CG2 THR A 136      45.410   2.018  10.470  1.00 48.88           C  
ANISOU 1646  CG2 THR A 136     6611   5496   6466   -983    411  -1218       C  
ATOM   1647  N   CYS A 137      46.456  -1.146  12.282  1.00 52.37           N  
ANISOU 1647  N   CYS A 137     6608   6344   6945   -793      5   -995       N  
ATOM   1648  CA  CYS A 137      47.485  -1.348  13.295  1.00 54.32           C  
ANISOU 1648  CA  CYS A 137     6717   6772   7152   -895   -174   -982       C  
ATOM   1649  C   CYS A 137      48.660  -2.141  12.741  1.00 52.55           C  
ANISOU 1649  C   CYS A 137     6210   6698   7059   -825   -231   -908       C  
ATOM   1650  O   CYS A 137      49.809  -1.901  13.126  1.00 56.24           O  
ANISOU 1650  O   CYS A 137     6501   7326   7541   -955   -340   -918       O  
ATOM   1651  CB  CYS A 137      46.894  -2.065  14.508  1.00 51.63           C  
ANISOU 1651  CB  CYS A 137     6469   6459   6689   -824   -289   -943       C  
ATOM   1652  SG  CYS A 137      45.725  -1.074  15.456  1.00 55.91           S  
ANISOU 1652  SG  CYS A 137     7327   6864   7052   -922   -235  -1027       S  
ATOM   1653  N   MET A 138      48.393  -3.087  11.840  1.00 51.22           N  
ANISOU 1653  N   MET A 138     5996   6483   6981   -618   -161   -830       N  
ATOM   1654  CA  MET A 138      49.474  -3.861  11.241  1.00 52.07           C  
ANISOU 1654  CA  MET A 138     5859   6720   7207   -516   -188   -752       C  
ATOM   1655  C   MET A 138      50.335  -2.995  10.330  1.00 56.90           C  
ANISOU 1655  C   MET A 138     6344   7349   7927   -639    -81   -795       C  
ATOM   1656  O   MET A 138      51.566  -3.104  10.344  1.00 63.40           O  
ANISOU 1656  O   MET A 138     6916   8352   8820   -683   -145   -767       O  
ATOM   1657  CB  MET A 138      48.899  -5.047  10.469  1.00 61.73           C  
ANISOU 1657  CB  MET A 138     7125   7853   8478   -267   -125   -660       C  
ATOM   1658  CG  MET A 138      48.458  -6.210  11.347  1.00 55.53           C  
ANISOU 1658  CG  MET A 138     6397   7101   7601   -134   -249   -588       C  
ATOM   1659  SD  MET A 138      49.796  -6.895  12.348  1.00 60.74           S  
ANISOU 1659  SD  MET A 138     6832   8015   8232   -106   -460   -528       S  
ATOM   1660  CE  MET A 138      51.048  -7.224  11.108  1.00 53.66           C  
ANISOU 1660  CE  MET A 138     5671   7216   7502      3   -390   -463       C  
ATOM   1661  N   SER A 139      49.709  -2.130   9.529  1.00 56.94           N  
ANISOU 1661  N   SER A 139     6517   7174   7945   -694     85   -863       N  
ATOM   1662  CA  SER A 139      50.483  -1.286   8.626  1.00 55.72           C  
ANISOU 1662  CA  SER A 139     6280   7009   7881   -818    208   -907       C  
ATOM   1663  C   SER A 139      51.303  -0.262   9.396  1.00 59.62           C  
ANISOU 1663  C   SER A 139     6699   7622   8332  -1100    131   -984       C  
ATOM   1664  O   SER A 139      52.399   0.108   8.958  1.00 59.37           O  
ANISOU 1664  O   SER A 139     6472   7693   8391  -1221    166   -990       O  
ATOM   1665  CB  SER A 139      49.556  -0.590   7.632  1.00 51.13           C  
ANISOU 1665  CB  SER A 139     5941   6188   7297   -799    396   -964       C  
ATOM   1666  OG  SER A 139      48.922  -1.533   6.785  1.00 55.16           O  
ANISOU 1666  OG  SER A 139     6503   6595   7859   -557    460   -891       O  
ATOM   1667  N   VAL A 140      50.795   0.208  10.536  1.00 60.56           N  
ANISOU 1667  N   VAL A 140     6976   7727   8308  -1216     29  -1041       N  
ATOM   1668  CA  VAL A 140      51.574   1.119  11.367  1.00 64.56           C  
ANISOU 1668  CA  VAL A 140     7438   8341   8751  -1494    -75  -1111       C  
ATOM   1669  C   VAL A 140      52.729   0.375  12.023  1.00 65.71           C  
ANISOU 1669  C   VAL A 140     7272   8754   8941  -1502   -273  -1045       C  
ATOM   1670  O   VAL A 140      53.858   0.877  12.081  1.00 70.59           O  
ANISOU 1670  O   VAL A 140     7687   9524   9609  -1701   -326  -1068       O  
ATOM   1671  CB  VAL A 140      50.669   1.790  12.416  1.00 60.25           C  
ANISOU 1671  CB  VAL A 140     7187   7685   8019  -1592   -123  -1186       C  
ATOM   1672  CG1 VAL A 140      51.508   2.526  13.453  1.00 59.72           C  
ANISOU 1672  CG1 VAL A 140     7087   7743   7863  -1871   -280  -1246       C  
ATOM   1673  CG2 VAL A 140      49.692   2.743  11.744  1.00 58.28           C  
ANISOU 1673  CG2 VAL A 140     7229   7192   7723  -1605     76  -1261       C  
ATOM   1674  N   ASP A 141      52.469  -0.837  12.516  1.00 71.05           N  
ANISOU 1674  N   ASP A 141     7903   9495   9597  -1285   -385   -959       N  
ATOM   1675  CA  ASP A 141      53.517  -1.604  13.177  1.00 73.08           C  
ANISOU 1675  CA  ASP A 141     7884  10004   9879  -1251   -584   -890       C  
ATOM   1676  C   ASP A 141      54.640  -1.954  12.208  1.00 75.89           C  
ANISOU 1676  C   ASP A 141     7918  10506  10411  -1191   -525   -827       C  
ATOM   1677  O   ASP A 141      55.822  -1.870  12.561  1.00 78.53           O  
ANISOU 1677  O   ASP A 141     7973  11070  10793  -1305   -651   -815       O  
ATOM   1678  CB  ASP A 141      52.924  -2.870  13.794  1.00 72.06           C  
ANISOU 1678  CB  ASP A 141     7825   9878   9679  -1005   -687   -808       C  
ATOM   1679  CG  ASP A 141      53.763  -3.408  14.935  1.00 86.81           C  
ANISOU 1679  CG  ASP A 141     9523  11971  11489  -1009   -937   -768       C  
ATOM   1680  OD1 ASP A 141      53.718  -2.816  16.036  1.00 82.96           O  
ANISOU 1680  OD1 ASP A 141     9147  11505  10870  -1188  -1073   -832       O  
ATOM   1681  OD2 ASP A 141      54.469  -4.418  14.731  1.00 98.49           O  
ANISOU 1681  OD2 ASP A 141    10774  13602  13043   -822  -1000   -671       O  
ATOM   1682  N   ARG A 142      54.292  -2.346  10.979  1.00 71.21           N  
ANISOU 1682  N   ARG A 142     7355   9785   9914  -1011   -333   -784       N  
ATOM   1683  CA  ARG A 142      55.325  -2.663   9.997  1.00 70.10           C  
ANISOU 1683  CA  ARG A 142     6937   9763   9936   -937   -243   -720       C  
ATOM   1684  C   ARG A 142      56.111  -1.421   9.592  1.00 75.66           C  
ANISOU 1684  C   ARG A 142     7525  10512  10709  -1224   -156   -797       C  
ATOM   1685  O   ARG A 142      57.328  -1.494   9.388  1.00 82.16           O  
ANISOU 1685  O   ARG A 142     8021  11550  11645  -1272   -174   -757       O  
ATOM   1686  CB  ARG A 142      54.708  -3.335   8.772  1.00 68.42           C  
ANISOU 1686  CB  ARG A 142     6840   9369   9787   -684    -56   -660       C  
ATOM   1687  CG  ARG A 142      54.361  -4.800   8.997  1.00 73.72           C  
ANISOU 1687  CG  ARG A 142     7533  10055  10424   -387   -140   -552       C  
ATOM   1688  CD  ARG A 142      54.018  -5.505   7.695  1.00 78.61           C  
ANISOU 1688  CD  ARG A 142     8233  10521  11116   -150     35   -483       C  
ATOM   1689  NE  ARG A 142      53.803  -6.936   7.892  1.00 69.60           N  
ANISOU 1689  NE  ARG A 142     7119   9392   9932    122    -45   -374       N  
ATOM   1690  CZ  ARG A 142      53.512  -7.793   6.918  1.00 68.32           C  
ANISOU 1690  CZ  ARG A 142     7053   9103   9804    353     68   -297       C  
ATOM   1691  NH1 ARG A 142      53.400  -7.370   5.665  1.00 63.36           N  
ANISOU 1691  NH1 ARG A 142     6493   8326   9256    357    264   -315       N  
ATOM   1692  NH2 ARG A 142      53.337  -9.077   7.199  1.00 68.33           N  
ANISOU 1692  NH2 ARG A 142     7107   9112   9743    579    -16   -202       N  
ATOM   1693  N   TYR A 143      55.441  -0.273   9.465  1.00 78.11           N  
ANISOU 1693  N   TYR A 143     8101  10627  10950  -1417    -53   -906       N  
ATOM   1694  CA  TYR A 143      56.174   0.959   9.191  1.00 73.88           C  
ANISOU 1694  CA  TYR A 143     7501  10120  10452  -1723     23   -988       C  
ATOM   1695  C   TYR A 143      57.099   1.300  10.351  1.00 81.43           C  
ANISOU 1695  C   TYR A 143     8254  11317  11368  -1967   -203  -1014       C  
ATOM   1696  O   TYR A 143      58.216   1.790  10.146  1.00 82.90           O  
ANISOU 1696  O   TYR A 143     8185  11667  11646  -2173   -197  -1026       O  
ATOM   1697  CB  TYR A 143      55.210   2.112   8.918  1.00 67.29           C  
ANISOU 1697  CB  TYR A 143     7043   9010   9516  -1862    166  -1100       C  
ATOM   1698  CG  TYR A 143      55.913   3.444   8.787  1.00 65.06           C  
ANISOU 1698  CG  TYR A 143     6757   8733   9232  -2210    232  -1195       C  
ATOM   1699  CD1 TYR A 143      56.537   3.808   7.604  1.00 65.85           C  
ANISOU 1699  CD1 TYR A 143     6754   8808   9457  -2270    433  -1195       C  
ATOM   1700  CD2 TYR A 143      55.959   4.334   9.852  1.00 71.33           C  
ANISOU 1700  CD2 TYR A 143     7672   9543   9887  -2489     99  -1283       C  
ATOM   1701  CE1 TYR A 143      57.187   5.020   7.482  1.00 68.01           C  
ANISOU 1701  CE1 TYR A 143     7036   9080   9723  -2611    503  -1281       C  
ATOM   1702  CE2 TYR A 143      56.606   5.551   9.739  1.00 75.97           C  
ANISOU 1702  CE2 TYR A 143     8283  10124  10459  -2832    156  -1371       C  
ATOM   1703  CZ  TYR A 143      57.217   5.889   8.550  1.00 72.45           C  
ANISOU 1703  CZ  TYR A 143     7725   9660  10145  -2899    361  -1370       C  
ATOM   1704  OH  TYR A 143      57.864   7.099   8.428  1.00 76.36           O  
ANISOU 1704  OH  TYR A 143     8256  10139  10618  -3261    429  -1458       O  
ATOM   1705  N   GLN A 144      56.648   1.047  11.582  1.00 82.44           N  
ANISOU 1705  N   GLN A 144     8495  11470  11357  -1955   -405  -1022       N  
ATOM   1706  CA  GLN A 144      57.515   1.227  12.739  1.00 86.59           C  
ANISOU 1706  CA  GLN A 144     8838  12230  11833  -2155   -654  -1038       C  
ATOM   1707  C   GLN A 144      58.699   0.270  12.694  1.00 93.53           C  
ANISOU 1707  C   GLN A 144     9278  13410  12848  -2025   -768   -929       C  
ATOM   1708  O   GLN A 144      59.801   0.623  13.127  1.00104.03           O  
ANISOU 1708  O   GLN A 144    10333  14978  14217  -2239   -910   -939       O  
ATOM   1709  CB  GLN A 144      56.716   1.023  14.027  1.00 83.40           C  
ANISOU 1709  CB  GLN A 144     8680  11766  11240  -2119   -833  -1058       C  
ATOM   1710  CG  GLN A 144      55.776   2.166  14.366  1.00 68.14           C  
ANISOU 1710  CG  GLN A 144     7151   9592   9149  -2306   -763  -1174       C  
ATOM   1711  CD  GLN A 144      55.192   2.042  15.759  1.00 69.04           C  
ANISOU 1711  CD  GLN A 144     7480   9681   9071  -2307   -950  -1193       C  
ATOM   1712  OE1 GLN A 144      54.173   1.382  15.960  1.00 74.38           O  
ANISOU 1712  OE1 GLN A 144     8339  10237   9685  -2077   -921  -1157       O  
ATOM   1713  NE2 GLN A 144      55.837   2.675  16.731  1.00 95.48           N  
ANISOU 1713  NE2 GLN A 144    10816  13140  12321  -2575  -1141  -1249       N  
ATOM   1714  N   SER A 145      58.491  -0.941  12.172  1.00 90.98           N  
ANISOU 1714  N   SER A 145     8889  13085  12593  -1675   -710   -822       N  
ATOM   1715  CA  SER A 145      59.563  -1.929  12.134  1.00105.82           C  
ANISOU 1715  CA  SER A 145    10379  15242  14586  -1497   -808   -709       C  
ATOM   1716  C   SER A 145      60.678  -1.525  11.176  1.00115.87           C  
ANISOU 1716  C   SER A 145    11325  16661  16040  -1607   -668   -692       C  
ATOM   1717  O   SER A 145      61.846  -1.851  11.416  1.00122.41           O  
ANISOU 1717  O   SER A 145    11763  17790  16957  -1610   -793   -631       O  
ATOM   1718  CB  SER A 145      58.997  -3.291  11.730  1.00100.45           C  
ANISOU 1718  CB  SER A 145     9774  14479  13912  -1094   -751   -601       C  
ATOM   1719  OG  SER A 145      57.981  -3.708  12.626  1.00102.18           O  
ANISOU 1719  OG  SER A 145    10282  14574  13967  -1003   -870   -611       O  
ATOM   1720  N   VAL A 146      60.344  -0.824  10.094  1.00113.45           N  
ANISOU 1720  N   VAL A 146    11167  16150  15789  -1691   -407   -742       N  
ATOM   1721  CA  VAL A 146      61.352  -0.455   9.106  1.00112.51           C  
ANISOU 1721  CA  VAL A 146    10765  16143  15840  -1789   -235   -722       C  
ATOM   1722  C   VAL A 146      62.127   0.781   9.548  1.00113.20           C  
ANISOU 1722  C   VAL A 146    10717  16363  15932  -2223   -305   -816       C  
ATOM   1723  O   VAL A 146      63.355   0.831   9.426  1.00124.47           O  
ANISOU 1723  O   VAL A 146    11739  18064  17490  -2334   -330   -776       O  
ATOM   1724  CB  VAL A 146      60.688  -0.251   7.732  1.00110.72           C  
ANISOU 1724  CB  VAL A 146    10782  15627  15659  -1688     76   -735       C  
ATOM   1725  CG1 VAL A 146      61.670   0.360   6.750  1.00111.86           C  
ANISOU 1725  CG1 VAL A 146    10697  15849  15957  -1849    279   -736       C  
ATOM   1726  CG2 VAL A 146      60.162  -1.575   7.198  1.00 88.31           C  
ANISOU 1726  CG2 VAL A 146     8014  12701  12839  -1267    137   -625       C  
ATOM   1727  N   ILE A 147      61.430   1.795  10.065  1.00 97.88           N  
ANISOU 1727  N   ILE A 147     9113  14235  13843  -2478   -336   -937       N  
ATOM   1728  CA  ILE A 147      62.108   3.022  10.471  1.00101.83           C  
ANISOU 1728  CA  ILE A 147     9549  14823  14320  -2917   -398  -1034       C  
ATOM   1729  C   ILE A 147      62.949   2.793  11.722  1.00116.89           C  
ANISOU 1729  C   ILE A 147    11166  17047  16201  -3038   -727  -1013       C  
ATOM   1730  O   ILE A 147      63.987   3.440  11.908  1.00118.69           O  
ANISOU 1730  O   ILE A 147    11126  17483  16487  -3357   -804  -1043       O  
ATOM   1731  CB  ILE A 147      61.078   4.147  10.696  1.00102.72           C  
ANISOU 1731  CB  ILE A 147    10153  14622  14253  -3124   -335  -1166       C  
ATOM   1732  CG1 ILE A 147      60.230   4.374   9.441  1.00 94.89           C  
ANISOU 1732  CG1 ILE A 147     9450  13322  13283  -2984    -24  -1185       C  
ATOM   1733  CG2 ILE A 147      61.777   5.437  11.105  1.00110.88           C  
ANISOU 1733  CG2 ILE A 147    11170  15719  15240  -3596   -394  -1268       C  
ATOM   1734  CD1 ILE A 147      61.012   4.838   8.225  1.00 97.23           C  
ANISOU 1734  CD1 ILE A 147     9577  13634  13733  -3105    217  -1183       C  
ATOM   1735  N   TYR A 148      62.524   1.878  12.594  1.00119.38           N  
ANISOU 1735  N   TYR A 148     9046  14410  21902  -3637   1110  -1543       N  
ATOM   1736  CA  TYR A 148      63.180   1.615  13.875  1.00121.56           C  
ANISOU 1736  CA  TYR A 148     8988  15164  22037  -3409    781  -2111       C  
ATOM   1737  C   TYR A 148      63.465   0.122  13.963  1.00118.24           C  
ANISOU 1737  C   TYR A 148     8690  15301  20933  -3154    864  -1878       C  
ATOM   1738  O   TYR A 148      62.603  -0.659  14.389  1.00114.54           O  
ANISOU 1738  O   TYR A 148     8543  15170  19807  -2848    808  -1791       O  
ATOM   1739  CB  TYR A 148      62.316   2.088  15.041  1.00122.09           C  
ANISOU 1739  CB  TYR A 148     9086  15337  21966  -3178    429  -2597       C  
ATOM   1740  CG  TYR A 148      61.806   3.503  14.878  1.00126.92           C  
ANISOU 1740  CG  TYR A 148     9662  15381  23180  -3406    364  -2759       C  
ATOM   1741  CD1 TYR A 148      62.585   4.592  15.248  1.00134.63           C  
ANISOU 1741  CD1 TYR A 148    10194  16118  24843  -3605    179  -3233       C  
ATOM   1742  CD2 TYR A 148      60.544   3.748  14.354  1.00121.79           C  
ANISOU 1742  CD2 TYR A 148     9423  14435  22418  -3420    483  -2444       C  
ATOM   1743  CE1 TYR A 148      62.121   5.886  15.098  1.00137.82           C  
ANISOU 1743  CE1 TYR A 148    10569  15997  25801  -3813    115  -3382       C  
ATOM   1744  CE2 TYR A 148      60.071   5.036  14.201  1.00126.69           C  
ANISOU 1744  CE2 TYR A 148    10018  14532  23586  -3623    415  -2594       C  
ATOM   1745  CZ  TYR A 148      60.862   6.102  14.575  1.00142.88           C  
ANISOU 1745  CZ  TYR A 148    11629  16349  26310  -3819    231  -3059       C  
ATOM   1746  OH  TYR A 148      60.393   7.387  14.424  1.00153.59           O  
ANISOU 1746  OH  TYR A 148    12965  17178  28216  -4020    159  -3209       O  
ATOM   1747  N   PRO A 149      64.665  -0.318  13.564  1.00123.38           N  
ANISOU 1747  N   PRO A 149     9096  16064  21718  -3271    999  -1774       N  
ATOM   1748  CA  PRO A 149      64.937  -1.768  13.581  1.00120.11           C  
ANISOU 1748  CA  PRO A 149     8814  16169  20653  -3033   1090  -1522       C  
ATOM   1749  C   PRO A 149      64.853  -2.406  14.960  1.00120.78           C  
ANISOU 1749  C   PRO A 149     8853  16834  20205  -2636    751  -1958       C  
ATOM   1750  O   PRO A 149      64.386  -3.547  15.075  1.00121.34           O  
ANISOU 1750  O   PRO A 149     9231  17294  19579  -2366    800  -1710       O  
ATOM   1751  CB  PRO A 149      66.364  -1.856  13.012  1.00123.06           C  
ANISOU 1751  CB  PRO A 149     8834  16504  21420  -3267   1245  -1459       C  
ATOM   1752  CG  PRO A 149      66.557  -0.590  12.237  1.00125.81           C  
ANISOU 1752  CG  PRO A 149     9035  16220  22547  -3674   1384  -1414       C  
ATOM   1753  CD  PRO A 149      65.777   0.452  12.977  1.00127.56           C  
ANISOU 1753  CD  PRO A 149     9247  16231  22988  -3639   1109  -1829       C  
ATOM   1754  N   PHE A 150      65.291  -1.714  16.011  1.00135.64           N  
ANISOU 1754  N   PHE A 150    10367  18784  22387  -2591    408  -2598       N  
ATOM   1755  CA  PHE A 150      65.273  -2.274  17.360  1.00140.85           C  
ANISOU 1755  CA  PHE A 150    10965  19989  22561  -2218     71  -3044       C  
ATOM   1756  C   PHE A 150      63.901  -2.087  18.003  1.00153.53           C  
ANISOU 1756  C   PHE A 150    12883  21631  23822  -2003    -93  -3170       C  
ATOM   1757  O   PHE A 150      63.807  -1.640  19.150  1.00147.10           O  
ANISOU 1757  O   PHE A 150    11893  20967  23030  -1845   -436  -3731       O  
ATOM   1758  CB  PHE A 150      66.369  -1.628  18.213  1.00142.29           C  
ANISOU 1758  CB  PHE A 150    10609  20240  23214  -2255   -231  -3687       C  
ATOM   1759  CG  PHE A 150      67.595  -2.480  18.369  1.00126.79           C  
ANISOU 1759  CG  PHE A 150     8390  18671  21113  -2172   -247  -3751       C  
ATOM   1760  CD1 PHE A 150      68.607  -2.446  17.425  1.00118.15           C  
ANISOU 1760  CD1 PHE A 150     7078  17372  20440  -2462      0  -3512       C  
ATOM   1761  CD2 PHE A 150      67.736  -3.312  19.467  1.00136.15           C  
ANISOU 1761  CD2 PHE A 150     9555  20431  21746  -1803   -511  -4056       C  
ATOM   1762  CE1 PHE A 150      69.734  -3.228  17.571  1.00119.06           C  
ANISOU 1762  CE1 PHE A 150     6950  17852  20434  -2382    -21  -3585       C  
ATOM   1763  CE2 PHE A 150      68.861  -4.096  19.619  1.00154.60           C  
ANISOU 1763  CE2 PHE A 150    11659  23127  23954  -1717   -540  -4125       C  
ATOM   1764  CZ  PHE A 150      69.861  -4.054  18.670  1.00124.53           C  
ANISOU 1764  CZ  PHE A 150     7625  19114  20577  -2006   -296  -3893       C  
ATOM   1765  N   LEU A 151      62.830  -2.459  17.293  1.00154.58           N  
ANISOU 1765  N   LEU A 151    13477  21642  23615  -1986    148  -2659       N  
ATOM   1766  CA  LEU A 151      61.490  -2.118  17.764  1.00150.60           C  
ANISOU 1766  CA  LEU A 151    13260  21078  22883  -1838     22  -2763       C  
ATOM   1767  C   LEU A 151      61.027  -2.950  18.957  1.00152.88           C  
ANISOU 1767  C   LEU A 151    13687  21941  22461  -1424   -223  -3027       C  
ATOM   1768  O   LEU A 151      60.183  -2.482  19.729  1.00155.12           O  
ANISOU 1768  O   LEU A 151    14053  22234  22653  -1286   -442  -3349       O  
ATOM   1769  CB  LEU A 151      60.484  -2.280  16.619  1.00150.85           C  
ANISOU 1769  CB  LEU A 151    13744  20804  22768  -1942    357  -2135       C  
ATOM   1770  CG  LEU A 151      59.071  -1.742  16.861  1.00136.45           C  
ANISOU 1770  CG  LEU A 151    12214  18790  20840  -1863    274  -2191       C  
ATOM   1771  CD1 LEU A 151      59.066  -0.221  16.907  1.00122.77           C  
ANISOU 1771  CD1 LEU A 151    10237  16556  19854  -2111    140  -2531       C  
ATOM   1772  CD2 LEU A 151      58.116  -2.254  15.791  1.00111.37           C  
ANISOU 1772  CD2 LEU A 151     9519  15447  17350  -1890    607  -1539       C  
ATOM   1773  N   SER A 152      61.548  -4.166  19.144  1.00148.97           N  
ANISOU 1773  N   SER A 152    13224  21923  21454  -1221   -196  -2907       N  
ATOM   1774  CA  SER A 152      61.084  -4.971  20.273  1.00148.04           C  
ANISOU 1774  CA  SER A 152    13263  22344  20641   -828   -423  -3145       C  
ATOM   1775  C   SER A 152      61.427  -4.306  21.603  1.00148.41           C  
ANISOU 1775  C   SER A 152    12962  22545  20880   -707   -836  -3878       C  
ATOM   1776  O   SER A 152      60.583  -4.214  22.501  1.00147.59           O  
ANISOU 1776  O   SER A 152    13000  22610  20468   -485  -1050  -4167       O  
ATOM   1777  CB  SER A 152      61.682  -6.375  20.206  1.00147.36           C  
ANISOU 1777  CB  SER A 152    13254  22726  20010   -645   -324  -2888       C  
ATOM   1778  OG  SER A 152      61.511  -7.051  21.441  1.00149.45           O  
ANISOU 1778  OG  SER A 152    13574  23523  19689   -276   -597  -3227       O  
ATOM   1779  N   GLN A 153      62.668  -3.830  21.741  1.00148.73           N  
ANISOU 1779  N   GLN A 153    12542  22530  21438   -854   -951  -4193       N  
ATOM   1780  CA  GLN A 153      63.048  -3.083  22.936  1.00150.19           C  
ANISOU 1780  CA  GLN A 153    12365  22809  21891   -771  -1342  -4900       C  
ATOM   1781  C   GLN A 153      62.467  -1.676  22.908  1.00147.21           C  
ANISOU 1781  C   GLN A 153    11911  21935  22086   -975  -1419  -5122       C  
ATOM   1782  O   GLN A 153      62.085  -1.135  23.953  1.00130.22           O  
ANISOU 1782  O   GLN A 153     9669  19869  19939   -828  -1729  -5629       O  
ATOM   1783  CB  GLN A 153      64.568  -3.047  23.081  1.00154.30           C  
ANISOU 1783  CB  GLN A 153    12412  23432  22782   -859  -1439  -5170       C  
ATOM   1784  CG  GLN A 153      65.184  -4.409  23.375  1.00142.10           C  
ANISOU 1784  CG  GLN A 153    10901  22438  20652   -603  -1450  -5081       C  
ATOM   1785  CD  GLN A 153      65.719  -5.092  22.133  1.00140.23           C  
ANISOU 1785  CD  GLN A 153    10742  22124  20417   -776  -1083  -4493       C  
ATOM   1786  OE1 GLN A 153      65.081  -5.084  21.080  1.00138.20           O  
ANISOU 1786  OE1 GLN A 153    10775  21555  20181   -947   -768  -3970       O  
ATOM   1787  NE2 GLN A 153      66.903  -5.682  22.249  1.00123.36           N  
ANISOU 1787  NE2 GLN A 153     8340  20270  18263   -731  -1124  -4585       N  
ATOM   1788  N   ARG A 154      62.393  -1.067  21.717  1.00152.17           N  
ANISOU 1788  N   ARG A 154    12579  22038  23202  -1314  -1141  -4747       N  
ATOM   1789  CA  ARG A 154      61.855   0.278  21.557  1.00154.26           C  
ANISOU 1789  CA  ARG A 154    12788  21784  24039  -1533  -1187  -4906       C  
ATOM   1790  C   ARG A 154      60.388   0.361  21.942  1.00151.59           C  
ANISOU 1790  C   ARG A 154    12821  21452  23325  -1351  -1260  -4912       C  
ATOM   1791  O   ARG A 154      59.870   1.469  22.124  1.00153.57           O  
ANISOU 1791  O   ARG A 154    13011  21357  23982  -1459  -1387  -5171       O  
ATOM   1792  CB  ARG A 154      62.013   0.727  20.100  1.00153.99           C  
ANISOU 1792  CB  ARG A 154    12798  21210  24502  -1915   -833  -4409       C  
ATOM   1793  CG  ARG A 154      62.402   2.177  19.911  1.00158.56           C  
ANISOU 1793  CG  ARG A 154    13044  21263  25938  -2237   -902  -4687       C  
ATOM   1794  CD  ARG A 154      61.286   2.970  19.257  1.00157.32           C  
ANISOU 1794  CD  ARG A 154    13169  20599  26005  -2403   -773  -4446       C  
ATOM   1795  NE  ARG A 154      61.658   4.366  19.051  1.00161.75           N  
ANISOU 1795  NE  ARG A 154    13424  20639  27394  -2719   -835  -4700       N  
ATOM   1796  CZ  ARG A 154      60.870   5.278  18.492  1.00161.78           C  
ANISOU 1796  CZ  ARG A 154    13591  20130  27747  -2911   -755  -4564       C  
ATOM   1797  NH1 ARG A 154      59.653   4.951  18.075  1.00157.59           N  
ANISOU 1797  NH1 ARG A 154    13523  19538  26817  -2819   -609  -4183       N  
ATOM   1798  NH2 ARG A 154      61.302   6.523  18.349  1.00166.07           N  
ANISOU 1798  NH2 ARG A 154    13835  20218  29048  -3196   -824  -4817       N  
ATOM   1799  N   ARG A 155      59.716  -0.775  22.081  1.00153.83           N  
ANISOU 1799  N   ARG A 155    13478  22119  22851  -1079  -1185  -4645       N  
ATOM   1800  CA  ARG A 155      58.289  -0.783  22.332  1.00150.93           C  
ANISOU 1800  CA  ARG A 155    13491  21755  22100   -917  -1208  -4591       C  
ATOM   1801  C   ARG A 155      58.021  -0.477  23.799  1.00153.08           C  
ANISOU 1801  C   ARG A 155    13630  22316  22216   -663  -1605  -5241       C  
ATOM   1802  O   ARG A 155      58.902  -0.563  24.654  1.00155.98           O  
ANISOU 1802  O   ARG A 155    13675  22986  22602   -548  -1850  -5675       O  
ATOM   1803  CB  ARG A 155      57.713  -2.148  21.951  1.00147.36           C  
ANISOU 1803  CB  ARG A 155    13478  21621  20891   -720   -976  -4072       C  
ATOM   1804  CG  ARG A 155      56.232  -2.187  21.626  1.00144.26           C  
ANISOU 1804  CG  ARG A 155    13538  21081  20192   -661   -844  -3778       C  
ATOM   1805  CD  ARG A 155      55.946  -3.401  20.750  1.00139.12           C  
ANISOU 1805  CD  ARG A 155    13268  20576  19017   -604   -509  -3122       C  
ATOM   1806  NE  ARG A 155      56.489  -4.625  21.341  1.00136.42           N  
ANISOU 1806  NE  ARG A 155    12926  20816  18091   -338   -570  -3151       N  
ATOM   1807  CZ  ARG A 155      57.070  -5.612  20.660  1.00134.07           C  
ANISOU 1807  CZ  ARG A 155    12707  20683  17551   -346   -336  -2715       C  
ATOM   1808  NH1 ARG A 155      57.525  -6.676  21.308  1.00132.78           N  
ANISOU 1808  NH1 ARG A 155    12541  21055  16854    -84   -431  -2795       N  
ATOM   1809  NH2 ARG A 155      57.214  -5.540  19.342  1.00133.10           N  
ANISOU 1809  NH2 ARG A 155    12664  20192  17717   -613    -13  -2207       N  
ATOM   1810  N   ASN A 156      56.763  -0.212  24.099  1.00143.71           N  
ANISOU 1810  N   ASN A 156    12716  21068  20819   -553  -1665  -5296       N  
ATOM   1811  CA  ASN A 156      56.330  -0.052  25.472  1.00142.00           C  
ANISOU 1811  CA  ASN A 156    12449  21159  20345   -284  -2013  -5860       C  
ATOM   1812  C   ASN A 156      55.526  -1.288  25.821  1.00139.63           C  
ANISOU 1812  C   ASN A 156    12559  21321  19171     37  -1956  -5646       C  
ATOM   1813  O   ASN A 156      54.572  -1.613  25.101  1.00146.46           O  
ANISOU 1813  O   ASN A 156    13813  22052  19784     20  -1709  -5184       O  
ATOM   1814  CB  ASN A 156      55.472   1.207  25.645  1.00148.43           C  
ANISOU 1814  CB  ASN A 156    13255  21572  21570   -388  -2145  -6134       C  
ATOM   1815  CG  ASN A 156      54.852   1.322  27.038  1.00147.46           C  
ANISOU 1815  CG  ASN A 156    13136  21775  21119    -94  -2484  -6684       C  
ATOM   1816  OD1 ASN A 156      54.799   0.357  27.800  1.00144.38           O  
ANISOU 1816  OD1 ASN A 156    12862  21909  20087    205  -2578  -6776       O  
ATOM   1817  ND2 ASN A 156      54.369   2.516  27.368  1.00150.44           N  
ANISOU 1817  ND2 ASN A 156    13391  21834  21936   -183  -2666  -7052       N  
ATOM   1818  N   PRO A 157      55.865  -2.006  26.894  1.00143.04           N  
ANISOU 1818  N   PRO A 157    12929  22294  19125    331  -2174  -5960       N  
ATOM   1819  CA  PRO A 157      55.175  -3.280  27.139  1.00138.71           C  
ANISOU 1819  CA  PRO A 157    12786  22189  17729    624  -2086  -5702       C  
ATOM   1820  C   PRO A 157      53.673  -3.130  27.237  1.00137.17           C  
ANISOU 1820  C   PRO A 157    12956  21908  17252    715  -2052  -5636       C  
ATOM   1821  O   PRO A 157      52.937  -4.050  26.861  1.00140.55           O  
ANISOU 1821  O   PRO A 157    13787  22493  17124    834  -1836  -5204       O  
ATOM   1822  CB  PRO A 157      55.784  -3.760  28.466  1.00140.78           C  
ANISOU 1822  CB  PRO A 157    12861  22990  17639    914  -2404  -6198       C  
ATOM   1823  CG  PRO A 157      57.097  -3.049  28.571  1.00145.54           C  
ANISOU 1823  CG  PRO A 157    12958  23455  18886    742  -2563  -6541       C  
ATOM   1824  CD  PRO A 157      56.882  -1.717  27.923  1.00147.46           C  
ANISOU 1824  CD  PRO A 157    13062  23088  19879    417  -2507  -6556       C  
ATOM   1825  N   TRP A 158      53.194  -1.988  27.721  1.00150.34           N  
ANISOU 1825  N   TRP A 158    14493  23328  19302    660  -2258  -6056       N  
ATOM   1826  CA  TRP A 158      51.769  -1.778  27.925  1.00148.21           C  
ANISOU 1826  CA  TRP A 158    14540  22989  18785    758  -2261  -6067       C  
ATOM   1827  C   TRP A 158      51.030  -1.402  26.645  1.00145.78           C  
ANISOU 1827  C   TRP A 158    14474  22175  18741    518  -1960  -5568       C  
ATOM   1828  O   TRP A 158      49.795  -1.440  26.636  1.00143.16           O  
ANISOU 1828  O   TRP A 158    14468  21802  18125    606  -1901  -5462       O  
ATOM   1829  CB  TRP A 158      51.563  -0.714  28.997  1.00152.04           C  
ANISOU 1829  CB  TRP A 158    14779  23427  19564    809  -2618  -6741       C  
ATOM   1830  CG  TRP A 158      52.054  -1.185  30.331  1.00153.87           C  
ANISOU 1830  CG  TRP A 158    14854  24201  19411   1096  -2915  -7221       C  
ATOM   1831  CD1 TRP A 158      53.245  -0.870  30.916  1.00158.02           C  
ANISOU 1831  CD1 TRP A 158    14984  24804  20252   1094  -3117  -7598       C  
ATOM   1832  CD2 TRP A 158      51.414  -2.123  31.205  1.00151.58           C  
ANISOU 1832  CD2 TRP A 158    14919  24299  18377   1451  -2864  -7139       C  
ATOM   1833  NE1 TRP A 158      53.368  -1.516  32.121  1.00158.53           N  
ANISOU 1833  NE1 TRP A 158    15202  25210  19822   1443  -3137  -7686       N  
ATOM   1834  CE2 TRP A 158      52.260  -2.297  32.320  1.00154.63           C  
ANISOU 1834  CE2 TRP A 158    15147  24893  18712   1655  -2970  -7381       C  
ATOM   1835  CE3 TRP A 158      50.203  -2.820  31.162  1.00147.35           C  
ANISOU 1835  CE3 TRP A 158    14844  23854  17290   1611  -2657  -6770       C  
ATOM   1836  CZ2 TRP A 158      51.931  -3.133  33.383  1.00153.61           C  
ANISOU 1836  CZ2 TRP A 158    15269  25044  18052   1989  -2885  -7260       C  
ATOM   1837  CZ3 TRP A 158      49.879  -3.651  32.219  1.00148.06           C  
ANISOU 1837  CZ3 TRP A 158    15165  24188  16901   1928  -2555  -6606       C  
ATOM   1838  CH2 TRP A 158      50.740  -3.801  33.313  1.00149.77           C  
ANISOU 1838  CH2 TRP A 158    15186  24597  17122   2103  -2675  -6851       C  
ATOM   1839  N   GLN A 159      51.744  -1.036  25.576  1.00130.12           N  
ANISOU 1839  N   GLN A 159    12344  19805  17291    219  -1771  -5267       N  
ATOM   1840  CA  GLN A 159      51.086  -0.498  24.388  1.00132.30           C  
ANISOU 1840  CA  GLN A 159    12818  19547  17904    -29  -1517  -4848       C  
ATOM   1841  C   GLN A 159      50.050  -1.472  23.840  1.00122.45           C  
ANISOU 1841  C   GLN A 159    12067  18418  16040     98  -1250  -4324       C  
ATOM   1842  O   GLN A 159      48.911  -1.086  23.555  1.00 99.55           O  
ANISOU 1842  O   GLN A 159     9421  15264  13140     76  -1185  -4215       O  
ATOM   1843  CB  GLN A 159      52.121  -0.170  23.310  1.00143.36           C  
ANISOU 1843  CB  GLN A 159    14005  20584  19880   -351  -1325  -4557       C  
ATOM   1844  CG  GLN A 159      51.547   0.593  22.122  1.00102.28           C  
ANISOU 1844  CG  GLN A 159     8957  14772  15134   -636  -1098  -4189       C  
ATOM   1845  CD  GLN A 159      52.595   0.953  21.087  1.00129.41           C  
ANISOU 1845  CD  GLN A 159    12175  17845  19150   -964   -909  -3922       C  
ATOM   1846  OE1 GLN A 159      53.790   0.739  21.294  1.00130.12           O  
ANISOU 1846  OE1 GLN A 159    11956  18118  19364   -992   -966  -4060       O  
ATOM   1847  NE2 GLN A 159      52.151   1.498  19.960  1.00112.47           N  
ANISOU 1847  NE2 GLN A 159    10195  15181  17359  -1212   -680  -3537       N  
ATOM   1848  N   ALA A 160      50.424  -2.743  23.683  1.00108.53           N  
ANISOU 1848  N   ALA A 160    10448  17038  13751    234  -1097  -3999       N  
ATOM   1849  CA  ALA A 160      49.475  -3.711  23.145  1.00102.73           C  
ANISOU 1849  CA  ALA A 160    10182  16423  12429    354   -837  -3491       C  
ATOM   1850  C   ALA A 160      48.297  -3.901  24.091  1.00104.12           C  
ANISOU 1850  C   ALA A 160    10596  16870  12096    628   -989  -3753       C  
ATOM   1851  O   ALA A 160      47.176  -4.164  23.644  1.00 95.29           O  
ANISOU 1851  O   ALA A 160     9847  15662  10696    669   -814  -3439       O  
ATOM   1852  CB  ALA A 160      50.171  -5.045  22.881  1.00 97.09           C  
ANISOU 1852  CB  ALA A 160     9551  16092  11247    460   -668  -3133       C  
ATOM   1853  N   SER A 161      48.532  -3.774  25.400  1.00120.97           N  
ANISOU 1853  N   SER A 161    12523  19336  14105    818  -1313  -4330       N  
ATOM   1854  CA  SER A 161      47.452  -3.881  26.372  1.00113.29           C  
ANISOU 1854  CA  SER A 161    11748  18622  12675   1072  -1474  -4630       C  
ATOM   1855  C   SER A 161      46.460  -2.732  26.244  1.00101.83           C  
ANISOU 1855  C   SER A 161    10342  16733  11617    950  -1525  -4784       C  
ATOM   1856  O   SER A 161      45.302  -2.878  26.649  1.00 78.17           O  
ANISOU 1856  O   SER A 161     7614  13849   8236   1115  -1547  -4850       O  
ATOM   1857  CB  SER A 161      48.021  -3.924  27.790  1.00106.41           C  
ANISOU 1857  CB  SER A 161    10617  18181  11633   1287  -1820  -5233       C  
ATOM   1858  OG  SER A 161      48.886  -5.035  27.951  1.00125.58           O  
ANISOU 1858  OG  SER A 161    13026  21033  13654   1424  -1786  -5098       O  
ATOM   1859  N   TYR A 162      46.895  -1.597  25.692  1.00 95.36           N  
ANISOU 1859  N   TYR A 162     9263  15414  11554    664  -1545  -4848       N  
ATOM   1860  CA  TYR A 162      46.041  -0.435  25.478  1.00 87.77           C  
ANISOU 1860  CA  TYR A 162     8326  13986  11037    522  -1595  -4980       C  
ATOM   1861  C   TYR A 162      45.458  -0.398  24.069  1.00 81.03           C  
ANISOU 1861  C   TYR A 162     7759  12697  10333    324  -1263  -4379       C  
ATOM   1862  O   TYR A 162      44.288  -0.041  23.897  1.00 79.47           O  
ANISOU 1862  O   TYR A 162     7802  12287  10108    333  -1228  -4332       O  
ATOM   1863  CB  TYR A 162      46.833   0.854  25.720  1.00 91.62           C  
ANISOU 1863  CB  TYR A 162     8365  14157  12290    321  -1825  -5423       C  
ATOM   1864  CG  TYR A 162      46.841   1.333  27.153  1.00 98.46           C  
ANISOU 1864  CG  TYR A 162     8991  15277  13142    500  -2207  -6128       C  
ATOM   1865  CD1 TYR A 162      47.135   0.466  28.197  1.00106.27           C  
ANISOU 1865  CD1 TYR A 162     9960  16855  13563    785  -2358  -6374       C  
ATOM   1866  CD2 TYR A 162      46.572   2.661  27.460  1.00 95.80           C  
ANISOU 1866  CD2 TYR A 162     8449  14587  13365    383  -2422  -6550       C  
ATOM   1867  CE1 TYR A 162      47.146   0.906  29.509  1.00103.86           C  
ANISOU 1867  CE1 TYR A 162     9441  16784  13238    952  -2708  -7020       C  
ATOM   1868  CE2 TYR A 162      46.583   3.109  28.766  1.00 99.37           C  
ANISOU 1868  CE2 TYR A 162     8677  15270  13808    547  -2773  -7201       C  
ATOM   1869  CZ  TYR A 162      46.871   2.228  29.786  1.00103.51           C  
ANISOU 1869  CZ  TYR A 162     9189  16385  13756    832  -2913  -7433       C  
ATOM   1870  OH  TYR A 162      46.883   2.672  31.088  1.00114.03           O  
ANISOU 1870  OH  TYR A 162    10397  17838  15092   1039  -3091  -7809       O  
ATOM   1871  N   ILE A 163      46.253  -0.757  23.059  1.00 85.33           N  
ANISOU 1871  N   ILE A 163     8281  13104  11037    146  -1021  -3924       N  
ATOM   1872  CA  ILE A 163      45.791  -0.658  21.678  1.00 80.00           C  
ANISOU 1872  CA  ILE A 163     7858  11987  10553    -61   -709  -3355       C  
ATOM   1873  C   ILE A 163      44.661  -1.647  21.421  1.00 74.94           C  
ANISOU 1873  C   ILE A 163     7686  11548   9241    129   -508  -2970       C  
ATOM   1874  O   ILE A 163      43.654  -1.308  20.788  1.00 76.30           O  
ANISOU 1874  O   ILE A 163     8116  11387   9487     60   -381  -2742       O  
ATOM   1875  CB  ILE A 163      46.967  -0.881  20.709  1.00 80.49           C  
ANISOU 1875  CB  ILE A 163     7776  11899  10906   -284   -496  -2970       C  
ATOM   1876  CG1 ILE A 163      47.976   0.267  20.807  1.00 85.56           C  
ANISOU 1876  CG1 ILE A 163     7966  12234  12308   -521   -668  -3327       C  
ATOM   1877  CG2 ILE A 163      46.462  -1.022  19.280  1.00 77.24           C  
ANISOU 1877  CG2 ILE A 163     7681  11109  10556   -457   -145  -2324       C  
ATOM   1878  CD1 ILE A 163      47.519   1.550  20.141  1.00 87.17           C  
ANISOU 1878  CD1 ILE A 163     8158  11803  13160   -784   -645  -3310       C  
ATOM   1879  N   VAL A 164      44.804  -2.883  21.905  1.00 70.70           N  
ANISOU 1879  N   VAL A 164     7269  11553   8041    371   -479  -2894       N  
ATOM   1880  CA  VAL A 164      43.800  -3.907  21.617  1.00 70.55           C  
ANISOU 1880  CA  VAL A 164     7696  11738   7372    546   -267  -2497       C  
ATOM   1881  C   VAL A 164      42.435  -3.521  22.172  1.00 65.92           C  
ANISOU 1881  C   VAL A 164     7308  11126   6614    681   -384  -2752       C  
ATOM   1882  O   VAL A 164      41.454  -3.541  21.409  1.00 68.34           O  
ANISOU 1882  O   VAL A 164     7927  11182   6856    639   -187  -2403       O  
ATOM   1883  CB  VAL A 164      44.283  -5.278  22.124  1.00 67.06           C  
ANISOU 1883  CB  VAL A 164     7321  11893   6264    784   -241  -2413       C  
ATOM   1884  CG1 VAL A 164      43.138  -6.279  22.137  1.00 64.82           C  
ANISOU 1884  CG1 VAL A 164     7482  11879   5268   1007    -87  -2138       C  
ATOM   1885  CG2 VAL A 164      45.423  -5.785  21.252  1.00 67.50           C  
ANISOU 1885  CG2 VAL A 164     7277  11918   6450    635    -38  -2005       C  
ATOM   1886  N   PRO A 165      42.286  -3.174  23.455  1.00 67.17           N  
ANISOU 1886  N   PRO A 165     7306  11529   6686    845   -693  -3345       N  
ATOM   1887  CA  PRO A 165      40.971  -2.702  23.919  1.00 66.61           C  
ANISOU 1887  CA  PRO A 165     7409  11386   6512    948   -798  -3595       C  
ATOM   1888  C   PRO A 165      40.464  -1.495  23.149  1.00 67.66           C  
ANISOU 1888  C   PRO A 165     7532  10894   7280    704   -767  -3546       C  
ATOM   1889  O   PRO A 165      39.261  -1.392  22.881  1.00 65.39           O  
ANISOU 1889  O   PRO A 165     7530  10449   6865    741   -685  -3428       O  
ATOM   1890  CB  PRO A 165      41.219  -2.371  25.399  1.00 70.01           C  
ANISOU 1890  CB  PRO A 165     7573  12142   6884   1118  -1158  -4280       C  
ATOM   1891  CG  PRO A 165      42.373  -3.211  25.785  1.00 70.59           C  
ANISOU 1891  CG  PRO A 165     7492  12635   6693   1214  -1188  -4283       C  
ATOM   1892  CD  PRO A 165      43.247  -3.305  24.565  1.00 78.99           C  
ANISOU 1892  CD  PRO A 165     8488  13419   8104    972   -953  -3804       C  
ATOM   1893  N   LEU A 166      41.357  -0.572  22.783  1.00 71.12           N  
ANISOU 1893  N   LEU A 166     7650  10966   8407    455   -832  -3637       N  
ATOM   1894  CA  LEU A 166      40.931   0.631  22.077  1.00 72.48           C  
ANISOU 1894  CA  LEU A 166     7803  10526   9212    215   -820  -3611       C  
ATOM   1895  C   LEU A 166      40.304   0.292  20.731  1.00 68.68           C  
ANISOU 1895  C   LEU A 166     7682   9742   8671    106   -480  -2965       C  
ATOM   1896  O   LEU A 166      39.302   0.899  20.335  1.00 67.93           O  
ANISOU 1896  O   LEU A 166     7768   9292   8751     50   -453  -2915       O  
ATOM   1897  CB  LEU A 166      42.123   1.569  21.884  1.00 76.86           C  
ANISOU 1897  CB  LEU A 166     7948  10763  10490    -41   -924  -3785       C  
ATOM   1898  CG  LEU A 166      41.828   2.926  21.242  1.00 79.53           C  
ANISOU 1898  CG  LEU A 166     8216  10453  11548   -304   -949  -3819       C  
ATOM   1899  CD1 LEU A 166      41.227   3.881  22.264  1.00 81.77           C  
ANISOU 1899  CD1 LEU A 166     8358  10692  12019   -221  -1277  -4442       C  
ATOM   1900  CD2 LEU A 166      43.085   3.515  20.619  1.00 82.15           C  
ANISOU 1900  CD2 LEU A 166     8237  10456  12518   -596   -908  -3738       C  
ATOM   1901  N   VAL A 167      40.882  -0.670  20.011  1.00 68.32           N  
ANISOU 1901  N   VAL A 167     7746   9830   8384     79   -223  -2468       N  
ATOM   1902  CA  VAL A 167      40.378  -1.009  18.682  1.00 62.77           C  
ANISOU 1902  CA  VAL A 167     7375   8836   7640    -33    108  -1836       C  
ATOM   1903  C   VAL A 167      38.955  -1.544  18.773  1.00 58.94           C  
ANISOU 1903  C   VAL A 167     7287   8492   6616    175    184  -1718       C  
ATOM   1904  O   VAL A 167      38.053  -1.086  18.062  1.00 62.92           O  
ANISOU 1904  O   VAL A 167     8009   8603   7293     88    288  -1516       O  
ATOM   1905  CB  VAL A 167      41.316  -2.015  17.992  1.00 61.47           C  
ANISOU 1905  CB  VAL A 167     7235   8846   7275    -79    355  -1358       C  
ATOM   1906  CG1 VAL A 167      40.672  -2.560  16.726  1.00 56.80           C  
ANISOU 1906  CG1 VAL A 167     7032   8046   6503   -136    697   -705       C  
ATOM   1907  CG2 VAL A 167      42.651  -1.357  17.669  1.00 64.77           C  
ANISOU 1907  CG2 VAL A 167     7276   9015   8318   -335    321  -1418       C  
ATOM   1908  N   TRP A 168      38.731  -2.526  19.650  1.00 57.17           N  
ANISOU 1908  N   TRP A 168     7164   8829   5730    453    133  -1847       N  
ATOM   1909  CA  TRP A 168      37.395  -3.097  19.783  1.00 56.87           C  
ANISOU 1909  CA  TRP A 168     7499   8957   5152    655    214  -1746       C  
ATOM   1910  C   TRP A 168      36.374  -2.054  20.219  1.00 58.90           C  
ANISOU 1910  C   TRP A 168     7760   8960   5658    664     20  -2146       C  
ATOM   1911  O   TRP A 168      35.214  -2.110  19.796  1.00 62.23           O  
ANISOU 1911  O   TRP A 168     8492   9232   5921    707    140  -1953       O  
ATOM   1912  CB  TRP A 168      37.414  -4.259  20.775  1.00 53.23           C  
ANISOU 1912  CB  TRP A 168     7113   9151   3962    948    163  -1879       C  
ATOM   1913  CG  TRP A 168      38.016  -5.514  20.221  1.00 50.86           C  
ANISOU 1913  CG  TRP A 168     6948   9117   3260    987    410  -1382       C  
ATOM   1914  CD1 TRP A 168      39.257  -6.015  20.485  1.00 52.48           C  
ANISOU 1914  CD1 TRP A 168     6933   9607   3401    999    375  -1402       C  
ATOM   1915  CD2 TRP A 168      37.401  -6.429  19.305  1.00 46.82           C  
ANISOU 1915  CD2 TRP A 168     6783   8353   2652    903    678   -734       C  
ATOM   1916  NE1 TRP A 168      39.453  -7.186  19.792  1.00 47.71           N  
ANISOU 1916  NE1 TRP A 168     6536   8952   2640    957    609   -806       N  
ATOM   1917  CE2 TRP A 168      38.328  -7.461  19.060  1.00 46.27           C  
ANISOU 1917  CE2 TRP A 168     6672   8279   2629    812    749   -414       C  
ATOM   1918  CE3 TRP A 168      36.157  -6.475  18.668  1.00 55.64           C  
ANISOU 1918  CE3 TRP A 168     8157   9056   3927    760    783   -451       C  
ATOM   1919  CZ2 TRP A 168      38.050  -8.528  18.206  1.00 46.38           C  
ANISOU 1919  CZ2 TRP A 168     6869   7843   2912    548    853     26       C  
ATOM   1920  CZ3 TRP A 168      35.884  -7.535  17.819  1.00 53.69           C  
ANISOU 1920  CZ3 TRP A 168     7985   8470   3947    457    864    -15       C  
ATOM   1921  CH2 TRP A 168      36.826  -8.546  17.596  1.00 47.38           C  
ANISOU 1921  CH2 TRP A 168     7116   7662   3225    387    872    162       C  
ATOM   1922  N   CYS A 169      36.779  -1.098  21.056  1.00 59.29           N  
ANISOU 1922  N   CYS A 169     7469   8959   6101    628   -282  -2709       N  
ATOM   1923  CA  CYS A 169      35.852  -0.049  21.468  1.00 60.95           C  
ANISOU 1923  CA  CYS A 169     7661   8911   6587    628   -479  -3108       C  
ATOM   1924  C   CYS A 169      35.519   0.879  20.307  1.00 61.24           C  
ANISOU 1924  C   CYS A 169     7764   8292   7212    373   -369  -2847       C  
ATOM   1925  O   CYS A 169      34.355   1.248  20.115  1.00 59.98           O  
ANISOU 1925  O   CYS A 169     7820   7910   7060    400   -359  -2850       O  
ATOM   1926  CB  CYS A 169      36.437   0.738  22.639  1.00 65.56           C  
ANISOU 1926  CB  CYS A 169     7850   9603   7458    650   -831  -3773       C  
ATOM   1927  SG  CYS A 169      36.471  -0.185  24.192  1.00 77.81           S  
ANISOU 1927  SG  CYS A 169     9369  11907   8289    992  -1016  -4190       S  
ATOM   1928  N   MET A 170      36.527   1.272  19.524  1.00 68.81           N  
ANISOU 1928  N   MET A 170     8542   8932   8670    123   -286  -2624       N  
ATOM   1929  CA  MET A 170      36.260   2.087  18.343  1.00 68.99           C  
ANISOU 1929  CA  MET A 170     8655   8328   9231   -127   -156  -2324       C  
ATOM   1930  C   MET A 170      35.341   1.355  17.375  1.00 64.27           C  
ANISOU 1930  C   MET A 170     8498   7654   8270    -83    144  -1758       C  
ATOM   1931  O   MET A 170      34.424   1.955  16.803  1.00 63.60           O  
ANISOU 1931  O   MET A 170     8600   7162   8403   -152    182  -1658       O  
ATOM   1932  CB  MET A 170      37.571   2.457  17.651  1.00 71.40           C  
ANISOU 1932  CB  MET A 170     8709   8359  10061   -397    -81  -2136       C  
ATOM   1933  CG  MET A 170      38.436   3.432  18.429  1.00 76.49           C  
ANISOU 1933  CG  MET A 170     8908   8938  11218   -494   -376  -2688       C  
ATOM   1934  SD  MET A 170      39.888   3.967  17.501  1.00 82.08           S  
ANISOU 1934  SD  MET A 170     9334   9252  12601   -843   -263  -2451       S  
ATOM   1935  CE  MET A 170      40.754   2.415  17.289  1.00 76.58           C  
ANISOU 1935  CE  MET A 170     8695   9058  11344   -745    -28  -2039       C  
ATOM   1936  N   ALA A 171      35.571   0.054  17.181  1.00 64.65           N  
ANISOU 1936  N   ALA A 171     8716   8088   7762     36    354  -1387       N  
ATOM   1937  CA  ALA A 171      34.669  -0.737  16.353  1.00 66.74           C  
ANISOU 1937  CA  ALA A 171     9401   8336   7621    108    632   -871       C  
ATOM   1938  C   ALA A 171      33.279  -0.802  16.973  1.00 64.34           C  
ANISOU 1938  C   ALA A 171     9320   8176   6951    325    542  -1110       C  
ATOM   1939  O   ALA A 171      32.269  -0.743  16.262  1.00 65.97           O  
ANISOU 1939  O   ALA A 171     9822   8114   7131    316    680   -844       O  
ATOM   1940  CB  ALA A 171      35.236  -2.143  16.155  1.00 61.47           C  
ANISOU 1940  CB  ALA A 171     8846   8099   6410    210    849   -479       C  
ATOM   1941  N   CYS A 172      33.209  -0.930  18.299  1.00 70.51           N  
ANISOU 1941  N   CYS A 172     9964   9383   7445    524    310  -1617       N  
ATOM   1942  CA  CYS A 172      31.918  -0.932  18.980  1.00 69.38           C  
ANISOU 1942  CA  CYS A 172    10002   9388   6973    726    208  -1900       C  
ATOM   1943  C   CYS A 172      31.176   0.380  18.752  1.00 67.97           C  
ANISOU 1943  C   CYS A 172     9802   8684   7340    601     77  -2118       C  
ATOM   1944  O   CYS A 172      29.992   0.383  18.398  1.00 70.41           O  
ANISOU 1944  O   CYS A 172    10395   8841   7516    660    160  -1995       O  
ATOM   1945  CB  CYS A 172      32.123  -1.187  20.474  1.00 73.67           C  
ANISOU 1945  CB  CYS A 172    10358  10457   7175    937    -38  -2442       C  
ATOM   1946  SG  CYS A 172      30.608  -1.149  21.458  1.00 98.82           S  
ANISOU 1946  SG  CYS A 172    13684  13778  10084   1103   -160  -2713       S  
ATOM   1947  N   LEU A 173      31.858   1.510  18.954  1.00 66.62           N  
ANISOU 1947  N   LEU A 173     9294   8226   7794    430   -134  -2450       N  
ATOM   1948  CA  LEU A 173      31.219   2.803  18.730  1.00 66.25           C  
ANISOU 1948  CA  LEU A 173     9214   7658   8300    301   -272  -2664       C  
ATOM   1949  C   LEU A 173      30.817   2.979  17.271  1.00 64.61           C  
ANISOU 1949  C   LEU A 173     9267   6941   8342    128    -25  -2115       C  
ATOM   1950  O   LEU A 173      29.783   3.590  16.975  1.00 67.57           O  
ANISOU 1950  O   LEU A 173     9805   6982   8888    116    -56  -2153       O  
ATOM   1951  CB  LEU A 173      32.150   3.936  19.163  1.00 68.61           C  
ANISOU 1951  CB  LEU A 173     9093   7742   9235    135   -529  -3089       C  
ATOM   1952  CG  LEU A 173      32.062   4.377  20.626  1.00 71.50           C  
ANISOU 1952  CG  LEU A 173     9209   8396   9564    288   -868  -3793       C  
ATOM   1953  CD1 LEU A 173      32.351   3.228  21.580  1.00 70.20           C  
ANISOU 1953  CD1 LEU A 173     9035   8909   8730    532   -883  -3915       C  
ATOM   1954  CD2 LEU A 173      33.013   5.540  20.877  1.00 76.47           C  
ANISOU 1954  CD2 LEU A 173     9428   8744  10885     93  -1098  -4157       C  
ATOM   1955  N   SER A 174      31.616   2.448  16.344  1.00 69.57           N  
ANISOU 1955  N   SER A 174     9939   7503   8990     -5    219  -1603       N  
ATOM   1956  CA  SER A 174      31.310   2.626  14.929  1.00 69.24           C  
ANISOU 1956  CA  SER A 174    10140   6969   9198   -179    456  -1070       C  
ATOM   1957  C   SER A 174      30.067   1.848  14.521  1.00 68.81           C  
ANISOU 1957  C   SER A 174    10507   7006   8632    -11    646   -754       C  
ATOM   1958  O   SER A 174      29.380   2.238  13.569  1.00 72.09           O  
ANISOU 1958  O   SER A 174    11148   6978   9264   -106    761   -470       O  
ATOM   1959  CB  SER A 174      32.505   2.202  14.077  1.00 66.06           C  
ANISOU 1959  CB  SER A 174     9674   6507   8919   -357    675   -612       C  
ATOM   1960  OG  SER A 174      33.634   3.010  14.354  1.00 56.57           O  
ANISOU 1960  OG  SER A 174     8083   5160   8254   -538    510   -894       O  
ATOM   1961  N   SER A 175      29.760   0.757  15.219  1.00 78.98           N  
ANISOU 1961  N   SER A 175    10537   9009  10462   1108   -857   -892       N  
ATOM   1962  CA  SER A 175      28.602  -0.070  14.911  1.00 78.40           C  
ANISOU 1962  CA  SER A 175    10484   8918  10389   1055   -776   -790       C  
ATOM   1963  C   SER A 175      27.395   0.258  15.779  1.00 78.04           C  
ANISOU 1963  C   SER A 175    10525   8847  10280   1057   -669   -681       C  
ATOM   1964  O   SER A 175      26.371  -0.424  15.676  1.00 77.44           O  
ANISOU 1964  O   SER A 175    10463   8758  10201   1008   -596   -591       O  
ATOM   1965  CB  SER A 175      28.957  -1.553  15.069  1.00 78.01           C  
ANISOU 1965  CB  SER A 175    10519   8804  10317   1089   -843   -800       C  
ATOM   1966  OG  SER A 175      29.365  -1.840  16.394  1.00 80.09           O  
ANISOU 1966  OG  SER A 175    10938   8998  10495   1189   -909   -810       O  
ATOM   1967  N   LEU A 176      27.489   1.283  16.627  1.00 71.56           N  
ANISOU 1967  N   LEU A 176     9765   8016   9408   1107   -649   -688       N  
ATOM   1968  CA  LEU A 176      26.350   1.659  17.462  1.00 68.41           C  
ANISOU 1968  CA  LEU A 176     9455   7583   8953   1117   -522   -587       C  
ATOM   1969  C   LEU A 176      25.134   2.055  16.639  1.00 68.89           C  
ANISOU 1969  C   LEU A 176     9382   7707   9084   1046   -397   -494       C  
ATOM   1970  O   LEU A 176      24.021   1.607  16.967  1.00 71.51           O  
ANISOU 1970  O   LEU A 176     9742   8021   9407   1025   -297   -392       O  
ATOM   1971  CB  LEU A 176      26.762   2.786  18.413  1.00 64.99           C  
ANISOU 1971  CB  LEU A 176     9126   7121   8448   1177   -519   -621       C  
ATOM   1972  CG  LEU A 176      27.364   2.338  19.746  1.00 65.19           C  
ANISOU 1972  CG  LEU A 176     9355   7054   8361   1250   -601   -651       C  
ATOM   1973  CD1 LEU A 176      28.005   3.508  20.470  1.00 65.54           C  
ANISOU 1973  CD1 LEU A 176     9487   7079   8336   1285   -632   -707       C  
ATOM   1974  CD2 LEU A 176      26.296   1.692  20.620  1.00 65.67           C  
ANISOU 1974  CD2 LEU A 176     9566   7035   8351   1261   -492   -549       C  
ATOM   1975  N   PRO A 177      25.253   2.878  15.593  1.00 74.09           N  
ANISOU 1975  N   PRO A 177     9898   8438   9814   1005   -396   -519       N  
ATOM   1976  CA  PRO A 177      24.072   3.172  14.764  1.00 74.02           C  
ANISOU 1976  CA  PRO A 177     9760   8490   9874    942   -300   -421       C  
ATOM   1977  C   PRO A 177      23.347   1.925  14.288  1.00 71.14           C  
ANISOU 1977  C   PRO A 177     9352   8135   9542    865   -296   -353       C  
ATOM   1978  O   PRO A 177      22.113   1.917  14.223  1.00 66.60           O  
ANISOU 1978  O   PRO A 177     8718   7590   8999    827   -200   -241       O  
ATOM   1979  CB  PRO A 177      24.664   3.972  13.595  1.00 76.73           C  
ANISOU 1979  CB  PRO A 177     9986   8892  10274    904   -346   -489       C  
ATOM   1980  CG  PRO A 177      25.871   4.621  14.165  1.00 71.40           C  
ANISOU 1980  CG  PRO A 177     9389   8189   9551    962   -406   -600       C  
ATOM   1981  CD  PRO A 177      26.437   3.640  15.157  1.00 76.74           C  
ANISOU 1981  CD  PRO A 177    10190   8802  10167   1013   -478   -634       C  
ATOM   1982  N   THR A 178      24.085   0.866  13.950  1.00 69.60           N  
ANISOU 1982  N   THR A 178     9186   7915   9342    840   -394   -417       N  
ATOM   1983  CA  THR A 178      23.439  -0.372  13.531  1.00 66.54           C  
ANISOU 1983  CA  THR A 178     8794   7522   8968    757   -388   -358       C  
ATOM   1984  C   THR A 178      22.605  -0.966  14.659  1.00 65.36           C  
ANISOU 1984  C   THR A 178     8758   7318   8759    773   -308   -275       C  
ATOM   1985  O   THR A 178      21.486  -1.436  14.430  1.00 65.38           O  
ANISOU 1985  O   THR A 178     8712   7345   8786    689   -237   -178       O  
ATOM   1986  CB  THR A 178      24.487  -1.378  13.053  1.00 67.32           C  
ANISOU 1986  CB  THR A 178     8936   7583   9060    747   -496   -449       C  
ATOM   1987  OG1 THR A 178      25.306  -0.774  12.044  1.00 68.20           O  
ANISOU 1987  OG1 THR A 178     8946   7738   9227    731   -552   -534       O  
ATOM   1988  CG2 THR A 178      23.816  -2.618  12.476  1.00 67.91           C  
ANISOU 1988  CG2 THR A 178     9021   7645   9137    642   -485   -390       C  
ATOM   1989  N   PHE A 179      23.124  -0.944  15.889  1.00 71.93           N  
ANISOU 1989  N   PHE A 179     9746   8075   9509    871   -317   -312       N  
ATOM   1990  CA  PHE A 179      22.384  -1.543  16.994  1.00 71.54           C  
ANISOU 1990  CA  PHE A 179     9838   7955   9387    883   -232   -240       C  
ATOM   1991  C   PHE A 179      21.136  -0.745  17.345  1.00 71.21           C  
ANISOU 1991  C   PHE A 179     9738   7946   9372    873    -73   -135       C  
ATOM   1992  O   PHE A 179      20.136  -1.327  17.781  1.00 71.24           O  
ANISOU 1992  O   PHE A 179     9777   7927   9362    828     31    -48       O  
ATOM   1993  CB  PHE A 179      23.280  -1.670  18.226  1.00 71.46           C  
ANISOU 1993  CB  PHE A 179    10033   7847   9271    990   -292   -305       C  
ATOM   1994  CG  PHE A 179      22.698  -2.534  19.312  1.00 71.75           C  
ANISOU 1994  CG  PHE A 179    10261   7786   9215    997   -224   -247       C  
ATOM   1995  CD1 PHE A 179      21.827  -1.998  20.248  1.00 72.58           C  
ANISOU 1995  CD1 PHE A 179    10441   7857   9278   1014    -78   -175       C  
ATOM   1996  CD2 PHE A 179      23.014  -3.881  19.393  1.00 72.53           C  
ANISOU 1996  CD2 PHE A 179    10480   7816   9263    986   -291   -266       C  
ATOM   1997  CE1 PHE A 179      21.287  -2.786  21.248  1.00 72.48           C  
ANISOU 1997  CE1 PHE A 179    10620   7745   9174   1011      1   -125       C  
ATOM   1998  CE2 PHE A 179      22.476  -4.675  20.392  1.00 72.19           C  
ANISOU 1998  CE2 PHE A 179    10636   7671   9121    985   -222   -215       C  
ATOM   1999  CZ  PHE A 179      21.612  -4.126  21.320  1.00 72.87           C  
ANISOU 1999  CZ  PHE A 179    10795   7725   9165    991    -74   -146       C  
ATOM   2000  N   TYR A 180      21.167   0.576  17.167  1.00 64.86           N  
ANISOU 2000  N   TYR A 180     8848   7191   8606    915    -43   -141       N  
ATOM   2001  CA  TYR A 180      19.999   1.380  17.510  1.00 64.69           C  
ANISOU 2001  CA  TYR A 180     8770   7194   8614    929    119    -38       C  
ATOM   2002  C   TYR A 180      18.883   1.202  16.486  1.00 64.64           C  
ANISOU 2002  C   TYR A 180     8558   7284   8717    831    166     59       C  
ATOM   2003  O   TYR A 180      17.701   1.194  16.848  1.00 65.65           O  
ANISOU 2003  O   TYR A 180     8639   7428   8877    813    302    166       O  
ATOM   2004  CB  TYR A 180      20.393   2.852  17.634  1.00 65.40           C  
ANISOU 2004  CB  TYR A 180     8855   7293   8699   1009    140    -73       C  
ATOM   2005  CG  TYR A 180      19.349   3.697  18.331  1.00 67.68           C  
ANISOU 2005  CG  TYR A 180     9155   7570   8992   1063    323     23       C  
ATOM   2006  CD1 TYR A 180      19.133   3.580  19.698  1.00 74.19           C  
ANISOU 2006  CD1 TYR A 180    10174   8292   9722   1117    424     44       C  
ATOM   2007  CD2 TYR A 180      18.580   4.613  17.622  1.00 71.73           C  
ANISOU 2007  CD2 TYR A 180     9494   8161   9598   1066    401     94       C  
ATOM   2008  CE1 TYR A 180      18.178   4.350  20.341  1.00 86.01           C  
ANISOU 2008  CE1 TYR A 180    11690   9767  11224   1172    616    131       C  
ATOM   2009  CE2 TYR A 180      17.623   5.388  18.257  1.00 71.77           C  
ANISOU 2009  CE2 TYR A 180     9503   8152   9616   1133    583    185       C  
ATOM   2010  CZ  TYR A 180      17.427   5.252  19.615  1.00 78.11           C  
ANISOU 2010  CZ  TYR A 180    10497   8850  10329   1185    699    202       C  
ATOM   2011  OH  TYR A 180      16.476   6.021  20.248  1.00 83.51           O  
ANISOU 2011  OH  TYR A 180    11194   9509  11028   1256    902    291       O  
ATOM   2012  N   PHE A 181      19.236   1.047  15.208  1.00 62.22           N  
ANISOU 2012  N   PHE A 181     8129   7043   8469    760     55     25       N  
ATOM   2013  CA  PHE A 181      18.259   1.051  14.127  1.00 53.43           C  
ANISOU 2013  CA  PHE A 181     6820   6026   7454    663     71    114       C  
ATOM   2014  C   PHE A 181      18.038  -0.306  13.477  1.00 57.14           C  
ANISOU 2014  C   PHE A 181     7272   6507   7933    530      7    130       C  
ATOM   2015  O   PHE A 181      16.917  -0.588  13.051  1.00 64.41           O  
ANISOU 2015  O   PHE A 181     8068   7491   8915    435     52    233       O  
ATOM   2016  CB  PHE A 181      18.676   2.043  13.033  1.00 52.26           C  
ANISOU 2016  CB  PHE A 181     6556   5941   7361    666      3     76       C  
ATOM   2017  CG  PHE A 181      18.735   3.469  13.496  1.00 56.95           C  
ANISOU 2017  CG  PHE A 181     7159   6532   7950    780     77     74       C  
ATOM   2018  CD1 PHE A 181      17.593   4.113  13.942  1.00 58.89           C  
ANISOU 2018  CD1 PHE A 181     7338   6802   8236    827    218    187       C  
ATOM   2019  CD2 PHE A 181      19.927   4.172  13.470  1.00 65.79           C  
ANISOU 2019  CD2 PHE A 181     8350   7620   9025    835     12    -40       C  
ATOM   2020  CE1 PHE A 181      17.641   5.428  14.364  1.00 64.23           C  
ANISOU 2020  CE1 PHE A 181     8046   7459   8898    936    299    187       C  
ATOM   2021  CE2 PHE A 181      19.981   5.489  13.890  1.00 63.99           C  
ANISOU 2021  CE2 PHE A 181     8154   7379   8779    926     84    -44       C  
ATOM   2022  CZ  PHE A 181      18.836   6.117  14.338  1.00 61.04           C  
ANISOU 2022  CZ  PHE A 181     7739   7017   8435    981    230     71       C  
ATOM   2023  N   ARG A 182      19.068  -1.146  13.373  1.00 57.51           N  
ANISOU 2023  N   ARG A 182     7438   6491   7920    519    -95     34       N  
ATOM   2024  CA  ARG A 182      18.916  -2.439  12.713  1.00 60.16           C  
ANISOU 2024  CA  ARG A 182     7787   6821   8251    392   -149     44       C  
ATOM   2025  C   ARG A 182      17.782  -3.221  13.365  1.00 61.17           C  
ANISOU 2025  C   ARG A 182     7946   6934   8362    325    -48    144       C  
ATOM   2026  O   ARG A 182      17.885  -3.625  14.528  1.00 59.78           O  
ANISOU 2026  O   ARG A 182     7931   6673   8111    385      7    134       O  
ATOM   2027  CB  ARG A 182      20.222  -3.237  12.766  1.00 62.66           C  
ANISOU 2027  CB  ARG A 182     8258   7051   8499    428   -249    -73       C  
ATOM   2028  CG  ARG A 182      20.191  -4.566  12.014  1.00 56.90           C  
ANISOU 2028  CG  ARG A 182     7573   6296   7752    305   -300    -74       C  
ATOM   2029  CD  ARG A 182      20.100  -4.386  10.505  1.00 59.50           C  
ANISOU 2029  CD  ARG A 182     7767   6695   8147    194   -357    -71       C  
ATOM   2030  NE  ARG A 182      21.281  -3.742   9.939  1.00 55.76           N  
ANISOU 2030  NE  ARG A 182     7271   6222   7692    261   -430   -180       N  
ATOM   2031  CZ  ARG A 182      21.482  -3.564   8.636  1.00 61.26           C  
ANISOU 2031  CZ  ARG A 182     7891   6955   8430    179   -482   -205       C  
ATOM   2032  NH1 ARG A 182      22.587  -2.966   8.211  1.00 71.81           N  
ANISOU 2032  NH1 ARG A 182     9216   8286   9784    239   -529   -310       N  
ATOM   2033  NH2 ARG A 182      20.582  -3.985   7.755  1.00 57.30           N  
ANISOU 2033  NH2 ARG A 182     7331   6492   7947     26   -488   -126       N  
ATOM   2034  N   ASP A 183      16.697  -3.434  12.625  1.00 83.15           N  
ANISOU 2034  N   ASP A 183    10581   9798  11214    192    -26    240       N  
ATOM   2035  CA  ASP A 183      15.547  -4.155  13.150  1.00 83.06           C  
ANISOU 2035  CA  ASP A 183    10568   9790  11202    103     78    339       C  
ATOM   2036  C   ASP A 183      14.698  -4.634  11.981  1.00 83.27           C  
ANISOU 2036  C   ASP A 183    10440   9905  11294    -80     34    415       C  
ATOM   2037  O   ASP A 183      14.778  -4.101  10.871  1.00 83.28           O  
ANISOU 2037  O   ASP A 183    10310   9978  11353   -115    -53    415       O  
ATOM   2038  CB  ASP A 183      14.718  -3.277  14.095  1.00 82.94           C  
ANISOU 2038  CB  ASP A 183    10486   9800  11229    188    230    417       C  
ATOM   2039  CG  ASP A 183      13.835  -4.088  15.028  1.00 84.56           C  
ANISOU 2039  CG  ASP A 183    10764   9963  11401    129    363    486       C  
ATOM   2040  OD1 ASP A 183      14.140  -5.278  15.263  1.00 85.36           O  
ANISOU 2040  OD1 ASP A 183    11039   9980  11413     64    335    448       O  
ATOM   2041  OD2 ASP A 183      12.828  -3.535  15.523  1.00 84.55           O  
ANISOU 2041  OD2 ASP A 183    10652  10008  11466    148    506    578       O  
ATOM   2042  N   VAL A 184      13.883  -5.647  12.251  1.00 77.43           N  
ANISOU 2042  N   VAL A 184     9731   9155  10534   -207     92    479       N  
ATOM   2043  CA  VAL A 184      13.043  -6.253  11.223  1.00 74.56           C  
ANISOU 2043  CA  VAL A 184     9243   8870  10216   -409     44    554       C  
ATOM   2044  C   VAL A 184      11.841  -5.359  10.951  1.00 67.72           C  
ANISOU 2044  C   VAL A 184     8103   8144   9483   -434     94    676       C  
ATOM   2045  O   VAL A 184      11.172  -4.890  11.880  1.00 59.85           O  
ANISOU 2045  O   VAL A 184     7043   7165   8530   -359    234    738       O  
ATOM   2046  CB  VAL A 184      12.597  -7.662  11.644  1.00 71.31           C  
ANISOU 2046  CB  VAL A 184     8972   8394   9729   -550     95    578       C  
ATOM   2047  CG1 VAL A 184      11.540  -8.190  10.687  1.00 69.57           C  
ANISOU 2047  CG1 VAL A 184     8601   8270   9563   -779     58    672       C  
ATOM   2048  CG2 VAL A 184      13.790  -8.602  11.689  1.00 75.46           C  
ANISOU 2048  CG2 VAL A 184     9763   8781  10127   -527     25    464       C  
ATOM   2049  N   ARG A 185      11.563  -5.124   9.672  1.00 64.26           N  
ANISOU 2049  N   ARG A 185     7509   7799   9109   -534    -20    714       N  
ATOM   2050  CA  ARG A 185      10.399  -4.360   9.254  1.00 60.04           C  
ANISOU 2050  CA  ARG A 185     6701   7406   8707   -566     -4    839       C  
ATOM   2051  C   ARG A 185       9.749  -5.087   8.086  1.00 67.50           C  
ANISOU 2051  C   ARG A 185     7548   8425   9674   -799   -121    903       C  
ATOM   2052  O   ARG A 185      10.427  -5.697   7.255  1.00 71.25           O  
ANISOU 2052  O   ARG A 185     8150   8848  10072   -895   -241    835       O  
ATOM   2053  CB  ARG A 185      10.769  -2.925   8.859  1.00 59.12           C  
ANISOU 2053  CB  ARG A 185     6485   7332   8648   -411    -41    825       C  
ATOM   2054  CG  ARG A 185      11.221  -2.060  10.029  1.00 63.71           C  
ANISOU 2054  CG  ARG A 185     7141   7852   9214   -195     83    782       C  
ATOM   2055  CD  ARG A 185      10.069  -1.721  10.960  1.00 60.05           C  
ANISOU 2055  CD  ARG A 185     6550   7435   8829   -145    256    893       C  
ATOM   2056  NE  ARG A 185      10.496  -0.903  12.095  1.00 59.63           N  
ANISOU 2056  NE  ARG A 185     6605   7308   8745     53    383    851       N  
ATOM   2057  CZ  ARG A 185      10.938  -1.389  13.252  1.00 59.54           C  
ANISOU 2057  CZ  ARG A 185     6807   7182   8636    103    472    792       C  
ATOM   2058  NH1 ARG A 185      11.019  -2.699  13.447  1.00 62.02           N  
ANISOU 2058  NH1 ARG A 185     7251   7439   8876    -18    455    767       N  
ATOM   2059  NH2 ARG A 185      11.299  -0.560  14.221  1.00 60.97           N  
ANISOU 2059  NH2 ARG A 185     7088   7295   8782    273    576    760       N  
ATOM   2060  N   THR A 186       8.424  -5.016   8.035  1.00 67.91           N  
ANISOU 2060  N   THR A 186     7373   8597   9833   -891    -83   1036       N  
ATOM   2061  CA  THR A 186       7.660  -5.712   7.009  1.00 71.41           C  
ANISOU 2061  CA  THR A 186     7707   9124  10302  -1134   -198   1112       C  
ATOM   2062  C   THR A 186       7.600  -4.872   5.740  1.00 78.81           C  
ANISOU 2062  C   THR A 186     8492  10150  11302  -1142   -354   1148       C  
ATOM   2063  O   THR A 186       7.137  -3.726   5.767  1.00 77.21           O  
ANISOU 2063  O   THR A 186     8091  10035  11211  -1012   -331   1217       O  
ATOM   2064  CB  THR A 186       6.254  -6.025   7.513  1.00 72.04           C  
ANISOU 2064  CB  THR A 186     7591   9304  10479  -1241    -94   1242       C  
ATOM   2065  OG1 THR A 186       6.342  -6.789   8.723  1.00 75.63           O  
ANISOU 2065  OG1 THR A 186     8220   9657  10858  -1233     64   1202       O  
ATOM   2066  CG2 THR A 186       5.478  -6.817   6.472  1.00 79.44           C  
ANISOU 2066  CG2 THR A 186     8424  10329  11432  -1519   -227   1319       C  
ATOM   2067  N   ILE A 187       8.080  -5.436   4.635  1.00 87.02           N  
ANISOU 2067  N   ILE A 187     9646  11156  12263  -1289   -507   1102       N  
ATOM   2068  CA  ILE A 187       7.938  -4.820   3.322  1.00 89.35           C  
ANISOU 2068  CA  ILE A 187     9825  11525  12598  -1346   -671   1142       C  
ATOM   2069  C   ILE A 187       6.652  -5.375   2.719  1.00 90.27           C  
ANISOU 2069  C   ILE A 187     9760  11763  12774  -1583   -757   1276       C  
ATOM   2070  O   ILE A 187       6.584  -6.552   2.357  1.00 89.51           O  
ANISOU 2070  O   ILE A 187     9786  11630  12594  -1800   -810   1265       O  
ATOM   2071  CB  ILE A 187       9.145  -5.112   2.424  1.00 89.82           C  
ANISOU 2071  CB  ILE A 187    10119  11473  12535  -1387   -780   1019       C  
ATOM   2072  CG1 ILE A 187      10.450  -4.723   3.126  1.00 81.19           C  
ANISOU 2072  CG1 ILE A 187     9200  10263  11386  -1169   -692    881       C  
ATOM   2073  CG2 ILE A 187       9.012  -4.377   1.096  1.00 92.65           C  
ANISOU 2073  CG2 ILE A 187    10383  11895  12925  -1436   -939   1058       C  
ATOM   2074  CD1 ILE A 187      10.558  -3.252   3.472  1.00 90.27           C  
ANISOU 2074  CD1 ILE A 187    10228  11455  12615   -948   -643    887       C  
ATOM   2075  N   GLU A 188       5.631  -4.524   2.608  1.00 99.70           N  
ANISOU 2075  N   GLU A 188    10663  13103  14114  -1542   -773   1406       N  
ATOM   2076  CA  GLU A 188       4.300  -5.009   2.253  1.00100.02           C  
ANISOU 2076  CA  GLU A 188    10481  13282  14241  -1753   -837   1546       C  
ATOM   2077  C   GLU A 188       4.234  -5.433   0.791  1.00 99.12           C  
ANISOU 2077  C   GLU A 188    10404  13191  14068  -1983  -1065   1567       C  
ATOM   2078  O   GLU A 188       3.763  -6.532   0.474  1.00100.37           O  
ANISOU 2078  O   GLU A 188    10595  13363  14178  -2239  -1125   1599       O  
ATOM   2079  CB  GLU A 188       3.253  -3.939   2.558  1.00107.34           C  
ANISOU 2079  CB  GLU A 188    11069  14360  15354  -1619   -788   1682       C  
ATOM   2080  CG  GLU A 188       2.802  -3.924   4.014  1.00110.74           C  
ANISOU 2080  CG  GLU A 188    11422  14797  15858  -1500   -548   1707       C  
ATOM   2081  CD  GLU A 188       2.177  -5.243   4.446  1.00116.40           C  
ANISOU 2081  CD  GLU A 188    12150  15524  16553  -1727   -485   1734       C  
ATOM   2082  OE1 GLU A 188       1.723  -6.004   3.564  1.00122.28           O  
ANISOU 2082  OE1 GLU A 188    12859  16325  17276  -1985   -638   1781       O  
ATOM   2083  OE2 GLU A 188       2.147  -5.523   5.664  1.00116.64           O  
ANISOU 2083  OE2 GLU A 188    12246  15497  16576  -1658   -281   1708       O  
ATOM   2084  N   TYR A 189       4.692  -4.571  -0.119  1.00 94.37           N  
ANISOU 2084  N   TYR A 189     9814  12584  13457  -1907  -1192   1550       N  
ATOM   2085  CA  TYR A 189       4.581  -4.881  -1.539  1.00 93.27           C  
ANISOU 2085  CA  TYR A 189     9719  12461  13257  -2125  -1412   1578       C  
ATOM   2086  C   TYR A 189       5.384  -6.120  -1.912  1.00 91.98           C  
ANISOU 2086  C   TYR A 189     9880  12152  12918  -2306  -1437   1464       C  
ATOM   2087  O   TYR A 189       5.060  -6.778  -2.907  1.00 89.19           O  
ANISOU 2087  O   TYR A 189     9581  11809  12500  -2558  -1593   1501       O  
ATOM   2088  CB  TYR A 189       5.020  -3.675  -2.373  1.00 90.64           C  
ANISOU 2088  CB  TYR A 189     9381  12126  12934  -1989  -1520   1567       C  
ATOM   2089  CG  TYR A 189       6.507  -3.405  -2.370  1.00 92.40           C  
ANISOU 2089  CG  TYR A 189     9879  12187  13043  -1846  -1460   1400       C  
ATOM   2090  CD1 TYR A 189       7.349  -4.024  -3.286  1.00 95.97           C  
ANISOU 2090  CD1 TYR A 189    10596  12520  13349  -1988  -1550   1301       C  
ATOM   2091  CD2 TYR A 189       7.068  -2.520  -1.459  1.00 91.55           C  
ANISOU 2091  CD2 TYR A 189     9765  12044  12975  -1574  -1308   1340       C  
ATOM   2092  CE1 TYR A 189       8.708  -3.774  -3.290  1.00 93.61           C  
ANISOU 2092  CE1 TYR A 189    10521  12082  12964  -1857  -1487   1149       C  
ATOM   2093  CE2 TYR A 189       8.427  -2.265  -1.455  1.00 93.85           C  
ANISOU 2093  CE2 TYR A 189    10287  12200  13172  -1455  -1261   1188       C  
ATOM   2094  CZ  TYR A 189       9.242  -2.895  -2.373  1.00 95.38           C  
ANISOU 2094  CZ  TYR A 189    10714  12288  13238  -1594  -1350   1093       C  
ATOM   2095  OH  TYR A 189      10.595  -2.646  -2.376  1.00 99.83           O  
ANISOU 2095  OH  TYR A 189    11482  12726  13724  -1477  -1296    942       O  
ATOM   2096  N   LEU A 190       6.412  -6.458  -1.134  1.00 94.10           N  
ANISOU 2096  N   LEU A 190    10368  12281  13104  -2183  -1291   1331       N  
ATOM   2097  CA  LEU A 190       7.149  -7.699  -1.328  1.00 96.32           C  
ANISOU 2097  CA  LEU A 190    10953  12418  13227  -2328  -1286   1228       C  
ATOM   2098  C   LEU A 190       6.632  -8.834  -0.455  1.00 94.46           C  
ANISOU 2098  C   LEU A 190    10751  12172  12969  -2448  -1178   1251       C  
ATOM   2099  O   LEU A 190       6.929 -10.000  -0.739  1.00 91.40           O  
ANISOU 2099  O   LEU A 190    10597  11682  12450  -2626  -1194   1200       O  
ATOM   2100  CB  LEU A 190       8.636  -7.481  -1.041  1.00 97.22           C  
ANISOU 2100  CB  LEU A 190    11298  12380  13262  -2127  -1202   1068       C  
ATOM   2101  CG  LEU A 190       9.486  -7.086  -2.249  1.00105.20           C  
ANISOU 2101  CG  LEU A 190    12447  13321  14203  -2135  -1317    994       C  
ATOM   2102  CD1 LEU A 190      10.800  -6.465  -1.801  1.00105.23           C  
ANISOU 2102  CD1 LEU A 190    12569  13226  14187  -1887  -1221    857       C  
ATOM   2103  CD2 LEU A 190       9.741  -8.292  -3.141  1.00109.54           C  
ANISOU 2103  CD2 LEU A 190    13238  13769  14611  -2381  -1395    954       C  
ATOM   2104  N   GLY A 191       5.876  -8.523   0.596  1.00 94.16           N  
ANISOU 2104  N   GLY A 191    10504  12226  13048  -2355  -1056   1324       N  
ATOM   2105  CA  GLY A 191       5.314  -9.557   1.442  1.00 86.46           C  
ANISOU 2105  CA  GLY A 191     9557  11241  12052  -2477   -940   1350       C  
ATOM   2106  C   GLY A 191       6.332 -10.296   2.279  1.00 81.69           C  
ANISOU 2106  C   GLY A 191     9259  10460  11319  -2390   -807   1218       C  
ATOM   2107  O   GLY A 191       6.108 -11.460   2.624  1.00 82.57           O  
ANISOU 2107  O   GLY A 191     9512  10513  11349  -2552   -751   1213       O  
ATOM   2108  N   VAL A 192       7.445  -9.648   2.625  1.00 86.81           N  
ANISOU 2108  N   VAL A 192    10016  11021  11945  -2140   -758   1114       N  
ATOM   2109  CA  VAL A 192       8.518 -10.288   3.371  1.00 77.52           C  
ANISOU 2109  CA  VAL A 192     9125   9678  10651  -2035   -658    987       C  
ATOM   2110  C   VAL A 192       8.928  -9.408   4.543  1.00 70.18           C  
ANISOU 2110  C   VAL A 192     8153   8735   9777  -1753   -528    950       C  
ATOM   2111  O   VAL A 192       8.699  -8.197   4.562  1.00 72.42           O  
ANISOU 2111  O   VAL A 192     8233   9111  10171  -1614   -528    992       O  
ATOM   2112  CB  VAL A 192       9.748 -10.591   2.487  1.00 73.91           C  
ANISOU 2112  CB  VAL A 192     8910   9094  10077  -2038   -749    869       C  
ATOM   2113  CG1 VAL A 192       9.406 -11.644   1.446  1.00 75.44           C  
ANISOU 2113  CG1 VAL A 192     9219   9262  10181  -2329   -853    895       C  
ATOM   2114  CG2 VAL A 192      10.264  -9.317   1.828  1.00 75.43           C  
ANISOU 2114  CG2 VAL A 192     9000   9328  10332  -1893   -827    842       C  
ATOM   2115  N   ASN A 193       9.548 -10.050   5.528  1.00 67.03           N  
ANISOU 2115  N   ASN A 193     7970   8209   9289  -1671   -419    871       N  
ATOM   2116  CA  ASN A 193      10.077  -9.394   6.717  1.00 67.30           C  
ANISOU 2116  CA  ASN A 193     8034   8199   9340  -1418   -301    820       C  
ATOM   2117  C   ASN A 193      11.572  -9.191   6.504  1.00 60.37           C  
ANISOU 2117  C   ASN A 193     7338   7211   8390  -1265   -356    684       C  
ATOM   2118  O   ASN A 193      12.346 -10.151   6.562  1.00 60.03           O  
ANISOU 2118  O   ASN A 193     7537   7041   8233  -1285   -363    600       O  
ATOM   2119  CB  ASN A 193       9.808 -10.266   7.940  1.00 63.92           C  
ANISOU 2119  CB  ASN A 193     7744   7694   8850  -1433   -159    823       C  
ATOM   2120  CG  ASN A 193       8.332 -10.554   8.135  1.00 72.25           C  
ANISOU 2120  CG  ASN A 193     8616   8857   9978  -1608    -90    953       C  
ATOM   2121  OD1 ASN A 193       7.475  -9.937   7.500  1.00 77.51           O  
ANISOU 2121  OD1 ASN A 193     9013   9671  10766  -1677   -144   1050       O  
ATOM   2122  ND2 ASN A 193       8.031 -11.547   8.964  1.00 78.68           N  
ANISOU 2122  ND2 ASN A 193     9580   9595  10718  -1691     23    955       N  
ATOM   2123  N   ALA A 194      11.982  -7.949   6.260  1.00 59.33           N  
ANISOU 2123  N   ALA A 194     7091   7127   8325  -1112   -389    662       N  
ATOM   2124  CA  ALA A 194      13.368  -7.660   5.926  1.00 57.75           C  
ANISOU 2124  CA  ALA A 194     7026   6842   8075   -988   -446    534       C  
ATOM   2125  C   ALA A 194      14.134  -7.154   7.141  1.00 61.53           C  
ANISOU 2125  C   ALA A 194     7580   7259   8540   -757   -359    462       C  
ATOM   2126  O   ALA A 194      13.572  -6.521   8.039  1.00 57.23           O  
ANISOU 2126  O   ALA A 194     6935   6759   8049   -662   -264    517       O  
ATOM   2127  CB  ALA A 194      13.446  -6.624   4.800  1.00 57.20           C  
ANISOU 2127  CB  ALA A 194     6815   6850   8070   -984   -544    542       C  
ATOM   2128  N   CYS A 195      15.434  -7.448   7.155  1.00 58.69           N  
ANISOU 2128  N   CYS A 195     7402   6792   8107   -669   -392    338       N  
ATOM   2129  CA  CYS A 195      16.360  -6.978   8.185  1.00 57.11           C  
ANISOU 2129  CA  CYS A 195     7286   6528   7884   -457   -347    254       C  
ATOM   2130  C   CYS A 195      17.051  -5.727   7.649  1.00 53.89           C  
ANISOU 2130  C   CYS A 195     6784   6162   7530   -350   -398    198       C  
ATOM   2131  O   CYS A 195      18.045  -5.818   6.925  1.00 54.38           O  
ANISOU 2131  O   CYS A 195     6914   6178   7567   -344   -469    104       O  
ATOM   2132  CB  CYS A 195      17.351  -8.081   8.542  1.00 62.06           C  
ANISOU 2132  CB  CYS A 195     8153   7020   8407   -422   -361    159       C  
ATOM   2133  SG  CYS A 195      18.597  -7.637   9.766  1.00 54.08           S  
ANISOU 2133  SG  CYS A 195     7259   5928   7360   -174   -344     53       S  
ATOM   2134  N   ILE A 196      16.519  -4.554   8.001  1.00 55.32           N  
ANISOU 2134  N   ILE A 196     6815   6421   7782   -268   -349    254       N  
ATOM   2135  CA  ILE A 196      16.955  -3.290   7.424  1.00 54.46           C  
ANISOU 2135  CA  ILE A 196     6611   6359   7724   -190   -388    220       C  
ATOM   2136  C   ILE A 196      17.272  -2.299   8.539  1.00 53.10           C  
ANISOU 2136  C   ILE A 196     6443   6174   7557     -4   -311    194       C  
ATOM   2137  O   ILE A 196      17.065  -2.568   9.722  1.00 56.86           O  
ANISOU 2137  O   ILE A 196     6990   6611   8002     59   -228    212       O  
ATOM   2138  CB  ILE A 196      15.897  -2.700   6.466  1.00 61.03           C  
ANISOU 2138  CB  ILE A 196     7250   7303   8636   -288   -421    329       C  
ATOM   2139  CG1 ILE A 196      14.558  -2.509   7.188  1.00 54.80           C  
ANISOU 2139  CG1 ILE A 196     6323   6588   7911   -287   -327    461       C  
ATOM   2140  CG2 ILE A 196      15.714  -3.603   5.255  1.00 63.41           C  
ANISOU 2140  CG2 ILE A 196     7572   7607   8915   -485   -519    343       C  
ATOM   2141  CD1 ILE A 196      14.241  -1.070   7.523  1.00 55.72           C  
ANISOU 2141  CD1 ILE A 196     6311   6762   8097   -142   -265    505       C  
ATOM   2142  N   MET A 197      17.795  -1.141   8.136  1.00 51.90           N  
ANISOU 2142  N   MET A 197     6238   6048   7434     75   -337    148       N  
ATOM   2143  CA  MET A 197      18.073  -0.038   9.051  1.00 51.61           C  
ANISOU 2143  CA  MET A 197     6209   6002   7398    235   -267    126       C  
ATOM   2144  C   MET A 197      16.798   0.780   9.222  1.00 52.42           C  
ANISOU 2144  C   MET A 197     6160   6183   7572    257   -182    256       C  
ATOM   2145  O   MET A 197      16.402   1.523   8.318  1.00 52.44           O  
ANISOU 2145  O   MET A 197     6036   6255   7634    233   -215    302       O  
ATOM   2146  CB  MET A 197      19.213   0.830   8.526  1.00 55.94           C  
ANISOU 2146  CB  MET A 197     6778   6536   7939    296   -325     15       C  
ATOM   2147  CG  MET A 197      20.569   0.136   8.492  1.00 57.90           C  
ANISOU 2147  CG  MET A 197     7158   6710   8133    306   -394   -119       C  
ATOM   2148  SD  MET A 197      21.288  -0.086  10.131  1.00 56.00           S  
ANISOU 2148  SD  MET A 197     7068   6386   7822    446   -360   -182       S  
ATOM   2149  CE  MET A 197      21.757   1.596  10.532  1.00 58.01           C  
ANISOU 2149  CE  MET A 197     7301   6658   8081    567   -327   -226       C  
ATOM   2150  N   ALA A 198      16.154   0.642  10.382  1.00 54.18           N  
ANISOU 2150  N   ALA A 198     6403   6391   7791    309    -67    317       N  
ATOM   2151  CA  ALA A 198      14.865   1.284  10.639  1.00 54.28           C  
ANISOU 2151  CA  ALA A 198     6263   6477   7885    335     39    449       C  
ATOM   2152  C   ALA A 198      15.104   2.709  11.129  1.00 54.01           C  
ANISOU 2152  C   ALA A 198     6237   6429   7854    497    113    434       C  
ATOM   2153  O   ALA A 198      14.997   3.024  12.317  1.00 54.41           O  
ANISOU 2153  O   ALA A 198     6370   6430   7875    600    235    442       O  
ATOM   2154  CB  ALA A 198      14.057   0.470  11.642  1.00 56.85           C  
ANISOU 2154  CB  ALA A 198     6614   6782   8203    307    153    518       C  
ATOM   2155  N   PHE A 199      15.430   3.590  10.185  1.00 54.55           N  
ANISOU 2155  N   PHE A 199     6243   6534   7949    512     42    410       N  
ATOM   2156  CA  PHE A 199      15.630   4.989  10.519  1.00 54.70           C  
ANISOU 2156  CA  PHE A 199     6280   6538   7966    653    110    398       C  
ATOM   2157  C   PHE A 199      14.285   5.659  10.789  1.00 58.30           C  
ANISOU 2157  C   PHE A 199     6590   7053   8508    718    236    543       C  
ATOM   2158  O   PHE A 199      13.241   5.176  10.344  1.00 63.84           O  
ANISOU 2158  O   PHE A 199     7128   7835   9292    636    229    653       O  
ATOM   2159  CB  PHE A 199      16.341   5.723   9.385  1.00 53.86           C  
ANISOU 2159  CB  PHE A 199     6162   6446   7857    640      6    331       C  
ATOM   2160  CG  PHE A 199      17.709   5.192   9.073  1.00 54.12           C  
ANISOU 2160  CG  PHE A 199     6319   6424   7821    589    -99    184       C  
ATOM   2161  CD1 PHE A 199      18.718   5.238  10.018  1.00 50.68           C  
ANISOU 2161  CD1 PHE A 199     6036   5911   7310    665    -80     78       C  
ATOM   2162  CD2 PHE A 199      17.992   4.666   7.824  1.00 55.64           C  
ANISOU 2162  CD2 PHE A 199     6477   6640   8025    466   -217    152       C  
ATOM   2163  CE1 PHE A 199      19.977   4.755   9.728  1.00 49.85           C  
ANISOU 2163  CE1 PHE A 199     6016   5764   7159    630   -177    -52       C  
ATOM   2164  CE2 PHE A 199      19.251   4.184   7.530  1.00 52.23           C  
ANISOU 2164  CE2 PHE A 199     6149   6153   7541    430   -294     18       C  
ATOM   2165  CZ  PHE A 199      20.244   4.229   8.483  1.00 49.46           C  
ANISOU 2165  CZ  PHE A 199     5921   5737   7133    518   -274    -83       C  
ATOM   2166  N   PRO A 200      14.282   6.772  11.517  1.00 66.16           N  
ANISOU 2166  N   PRO A 200     7640   8010   9489    863    354    549       N  
ATOM   2167  CA  PRO A 200      13.048   7.557  11.661  1.00 70.62           C  
ANISOU 2167  CA  PRO A 200     8058   8628  10147    950    481    688       C  
ATOM   2168  C   PRO A 200      12.504   7.944  10.298  1.00 68.81           C  
ANISOU 2168  C   PRO A 200     7639   8498  10007    906    381    762       C  
ATOM   2169  O   PRO A 200      13.189   8.631   9.526  1.00 69.81           O  
ANISOU 2169  O   PRO A 200     7809   8613  10101    917    293    698       O  
ATOM   2170  CB  PRO A 200      13.496   8.794  12.460  1.00 62.75           C  
ANISOU 2170  CB  PRO A 200     7208   7548   9086   1109    598    646       C  
ATOM   2171  CG  PRO A 200      14.990   8.791  12.410  1.00 60.79           C  
ANISOU 2171  CG  PRO A 200     7144   7230   8726   1084    490    485       C  
ATOM   2172  CD  PRO A 200      15.399   7.360  12.275  1.00 59.55           C  
ANISOU 2172  CD  PRO A 200     7006   7075   8547    955    380    431       C  
ATOM   2173  N   PRO A 201      11.280   7.523   9.960  1.00 70.71           N  
ANISOU 2173  N   PRO A 201     7671   8836  10358    848    386    896       N  
ATOM   2174  CA  PRO A 201      10.786   7.771   8.594  1.00 75.21           C  
ANISOU 2174  CA  PRO A 201     8068   9502  11005    786    253    968       C  
ATOM   2175  C   PRO A 201      10.820   9.233   8.185  1.00 76.05           C  
ANISOU 2175  C   PRO A 201     8168   9604  11124    924    268    987       C  
ATOM   2176  O   PRO A 201      10.979   9.525   6.993  1.00 76.26           O  
ANISOU 2176  O   PRO A 201     8158   9664  11154    871    126    984       O  
ATOM   2177  CB  PRO A 201       9.349   7.232   8.639  1.00 78.95           C  
ANISOU 2177  CB  PRO A 201     8309  10084  11607    733    295   1124       C  
ATOM   2178  CG  PRO A 201       9.355   6.229   9.739  1.00 81.23           C  
ANISOU 2178  CG  PRO A 201     8683  10325  11858    688    398   1095       C  
ATOM   2179  CD  PRO A 201      10.308   6.762  10.766  1.00 72.40           C  
ANISOU 2179  CD  PRO A 201     7800   9080  10631    820    504    986       C  
ATOM   2180  N   GLU A 202      10.681  10.165   9.131  1.00 80.38           N  
ANISOU 2180  N   GLU A 202     8772  10100  11668   1096    440   1006       N  
ATOM   2181  CA  GLU A 202      10.689  11.577   8.768  1.00 80.91           C  
ANISOU 2181  CA  GLU A 202     8855  10149  11737   1234    467   1028       C  
ATOM   2182  C   GLU A 202      12.040  12.027   8.222  1.00 80.04           C  
ANISOU 2182  C   GLU A 202     8939   9965  11507   1205    366    878       C  
ATOM   2183  O   GLU A 202      12.100  13.040   7.517  1.00 89.52           O  
ANISOU 2183  O   GLU A 202    10151  11161  12703   1265    334    889       O  
ATOM   2184  CB  GLU A 202      10.282  12.445   9.964  1.00 82.09           C  
ANISOU 2184  CB  GLU A 202     9058  10239  11891   1422    693   1075       C  
ATOM   2185  CG  GLU A 202      11.233  12.430  11.151  1.00 81.98           C  
ANISOU 2185  CG  GLU A 202     9298  10101  11748   1455    793    951       C  
ATOM   2186  CD  GLU A 202      10.870  11.373  12.179  1.00 82.70           C  
ANISOU 2186  CD  GLU A 202     9390  10184  11850   1411    885    969       C  
ATOM   2187  OE1 GLU A 202      10.093  10.453  11.845  1.00 82.35           O  
ANISOU 2187  OE1 GLU A 202     9159  10231  11898   1311    842   1049       O  
ATOM   2188  OE2 GLU A 202      11.349  11.474  13.328  1.00 84.00           O  
ANISOU 2188  OE2 GLU A 202     9752  10244  11920   1469   1002    904       O  
ATOM   2189  N   LYS A 203      13.119  11.309   8.530  1.00 78.32           N  
ANISOU 2189  N   LYS A 203     8872   9689  11197   1117    319    740       N  
ATOM   2190  CA  LYS A 203      14.454  11.649   8.049  1.00 74.19           C  
ANISOU 2190  CA  LYS A 203     8514   9103  10574   1079    230    590       C  
ATOM   2191  C   LYS A 203      15.166  10.413   7.510  1.00 62.80           C  
ANISOU 2191  C   LYS A 203     7092   7668   9102    913     88    500       C  
ATOM   2192  O   LYS A 203      16.365  10.220   7.729  1.00 59.89           O  
ANISOU 2192  O   LYS A 203     6870   7234   8651    884     57    360       O  
ATOM   2193  CB  LYS A 203      15.282  12.290   9.161  1.00 68.14           C  
ANISOU 2193  CB  LYS A 203     7947   8233   9708   1178    341    493       C  
ATOM   2194  CG  LYS A 203      14.686  13.561   9.751  1.00 76.11           C  
ANISOU 2194  CG  LYS A 203     8986   9209  10724   1347    503    569       C  
ATOM   2195  CD  LYS A 203      14.857  14.758   8.832  1.00 75.40           C  
ANISOU 2195  CD  LYS A 203     8924   9108  10617   1391    471    564       C  
ATOM   2196  CE  LYS A 203      14.419  16.042   9.524  1.00 76.00           C  
ANISOU 2196  CE  LYS A 203     9079   9124  10675   1569    648    623       C  
ATOM   2197  NZ  LYS A 203      14.785  17.258   8.744  1.00 77.09           N  
ANISOU 2197  NZ  LYS A 203     9306   9222  10762   1611    626    593       N  
ATOM   2198  N   TYR A 204      14.441   9.556   6.788  1.00 63.61           N  
ANISOU 2198  N   TYR A 204     7048   7848   9274    800      0    581       N  
ATOM   2199  CA  TYR A 204      15.035   8.312   6.307  1.00 62.09           C  
ANISOU 2199  CA  TYR A 204     6891   7651   9048    643   -117    504       C  
ATOM   2200  C   TYR A 204      16.115   8.572   5.261  1.00 59.25           C  
ANISOU 2200  C   TYR A 204     6628   7254   8630    577   -226    386       C  
ATOM   2201  O   TYR A 204      17.199   7.978   5.314  1.00 52.52           O  
ANISOU 2201  O   TYR A 204     5891   6348   7717    523   -265    258       O  
ATOM   2202  CB  TYR A 204      13.948   7.400   5.734  1.00 65.63           C  
ANISOU 2202  CB  TYR A 204     7174   8187   9574    521   -185    624       C  
ATOM   2203  CG  TYR A 204      14.384   5.961   5.575  1.00 62.51           C  
ANISOU 2203  CG  TYR A 204     6838   7774   9140    370   -262    562       C  
ATOM   2204  CD1 TYR A 204      15.060   5.541   4.436  1.00 66.11           C  
ANISOU 2204  CD1 TYR A 204     7354   8212   9554    244   -393    487       C  
ATOM   2205  CD2 TYR A 204      14.125   5.025   6.565  1.00 60.83           C  
ANISOU 2205  CD2 TYR A 204     6641   7548   8923    355   -192    577       C  
ATOM   2206  CE1 TYR A 204      15.464   4.227   4.289  1.00 69.34           C  
ANISOU 2206  CE1 TYR A 204     7834   8590   9922    117   -450    431       C  
ATOM   2207  CE2 TYR A 204      14.528   3.712   6.429  1.00 64.96           C  
ANISOU 2207  CE2 TYR A 204     7240   8040   9400    227   -256    522       C  
ATOM   2208  CZ  TYR A 204      15.194   3.316   5.288  1.00 69.81           C  
ANISOU 2208  CZ  TYR A 204     7910   8638   9978    112   -384    450       C  
ATOM   2209  OH  TYR A 204      15.594   2.005   5.149  1.00 71.17           O  
ANISOU 2209  OH  TYR A 204     8174   8768  10101     -7   -436    397       O  
ATOM   2210  N   ALA A 205      15.837   9.455   4.300  1.00 62.00           N  
ANISOU 2210  N   ALA A 205     6933   7626   8996    584   -271    428       N  
ATOM   2211  CA  ALA A 205      16.808   9.729   3.244  1.00 55.12           C  
ANISOU 2211  CA  ALA A 205     6164   6713   8067    510   -361    318       C  
ATOM   2212  C   ALA A 205      18.073  10.368   3.802  1.00 56.93           C  
ANISOU 2212  C   ALA A 205     6550   6861   8221    579   -298    171       C  
ATOM   2213  O   ALA A 205      19.186  10.035   3.378  1.00 55.81           O  
ANISOU 2213  O   ALA A 205     6500   6675   8030    500   -350     38       O  
ATOM   2214  CB  ALA A 205      16.181  10.624   2.175  1.00 56.31           C  
ANISOU 2214  CB  ALA A 205     6257   6895   8241    514   -416    403       C  
ATOM   2215  N   GLN A 206      17.924  11.284   4.760  1.00 57.75           N  
ANISOU 2215  N   GLN A 206     6686   6942   8314    722   -181    191       N  
ATOM   2216  CA  GLN A 206      19.087  11.975   5.307  1.00 56.16           C  
ANISOU 2216  CA  GLN A 206     6638   6667   8034    775   -128     56       C  
ATOM   2217  C   GLN A 206      19.980  11.022   6.092  1.00 49.36           C  
ANISOU 2217  C   GLN A 206     5842   5774   7138    743   -141    -50       C  
ATOM   2218  O   GLN A 206      21.210  11.129   6.037  1.00 50.24           O  
ANISOU 2218  O   GLN A 206     6050   5841   7197    713   -169   -191       O  
ATOM   2219  CB  GLN A 206      18.633  13.140   6.188  1.00 55.58           C  
ANISOU 2219  CB  GLN A 206     6606   6566   7945    929      5    113       C  
ATOM   2220  CG  GLN A 206      17.949  14.269   5.430  1.00 65.71           C  
ANISOU 2220  CG  GLN A 206     7858   7860   9247    988     22    201       C  
ATOM   2221  CD  GLN A 206      16.493  13.982   5.114  1.00 74.07           C  
ANISOU 2221  CD  GLN A 206     8730   9002  10410   1010      9    378       C  
ATOM   2222  OE1 GLN A 206      15.678  13.782   6.014  1.00 74.06           O  
ANISOU 2222  OE1 GLN A 206     8651   9027  10461   1090    101    472       O  
ATOM   2223  NE2 GLN A 206      16.158  13.968   3.828  1.00 72.76           N  
ANISOU 2223  NE2 GLN A 206     8493   8879  10274    934   -107    424       N  
ATOM   2224  N   TRP A 207      19.382  10.081   6.825  1.00 49.74           N  
ANISOU 2224  N   TRP A 207     5838   5844   7218    749   -120     17       N  
ATOM   2225  CA  TRP A 207      20.176   9.112   7.572  1.00 49.26           C  
ANISOU 2225  CA  TRP A 207     5852   5747   7120    728   -141    -72       C  
ATOM   2226  C   TRP A 207      20.907   8.160   6.633  1.00 52.90           C  
ANISOU 2226  C   TRP A 207     6311   6208   7582    602   -256   -156       C  
ATOM   2227  O   TRP A 207      22.113   7.929   6.780  1.00 48.64           O  
ANISOU 2227  O   TRP A 207     5853   5625   7002    591   -292   -287       O  
ATOM   2228  CB  TRP A 207      19.282   8.331   8.534  1.00 49.97           C  
ANISOU 2228  CB  TRP A 207     5905   5849   7233    757    -80     25       C  
ATOM   2229  CG  TRP A 207      19.095   8.996   9.858  1.00 50.44           C  
ANISOU 2229  CG  TRP A 207     6044   5865   7257    885     45     48       C  
ATOM   2230  CD1 TRP A 207      18.036   9.760  10.251  1.00 51.37           C  
ANISOU 2230  CD1 TRP A 207     6112   5998   7409    977    165    165       C  
ATOM   2231  CD2 TRP A 207      19.996   8.956  10.970  1.00 50.18           C  
ANISOU 2231  CD2 TRP A 207     6165   5759   7142    937     65    -48       C  
ATOM   2232  NE1 TRP A 207      18.221  10.197  11.541  1.00 51.66           N  
ANISOU 2232  NE1 TRP A 207     6282   5965   7382   1077    274    145       N  
ATOM   2233  CE2 TRP A 207      19.418   9.718  12.004  1.00 50.94           C  
ANISOU 2233  CE2 TRP A 207     6321   5820   7213   1048    204     16       C  
ATOM   2234  CE3 TRP A 207      21.236   8.350  11.191  1.00 49.52           C  
ANISOU 2234  CE3 TRP A 207     6175   5636   7006    904    -24   -178       C  
ATOM   2235  CZ2 TRP A 207      20.036   9.890  13.239  1.00 51.03           C  
ANISOU 2235  CZ2 TRP A 207     6503   5751   7134   1111    248    -48       C  
ATOM   2236  CZ3 TRP A 207      21.847   8.521  12.418  1.00 49.66           C  
ANISOU 2236  CZ3 TRP A 207     6337   5587   6944    974      5   -237       C  
ATOM   2237  CH2 TRP A 207      21.247   9.285  13.426  1.00 50.39           C  
ANISOU 2237  CH2 TRP A 207     6507   5639   6999   1069    136   -173       C  
ATOM   2238  N   SER A 208      20.189   7.588   5.663  1.00 50.43           N  
ANISOU 2238  N   SER A 208     5907   5941   7315    504   -314    -80       N  
ATOM   2239  CA  SER A 208      20.823   6.679   4.715  1.00 48.47           C  
ANISOU 2239  CA  SER A 208     5680   5679   7058    379   -409   -153       C  
ATOM   2240  C   SER A 208      22.017   7.337   4.037  1.00 47.78           C  
ANISOU 2240  C   SER A 208     5665   5552   6938    361   -434   -288       C  
ATOM   2241  O   SER A 208      23.065   6.708   3.859  1.00 50.01           O  
ANISOU 2241  O   SER A 208     6004   5796   7202    316   -470   -404       O  
ATOM   2242  CB  SER A 208      19.804   6.218   3.674  1.00 55.45           C  
ANISOU 2242  CB  SER A 208     6471   6615   7983    266   -471    -43       C  
ATOM   2243  OG  SER A 208      18.749   5.495   4.284  1.00 52.39           O  
ANISOU 2243  OG  SER A 208     6007   6269   7632    260   -447     73       O  
ATOM   2244  N   ALA A 209      21.875   8.606   3.647  1.00 51.43           N  
ANISOU 2244  N   ALA A 209     6128   6019   7393    395   -406   -274       N  
ATOM   2245  CA  ALA A 209      22.996   9.316   3.043  1.00 50.88           C  
ANISOU 2245  CA  ALA A 209     6138   5907   7287    369   -412   -405       C  
ATOM   2246  C   ALA A 209      24.106   9.554   4.060  1.00 50.50           C  
ANISOU 2246  C   ALA A 209     6159   5822   7205    439   -373   -526       C  
ATOM   2247  O   ALA A 209      25.290   9.384   3.748  1.00 50.07           O  
ANISOU 2247  O   ALA A 209     6146   5739   7138    391   -399   -661       O  
ATOM   2248  CB  ALA A 209      22.522  10.641   2.448  1.00 55.72           C  
ANISOU 2248  CB  ALA A 209     6759   6524   7888    394   -386   -355       C  
ATOM   2249  N   GLY A 210      23.742   9.934   5.286  1.00 48.01           N  
ANISOU 2249  N   GLY A 210     5859   5508   6876    548   -311   -479       N  
ATOM   2250  CA  GLY A 210      24.753  10.209   6.293  1.00 49.83           C  
ANISOU 2250  CA  GLY A 210     6171   5702   7062    607   -290   -585       C  
ATOM   2251  C   GLY A 210      25.472   8.958   6.757  1.00 49.57           C  
ANISOU 2251  C   GLY A 210     6142   5657   7034    591   -349   -654       C  
ATOM   2252  O   GLY A 210      26.697   8.955   6.908  1.00 46.61           O  
ANISOU 2252  O   GLY A 210     5804   5261   6644    585   -383   -784       O  
ATOM   2253  N   ILE A 211      24.724   7.879   6.993  1.00 51.05           N  
ANISOU 2253  N   ILE A 211     6292   5858   7246    586   -363   -567       N  
ATOM   2254  CA  ILE A 211      25.344   6.638   7.444  1.00 47.02           C  
ANISOU 2254  CA  ILE A 211     5808   5324   6732    581   -418   -622       C  
ATOM   2255  C   ILE A 211      26.221   6.053   6.344  1.00 46.67           C  
ANISOU 2255  C   ILE A 211     5747   5271   6714    492   -481   -720       C  
ATOM   2256  O   ILE A 211      27.272   5.462   6.618  1.00 50.85           O  
ANISOU 2256  O   ILE A 211     6305   5774   7243    509   -524   -821       O  
ATOM   2257  CB  ILE A 211      24.263   5.641   7.899  1.00 47.46           C  
ANISOU 2257  CB  ILE A 211     5846   5389   6799    581   -404   -502       C  
ATOM   2258  CG1 ILE A 211      23.483   6.201   9.094  1.00 53.71           C  
ANISOU 2258  CG1 ILE A 211     6665   6177   7565    677   -317   -416       C  
ATOM   2259  CG2 ILE A 211      24.884   4.297   8.246  1.00 47.50           C  
ANISOU 2259  CG2 ILE A 211     5901   5356   6790    573   -461   -556       C  
ATOM   2260  CD1 ILE A 211      24.337   6.524  10.307  1.00 52.52           C  
ANISOU 2260  CD1 ILE A 211     6626   5976   7353    766   -311   -496       C  
ATOM   2261  N   ALA A 212      25.809   6.208   5.084  1.00 46.56           N  
ANISOU 2261  N   ALA A 212     5693   5275   6723    401   -486   -689       N  
ATOM   2262  CA  ALA A 212      26.618   5.703   3.980  1.00 48.64           C  
ANISOU 2262  CA  ALA A 212     5963   5515   7002    309   -525   -783       C  
ATOM   2263  C   ALA A 212      27.959   6.422   3.911  1.00 49.66           C  
ANISOU 2263  C   ALA A 212     6113   5626   7130    323   -516   -931       C  
ATOM   2264  O   ALA A 212      28.991   5.803   3.627  1.00 46.10           O  
ANISOU 2264  O   ALA A 212     5666   5150   6701    300   -540  -1038       O  
ATOM   2265  CB  ALA A 212      25.859   5.855   2.662  1.00 46.41           C  
ANISOU 2265  CB  ALA A 212     5661   5245   6728    202   -535   -715       C  
ATOM   2266  N   LEU A 213      27.965   7.730   4.175  1.00 49.47           N  
ANISOU 2266  N   LEU A 213     6102   5612   7081    360   -475   -939       N  
ATOM   2267  CA  LEU A 213      29.204   8.493   4.086  1.00 50.71           C  
ANISOU 2267  CA  LEU A 213     6280   5756   7232    351   -462  -1081       C  
ATOM   2268  C   LEU A 213      30.147   8.164   5.237  1.00 48.95           C  
ANISOU 2268  C   LEU A 213     6058   5530   7009    426   -496  -1162       C  
ATOM   2269  O   LEU A 213      31.370   8.216   5.066  1.00 54.95           O  
ANISOU 2269  O   LEU A 213     6799   6286   7793    403   -513  -1294       O  
ATOM   2270  CB  LEU A 213      28.895   9.989   4.052  1.00 51.15           C  
ANISOU 2270  CB  LEU A 213     6377   5813   7246    363   -405  -1062       C  
ATOM   2271  CG  LEU A 213      28.114  10.458   2.820  1.00 51.00           C  
ANISOU 2271  CG  LEU A 213     6364   5791   7222    293   -386   -994       C  
ATOM   2272  CD1 LEU A 213      27.641  11.893   2.989  1.00 60.33           C  
ANISOU 2272  CD1 LEU A 213     7599   6966   8356    339   -326   -950       C  
ATOM   2273  CD2 LEU A 213      28.950  10.319   1.556  1.00 50.14           C  
ANISOU 2273  CD2 LEU A 213     6270   5654   7126    177   -391  -1103       C  
ATOM   2274  N   MET A 214      29.609   7.828   6.412  1.00 55.09           N  
ANISOU 2274  N   MET A 214     6860   6309   7762    512   -508  -1086       N  
ATOM   2275  CA  MET A 214      30.464   7.420   7.521  1.00 55.44           C  
ANISOU 2275  CA  MET A 214     6924   6343   7796    584   -561  -1153       C  
ATOM   2276  C   MET A 214      31.049   6.032   7.290  1.00 53.94           C  
ANISOU 2276  C   MET A 214     6702   6141   7653    580   -622  -1198       C  
ATOM   2277  O   MET A 214      32.066   5.690   7.902  1.00 55.30           O  
ANISOU 2277  O   MET A 214     6869   6307   7836    632   -682  -1283       O  
ATOM   2278  CB  MET A 214      29.676   7.468   8.837  1.00 55.42           C  
ANISOU 2278  CB  MET A 214     6990   6329   7739    672   -545  -1055       C  
ATOM   2279  CG  MET A 214      29.121   6.136   9.347  1.00 58.88           C  
ANISOU 2279  CG  MET A 214     7445   6750   8178    708   -572   -979       C  
ATOM   2280  SD  MET A 214      28.410   6.276  11.009  1.00 73.63           S  
ANISOU 2280  SD  MET A 214     9419   8585   9970    809   -538   -889       S  
ATOM   2281  CE  MET A 214      29.645   5.504  12.049  1.00 56.09           C  
ANISOU 2281  CE  MET A 214     7265   6328   7719    877   -649   -985       C  
ATOM   2282  N   LYS A 215      30.425   5.223   6.428  1.00 55.95           N  
ANISOU 2282  N   LYS A 215     6941   6386   7930    522   -612  -1139       N  
ATOM   2283  CA  LYS A 215      31.025   3.950   6.039  1.00 56.57           C  
ANISOU 2283  CA  LYS A 215     7009   6437   8046    511   -651  -1189       C  
ATOM   2284  C   LYS A 215      32.268   4.159   5.184  1.00 55.90           C  
ANISOU 2284  C   LYS A 215     6876   6351   8015    466   -646  -1328       C  
ATOM   2285  O   LYS A 215      33.267   3.450   5.349  1.00 56.25           O  
ANISOU 2285  O   LYS A 215     6895   6379   8099    510   -685  -1412       O  
ATOM   2286  CB  LYS A 215      29.999   3.092   5.298  1.00 57.24           C  
ANISOU 2286  CB  LYS A 215     7114   6507   8129    438   -636  -1089       C  
ATOM   2287  CG  LYS A 215      29.269   2.107   6.192  1.00 60.71           C  
ANISOU 2287  CG  LYS A 215     7601   6927   8536    487   -655   -994       C  
ATOM   2288  CD  LYS A 215      28.254   1.263   5.427  1.00 63.41           C  
ANISOU 2288  CD  LYS A 215     7959   7259   8873    390   -643   -898       C  
ATOM   2289  CE  LYS A 215      26.836   1.734   5.724  1.00 61.95           C  
ANISOU 2289  CE  LYS A 215     7753   7116   8671    373   -610   -759       C  
ATOM   2290  NZ  LYS A 215      25.814   1.091   4.859  1.00 64.37           N  
ANISOU 2290  NZ  LYS A 215     8049   7429   8978    255   -611   -663       N  
ATOM   2291  N   ASN A 216      32.225   5.121   4.261  1.00 49.27           N  
ANISOU 2291  N   ASN A 216     6023   5522   7177    381   -594  -1354       N  
ATOM   2292  CA  ASN A 216      33.396   5.398   3.438  1.00 51.69           C  
ANISOU 2292  CA  ASN A 216     6289   5821   7530    325   -568  -1491       C  
ATOM   2293  C   ASN A 216      34.530   5.973   4.276  1.00 52.56           C  
ANISOU 2293  C   ASN A 216     6350   5960   7660    384   -597  -1599       C  
ATOM   2294  O   ASN A 216      35.685   5.552   4.143  1.00 55.13           O  
ANISOU 2294  O   ASN A 216     6611   6286   8051    395   -612  -1710       O  
ATOM   2295  CB  ASN A 216      33.025   6.355   2.306  1.00 49.97           C  
ANISOU 2295  CB  ASN A 216     6098   5597   7291    216   -503  -1488       C  
ATOM   2296  CG  ASN A 216      32.040   5.746   1.329  1.00 46.30           C  
ANISOU 2296  CG  ASN A 216     5678   5103   6809    138   -494  -1393       C  
ATOM   2297  OD1 ASN A 216      32.005   4.530   1.138  1.00 46.47           O  
ANISOU 2297  OD1 ASN A 216     5711   5098   6849    132   -514  -1377       O  
ATOM   2298  ND2 ASN A 216      31.231   6.592   0.704  1.00 50.33           N  
ANISOU 2298  ND2 ASN A 216     6223   5618   7281     76   -469  -1328       N  
ATOM   2299  N   ILE A 217      34.215   6.929   5.149  1.00 48.41           N  
ANISOU 2299  N   ILE A 217     5855   5458   7081    420   -604  -1566       N  
ATOM   2300  CA  ILE A 217      35.250   7.618   5.915  1.00 49.48           C  
ANISOU 2300  CA  ILE A 217     5961   5621   7219    449   -638  -1666       C  
ATOM   2301  C   ILE A 217      35.904   6.663   6.908  1.00 48.27           C  
ANISOU 2301  C   ILE A 217     5774   5473   7093    551   -736  -1692       C  
ATOM   2302  O   ILE A 217      37.110   6.397   6.841  1.00 51.16           O  
ANISOU 2302  O   ILE A 217     6052   5857   7528    559   -775  -1805       O  
ATOM   2303  CB  ILE A 217      34.657   8.849   6.623  1.00 50.11           C  
ANISOU 2303  CB  ILE A 217     6119   5707   7215    461   -614  -1614       C  
ATOM   2304  CG1 ILE A 217      34.138   9.849   5.585  1.00 59.49           C  
ANISOU 2304  CG1 ILE A 217     7342   6883   8377    371   -522  -1598       C  
ATOM   2305  CG2 ILE A 217      35.697   9.497   7.522  1.00 53.43           C  
ANISOU 2305  CG2 ILE A 217     6531   6150   7620    479   -664  -1712       C  
ATOM   2306  CD1 ILE A 217      33.348  11.004   6.173  1.00 56.38           C  
ANISOU 2306  CD1 ILE A 217     7041   6481   7899    398   -478  -1523       C  
ATOM   2307  N   LEU A 218      35.116   6.135   7.844  1.00 48.21           N  
ANISOU 2307  N   LEU A 218     5837   5447   7034    631   -776  -1586       N  
ATOM   2308  CA  LEU A 218      35.675   5.277   8.883  1.00 48.92           C  
ANISOU 2308  CA  LEU A 218     5929   5530   7128    735   -877  -1601       C  
ATOM   2309  C   LEU A 218      36.165   3.942   8.335  1.00 50.15           C  
ANISOU 2309  C   LEU A 218     6033   5664   7357    762   -902  -1632       C  
ATOM   2310  O   LEU A 218      37.069   3.333   8.917  1.00 50.09           O  
ANISOU 2310  O   LEU A 218     5988   5658   7385    846   -990  -1688       O  
ATOM   2311  CB  LEU A 218      34.629   5.039   9.972  1.00 49.61           C  
ANISOU 2311  CB  LEU A 218     6132   5586   7129    803   -891  -1477       C  
ATOM   2312  CG  LEU A 218      34.167   6.273  10.745  1.00 48.76           C  
ANISOU 2312  CG  LEU A 218     6103   5483   6941    803   -861  -1440       C  
ATOM   2313  CD1 LEU A 218      33.011   5.918  11.660  1.00 48.74           C  
ANISOU 2313  CD1 LEU A 218     6214   5442   6864    864   -840  -1310       C  
ATOM   2314  CD2 LEU A 218      35.321   6.858  11.546  1.00 49.54           C  
ANISOU 2314  CD2 LEU A 218     6198   5601   7024    825   -945  -1541       C  
ATOM   2315  N   GLY A 219      35.596   3.474   7.228  1.00 54.34           N  
ANISOU 2315  N   GLY A 219     6569   6169   7907    695   -830  -1595       N  
ATOM   2316  CA  GLY A 219      35.866   2.125   6.772  1.00 52.74           C  
ANISOU 2316  CA  GLY A 219     6362   5926   7751    722   -839  -1605       C  
ATOM   2317  C   GLY A 219      36.802   2.011   5.588  1.00 53.51           C  
ANISOU 2317  C   GLY A 219     6377   6020   7935    666   -787  -1716       C  
ATOM   2318  O   GLY A 219      37.223   0.903   5.240  1.00 54.49           O  
ANISOU 2318  O   GLY A 219     6497   6102   8104    703   -787  -1740       O  
ATOM   2319  N   PHE A 220      37.148   3.135   4.962  1.00 53.77           N  
ANISOU 2319  N   PHE A 220     6356   6085   7988    578   -731  -1786       N  
ATOM   2320  CA  PHE A 220      38.007   3.093   3.784  1.00 55.19           C  
ANISOU 2320  CA  PHE A 220     6470   6253   8247    509   -657  -1895       C  
ATOM   2321  C   PHE A 220      38.953   4.285   3.733  1.00 51.14           C  
ANISOU 2321  C   PHE A 220     5864   5792   7774    462   -638  -2013       C  
ATOM   2322  O   PHE A 220      40.176   4.111   3.753  1.00 50.82           O  
ANISOU 2322  O   PHE A 220     5709   5776   7826    495   -650  -2125       O  
ATOM   2323  CB  PHE A 220      37.163   3.043   2.509  1.00 49.63           C  
ANISOU 2323  CB  PHE A 220     5847   5501   7509    389   -567  -1844       C  
ATOM   2324  CG  PHE A 220      37.945   2.678   1.280  1.00 49.35           C  
ANISOU 2324  CG  PHE A 220     5788   5423   7540    322   -479  -1942       C  
ATOM   2325  CD1 PHE A 220      38.359   1.374   1.070  1.00 50.00           C  
ANISOU 2325  CD1 PHE A 220     5875   5453   7669    378   -471  -1960       C  
ATOM   2326  CD2 PHE A 220      38.260   3.637   0.334  1.00 49.27           C  
ANISOU 2326  CD2 PHE A 220     5769   5412   7539    205   -391  -2017       C  
ATOM   2327  CE1 PHE A 220      39.076   1.034  -0.060  1.00 50.58           C  
ANISOU 2327  CE1 PHE A 220     5940   5474   7803    321   -369  -2051       C  
ATOM   2328  CE2 PHE A 220      38.974   3.303  -0.796  1.00 49.83           C  
ANISOU 2328  CE2 PHE A 220     5835   5432   7667    138   -292  -2111       C  
ATOM   2329  CZ  PHE A 220      39.384   2.000  -0.994  1.00 50.50           C  
ANISOU 2329  CZ  PHE A 220     5919   5464   7804    197   -277  -2128       C  
ATOM   2330  N   ILE A 221      38.400   5.494   3.666  1.00 56.89           N  
ANISOU 2330  N   ILE A 221     8071   5484   8061    -48    237    250       N  
ATOM   2331  CA  ILE A 221      39.203   6.698   3.492  1.00 52.51           C  
ANISOU 2331  CA  ILE A 221     7525   4854   7573    -94    287    298       C  
ATOM   2332  C   ILE A 221      40.252   6.757   4.594  1.00 53.87           C  
ANISOU 2332  C   ILE A 221     7669   4984   7816   -203    238    270       C  
ATOM   2333  O   ILE A 221      41.453   6.636   4.331  1.00 54.62           O  
ANISOU 2333  O   ILE A 221     7691   5091   7972   -248    247    307       O  
ATOM   2334  CB  ILE A 221      38.325   7.962   3.511  1.00 56.57           C  
ANISOU 2334  CB  ILE A 221     8121   5288   8085    -65    319    312       C  
ATOM   2335  CG1 ILE A 221      37.352   7.967   2.327  1.00 57.31           C  
ANISOU 2335  CG1 ILE A 221     8234   5422   8119     41    350    358       C  
ATOM   2336  CG2 ILE A 221      39.197   9.215   3.497  1.00 54.42           C  
ANISOU 2336  CG2 ILE A 221     7878   4917   7883   -135    355    358       C  
ATOM   2337  CD1 ILE A 221      38.014   7.856   0.966  1.00 64.69           C  
ANISOU 2337  CD1 ILE A 221     9152   6393   9033     61    400    432       C  
ATOM   2338  N   ILE A 222      39.801   6.947   5.835  1.00 54.56           N  
ANISOU 2338  N   ILE A 222     7814   5023   7896   -246    187    208       N  
ATOM   2339  CA  ILE A 222      40.737   7.049   6.954  1.00 48.93           C  
ANISOU 2339  CA  ILE A 222     7099   4258   7236   -361    119    180       C  
ATOM   2340  C   ILE A 222      41.644   5.826   7.034  1.00 45.65           C  
ANISOU 2340  C   ILE A 222     6584   3913   6847   -385     59    180       C  
ATOM   2341  O   ILE A 222      42.871   5.998   7.120  1.00 53.75           O  
ANISOU 2341  O   ILE A 222     7542   4921   7959   -458     34    215       O  
ATOM   2342  CB  ILE A 222      39.972   7.310   8.262  1.00 44.02           C  
ANISOU 2342  CB  ILE A 222     6580   3578   6567   -394     80    104       C  
ATOM   2343  CG1 ILE A 222      39.371   8.719   8.233  1.00 45.24           C  
ANISOU 2343  CG1 ILE A 222     6832   3634   6723   -373    143    107       C  
ATOM   2344  CG2 ILE A 222      40.892   7.127   9.461  1.00 44.63           C  
ANISOU 2344  CG2 ILE A 222     6670   3615   6674   -517    -18     71       C  
ATOM   2345  CD1 ILE A 222      38.483   9.041   9.417  1.00 51.72           C  
ANISOU 2345  CD1 ILE A 222     7765   4399   7489   -377    140     27       C  
ATOM   2346  N   PRO A 223      41.134   4.592   7.021  1.00 45.34           N  
ANISOU 2346  N   PRO A 223     6530   3949   6750   -329     27    148       N  
ATOM   2347  CA  PRO A 223      42.047   3.437   6.958  1.00 49.84           C  
ANISOU 2347  CA  PRO A 223     7011   4573   7353   -331    -25    152       C  
ATOM   2348  C   PRO A 223      43.069   3.539   5.838  1.00 46.83           C  
ANISOU 2348  C   PRO A 223     6531   4222   7041   -302     45    219       C  
ATOM   2349  O   PRO A 223      44.273   3.410   6.087  1.00 47.67           O  
ANISOU 2349  O   PRO A 223     6546   4327   7241   -355     12    243       O  
ATOM   2350  CB  PRO A 223      41.087   2.256   6.762  1.00 52.83           C  
ANISOU 2350  CB  PRO A 223     7416   5017   7641   -257    -45    117       C  
ATOM   2351  CG  PRO A 223      39.828   2.691   7.410  1.00 52.87           C  
ANISOU 2351  CG  PRO A 223     7511   4997   7580   -266    -45     78       C  
ATOM   2352  CD  PRO A 223      39.728   4.178   7.182  1.00 49.90           C  
ANISOU 2352  CD  PRO A 223     7169   4557   7235   -272     28    105       C  
ATOM   2353  N   LEU A 224      42.620   3.781   4.604  1.00 48.39           N  
ANISOU 2353  N   LEU A 224     6742   4448   7195   -222    143    255       N  
ATOM   2354  CA  LEU A 224      43.539   3.811   3.473  1.00 48.27           C  
ANISOU 2354  CA  LEU A 224     6647   4471   7223   -190    232    319       C  
ATOM   2355  C   LEU A 224      44.585   4.909   3.610  1.00 51.94           C  
ANISOU 2355  C   LEU A 224     7055   4886   7796   -285    261    376       C  
ATOM   2356  O   LEU A 224      45.662   4.800   3.014  1.00 58.23           O  
ANISOU 2356  O   LEU A 224     7743   5719   8662   -287    320    428       O  
ATOM   2357  CB  LEU A 224      42.763   3.994   2.168  1.00 50.15           C  
ANISOU 2357  CB  LEU A 224     6946   4737   7371   -100    323    350       C  
ATOM   2358  CG  LEU A 224      43.596   3.912   0.887  1.00 50.97           C  
ANISOU 2358  CG  LEU A 224     6996   4888   7484    -55    435    412       C  
ATOM   2359  CD1 LEU A 224      44.276   2.551   0.763  1.00 50.27           C  
ANISOU 2359  CD1 LEU A 224     6832   4862   7406     -2    425    383       C  
ATOM   2360  CD2 LEU A 224      42.732   4.191  -0.332  1.00 51.25           C  
ANISOU 2360  CD2 LEU A 224     7125   4938   7411     20    504    445       C  
ATOM   2361  N   ILE A 225      44.296   5.966   4.372  1.00 46.81           N  
ANISOU 2361  N   ILE A 225     6475   4149   7162   -365    225    368       N  
ATOM   2362  CA  ILE A 225      45.301   6.999   4.597  1.00 47.47           C  
ANISOU 2362  CA  ILE A 225     6517   4170   7349   -479    229    421       C  
ATOM   2363  C   ILE A 225      46.478   6.431   5.374  1.00 44.94           C  
ANISOU 2363  C   ILE A 225     6078   3867   7130   -556    139    419       C  
ATOM   2364  O   ILE A 225      47.625   6.843   5.168  1.00 53.16           O  
ANISOU 2364  O   ILE A 225     7010   4908   8281   -628    160    486       O  
ATOM   2365  CB  ILE A 225      44.678   8.207   5.324  1.00 51.45           C  
ANISOU 2365  CB  ILE A 225     7153   4559   7837   -543    198    399       C  
ATOM   2366  CG1 ILE A 225      43.732   8.960   4.385  1.00 50.22           C  
ANISOU 2366  CG1 ILE A 225     7089   4378   7615   -465    292    429       C  
ATOM   2367  CG2 ILE A 225      45.771   9.132   5.841  1.00 56.12           C  
ANISOU 2367  CG2 ILE A 225     7716   5070   8535   -689    158    441       C  
ATOM   2368  CD1 ILE A 225      42.868   9.995   5.071  1.00 48.38           C  
ANISOU 2368  CD1 ILE A 225     6997   4032   7354   -482    271    392       C  
ATOM   2369  N   PHE A 226      46.219   5.480   6.273  1.00 43.85           N  
ANISOU 2369  N   PHE A 226     5956   3744   6962   -547     34    352       N  
ATOM   2370  CA  PHE A 226      47.294   4.865   7.044  1.00 47.65           C  
ANISOU 2370  CA  PHE A 226     6330   4238   7538   -612    -74    353       C  
ATOM   2371  C   PHE A 226      48.087   3.874   6.201  1.00 50.39           C  
ANISOU 2371  C   PHE A 226     6524   4678   7942   -525    -22    389       C  
ATOM   2372  O   PHE A 226      49.317   3.966   6.117  1.00 58.96           O  
ANISOU 2372  O   PHE A 226     7461   5783   9158   -572    -22    447       O  
ATOM   2373  CB  PHE A 226      46.721   4.168   8.278  1.00 49.25           C  
ANISOU 2373  CB  PHE A 226     6621   4417   7674   -631   -205    274       C  
ATOM   2374  CG  PHE A 226      46.319   5.110   9.374  1.00 47.57           C  
ANISOU 2374  CG  PHE A 226     6542   4104   7427   -740   -273    238       C  
ATOM   2375  CD1 PHE A 226      45.155   5.851   9.275  1.00 48.98           C  
ANISOU 2375  CD1 PHE A 226     6856   4240   7515   -709   -201    206       C  
ATOM   2376  CD2 PHE A 226      47.103   5.253  10.505  1.00 44.37           C  
ANISOU 2376  CD2 PHE A 226     6134   3643   7080   -868   -410    234       C  
ATOM   2377  CE1 PHE A 226      44.783   6.719  10.283  1.00 52.20           C  
ANISOU 2377  CE1 PHE A 226     7401   4548   7887   -793   -247    163       C  
ATOM   2378  CE2 PHE A 226      46.736   6.119  11.514  1.00 45.75           C  
ANISOU 2378  CE2 PHE A 226     6461   3716   7205   -968   -469    191       C  
ATOM   2379  CZ  PHE A 226      45.574   6.853  11.403  1.00 47.79           C  
ANISOU 2379  CZ  PHE A 226     6861   3929   7369   -925   -377    152       C  
ATOM   2380  N   ILE A 227      47.401   2.914   5.575  1.00 57.79           N  
ANISOU 2380  N   ILE A 227     7498   5672   8788   -398     24    353       N  
ATOM   2381  CA  ILE A 227      48.096   1.907   4.779  1.00 58.71           C  
ANISOU 2381  CA  ILE A 227     7499   5866   8943   -298     80    372       C  
ATOM   2382  C   ILE A 227      48.923   2.569   3.683  1.00 59.53           C  
ANISOU 2382  C   ILE A 227     7498   6005   9117   -292    228    454       C  
ATOM   2383  O   ILE A 227      50.066   2.174   3.423  1.00 61.06           O  
ANISOU 2383  O   ILE A 227     7532   6247   9422   -273    262    494       O  
ATOM   2384  CB  ILE A 227      47.089   0.902   4.188  1.00 59.47           C  
ANISOU 2384  CB  ILE A 227     7692   6000   8905   -173    107    319       C  
ATOM   2385  CG1 ILE A 227      46.329   0.181   5.304  1.00 58.81           C  
ANISOU 2385  CG1 ILE A 227     7699   5887   8759   -194    -36    248       C  
ATOM   2386  CG2 ILE A 227      47.805  -0.112   3.306  1.00 66.50           C  
ANISOU 2386  CG2 ILE A 227     8490   6954   9821    -58    178    329       C  
ATOM   2387  CD1 ILE A 227      44.858   0.541   5.378  1.00 56.78           C  
ANISOU 2387  CD1 ILE A 227     7589   5610   8376   -194    -31    212       C  
ATOM   2388  N   ALA A 228      48.360   3.583   3.024  1.00 46.68           N  
ANISOU 2388  N   ALA A 228     5955   4354   7428   -306    322    485       N  
ATOM   2389  CA  ALA A 228      49.090   4.268   1.963  1.00 55.20           C  
ANISOU 2389  CA  ALA A 228     6956   5462   8556   -313    470    571       C  
ATOM   2390  C   ALA A 228      50.306   4.997   2.517  1.00 53.69           C  
ANISOU 2390  C   ALA A 228     6625   5246   8528   -450    438    636       C  
ATOM   2391  O   ALA A 228      51.416   4.863   1.990  1.00 55.14           O  
ANISOU 2391  O   ALA A 228     6644   5492   8817   -447    522    700       O  
ATOM   2392  CB  ALA A 228      48.164   5.243   1.234  1.00 60.21           C  
ANISOU 2392  CB  ALA A 228     7733   6058   9086   -308    551    596       C  
ATOM   2393  N   THR A 229      50.116   5.776   3.584  1.00 51.98           N  
ANISOU 2393  N   THR A 229     6474   4941   8337   -574    317    622       N  
ATOM   2394  CA  THR A 229      51.237   6.491   4.184  1.00 54.74           C  
ANISOU 2394  CA  THR A 229     6707   5254   8837   -726    256    683       C  
ATOM   2395  C   THR A 229      52.302   5.525   4.686  1.00 56.70           C  
ANISOU 2395  C   THR A 229     6770   5561   9213   -724    174    689       C  
ATOM   2396  O   THR A 229      53.502   5.758   4.500  1.00 60.60           O  
ANISOU 2396  O   THR A 229     7078   6091   9857   -788    203    771       O  
ATOM   2397  CB  THR A 229      50.739   7.376   5.328  1.00 48.75           C  
ANISOU 2397  CB  THR A 229     6093   4375   8056   -849    125    646       C  
ATOM   2398  OG1 THR A 229      49.810   8.341   4.818  1.00 57.04           O  
ANISOU 2398  OG1 THR A 229     7302   5362   9008   -838    207    648       O  
ATOM   2399  CG2 THR A 229      51.898   8.093   5.998  1.00 50.36           C  
ANISOU 2399  CG2 THR A 229     6195   4529   8409  -1024     33    707       C  
ATOM   2400  N   CYS A 230      51.881   4.433   5.325  1.00 49.57           N  
ANISOU 2400  N   CYS A 230     5907   4667   8259   -653     70    611       N  
ATOM   2401  CA  CYS A 230      52.843   3.463   5.835  1.00 51.11           C  
ANISOU 2401  CA  CYS A 230     5939   4906   8574   -638    -26    617       C  
ATOM   2402  C   CYS A 230      53.619   2.804   4.703  1.00 52.73           C  
ANISOU 2402  C   CYS A 230     5970   5214   8851   -514    125    663       C  
ATOM   2403  O   CYS A 230      54.830   2.583   4.818  1.00 63.83           O  
ANISOU 2403  O   CYS A 230     7165   6663  10424   -535    105    721       O  
ATOM   2404  CB  CYS A 230      52.123   2.418   6.682  1.00 53.23           C  
ANISOU 2404  CB  CYS A 230     6319   5154   8752   -584   -163    526       C  
ATOM   2405  SG  CYS A 230      51.572   3.059   8.280  1.00 60.33           S  
ANISOU 2405  SG  CYS A 230     7385   5940   9599   -744   -357    476       S  
ATOM   2406  N   TYR A 231      52.943   2.475   3.602  1.00 52.27           N  
ANISOU 2406  N   TYR A 231     5996   5196   8667   -383    277    639       N  
ATOM   2407  CA  TYR A 231      53.626   1.842   2.480  1.00 52.09           C  
ANISOU 2407  CA  TYR A 231     5842   5265   8685   -255    441    671       C  
ATOM   2408  C   TYR A 231      54.662   2.777   1.867  1.00 53.53           C  
ANISOU 2408  C   TYR A 231     5860   5487   8992   -333    574    781       C  
ATOM   2409  O   TYR A 231      55.847   2.439   1.774  1.00 62.57           O  
ANISOU 2409  O   TYR A 231     6781   6695  10296   -316    611    835       O  
ATOM   2410  CB  TYR A 231      52.613   1.406   1.423  1.00 58.88           C  
ANISOU 2410  CB  TYR A 231     6866   6145   9359   -118    565    622       C  
ATOM   2411  CG  TYR A 231      53.260   1.033   0.109  1.00 58.99           C  
ANISOU 2411  CG  TYR A 231     6787   6244   9381      0    771    660       C  
ATOM   2412  CD1 TYR A 231      53.955  -0.160  -0.030  1.00 62.03           C  
ANISOU 2412  CD1 TYR A 231     7055   6681   9833    128    794    637       C  
ATOM   2413  CD2 TYR A 231      53.186   1.880  -0.988  1.00 61.50           C  
ANISOU 2413  CD2 TYR A 231     7147   6585   9637    -14    946    720       C  
ATOM   2414  CE1 TYR A 231      54.554  -0.501  -1.226  1.00 61.32           C  
ANISOU 2414  CE1 TYR A 231     6889   6666   9742    247   1002    664       C  
ATOM   2415  CE2 TYR A 231      53.781   1.546  -2.188  1.00 64.50           C  
ANISOU 2415  CE2 TYR A 231     7457   7043  10005     91   1150    754       C  
ATOM   2416  CZ  TYR A 231      54.464   0.354  -2.301  1.00 63.91           C  
ANISOU 2416  CZ  TYR A 231     7265   7022   9994    224   1185    721       C  
ATOM   2417  OH  TYR A 231      55.061   0.016  -3.493  1.00 66.89           O  
ANISOU 2417  OH  TYR A 231     7585   7477  10353    339   1407    747       O  
ATOM   2418  N   PHE A 232      54.226   3.959   1.425  1.00 56.04           N  
ANISOU 2418  N   PHE A 232     6280   5768   9245   -417    649    822       N  
ATOM   2419  CA  PHE A 232      55.157   4.907   0.821  1.00 59.82           C  
ANISOU 2419  CA  PHE A 232     6621   6276   9831   -512    778    936       C  
ATOM   2420  C   PHE A 232      56.212   5.376   1.815  1.00 64.58           C  
ANISOU 2420  C   PHE A 232     7045   6858  10634   -674    644    996       C  
ATOM   2421  O   PHE A 232      57.308   5.780   1.409  1.00 57.79           O  
ANISOU 2421  O   PHE A 232     5985   6054   9919   -740    738   1098       O  
ATOM   2422  CB  PHE A 232      54.391   6.094   0.243  1.00 54.94           C  
ANISOU 2422  CB  PHE A 232     6181   5598   9094   -576    856    967       C  
ATOM   2423  CG  PHE A 232      53.640   5.767  -1.014  1.00 62.78           C  
ANISOU 2423  CG  PHE A 232     7307   6632   9915   -431   1017    946       C  
ATOM   2424  CD1 PHE A 232      54.309   5.653  -2.221  1.00 61.59           C  
ANISOU 2424  CD1 PHE A 232     7063   6569   9769   -371   1226   1012       C  
ATOM   2425  CD2 PHE A 232      52.271   5.562  -0.991  1.00 69.59           C  
ANISOU 2425  CD2 PHE A 232     8387   7447  10609   -360    958    865       C  
ATOM   2426  CE1 PHE A 232      53.628   5.348  -3.381  1.00 68.12           C  
ANISOU 2426  CE1 PHE A 232     8036   7426  10420   -246   1363    993       C  
ATOM   2427  CE2 PHE A 232      51.584   5.256  -2.150  1.00 71.23           C  
ANISOU 2427  CE2 PHE A 232     8719   7688  10657   -239   1082    852       C  
ATOM   2428  CZ  PHE A 232      52.265   5.150  -3.347  1.00 74.96           C  
ANISOU 2428  CZ  PHE A 232     9123   8239  11121   -184   1279    914       C  
ATOM   2429  N   GLY A 233      55.907   5.330   3.112  1.00 60.69           N  
ANISOU 2429  N   GLY A 233     6623   6288  10150   -749    425    940       N  
ATOM   2430  CA  GLY A 233      56.932   5.609   4.103  1.00 63.23           C  
ANISOU 2430  CA  GLY A 233     6781   6588  10655   -899    267    992       C  
ATOM   2431  C   GLY A 233      57.962   4.500   4.180  1.00 62.74           C  
ANISOU 2431  C   GLY A 233     6473   6620  10747   -812    247   1013       C  
ATOM   2432  O   GLY A 233      59.153   4.755   4.381  1.00 65.07           O  
ANISOU 2432  O   GLY A 233     6534   6950  11238   -907    215   1104       O  
ATOM   2433  N   ILE A 234      57.517   3.252   4.023  1.00 57.57           N  
ANISOU 2433  N   ILE A 234     5865   5999  10011   -629    260    932       N  
ATOM   2434  CA  ILE A 234      58.444   2.130   3.939  1.00 57.75           C  
ANISOU 2434  CA  ILE A 234     5668   6103  10171   -506    268    947       C  
ATOM   2435  C   ILE A 234      59.229   2.185   2.635  1.00 64.09           C  
ANISOU 2435  C   ILE A 234     6288   7014  11051   -427    524   1023       C  
ATOM   2436  O   ILE A 234      60.426   1.879   2.599  1.00 68.61           O  
ANISOU 2436  O   ILE A 234     6587   7659  11821   -408    550   1093       O  
ATOM   2437  CB  ILE A 234      57.682   0.799   4.083  1.00 63.13           C  
ANISOU 2437  CB  ILE A 234     6486   6773  10727   -335    214    836       C  
ATOM   2438  CG1 ILE A 234      57.233   0.599   5.533  1.00 74.23           C  
ANISOU 2438  CG1 ILE A 234     8011   8089  12105   -423    -52    781       C  
ATOM   2439  CG2 ILE A 234      58.545  -0.364   3.606  1.00 66.68           C  
ANISOU 2439  CG2 ILE A 234     6739   7305  11291   -159    291    846       C  
ATOM   2440  CD1 ILE A 234      56.248  -0.539   5.725  1.00 71.22           C  
ANISOU 2440  CD1 ILE A 234     7814   7679  11568   -292   -110    674       C  
ATOM   2441  N   ARG A 235      58.570   2.580   1.543  1.00 67.69           N  
ANISOU 2441  N   ARG A 235     6887   7482  11350   -380    720   1016       N  
ATOM   2442  CA  ARG A 235      59.222   2.548   0.238  1.00 67.22           C  
ANISOU 2442  CA  ARG A 235     6693   7526  11323   -291    985   1080       C  
ATOM   2443  C   ARG A 235      60.422   3.483   0.178  1.00 68.35           C  
ANISOU 2443  C   ARG A 235     6586   7715  11667   -447   1043   1217       C  
ATOM   2444  O   ARG A 235      61.475   3.113  -0.352  1.00 80.64           O  
ANISOU 2444  O   ARG A 235     7893   9376  13369   -379   1187   1281       O  
ATOM   2445  CB  ARG A 235      58.217   2.924  -0.849  1.00 66.59           C  
ANISOU 2445  CB  ARG A 235     6850   7434  11018   -241   1153   1055       C  
ATOM   2446  CG  ARG A 235      58.821   2.987  -2.235  1.00 75.29           C  
ANISOU 2446  CG  ARG A 235     7854   8635  12117   -165   1438   1122       C  
ATOM   2447  CD  ARG A 235      57.768   3.139  -3.313  1.00 67.95           C  
ANISOU 2447  CD  ARG A 235     7186   7691  10942    -91   1579   1086       C  
ATOM   2448  NE  ARG A 235      58.394   3.343  -4.617  1.00 81.70           N  
ANISOU 2448  NE  ARG A 235     8851   9522  12668    -46   1856   1163       N  
ATOM   2449  CZ  ARG A 235      58.747   4.536  -5.091  1.00 90.84           C  
ANISOU 2449  CZ  ARG A 235     9973  10689  13852   -190   1970   1277       C  
ATOM   2450  NH1 ARG A 235      58.544   5.632  -4.369  1.00 92.19           N  
ANISOU 2450  NH1 ARG A 235    10182  10776  14071   -382   1822   1321       N  
ATOM   2451  NH2 ARG A 235      59.315   4.638  -6.285  1.00 93.82           N  
ANISOU 2451  NH2 ARG A 235    10289  11156  14203   -145   2236   1346       N  
ATOM   2452  N   LYS A 236      60.294   4.695   0.719  1.00 71.67           N  
ANISOU 2452  N   LYS A 236     7068   8059  12105   -658    936   1265       N  
ATOM   2453  CA  LYS A 236      61.414   5.627   0.652  1.00 72.02           C  
ANISOU 2453  CA  LYS A 236     6885   8139  12339   -831    980   1403       C  
ATOM   2454  C   LYS A 236      62.537   5.196   1.585  1.00 76.25           C  
ANISOU 2454  C   LYS A 236     7140   8710  13121   -882    814   1447       C  
ATOM   2455  O   LYS A 236      63.718   5.345   1.253  1.00 80.81           O  
ANISOU 2455  O   LYS A 236     7425   9382  13897   -925    912   1559       O  
ATOM   2456  CB  LYS A 236      60.953   7.049   0.969  1.00 71.04           C  
ANISOU 2456  CB  LYS A 236     6931   7902  12160  -1045    901   1439       C  
ATOM   2457  CG  LYS A 236      60.470   7.267   2.383  1.00 79.45           C  
ANISOU 2457  CG  LYS A 236     8134   8843  13212  -1158    612   1374       C  
ATOM   2458  CD  LYS A 236      60.091   8.725   2.596  1.00 83.93           C  
ANISOU 2458  CD  LYS A 236     8870   9291  13730  -1358    562   1411       C  
ATOM   2459  CE  LYS A 236      59.506   8.953   3.979  1.00 88.70           C  
ANISOU 2459  CE  LYS A 236     9652   9762  14288  -1455    297   1330       C  
ATOM   2460  NZ  LYS A 236      60.465   8.593   5.059  1.00107.31           N  
ANISOU 2460  NZ  LYS A 236    11817  12127  16829  -1550     87   1355       N  
ATOM   2461  N   HIS A 237      62.192   4.651   2.752  1.00 76.93           N  
ANISOU 2461  N   HIS A 237     7306   8726  13200   -878    562   1366       N  
ATOM   2462  CA  HIS A 237      63.222   4.205   3.683  1.00 78.34           C  
ANISOU 2462  CA  HIS A 237     7234   8929  13605   -925    373   1411       C  
ATOM   2463  C   HIS A 237      64.067   3.103   3.056  1.00 80.80           C  
ANISOU 2463  C   HIS A 237     7281   9368  14050   -722    518   1434       C  
ATOM   2464  O   HIS A 237      65.301   3.129   3.131  1.00 88.19           O  
ANISOU 2464  O   HIS A 237     7893  10383  15231   -768    517   1540       O  
ATOM   2465  CB  HIS A 237      62.587   3.723   4.985  1.00 78.06           C  
ANISOU 2465  CB  HIS A 237     7374   8788  13496   -940     88   1313       C  
ATOM   2466  CG  HIS A 237      63.585   3.345   6.035  1.00 90.92           C  
ANISOU 2466  CG  HIS A 237     8781  10424  15342  -1009   -147   1363       C  
ATOM   2467  ND1 HIS A 237      64.009   4.225   7.008  1.00 94.00           N  
ANISOU 2467  ND1 HIS A 237     9142  10743  15829  -1252   -365   1423       N  
ATOM   2468  CD2 HIS A 237      64.257   2.190   6.253  1.00 89.23           C  
ANISOU 2468  CD2 HIS A 237     8366  10270  15267   -868   -209   1366       C  
ATOM   2469  CE1 HIS A 237      64.890   3.623   7.787  1.00 95.99           C  
ANISOU 2469  CE1 HIS A 237     9183  11019  16270  -1264   -562   1465       C  
ATOM   2470  NE2 HIS A 237      65.058   2.388   7.351  1.00 87.54           N  
ANISOU 2470  NE2 HIS A 237     7999  10027  15234  -1027   -470   1434       N  
ATOM   2471  N   LEU A 238      63.418   2.123   2.423  1.00 87.67           N  
ANISOU 2471  N   LEU A 238     8284  10259  14768   -494    645   1336       N  
ATOM   2472  CA  LEU A 238      64.164   1.040   1.792  1.00 97.54           C  
ANISOU 2472  CA  LEU A 238     9318  11616  16127   -278    798   1342       C  
ATOM   2473  C   LEU A 238      65.020   1.569   0.649  1.00102.69           C  
ANISOU 2473  C   LEU A 238     9751  12388  16880   -281   1089   1453       C  
ATOM   2474  O   LEU A 238      66.121   1.061   0.407  1.00103.88           O  
ANISOU 2474  O   LEU A 238     9593  12641  17236   -188   1183   1515       O  
ATOM   2475  CB  LEU A 238      63.203  -0.039   1.296  1.00 90.73           C  
ANISOU 2475  CB  LEU A 238     8692  10731  15051    -49    875   1208       C  
ATOM   2476  CG  LEU A 238      62.473  -0.812   2.397  1.00 84.58           C  
ANISOU 2476  CG  LEU A 238     8092   9851  14192    -19    605   1105       C  
ATOM   2477  CD1 LEU A 238      61.351  -1.655   1.811  1.00 92.36           C  
ANISOU 2477  CD1 LEU A 238     9351  10805  14938    161    688    981       C  
ATOM   2478  CD2 LEU A 238      63.439  -1.683   3.181  1.00 92.70           C  
ANISOU 2478  CD2 LEU A 238     8881  10898  15442     45    440   1130       C  
ATOM   2479  N   LEU A 239      64.530   2.587  -0.062  1.00 95.91           N  
ANISOU 2479  N   LEU A 239     9045  11515  15881   -386   1237   1482       N  
ATOM   2480  CA  LEU A 239      65.285   3.195  -1.150  1.00100.11           C  
ANISOU 2480  CA  LEU A 239     9398  12154  16485   -418   1518   1597       C  
ATOM   2481  C   LEU A 239      66.421   4.066  -0.631  1.00 98.97           C  
ANISOU 2481  C   LEU A 239     8957  12044  16604   -645   1437   1746       C  
ATOM   2482  O   LEU A 239      67.322   4.418  -1.401  1.00103.20           O  
ANISOU 2482  O   LEU A 239     9253  12691  17266   -673   1660   1861       O  
ATOM   2483  CB  LEU A 239      64.357   4.026  -2.039  1.00 93.04           C  
ANISOU 2483  CB  LEU A 239     8787  11217  15346   -469   1676   1589       C  
ATOM   2484  CG  LEU A 239      63.732   3.326  -3.249  1.00 90.91           C  
ANISOU 2484  CG  LEU A 239     8697  10987  14858   -244   1917   1509       C  
ATOM   2485  CD1 LEU A 239      62.833   2.168  -2.843  1.00 92.21           C  
ANISOU 2485  CD1 LEU A 239     9063  11087  14885    -68   1777   1356       C  
ATOM   2486  CD2 LEU A 239      62.953   4.334  -4.087  1.00 90.26           C  
ANISOU 2486  CD2 LEU A 239     8863  10864  14567   -333   2049   1534       C  
ATOM   2487  N   LYS A 240      66.395   4.423   0.652  1.00 87.46           N  
ANISOU 2487  N   LYS A 240     7514  10492  15223   -814   1125   1747       N  
ATOM   2488  CA  LYS A 240      67.402   5.285   1.252  1.00 86.71           C  
ANISOU 2488  CA  LYS A 240     7170  10409  15368  -1058    998   1884       C  
ATOM   2489  C   LYS A 240      68.586   4.535   1.849  1.00 96.77           C  
ANISOU 2489  C   LYS A 240     8076  11765  16928  -1013    880   1943       C  
ATOM   2490  O   LYS A 240      69.603   5.170   2.152  1.00 96.92           O  
ANISOU 2490  O   LYS A 240     7817  11826  17180  -1201    814   2079       O  
ATOM   2491  CB  LYS A 240      66.766   6.145   2.354  1.00 85.93           C  
ANISOU 2491  CB  LYS A 240     7307  10151  15193  -1281    709   1856       C  
ATOM   2492  CG  LYS A 240      65.945   7.319   1.842  1.00 85.20           C  
ANISOU 2492  CG  LYS A 240     7491   9975  14907  -1407    807   1859       C  
ATOM   2493  CD  LYS A 240      65.047   7.928   2.923  1.00 85.31           C  
ANISOU 2493  CD  LYS A 240     7804   9816  14794  -1551    539   1783       C  
ATOM   2494  CE  LYS A 240      65.822   8.367   4.164  1.00 90.53           C  
ANISOU 2494  CE  LYS A 240     8324  10423  15650  -1775    251   1847       C  
ATOM   2495  NZ  LYS A 240      66.060   7.256   5.131  1.00 92.58           N  
ANISOU 2495  NZ  LYS A 240     8491  10693  15993  -1682     34   1789       N  
ATOM   2496  N   THR A 241      68.488   3.219   2.052  1.00101.10           N  
ANISOU 2496  N   THR A 241     8610  12329  17473   -778    835   1850       N  
ATOM   2497  CA  THR A 241      69.555   2.526   2.767  1.00107.79           C  
ANISOU 2497  CA  THR A 241     9127  13232  18597   -739    671   1906       C  
ATOM   2498  C   THR A 241      70.775   2.260   1.889  1.00119.12           C  
ANISOU 2498  C   THR A 241    10160  14838  20263   -632    934   2017       C  
ATOM   2499  O   THR A 241      71.900   2.610   2.262  1.00125.44           O  
ANISOU 2499  O   THR A 241    10611  15705  21344   -766    852   2154       O  
ATOM   2500  CB  THR A 241      69.030   1.196   3.319  1.00111.97           C  
ANISOU 2500  CB  THR A 241     9793  13703  19046   -524    521   1773       C  
ATOM   2501  OG1 THR A 241      68.531   0.396   2.237  1.00110.09           O  
ANISOU 2501  OG1 THR A 241     9675  13507  18645   -261    794   1682       O  
ATOM   2502  CG2 THR A 241      67.923   1.425   4.335  1.00104.52           C  
ANISOU 2502  CG2 THR A 241     9208  12602  17903   -643    247   1676       C  
ATOM   2503  N   ASN A 242      70.579   1.648   0.725  1.00141.85           N  
ANISOU 2503  N   ASN A 242    13078  17788  23028   -394   1251   1962       N  
ATOM   2504  CA  ASN A 242      71.701   1.172  -0.079  1.00145.10           C  
ANISOU 2504  CA  ASN A 242    13122  18363  23648   -237   1517   2044       C  
ATOM   2505  C   ASN A 242      71.224   0.939  -1.508  1.00144.73           C  
ANISOU 2505  C   ASN A 242    13243  18369  23380    -51   1898   1982       C  
ATOM   2506  O   ASN A 242      70.068   1.205  -1.852  1.00142.05           O  
ANISOU 2506  O   ASN A 242    13282  17942  22747    -63   1932   1891       O  
ATOM   2507  CB  ASN A 242      72.341  -0.073   0.538  1.00146.37           C  
ANISOU 2507  CB  ASN A 242    13052  18549  24015    -37   1373   2022       C  
ATOM   2508  CG  ASN A 242      73.707   0.222   1.133  1.00149.72           C  
ANISOU 2508  CG  ASN A 242    13016  19061  24812   -171   1243   2187       C  
ATOM   2509  OD1 ASN A 242      74.700   0.327   0.413  1.00155.43           O  
ANISOU 2509  OD1 ASN A 242    13391  19933  25733   -131   1492   2299       O  
ATOM   2510  ND2 ASN A 242      73.758   0.385   2.450  1.00149.22           N  
ANISOU 2510  ND2 ASN A 242    12949  18905  24841   -340    852   2207       N  
ATOM   2511  N   SER A 243      72.143   0.442  -2.350  1.00150.12           N  
ANISOU 2511  N   SER A 243    13634  19197  24209    125   2188   2035       N  
ATOM   2512  CA  SER A 243      71.837   0.188  -3.753  1.00148.36           C  
ANISOU 2512  CA  SER A 243    13552  19034  23783    307   2571   1983       C  
ATOM   2513  C   SER A 243      72.488  -1.092  -4.274  1.00155.95           C  
ANISOU 2513  C   SER A 243    14315  20088  24849    634   2775   1940       C  
ATOM   2514  O   SER A 243      72.619  -1.255  -5.494  1.00154.51           O  
ANISOU 2514  O   SER A 243    14146  19993  24568    780   3140   1931       O  
ATOM   2515  CB  SER A 243      72.291   1.366  -4.625  1.00142.08           C  
ANISOU 2515  CB  SER A 243    12645  18337  23004    125   2838   2124       C  
ATOM   2516  OG  SER A 243      73.707   1.466  -4.649  1.00145.94           O  
ANISOU 2516  OG  SER A 243    12650  18974  23828     94   2945   2275       O  
ATOM   2517  N   TYR A 244      72.896  -2.002  -3.390  1.00159.76           N  
ANISOU 2517  N   TYR A 244    14632  20548  25524    758   2551   1911       N  
ATOM   2518  CA  TYR A 244      73.565  -3.221  -3.826  1.00161.30           C  
ANISOU 2518  CA  TYR A 244    14626  20817  25844   1081   2731   1872       C  
ATOM   2519  C   TYR A 244      72.681  -3.998  -4.797  1.00159.83           C  
ANISOU 2519  C   TYR A 244    14807  20583  25340   1327   2953   1710       C  
ATOM   2520  O   TYR A 244      71.452  -3.883  -4.785  1.00157.25           O  
ANISOU 2520  O   TYR A 244    14892  20137  24719   1272   2852   1607       O  
ATOM   2521  CB  TYR A 244      73.904  -4.114  -2.630  1.00161.46           C  
ANISOU 2521  CB  TYR A 244    14498  20776  26073   1175   2396   1849       C  
ATOM   2522  CG  TYR A 244      74.944  -3.552  -1.689  1.00163.59           C  
ANISOU 2522  CG  TYR A 244    14362  21103  26692    972   2171   2013       C  
ATOM   2523  CD1 TYR A 244      76.298  -3.661  -1.972  1.00167.74           C  
ANISOU 2523  CD1 TYR A 244    14398  21787  27547   1051   2339   2142       C  
ATOM   2524  CD2 TYR A 244      74.571  -2.931  -0.505  1.00169.65           C  
ANISOU 2524  CD2 TYR A 244    15234  21764  27461    704   1785   2037       C  
ATOM   2525  CE1 TYR A 244      77.251  -3.155  -1.110  1.00169.87           C  
ANISOU 2525  CE1 TYR A 244    14286  22110  28146    854   2112   2300       C  
ATOM   2526  CE2 TYR A 244      75.517  -2.423   0.364  1.00163.72           C  
ANISOU 2526  CE2 TYR A 244    14133  21057  27019    507   1557   2186       C  
ATOM   2527  CZ  TYR A 244      76.855  -2.537   0.057  1.00167.83           C  
ANISOU 2527  CZ  TYR A 244    14160  21736  27871    577   1711   2321       C  
ATOM   2528  OH  TYR A 244      77.799  -2.031   0.920  1.00170.08           O  
ANISOU 2528  OH  TYR A 244    14085  22065  28473    368   1464   2477       O  
ATOM   2529  N   GLY A 245      73.323  -4.799  -5.648  1.00173.04           N  
ANISOU 2529  N   GLY A 245    16324  22349  27075   1604   3260   1688       N  
ATOM   2530  CA  GLY A 245      72.570  -5.630  -6.573  1.00165.49           C  
ANISOU 2530  CA  GLY A 245    15715  21340  25823   1851   3466   1530       C  
ATOM   2531  C   GLY A 245      71.877  -6.785  -5.876  1.00148.27           C  
ANISOU 2531  C   GLY A 245    13771  19007  23559   2014   3193   1380       C  
ATOM   2532  O   GLY A 245      70.764  -7.169  -6.247  1.00159.27           O  
ANISOU 2532  O   GLY A 245    15578  20295  24641   2083   3193   1245       O  
ATOM   2533  N   LYS A 246      72.523  -7.354  -4.856  1.00168.62           N  
ANISOU 2533  N   LYS A 246    16089  21566  26412   2071   2948   1411       N  
ATOM   2534  CA  LYS A 246      71.907  -8.428  -4.086  1.00166.68           C  
ANISOU 2534  CA  LYS A 246    16061  21168  26101   2203   2661   1286       C  
ATOM   2535  C   LYS A 246      70.919  -7.874  -3.067  1.00163.02           C  
ANISOU 2535  C   LYS A 246    15851  20585  25505   1939   2297   1269       C  
ATOM   2536  O   LYS A 246      69.799  -8.381  -2.940  1.00160.24           O  
ANISOU 2536  O   LYS A 246    15879  20103  24900   1980   2173   1139       O  
ATOM   2537  CB  LYS A 246      72.983  -9.264  -3.394  1.00169.35           C  
ANISOU 2537  CB  LYS A 246    16036  21528  26783   2372   2532   1331       C  
ATOM   2538  CG  LYS A 246      72.631  -9.689  -1.976  1.00167.44           C  
ANISOU 2538  CG  LYS A 246    15875  21149  26597   2301   2076   1307       C  
ATOM   2539  CD  LYS A 246      73.563 -10.774  -1.448  1.00170.11           C  
ANISOU 2539  CD  LYS A 246    15927  21480  27228   2538   1962   1324       C  
ATOM   2540  CE  LYS A 246      75.000 -10.641  -1.950  1.00174.51           C  
ANISOU 2540  CE  LYS A 246    15979  22213  28113   2647   2217   1452       C  
ATOM   2541  NZ  LYS A 246      75.646  -9.347  -1.602  1.00175.52           N  
ANISOU 2541  NZ  LYS A 246    15790  22460  28439   2342   2165   1629       N  
ATOM   2542  N   ASN A 247      71.316  -6.837  -2.324  1.00150.62           N  
ANISOU 2542  N   ASN A 247    14076  19051  24101   1664   2124   1399       N  
ATOM   2543  CA  ASN A 247      70.390  -6.232  -1.375  1.00135.46           C  
ANISOU 2543  CA  ASN A 247    12406  17016  22046   1413   1804   1380       C  
ATOM   2544  C   ASN A 247      69.132  -5.742  -2.076  1.00132.68           C  
ANISOU 2544  C   ASN A 247    12461  16612  21339   1342   1925   1297       C  
ATOM   2545  O   ASN A 247      68.095  -5.571  -1.425  1.00130.31           O  
ANISOU 2545  O   ASN A 247    12452  16195  20864   1217   1691   1233       O  
ATOM   2546  CB  ASN A 247      71.062  -5.076  -0.635  1.00143.94           C  
ANISOU 2546  CB  ASN A 247    13212  18140  23339   1121   1643   1536       C  
ATOM   2547  N   ARG A 248      69.205  -5.507  -3.389  1.00122.39           N  
ANISOU 2547  N   ARG A 248    11180  15394  19928   1420   2286   1301       N  
ATOM   2548  CA  ARG A 248      68.009  -5.168  -4.147  1.00112.49           C  
ANISOU 2548  CA  ARG A 248    10321  14088  18333   1385   2401   1220       C  
ATOM   2549  C   ARG A 248      66.973  -6.274  -4.015  1.00115.35           C  
ANISOU 2549  C   ARG A 248    11025  14323  18479   1549   2275   1056       C  
ATOM   2550  O   ARG A 248      65.777  -6.010  -3.844  1.00109.62           O  
ANISOU 2550  O   ARG A 248    10627  13504  17521   1443   2143    990       O  
ATOM   2551  CB  ARG A 248      68.355  -5.002  -5.624  1.00115.63           C  
ANISOU 2551  CB  ARG A 248    10691  14595  18646   1491   2818   1242       C  
ATOM   2552  CG  ARG A 248      67.279  -4.337  -6.465  1.00114.72           C  
ANISOU 2552  CG  ARG A 248    10935  14447  18207   1400   2943   1204       C  
ATOM   2553  CD  ARG A 248      67.371  -4.764  -7.922  1.00120.79           C  
ANISOU 2553  CD  ARG A 248    11800  15282  18814   1604   3322   1159       C  
ATOM   2554  NE  ARG A 248      66.789  -6.097  -8.106  1.00123.65           N  
ANISOU 2554  NE  ARG A 248    12405  15557  19018   1854   3298    998       N  
ATOM   2555  CZ  ARG A 248      67.460  -7.237  -8.256  1.00125.87           C  
ANISOU 2555  CZ  ARG A 248    12555  15857  19413   2117   3397    944       C  
ATOM   2556  NH1 ARG A 248      66.784  -8.367  -8.423  1.00134.17           N  
ANISOU 2556  NH1 ARG A 248    13887  16804  20287   2314   3351    795       N  
ATOM   2557  NH2 ARG A 248      68.785  -7.267  -8.217  1.00135.28           N  
ANISOU 2557  NH2 ARG A 248    13335  17164  20899   2184   3532   1040       N  
ATOM   2558  N   ILE A 249      67.428  -7.527  -4.095  1.00142.99           N  
ANISOU 2558  N   ILE A 249    14448  17817  22064   1811   2313    994       N  
ATOM   2559  CA  ILE A 249      66.536  -8.676  -3.979  1.00149.40           C  
ANISOU 2559  CA  ILE A 249    15575  18502  22689   1975   2192    843       C  
ATOM   2560  C   ILE A 249      65.875  -8.709  -2.607  1.00131.26           C  
ANISOU 2560  C   ILE A 249    13398  16088  20386   1822   1796    822       C  
ATOM   2561  O   ILE A 249      64.661  -8.917  -2.489  1.00124.72           O  
ANISOU 2561  O   ILE A 249    12915  15158  19314   1788   1677    727       O  
ATOM   2562  CB  ILE A 249      67.316  -9.973  -4.268  1.00137.11           C  
ANISOU 2562  CB  ILE A 249    13879  16952  21264   2287   2305    794       C  
ATOM   2563  CG1 ILE A 249      67.664 -10.056  -5.757  1.00131.68           C  
ANISOU 2563  CG1 ILE A 249    13191  16355  20484   2460   2724    774       C  
ATOM   2564  CG2 ILE A 249      66.520 -11.193  -3.838  1.00138.37           C  
ANISOU 2564  CG2 ILE A 249    14328  16959  21288   2426   2099    657       C  
ATOM   2565  CD1 ILE A 249      69.093 -10.466  -6.032  1.00148.92           C  
ANISOU 2565  CD1 ILE A 249    14979  18649  22955   2656   2929    838       C  
ATOM   2566  N   THR A 250      66.658  -8.499  -1.548  1.00126.99           N  
ANISOU 2566  N   THR A 250    12575  15564  20112   1722   1587    915       N  
ATOM   2567  CA  THR A 250      66.081  -8.531  -0.210  1.00119.35           C  
ANISOU 2567  CA  THR A 250    11731  14487  19131   1574   1215    898       C  
ATOM   2568  C   THR A 250      65.168  -7.339   0.039  1.00113.92           C  
ANISOU 2568  C   THR A 250    11242  13769  18273   1304   1133    911       C  
ATOM   2569  O   THR A 250      64.158  -7.470   0.738  1.00113.72           O  
ANISOU 2569  O   THR A 250    11481  13638  18090   1223    915    842       O  
ATOM   2570  CB  THR A 250      67.190  -8.563   0.843  1.00122.05           C  
ANISOU 2570  CB  THR A 250    11727  14851  19794   1525   1002   1001       C  
ATOM   2571  OG1 THR A 250      68.075  -9.659   0.578  1.00124.60           O  
ANISOU 2571  OG1 THR A 250    11843  15204  20297   1796   1089    995       O  
ATOM   2572  CG2 THR A 250      66.599  -8.720   2.237  1.00104.43           C  
ANISOU 2572  CG2 THR A 250     9654  12497  17526   1387    617    975       C  
ATOM   2573  N   ARG A 251      65.500  -6.173  -0.516  1.00104.10           N  
ANISOU 2573  N   ARG A 251     9879  12614  17059   1165   1308   1002       N  
ATOM   2574  CA  ARG A 251      64.652  -5.004  -0.316  1.00 91.35           C  
ANISOU 2574  CA  ARG A 251     8459  10960  15289    922   1237   1016       C  
ATOM   2575  C   ARG A 251      63.406  -5.046  -1.196  1.00 82.03           C  
ANISOU 2575  C   ARG A 251     7636   9739  13794    976   1375    917       C  
ATOM   2576  O   ARG A 251      62.341  -4.586  -0.771  1.00 80.84           O  
ANISOU 2576  O   ARG A 251     7732   9509  13475    841   1232    876       O  
ATOM   2577  CB  ARG A 251      65.461  -3.719  -0.544  1.00 98.49           C  
ANISOU 2577  CB  ARG A 251     9118  11957  16345    737   1351   1157       C  
ATOM   2578  CG  ARG A 251      65.560  -3.204  -1.981  1.00101.25           C  
ANISOU 2578  CG  ARG A 251     9471  12398  16602    775   1709   1191       C  
ATOM   2579  CD  ARG A 251      64.871  -1.846  -2.146  1.00100.04           C  
ANISOU 2579  CD  ARG A 251     9495  12215  16301    543   1720   1231       C  
ATOM   2580  NE  ARG A 251      65.698  -0.894  -2.887  1.00105.56           N  
ANISOU 2580  NE  ARG A 251     9983  13020  17105    442   1951   1362       N  
ATOM   2581  CZ  ARG A 251      66.742  -0.249  -2.373  1.00108.05           C  
ANISOU 2581  CZ  ARG A 251     9984  13390  17681    283   1890   1491       C  
ATOM   2582  NH1 ARG A 251      67.099  -0.452  -1.111  1.00108.92           N  
ANISOU 2582  NH1 ARG A 251     9960  13456  17967    212   1594   1505       N  
ATOM   2583  NH2 ARG A 251      67.436   0.599  -3.122  1.00110.61           N  
ANISOU 2583  NH2 ARG A 251    10131  13811  18085    185   2117   1613       N  
ATOM   2584  N   ASP A 252      63.512  -5.592  -2.411  1.00 86.71           N  
ANISOU 2584  N   ASP A 252     8261  10382  14300   1174   1650    877       N  
ATOM   2585  CA  ASP A 252      62.341  -5.692  -3.276  1.00 83.38           C  
ANISOU 2585  CA  ASP A 252     8186   9919  13576   1226   1762    786       C  
ATOM   2586  C   ASP A 252      61.312  -6.667  -2.715  1.00 78.07           C  
ANISOU 2586  C   ASP A 252     7781   9128  12754   1297   1547    662       C  
ATOM   2587  O   ASP A 252      60.103  -6.432  -2.827  1.00 76.07           O  
ANISOU 2587  O   ASP A 252     7812   8814  12275   1227   1492    606       O  
ATOM   2588  CB  ASP A 252      62.764  -6.122  -4.681  1.00 85.66           C  
ANISOU 2588  CB  ASP A 252     8462  10285  13802   1425   2099    768       C  
ATOM   2589  CG  ASP A 252      63.520  -5.035  -5.422  1.00 91.78           C  
ANISOU 2589  CG  ASP A 252     9042  11175  14653   1329   2348    891       C  
ATOM   2590  OD1 ASP A 252      63.613  -3.906  -4.895  1.00 99.08           O  
ANISOU 2590  OD1 ASP A 252     9874  12110  15662   1099   2250    985       O  
ATOM   2591  OD2 ASP A 252      64.024  -5.311  -6.532  1.00 88.91           O  
ANISOU 2591  OD2 ASP A 252     8631  10891  14261   1481   2646    893       O  
ATOM   2592  N   GLN A 253      61.766  -7.767  -2.109  1.00 78.81           N  
ANISOU 2592  N   GLN A 253     7783   9186  12975   1433   1420    625       N  
ATOM   2593  CA  GLN A 253      60.819  -8.702  -1.511  1.00 79.85           C  
ANISOU 2593  CA  GLN A 253     8167   9200  12972   1481   1204    519       C  
ATOM   2594  C   GLN A 253      60.057  -8.060  -0.361  1.00 75.03           C  
ANISOU 2594  C   GLN A 253     7662   8526  12321   1253    938    531       C  
ATOM   2595  O   GLN A 253      58.895  -8.404  -0.118  1.00 76.16           O  
ANISOU 2595  O   GLN A 253     8078   8588  12273   1231    816    451       O  
ATOM   2596  CB  GLN A 253      61.533  -9.972  -1.050  1.00 86.64           C  
ANISOU 2596  CB  GLN A 253     8904  10024  13991   1667   1110    490       C  
ATOM   2597  CG  GLN A 253      61.798 -10.950  -2.184  1.00 76.89           C  
ANISOU 2597  CG  GLN A 253     7717   8799  12699   1935   1346    419       C  
ATOM   2598  CD  GLN A 253      62.246 -12.309  -1.693  1.00 88.58           C  
ANISOU 2598  CD  GLN A 253     9154  10205  14297   2131   1221    369       C  
ATOM   2599  OE1 GLN A 253      63.258 -12.431  -1.008  1.00106.05           O  
ANISOU 2599  OE1 GLN A 253    11080  12443  16770   2156   1127    440       O  
ATOM   2600  NE2 GLN A 253      61.485 -13.343  -2.037  1.00 88.62           N  
ANISOU 2600  NE2 GLN A 253     9449  10110  14112   2269   1205    251       N  
ATOM   2601  N   VAL A 254      60.685  -7.126   0.355  1.00 76.81           N  
ANISOU 2601  N   VAL A 254     7678   8787  12720   1080    848    630       N  
ATOM   2602  CA  VAL A 254      59.967  -6.403   1.399  1.00 74.04           C  
ANISOU 2602  CA  VAL A 254     7447   8372  12314    861    621    637       C  
ATOM   2603  C   VAL A 254      58.953  -5.454   0.774  1.00 64.87           C  
ANISOU 2603  C   VAL A 254     6495   7209  10944    756    731    624       C  
ATOM   2604  O   VAL A 254      57.806  -5.364   1.225  1.00 66.50           O  
ANISOU 2604  O   VAL A 254     6937   7342  10986    679    601    566       O  
ATOM   2605  CB  VAL A 254      60.956  -5.656   2.313  1.00 77.27           C  
ANISOU 2605  CB  VAL A 254     7592   8808  12961    699    487    746       C  
ATOM   2606  CG1 VAL A 254      60.206  -4.824   3.342  1.00 72.39           C  
ANISOU 2606  CG1 VAL A 254     7125   8115  12263    472    274    745       C  
ATOM   2607  CG2 VAL A 254      61.890  -6.638   3.004  1.00 78.48           C  
ANISOU 2607  CG2 VAL A 254     7544   8954  13322    804    340    763       C  
ATOM   2608  N   LEU A 255      59.358  -4.731  -0.273  1.00 67.71           N  
ANISOU 2608  N   LEU A 255     6769   7648  11310    754    974    683       N  
ATOM   2609  CA  LEU A 255      58.420  -3.863  -0.976  1.00 68.10           C  
ANISOU 2609  CA  LEU A 255     7023   7691  11160    674   1084    677       C  
ATOM   2610  C   LEU A 255      57.270  -4.664  -1.573  1.00 65.14           C  
ANISOU 2610  C   LEU A 255     6935   7271  10544    801   1113    568       C  
ATOM   2611  O   LEU A 255      56.113  -4.232  -1.525  1.00 67.43           O  
ANISOU 2611  O   LEU A 255     7444   7511  10664    718   1049    535       O  
ATOM   2612  CB  LEU A 255      59.149  -3.082  -2.069  1.00 70.38           C  
ANISOU 2612  CB  LEU A 255     7172   8074  11495    664   1352    766       C  
ATOM   2613  CG  LEU A 255      60.032  -1.925  -1.602  1.00 72.25           C  
ANISOU 2613  CG  LEU A 255     7173   8347  11930    474   1329    890       C  
ATOM   2614  CD1 LEU A 255      60.948  -1.455  -2.719  1.00 95.93           C  
ANISOU 2614  CD1 LEU A 255     9992  11455  15003    497   1616    982       C  
ATOM   2615  CD2 LEU A 255      59.168  -0.777  -1.112  1.00 70.85           C  
ANISOU 2615  CD2 LEU A 255     7167   8097  11655    270   1205    902       C  
ATOM   2616  N   LYS A 256      57.570  -5.835  -2.140  1.00 62.04           N  
ANISOU 2616  N   LYS A 256     6543   6891  10137   1005   1205    513       N  
ATOM   2617  CA  LYS A 256      56.513  -6.689  -2.671  1.00 65.97           C  
ANISOU 2617  CA  LYS A 256     7321   7334  10410   1119   1207    407       C  
ATOM   2618  C   LYS A 256      55.498  -7.044  -1.593  1.00 65.60           C  
ANISOU 2618  C   LYS A 256     7440   7195  10290   1041    940    348       C  
ATOM   2619  O   LYS A 256      54.288  -7.062  -1.849  1.00 67.53           O  
ANISOU 2619  O   LYS A 256     7925   7399  10335   1017    907    294       O  
ATOM   2620  CB  LYS A 256      57.116  -7.954  -3.280  1.00 64.95           C  
ANISOU 2620  CB  LYS A 256     7164   7213  10302   1351   1322    352       C  
ATOM   2621  CG  LYS A 256      57.834  -7.720  -4.597  1.00 61.72           C  
ANISOU 2621  CG  LYS A 256     6672   6894   9887   1454   1634    387       C  
ATOM   2622  N   MET A 257      55.970  -7.333  -0.380  1.00 64.57           N  
ANISOU 2622  N   MET A 257     7181   7033  10318    997    746    362       N  
ATOM   2623  CA  MET A 257      55.069  -7.695   0.706  1.00 63.71           C  
ANISOU 2623  CA  MET A 257     7229   6840  10139    917    500    311       C  
ATOM   2624  C   MET A 257      54.347  -6.480   1.272  1.00 63.88           C  
ANISOU 2624  C   MET A 257     7319   6848  10105    713    420    341       C  
ATOM   2625  O   MET A 257      53.200  -6.599   1.720  1.00 61.27           O  
ANISOU 2625  O   MET A 257     7184   6461   9632    655    300    289       O  
ATOM   2626  CB  MET A 257      55.849  -8.407   1.812  1.00 66.08           C  
ANISOU 2626  CB  MET A 257     7386   7106  10616    937    315    322       C  
ATOM   2627  CG  MET A 257      56.530  -9.687   1.353  1.00 74.48           C  
ANISOU 2627  CG  MET A 257     8390   8163  11745   1158    374    286       C  
ATOM   2628  SD  MET A 257      57.922 -10.158   2.397  1.00 83.04           S  
ANISOU 2628  SD  MET A 257     9190   9244  13120   1192    216    347       S  
ATOM   2629  CE  MET A 257      57.066 -10.587   3.907  1.00 77.18           C  
ANISOU 2629  CE  MET A 257     8630   8389  12304   1063   -117    311       C  
ATOM   2630  N   ALA A 258      54.994  -5.312   1.265  1.00 66.04           N  
ANISOU 2630  N   ALA A 258     7434   7168  10491    603    487    426       N  
ATOM   2631  CA  ALA A 258      54.322  -4.094   1.702  1.00 62.41           C  
ANISOU 2631  CA  ALA A 258     7058   6682   9973    423    430    451       C  
ATOM   2632  C   ALA A 258      53.329  -3.604   0.657  1.00 62.67           C  
ANISOU 2632  C   ALA A 258     7272   6724   9816    436    573    433       C  
ATOM   2633  O   ALA A 258      52.303  -3.011   1.008  1.00 58.10           O  
ANISOU 2633  O   ALA A 258     6844   6101   9129    339    499    415       O  
ATOM   2634  CB  ALA A 258      55.350  -3.005   2.007  1.00 53.07           C  
ANISOU 2634  CB  ALA A 258     5663   5531   8971    291    444    550       C  
ATOM   2635  N   ALA A 259      53.615  -3.838  -0.624  1.00 64.41           N  
ANISOU 2635  N   ALA A 259     7484   6999   9991    559    778    440       N  
ATOM   2636  CA  ALA A 259      52.710  -3.442  -1.694  1.00 58.94           C  
ANISOU 2636  CA  ALA A 259     6974   6312   9108    578    904    428       C  
ATOM   2637  C   ALA A 259      51.514  -4.372  -1.833  1.00 55.17           C  
ANISOU 2637  C   ALA A 259     6724   5791   8449    656    826    335       C  
ATOM   2638  O   ALA A 259      50.560  -4.024  -2.536  1.00 61.06           O  
ANISOU 2638  O   ALA A 259     7638   6531   9032    650    875    325       O  
ATOM   2639  CB  ALA A 259      53.465  -3.384  -3.025  1.00 64.54           C  
ANISOU 2639  CB  ALA A 259     7612   7094   9814    676   1154    469       C  
ATOM   2640  N   ALA A 260      51.537  -5.538  -1.186  1.00 59.39           N  
ANISOU 2640  N   ALA A 260     7268   6289   9009    722    695    274       N  
ATOM   2641  CA  ALA A 260      50.419  -6.467  -1.294  1.00 57.36           C  
ANISOU 2641  CA  ALA A 260     7226   5984   8585    779    611    191       C  
ATOM   2642  C   ALA A 260      49.277  -6.072  -0.364  1.00 61.53           C  
ANISOU 2642  C   ALA A 260     7862   6468   9049    645    442    176       C  
ATOM   2643  O   ALA A 260      48.108  -6.110  -0.763  1.00 60.97           O  
ANISOU 2643  O   ALA A 260     7964   6383   8820    639    428    144       O  
ATOM   2644  CB  ALA A 260      50.888  -7.891  -0.989  1.00 57.81           C  
ANISOU 2644  CB  ALA A 260     7267   6007   8691    901    538    136       C  
ATOM   2645  N   VAL A 261      49.594  -5.696   0.878  1.00 61.54           N  
ANISOU 2645  N   VAL A 261     7765   6448   9171    536    314    199       N  
ATOM   2646  CA  VAL A 261      48.550  -5.302   1.819  1.00 61.45           C  
ANISOU 2646  CA  VAL A 261     7857   6395   9097    413    173    181       C  
ATOM   2647  C   VAL A 261      47.796  -4.085   1.300  1.00 61.27           C  
ANISOU 2647  C   VAL A 261     7903   6384   8991    348    258    211       C  
ATOM   2648  O   VAL A 261      46.568  -3.996   1.426  1.00 61.73           O  
ANISOU 2648  O   VAL A 261     8101   6423   8933    314    203    181       O  
ATOM   2649  CB  VAL A 261      49.150  -5.041   3.215  1.00 61.98           C  
ANISOU 2649  CB  VAL A 261     7819   6432   9300    304     30    203       C  
ATOM   2650  CG1 VAL A 261      49.737  -6.322   3.789  1.00 63.05           C  
ANISOU 2650  CG1 VAL A 261     7910   6542   9504    371    -86    175       C  
ATOM   2651  CG2 VAL A 261      50.207  -3.946   3.156  1.00 65.25           C  
ANISOU 2651  CG2 VAL A 261     8060   6875   9858    240    106    279       C  
ATOM   2652  N   VAL A 262      48.512  -3.131   0.702  1.00 50.28           N  
ANISOU 2652  N   VAL A 262     6412   5025   7667    330    391    276       N  
ATOM   2653  CA  VAL A 262      47.862  -1.917   0.222  1.00 57.54           C  
ANISOU 2653  CA  VAL A 262     7402   5942   8517    268    464    314       C  
ATOM   2654  C   VAL A 262      47.012  -2.213  -1.007  1.00 55.93           C  
ANISOU 2654  C   VAL A 262     7344   5758   8147    359    550    295       C  
ATOM   2655  O   VAL A 262      45.923  -1.652  -1.173  1.00 52.72           O  
ANISOU 2655  O   VAL A 262     7054   5334   7642    325    531    297       O  
ATOM   2656  CB  VAL A 262      48.911  -0.824  -0.060  1.00 56.77           C  
ANISOU 2656  CB  VAL A 262     7166   5867   8539    207    575    399       C  
ATOM   2657  CG1 VAL A 262      49.861  -1.256  -1.168  1.00 64.70           C  
ANISOU 2657  CG1 VAL A 262     8078   6934   9570    313    742    428       C  
ATOM   2658  CG2 VAL A 262      48.227   0.486  -0.422  1.00 60.92           C  
ANISOU 2658  CG2 VAL A 262     7779   6367   9000    133    626    441       C  
ATOM   2659  N   LEU A 263      47.487  -3.101  -1.884  1.00 55.02           N  
ANISOU 2659  N   LEU A 263     7231   5677   7999    479    640    278       N  
ATOM   2660  CA  LEU A 263      46.717  -3.444  -3.075  1.00 50.57           C  
ANISOU 2660  CA  LEU A 263     6828   5124   7261    561    709    256       C  
ATOM   2661  C   LEU A 263      45.554  -4.372  -2.746  1.00 52.15           C  
ANISOU 2661  C   LEU A 263     7172   5290   7352    577    562    185       C  
ATOM   2662  O   LEU A 263      44.450  -4.196  -3.271  1.00 51.54           O  
ANISOU 2662  O   LEU A 263     7230   5209   7143    571    544    182       O  
ATOM   2663  CB  LEU A 263      47.624  -4.086  -4.124  1.00 50.52           C  
ANISOU 2663  CB  LEU A 263     6798   5156   7241    687    865    253       C  
ATOM   2664  CG  LEU A 263      48.089  -3.149  -5.240  1.00 52.18           C  
ANISOU 2664  CG  LEU A 263     6992   5411   7425    689   1061    327       C  
ATOM   2665  CD1 LEU A 263      48.804  -1.935  -4.669  1.00 60.07           C  
ANISOU 2665  CD1 LEU A 263     7823   6420   8582    571   1087    408       C  
ATOM   2666  CD2 LEU A 263      48.986  -3.893  -6.219  1.00 49.88           C  
ANISOU 2666  CD2 LEU A 263     6681   5160   7110    824   1231    314       C  
ATOM   2667  N   ALA A 264      45.781  -5.367  -1.886  1.00 52.96           N  
ANISOU 2667  N   ALA A 264     7245   5368   7512    592    449    135       N  
ATOM   2668  CA  ALA A 264      44.704  -6.271  -1.502  1.00 47.88           C  
ANISOU 2668  CA  ALA A 264     6733   4689   6770    588    305     75       C  
ATOM   2669  C   ALA A 264      43.580  -5.545  -0.776  1.00 45.19           C  
ANISOU 2669  C   ALA A 264     6431   4338   6403    473    211     86       C  
ATOM   2670  O   ALA A 264      42.439  -6.019  -0.790  1.00 48.59           O  
ANISOU 2670  O   ALA A 264     6978   4757   6727    462    128     56       O  
ATOM   2671  CB  ALA A 264      45.252  -7.397  -0.624  1.00 53.10           C  
ANISOU 2671  CB  ALA A 264     7352   5314   7508    615    197     32       C  
ATOM   2672  N   PHE A 265      43.872  -4.411  -0.140  1.00 45.38           N  
ANISOU 2672  N   PHE A 265     6360   4362   6522    388    224    129       N  
ATOM   2673  CA  PHE A 265      42.826  -3.676   0.561  1.00 45.92           C  
ANISOU 2673  CA  PHE A 265     6469   4413   6565    296    154    133       C  
ATOM   2674  C   PHE A 265      41.930  -2.913  -0.408  1.00 42.05           C  
ANISOU 2674  C   PHE A 265     6059   3939   5980    310    221    165       C  
ATOM   2675  O   PHE A 265      40.704  -2.918  -0.255  1.00 48.30           O  
ANISOU 2675  O   PHE A 265     6927   4728   6698    287    154    151       O  
ATOM   2676  CB  PHE A 265      43.451  -2.718   1.574  1.00 46.85           C  
ANISOU 2676  CB  PHE A 265     6485   4507   6806    202    139    160       C  
ATOM   2677  CG  PHE A 265      42.448  -2.004   2.434  1.00 45.28           C  
ANISOU 2677  CG  PHE A 265     6338   4281   6584    116     74    151       C  
ATOM   2678  CD1 PHE A 265      41.882  -2.634   3.529  1.00 46.87           C  
ANISOU 2678  CD1 PHE A 265     6579   4464   6764     69    -46    105       C  
ATOM   2679  CD2 PHE A 265      42.076  -0.700   2.151  1.00 44.49           C  
ANISOU 2679  CD2 PHE A 265     6252   4169   6483     87    141    191       C  
ATOM   2680  CE1 PHE A 265      40.961  -1.978   4.324  1.00 45.87           C  
ANISOU 2680  CE1 PHE A 265     6498   4317   6612     -1    -82     93       C  
ATOM   2681  CE2 PHE A 265      41.157  -0.039   2.942  1.00 45.60           C  
ANISOU 2681  CE2 PHE A 265     6441   4278   6606     27     96    177       C  
ATOM   2682  CZ  PHE A 265      40.598  -0.678   4.030  1.00 45.87           C  
ANISOU 2682  CZ  PHE A 265     6507   4304   6616    -14     -7    126       C  
ATOM   2683  N   ILE A 266      42.516  -2.257  -1.409  1.00 43.82           N  
ANISOU 2683  N   ILE A 266     6264   4181   6206    345    352    215       N  
ATOM   2684  CA  ILE A 266      41.705  -1.482  -2.341  1.00 45.90           C  
ANISOU 2684  CA  ILE A 266     6612   4451   6377    356    404    257       C  
ATOM   2685  C   ILE A 266      40.979  -2.397  -3.320  1.00 46.16           C  
ANISOU 2685  C   ILE A 266     6772   4503   6263    430    385    231       C  
ATOM   2686  O   ILE A 266      39.862  -2.089  -3.750  1.00 50.23           O  
ANISOU 2686  O   ILE A 266     7373   5020   6693    427    347    249       O  
ATOM   2687  CB  ILE A 266      42.565  -0.439  -3.076  1.00 45.57           C  
ANISOU 2687  CB  ILE A 266     6524   4415   6375    353    548    329       C  
ATOM   2688  CG1 ILE A 266      43.491  -1.104  -4.095  1.00 49.44           C  
ANISOU 2688  CG1 ILE A 266     7009   4943   6832    437    665    332       C  
ATOM   2689  CG2 ILE A 266      43.385   0.371  -2.080  1.00 45.17           C  
ANISOU 2689  CG2 ILE A 266     6348   4339   6476    265    548    354       C  
ATOM   2690  CD1 ILE A 266      42.906  -1.194  -5.498  1.00 60.17           C  
ANISOU 2690  CD1 ILE A 266     8515   6319   8028    503    727    350       C  
ATOM   2691  N   ILE A 267      41.590  -3.523  -3.695  1.00 45.64           N  
ANISOU 2691  N   ILE A 267     6725   4446   6169    500    405    190       N  
ATOM   2692  CA  ILE A 267      40.935  -4.441  -4.621  1.00 44.97           C  
ANISOU 2692  CA  ILE A 267     6788   4365   5935    564    376    158       C  
ATOM   2693  C   ILE A 267      39.678  -5.021  -3.987  1.00 48.54           C  
ANISOU 2693  C   ILE A 267     7298   4802   6342    517    213    122       C  
ATOM   2694  O   ILE A 267      38.659  -5.220  -4.659  1.00 52.47           O  
ANISOU 2694  O   ILE A 267     7910   5305   6722    522    158    125       O  
ATOM   2695  CB  ILE A 267      41.909  -5.554  -5.053  1.00 50.12           C  
ANISOU 2695  CB  ILE A 267     7457   5013   6574    657    435    112       C  
ATOM   2696  CG1 ILE A 267      43.007  -4.993  -5.963  1.00 47.62           C  
ANISOU 2696  CG1 ILE A 267     7096   4726   6272    713    626    155       C  
ATOM   2697  CG2 ILE A 267      41.155  -6.685  -5.741  1.00 51.31           C  
ANISOU 2697  CG2 ILE A 267     7783   5143   6568    709    364     59       C  
ATOM   2698  CD1 ILE A 267      42.514  -4.504  -7.313  1.00 68.94           C  
ANISOU 2698  CD1 ILE A 267     9934   7441   8818    737    706    195       C  
ATOM   2699  N   CYS A 268      39.729  -5.296  -2.682  1.00 47.88           N  
ANISOU 2699  N   CYS A 268     7138   4703   6350    461    128     93       N  
ATOM   2700  CA  CYS A 268      38.608  -5.941  -2.012  1.00 42.80           C  
ANISOU 2700  CA  CYS A 268     6543   4051   5667    408    -15     62       C  
ATOM   2701  C   CYS A 268      37.550  -4.941  -1.563  1.00 44.31           C  
ANISOU 2701  C   CYS A 268     6706   4259   5872    339    -45     97       C  
ATOM   2702  O   CYS A 268      36.358  -5.268  -1.568  1.00 54.05           O  
ANISOU 2702  O   CYS A 268     7991   5505   7041    311   -133     94       O  
ATOM   2703  CB  CYS A 268      39.108  -6.739  -0.806  1.00 46.39           C  
ANISOU 2703  CB  CYS A 268     6949   4478   6198    376    -93     19       C  
ATOM   2704  SG  CYS A 268      40.136  -8.172  -1.221  1.00 48.46           S  
ANISOU 2704  SG  CYS A 268     7259   4707   6449    474    -91    -33       S  
ATOM   2705  N   TRP A 269      37.953  -3.730  -1.177  1.00 38.98           N  
ANISOU 2705  N   TRP A 269     5948   3579   5284    313     25    132       N  
ATOM   2706  CA  TRP A 269      37.043  -2.780  -0.550  1.00 47.00           C  
ANISOU 2706  CA  TRP A 269     6936   4594   6329    258      3    154       C  
ATOM   2707  C   TRP A 269      36.636  -1.612  -1.432  1.00 43.40           C  
ANISOU 2707  C   TRP A 269     6498   4140   5851    287     71    215       C  
ATOM   2708  O   TRP A 269      35.551  -1.062  -1.231  1.00 39.78           O  
ANISOU 2708  O   TRP A 269     6041   3686   5387    272     36    234       O  
ATOM   2709  CB  TRP A 269      37.660  -2.238   0.744  1.00 44.40           C  
ANISOU 2709  CB  TRP A 269     6525   4235   6109    195      8    141       C  
ATOM   2710  CG  TRP A 269      37.600  -3.241   1.843  1.00 46.09           C  
ANISOU 2710  CG  TRP A 269     6736   4443   6332    147    -90     90       C  
ATOM   2711  CD1 TRP A 269      38.646  -3.887   2.429  1.00 47.51           C  
ANISOU 2711  CD1 TRP A 269     6882   4602   6566    135   -119     63       C  
ATOM   2712  CD2 TRP A 269      36.415  -3.732   2.478  1.00 49.83           C  
ANISOU 2712  CD2 TRP A 269     7242   4932   6759    102   -174     67       C  
ATOM   2713  NE1 TRP A 269      38.187  -4.746   3.399  1.00 51.04           N  
ANISOU 2713  NE1 TRP A 269     7357   5042   6993     82   -224     25       N  
ATOM   2714  CE2 TRP A 269      36.819  -4.669   3.447  1.00 52.69           C  
ANISOU 2714  CE2 TRP A 269     7606   5275   7137     56   -252     27       C  
ATOM   2715  CE3 TRP A 269      35.051  -3.467   2.322  1.00 50.95           C  
ANISOU 2715  CE3 TRP A 269     7401   5103   6853     95   -193     83       C  
ATOM   2716  CZ2 TRP A 269      35.908  -5.341   4.257  1.00 54.52           C  
ANISOU 2716  CZ2 TRP A 269     7871   5517   7328     -7   -337      4       C  
ATOM   2717  CZ3 TRP A 269      34.148  -4.134   3.128  1.00 52.16           C  
ANISOU 2717  CZ3 TRP A 269     7564   5275   6978     36   -271     60       C  
ATOM   2718  CH2 TRP A 269      34.580  -5.060   4.084  1.00 53.68           C  
ANISOU 2718  CH2 TRP A 269     7772   5448   7176    -19   -338     21       C  
ATOM   2719  N   LEU A 270      37.465  -1.206  -2.390  1.00 43.88           N  
ANISOU 2719  N   LEU A 270     6573   4198   5901    329    169    252       N  
ATOM   2720  CA  LEU A 270      37.071  -0.103  -3.260  1.00 44.36           C  
ANISOU 2720  CA  LEU A 270     6672   4253   5930    351    224    320       C  
ATOM   2721  C   LEU A 270      35.773  -0.384  -4.008  1.00 44.85           C  
ANISOU 2721  C   LEU A 270     6818   4337   5884    381    147    337       C  
ATOM   2722  O   LEU A 270      34.976   0.555  -4.181  1.00 41.97           O  
ANISOU 2722  O   LEU A 270     6458   3962   5524    385    137    386       O  
ATOM   2723  CB  LEU A 270      38.200   0.218  -4.247  1.00 46.14           C  
ANISOU 2723  CB  LEU A 270     6912   4477   6140    384    349    360       C  
ATOM   2724  CG  LEU A 270      37.968   1.446  -5.131  1.00 44.04           C  
ANISOU 2724  CG  LEU A 270     6696   4194   5844    395    414    443       C  
ATOM   2725  CD1 LEU A 270      37.842   2.709  -4.288  1.00 41.47           C  
ANISOU 2725  CD1 LEU A 270     6311   3820   5627    343    418    470       C  
ATOM   2726  CD2 LEU A 270      39.084   1.592  -6.154  1.00 56.54           C  
ANISOU 2726  CD2 LEU A 270     8304   5788   7393    421    550    484       C  
ATOM   2727  N   PRO A 271      35.498  -1.606  -4.475  1.00 47.39           N  
ANISOU 2727  N   PRO A 271     7209   4683   6112    402     83    302       N  
ATOM   2728  CA  PRO A 271      34.204  -1.845  -5.144  1.00 41.49           C  
ANISOU 2728  CA  PRO A 271     6537   3957   5270    412    -16    326       C  
ATOM   2729  C   PRO A 271      33.003  -1.535  -4.264  1.00 40.04           C  
ANISOU 2729  C   PRO A 271     6280   3788   5147    371   -101    332       C  
ATOM   2730  O   PRO A 271      32.085  -0.826  -4.697  1.00 40.44           O  
ANISOU 2730  O   PRO A 271     6334   3845   5187    388   -132    389       O  
ATOM   2731  CB  PRO A 271      34.279  -3.334  -5.518  1.00 40.76           C  
ANISOU 2731  CB  PRO A 271     6532   3872   5082    422    -79    271       C  
ATOM   2732  CG  PRO A 271      35.737  -3.636  -5.592  1.00 46.34           C  
ANISOU 2732  CG  PRO A 271     7235   4562   5809    458     31    239       C  
ATOM   2733  CD  PRO A 271      36.382  -2.785  -4.540  1.00 46.34           C  
ANISOU 2733  CD  PRO A 271     7101   4551   5954    424     95    246       C  
ATOM   2734  N   PHE A 272      32.982  -2.048  -3.031  1.00 45.56           N  
ANISOU 2734  N   PHE A 272     6911   4490   5909    321   -136    279       N  
ATOM   2735  CA  PHE A 272      31.837  -1.818  -2.157  1.00 41.60           C  
ANISOU 2735  CA  PHE A 272     6339   4010   5458    283   -195    282       C  
ATOM   2736  C   PHE A 272      31.676  -0.340  -1.828  1.00 40.51           C  
ANISOU 2736  C   PHE A 272     6144   3847   5402    302   -123    319       C  
ATOM   2737  O   PHE A 272      30.555   0.182  -1.816  1.00 47.42           O  
ANISOU 2737  O   PHE A 272     6983   4740   6297    317   -156    355       O  
ATOM   2738  CB  PHE A 272      31.983  -2.627  -0.869  1.00 43.37           C  
ANISOU 2738  CB  PHE A 272     6522   4236   5719    218   -230    220       C  
ATOM   2739  CG  PHE A 272      31.069  -2.175   0.236  1.00 48.45           C  
ANISOU 2739  CG  PHE A 272     7087   4897   6425    177   -241    217       C  
ATOM   2740  CD1 PHE A 272      29.762  -2.630   0.305  1.00 48.19           C  
ANISOU 2740  CD1 PHE A 272     7026   4914   6370    150   -321    233       C  
ATOM   2741  CD2 PHE A 272      31.516  -1.288   1.204  1.00 47.52           C  
ANISOU 2741  CD2 PHE A 272     6924   4745   6387    163   -166    200       C  
ATOM   2742  CE1 PHE A 272      28.921  -2.213   1.319  1.00 47.40           C  
ANISOU 2742  CE1 PHE A 272     6843   4837   6327    121   -307    231       C  
ATOM   2743  CE2 PHE A 272      30.678  -0.867   2.218  1.00 47.25           C  
ANISOU 2743  CE2 PHE A 272     6835   4722   6397    135   -157    190       C  
ATOM   2744  CZ  PHE A 272      29.378  -1.331   2.276  1.00 50.49           C  
ANISOU 2744  CZ  PHE A 272     7207   5191   6786    120   -217    205       C  
ATOM   2745  N   HIS A 273      32.782   0.349  -1.546  1.00 45.70           N  
ANISOU 2745  N   HIS A 273     6789   4459   6116    300    -31    314       N  
ATOM   2746  CA  HIS A 273      32.685   1.731  -1.091  1.00 43.26           C  
ANISOU 2746  CA  HIS A 273     6445   4106   5886    307     30    340       C  
ATOM   2747  C   HIS A 273      32.317   2.678  -2.224  1.00 40.12           C  
ANISOU 2747  C   HIS A 273     6089   3690   5465    367     54    417       C  
ATOM   2748  O   HIS A 273      31.680   3.709  -1.980  1.00 45.37           O  
ANISOU 2748  O   HIS A 273     6732   4322   6183    394     68    447       O  
ATOM   2749  CB  HIS A 273      33.996   2.150  -0.431  1.00 44.59           C  
ANISOU 2749  CB  HIS A 273     6594   4226   6122    267    102    315       C  
ATOM   2750  CG  HIS A 273      34.190   1.563   0.932  1.00 47.91           C  
ANISOU 2750  CG  HIS A 273     6975   4647   6581    204     68    248       C  
ATOM   2751  ND1 HIS A 273      33.593   2.088   2.058  1.00 43.98           N  
ANISOU 2751  ND1 HIS A 273     6455   4129   6128    174     67    221       N  
ATOM   2752  CD2 HIS A 273      34.900   0.488   1.349  1.00 47.34           C  
ANISOU 2752  CD2 HIS A 273     6896   4590   6502    167     33    203       C  
ATOM   2753  CE1 HIS A 273      33.934   1.368   3.111  1.00 48.27           C  
ANISOU 2753  CE1 HIS A 273     6985   4676   6680    111     30    166       C  
ATOM   2754  NE2 HIS A 273      34.727   0.391   2.708  1.00 50.41           N  
ANISOU 2754  NE2 HIS A 273     7262   4966   6925    106      1    157       N  
ATOM   2755  N   VAL A 274      32.700   2.358  -3.460  1.00 40.38           N  
ANISOU 2755  N   VAL A 274     6194   3736   5413    395     59    452       N  
ATOM   2756  CA  VAL A 274      32.250   3.163  -4.591  1.00 42.12           C  
ANISOU 2756  CA  VAL A 274     6475   3940   5588    446     61    534       C  
ATOM   2757  C   VAL A 274      30.737   3.062  -4.729  1.00 45.80           C  
ANISOU 2757  C   VAL A 274     6921   4440   6040    474    -49    560       C  
ATOM   2758  O   VAL A 274      30.037   4.071  -4.869  1.00 46.67           O  
ANISOU 2758  O   VAL A 274     7017   4522   6192    518    -57    617       O  
ATOM   2759  CB  VAL A 274      32.964   2.727  -5.883  1.00 41.86           C  
ANISOU 2759  CB  VAL A 274     6544   3918   5443    464     94    560       C  
ATOM   2760  CG1 VAL A 274      32.318   3.385  -7.093  1.00 42.90           C  
ANISOU 2760  CG1 VAL A 274     6762   4038   5500    510     65    649       C  
ATOM   2761  CG2 VAL A 274      34.440   3.072  -5.814  1.00 47.94           C  
ANISOU 2761  CG2 VAL A 274     7304   4658   6252    442    222    556       C  
ATOM   2762  N   LEU A 275      30.208   1.838  -4.672  1.00 41.81           N  
ANISOU 2762  N   LEU A 275     6410   3992   5484    449   -140    524       N  
ATOM   2763  CA  LEU A 275      28.763   1.655  -4.726  1.00 41.67           C  
ANISOU 2763  CA  LEU A 275     6346   4019   5467    458   -253    554       C  
ATOM   2764  C   LEU A 275      28.086   2.305  -3.526  1.00 46.61           C  
ANISOU 2764  C   LEU A 275     6852   4643   6215    463   -229    541       C  
ATOM   2765  O   LEU A 275      26.997   2.878  -3.651  1.00 44.60           O  
ANISOU 2765  O   LEU A 275     6541   4402   6004    508   -273    593       O  
ATOM   2766  CB  LEU A 275      28.429   0.167  -4.801  1.00 41.48           C  
ANISOU 2766  CB  LEU A 275     6344   4048   5368    408   -355    515       C  
ATOM   2767  CG  LEU A 275      28.941  -0.546  -6.056  1.00 44.13           C  
ANISOU 2767  CG  LEU A 275     6823   4379   5565    414   -386    520       C  
ATOM   2768  CD1 LEU A 275      28.662  -2.040  -5.977  1.00 50.33           C  
ANISOU 2768  CD1 LEU A 275     7643   5195   6283    359   -489    469       C  
ATOM   2769  CD2 LEU A 275      28.327   0.048  -7.316  1.00 43.09           C  
ANISOU 2769  CD2 LEU A 275     6764   4244   5365    459   -444    608       C  
ATOM   2770  N   THR A 276      28.716   2.228  -2.352  1.00 45.65           N  
ANISOU 2770  N   THR A 276     6693   4504   6148    420   -160    473       N  
ATOM   2771  CA  THR A 276      28.154   2.880  -1.175  1.00 43.40           C  
ANISOU 2771  CA  THR A 276     6322   4209   5960    425   -118    450       C  
ATOM   2772  C   THR A 276      28.097   4.390  -1.368  1.00 44.56           C  
ANISOU 2772  C   THR A 276     6477   4284   6169    496    -54    497       C  
ATOM   2773  O   THR A 276      27.097   5.032  -1.023  1.00 49.03           O  
ANISOU 2773  O   THR A 276     6978   4850   6801    550    -52    517       O  
ATOM   2774  CB  THR A 276      28.979   2.524   0.061  1.00 39.80           C  
ANISOU 2774  CB  THR A 276     5858   3735   5529    356    -66    370       C  
ATOM   2775  OG1 THR A 276      28.887   1.115   0.308  1.00 39.32           O  
ANISOU 2775  OG1 THR A 276     5792   3731   5416    294   -137    331       O  
ATOM   2776  CG2 THR A 276      28.484   3.287   1.281  1.00 46.47           C  
ANISOU 2776  CG2 THR A 276     6647   4556   6454    361     -6    339       C  
ATOM   2777  N   PHE A 277      29.160   4.976  -1.922  1.00 49.44           N  
ANISOU 2777  N   PHE A 277     7174   4840   6771    501      3    519       N  
ATOM   2778  CA  PHE A 277      29.165   6.414  -2.165  1.00 49.94           C  
ANISOU 2778  CA  PHE A 277     7268   4819   6887    558     56    571       C  
ATOM   2779  C   PHE A 277      28.108   6.798  -3.191  1.00 49.12           C  
ANISOU 2779  C   PHE A 277     7170   4727   6768    638    -15    658       C  
ATOM   2780  O   PHE A 277      27.421   7.815  -3.037  1.00 47.03           O  
ANISOU 2780  O   PHE A 277     6880   4414   6577    710     -5    693       O  
ATOM   2781  CB  PHE A 277      30.551   6.866  -2.626  1.00 51.19           C  
ANISOU 2781  CB  PHE A 277     7508   4917   7026    526    128    589       C  
ATOM   2782  CG  PHE A 277      30.642   8.337  -2.908  1.00 47.33           C  
ANISOU 2782  CG  PHE A 277     7071   4328   6586    568    178    649       C  
ATOM   2783  CD1 PHE A 277      30.591   9.259  -1.877  1.00 49.35           C  
ANISOU 2783  CD1 PHE A 277     7314   4504   6933    573    227    616       C  
ATOM   2784  CD2 PHE A 277      30.778   8.799  -4.205  1.00 48.93           C  
ANISOU 2784  CD2 PHE A 277     7354   4506   6733    599    174    739       C  
ATOM   2785  CE1 PHE A 277      30.671  10.616  -2.134  1.00 48.49           C  
ANISOU 2785  CE1 PHE A 277     7272   4285   6869    611    266    671       C  
ATOM   2786  CE2 PHE A 277      30.860  10.154  -4.468  1.00 52.02           C  
ANISOU 2786  CE2 PHE A 277     7807   4793   7167    632    212    802       C  
ATOM   2787  CZ  PHE A 277      30.806  11.063  -3.430  1.00 47.42           C  
ANISOU 2787  CZ  PHE A 277     7210   4124   6686    639    255    768       C  
ATOM   2788  N   LEU A 278      27.964   5.995  -4.248  1.00 52.22           N  
ANISOU 2788  N   LEU A 278     7602   5176   7062    631    -95    695       N  
ATOM   2789  CA  LEU A 278      26.953   6.281  -5.261  1.00 51.08           C  
ANISOU 2789  CA  LEU A 278     7470   5045   6893    695   -192    784       C  
ATOM   2790  C   LEU A 278      25.552   6.178  -4.669  1.00 52.18           C  
ANISOU 2790  C   LEU A 278     7475   5238   7113    731   -260    787       C  
ATOM   2791  O   LEU A 278      24.701   7.043  -4.904  1.00 55.35           O  
ANISOU 2791  O   LEU A 278     7837   5615   7580    815   -292    853       O  
ATOM   2792  CB  LEU A 278      27.116   5.326  -6.443  1.00 44.58           C  
ANISOU 2792  CB  LEU A 278     6740   4270   5930    665   -271    810       C  
ATOM   2793  CG  LEU A 278      28.438   5.449  -7.202  1.00 44.58           C  
ANISOU 2793  CG  LEU A 278     6870   4227   5842    643   -188    820       C  
ATOM   2794  CD1 LEU A 278      28.596   4.311  -8.196  1.00 44.77           C  
ANISOU 2794  CD1 LEU A 278     6992   4300   5716    616   -251    818       C  
ATOM   2795  CD2 LEU A 278      28.538   6.793  -7.906  1.00 45.62           C  
ANISOU 2795  CD2 LEU A 278     7074   4279   5980    695   -154    912       C  
ATOM   2796  N   ASP A 279      25.293   5.118  -3.900  1.00 61.21           N  
ANISOU 2796  N   ASP A 279     8543   6456   8258    670   -281    721       N  
ATOM   2797  CA  ASP A 279      24.011   5.000  -3.215  1.00 61.04           C  
ANISOU 2797  CA  ASP A 279     8375   6495   8321    691   -320    722       C  
ATOM   2798  C   ASP A 279      23.739   6.231  -2.361  1.00 61.41           C  
ANISOU 2798  C   ASP A 279     8363   6481   8487    769   -217    712       C  
ATOM   2799  O   ASP A 279      22.599   6.705  -2.281  1.00 62.08           O  
ANISOU 2799  O   ASP A 279     8342   6588   8657    847   -243    756       O  
ATOM   2800  CB  ASP A 279      23.987   3.737  -2.355  1.00 61.20           C  
ANISOU 2800  CB  ASP A 279     8345   6589   8321    594   -331    647       C  
ATOM   2801  CG  ASP A 279      22.652   3.525  -1.665  1.00 64.58           C  
ANISOU 2801  CG  ASP A 279     8613   7095   8830    599   -361    656       C  
ATOM   2802  OD1 ASP A 279      21.673   3.167  -2.354  1.00 70.58           O  
ANISOU 2802  OD1 ASP A 279     9311   7918   9589    605   -483    724       O  
ATOM   2803  OD2 ASP A 279      22.582   3.716  -0.432  1.00 61.46           O  
ANISOU 2803  OD2 ASP A 279     8156   6700   8497    592   -261    597       O  
ATOM   2804  N   ALA A 280      24.777   6.762  -1.710  1.00 53.32           N  
ANISOU 2804  N   ALA A 280     7407   5377   7474    750   -103    653       N  
ATOM   2805  CA  ALA A 280      24.611   7.990  -0.940  1.00 54.14           C  
ANISOU 2805  CA  ALA A 280     7495   5399   7676    822     -6    636       C  
ATOM   2806  C   ALA A 280      24.231   9.152  -1.848  1.00 54.26           C  
ANISOU 2806  C   ALA A 280     7545   5341   7731    931    -31    728       C  
ATOM   2807  O   ALA A 280      23.374   9.971  -1.496  1.00 53.62           O  
ANISOU 2807  O   ALA A 280     7400   5227   7747   1034     -5    745       O  
ATOM   2808  CB  ALA A 280      25.893   8.308  -0.172  1.00 54.22           C  
ANISOU 2808  CB  ALA A 280     7594   5329   7679    759     94    563       C  
ATOM   2809  N   LEU A 281      24.859   9.241  -3.023  1.00 56.89           N  
ANISOU 2809  N   LEU A 281     7986   5643   7987    917    -76    791       N  
ATOM   2810  CA  LEU A 281      24.481  10.268  -3.985  1.00 53.78           C  
ANISOU 2810  CA  LEU A 281     7642   5178   7613   1011   -119    893       C  
ATOM   2811  C   LEU A 281      23.054  10.084  -4.476  1.00 48.64           C  
ANISOU 2811  C   LEU A 281     6883   4600   7000   1088   -240    964       C  
ATOM   2812  O   LEU A 281      22.438  11.051  -4.936  1.00 57.69           O  
ANISOU 2812  O   LEU A 281     8028   5684   8208   1196   -277   1044       O  
ATOM   2813  CB  LEU A 281      25.441  10.263  -5.175  1.00 59.30           C  
ANISOU 2813  CB  LEU A 281     8487   5845   8198    964   -138    949       C  
ATOM   2814  CG  LEU A 281      26.876  10.718  -4.904  1.00 46.84           C  
ANISOU 2814  CG  LEU A 281     7010   4184   6604    898    -21    911       C  
ATOM   2815  CD1 LEU A 281      27.729  10.503  -6.140  1.00 47.43           C  
ANISOU 2815  CD1 LEU A 281     7205   4258   6557    849    -30    970       C  
ATOM   2816  CD2 LEU A 281      26.915  12.175  -4.473  1.00 47.67           C  
ANISOU 2816  CD2 LEU A 281     7154   4153   6804    959     46    927       C  
ATOM   2817  N   ALA A 282      22.516   8.866  -4.389  1.00 54.13           N  
ANISOU 2817  N   ALA A 282     7485   5417   7664   1031   -314    944       N  
ATOM   2818  CA  ALA A 282      21.117   8.649  -4.739  1.00 49.44           C  
ANISOU 2818  CA  ALA A 282     6759   4903   7125   1087   -437   1014       C  
ATOM   2819  C   ALA A 282      20.195   9.228  -3.673  1.00 51.80           C  
ANISOU 2819  C   ALA A 282     6898   5207   7577   1179   -365    992       C  
ATOM   2820  O   ALA A 282      19.294  10.017  -3.979  1.00 52.64           O  
ANISOU 2820  O   ALA A 282     6930   5290   7779   1302   -409   1068       O  
ATOM   2821  CB  ALA A 282      20.852   7.157  -4.930  1.00 48.90           C  
ANISOU 2821  CB  ALA A 282     6648   4955   6977    980   -539    999       C  
ATOM   2822  N   TRP A 283      20.413   8.856  -2.408  1.00 54.28           N  
ANISOU 2822  N   TRP A 283     7164   5548   7913   1127   -251    888       N  
ATOM   2823  CA  TRP A 283      19.591   9.394  -1.330  1.00 51.35           C  
ANISOU 2823  CA  TRP A 283     6659   5181   7670   1214   -153    854       C  
ATOM   2824  C   TRP A 283      19.670  10.913  -1.276  1.00 56.58           C  
ANISOU 2824  C   TRP A 283     7384   5701   8411   1350    -75    869       C  
ATOM   2825  O   TRP A 283      18.734  11.567  -0.801  1.00 64.54           O  
ANISOU 2825  O   TRP A 283     8279   6700   9542   1476    -25    878       O  
ATOM   2826  CB  TRP A 283      20.018   8.797   0.009  1.00 50.57           C  
ANISOU 2826  CB  TRP A 283     6552   5114   7549   1121    -36    736       C  
ATOM   2827  CG  TRP A 283      19.700   7.344   0.142  1.00 60.32           C  
ANISOU 2827  CG  TRP A 283     7704   6485   8731   1002   -106    724       C  
ATOM   2828  CD1 TRP A 283      20.579   6.300   0.082  1.00 62.02           C  
ANISOU 2828  CD1 TRP A 283     8009   6724   8831    867   -143    680       C  
ATOM   2829  CD2 TRP A 283      18.407   6.768   0.355  1.00 60.08           C  
ANISOU 2829  CD2 TRP A 283     7481   6579   8767   1004   -153    760       C  
ATOM   2830  NE1 TRP A 283      19.911   5.111   0.249  1.00 64.52           N  
ANISOU 2830  NE1 TRP A 283     8223   7160   9130    782   -215    684       N  
ATOM   2831  CE2 TRP A 283      18.577   5.371   0.417  1.00 60.79           C  
ANISOU 2831  CE2 TRP A 283     7573   6756   8768    855   -223    736       C  
ATOM   2832  CE3 TRP A 283      17.121   7.298   0.501  1.00 63.42           C  
ANISOU 2832  CE3 TRP A 283     7724   7048   9325   1120   -140    814       C  
ATOM   2833  CZ2 TRP A 283      17.510   4.499   0.618  1.00 69.48           C  
ANISOU 2833  CZ2 TRP A 283     8509   7985   9904    799   -286    768       C  
ATOM   2834  CZ3 TRP A 283      16.065   6.431   0.701  1.00 68.53           C  
ANISOU 2834  CZ3 TRP A 283     8185   7836  10016   1070   -195    848       C  
ATOM   2835  CH2 TRP A 283      16.265   5.047   0.757  1.00 74.18           C  
ANISOU 2835  CH2 TRP A 283     8915   8635  10635    902   -270    827       C  
ATOM   2836  N   MET A 284      20.771  11.491  -1.750  1.00 54.68           N  
ANISOU 2836  N   MET A 284     7323   5345   8108   1328    -59    874       N  
ATOM   2837  CA  MET A 284      20.914  12.940  -1.773  1.00 55.77           C  
ANISOU 2837  CA  MET A 284     7549   5328   8312   1441      1    896       C  
ATOM   2838  C   MET A 284      20.260  13.578  -2.991  1.00 53.58           C  
ANISOU 2838  C   MET A 284     7272   5014   8070   1551   -119   1028       C  
ATOM   2839  O   MET A 284      20.150  14.807  -3.038  1.00 57.06           O  
ANISOU 2839  O   MET A 284     7772   5323   8585   1668    -86   1060       O  
ATOM   2840  CB  MET A 284      22.395  13.323  -1.720  1.00 61.03           C  
ANISOU 2840  CB  MET A 284     8402   5883   8902   1352     69    854       C  
ATOM   2841  CG  MET A 284      22.988  13.259  -0.320  1.00 61.54           C  
ANISOU 2841  CG  MET A 284     8489   5922   8972   1287    199    727       C  
ATOM   2842  SD  MET A 284      24.696  13.829  -0.246  1.00 63.27           S  
ANISOU 2842  SD  MET A 284     8904   6005   9130   1180    262    693       S  
ATOM   2843  CE  MET A 284      25.563  12.368  -0.809  1.00 64.60           C  
ANISOU 2843  CE  MET A 284     9071   6298   9175   1027    200    691       C  
ATOM   2844  N   GLY A 285      19.824  12.785  -3.966  1.00 53.31           N  
ANISOU 2844  N   GLY A 285     7190   5084   7982   1516   -267   1106       N  
ATOM   2845  CA  GLY A 285      19.144  13.320  -5.124  1.00 59.78           C  
ANISOU 2845  CA  GLY A 285     8012   5875   8827   1613   -406   1239       C  
ATOM   2846  C   GLY A 285      20.038  13.659  -6.292  1.00 65.58           C  
ANISOU 2846  C   GLY A 285     8953   6525   9441   1568   -461   1309       C  
ATOM   2847  O   GLY A 285      19.585  14.344  -7.217  1.00 75.75           O  
ANISOU 2847  O   GLY A 285    10284   7754  10745   1656   -566   1424       O  
ATOM   2848  N   VAL A 286      21.291  13.209  -6.279  1.00 65.34           N  
ANISOU 2848  N   VAL A 286     9049   6488   9291   1437   -392   1248       N  
ATOM   2849  CA  VAL A 286      22.198  13.503  -7.381  1.00 60.35           C  
ANISOU 2849  CA  VAL A 286     8608   5785   8538   1387   -417   1314       C  
ATOM   2850  C   VAL A 286      22.007  12.507  -8.515  1.00 58.14           C  
ANISOU 2850  C   VAL A 286     8358   5606   8127   1325   -560   1375       C  
ATOM   2851  O   VAL A 286      21.950  12.889  -9.688  1.00 64.96           O  
ANISOU 2851  O   VAL A 286     9337   6427   8919   1347   -655   1483       O  
ATOM   2852  CB  VAL A 286      23.652  13.498  -6.873  1.00 62.79           C  
ANISOU 2852  CB  VAL A 286     9022   6044   8790   1279   -272   1229       C  
ATOM   2853  CG1 VAL A 286      24.597  14.030  -7.942  1.00 72.90           C  
ANISOU 2853  CG1 VAL A 286    10492   7240   9968   1237   -266   1306       C  
ATOM   2854  CG2 VAL A 286      23.770  14.290  -5.579  1.00 60.10           C  
ANISOU 2854  CG2 VAL A 286     8649   5615   8569   1321   -145   1149       C  
ATOM   2855  N   ILE A 287      21.896  11.226  -8.184  1.00 63.14           N  
ANISOU 2855  N   ILE A 287     8907   6364   8719   1242   -582   1307       N  
ATOM   2856  CA  ILE A 287      21.751  10.157  -9.164  1.00 67.95           C  
ANISOU 2856  CA  ILE A 287     9562   7063   9194   1170   -716   1344       C  
ATOM   2857  C   ILE A 287      20.285   9.742  -9.180  1.00 67.56           C  
ANISOU 2857  C   ILE A 287     9342   7105   9222   1213   -868   1391       C  
ATOM   2858  O   ILE A 287      19.830   8.984  -8.319  1.00 68.03           O  
ANISOU 2858  O   ILE A 287     9251   7255   9341   1178   -855   1324       O  
ATOM   2859  CB  ILE A 287      22.669   8.972  -8.847  1.00 61.66           C  
ANISOU 2859  CB  ILE A 287     8804   6327   8296   1044   -650   1240       C  
ATOM   2860  CG1 ILE A 287      24.130   9.426  -8.840  1.00 60.45           C  
ANISOU 2860  CG1 ILE A 287     8791   6091   8087   1003   -501   1205       C  
ATOM   2861  CG2 ILE A 287      22.459   7.852  -9.858  1.00 65.16           C  
ANISOU 2861  CG2 ILE A 287     9315   6848   8594    977   -793   1270       C  
ATOM   2862  CD1 ILE A 287      25.096   8.374  -8.353  1.00 58.64           C  
ANISOU 2862  CD1 ILE A 287     8576   5912   7794    900   -421   1099       C  
ATOM   2863  N   ASN A 288      19.536  10.244 -10.160  1.00 74.89           N  
ANISOU 2863  N   ASN A 288    10290   8012  10153   1285  -1017   1515       N  
ATOM   2864  CA  ASN A 288      18.136   9.884 -10.329  1.00 81.65           C  
ANISOU 2864  CA  ASN A 288    10976   8958  11089   1322  -1188   1583       C  
ATOM   2865  C   ASN A 288      17.927   8.861 -11.439  1.00 83.72           C  
ANISOU 2865  C   ASN A 288    11324   9291  11196   1225  -1377   1635       C  
ATOM   2866  O   ASN A 288      16.783   8.478 -11.703  1.00 90.94           O  
ANISOU 2866  O   ASN A 288    12107  10283  12163   1231  -1551   1703       O  
ATOM   2867  CB  ASN A 288      17.309  11.140 -10.622  1.00 91.05           C  
ANISOU 2867  CB  ASN A 288    12108  10075  12411   1479  -1255   1696       C  
ATOM   2868  CG  ASN A 288      17.313  12.127  -9.467  1.00 81.84           C  
ANISOU 2868  CG  ASN A 288    10849   8836  11410   1590  -1080   1640       C  
ATOM   2869  OD1 ASN A 288      17.073  11.757  -8.317  1.00 75.76           O  
ANISOU 2869  OD1 ASN A 288     9925   8130  10731   1583   -976   1548       O  
ATOM   2870  ND2 ASN A 288      17.599  13.389  -9.769  1.00 78.45           N  
ANISOU 2870  ND2 ASN A 288    10534   8263  11010   1688  -1045   1695       N  
ATOM   2871  N   SER A 289      19.000   8.411 -12.086  1.00 84.42           N  
ANISOU 2871  N   SER A 289    11629   9351  11095   1135  -1346   1604       N  
ATOM   2872  CA  SER A 289      18.901   7.422 -13.154  1.00 85.51           C  
ANISOU 2872  CA  SER A 289    11892   9539  11058   1043  -1510   1637       C  
ATOM   2873  C   SER A 289      18.567   6.050 -12.580  1.00 81.07           C  
ANISOU 2873  C   SER A 289    11220   9088  10495    942  -1552   1556       C  
ATOM   2874  O   SER A 289      19.305   5.531 -11.737  1.00 85.81           O  
ANISOU 2874  O   SER A 289    11808   9702  11093    889  -1402   1440       O  
ATOM   2875  CB  SER A 289      20.215   7.368 -13.932  1.00 84.01           C  
ANISOU 2875  CB  SER A 289    11966   9286  10670    990  -1423   1615       C  
ATOM   2876  OG  SER A 289      20.214   6.317 -14.883  1.00 81.38           O  
ANISOU 2876  OG  SER A 289    11779   8995  10149    900  -1556   1621       O  
ATOM   2877  N   CYS A 290      17.457   5.459 -13.032  1.00 88.31           N  
ANISOU 2877  N   CYS A 290    12059  10078  11416    908  -1767   1624       N  
ATOM   2878  CA  CYS A 290      17.103   4.125 -12.554  1.00 87.73           C  
ANISOU 2878  CA  CYS A 290    11897  10102  11335    794  -1826   1559       C  
ATOM   2879  C   CYS A 290      18.052   3.059 -13.085  1.00 79.75           C  
ANISOU 2879  C   CYS A 290    11116   9077  10107    683  -1820   1483       C  
ATOM   2880  O   CYS A 290      18.313   2.070 -12.391  1.00 82.40           O  
ANISOU 2880  O   CYS A 290    11419   9456  10433    600  -1769   1386       O  
ATOM   2881  CB  CYS A 290      15.661   3.780 -12.928  1.00 93.94           C  
ANISOU 2881  CB  CYS A 290    12534  10969  12189    772  -2071   1661       C  
ATOM   2882  SG  CYS A 290      14.470   4.166 -11.617  1.00114.25           S  
ANISOU 2882  SG  CYS A 290    14731  13630  15051    843  -2026   1680       S  
ATOM   2883  N   GLU A 291      18.568   3.224 -14.306  1.00 80.53           N  
ANISOU 2883  N   GLU A 291    11456   9114  10028    684  -1870   1526       N  
ATOM   2884  CA  GLU A 291      19.505   2.237 -14.833  1.00 79.49           C  
ANISOU 2884  CA  GLU A 291    11552   8964   9688    597  -1842   1447       C  
ATOM   2885  C   GLU A 291      20.766   2.179 -13.980  1.00 79.18           C  
ANISOU 2885  C   GLU A 291    11522   8898   9663    601  -1590   1327       C  
ATOM   2886  O   GLU A 291      21.338   1.102 -13.777  1.00 77.89           O  
ANISOU 2886  O   GLU A 291    11428   8750   9416    529  -1550   1231       O  
ATOM   2887  CB  GLU A 291      19.855   2.552 -16.287  1.00 87.21           C  
ANISOU 2887  CB  GLU A 291    12793   9877  10464    608  -1910   1518       C  
ATOM   2888  CG  GLU A 291      20.688   1.462 -16.954  1.00100.02           C  
ANISOU 2888  CG  GLU A 291    14664  11483  11855    528  -1894   1438       C  
ATOM   2889  CD  GLU A 291      20.962   1.737 -18.420  1.00102.20           C  
ANISOU 2889  CD  GLU A 291    15218  11700  11911    532  -1960   1510       C  
ATOM   2890  OE1 GLU A 291      20.408   2.720 -18.957  1.00107.28           O  
ANISOU 2890  OE1 GLU A 291    15863  12318  12581    586  -2055   1633       O  
ATOM   2891  OE2 GLU A 291      21.734   0.968 -19.033  1.00114.19           O  
ANISOU 2891  OE2 GLU A 291    16963  13195  13227    487  -1912   1443       O  
ATOM   2892  N   VAL A 292      21.212   3.327 -13.469  1.00 80.76           N  
ANISOU 2892  N   VAL A 292    11659   9053   9974    684  -1429   1334       N  
ATOM   2893  CA  VAL A 292      22.386   3.342 -12.602  1.00 73.62           C  
ANISOU 2893  CA  VAL A 292    10748   8124   9102    680  -1208   1229       C  
ATOM   2894  C   VAL A 292      22.050   2.697 -11.264  1.00 69.01           C  
ANISOU 2894  C   VAL A 292     9973   7602   8646    640  -1178   1147       C  
ATOM   2895  O   VAL A 292      22.794   1.851 -10.757  1.00 74.33           O  
ANISOU 2895  O   VAL A 292    10676   8286   9279    581  -1098   1049       O  
ATOM   2896  CB  VAL A 292      22.901   4.781 -12.424  1.00 75.70           C  
ANISOU 2896  CB  VAL A 292    11006   8310   9447    764  -1066   1265       C  
ATOM   2897  CG1 VAL A 292      23.975   4.836 -11.351  1.00 74.52           C  
ANISOU 2897  CG1 VAL A 292    10812   8140   9363    749   -862   1162       C  
ATOM   2898  CG2 VAL A 292      23.438   5.319 -13.741  1.00 82.09           C  
ANISOU 2898  CG2 VAL A 292    12032   9054  10104    782  -1069   1342       C  
ATOM   2899  N   ILE A 293      20.917   3.088 -10.677  1.00 67.80           N  
ANISOU 2899  N   ILE A 293     9623   7490   8649    676  -1241   1192       N  
ATOM   2900  CA  ILE A 293      20.507   2.534  -9.391  1.00 68.03           C  
ANISOU 2900  CA  ILE A 293     9469   7584   8797    636  -1203   1124       C  
ATOM   2901  C   ILE A 293      20.304   1.030  -9.499  1.00 71.10           C  
ANISOU 2901  C   ILE A 293     9891   8033   9093    518  -1319   1084       C  
ATOM   2902  O   ILE A 293      20.577   0.288  -8.547  1.00 69.20           O  
ANISOU 2902  O   ILE A 293     9597   7819   8876    455  -1251    998       O  
ATOM   2903  CB  ILE A 293      19.233   3.248  -8.893  1.00 76.26           C  
ANISOU 2903  CB  ILE A 293    10290   8666  10018    706  -1246   1192       C  
ATOM   2904  CG1 ILE A 293      19.530   4.731  -8.647  1.00 77.85           C  
ANISOU 2904  CG1 ILE A 293    10480   8786  10315    828  -1114   1214       C  
ATOM   2905  CG2 ILE A 293      18.705   2.577  -7.633  1.00 83.01           C  
ANISOU 2905  CG2 ILE A 293    10960   9603  10976    651  -1209   1132       C  
ATOM   2906  CD1 ILE A 293      18.308   5.571  -8.372  1.00 85.09           C  
ANISOU 2906  CD1 ILE A 293    11206   9722  11402    933  -1157   1291       C  
ATOM   2907  N   ALA A 294      19.821   0.555 -10.649  1.00 68.54           N  
ANISOU 2907  N   ALA A 294     9669   7719   8653    480  -1504   1146       N  
ATOM   2908  CA  ALA A 294      19.666  -0.882 -10.845  1.00 65.05           C  
ANISOU 2908  CA  ALA A 294     9297   7312   8105    362  -1627   1106       C  
ATOM   2909  C   ALA A 294      21.018  -1.585 -10.856  1.00 67.89           C  
ANISOU 2909  C   ALA A 294     9841   7620   8333    330  -1510    998       C  
ATOM   2910  O   ALA A 294      21.168  -2.663 -10.267  1.00 66.58           O  
ANISOU 2910  O   ALA A 294     9672   7473   8152    250  -1513    922       O  
ATOM   2911  CB  ALA A 294      18.913  -1.154 -12.147  1.00 75.37           C  
ANISOU 2911  CB  ALA A 294    10708   8625   9302    328  -1860   1196       C  
ATOM   2912  N   VAL A 295      22.011  -0.993 -11.523  1.00 62.64           N  
ANISOU 2912  N   VAL A 295     9335   6890   7577    393  -1404    995       N  
ATOM   2913  CA  VAL A 295      23.351  -1.574 -11.528  1.00 57.45           C  
ANISOU 2913  CA  VAL A 295     8825   6188   6815    380  -1271    898       C  
ATOM   2914  C   VAL A 295      23.914  -1.618 -10.114  1.00 56.95           C  
ANISOU 2914  C   VAL A 295     8625   6133   6880    376  -1118    816       C  
ATOM   2915  O   VAL A 295      24.496  -2.625  -9.692  1.00 56.86           O  
ANISOU 2915  O   VAL A 295     8657   6118   6829    326  -1088    730       O  
ATOM   2916  CB  VAL A 295      24.272  -0.786 -12.479  1.00 54.26           C  
ANISOU 2916  CB  VAL A 295     8586   5724   6308    447  -1167    927       C  
ATOM   2917  CG1 VAL A 295      25.714  -1.253 -12.340  1.00 57.20           C  
ANISOU 2917  CG1 VAL A 295     9058   6061   6613    449   -996    831       C  
ATOM   2918  CG2 VAL A 295      23.806  -0.940 -13.917  1.00 57.28           C  
ANISOU 2918  CG2 VAL A 295     9152   6092   6521    437  -1325    998       C  
ATOM   2919  N   ILE A 296      23.749  -0.531  -9.358  1.00 51.23           N  
ANISOU 2919  N   ILE A 296     7747   5410   6306    429  -1028    841       N  
ATOM   2920  CA  ILE A 296      24.228  -0.509  -7.978  1.00 59.08           C  
ANISOU 2920  CA  ILE A 296     8626   6408   7414    418   -894    765       C  
ATOM   2921  C   ILE A 296      23.601  -1.646  -7.179  1.00 58.44           C  
ANISOU 2921  C   ILE A 296     8458   6385   7362    331   -974    721       C  
ATOM   2922  O   ILE A 296      24.290  -2.366  -6.447  1.00 54.97           O  
ANISOU 2922  O   ILE A 296     8033   5938   6917    285   -912    639       O  
ATOM   2923  CB  ILE A 296      23.946   0.860  -7.333  1.00 61.11           C  
ANISOU 2923  CB  ILE A 296     8750   6650   7818    490   -804    801       C  
ATOM   2924  CG1 ILE A 296      24.677   1.964  -8.101  1.00 58.55           C  
ANISOU 2924  CG1 ILE A 296     8532   6254   7461    561   -723    847       C  
ATOM   2925  CG2 ILE A 296      24.382   0.858  -5.872  1.00 63.42           C  
ANISOU 2925  CG2 ILE A 296     8943   6943   8211    468   -679    720       C  
ATOM   2926  CD1 ILE A 296      24.302   3.367  -7.673  1.00 62.57           C  
ANISOU 2926  CD1 ILE A 296     8944   6727   8103    640   -662    895       C  
ATOM   2927  N   ASP A 297      22.281  -1.826  -7.312  1.00 61.35           N  
ANISOU 2927  N   ASP A 297     8731   6813   7768    302  -1119    784       N  
ATOM   2928  CA  ASP A 297      21.590  -2.867  -6.559  1.00 60.66           C  
ANISOU 2928  CA  ASP A 297     8549   6786   7714    203  -1197    758       C  
ATOM   2929  C   ASP A 297      22.007  -4.255  -7.027  1.00 59.60           C  
ANISOU 2929  C   ASP A 297     8580   6629   7435    118  -1287    707       C  
ATOM   2930  O   ASP A 297      22.074  -5.186  -6.217  1.00 59.56           O  
ANISOU 2930  O   ASP A 297     8554   6637   7439     38  -1291    649       O  
ATOM   2931  CB  ASP A 297      20.072  -2.703  -6.684  1.00 65.15           C  
ANISOU 2931  CB  ASP A 297     8958   7429   8366    187  -1334    851       C  
ATOM   2932  CG  ASP A 297      19.565  -1.392  -6.096  1.00 78.29           C  
ANISOU 2932  CG  ASP A 297    10444   9112  10189    285  -1237    895       C  
ATOM   2933  OD1 ASP A 297      20.353  -0.682  -5.436  1.00 88.04           O  
ANISOU 2933  OD1 ASP A 297    11682  10300  11468    345  -1065    843       O  
ATOM   2934  OD2 ASP A 297      18.371  -1.078  -6.300  1.00 78.59           O  
ANISOU 2934  OD2 ASP A 297    10340   9208  10312    304  -1338    982       O  
ATOM   2935  N   LEU A 298      22.308  -4.406  -8.320  1.00 55.62           N  
ANISOU 2935  N   LEU A 298     8259   6084   6791    136  -1358    725       N  
ATOM   2936  CA  LEU A 298      22.697  -5.708  -8.850  1.00 54.48           C  
ANISOU 2936  CA  LEU A 298     8299   5903   6496     70  -1442    670       C  
ATOM   2937  C   LEU A 298      24.127  -6.057  -8.459  1.00 52.73           C  
ANISOU 2937  C   LEU A 298     8172   5625   6238    100  -1285    571       C  
ATOM   2938  O   LEU A 298      24.441  -7.235  -8.257  1.00 49.11           O  
ANISOU 2938  O   LEU A 298     7800   5140   5718     43  -1324    504       O  
ATOM   2939  CB  LEU A 298      22.552  -5.726 -10.373  1.00 60.54           C  
ANISOU 2939  CB  LEU A 298     9253   6642   7109     85  -1560    718       C  
ATOM   2940  CG  LEU A 298      22.716  -7.094 -11.041  1.00 63.36           C  
ANISOU 2940  CG  LEU A 298     9825   6953   7294     13  -1680    665       C  
ATOM   2941  CD1 LEU A 298      21.424  -7.893 -10.947  1.00 68.21           C  
ANISOU 2941  CD1 LEU A 298    10379   7612   7926   -111  -1900    707       C  
ATOM   2942  CD2 LEU A 298      23.159  -6.939 -12.488  1.00 60.34           C  
ANISOU 2942  CD2 LEU A 298     9681   6517   6729     63  -1699    680       C  
ATOM   2943  N   ALA A 299      24.995  -5.053  -8.340  1.00 51.78           N  
ANISOU 2943  N   ALA A 299     8031   5481   6161    187  -1117    565       N  
ATOM   2944  CA  ALA A 299      26.398  -5.269  -8.026  1.00 48.43           C  
ANISOU 2944  CA  ALA A 299     7672   5010   5720    221   -968    484       C  
ATOM   2945  C   ALA A 299      26.690  -5.223  -6.532  1.00 48.19           C  
ANISOU 2945  C   ALA A 299     7495   4992   5824    198   -879    437       C  
ATOM   2946  O   ALA A 299      27.799  -5.584  -6.124  1.00 51.24           O  
ANISOU 2946  O   ALA A 299     7918   5341   6209    210   -786    370       O  
ATOM   2947  CB  ALA A 299      27.257  -4.222  -8.742  1.00 48.69           C  
ANISOU 2947  CB  ALA A 299     7767   5009   5724    310   -836    511       C  
ATOM   2948  N   LEU A 300      25.732  -4.792  -5.712  1.00 48.38           N  
ANISOU 2948  N   LEU A 300     7355   5065   5961    168   -905    471       N  
ATOM   2949  CA  LEU A 300      25.994  -4.664  -4.282  1.00 44.66           C  
ANISOU 2949  CA  LEU A 300     6767   4602   5601    145   -813    427       C  
ATOM   2950  C   LEU A 300      26.323  -5.995  -3.619  1.00 45.69           C  
ANISOU 2950  C   LEU A 300     6940   4721   5701     67   -854    358       C  
ATOM   2951  O   LEU A 300      27.273  -6.036  -2.817  1.00 52.87           O  
ANISOU 2951  O   LEU A 300     7843   5599   6647     72   -760    303       O  
ATOM   2952  CB  LEU A 300      24.789  -4.013  -3.593  1.00 51.21           C  
ANISOU 2952  CB  LEU A 300     7424   5490   6542    133   -826    476       C  
ATOM   2953  CG  LEU A 300      25.084  -3.234  -2.310  1.00 51.89           C  
ANISOU 2953  CG  LEU A 300     7404   5571   6741    150   -688    444       C  
ATOM   2954  CD1 LEU A 300      25.685  -1.870  -2.627  1.00 50.68           C  
ANISOU 2954  CD1 LEU A 300     7261   5369   6624    245   -577    465       C  
ATOM   2955  CD2 LEU A 300      23.828  -3.090  -1.465  1.00 69.16           C  
ANISOU 2955  CD2 LEU A 300     9434   7826   9019    117   -705    472       C  
ATOM   2956  N   PRO A 301      25.610  -7.093  -3.884  1.00 51.25           N  
ANISOU 2956  N   PRO A 301     7692   5440   6340    -10   -999    363       N  
ATOM   2957  CA  PRO A 301      25.955  -8.355  -3.208  1.00 54.50           C  
ANISOU 2957  CA  PRO A 301     8160   5825   6725    -84  -1040    300       C  
ATOM   2958  C   PRO A 301      27.337  -8.869  -3.568  1.00 51.53           C  
ANISOU 2958  C   PRO A 301     7929   5372   6278    -29   -986    233       C  
ATOM   2959  O   PRO A 301      27.983  -9.516  -2.734  1.00 52.72           O  
ANISOU 2959  O   PRO A 301     8092   5489   6450    -54   -965    178       O  
ATOM   2960  CB  PRO A 301      24.856  -9.321  -3.677  1.00 50.89           C  
ANISOU 2960  CB  PRO A 301     7745   5389   6203   -179  -1221    332       C  
ATOM   2961  CG  PRO A 301      23.751  -8.453  -4.169  1.00 50.83           C  
ANISOU 2961  CG  PRO A 301     7629   5448   6238   -167  -1266    418       C  
ATOM   2962  CD  PRO A 301      24.414  -7.234  -4.732  1.00 50.61           C  
ANISOU 2962  CD  PRO A 301     7613   5399   6218    -44  -1146    431       C  
ATOM   2963  N   PHE A 302      27.811  -8.604  -4.788  1.00 51.29           N  
ANISOU 2963  N   PHE A 302     8009   5314   6166     49   -960    239       N  
ATOM   2964  CA  PHE A 302      29.146  -9.042  -5.177  1.00 47.63           C  
ANISOU 2964  CA  PHE A 302     7668   4787   5644    116   -882    177       C  
ATOM   2965  C   PHE A 302      30.217  -8.174  -4.532  1.00 45.41           C  
ANISOU 2965  C   PHE A 302     7290   4500   5463    174   -719    163       C  
ATOM   2966  O   PHE A 302      31.252  -8.683  -4.089  1.00 50.08           O  
ANISOU 2966  O   PHE A 302     7901   5053   6076    196   -666    107       O  
ATOM   2967  CB  PHE A 302      29.283  -9.025  -6.699  1.00 47.41           C  
ANISOU 2967  CB  PHE A 302     7798   4735   5480    176   -890    191       C  
ATOM   2968  CG  PHE A 302      28.396 -10.018  -7.393  1.00 47.40           C  
ANISOU 2968  CG  PHE A 302     7931   4719   5360    113  -1067    193       C  
ATOM   2969  CD1 PHE A 302      28.834 -11.310  -7.632  1.00 45.36           C  
ANISOU 2969  CD1 PHE A 302     7838   4391   5005    108  -1120    122       C  
ATOM   2970  CD2 PHE A 302      27.121  -9.662  -7.799  1.00 49.06           C  
ANISOU 2970  CD2 PHE A 302     8104   4978   5560     59  -1189    269       C  
ATOM   2971  CE1 PHE A 302      28.018 -12.227  -8.266  1.00 45.22           C  
ANISOU 2971  CE1 PHE A 302     7965   4346   4871     37  -1295    123       C  
ATOM   2972  CE2 PHE A 302      26.302 -10.576  -8.434  1.00 46.07           C  
ANISOU 2972  CE2 PHE A 302     7847   4583   5073    -16  -1371    277       C  
ATOM   2973  CZ  PHE A 302      26.752 -11.860  -8.666  1.00 45.85           C  
ANISOU 2973  CZ  PHE A 302     8003   4480   4940    -34  -1426    202       C  
ATOM   2974  N   ALA A 303      29.983  -6.863  -4.471  1.00 42.23           N  
ANISOU 2974  N   ALA A 303     6786   4131   5130    198   -648    216       N  
ATOM   2975  CA  ALA A 303      30.932  -5.982  -3.802  1.00 45.67           C  
ANISOU 2975  CA  ALA A 303     7134   4555   5665    232   -510    206       C  
ATOM   2976  C   ALA A 303      30.985  -6.286  -2.311  1.00 52.48           C  
ANISOU 2976  C   ALA A 303     7906   5419   6616    169   -519    168       C  
ATOM   2977  O   ALA A 303      32.054  -6.220  -1.693  1.00 51.28           O  
ANISOU 2977  O   ALA A 303     7727   5238   6520    181   -446    133       O  
ATOM   2978  CB  ALA A 303      30.553  -4.523  -4.042  1.00 46.12           C  
ANISOU 2978  CB  ALA A 303     7121   4630   5771    265   -449    272       C  
ATOM   2979  N   ILE A 304      29.836  -6.614  -1.716  1.00 49.97           N  
ANISOU 2979  N   ILE A 304     7539   5137   6310     96   -609    180       N  
ATOM   2980  CA  ILE A 304      29.803  -7.003  -0.311  1.00 46.88           C  
ANISOU 2980  CA  ILE A 304     7087   4748   5978     24   -620    147       C  
ATOM   2981  C   ILE A 304      30.584  -8.291  -0.095  1.00 47.04           C  
ANISOU 2981  C   ILE A 304     7197   4719   5957      4   -670     91       C  
ATOM   2982  O   ILE A 304      31.118  -8.529   0.995  1.00 51.24           O  
ANISOU 2982  O   ILE A 304     7701   5229   6538    -32   -658     59       O  
ATOM   2983  CB  ILE A 304      28.341  -7.138   0.165  1.00 46.06           C  
ANISOU 2983  CB  ILE A 304     6910   4702   5887    -53   -695    180       C  
ATOM   2984  CG1 ILE A 304      27.718  -5.750   0.354  1.00 49.87           C  
ANISOU 2984  CG1 ILE A 304     7278   5223   6447    -17   -618    224       C  
ATOM   2985  CG2 ILE A 304      28.262  -7.955   1.451  1.00 50.79           C  
ANISOU 2985  CG2 ILE A 304     7494   5300   6503   -148   -731    146       C  
ATOM   2986  CD1 ILE A 304      26.226  -5.767   0.618  1.00 49.58           C  
ANISOU 2986  CD1 ILE A 304     7144   5257   6437    -69   -677    269       C  
ATOM   2987  N   LEU A 305      30.671  -9.138  -1.122  1.00 39.02           N  
ANISOU 2987  N   LEU A 305     6302   3677   4848     30   -733     79       N  
ATOM   2988  CA  LEU A 305      31.400 -10.393  -0.982  1.00 48.82           C  
ANISOU 2988  CA  LEU A 305     7642   4856   6051     29   -782     23       C  
ATOM   2989  C   LEU A 305      32.909 -10.181  -1.027  1.00 51.95           C  
ANISOU 2989  C   LEU A 305     8038   5213   6489    119   -673    -10       C  
ATOM   2990  O   LEU A 305      33.655 -10.881  -0.333  1.00 42.78           O  
ANISOU 2990  O   LEU A 305     6887   4006   5360    116   -691    -50       O  
ATOM   2991  CB  LEU A 305      30.965 -11.369  -2.074  1.00 49.00           C  
ANISOU 2991  CB  LEU A 305     7815   4850   5952     30   -886     14       C  
ATOM   2992  CG  LEU A 305      31.559 -12.777  -1.994  1.00 49.39           C  
ANISOU 2992  CG  LEU A 305     7996   4819   5952     32   -955    -47       C  
ATOM   2993  CD1 LEU A 305      31.201 -13.452  -0.678  1.00 42.77           C  
ANISOU 2993  CD1 LEU A 305     7122   3970   5158    -76  -1040    -53       C  
ATOM   2994  CD2 LEU A 305      31.083 -13.611  -3.170  1.00 48.86           C  
ANISOU 2994  CD2 LEU A 305     8102   4713   5750     34  -1055    -59       C  
ATOM   2995  N   LEU A 306      33.382  -9.230  -1.838  1.00 48.22           N  
ANISOU 2995  N   LEU A 306     7547   4754   6020    196   -563     13       N  
ATOM   2996  CA  LEU A 306      34.809  -8.928  -1.850  1.00 50.35           C  
ANISOU 2996  CA  LEU A 306     7784   5000   6348    270   -448     -6       C  
ATOM   2997  C   LEU A 306      35.285  -8.418  -0.496  1.00 51.85           C  
ANISOU 2997  C   LEU A 306     7851   5190   6659    225   -421     -7       C  
ATOM   2998  O   LEU A 306      36.424  -8.688  -0.098  1.00 55.19           O  
ANISOU 2998  O   LEU A 306     8245   5582   7142    255   -390    -33       O  
ATOM   2999  CB  LEU A 306      35.129  -7.908  -2.941  1.00 50.91           C  
ANISOU 2999  CB  LEU A 306     7856   5091   6397    339   -331     34       C  
ATOM   3000  CG  LEU A 306      35.003  -8.414  -4.378  1.00 47.52           C  
ANISOU 3000  CG  LEU A 306     7575   4650   5829    399   -335     29       C  
ATOM   3001  CD1 LEU A 306      35.157  -7.267  -5.358  1.00 49.29           C  
ANISOU 3001  CD1 LEU A 306     7804   4900   6026    446   -225     84       C  
ATOM   3002  CD2 LEU A 306      36.038  -9.495  -4.654  1.00 45.00           C  
ANISOU 3002  CD2 LEU A 306     7338   4282   5479    471   -307    -33       C  
ATOM   3003  N   GLY A 307      34.437  -7.685   0.226  1.00 48.85           N  
ANISOU 3003  N   GLY A 307     7401   4843   6318    157   -434     20       N  
ATOM   3004  CA  GLY A 307      34.801  -7.287   1.575  1.00 48.10           C  
ANISOU 3004  CA  GLY A 307     7223   4739   6313    102   -422     10       C  
ATOM   3005  C   GLY A 307      35.065  -8.485   2.464  1.00 48.68           C  
ANISOU 3005  C   GLY A 307     7331   4778   6387     55   -516    -30       C  
ATOM   3006  O   GLY A 307      36.060  -8.530   3.192  1.00 52.86           O  
ANISOU 3006  O   GLY A 307     7826   5276   6983     52   -510    -47       O  
ATOM   3007  N   PHE A 308      34.172  -9.478   2.415  1.00 51.49           N  
ANISOU 3007  N   PHE A 308     7759   5135   6669     10   -617    -38       N  
ATOM   3008  CA  PHE A 308      34.411 -10.723   3.136  1.00 49.51           C  
ANISOU 3008  CA  PHE A 308     7569   4838   6406    -35   -718    -70       C  
ATOM   3009  C   PHE A 308      35.652 -11.435   2.616  1.00 45.44           C  
ANISOU 3009  C   PHE A 308     7105   4263   5898     59   -714   -103       C  
ATOM   3010  O   PHE A 308      36.322 -12.148   3.372  1.00 43.49           O  
ANISOU 3010  O   PHE A 308     6873   3965   5686     50   -772   -126       O  
ATOM   3011  CB  PHE A 308      33.197 -11.647   3.019  1.00 47.75           C  
ANISOU 3011  CB  PHE A 308     7423   4623   6099   -108   -829    -64       C  
ATOM   3012  CG  PHE A 308      32.030 -11.234   3.870  1.00 52.41           C  
ANISOU 3012  CG  PHE A 308     7947   5270   6697   -215   -842    -33       C  
ATOM   3013  CD1 PHE A 308      31.999 -11.534   5.222  1.00 49.53           C  
ANISOU 3013  CD1 PHE A 308     7573   4895   6352   -305   -878    -40       C  
ATOM   3014  CD2 PHE A 308      30.957 -10.553   3.316  1.00 50.23           C  
ANISOU 3014  CD2 PHE A 308     7618   5059   6407   -220   -817      6       C  
ATOM   3015  CE1 PHE A 308      30.922 -11.157   6.008  1.00 48.28           C  
ANISOU 3015  CE1 PHE A 308     7355   4794   6194   -397   -865    -14       C  
ATOM   3016  CE2 PHE A 308      29.879 -10.174   4.097  1.00 43.60           C  
ANISOU 3016  CE2 PHE A 308     6700   4277   5587   -303   -812     35       C  
ATOM   3017  CZ  PHE A 308      29.862 -10.477   5.444  1.00 41.50           C  
ANISOU 3017  CZ  PHE A 308     6427   4005   5335   -391   -826     22       C  
ATOM   3018  N   THR A 309      35.973 -11.259   1.331  1.00 51.72           N  
ANISOU 3018  N   THR A 309     7931   5062   6658    156   -643   -104       N  
ATOM   3019  CA  THR A 309      37.101 -11.977   0.747  1.00 54.06           C  
ANISOU 3019  CA  THR A 309     8280   5307   6956    262   -617   -140       C  
ATOM   3020  C   THR A 309      38.433 -11.507   1.316  1.00 51.85           C  
ANISOU 3020  C   THR A 309     7882   5019   6799    303   -545   -138       C  
ATOM   3021  O   THR A 309      39.363 -12.312   1.447  1.00 50.69           O  
ANISOU 3021  O   THR A 309     7748   4821   6692    366   -566   -166       O  
ATOM   3022  CB  THR A 309      37.099 -11.817  -0.775  1.00 45.16           C  
ANISOU 3022  CB  THR A 309     7223   4191   5744    351   -538   -140       C  
ATOM   3023  OG1 THR A 309      35.823 -12.204  -1.297  1.00 49.16           O  
ANISOU 3023  OG1 THR A 309     7835   4705   6139    298   -628   -134       O  
ATOM   3024  CG2 THR A 309      38.179 -12.679  -1.401  1.00 49.59           C  
ANISOU 3024  CG2 THR A 309     7855   4695   6291    471   -499   -186       C  
ATOM   3025  N   ASN A 310      38.554 -10.222   1.661  1.00 55.15           N  
ANISOU 3025  N   ASN A 310     8187   5481   7286    270   -469   -101       N  
ATOM   3026  CA  ASN A 310      39.794  -9.757   2.269  1.00 58.62           C  
ANISOU 3026  CA  ASN A 310     8511   5911   7849    284   -424    -92       C  
ATOM   3027  C   ASN A 310      40.078 -10.490   3.573  1.00 56.10           C  
ANISOU 3027  C   ASN A 310     8190   5548   7579    227   -546   -110       C  
ATOM   3028  O   ASN A 310      41.236 -10.554   3.997  1.00 58.98           O  
ANISOU 3028  O   ASN A 310     8478   5890   8044    257   -547   -108       O  
ATOM   3029  CB  ASN A 310      39.762  -8.248   2.513  1.00 57.70           C  
ANISOU 3029  CB  ASN A 310     8301   5834   7789    235   -343    -51       C  
ATOM   3030  CG  ASN A 310      41.143  -7.682   2.811  1.00 64.87           C  
ANISOU 3030  CG  ASN A 310     9089   6735   8823    253   -284    -32       C  
ATOM   3031  OD1 ASN A 310      42.164  -8.286   2.468  1.00 65.85           O  
ANISOU 3031  OD1 ASN A 310     9181   6844   8994    333   -261    -42       O  
ATOM   3032  ND2 ASN A 310      41.181  -6.516   3.441  1.00 62.88           N  
ANISOU 3032  ND2 ASN A 310     8770   6491   8631    180   -258     -5       N  
ATOM   3033  N   SER A 311      39.047 -11.047   4.214  1.00 53.46           N  
ANISOU 3033  N   SER A 311     7933   5203   7177    140   -652   -120       N  
ATOM   3034  CA  SER A 311      39.268 -11.911   5.366  1.00 49.82           C  
ANISOU 3034  CA  SER A 311     7503   4689   6736     83   -777   -134       C  
ATOM   3035  C   SER A 311      39.899 -13.235   4.960  1.00 42.82           C  
ANISOU 3035  C   SER A 311     6689   3736   5844    173   -838   -164       C  
ATOM   3036  O   SER A 311      40.518 -13.897   5.798  1.00 41.32           O  
ANISOU 3036  O   SER A 311     6504   3490   5705    164   -933   -169       O  
ATOM   3037  CB  SER A 311      37.946 -12.166   6.092  1.00 52.65           C  
ANISOU 3037  CB  SER A 311     7931   5059   7014    -40   -858   -130       C  
ATOM   3038  OG  SER A 311      37.321 -10.950   6.462  1.00 53.36           O  
ANISOU 3038  OG  SER A 311     7958   5207   7111   -105   -790   -108       O  
ATOM   3039  N   CYS A 312      39.747 -13.636   3.697  1.00 47.43           N  
ANISOU 3039  N   CYS A 312     7343   4316   6362    263   -790   -185       N  
ATOM   3040  CA  CYS A 312      40.446 -14.804   3.179  1.00 51.34           C  
ANISOU 3040  CA  CYS A 312     7916   4739   6852    376   -819   -223       C  
ATOM   3041  C   CYS A 312      41.862 -14.467   2.737  1.00 49.49           C  
ANISOU 3041  C   CYS A 312     7567   4511   6726    506   -704   -223       C  
ATOM   3042  O   CYS A 312      42.717 -15.359   2.699  1.00 51.05           O  
ANISOU 3042  O   CYS A 312     7780   4645   6970    607   -732   -249       O  
ATOM   3043  CB  CYS A 312      39.679 -15.409   2.002  1.00 58.04           C  
ANISOU 3043  CB  CYS A 312     8914   5570   7567    414   -818   -252       C  
ATOM   3044  SG  CYS A 312      38.013 -15.975   2.404  1.00 56.26           S  
ANISOU 3044  SG  CYS A 312     8813   5339   7226    257   -966   -244       S  
ATOM   3045  N   VAL A 313      42.120 -13.205   2.396  1.00 52.26           N  
ANISOU 3045  N   VAL A 313     7801   4935   7121    507   -575   -190       N  
ATOM   3046  CA  VAL A 313      43.449 -12.784   1.973  1.00 50.78           C  
ANISOU 3046  CA  VAL A 313     7484   4768   7044    610   -453   -176       C  
ATOM   3047  C   VAL A 313      44.329 -12.356   3.143  1.00 49.03           C  
ANISOU 3047  C   VAL A 313     7110   4546   6973    560   -500   -142       C  
ATOM   3048  O   VAL A 313      45.562 -12.408   3.026  1.00 54.64           O  
ANISOU 3048  O   VAL A 313     7703   5256   7802    648   -447   -131       O  
ATOM   3049  CB  VAL A 313      43.340 -11.636   0.952  1.00 53.69           C  
ANISOU 3049  CB  VAL A 313     7813   5207   7381    626   -291   -147       C  
ATOM   3050  CG1 VAL A 313      44.714 -11.244   0.438  1.00 61.74           C  
ANISOU 3050  CG1 VAL A 313     8696   6254   8510    726   -148   -126       C  
ATOM   3051  CG2 VAL A 313      42.433 -12.034  -0.203  1.00 51.10           C  
ANISOU 3051  CG2 VAL A 313     7648   4875   6891    665   -267   -175       C  
ATOM   3052  N   ASN A 314      43.737 -11.945   4.266  1.00 47.75           N  
ANISOU 3052  N   ASN A 314     6948   4385   6808    421   -597   -125       N  
ATOM   3053  CA  ASN A 314      44.542 -11.518   5.406  1.00 50.51           C  
ANISOU 3053  CA  ASN A 314     7181   4727   7284    358   -659    -94       C  
ATOM   3054  C   ASN A 314      45.508 -12.592   5.891  1.00 48.18           C  
ANISOU 3054  C   ASN A 314     6859   4369   7076    425   -764   -101       C  
ATOM   3055  O   ASN A 314      46.667 -12.251   6.186  1.00 50.03           O  
ANISOU 3055  O   ASN A 314     6944   4612   7454    450   -757    -68       O  
ATOM   3056  CB  ASN A 314      43.627 -11.066   6.552  1.00 50.65           C  
ANISOU 3056  CB  ASN A 314     7250   4744   7250    201   -749    -87       C  
ATOM   3057  CG  ASN A 314      42.962  -9.732   6.277  1.00 53.66           C  
ANISOU 3057  CG  ASN A 314     7609   5182   7597    143   -643    -69       C  
ATOM   3058  OD1 ASN A 314      43.474  -8.919   5.505  1.00 46.05           O  
ANISOU 3058  OD1 ASN A 314     6560   4254   6683    191   -519    -46       O  
ATOM   3059  ND2 ASN A 314      41.821  -9.494   6.916  1.00 58.23           N  
ANISOU 3059  ND2 ASN A 314     8263   5767   8094     40   -685    -76       N  
ATOM   3060  N   PRO A 315      45.120 -13.864   6.015  1.00 43.91           N  
ANISOU 3060  N   PRO A 315     6453   3762   6468    453   -870   -135       N  
ATOM   3061  CA  PRO A 315      46.108 -14.885   6.409  1.00 55.72           C  
ANISOU 3061  CA  PRO A 315     7924   5186   8060    540   -970   -138       C  
ATOM   3062  C   PRO A 315      47.348 -14.890   5.534  1.00 52.93           C  
ANISOU 3062  C   PRO A 315     7434   4852   7826    707   -846   -136       C  
ATOM   3063  O   PRO A 315      48.466 -15.027   6.045  1.00 53.87           O  
ANISOU 3063  O   PRO A 315     7420   4954   8096    752   -897   -106       O  
ATOM   3064  CB  PRO A 315      45.315 -16.194   6.287  1.00 55.14           C  
ANISOU 3064  CB  PRO A 315     8052   5035   7865    558  -1066   -182       C  
ATOM   3065  CG  PRO A 315      43.902 -15.790   6.530  1.00 47.76           C  
ANISOU 3065  CG  PRO A 315     7217   4135   6796    408  -1084   -182       C  
ATOM   3066  CD  PRO A 315      43.758 -14.418   5.926  1.00 46.12           C  
ANISOU 3066  CD  PRO A 315     6909   4023   6592    392   -925   -164       C  
ATOM   3067  N   PHE A 316      47.178 -14.747   4.219  1.00 51.47           N  
ANISOU 3067  N   PHE A 316     7277   4703   7575    799   -683   -161       N  
ATOM   3068  CA  PHE A 316      48.326 -14.746   3.318  1.00 55.73           C  
ANISOU 3068  CA  PHE A 316     7693   5269   8214    961   -532   -159       C  
ATOM   3069  C   PHE A 316      49.154 -13.474   3.450  1.00 51.24           C  
ANISOU 3069  C   PHE A 316     6903   4782   7782    917   -439    -95       C  
ATOM   3070  O   PHE A 316      50.358 -13.493   3.173  1.00 52.37           O  
ANISOU 3070  O   PHE A 316     6882   4948   8069   1024   -360    -71       O  
ATOM   3071  CB  PHE A 316      47.859 -14.931   1.876  1.00 49.68           C  
ANISOU 3071  CB  PHE A 316     7051   4515   7310   1057   -382   -205       C  
ATOM   3072  CG  PHE A 316      47.216 -16.261   1.615  1.00 47.68           C  
ANISOU 3072  CG  PHE A 316     7016   4168   6932   1115   -472   -270       C  
ATOM   3073  CD1 PHE A 316      45.870 -16.461   1.862  1.00 52.35           C  
ANISOU 3073  CD1 PHE A 316     7777   4735   7379    989   -583   -286       C  
ATOM   3074  CD2 PHE A 316      47.965 -17.316   1.124  1.00 56.32           C  
ANISOU 3074  CD2 PHE A 316     8146   5194   8059   1295   -444   -315       C  
ATOM   3075  CE1 PHE A 316      45.282 -17.689   1.620  1.00 47.70           C  
ANISOU 3075  CE1 PHE A 316     7393   4053   6677   1024   -677   -340       C  
ATOM   3076  CE2 PHE A 316      47.383 -18.545   0.881  1.00 55.14           C  
ANISOU 3076  CE2 PHE A 316     8220   4939   7790   1343   -535   -378       C  
ATOM   3077  CZ  PHE A 316      46.041 -18.731   1.129  1.00 51.69           C  
ANISOU 3077  CZ  PHE A 316     7955   4477   7207   1197   -658   -388       C  
ATOM   3078  N   LEU A 317      48.535 -12.366   3.862  1.00 53.06           N  
ANISOU 3078  N   LEU A 317     7127   5056   7977    762   -445    -64       N  
ATOM   3079  CA  LEU A 317      49.215 -11.078   3.819  1.00 49.32           C  
ANISOU 3079  CA  LEU A 317     6476   4652   7612    711   -344     -5       C  
ATOM   3080  C   LEU A 317      50.107 -10.855   5.032  1.00 49.40           C  
ANISOU 3080  C   LEU A 317     6336   4649   7786    638   -473     42       C  
ATOM   3081  O   LEU A 317      51.099 -10.124   4.937  1.00 53.87           O  
ANISOU 3081  O   LEU A 317     6714   5262   8493    634   -401     96       O  
ATOM   3082  CB  LEU A 317      48.191  -9.945   3.734  1.00 50.48           C  
ANISOU 3082  CB  LEU A 317     6691   4834   7654    585   -298      7       C  
ATOM   3083  CG  LEU A 317      47.522  -9.703   2.382  1.00 54.52           C  
ANISOU 3083  CG  LEU A 317     7298   5382   8034    642   -144    -10       C  
ATOM   3084  CD1 LEU A 317      46.387  -8.706   2.539  1.00 59.55           C  
ANISOU 3084  CD1 LEU A 317     8009   6038   8579    517   -148      3       C  
ATOM   3085  CD2 LEU A 317      48.526  -9.208   1.355  1.00 61.99           C  
ANISOU 3085  CD2 LEU A 317     8117   6383   9053    732     46     25       C  
ATOM   3086  N   TYR A 318      49.779 -11.464   6.167  1.00 46.80           N  
ANISOU 3086  N   TYR A 318     6089   4255   7438    569   -667     28       N  
ATOM   3087  CA  TYR A 318      50.490 -11.188   7.408  1.00 48.69           C  
ANISOU 3087  CA  TYR A 318     6220   4474   7804    473   -817     75       C  
ATOM   3088  C   TYR A 318      51.066 -12.451   8.039  1.00 55.79           C  
ANISOU 3088  C   TYR A 318     7120   5303   8776    545   -982     72       C  
ATOM   3089  O   TYR A 318      52.283 -12.616   8.091  1.00 74.18           O  
ANISOU 3089  O   TYR A 318     9270   7637  11279    622  -1000    111       O  
ATOM   3090  CB  TYR A 318      49.563 -10.480   8.401  1.00 51.66           C  
ANISOU 3090  CB  TYR A 318     6707   4837   8083    287   -910     73       C  
ATOM   3091  CG  TYR A 318      48.941  -9.214   7.852  1.00 51.87           C  
ANISOU 3091  CG  TYR A 318     6745   4919   8044    222   -763     78       C  
ATOM   3092  CD1 TYR A 318      49.657  -8.025   7.826  1.00 55.23           C  
ANISOU 3092  CD1 TYR A 318     7026   5382   8577    164   -698    129       C  
ATOM   3093  CD2 TYR A 318      47.644  -9.209   7.356  1.00 45.28           C  
ANISOU 3093  CD2 TYR A 318     6064   4094   7047    216   -700     37       C  
ATOM   3094  CE1 TYR A 318      49.101  -6.866   7.325  1.00 52.52           C  
ANISOU 3094  CE1 TYR A 318     6706   5073   8175    110   -571    137       C  
ATOM   3095  CE2 TYR A 318      47.079  -8.052   6.851  1.00 48.81           C  
ANISOU 3095  CE2 TYR A 318     6519   4584   7442    169   -577     47       C  
ATOM   3096  CZ  TYR A 318      47.814  -6.883   6.838  1.00 50.97           C  
ANISOU 3096  CZ  TYR A 318     6663   4883   7820    120   -512     96       C  
ATOM   3097  OH  TYR A 318      47.262  -5.726   6.340  1.00 52.44           O  
ANISOU 3097  OH  TYR A 318     6872   5097   7957     76   -397    110       O  
HETATM 3098  N   YCM A 319      50.198 -13.338   8.516  1.00 59.58           N  
ANISOU 3098  N   YCM A 319     8688   6096   7852    575   -233   2348       N  
HETATM 3099  CA  YCM A 319      50.645 -14.528   9.200  1.00 60.24           C  
ANISOU 3099  CA  YCM A 319     8738   6539   7611    827   -534   2393       C  
HETATM 3100  CB  YCM A 319      49.466 -15.411   9.627  1.00 58.16           C  
ANISOU 3100  CB  YCM A 319     8879   6154   7066   1077   -586   2513       C  
HETATM 3101  SG  YCM A 319      49.910 -16.982  10.299  1.00 58.08           S  
ANISOU 3101  SG  YCM A 319     8857   6550   6660   1431   -931   2618       S  
HETATM 3102  CD  YCM A 319      49.903 -16.767  12.058  1.00 62.77           C  
ANISOU 3102  CD  YCM A 319     9512   7343   6996   1244  -1186   2304       C  
HETATM 3103  CE  YCM A 319      51.257 -16.877  12.705  1.00 70.73           C  
ANISOU 3103  CE  YCM A 319    10165   8787   7921   1176  -1447   2152       C  
HETATM 3104  OZ1 YCM A 319      51.953 -15.851  12.872  1.00 75.41           O  
ANISOU 3104  OZ1 YCM A 319    10507   9441   8705    863  -1423   1937       O  
HETATM 3105  NZ2 YCM A 319      51.695 -18.108  13.113  1.00 89.25           N  
ANISOU 3105  NZ2 YCM A 319    12474  11457   9981   1459  -1710   2251       N  
HETATM 3106  C   YCM A 319      51.625 -15.386   8.399  1.00 61.98           C  
ANISOU 3106  C   YCM A 319     8697   7014   7839   1077   -610   2602       C  
HETATM 3107  O   YCM A 319      52.770 -15.634   8.786  1.00 71.69           O  
ANISOU 3107  O   YCM A 319     9629   8612   8999   1072   -821   2520       O  
ATOM   3108  N   PHE A 320      51.159 -15.851   7.243  1.00 66.08           N  
ANISOU 3108  N   PHE A 320     9331   7329   8447   1303   -432   2880       N  
ATOM   3109  CA  PHE A 320      51.939 -16.775   6.422  1.00 65.79           C  
ANISOU 3109  CA  PHE A 320     9091   7503   8402   1578   -491   3110       C  
ATOM   3110  C   PHE A 320      53.253 -16.163   5.939  1.00 68.76           C  
ANISOU 3110  C   PHE A 320     9039   8063   9024   1398   -474   3031       C  
ATOM   3111  O   PHE A 320      54.249 -16.869   5.791  1.00 81.30           O  
ANISOU 3111  O   PHE A 320    10375   9973  10543   1559   -638   3108       O  
ATOM   3112  CB  PHE A 320      51.111 -17.250   5.220  1.00 63.67           C  
ANISOU 3112  CB  PHE A 320     9023   6967   8202   1732   -288   3253       C  
ATOM   3113  CG  PHE A 320      49.847 -17.985   5.595  1.00 62.90           C  
ANISOU 3113  CG  PHE A 320     9215   6797   7885   1645   -387   2934       C  
ATOM   3114  CD1 PHE A 320      49.730 -18.617   6.824  1.00 62.31           C  
ANISOU 3114  CD1 PHE A 320     9235   6887   7554   1725   -620   2907       C  
ATOM   3115  CD2 PHE A 320      48.781 -18.051   4.712  1.00 62.46           C  
ANISOU 3115  CD2 PHE A 320     9232   6579   7922   1446   -281   2679       C  
ATOM   3116  CE1 PHE A 320      48.575 -19.296   7.165  1.00 61.08           C  
ANISOU 3116  CE1 PHE A 320     9188   6687   7333   1577   -685   2684       C  
ATOM   3117  CE2 PHE A 320      47.621 -18.728   5.049  1.00 62.06           C  
ANISOU 3117  CE2 PHE A 320     9254   6539   7787   1313   -391   2462       C  
ATOM   3118  CZ  PHE A 320      47.518 -19.351   6.276  1.00 60.66           C  
ANISOU 3118  CZ  PHE A 320     9120   6486   7442   1369   -561   2485       C  
ATOM   3119  N   VAL A 321      53.261 -14.857   5.693  1.00 63.09           N  
ANISOU 3119  N   VAL A 321     8237   7141   8592   1066   -277   2877       N  
ATOM   3120  CA  VAL A 321      54.477 -14.152   5.306  1.00 68.84           C  
ANISOU 3120  CA  VAL A 321     8564   8029   9565    857   -252   2773       C  
ATOM   3121  C   VAL A 321      55.066 -13.367   6.482  1.00 69.11           C  
ANISOU 3121  C   VAL A 321     8430   8257   9574    542   -408   2438       C  
ATOM   3122  O   VAL A 321      55.906 -12.491   6.280  1.00 73.32           O  
ANISOU 3122  O   VAL A 321     8665   8855  10338    289   -353   2297       O  
ATOM   3123  CB  VAL A 321      54.246 -13.242   4.089  1.00 62.99           C  
ANISOU 3123  CB  VAL A 321     7794   6951   9187    708     79   2847       C  
ATOM   3124  CG1 VAL A 321      53.503 -13.996   2.993  1.00 71.42           C  
ANISOU 3124  CG1 VAL A 321     9076   7794  10266   1015    240   3172       C  
ATOM   3125  CG2 VAL A 321      53.496 -11.984   4.491  1.00 63.15           C  
ANISOU 3125  CG2 VAL A 321     7974   6668   9351    373    242   2635       C  
ATOM   3126  N   GLY A 322      54.636 -13.666   7.709  1.00 69.87           N  
ANISOU 3126  N   GLY A 322     8712   8445   9392    551   -599   2307       N  
ATOM   3127  CA  GLY A 322      55.163 -12.951   8.860  1.00 74.21           C  
ANISOU 3127  CA  GLY A 322     9113   9180   9903    258   -753   1988       C  
ATOM   3128  C   GLY A 322      56.594 -13.326   9.199  1.00 76.49           C  
ANISOU 3128  C   GLY A 322     9025   9918  10120    280  -1002   1916       C  
ATOM   3129  O   GLY A 322      57.394 -12.466   9.579  1.00 79.44           O  
ANISOU 3129  O   GLY A 322     9135  10426  10624     -8  -1041   1684       O  
ATOM   3130  N   ASN A 323      56.941 -14.609   9.072  1.00 74.22           N  
ANISOU 3130  N   ASN A 323     8706   9870   9626    619  -1174   2110       N  
ATOM   3131  CA  ASN A 323      58.315 -15.024   9.345  1.00 77.28           C  
ANISOU 3131  CA  ASN A 323     8731  10687   9944    658  -1413   2056       C  
ATOM   3132  C   ASN A 323      59.280 -14.476   8.300  1.00 78.65           C  
ANISOU 3132  C   ASN A 323     8556  10892  10436    548  -1273   2090       C  
ATOM   3133  O   ASN A 323      60.421 -14.126   8.624  1.00 82.05           O  
ANISOU 3133  O   ASN A 323     8650  11600  10924    389  -1401   1925       O  
ATOM   3134  CB  ASN A 323      58.408 -16.548   9.410  1.00 75.99           C  
ANISOU 3134  CB  ASN A 323     8629  10757   9489   1059  -1621   2269       C  
ATOM   3135  CG  ASN A 323      57.672 -17.127  10.601  1.00 75.31           C  
ANISOU 3135  CG  ASN A 323     8834  10719   9062   1157  -1811   2205       C  
ATOM   3136  OD1 ASN A 323      57.045 -16.401  11.372  1.00 96.50           O  
ANISOU 3136  OD1 ASN A 323    11688  13253  11725    930  -1783   2005       O  
ATOM   3137  ND2 ASN A 323      57.752 -18.443  10.763  1.00 74.36           N  
ANISOU 3137  ND2 ASN A 323     8770  10811   8671   1495  -2009   2372       N  
ATOM   3138  N   ARG A 324      58.841 -14.391   7.042  1.00 77.41           N  
ANISOU 3138  N   ARG A 324     8473  10452  10488    630  -1010   2302       N  
ATOM   3139  CA  ARG A 324      59.719 -13.898   5.985  1.00 78.53           C  
ANISOU 3139  CA  ARG A 324     8295  10608  10934    538   -865   2351       C  
ATOM   3140  C   ARG A 324      59.915 -12.390   6.066  1.00 81.10           C  
ANISOU 3140  C   ARG A 324     8484  10793  11538    121   -713   2104       C  
ATOM   3141  O   ARG A 324      60.939 -11.878   5.602  1.00 84.45           O  
ANISOU 3141  O   ARG A 324     8567  11341  12177    -25   -677   2047       O  
ATOM   3142  CB  ARG A 324      59.155 -14.309   4.621  1.00 76.79           C  
ANISOU 3142  CB  ARG A 324     8210  10127  10841    764   -634   2660       C  
ATOM   3143  CG  ARG A 324      59.367 -15.788   4.310  1.00 81.22           C  
ANISOU 3143  CG  ARG A 324     8778  10896  11186   1173   -785   2916       C  
ATOM   3144  CD  ARG A 324      58.643 -16.268   3.051  1.00 82.18           C  
ANISOU 3144  CD  ARG A 324     9088  10741  11397   1415   -563   3226       C  
ATOM   3145  NE  ARG A 324      59.015 -15.548   1.835  1.00 77.65           N  
ANISOU 3145  NE  ARG A 324     8323  10007  11172   1290   -312   3294       N  
ATOM   3146  CZ  ARG A 324      58.228 -14.684   1.195  1.00 84.80           C  
ANISOU 3146  CZ  ARG A 324     9387  10522  12312   1134    -23   3312       C  
ATOM   3147  NH1 ARG A 324      57.002 -14.419   1.633  1.00 92.49           N  
ANISOU 3147  NH1 ARG A 324    10715  11213  13213   1082     60   3270       N  
ATOM   3148  NH2 ARG A 324      58.667 -14.087   0.097  1.00 91.04           N  
ANISOU 3148  NH2 ARG A 324     9980  11200  13410   1030    187   3377       N  
ATOM   3149  N   PHE A 325      58.963 -11.663   6.654  1.00 78.70           N  
ANISOU 3149  N   PHE A 325     8436  10233  11234    -78   -624   1953       N  
ATOM   3150  CA  PHE A 325      59.111 -10.216   6.780  1.00 80.73           C  
ANISOU 3150  CA  PHE A 325     8574  10350  11750   -480   -481   1710       C  
ATOM   3151  C   PHE A 325      60.197  -9.864   7.791  1.00 88.10           C  
ANISOU 3151  C   PHE A 325     9212  11637  12625   -687   -714   1436       C  
ATOM   3152  O   PHE A 325      61.149  -9.140   7.476  1.00 88.93           O  
ANISOU 3152  O   PHE A 325     8990  11840  12959   -895   -669   1328       O  
ATOM   3153  CB  PHE A 325      57.776  -9.581   7.177  1.00 78.89           C  
ANISOU 3153  CB  PHE A 325     8704   9753  11519   -626   -333   1622       C  
ATOM   3154  CG  PHE A 325      57.729  -8.090   6.974  1.00 80.10           C  
ANISOU 3154  CG  PHE A 325     8778   9667  11989  -1009   -112   1437       C  
ATOM   3155  CD1 PHE A 325      57.521  -7.556   5.712  1.00 78.55           C  
ANISOU 3155  CD1 PHE A 325     8567   9182  12095  -1056    180   1574       C  
ATOM   3156  CD2 PHE A 325      57.893  -7.223   8.042  1.00 82.79           C  
ANISOU 3156  CD2 PHE A 325     9061  10072  12325  -1322   -195   1125       C  
ATOM   3157  CE1 PHE A 325      57.479  -6.188   5.519  1.00 79.66           C  
ANISOU 3157  CE1 PHE A 325     8636   9102  12528  -1407    383   1406       C  
ATOM   3158  CE2 PHE A 325      57.850  -5.855   7.854  1.00 83.91           C  
ANISOU 3158  CE2 PHE A 325     9129   9994  12759  -1674      8    954       C  
ATOM   3159  CZ  PHE A 325      57.644  -5.337   6.591  1.00 82.34           C  
ANISOU 3159  CZ  PHE A 325     8916   9508  12861  -1716    298   1096       C  
ATOM   3160  N   GLN A 326      60.065 -10.368   9.022  1.00 90.66           N  
ANISOU 3160  N   GLN A 326     9647  12156  12642   -632   -965   1320       N  
ATOM   3161  CA  GLN A 326      61.017 -10.027  10.073  1.00 94.58           C  
ANISOU 3161  CA  GLN A 326     9889  12981  13065   -834  -1193   1048       C  
ATOM   3162  C   GLN A 326      62.440 -10.416   9.688  1.00 96.90           C  
ANISOU 3162  C   GLN A 326     9780  13628  13410   -757  -1324   1091       C  
ATOM   3163  O   GLN A 326      63.397  -9.704  10.015  1.00100.27           O  
ANISOU 3163  O   GLN A 326     9901  14239  13956  -1007  -1388    879       O  
ATOM   3164  CB  GLN A 326      60.624 -10.727  11.375  1.00 94.69           C  
ANISOU 3164  CB  GLN A 326    10105  13162  12710   -724  -1454    964       C  
ATOM   3165  CG  GLN A 326      59.230 -10.397  11.896  1.00 98.35           C  
ANISOU 3165  CG  GLN A 326    10971  13305  13092   -797  -1354    904       C  
ATOM   3166  CD  GLN A 326      59.104  -8.974  12.400  1.00104.42           C  
ANISOU 3166  CD  GLN A 326    11713  13920  14043  -1210  -1247    615       C  
ATOM   3167  OE1 GLN A 326      60.073  -8.380  12.873  1.00116.73           O  
ANISOU 3167  OE1 GLN A 326    12976  15702  15673  -1439  -1351    397       O  
ATOM   3168  NE2 GLN A 326      57.897  -8.424  12.317  1.00 93.50           N  
ANISOU 3168  NE2 GLN A 326    10642  12153  12732  -1306  -1040    608       N  
ATOM   3169  N   GLN A 327      62.598 -11.538   8.984  1.00104.33           N  
ANISOU 3169  N   GLN A 327    10713  14665  14264   -413  -1364   1363       N  
ATOM   3170  CA  GLN A 327      63.933 -12.009   8.631  1.00106.51           C  
ANISOU 3170  CA  GLN A 327    10615  15287  14568   -313  -1501   1416       C  
ATOM   3171  C   GLN A 327      64.605 -11.077   7.631  1.00107.75           C  
ANISOU 3171  C   GLN A 327    10488  15355  15097   -521  -1286   1399       C  
ATOM   3172  O   GLN A 327      65.797 -10.774   7.761  1.00109.98           O  
ANISOU 3172  O   GLN A 327    10412  15907  15466   -656  -1392   1266       O  
ATOM   3173  CB  GLN A 327      63.857 -13.431   8.073  1.00104.99           C  
ANISOU 3173  CB  GLN A 327    10502  15190  14200    109  -1577   1721       C  
ATOM   3174  CG  GLN A 327      65.206 -14.035   7.706  1.00106.03           C  
ANISOU 3174  CG  GLN A 327    10262  15686  14340    245  -1729   1794       C  
ATOM   3175  CD  GLN A 327      66.155 -14.104   8.891  1.00118.65           C  
ANISOU 3175  CD  GLN A 327    11632  17680  15769    146  -2035   1563       C  
ATOM   3176  OE1 GLN A 327      65.768 -14.510   9.987  1.00120.15           O  
ANISOU 3176  OE1 GLN A 327    11999  17971  15680    194  -2229   1472       O  
ATOM   3177  NE2 GLN A 327      67.405 -13.708   8.675  1.00111.82           N  
ANISOU 3177  NE2 GLN A 327    10375  17042  15071      7  -2078   1466       N  
ATOM   3178  N   LYS A 328      63.860 -10.611   6.626  1.00 97.08           N  
ANISOU 3178  N   LYS A 328     9290  13627  13968   -548   -986   1533       N  
ATOM   3179  CA  LYS A 328      64.456  -9.785   5.582  1.00 96.80           C  
ANISOU 3179  CA  LYS A 328     9000  13493  14288   -722   -769   1545       C  
ATOM   3180  C   LYS A 328      64.745  -8.363   6.046  1.00 97.38           C  
ANISOU 3180  C   LYS A 328     8927  13508  14565  -1145   -699   1243       C  
ATOM   3181  O   LYS A 328      65.518  -7.660   5.386  1.00102.53           O  
ANISOU 3181  O   LYS A 328     9293  14171  15492  -1320   -579   1202       O  
ATOM   3182  CB  LYS A 328      63.540  -9.776   4.357  1.00 88.11           C  
ANISOU 3182  CB  LYS A 328     8121  12006  13352   -605   -473   1792       C  
ATOM   3183  CG  LYS A 328      63.413 -11.145   3.706  1.00 85.53           C  
ANISOU 3183  CG  LYS A 328     7882  11747  12870   -189   -522   2106       C  
ATOM   3184  CD  LYS A 328      62.693 -11.090   2.375  1.00 82.22           C  
ANISOU 3184  CD  LYS A 328     7622  10970  12649    -87   -222   2352       C  
ATOM   3185  CE  LYS A 328      62.476 -12.491   1.821  1.00 95.06           C  
ANISOU 3185  CE  LYS A 328     9365  12658  14094    334   -281   2658       C  
ATOM   3186  NZ  LYS A 328      63.766 -13.173   1.505  1.00 87.27           N  
ANISOU 3186  NZ  LYS A 328     8031  12040  13088    487   -441   2735       N  
ATOM   3187  N   LEU A 329      64.155  -7.921   7.157  1.00 95.13           N  
ANISOU 3187  N   LEU A 329     8828  13164  14154  -1317   -769   1032       N  
ATOM   3188  CA  LEU A 329      64.575  -6.657   7.754  1.00 99.75           C  
ANISOU 3188  CA  LEU A 329     9241  13762  14898  -1713   -752    723       C  
ATOM   3189  C   LEU A 329      65.858  -6.838   8.558  1.00102.05           C  
ANISOU 3189  C   LEU A 329     9200  14499  15075  -1769  -1038    547       C  
ATOM   3190  O   LEU A 329      66.748  -5.982   8.517  1.00107.54           O  
ANISOU 3190  O   LEU A 329     9587  15295  15979  -2030  -1014    375       O  
ATOM   3191  CB  LEU A 329      63.462  -6.079   8.625  1.00100.44           C  
ANISOU 3191  CB  LEU A 329     9648  13611  14903  -1885   -712    558       C  
ATOM   3192  CG  LEU A 329      62.183  -5.709   7.870  1.00 94.12           C  
ANISOU 3192  CG  LEU A 329     9169  12345  14247  -1882   -412    696       C  
ATOM   3193  CD1 LEU A 329      61.091  -5.295   8.841  1.00 94.25           C  
ANISOU 3193  CD1 LEU A 329     9510  12162  14137  -2018   -410    536       C  
ATOM   3194  CD2 LEU A 329      62.454  -4.600   6.861  1.00 94.39           C  
ANISOU 3194  CD2 LEU A 329     9028  12165  14673  -2120   -136    681       C  
ATOM   3195  N   ARG A 330      65.965  -7.948   9.290  1.00102.06           N  
ANISOU 3195  N   ARG A 330     9259  14771  14748  -1526  -1310    589       N  
ATOM   3196  CA  ARG A 330      67.194  -8.279  10.000  1.00105.47           C  
ANISOU 3196  CA  ARG A 330     9378  15644  15052  -1533  -1596    454       C  
ATOM   3197  C   ARG A 330      68.354  -8.548   9.054  1.00113.55           C  
ANISOU 3197  C   ARG A 330    10046  16864  16235  -1440  -1590    580       C  
ATOM   3198  O   ARG A 330      69.513  -8.457   9.474  1.00110.40           O  
ANISOU 3198  O   ARG A 330     9319  16792  15835  -1537  -1767    431       O  
ATOM   3199  CB  ARG A 330      66.931  -9.497  10.886  1.00104.77           C  
ANISOU 3199  CB  ARG A 330     9468  15769  14572  -1257  -1871    510       C  
ATOM   3200  CG  ARG A 330      66.064  -9.211  12.104  1.00104.71           C  
ANISOU 3200  CG  ARG A 330     9741  15670  14374  -1386  -1949    320       C  
ATOM   3201  CD  ARG A 330      65.283 -10.443  12.524  1.00119.20           C  
ANISOU 3201  CD  ARG A 330    11889  17531  15871  -1056  -2093    482       C  
ATOM   3202  NE  ARG A 330      66.096 -11.643  12.675  1.00122.32           N  
ANISOU 3202  NE  ARG A 330    12122  18304  16050   -775  -2354    594       N  
ATOM   3203  CZ  ARG A 330      65.590 -12.873  12.713  1.00121.97           C  
ANISOU 3203  CZ  ARG A 330    12297  18302  15746   -428  -2462    802       C  
ATOM   3204  NH1 ARG A 330      66.390 -13.921  12.843  1.00125.97           N  
ANISOU 3204  NH1 ARG A 330    12634  19158  16069   -186  -2700    895       N  
ATOM   3205  NH2 ARG A 330      64.279 -13.055  12.609  1.00110.61           N  
ANISOU 3205  NH2 ARG A 330    11245  16550  14233   -323  -2331    919       N  
ATOM   3206  N   SER A 331      68.071  -8.876   7.793  1.00107.27           N  
ANISOU 3206  N   SER A 331     9305  15876  15576  -1255  -1390    848       N  
ATOM   3207  CA  SER A 331      69.132  -9.067   6.810  1.00104.88           C  
ANISOU 3207  CA  SER A 331     8669  15731  15450  -1179  -1356    971       C  
ATOM   3208  C   SER A 331      69.645  -7.721   6.313  1.00106.82           C  
ANISOU 3208  C   SER A 331     8674  15859  16054  -1527  -1155    821       C  
ATOM   3209  O   SER A 331      70.856  -7.482   6.276  1.00115.00           O  
ANISOU 3209  O   SER A 331     9342  17155  17196  -1636  -1240    719       O  
ATOM   3210  CB  SER A 331      68.627  -9.918   5.647  1.00105.94           C  
ANISOU 3210  CB  SER A 331     8956  15702  15594   -853  -1216   1314       C  
ATOM   3211  OG  SER A 331      68.238 -11.204   6.096  1.00108.10           O  
ANISOU 3211  OG  SER A 331     9429  16110  15536   -523  -1414   1455       O  
ATOM   3212  N   VAL A 332      68.727  -6.828   5.927  1.00115.26           N  
ANISOU 3212  N   VAL A 332     9947  16532  17313  -1705   -886    805       N  
ATOM   3213  CA  VAL A 332      69.113  -5.490   5.484  1.00123.42           C  
ANISOU 3213  CA  VAL A 332    10780  17424  18691  -2050   -682    656       C  
ATOM   3214  C   VAL A 332      69.505  -4.590   6.643  1.00121.13           C  
ANISOU 3214  C   VAL A 332    10365  17261  18397  -2384   -802    311       C  
ATOM   3215  O   VAL A 332      69.924  -3.448   6.412  1.00112.11           O  
ANISOU 3215  O   VAL A 332     9029  16038  17529  -2692   -661    154       O  
ATOM   3216  CB  VAL A 332      67.975  -4.813   4.694  1.00121.07           C  
ANISOU 3216  CB  VAL A 332    10748  16651  18601  -2134   -352    751       C  
ATOM   3217  CG1 VAL A 332      67.566  -5.675   3.511  1.00114.34           C  
ANISOU 3217  CG1 VAL A 332    10023  15660  17761  -1808   -222   1094       C  
ATOM   3218  CG2 VAL A 332      66.782  -4.538   5.597  1.00120.01           C  
ANISOU 3218  CG2 VAL A 332    10976  16305  18319  -2221   -350    633       C  
ATOM   3219  N   PHE A 333      69.379  -5.067   7.879  1.00129.18           N  
ANISOU 3219  N   PHE A 333    11490  18476  19115  -2334  -1057    189       N  
ATOM   3220  CA  PHE A 333      69.760  -4.334   9.078  1.00132.40           C  
ANISOU 3220  CA  PHE A 333    11788  19039  19481  -2627  -1204   -137       C  
ATOM   3221  C   PHE A 333      70.840  -5.104   9.832  1.00135.07           C  
ANISOU 3221  C   PHE A 333    11881  19845  19595  -2513  -1537   -207       C  
ATOM   3222  O   PHE A 333      70.826  -5.195  11.062  1.00136.57           O  
ANISOU 3222  O   PHE A 333    12124  20207  19560  -2571  -1755   -391       O  
ATOM   3223  CB  PHE A 333      68.551  -4.085   9.978  1.00131.08           C  
ANISOU 3223  CB  PHE A 333    11989  18660  19157  -2709  -1201   -250       C  
ATOM   3224  CG  PHE A 333      67.512  -3.174   9.374  1.00128.87           C  
ANISOU 3224  CG  PHE A 333    11937  17921  19106  -2871   -880   -228       C  
ATOM   3225  CD1 PHE A 333      67.855  -2.236   8.414  1.00129.39           C  
ANISOU 3225  CD1 PHE A 333    11817  17818  19527  -3071   -636   -231       C  
ATOM   3226  CD2 PHE A 333      66.188  -3.257   9.776  1.00127.98           C  
ANISOU 3226  CD2 PHE A 333    12226  17546  18854  -2826   -824   -205       C  
ATOM   3227  CE1 PHE A 333      66.898  -1.403   7.864  1.00127.37           C  
ANISOU 3227  CE1 PHE A 333    11772  17141  19482  -3220   -345   -210       C  
ATOM   3228  CE2 PHE A 333      65.228  -2.426   9.231  1.00127.61           C  
ANISOU 3228  CE2 PHE A 333    12390  17077  19018  -2974   -532   -186       C  
ATOM   3229  CZ  PHE A 333      65.583  -1.499   8.274  1.00126.24           C  
ANISOU 3229  CZ  PHE A 333    12028  16740  19198  -3171   -293   -187       C  
ATOM   3230  N   ARG A 334      71.779  -5.684   9.091  1.00130.38           N  
ANISOU 3230  N   ARG A 334    11020  19460  19058  -2343  -1581    -57       N  
ATOM   3231  CA  ARG A 334      72.847  -6.484   9.679  1.00123.55           C  
ANISOU 3231  CA  ARG A 334     9909  19042  17994  -2209  -1891    -95       C  
ATOM   3232  C   ARG A 334      74.014  -5.594  10.096  1.00124.11           C  
ANISOU 3232  C   ARG A 334     9603  19335  18217  -2520  -1967   -367       C  
ATOM   3233  O   ARG A 334      73.997  -4.995  11.171  1.00126.12           O  
ANISOU 3233  O   ARG A 334     9868  19649  18404  -2753  -2071   -629       O  
ATOM   3234  CB  ARG A 334      73.322  -7.554   8.690  1.00118.60           C  
ANISOU 3234  CB  ARG A 334     9167  18542  17353  -1873  -1907    195       C  
ATOM   3235  CG  ARG A 334      74.420  -8.456   9.238  1.00128.67           C  
ANISOU 3235  CG  ARG A 334    10191  20277  18421  -1710  -2227    175       C  
ATOM   3236  CD  ARG A 334      74.789  -9.576   8.269  1.00125.23           C  
ANISOU 3236  CD  ARG A 334     9673  19951  17957  -1359  -2242    474       C  
ATOM   3237  NE  ARG A 334      73.696 -10.526   8.072  1.00115.55           N  
ANISOU 3237  NE  ARG A 334     8812  18558  16534  -1048  -2218    714       N  
ATOM   3238  CZ  ARG A 334      72.962 -10.626   6.964  1.00112.82           C  
ANISOU 3238  CZ  ARG A 334     8647  17900  16319   -920  -1967    950       C  
ATOM   3239  NH1 ARG A 334      73.191  -9.840   5.920  1.00112.26           N  
ANISOU 3239  NH1 ARG A 334     8429  17646  16579  -1071  -1712    985       N  
ATOM   3240  NH2 ARG A 334      71.992 -11.528   6.899  1.00112.65           N  
ANISOU 3240  NH2 ARG A 334     8955  17752  16093   -636  -1972   1153       N  
TER    3241      ARG A 334                                                      
ATOM   3242  N   ALA B1001      64.617  11.418  54.835  1.00174.90           N  
ANISOU 3242  N   ALA B1001    23418  26742  16295   1117   2844    833       N  
ATOM   3243  CA  ALA B1001      63.209  11.367  55.208  1.00195.51           C  
ANISOU 3243  CA  ALA B1001    25680  29818  18787   1270   3073   1058       C  
ATOM   3244  C   ALA B1001      62.800   9.933  55.558  1.00180.36           C  
ANISOU 3244  C   ALA B1001    23420  28171  16939    932   2947   1439       C  
ATOM   3245  O   ALA B1001      63.233   9.398  56.579  1.00192.63           O  
ANISOU 3245  O   ALA B1001    25041  29834  18314    723   2917   1523       O  
ATOM   3246  CB  ALA B1001      62.345  11.922  54.085  1.00183.67           C  
ANISOU 3246  CB  ALA B1001    24019  28296  17472   1539   3144   1030       C  
ATOM   3247  N   ASP B1002      61.967   9.316  54.721  1.00162.77           N  
ANISOU 3247  N   ASP B1002    20832  26044  14968    880   2868   1668       N  
ATOM   3248  CA  ASP B1002      61.473   7.970  54.968  1.00167.96           C  
ANISOU 3248  CA  ASP B1002    21138  26964  15715    571   2756   2040       C  
ATOM   3249  C   ASP B1002      61.686   7.100  53.737  1.00170.88           C  
ANISOU 3249  C   ASP B1002    21356  27083  16488    341   2434   2162       C  
ATOM   3250  O   ASP B1002      61.803   7.592  52.612  1.00164.84           O  
ANISOU 3250  O   ASP B1002    20660  26037  15934    483   2360   2004       O  
ATOM   3251  CB  ASP B1002      59.982   7.981  55.341  1.00173.47           C  
ANISOU 3251  CB  ASP B1002    21462  28147  16302    735   3023   2250       C  
ATOM   3252  CG  ASP B1002      59.445   6.596  55.641  1.00184.15           C  
ANISOU 3252  CG  ASP B1002    22450  29782  17737    409   2924   2639       C  
ATOM   3253  OD1 ASP B1002      59.829   6.019  56.680  1.00177.19           O  
ANISOU 3253  OD1 ASP B1002    21635  29025  16663    181   2909   2751       O  
ATOM   3254  OD2 ASP B1002      58.643   6.080  54.834  1.00181.14           O  
ANISOU 3254  OD2 ASP B1002    21723  29490  17614    380   2856   2831       O  
ATOM   3255  N   LEU B1003      61.747   5.788  53.973  1.00173.81           N  
ANISOU 3255  N   LEU B1003    21526  27553  16959    -21   2239   2447       N  
ATOM   3256  CA  LEU B1003      61.922   4.839  52.878  1.00173.28           C  
ANISOU 3256  CA  LEU B1003    21287  27277  17275   -267   1922   2591       C  
ATOM   3257  C   LEU B1003      60.764   4.920  51.889  1.00177.69           C  
ANISOU 3257  C   LEU B1003    21514  27955  18045    -89   1977   2702       C  
ATOM   3258  O   LEU B1003      60.975   5.058  50.678  1.00180.24           O  
ANISOU 3258  O   LEU B1003    21868  27977  18638    -45   1819   2601       O  
ATOM   3259  CB  LEU B1003      62.063   3.426  53.446  1.00172.46           C  
ANISOU 3259  CB  LEU B1003    21006  27312  17207   -672   1729   2897       C  
ATOM   3260  CG  LEU B1003      62.371   2.299  52.462  1.00165.19           C  
ANISOU 3260  CG  LEU B1003    19920  26174  16670   -978   1369   3057       C  
ATOM   3261  CD1 LEU B1003      63.331   1.302  53.088  1.00152.63           C  
ANISOU 3261  CD1 LEU B1003    18441  24482  15068  -1358   1121   3151       C  
ATOM   3262  CD2 LEU B1003      61.089   1.599  52.037  1.00165.15           C  
ANISOU 3262  CD2 LEU B1003    19443  26469  16838  -1013   1385   3379       C  
ATOM   3263  N   GLU B1004      59.526   4.837  52.388  1.00202.29           N  
ANISOU 3263  N   GLU B1004    24310  31509  21044     16   2203   2906       N  
ATOM   3264  CA  GLU B1004      58.364   4.950  51.511  1.00201.82           C  
ANISOU 3264  CA  GLU B1004    23920  31585  21177    207   2267   3002       C  
ATOM   3265  C   GLU B1004      58.227   6.342  50.914  1.00200.88           C  
ANISOU 3265  C   GLU B1004    23993  31306  21026    619   2424   2695       C  
ATOM   3266  O   GLU B1004      57.736   6.486  49.789  1.00199.94           O  
ANISOU 3266  O   GLU B1004    23735  31083  21151    753   2356   2688       O  
ATOM   3267  CB  GLU B1004      57.070   4.613  52.243  1.00205.13           C  
ANISOU 3267  CB  GLU B1004    23955  32519  21466    238   2496   3264       C  
ATOM   3268  CG  GLU B1004      55.862   4.590  51.294  1.00205.98           C  
ANISOU 3268  CG  GLU B1004    23684  32765  21815    405   2526   3379       C  
ATOM   3269  CD  GLU B1004      54.562   4.217  51.968  1.00210.03           C  
ANISOU 3269  CD  GLU B1004    23787  33787  22229    423   2751   3635       C  
ATOM   3270  OE1 GLU B1004      54.550   4.084  53.203  1.00212.41           O  
ANISOU 3270  OE1 GLU B1004    24115  34348  22242    335   2919   3711       O  
ATOM   3271  OE2 GLU B1004      53.564   4.022  51.246  1.00210.85           O  
ANISOU 3271  OE2 GLU B1004    23540  34023  22550    513   2751   3761       O  
ATOM   3272  N   ASP B1005      58.603   7.382  51.659  1.00187.26           N  
ANISOU 3272  N   ASP B1005    22583  29568  18998    833   2637   2446       N  
ATOM   3273  CA  ASP B1005      58.539   8.715  51.079  1.00186.97           C  
ANISOU 3273  CA  ASP B1005    22757  29350  18934   1218   2771   2145       C  
ATOM   3274  C   ASP B1005      59.518   8.832  49.922  1.00184.65           C  
ANISOU 3274  C   ASP B1005    22719  28548  18891   1156   2512   1963       C  
ATOM   3275  O   ASP B1005      59.247   9.542  48.947  1.00183.20           O  
ANISOU 3275  O   ASP B1005    22583  28190  18836   1405   2525   1818       O  
ATOM   3276  CB  ASP B1005      58.828   9.772  52.142  1.00188.83           C  
ANISOU 3276  CB  ASP B1005    23295  29657  18796   1439   3036   1910       C  
ATOM   3277  CG  ASP B1005      57.767   9.813  53.221  1.00193.14           C  
ANISOU 3277  CG  ASP B1005    23590  30711  19083   1552   3330   2059       C  
ATOM   3278  OD1 ASP B1005      56.603   9.470  52.924  1.00194.96           O  
ANISOU 3278  OD1 ASP B1005    23427  31220  19429   1609   3394   2263       O  
ATOM   3279  OD2 ASP B1005      58.092  10.200  54.364  1.00194.78           O  
ANISOU 3279  OD2 ASP B1005    23996  31041  18972   1588   3499   1966       O  
ATOM   3280  N   ASN B1006      60.655   8.143  50.015  1.00171.45           N  
ANISOU 3280  N   ASN B1006    21219  26635  17289    827   2276   1964       N  
ATOM   3281  CA  ASN B1006      61.543   8.007  48.868  1.00181.09           C  
ANISOU 3281  CA  ASN B1006    22617  27397  18791    704   2002   1837       C  
ATOM   3282  C   ASN B1006      60.918   7.114  47.801  1.00181.00           C  
ANISOU 3282  C   ASN B1006    22254  27396  19122    576   1801   2077       C  
ATOM   3283  O   ASN B1006      61.242   7.247  46.617  1.00186.26           O  
ANISOU 3283  O   ASN B1006    23010  27730  20030    596   1637   1967       O  
ATOM   3284  CB  ASN B1006      62.899   7.467  49.314  1.00189.05           C  
ANISOU 3284  CB  ASN B1006    23877  28167  19787    383   1802   1772       C  
ATOM   3285  CG  ASN B1006      63.664   8.460  50.168  1.00199.89           C  
ANISOU 3285  CG  ASN B1006    25650  29439  20859    528   1969   1477       C  
ATOM   3286  OD1 ASN B1006      63.668   9.660  49.891  1.00209.98           O  
ANISOU 3286  OD1 ASN B1006    27149  30582  22051    842   2132   1217       O  
ATOM   3287  ND2 ASN B1006      64.310   7.966  51.217  1.00189.78           N  
ANISOU 3287  ND2 ASN B1006    24469  28221  19417    303   1923   1516       N  
ATOM   3288  N   TRP B1007      60.030   6.198  48.199  1.00161.76           N  
ANISOU 3288  N   TRP B1007    19419  25332  16710    438   1811   2403       N  
ATOM   3289  CA  TRP B1007      59.371   5.333  47.224  1.00161.49           C  
ANISOU 3289  CA  TRP B1007    19027  25330  17003    321   1624   2639       C  
ATOM   3290  C   TRP B1007      58.418   6.125  46.340  1.00158.95           C  
ANISOU 3290  C   TRP B1007    18591  25030  16772    679   1744   2566       C  
ATOM   3291  O   TRP B1007      58.185   5.745  45.187  1.00157.57           O  
ANISOU 3291  O   TRP B1007    18267  24706  16897    646   1554   2636       O  
ATOM   3292  CB  TRP B1007      58.620   4.216  47.949  1.00165.67           C  
ANISOU 3292  CB  TRP B1007    19162  26270  17517     95   1632   3000       C  
ATOM   3293  CG  TRP B1007      57.960   3.203  47.058  1.00164.52           C  
ANISOU 3293  CG  TRP B1007    18626  26177  17706    -64   1428   3266       C  
ATOM   3294  CD1 TRP B1007      58.558   2.445  46.093  1.00166.55           C  
ANISOU 3294  CD1 TRP B1007    18878  26128  18276   -304   1098   3312       C  
ATOM   3295  CD2 TRP B1007      56.578   2.820  47.070  1.00163.16           C  
ANISOU 3295  CD2 TRP B1007    18006  26394  17594      1   1540   3521       C  
ATOM   3296  NE1 TRP B1007      57.633   1.621  45.497  1.00165.68           N  
ANISOU 3296  NE1 TRP B1007    18351  26187  18415   -387    992   3581       N  
ATOM   3297  CE2 TRP B1007      56.410   1.831  46.080  1.00162.56           C  
ANISOU 3297  CE2 TRP B1007    17675  26217  17875   -205   1258   3713       C  
ATOM   3298  CE3 TRP B1007      55.466   3.219  47.820  1.00165.70           C  
ANISOU 3298  CE3 TRP B1007    18112  27139  17707    214   1853   3597       C  
ATOM   3299  CZ2 TRP B1007      55.175   1.238  45.819  1.00160.74           C  
ANISOU 3299  CZ2 TRP B1007    16984  26290  17801   -204   1276   3977       C  
ATOM   3300  CZ3 TRP B1007      54.235   2.642  47.544  1.00163.71           C  
ANISOU 3300  CZ3 TRP B1007    17397  27188  17616    215   1878   3851       C  
ATOM   3301  CH2 TRP B1007      54.105   1.649  46.568  1.00161.82           C  
ANISOU 3301  CH2 TRP B1007    16912  26837  17734      2   1588   4042       C  
ATOM   3302  N   GLU B1008      57.853   7.217  46.859  1.00153.38           N  
ANISOU 3302  N   GLU B1008    17953  24509  15815   1027   2050   2423       N  
ATOM   3303  CA  GLU B1008      57.080   8.116  46.009  1.00146.59           C  
ANISOU 3303  CA  GLU B1008    17056  23615  15028   1396   2154   2299       C  
ATOM   3304  C   GLU B1008      57.997   8.916  45.090  1.00149.30           C  
ANISOU 3304  C   GLU B1008    17806  23469  15452   1511   2049   1994       C  
ATOM   3305  O   GLU B1008      57.602   9.260  43.970  1.00150.64           O  
ANISOU 3305  O   GLU B1008    17946  23480  15810   1690   1985   1938       O  
ATOM   3306  CB  GLU B1008      56.213   9.040  46.861  1.00160.24           C  
ANISOU 3306  CB  GLU B1008    18734  25686  16463   1734   2507   2228       C  
ATOM   3307  CG  GLU B1008      55.096   8.316  47.603  1.00186.76           C  
ANISOU 3307  CG  GLU B1008    21643  29547  19770   1660   2637   2530       C  
ATOM   3308  CD  GLU B1008      54.186   7.531  46.674  1.00186.54           C  
ANISOU 3308  CD  GLU B1008    21197  29615  20065   1600   2486   2768       C  
ATOM   3309  OE1 GLU B1008      54.071   7.914  45.490  1.00181.80           O  
ANISOU 3309  OE1 GLU B1008    20636  28767  19673   1766   2373   2661       O  
ATOM   3310  OE2 GLU B1008      53.595   6.527  47.124  1.00187.50           O  
ANISOU 3310  OE2 GLU B1008    20957  30054  20230   1383   2478   3062       O  
ATOM   3311  N   THR B1009      59.218   9.217  45.543  1.00152.31           N  
ANISOU 3311  N   THR B1009    18573  23604  15695   1409   2029   1793       N  
ATOM   3312  CA  THR B1009      60.196   9.846  44.661  1.00156.20           C  
ANISOU 3312  CA  THR B1009    19451  23611  16287   1458   1910   1513       C  
ATOM   3313  C   THR B1009      60.471   8.970  43.447  1.00152.29           C  
ANISOU 3313  C   THR B1009    18851  22859  16152   1221   1593   1622       C  
ATOM   3314  O   THR B1009      60.626   9.476  42.329  1.00150.80           O  
ANISOU 3314  O   THR B1009    18820  22359  16116   1354   1515   1467       O  
ATOM   3315  CB  THR B1009      61.495  10.123  45.424  1.00160.22           C  
ANISOU 3315  CB  THR B1009    20348  23919  16611   1331   1918   1305       C  
ATOM   3316  OG1 THR B1009      61.266  11.126  46.424  1.00154.92           O  
ANISOU 3316  OG1 THR B1009    19823  23438  15603   1602   2219   1155       O  
ATOM   3317  CG2 THR B1009      62.613  10.546  44.478  1.00132.86           C  
ANISOU 3317  CG2 THR B1009    17254  19936  13292   1297   1758   1039       C  
ATOM   3318  N   LEU B1010      60.535   7.653  43.644  1.00150.90           N  
ANISOU 3318  N   LEU B1010    18418  22805  16113    869   1405   1887       N  
ATOM   3319  CA  LEU B1010      60.694   6.752  42.510  1.00149.95           C  
ANISOU 3319  CA  LEU B1010    18155  22477  16343    644   1101   2012       C  
ATOM   3320  C   LEU B1010      59.457   6.780  41.622  1.00145.53           C  
ANISOU 3320  C   LEU B1010    17290  22049  15956    849   1110   2143       C  
ATOM   3321  O   LEU B1010      59.551   7.025  40.413  1.00140.66           O  
ANISOU 3321  O   LEU B1010    16764  21140  15540    933    981   2042       O  
ATOM   3322  CB  LEU B1010      60.971   5.330  42.994  1.00155.83           C  
ANISOU 3322  CB  LEU B1010    18676  23347  17184    230    902   2278       C  
ATOM   3323  CG  LEU B1010      62.406   5.015  43.415  1.00142.07           C  
ANISOU 3323  CG  LEU B1010    17232  21340  15409    -55    752   2152       C  
ATOM   3324  CD1 LEU B1010      62.686   5.473  44.836  1.00143.39           C  
ANISOU 3324  CD1 LEU B1010    17573  21685  15223     -8    968   2067       C  
ATOM   3325  CD2 LEU B1010      62.672   3.527  43.261  1.00129.66           C  
ANISOU 3325  CD2 LEU B1010    15426  19765  14074   -462    450   2406       C  
ATOM   3326  N   ASN B1011      58.282   6.535  42.208  1.00137.56           N  
ANISOU 3326  N   ASN B1011    15916  21479  14871    934   1261   2361       N  
ATOM   3327  CA  ASN B1011      57.057   6.486  41.420  1.00135.17           C  
ANISOU 3327  CA  ASN B1011    15285  21329  14746   1120   1261   2495       C  
ATOM   3328  C   ASN B1011      56.687   7.845  40.841  1.00133.12           C  
ANISOU 3328  C   ASN B1011    15223  20940  14418   1548   1419   2244       C  
ATOM   3329  O   ASN B1011      55.943   7.899  39.856  1.00133.82           O  
ANISOU 3329  O   ASN B1011    15142  21002  14702   1706   1349   2287       O  
ATOM   3330  CB  ASN B1011      55.906   5.946  42.268  1.00134.51           C  
ANISOU 3330  CB  ASN B1011    14767  21756  14584   1108   1411   2770       C  
ATOM   3331  CG  ASN B1011      55.422   4.590  41.791  1.00131.70           C  
ANISOU 3331  CG  ASN B1011    14001  21518  14523    833   1180   3089       C  
ATOM   3332  OD1 ASN B1011      54.642   4.496  40.844  1.00135.72           O  
ANISOU 3332  OD1 ASN B1011    14281  22032  15253    955   1100   3163       O  
ATOM   3333  ND2 ASN B1011      55.891   3.530  42.439  1.00128.88           N  
ANISOU 3333  ND2 ASN B1011    13555  21244  14169    462   1062   3278       N  
ATOM   3334  N   ASP B1012      57.184   8.939  41.422  1.00118.72           N  
ANISOU 3334  N   ASP B1012    13757  19027  12322   1743   1620   1980       N  
ATOM   3335  CA  ASP B1012      56.980  10.245  40.806  1.00119.04           C  
ANISOU 3335  CA  ASP B1012    14041  18883  12307   2134   1742   1720       C  
ATOM   3336  C   ASP B1012      57.902  10.435  39.608  1.00115.45           C  
ANISOU 3336  C   ASP B1012    13907  17921  12039   2077   1529   1542       C  
ATOM   3337  O   ASP B1012      57.489  10.993  38.586  1.00115.22           O  
ANISOU 3337  O   ASP B1012    13928  17725  12124   2314   1500   1452       O  
ATOM   3338  CB  ASP B1012      57.202  11.358  41.831  1.00120.85           C  
ANISOU 3338  CB  ASP B1012    14548  19185  12186   2362   2028   1494       C  
ATOM   3339  CG  ASP B1012      56.047  11.493  42.805  1.00130.90           C  
ANISOU 3339  CG  ASP B1012    15514  20954  13266   2542   2286   1620       C  
ATOM   3340  OD1 ASP B1012      55.055  10.747  42.665  1.00128.95           O  
ANISOU 3340  OD1 ASP B1012    14836  20993  13166   2495   2249   1878       O  
ATOM   3341  OD2 ASP B1012      56.131  12.350  43.710  1.00135.08           O  
ANISOU 3341  OD2 ASP B1012    16232  21588  13502   2731   2529   1455       O  
ATOM   3342  N   ASN B1013      59.152   9.977  39.715  1.00112.09           N  
ANISOU 3342  N   ASN B1013    13702  17241  11646   1765   1378   1484       N  
ATOM   3343  CA  ASN B1013      60.055  10.009  38.572  1.00100.41           C  
ANISOU 3343  CA  ASN B1013    12496  15290  10367   1662   1164   1332       C  
ATOM   3344  C   ASN B1013      59.721   8.932  37.547  1.00100.80           C  
ANISOU 3344  C   ASN B1013    12251  15296  10753   1467    891   1557       C  
ATOM   3345  O   ASN B1013      60.068   9.086  36.372  1.00 96.80           O  
ANISOU 3345  O   ASN B1013    11910  14441  10430   1481    738   1448       O  
ATOM   3346  CB  ASN B1013      61.503   9.858  39.040  1.00 96.47           C  
ANISOU 3346  CB  ASN B1013    12312  14538   9802   1390   1091   1182       C  
ATOM   3347  CG  ASN B1013      62.024  11.107  39.725  1.00 94.76           C  
ANISOU 3347  CG  ASN B1013    12485  14228   9292   1608   1329    885       C  
ATOM   3348  OD1 ASN B1013      62.328  12.104  39.070  1.00 95.12           O  
ANISOU 3348  OD1 ASN B1013    12851  13970   9319   1819   1380    633       O  
ATOM   3349  ND2 ASN B1013      62.133  11.059  41.047  1.00103.81           N  
ANISOU 3349  ND2 ASN B1013    13614  15628  10202   1556   1472    914       N  
ATOM   3350  N   LEU B1014      59.059   7.848  37.963  1.00117.27           N  
ANISOU 3350  N   LEU B1014    13910  17725  12923   1284    827   1866       N  
ATOM   3351  CA  LEU B1014      58.580   6.864  36.998  1.00117.02           C  
ANISOU 3351  CA  LEU B1014    13563  17688  13213   1136    581   2089       C  
ATOM   3352  C   LEU B1014      57.536   7.469  36.070  1.00101.03           C  
ANISOU 3352  C   LEU B1014    11433  15674  11278   1480    623   2070       C  
ATOM   3353  O   LEU B1014      57.469   7.120  34.886  1.00103.28           O  
ANISOU 3353  O   LEU B1014    11668  15751  11823   1441    409   2108       O  
ATOM   3354  CB  LEU B1014      58.002   5.649  37.723  1.00123.97           C  
ANISOU 3354  CB  LEU B1014    14001  18959  14142    891    533   2424       C  
ATOM   3355  CG  LEU B1014      58.937   4.458  37.939  1.00121.49           C  
ANISOU 3355  CG  LEU B1014    13665  18546  13950    443    295   2547       C  
ATOM   3356  CD1 LEU B1014      58.316   3.463  38.906  1.00130.50           C  
ANISOU 3356  CD1 LEU B1014    14415  20111  15057    245    316   2860       C  
ATOM   3357  CD2 LEU B1014      59.256   3.782  36.615  1.00111.42           C  
ANISOU 3357  CD2 LEU B1014    12351  16967  13015    269    -19   2589       C  
ATOM   3358  N   LYS B1015      56.706   8.376  36.590  1.00 92.61           N  
ANISOU 3358  N   LYS B1015    10335  14849  10003   1825    890   2006       N  
ATOM   3359  CA  LYS B1015      55.700   9.016  35.750  1.00 94.00           C  
ANISOU 3359  CA  LYS B1015    10425  15035  10256   2177    930   1968       C  
ATOM   3360  C   LYS B1015      56.349   9.962  34.748  1.00102.23           C  
ANISOU 3360  C   LYS B1015    11911  15613  11318   2348    882   1683       C  
ATOM   3361  O   LYS B1015      55.889  10.077  33.606  1.00115.62           O  
ANISOU 3361  O   LYS B1015    13575  17159  13198   2491    758   1680       O  
ATOM   3362  CB  LYS B1015      54.692   9.766  36.620  1.00 97.90           C  
ANISOU 3362  CB  LYS B1015    10779  15904  10513   2502   1233   1953       C  
ATOM   3363  N   VAL B1016      57.418  10.647  35.159  1.00104.45           N  
ANISOU 3363  N   VAL B1016    12617  15660  11409   2335    976   1439       N  
ATOM   3364  CA  VAL B1016      58.113  11.557  34.254  1.00106.15           C  
ANISOU 3364  CA  VAL B1016    13279  15421  11631   2473    944   1158       C  
ATOM   3365  C   VAL B1016      58.722  10.800  33.082  1.00103.01           C  
ANISOU 3365  C   VAL B1016    12923  14690  11525   2212    643   1200       C  
ATOM   3366  O   VAL B1016      58.778  11.320  31.960  1.00108.27           O  
ANISOU 3366  O   VAL B1016    13802  15046  12289   2360    567   1066       O  
ATOM   3367  CB  VAL B1016      59.187  12.355  35.021  1.00104.41           C  
ANISOU 3367  CB  VAL B1016    13484  15031  11157   2474   1105    895       C  
ATOM   3368  CG1 VAL B1016      59.976  13.239  34.065  1.00109.54           C  
ANISOU 3368  CG1 VAL B1016    14603  15190  11826   2579   1068    607       C  
ATOM   3369  CG2 VAL B1016      58.546  13.189  36.119  1.00104.65           C  
ANISOU 3369  CG2 VAL B1016    13490  15380  10893   2765   1407    836       C  
ATOM   3370  N   ILE B1017      59.184   9.569  33.311  1.00 93.94           N  
ANISOU 3370  N   ILE B1017    11581  13595  10516   1823    466   1382       N  
ATOM   3371  CA  ILE B1017      59.858   8.824  32.251  1.00 91.98           C  
ANISOU 3371  CA  ILE B1017    11381  13024  10542   1554    178   1406       C  
ATOM   3372  C   ILE B1017      58.881   8.476  31.134  1.00 93.98           C  
ANISOU 3372  C   ILE B1017    11370  13303  11035   1663     25   1562       C  
ATOM   3373  O   ILE B1017      59.186   8.643  29.948  1.00 99.52           O  
ANISOU 3373  O   ILE B1017    12266  13659  11889   1685   -121   1457       O  
ATOM   3374  CB  ILE B1017      60.522   7.561  32.828  1.00 87.90           C  
ANISOU 3374  CB  ILE B1017    10695  12585  10118   1120     18   1572       C  
ATOM   3375  CG1 ILE B1017      61.646   7.948  33.791  1.00 86.43           C  
ANISOU 3375  CG1 ILE B1017    10831  12295   9712   1008    135   1376       C  
ATOM   3376  CG2 ILE B1017      61.042   6.677  31.702  1.00 88.53           C  
ANISOU 3376  CG2 ILE B1017    10749  12380  10510    849   -295   1629       C  
ATOM   3377  CD1 ILE B1017      62.150   6.802  34.645  1.00 86.79           C  
ANISOU 3377  CD1 ILE B1017    10695  12494   9786    630     21   1547       C  
ATOM   3378  N   GLU B1018      57.692   7.987  31.493  1.00 95.84           N  
ANISOU 3378  N   GLU B1018    11160  13946  11309   1731     56   1810       N  
ATOM   3379  CA  GLU B1018      56.713   7.631  30.469  1.00 99.19           C  
ANISOU 3379  CA  GLU B1018    11306  14413  11970   1841    -94   1961       C  
ATOM   3380  C   GLU B1018      56.157   8.865  29.770  1.00 95.98           C  
ANISOU 3380  C   GLU B1018    11106  13867  11494   2268     13   1773       C  
ATOM   3381  O   GLU B1018      55.712   8.772  28.620  1.00 94.17           O  
ANISOU 3381  O   GLU B1018    10820  13496  11464   2363   -151   1806       O  
ATOM   3382  CB  GLU B1018      55.589   6.785  31.062  1.00106.09           C  
ANISOU 3382  CB  GLU B1018    11640  15761  12908   1795    -81   2268       C  
ATOM   3383  CG  GLU B1018      56.029   5.366  31.397  1.00113.87           C  
ANISOU 3383  CG  GLU B1018    12382  16837  14046   1352   -272   2499       C  
ATOM   3384  CD  GLU B1018      54.909   4.516  31.958  1.00116.90           C  
ANISOU 3384  CD  GLU B1018    12235  17682  14500   1293   -256   2809       C  
ATOM   3385  OE1 GLU B1018      53.800   5.050  32.168  1.00125.85           O  
ANISOU 3385  OE1 GLU B1018    13183  19084  15552   1598    -77   2834       O  
ATOM   3386  OE2 GLU B1018      55.135   3.308  32.179  1.00120.16           O  
ANISOU 3386  OE2 GLU B1018    12416  18186  15055    940   -424   3023       O  
ATOM   3387  N   LYS B1019      56.170  10.016  30.434  1.00103.96           N  
ANISOU 3387  N   LYS B1019    12362  14913  12227   2532    276   1574       N  
ATOM   3388  CA  LYS B1019      55.738  11.270  29.829  1.00115.84           C  
ANISOU 3388  CA  LYS B1019    14113  16259  13643   2943    382   1369       C  
ATOM   3389  C   LYS B1019      56.973  12.126  29.568  1.00115.77           C  
ANISOU 3389  C   LYS B1019    14668  15810  13510   2943    423   1067       C  
ATOM   3390  O   LYS B1019      57.255  13.105  30.263  1.00117.98           O  
ANISOU 3390  O   LYS B1019    15215  16077  13533   3116    648    869       O  
ATOM   3391  CB  LYS B1019      54.734  11.985  30.740  1.00108.84           C  
ANISOU 3391  CB  LYS B1019    13069  15746  12541   3272    652   1362       C  
ATOM   3392  N   ALA B1020      57.718  11.730  28.539  1.00114.98           N  
ANISOU 3392  N   ALA B1020    14742  15343  13603   2739    199   1030       N  
ATOM   3393  CA  ALA B1020      58.928  12.416  28.118  1.00107.41           C  
ANISOU 3393  CA  ALA B1020    14303  13933  12574   2696    208    752       C  
ATOM   3394  C   ALA B1020      59.140  12.128  26.639  1.00112.93           C  
ANISOU 3394  C   ALA B1020    15111  14281  13515   2622    -36    743       C  
ATOM   3395  O   ALA B1020      58.769  11.060  26.144  1.00107.07           O  
ANISOU 3395  O   ALA B1020    14040  13629  13013   2447   -251    966       O  
ATOM   3396  CB  ALA B1020      60.147  11.974  28.935  1.00103.60           C  
ANISOU 3396  CB  ALA B1020    13941  13393  12029   2347    216    701       C  
ATOM   3397  N   ASP B1021      59.742  13.086  25.940  1.00101.39           N  
ANISOU 3397  N   ASP B1021    14121  12418  11985   2754      1    482       N  
ATOM   3398  CA  ASP B1021      59.973  12.977  24.505  1.00 99.91           C  
ANISOU 3398  CA  ASP B1021    14104  11865  11992   2714   -204    440       C  
ATOM   3399  C   ASP B1021      61.441  12.820  24.145  1.00100.70           C  
ANISOU 3399  C   ASP B1021    14551  11568  12144   2400   -286    271       C  
ATOM   3400  O   ASP B1021      61.764  12.088  23.207  1.00100.47           O  
ANISOU 3400  O   ASP B1021    14495  11338  12341   2184   -513    332       O  
ATOM   3401  CB  ASP B1021      59.405  14.202  23.780  1.00103.22           C  
ANISOU 3401  CB  ASP B1021    14800  12107  12313   3129   -118    280       C  
ATOM   3402  CG  ASP B1021      60.021  15.501  24.256  1.00104.93           C  
ANISOU 3402  CG  ASP B1021    15475  12138  12257   3304    124    -11       C  
ATOM   3403  OD1 ASP B1021      60.824  15.467  25.213  1.00105.56           O  
ANISOU 3403  OD1 ASP B1021    15635  12257  12217   3121    237    -87       O  
ATOM   3404  OD2 ASP B1021      59.702  16.557  23.669  1.00104.92           O  
ANISOU 3404  OD2 ASP B1021    15759  11944  12161   3627    195   -167       O  
ATOM   3405  N   ASN B1022      62.337  13.487  24.864  1.00 98.78           N  
ANISOU 3405  N   ASN B1022    14628  11204  11701   2369   -107     53       N  
ATOM   3406  CA  ASN B1022      63.768  13.390  24.627  1.00 97.58           C  
ANISOU 3406  CA  ASN B1022    14803  10683  11589   2072   -164   -133       C  
ATOM   3407  C   ASN B1022      64.424  12.567  25.728  1.00 98.20           C  
ANISOU 3407  C   ASN B1022    14700  10945  11664   1745   -176    -62       C  
ATOM   3408  O   ASN B1022      63.885  12.411  26.827  1.00 97.64           O  
ANISOU 3408  O   ASN B1022    14366  11256  11477   1798    -67     69       O  
ATOM   3409  CB  ASN B1022      64.407  14.782  24.549  1.00 97.47           C  
ANISOU 3409  CB  ASN B1022    15324  10343  11365   2264     35   -462       C  
ATOM   3410  CG  ASN B1022      64.232  15.578  25.826  1.00100.83           C  
ANISOU 3410  CG  ASN B1022    15798  10999  11514   2469    298   -548       C  
ATOM   3411  OD1 ASN B1022      64.759  15.213  26.876  1.00100.69           O  
ANISOU 3411  OD1 ASN B1022    15696  11135  11427   2275    353   -541       O  
ATOM   3412  ND2 ASN B1022      63.492  16.677  25.741  1.00104.57           N  
ANISOU 3412  ND2 ASN B1022    16413  11492  11826   2867    456   -636       N  
ATOM   3413  N   ALA B1023      65.607  12.032  25.412  1.00120.83           N  
ANISOU 3413  N   ALA B1023    17716  13531  14662   1403   -314   -153       N  
ATOM   3414  CA  ALA B1023      66.323  11.187  26.361  1.00117.16           C  
ANISOU 3414  CA  ALA B1023    17100  13196  14219   1070   -365    -96       C  
ATOM   3415  C   ALA B1023      66.922  11.982  27.511  1.00106.68           C  
ANISOU 3415  C   ALA B1023    16018  11889  12628   1129   -131   -297       C  
ATOM   3416  O   ALA B1023      67.240  11.396  28.551  1.00103.86           O  
ANISOU 3416  O   ALA B1023    15495  11738  12228    933   -132   -222       O  
ATOM   3417  CB  ALA B1023      67.426  10.408  25.643  1.00118.82           C  
ANISOU 3417  CB  ALA B1023    17403  13083  14659    697   -590   -158       C  
ATOM   3418  N   ALA B1024      67.086  13.297  27.354  1.00107.19           N  
ANISOU 3418  N   ALA B1024    16477  11738  12512   1395     63   -551       N  
ATOM   3419  CA  ALA B1024      67.614  14.102  28.449  1.00107.38           C  
ANISOU 3419  CA  ALA B1024    16735  11784  12281   1473    289   -749       C  
ATOM   3420  C   ALA B1024      66.647  14.128  29.625  1.00105.94           C  
ANISOU 3420  C   ALA B1024    16253  12077  11921   1655    435   -578       C  
ATOM   3421  O   ALA B1024      67.072  14.124  30.786  1.00104.04           O  
ANISOU 3421  O   ALA B1024    16017  11985  11530   1572    539   -619       O  
ATOM   3422  CB  ALA B1024      67.905  15.521  27.964  1.00106.45           C  
ANISOU 3422  CB  ALA B1024    17097  11333  12015   1736    461  -1047       C  
ATOM   3423  N   GLN B1025      65.342  14.159  29.345  1.00109.49           N  
ANISOU 3423  N   GLN B1025    16443  12771  12386   1904    447   -393       N  
ATOM   3424  CA  GLN B1025      64.356  14.102  30.418  1.00105.80           C  
ANISOU 3424  CA  GLN B1025    15652  12775  11770   2064    584   -217       C  
ATOM   3425  C   GLN B1025      64.357  12.741  31.104  1.00 99.77           C  
ANISOU 3425  C   GLN B1025    14492  12304  11114   1738    450     42       C  
ATOM   3426  O   GLN B1025      64.323  12.663  32.338  1.00 99.90           O  
ANISOU 3426  O   GLN B1025    14397  12601  10959   1712    576     89       O  
ATOM   3427  CB  GLN B1025      62.968  14.424  29.864  1.00110.91           C  
ANISOU 3427  CB  GLN B1025    16104  13596  12441   2400    611    -92       C  
ATOM   3428  CG  GLN B1025      62.798  15.867  29.417  1.00114.36           C  
ANISOU 3428  CG  GLN B1025    16916  13813  12722   2777    775   -336       C  
ATOM   3429  CD  GLN B1025      61.452  16.123  28.769  1.00111.27           C  
ANISOU 3429  CD  GLN B1025    16331  13565  12383   3101    763   -217       C  
ATOM   3430  OE1 GLN B1025      60.803  15.201  28.273  1.00113.57           O  
ANISOU 3430  OE1 GLN B1025    16266  14002  12884   3012    584     21       O  
ATOM   3431  NE2 GLN B1025      61.023  17.379  28.772  1.00109.73           N  
ANISOU 3431  NE2 GLN B1025    16367  13324  12000   3482    947   -389       N  
ATOM   3432  N   VAL B1026      64.397  11.658  30.325  1.00 97.30           N  
ANISOU 3432  N   VAL B1026    13968  11926  11075   1486    192    211       N  
ATOM   3433  CA  VAL B1026      64.429  10.321  30.914  1.00 97.23           C  
ANISOU 3433  CA  VAL B1026    13592  12168  11183   1160     42    460       C  
ATOM   3434  C   VAL B1026      65.734  10.110  31.670  1.00 98.18           C  
ANISOU 3434  C   VAL B1026    13911  12156  11238    877     32    321       C  
ATOM   3435  O   VAL B1026      65.743   9.652  32.819  1.00 92.47           O  
ANISOU 3435  O   VAL B1026    13015  11713  10408    756     77    434       O  
ATOM   3436  CB  VAL B1026      64.231   9.254  29.823  1.00 94.31           C  
ANISOU 3436  CB  VAL B1026    12979  11719  11134    961   -246    650       C  
ATOM   3437  CG1 VAL B1026      64.202   7.864  30.440  1.00106.32           C  
ANISOU 3437  CG1 VAL B1026    14111  13508  12778    631   -406    921       C  
ATOM   3438  CG2 VAL B1026      62.959   9.528  29.036  1.00107.67           C  
ANISOU 3438  CG2 VAL B1026    14499  13518  12893   1261   -243    764       C  
ATOM   3439  N   LYS B1027      66.857  10.438  31.028  1.00 95.38           N  
ANISOU 3439  N   LYS B1027    13926  11368  10946    765    -29     70       N  
ATOM   3440  CA  LYS B1027      68.157  10.354  31.686  1.00 88.10           C  
ANISOU 3440  CA  LYS B1027    13227  10280   9968    517    -36   -108       C  
ATOM   3441  C   LYS B1027      68.171  11.165  32.974  1.00 84.08           C  
ANISOU 3441  C   LYS B1027    12848   9952   9146    694    224   -221       C  
ATOM   3442  O   LYS B1027      68.722  10.724  33.989  1.00 84.27           O  
ANISOU 3442  O   LYS B1027    12833  10092   9095    496    217   -208       O  
ATOM   3443  CB  LYS B1027      69.233  10.824  30.708  1.00 91.12           C  
ANISOU 3443  CB  LYS B1027    14014  10159  10449    440    -93   -396       C  
ATOM   3444  CG  LYS B1027      70.673  10.755  31.184  1.00 90.26           C  
ANISOU 3444  CG  LYS B1027    14157   9811  10326    173   -122   -620       C  
ATOM   3445  CD  LYS B1027      71.598  10.917  29.979  1.00 91.16           C  
ANISOU 3445  CD  LYS B1027    14572   9447  10618     44   -231   -843       C  
ATOM   3446  CE  LYS B1027      72.971  11.461  30.343  1.00 89.38           C  
ANISOU 3446  CE  LYS B1027    14731   8914  10313    -79   -156  -1177       C  
ATOM   3447  NZ  LYS B1027      73.717  10.646  31.333  1.00102.64           N  
ANISOU 3447  NZ  LYS B1027    16293  10694  12011   -378   -259  -1154       N  
ATOM   3448  N   ASP B1028      67.566  12.354  32.952  1.00 88.31           N  
ANISOU 3448  N   ASP B1028    13546  10513   9496   1070    448   -336       N  
ATOM   3449  CA  ASP B1028      67.496  13.172  34.158  1.00 88.51           C  
ANISOU 3449  CA  ASP B1028    13688  10724   9218   1267    703   -444       C  
ATOM   3450  C   ASP B1028      66.664  12.491  35.239  1.00 88.88           C  
ANISOU 3450  C   ASP B1028    13328  11265   9176   1245    744   -165       C  
ATOM   3451  O   ASP B1028      67.048  12.481  36.416  1.00 89.91           O  
ANISOU 3451  O   ASP B1028    13488  11547   9127   1172    839   -196       O  
ATOM   3452  CB  ASP B1028      66.912  14.544  33.821  1.00 89.14           C  
ANISOU 3452  CB  ASP B1028    13996  10735   9139   1687    916   -608       C  
ATOM   3453  CG  ASP B1028      66.855  15.466  35.023  1.00 95.08           C  
ANISOU 3453  CG  ASP B1028    14891  11660   9576   1909   1183   -743       C  
ATOM   3454  OD1 ASP B1028      67.499  15.152  36.047  1.00 92.25           O  
ANISOU 3454  OD1 ASP B1028    14541  11392   9117   1723   1204   -766       O  
ATOM   3455  OD2 ASP B1028      66.159  16.501  34.946  1.00 91.31           O  
ANISOU 3455  OD2 ASP B1028    14517  11227   8950   2275   1366   -829       O  
ATOM   3456  N   ALA B1029      65.519  11.918  34.860  1.00 96.99           N  
ANISOU 3456  N   ALA B1029    13977  12549  10325   1305    675    108       N  
ATOM   3457  CA  ALA B1029      64.654  11.268  35.840  1.00 88.54           C  
ANISOU 3457  CA  ALA B1029    12507  11956   9177   1284    726    382       C  
ATOM   3458  C   ALA B1029      65.328  10.047  36.452  1.00 91.80           C  
ANISOU 3458  C   ALA B1029    12766  12441   9673    875    553    524       C  
ATOM   3459  O   ALA B1029      65.224   9.817  37.663  1.00 96.52           O  
ANISOU 3459  O   ALA B1029    13245  13333  10095    822    652    616       O  
ATOM   3460  CB  ALA B1029      63.328  10.874  35.190  1.00 81.24           C  
ANISOU 3460  CB  ALA B1029    11207  11258   8403   1416    669    632       C  
ATOM   3461  N   LEU B1030      66.018   9.249  35.634  1.00 89.86           N  
ANISOU 3461  N   LEU B1030    12523  11928   9690    584    289    543       N  
ATOM   3462  CA  LEU B1030      66.695   8.068  36.156  1.00 83.25           C  
ANISOU 3462  CA  LEU B1030    11548  11133   8950    192     97    669       C  
ATOM   3463  C   LEU B1030      67.751   8.440  37.189  1.00 93.63           C  
ANISOU 3463  C   LEU B1030    13152  12362  10061    105    190    458       C  
ATOM   3464  O   LEU B1030      67.990   7.678  38.133  1.00 95.51           O  
ANISOU 3464  O   LEU B1030    13249  12789  10249   -118    131    588       O  
ATOM   3465  CB  LEU B1030      67.337   7.284  35.013  1.00 83.69           C  
ANISOU 3465  CB  LEU B1030    11604  10870   9326    -80   -197    673       C  
ATOM   3466  CG  LEU B1030      66.390   6.543  34.069  1.00 90.38           C  
ANISOU 3466  CG  LEU B1030    12101  11821  10417    -92   -361    932       C  
ATOM   3467  CD1 LEU B1030      67.129   6.115  32.811  1.00 86.56           C  
ANISOU 3467  CD1 LEU B1030    11730  10944  10215   -293   -609    847       C  
ATOM   3468  CD2 LEU B1030      65.773   5.339  34.760  1.00 94.30           C  
ANISOU 3468  CD2 LEU B1030    12157  12704  10968   -288   -460   1275       C  
ATOM   3469  N   THR B1031      68.395   9.598  37.025  1.00 94.66           N  
ANISOU 3469  N   THR B1031    13694  12202  10072    276    330    133       N  
ATOM   3470  CA  THR B1031      69.398  10.025  37.994  1.00 99.00           C  
ANISOU 3470  CA  THR B1031    14529  12657  10428    214    423    -89       C  
ATOM   3471  C   THR B1031      68.783  10.215  39.376  1.00 96.92           C  
ANISOU 3471  C   THR B1031    14142  12806   9879    350    628     17       C  
ATOM   3472  O   THR B1031      69.353   9.778  40.382  1.00 95.90           O  
ANISOU 3472  O   THR B1031    14020  12767   9649    157    600     29       O  
ATOM   3473  CB  THR B1031      70.064  11.318  37.521  1.00104.82           C  
ANISOU 3473  CB  THR B1031    15719  13021  11087    407    558   -453       C  
ATOM   3474  OG1 THR B1031      70.524  11.155  36.173  1.00102.69           O  
ANISOU 3474  OG1 THR B1031    15556  12383  11077    294    383   -537       O  
ATOM   3475  CG2 THR B1031      71.241  11.676  38.418  1.00122.79           C  
ANISOU 3475  CG2 THR B1031    18297  15149  13209    303    616   -703       C  
ATOM   3476  N   LYS B1032      67.618  10.864  39.446  1.00 97.01           N  
ANISOU 3476  N   LYS B1032    14039  13068   9753    683    834     89       N  
ATOM   3477  CA  LYS B1032      66.945  11.024  40.730  1.00 94.74           C  
ANISOU 3477  CA  LYS B1032    13606  13195   9196    817   1040    200       C  
ATOM   3478  C   LYS B1032      66.550   9.673  41.314  1.00 93.06           C  
ANISOU 3478  C   LYS B1032    12997  13311   9048    547    908    538       C  
ATOM   3479  O   LYS B1032      66.665   9.454  42.526  1.00 93.77           O  
ANISOU 3479  O   LYS B1032    13054  13631   8944    466    984    595       O  
ATOM   3480  CB  LYS B1032      65.713  11.915  40.573  1.00 94.95           C  
ANISOU 3480  CB  LYS B1032    13551  13425   9101   1223   1267    217       C  
ATOM   3481  CG  LYS B1032      66.021  13.343  40.153  1.00 95.17           C  
ANISOU 3481  CG  LYS B1032    13982  13161   9017   1524   1428   -115       C  
ATOM   3482  CD  LYS B1032      64.755  14.184  40.096  1.00 97.45           C  
ANISOU 3482  CD  LYS B1032    14168  13680   9177   1931   1643    -89       C  
ATOM   3483  CE  LYS B1032      65.066  15.641  39.794  1.00107.80           C  
ANISOU 3483  CE  LYS B1032    15899  14710  10351   2237   1810   -421       C  
ATOM   3484  NZ  LYS B1032      65.576  15.831  38.408  1.00103.65           N  
ANISOU 3484  NZ  LYS B1032    15595  13742  10043   2205   1658   -557       N  
ATOM   3485  N   MET B1033      66.079   8.755  40.467  1.00 94.10           N  
ANISOU 3485  N   MET B1033    12834  13467   9451    403    706    765       N  
ATOM   3486  CA  MET B1033      65.641   7.455  40.962  1.00 91.17           C  
ANISOU 3486  CA  MET B1033    12075  13406   9158    146    575   1099       C  
ATOM   3487  C   MET B1033      66.806   6.662  41.540  1.00 95.71           C  
ANISOU 3487  C   MET B1033    12747  13858   9760   -221    391   1084       C  
ATOM   3488  O   MET B1033      66.661   6.007  42.579  1.00103.76           O  
ANISOU 3488  O   MET B1033    13597  15164  10665   -372    395   1269       O  
ATOM   3489  CB  MET B1033      64.966   6.669  39.840  1.00 88.34           C  
ANISOU 3489  CB  MET B1033    11403  13056   9107     69    379   1321       C  
ATOM   3490  CG  MET B1033      63.687   7.305  39.328  1.00 95.75           C  
ANISOU 3490  CG  MET B1033    12183  14164  10032    422    539   1376       C  
ATOM   3491  SD  MET B1033      62.934   6.367  37.986  1.00 87.33           S  
ANISOU 3491  SD  MET B1033    10755  13088   9337    330    288   1625       S  
ATOM   3492  CE  MET B1033      62.468   4.862  38.838  1.00 94.61           C  
ANISOU 3492  CE  MET B1033    11221  14411  10314      8    174   2012       C  
ATOM   3493  N   ARG B1034      67.968   6.704  40.884  1.00 97.56           N  
ANISOU 3493  N   ARG B1034    13257  13667  10146   -369    226    862       N  
ATOM   3494  CA  ARG B1034      69.117   5.960  41.389  1.00 96.97           C  
ANISOU 3494  CA  ARG B1034    13276  13451  10115   -714     33    823       C  
ATOM   3495  C   ARG B1034      69.544   6.485  42.755  1.00 99.81           C  
ANISOU 3495  C   ARG B1034    13842  13924  10157   -658    211    692       C  
ATOM   3496  O   ARG B1034      69.917   5.707  43.640  1.00107.75           O  
ANISOU 3496  O   ARG B1034    14776  15054  11109   -899    110    805       O  
ATOM   3497  CB  ARG B1034      70.276   6.033  40.396  1.00 95.66           C  
ANISOU 3497  CB  ARG B1034    13380  12799  10170   -855   -150    570       C  
ATOM   3498  CG  ARG B1034      71.127   4.771  40.373  1.00 97.30           C  
ANISOU 3498  CG  ARG B1034    13500  12878  10593  -1268   -467    650       C  
ATOM   3499  CD  ARG B1034      72.425   4.958  39.605  1.00101.67           C  
ANISOU 3499  CD  ARG B1034    14362  12949  11319  -1407   -612    344       C  
ATOM   3500  NE  ARG B1034      73.258   3.757  39.656  1.00108.21           N  
ANISOU 3500  NE  ARG B1034    15105  13662  12349  -1797   -918    404       N  
ATOM   3501  CZ  ARG B1034      74.292   3.580  40.477  1.00112.21           C  
ANISOU 3501  CZ  ARG B1034    15782  14068  12783  -1980   -991    262       C  
ATOM   3502  NH1 ARG B1034      74.650   4.525  41.337  1.00117.57           N  
ANISOU 3502  NH1 ARG B1034    16735  14746  13190  -1815   -777     47       N  
ATOM   3503  NH2 ARG B1034      74.974   2.445  40.435  1.00113.69           N  
ANISOU 3503  NH2 ARG B1034    15869  14151  13178  -2328  -1289    328       N  
ATOM   3504  N   ALA B1035      69.494   7.805  42.944  1.00 98.75           N  
ANISOU 3504  N   ALA B1035    13971  13743   9806   -338    471    454       N  
ATOM   3505  CA  ALA B1035      69.814   8.372  44.248  1.00 99.41           C  
ANISOU 3505  CA  ALA B1035    14247  13952   9573   -253    658    328       C  
ATOM   3506  C   ALA B1035      68.781   7.965  45.291  1.00113.54           C  
ANISOU 3506  C   ALA B1035    15733  16238  11169   -213    788    617       C  
ATOM   3507  O   ALA B1035      69.134   7.651  46.434  1.00119.88           O  
ANISOU 3507  O   ALA B1035    16568  17187  11792   -343    799    653       O  
ATOM   3508  CB  ALA B1035      69.903   9.895  44.149  1.00115.38           C  
ANISOU 3508  CB  ALA B1035    16603  15818  11418     98    909     15       C  
ATOM   3509  N   ALA B1036      67.499   7.969  44.917  1.00113.04           N  
ANISOU 3509  N   ALA B1036    15377  16436  11136    -35    888    821       N  
ATOM   3510  CA  ALA B1036      66.452   7.599  45.864  1.00105.13           C  
ANISOU 3510  CA  ALA B1036    14070  15916   9959      7   1031   1094       C  
ATOM   3511  C   ALA B1036      66.535   6.123  46.235  1.00108.15           C  
ANISOU 3511  C   ALA B1036    14186  16447  10459   -374    803   1388       C  
ATOM   3512  O   ALA B1036      66.385   5.764  47.408  1.00121.75           O  
ANISOU 3512  O   ALA B1036    15829  18455  11975   -459    878   1524       O  
ATOM   3513  CB  ALA B1036      65.079   7.925  45.278  1.00110.78           C  
ANISOU 3513  CB  ALA B1036    14521  16853  10718    281   1173   1227       C  
ATOM   3514  N   ALA B1037      66.776   5.254  45.251  1.00107.27           N  
ANISOU 3514  N   ALA B1037    13942  16141  10674   -607    521   1489       N  
ATOM   3515  CA  ALA B1037      66.881   3.827  45.537  1.00111.59           C  
ANISOU 3515  CA  ALA B1037    14242  16804  11356   -976    281   1765       C  
ATOM   3516  C   ALA B1037      68.033   3.546  46.492  1.00119.76           C  
ANISOU 3516  C   ALA B1037    15511  17731  12262  -1202    187   1660       C  
ATOM   3517  O   ALA B1037      67.872   2.834  47.490  1.00112.99           O  
ANISOU 3517  O   ALA B1037    14515  17140  11277  -1370    171   1868       O  
ATOM   3518  CB  ALA B1037      67.061   3.046  44.235  1.00108.98           C  
ANISOU 3518  CB  ALA B1037    13773  16229  11406  -1170    -14   1841       C  
ATOM   3519  N   LEU B1038      69.208   4.107  46.200  1.00138.20           N  
ANISOU 3519  N   LEU B1038    18210  19672  14628  -1209    123   1332       N  
ATOM   3520  CA  LEU B1038      70.360   3.921  47.075  1.00143.74           C  
ANISOU 3520  CA  LEU B1038    19156  20242  15217  -1405     27   1193       C  
ATOM   3521  C   LEU B1038      70.094   4.485  48.465  1.00145.09           C  
ANISOU 3521  C   LEU B1038    19422  20704  15004  -1245    288   1179       C  
ATOM   3522  O   LEU B1038      70.551   3.926  49.469  1.00153.09           O  
ANISOU 3522  O   LEU B1038    20472  21807  15888  -1442    210   1244       O  
ATOM   3523  CB  LEU B1038      71.590   4.581  46.455  1.00127.99           C  
ANISOU 3523  CB  LEU B1038    17533  17773  13324  -1398    -48    813       C  
ATOM   3524  CG  LEU B1038      72.133   3.977  45.161  1.00130.42           C  
ANISOU 3524  CG  LEU B1038    17804  17742  14006  -1605   -332    781       C  
ATOM   3525  CD1 LEU B1038      73.057   4.964  44.470  1.00129.18           C  
ANISOU 3525  CD1 LEU B1038    18018  17159  13906  -1494   -298    390       C  
ATOM   3526  CD2 LEU B1038      72.867   2.682  45.461  1.00131.61           C  
ANISOU 3526  CD2 LEU B1038    17866  17832  14306  -2002   -648    899       C  
ATOM   3527  N   ASP B1039      69.359   5.596  48.543  1.00128.31           N  
ANISOU 3527  N   ASP B1039    17343  18722  12687   -885    594   1091       N  
ATOM   3528  CA  ASP B1039      69.063   6.204  49.836  1.00125.15           C  
ANISOU 3528  CA  ASP B1039    17033  18603  11914   -708    860   1063       C  
ATOM   3529  C   ASP B1039      68.203   5.285  50.697  1.00128.20           C  
ANISOU 3529  C   ASP B1039    17090  19433  12188   -839    888   1429       C  
ATOM   3530  O   ASP B1039      68.413   5.182  51.911  1.00126.92           O  
ANISOU 3530  O   ASP B1039    17013  19442  11769   -901    956   1456       O  
ATOM   3531  CB  ASP B1039      68.365   7.548  49.621  1.00128.86           C  
ANISOU 3531  CB  ASP B1039    17588  19137  12235   -287   1169    903       C  
ATOM   3532  CG  ASP B1039      68.185   8.328  50.907  1.00134.03           C  
ANISOU 3532  CG  ASP B1039    18389  20034  12503    -79   1451    813       C  
ATOM   3533  OD1 ASP B1039      68.836   7.978  51.913  1.00128.89           O  
ANISOU 3533  OD1 ASP B1039    17859  19417  11695   -252   1400    805       O  
ATOM   3534  OD2 ASP B1039      67.390   9.291  50.910  1.00134.99           O  
ANISOU 3534  OD2 ASP B1039    18505  20308  12477    261   1719    746       O  
ATOM   3535  N   ALA B1040      67.225   4.613  50.087  1.00125.12           N  
ANISOU 3535  N   ALA B1040    16326  19229  11984   -885    837   1712       N  
ATOM   3536  CA  ALA B1040      66.343   3.728  50.841  1.00126.45           C  
ANISOU 3536  CA  ALA B1040    16160  19821  12063  -1016    873   2069       C  
ATOM   3537  C   ALA B1040      67.093   2.560  51.475  1.00129.05           C  
ANISOU 3537  C   ALA B1040    16494  20123  12416  -1406    618   2210       C  
ATOM   3538  O   ALA B1040      66.652   2.028  52.500  1.00136.33           O  
ANISOU 3538  O   ALA B1040    17278  21376  13147  -1510    688   2436       O  
ATOM   3539  CB  ALA B1040      65.231   3.207  49.930  1.00126.68           C  
ANISOU 3539  CB  ALA B1040    15790  20008  12337  -1005    836   2325       C  
ATOM   3540  N   GLN B1041      68.213   2.144  50.887  1.00136.26           N  
ANISOU 3540  N   GLN B1041    17565  20649  13560  -1627    323   2080       N  
ATOM   3541  CA  GLN B1041      68.966   1.015  51.424  1.00139.62           C  
ANISOU 3541  CA  GLN B1041    17998  21019  14033  -1997     49   2200       C  
ATOM   3542  C   GLN B1041      69.389   1.264  52.868  1.00145.39           C  
ANISOU 3542  C   GLN B1041    18956  21877  14409  -1998    166   2131       C  
ATOM   3543  O   GLN B1041      69.846   2.355  53.220  1.00157.84           O  
ANISOU 3543  O   GLN B1041    20841  23343  15787  -1778    339   1835       O  
ATOM   3544  CB  GLN B1041      70.199   0.751  50.560  1.00145.66           C  
ANISOU 3544  CB  GLN B1041    18945  21312  15089  -2186   -260   1993       C  
ATOM   3545  CG  GLN B1041      69.888   0.077  49.236  1.00147.99           C  
ANISOU 3545  CG  GLN B1041    18981  21489  15760  -2302   -466   2131       C  
ATOM   3546  CD  GLN B1041      71.091  -0.021  48.308  1.00146.42           C  
ANISOU 3546  CD  GLN B1041    18981  20814  15839  -2450   -732   1885       C  
ATOM   3547  OE1 GLN B1041      70.934  -0.169  47.096  1.00147.61           O  
ANISOU 3547  OE1 GLN B1041    19013  20802  16269  -2455   -843   1892       O  
ATOM   3548  NE2 GLN B1041      72.294   0.056  48.871  1.00141.55           N  
ANISOU 3548  NE2 GLN B1041    18664  19971  15147  -2570   -836   1660       N  
ATOM   3549  N   LYS B1042      69.244   0.228  53.702  1.00143.73           N  
ANISOU 3549  N   LYS B1042    18599  21895  14118  -2253     63   2407       N  
ATOM   3550  CA  LYS B1042      69.580   0.309  55.121  1.00147.86           C  
ANISOU 3550  CA  LYS B1042    19318  22567  14296  -2284    154   2388       C  
ATOM   3551  C   LYS B1042      69.140   1.629  55.738  1.00148.09           C  
ANISOU 3551  C   LYS B1042    19502  22773  13991  -1914    538   2215       C  
ATOM   3552  O   LYS B1042      69.870   2.223  56.538  1.00146.55           O  
ANISOU 3552  O   LYS B1042    19631  22492  13560  -1844    605   1988       O  
ATOM   3553  CB  LYS B1042      71.079   0.083  55.348  1.00152.48           C  
ANISOU 3553  CB  LYS B1042    20222  22786  14928  -2488   -117   2164       C  
ATOM   3554  CG  LYS B1042      71.600  -1.251  54.825  1.00158.96           C  
ANISOU 3554  CG  LYS B1042    20906  23422  16070  -2865   -517   2319       C  
ATOM   3555  CD  LYS B1042      70.777  -2.400  55.409  1.00157.70           C  
ANISOU 3555  CD  LYS B1042    20437  23623  15860  -3080   -565   2745       C  
ATOM   3556  CE  LYS B1042      71.374  -3.763  55.111  1.00159.42           C  
ANISOU 3556  CE  LYS B1042    20553  23667  16353  -3469   -975   2900       C  
ATOM   3557  NZ  LYS B1042      70.437  -4.856  55.504  1.00167.05           N  
ANISOU 3557  NZ  LYS B1042    21184  24984  17305  -3665  -1008   3331       N  
ATOM   3558  N   ALA B1043      67.949   2.094  55.371  1.00151.83           N  
ANISOU 3558  N   ALA B1043    19747  23494  14449  -1672    785   2313       N  
ATOM   3559  CA  ALA B1043      67.430   3.379  55.831  1.00154.29           C  
ANISOU 3559  CA  ALA B1043    20176  23976  14472  -1296   1152   2145       C  
ATOM   3560  C   ALA B1043      66.055   3.124  56.438  1.00161.74           C  
ANISOU 3560  C   ALA B1043    20790  25421  15242  -1231   1389   2454       C  
ATOM   3561  O   ALA B1043      65.055   3.013  55.721  1.00170.14           O  
ANISOU 3561  O   ALA B1043    21541  26637  16468  -1146   1454   2614       O  
ATOM   3562  CB  ALA B1043      67.361   4.390  54.691  1.00150.70           C  
ANISOU 3562  CB  ALA B1043    19795  23288  14175  -1015   1235   1900       C  
ATOM   3563  N   THR B1044      66.031   3.031  57.766  1.00171.35           N  
ANISOU 3563  N   THR B1044    22087  26888  16129  -1276   1515   2528       N  
ATOM   3564  CA  THR B1044      64.860   2.888  58.617  1.00172.53           C  
ANISOU 3564  CA  THR B1044    21993  27526  16035  -1216   1780   2782       C  
ATOM   3565  C   THR B1044      63.676   2.186  57.966  1.00174.60           C  
ANISOU 3565  C   THR B1044    21796  28028  16515  -1277   1785   3100       C  
ATOM   3566  O   THR B1044      62.617   2.801  57.791  1.00174.60           O  
ANISOU 3566  O   THR B1044    21606  28270  16464  -1005   2053   3117       O  
ATOM   3567  CB  THR B1044      64.409   4.274  59.109  1.00174.17           C  
ANISOU 3567  CB  THR B1044    22340  27896  15943   -813   2157   2564       C  
ATOM   3568  OG1 THR B1044      63.338   4.129  60.050  1.00178.25           O  
ANISOU 3568  OG1 THR B1044    22638  28894  16196   -768   2424   2795       O  
ATOM   3569  CG2 THR B1044      63.938   5.155  57.942  1.00173.01           C  
ANISOU 3569  CG2 THR B1044    22123  27628  15986   -509   2258   2399       C  
ATOM   3570  N   PRO B1045      63.786   0.912  57.602  1.00168.27           N  
ANISOU 3570  N   PRO B1045    20799  27176  15960  -1619   1495   3350       N  
ATOM   3571  CA  PRO B1045      62.587   0.185  57.185  1.00168.97           C  
ANISOU 3571  CA  PRO B1045    20436  27550  16217  -1691   1522   3680       C  
ATOM   3572  C   PRO B1045      61.626   0.087  58.355  1.00172.76           C  
ANISOU 3572  C   PRO B1045    20748  28514  16378  -1664   1813   3896       C  
ATOM   3573  O   PRO B1045      61.962  -0.510  59.390  1.00178.37           O  
ANISOU 3573  O   PRO B1045    21553  29335  16885  -1887   1772   4025       O  
ATOM   3574  CB  PRO B1045      63.124  -1.194  56.771  1.00169.29           C  
ANISOU 3574  CB  PRO B1045    20371  27411  16542  -2098   1128   3884       C  
ATOM   3575  CG  PRO B1045      64.443  -1.323  57.460  1.00164.84           C  
ANISOU 3575  CG  PRO B1045    20182  26604  15845  -2270    951   3732       C  
ATOM   3576  CD  PRO B1045      64.997   0.072  57.548  1.00161.96           C  
ANISOU 3576  CD  PRO B1045    20172  26056  15308  -1953   1125   3339       C  
ATOM   3577  N   PRO B1046      60.420   0.652  58.239  1.00168.34           N  
ANISOU 3577  N   PRO B1046    19943  28254  15765  -1396   2112   3939       N  
ATOM   3578  CA  PRO B1046      59.552   0.711  59.428  1.00184.92           C  
ANISOU 3578  CA  PRO B1046    21919  30817  17527  -1341   2430   4097       C  
ATOM   3579  C   PRO B1046      59.071  -0.653  59.871  1.00186.07           C  
ANISOU 3579  C   PRO B1046    21775  31220  17702  -1695   2340   4496       C  
ATOM   3580  O   PRO B1046      58.986  -0.919  61.077  1.00189.87           O  
ANISOU 3580  O   PRO B1046    22312  31954  17876  -1807   2471   4622       O  
ATOM   3581  CB  PRO B1046      58.400   1.616  58.973  1.00185.58           C  
ANISOU 3581  CB  PRO B1046    21781  31112  17621   -968   2729   4026       C  
ATOM   3582  CG  PRO B1046      58.327   1.404  57.505  1.00179.51           C  
ANISOU 3582  CG  PRO B1046    20843  30092  17270   -968   2506   4025       C  
ATOM   3583  CD  PRO B1046      59.745   1.181  57.039  1.00170.94           C  
ANISOU 3583  CD  PRO B1046    20076  28531  16344  -1148   2165   3865       C  
ATOM   3584  N   LYS B1047      58.754  -1.532  58.921  1.00168.92           N  
ANISOU 3584  N   LYS B1047    19302  28987  15893  -1877   2117   4699       N  
ATOM   3585  CA  LYS B1047      58.290  -2.867  59.263  1.00175.44           C  
ANISOU 3585  CA  LYS B1047    19842  30041  16778  -2226   2014   5086       C  
ATOM   3586  C   LYS B1047      59.380  -3.688  59.935  1.00169.37           C  
ANISOU 3586  C   LYS B1047    19327  29102  15925  -2569   1749   5154       C  
ATOM   3587  O   LYS B1047      59.071  -4.702  60.570  1.00182.42           O  
ANISOU 3587  O   LYS B1047    20824  30973  17512  -2855   1708   5464       O  
ATOM   3588  CB  LYS B1047      57.794  -3.579  58.005  1.00174.35           C  
ANISOU 3588  CB  LYS B1047    19345  29829  17071  -2331   1806   5256       C  
ATOM   3589  CG  LYS B1047      57.228  -4.968  58.241  1.00181.36           C  
ANISOU 3589  CG  LYS B1047    19901  30949  18061  -2685   1695   5663       C  
ATOM   3590  CD  LYS B1047      56.526  -5.475  56.992  1.00176.35           C  
ANISOU 3590  CD  LYS B1047    18877  30294  17836  -2712   1556   5809       C  
ATOM   3591  CE  LYS B1047      56.174  -6.947  57.098  1.00173.31           C  
ANISOU 3591  CE  LYS B1047    18193  30053  17604  -3104   1370   6199       C  
ATOM   3592  NZ  LYS B1047      55.599  -7.462  55.826  1.00173.50           N  
ANISOU 3592  NZ  LYS B1047    17859  30015  18049  -3138   1197   6323       N  
ATOM   3593  N   LEU B1048      60.643  -3.267  59.821  1.00181.65           N  
ANISOU 3593  N   LEU B1048    21271  30269  17478  -2548   1569   4869       N  
ATOM   3594  CA  LEU B1048      61.753  -3.995  60.419  1.00180.52           C  
ANISOU 3594  CA  LEU B1048    21388  29931  17272  -2857   1294   4896       C  
ATOM   3595  C   LEU B1048      62.610  -3.094  61.302  1.00180.85           C  
ANISOU 3595  C   LEU B1048    21872  29865  16978  -2705   1402   4600       C  
ATOM   3596  O   LEU B1048      63.815  -3.320  61.439  1.00178.65           O  
ANISOU 3596  O   LEU B1048    21891  29270  16719  -2862   1137   4466       O  
ATOM   3597  CB  LEU B1048      62.618  -4.638  59.335  1.00179.81           C  
ANISOU 3597  CB  LEU B1048    21320  29419  17579  -3062    873   4854       C  
ATOM   3598  CG  LEU B1048      61.864  -5.347  58.207  1.00182.55           C  
ANISOU 3598  CG  LEU B1048    21256  29798  18308  -3156    745   5075       C  
ATOM   3599  CD1 LEU B1048      62.830  -5.828  57.137  1.00185.86           C  
ANISOU 3599  CD1 LEU B1048    21749  29770  19098  -3325    342   4974       C  
ATOM   3600  CD2 LEU B1048      61.043  -6.507  58.748  1.00180.21           C  
ANISOU 3600  CD2 LEU B1048    20639  29845  17987  -3430    746   5491       C  
ATOM   3601  N   GLU B1049      62.010  -2.065  61.909  1.00190.94           N  
ANISOU 3601  N   GLU B1049    22988  25678  23882  -1120  -2322   2641       N  
ATOM   3602  CA  GLU B1049      62.714  -1.347  62.967  1.00193.38           C  
ANISOU 3602  CA  GLU B1049    22912  26453  24109   -964  -2631   2858       C  
ATOM   3603  C   GLU B1049      63.077  -2.294  64.099  1.00179.73           C  
ANISOU 3603  C   GLU B1049    21286  24722  22284   -691  -2446   3240       C  
ATOM   3604  O   GLU B1049      64.091  -2.102  64.779  1.00187.00           O  
ANISOU 3604  O   GLU B1049    21952  25929  23169   -403  -2569   3554       O  
ATOM   3605  CB  GLU B1049      61.867  -0.186  63.489  1.00204.19           C  
ANISOU 3605  CB  GLU B1049    24041  28147  25395  -1303  -3023   2550       C  
ATOM   3606  CG  GLU B1049      62.552   0.636  64.578  1.00194.29           C  
ANISOU 3606  CG  GLU B1049    22371  27393  24056  -1161  -3368   2747       C  
ATOM   3607  CD  GLU B1049      63.691   1.487  64.051  1.00199.83           C  
ANISOU 3607  CD  GLU B1049    22738  28337  24852   -990  -3581   2835       C  
ATOM   3608  OE1 GLU B1049      63.740   1.731  62.827  1.00196.59           O  
ANISOU 3608  OE1 GLU B1049    22373  27760  24561  -1074  -3547   2651       O  
ATOM   3609  OE2 GLU B1049      64.542   1.907  64.863  1.00205.03           O  
ANISOU 3609  OE2 GLU B1049    23087  29353  25463   -770  -3781   3090       O  
ATOM   3610  N   ASP B1050      62.254  -3.323  64.308  1.00170.34           N  
ANISOU 3610  N   ASP B1050    20469  23205  21048   -780  -2149   3216       N  
ATOM   3611  CA  ASP B1050      62.522  -4.292  65.362  1.00167.04           C  
ANISOU 3611  CA  ASP B1050    20187  22748  20534   -535  -1951   3572       C  
ATOM   3612  C   ASP B1050      63.817  -5.046  65.090  1.00169.88           C  
ANISOU 3612  C   ASP B1050    20598  22981  20969   -101  -1716   3962       C  
ATOM   3613  O   ASP B1050      64.586  -5.330  66.016  1.00172.13           O  
ANISOU 3613  O   ASP B1050    20777  23442  21184    198  -1721   4321       O  
ATOM   3614  CB  ASP B1050      61.340  -5.258  65.469  1.00167.99           C  
ANISOU 3614  CB  ASP B1050    20723  22498  20608   -740  -1657   3437       C  
ATOM   3615  CG  ASP B1050      61.009  -5.928  64.143  1.00168.02           C  
ANISOU 3615  CG  ASP B1050    21064  22029  20745   -819  -1342   3263       C  
ATOM   3616  OD1 ASP B1050      61.784  -5.757  63.178  1.00167.67           O  
ANISOU 3616  OD1 ASP B1050    20951  21933  20825   -674  -1321   3293       O  
ATOM   3617  OD2 ASP B1050      59.973  -6.622  64.064  1.00168.40           O  
ANISOU 3617  OD2 ASP B1050    21447  21762  20775  -1028  -1116   3092       O  
ATOM   3618  N   LYS B1051      64.070  -5.380  63.828  1.00195.84           N  
ANISOU 3618  N   LYS B1051    24046  25965  24398    -58  -1510   3893       N  
ATOM   3619  CA  LYS B1051      65.244  -6.162  63.472  1.00202.48           C  
ANISOU 3619  CA  LYS B1051    24964  26648  25321    343  -1260   4239       C  
ATOM   3620  C   LYS B1051      66.531  -5.375  63.687  1.00197.39           C  
ANISOU 3620  C   LYS B1051    23904  26401  24694    610  -1523   4463       C  
ATOM   3621  O   LYS B1051      66.584  -4.162  63.468  1.00214.51           O  
ANISOU 3621  O   LYS B1051    25753  28869  26881    459  -1859   4271       O  
ATOM   3622  CB  LYS B1051      65.166  -6.598  62.009  1.00198.88           C  
ANISOU 3622  CB  LYS B1051    24758  25793  25014    297  -1002   4073       C  
ATOM   3623  CG  LYS B1051      64.073  -7.601  61.703  1.00204.05           C  
ANISOU 3623  CG  LYS B1051    25863  25994  25672    105   -671   3907       C  
ATOM   3624  CD  LYS B1051      64.200  -8.118  60.277  1.00204.44           C  
ANISOU 3624  CD  LYS B1051    26150  25654  25874    132   -397   3803       C  
ATOM   3625  CE  LYS B1051      63.554  -9.484  60.115  1.00215.10           C  
ANISOU 3625  CE  LYS B1051    27970  26520  27237    115     23   3813       C  
ATOM   3626  NZ  LYS B1051      62.538  -9.496  59.029  1.00199.40           N  
ANISOU 3626  NZ  LYS B1051    26212  24225  25325   -215    129   3404       N  
ATOM   3627  N   SER B1052      67.574  -6.081  64.122  1.00201.92           N  
ANISOU 3627  N   SER B1052    24483  26973  25264   1012  -1367   4871       N  
ATOM   3628  CA  SER B1052      68.907  -5.510  64.214  1.00202.29           C  
ANISOU 3628  CA  SER B1052    24170  27343  25348   1312  -1555   5111       C  
ATOM   3629  C   SER B1052      69.431  -5.356  62.787  1.00206.05           C  
ANISOU 3629  C   SER B1052    24644  27658  25987   1351  -1472   5009       C  
ATOM   3630  O   SER B1052      68.816  -5.849  61.838  1.00207.66           O  
ANISOU 3630  O   SER B1052    25152  27484  26266   1191  -1236   4803       O  
ATOM   3631  CB  SER B1052      69.805  -6.390  65.078  1.00205.99           C  
ANISOU 3631  CB  SER B1052    24676  27826  25763   1728  -1391   5565       C  
ATOM   3632  OG  SER B1052      70.030  -7.650  64.478  1.00208.55           O  
ANISOU 3632  OG  SER B1052    25363  27712  26165   1919   -976   5712       O  
ATOM   3633  N   PRO B1053      70.563  -4.672  62.591  1.00198.76           N  
ANISOU 3633  N   PRO B1053    23381  27016  25124   1558  -1659   5143       N  
ATOM   3634  CA  PRO B1053      70.986  -4.375  61.209  1.00217.57           C  
ANISOU 3634  CA  PRO B1053    25736  29276  27656   1548  -1616   5006       C  
ATOM   3635  C   PRO B1053      71.051  -5.584  60.285  1.00216.23           C  
ANISOU 3635  C   PRO B1053    25959  28617  27583   1672  -1181   5059       C  
ATOM   3636  O   PRO B1053      70.539  -5.515  59.160  1.00219.52           O  
ANISOU 3636  O   PRO B1053    26529  28792  28085   1457  -1091   4775       O  
ATOM   3637  CB  PRO B1053      72.372  -3.739  61.408  1.00235.97           C  
ANISOU 3637  CB  PRO B1053    27665  31975  30019   1849  -1824   5256       C  
ATOM   3638  CG  PRO B1053      72.330  -3.159  62.775  1.00225.04           C  
ANISOU 3638  CG  PRO B1053    26014  30992  28500   1846  -2123   5353       C  
ATOM   3639  CD  PRO B1053      71.484  -4.096  63.589  1.00218.06           C  
ANISOU 3639  CD  PRO B1053    25444  29905  27503   1794  -1927   5408       C  
ATOM   3640  N   ASP B1054      71.655  -6.688  60.716  1.00178.24           N  
ANISOU 3640  N   ASP B1054    21315  23648  22760   2011   -911   5407       N  
ATOM   3641  CA  ASP B1054      71.842  -7.852  59.858  1.00174.72           C  
ANISOU 3641  CA  ASP B1054    21223  22750  22413   2167   -500   5485       C  
ATOM   3642  C   ASP B1054      70.793  -8.912  60.178  1.00171.82           C  
ANISOU 3642  C   ASP B1054    21277  22021  21986   2041   -220   5441       C  
ATOM   3643  O   ASP B1054      70.652  -9.322  61.335  1.00181.66           O  
ANISOU 3643  O   ASP B1054    22565  23339  23116   2125   -211   5634       O  
ATOM   3644  CB  ASP B1054      73.246  -8.438  60.014  1.00188.35           C  
ANISOU 3644  CB  ASP B1054    22876  24505  24182   2642   -362   5898       C  
ATOM   3645  CG  ASP B1054      73.535  -9.531  59.001  1.00181.46           C  
ANISOU 3645  CG  ASP B1054    22332  23185  23428   2809     41   5962       C  
ATOM   3646  OD1 ASP B1054      73.696  -9.208  57.804  1.00177.88           O  
ANISOU 3646  OD1 ASP B1054    21860  22636  23090   2735     66   5781       O  
ATOM   3647  OD2 ASP B1054      73.597 -10.713  59.399  1.00180.49           O  
ANISOU 3647  OD2 ASP B1054    22489  22807  23282   3014    331   6193       O  
ATOM   3648  N   SER B1055      70.069  -9.356  59.152  1.00159.67           N  
ANISOU 3648  N   SER B1055    20048  20094  20526   1842      9   5188       N  
ATOM   3649  CA  SER B1055      69.137 -10.469  59.281  1.00156.32           C  
ANISOU 3649  CA  SER B1055    20053  19271  20070   1740    323   5146       C  
ATOM   3650  C   SER B1055      68.897 -11.046  57.895  1.00162.62           C  
ANISOU 3650  C   SER B1055    21149  19638  21003   1674    616   4963       C  
ATOM   3651  O   SER B1055      68.897 -10.297  56.912  1.00161.91           O  
ANISOU 3651  O   SER B1055    20934  19589  20994   1522    493   4717       O  
ATOM   3652  CB  SER B1055      67.814 -10.021  59.917  1.00163.33           C  
ANISOU 3652  CB  SER B1055    20966  20247  20845   1350    151   4873       C  
ATOM   3653  OG  SER B1055      67.121  -9.118  59.076  1.00160.13           O  
ANISOU 3653  OG  SER B1055    20485  19869  20487    998    -26   4463       O  
ATOM   3654  N   PRO B1056      68.691 -12.362  57.779  1.00177.34           N  
ANISOU 3654  N   PRO B1056    23405  21084  22891   1784   1002   5075       N  
ATOM   3655  CA  PRO B1056      68.542 -12.951  56.437  1.00176.53           C  
ANISOU 3655  CA  PRO B1056    23583  20567  22923   1750   1292   4916       C  
ATOM   3656  C   PRO B1056      67.345 -12.419  55.670  1.00161.50           C  
ANISOU 3656  C   PRO B1056    21771  18547  21043   1311   1221   4451       C  
ATOM   3657  O   PRO B1056      67.360 -12.431  54.432  1.00157.00           O  
ANISOU 3657  O   PRO B1056    21297  17767  20589   1255   1334   4269       O  
ATOM   3658  CB  PRO B1056      68.408 -14.454  56.727  1.00188.53           C  
ANISOU 3658  CB  PRO B1056    25505  21690  24439   1926   1692   5129       C  
ATOM   3659  CG  PRO B1056      67.900 -14.528  58.128  1.00166.30           C  
ANISOU 3659  CG  PRO B1056    22683  19031  21470   1866   1595   5237       C  
ATOM   3660  CD  PRO B1056      68.509 -13.359  58.849  1.00196.31           C  
ANISOU 3660  CD  PRO B1056    26027  23364  25199   1922   1191   5330       C  
ATOM   3661  N   GLU B1057      66.305 -11.952  56.364  1.00197.38           N  
ANISOU 3661  N   GLU B1057    26290  23224  25482   1000   1036   4249       N  
ATOM   3662  CA  GLU B1057      65.167 -11.356  55.673  1.00199.87           C  
ANISOU 3662  CA  GLU B1057    26663  23461  25816    578    934   3795       C  
ATOM   3663  C   GLU B1057      65.515  -9.964  55.162  1.00180.84           C  
ANISOU 3663  C   GLU B1057    23879  21394  23439    470    575   3618       C  
ATOM   3664  O   GLU B1057      65.093  -9.571  54.068  1.00186.16           O  
ANISOU 3664  O   GLU B1057    24600  21941  24190    253    558   3303       O  
ATOM   3665  CB  GLU B1057      63.956 -11.301  56.603  1.00205.02           C  
ANISOU 3665  CB  GLU B1057    27400  24155  26343    284    848   3634       C  
ATOM   3666  N   MET B1058      66.285  -9.206  55.946  1.00173.32           N  
ANISOU 3666  N   MET B1058    22553  20875  22427    619    283   3818       N  
ATOM   3667  CA  MET B1058      66.749  -7.888  55.533  1.00171.44           C  
ANISOU 3667  CA  MET B1058    21936  20981  22221    553    -62   3694       C  
ATOM   3668  C   MET B1058      67.838  -7.950  54.471  1.00169.18           C  
ANISOU 3668  C   MET B1058    21596  20619  22066    797     49   3806       C  
ATOM   3669  O   MET B1058      68.176  -6.909  53.899  1.00167.16           O  
ANISOU 3669  O   MET B1058    21070  20588  21855    720   -198   3669       O  
ATOM   3670  CB  MET B1058      67.255  -7.104  56.744  1.00170.90           C  
ANISOU 3670  CB  MET B1058    21487  21397  22049    650   -399   3885       C  
ATOM   3671  CG  MET B1058      66.146  -6.656  57.680  1.00172.54           C  
ANISOU 3671  CG  MET B1058    21660  21769  22129    343   -609   3696       C  
ATOM   3672  SD  MET B1058      66.739  -5.675  59.070  1.00173.65           S  
ANISOU 3672  SD  MET B1058    21336  22492  22149    450  -1021   3902       S  
ATOM   3673  CE  MET B1058      67.268  -4.184  58.230  1.00168.78           C  
ANISOU 3673  CE  MET B1058    20323  22189  21616    354  -1381   3706       C  
ATOM   3674  N   LYS B1059      68.418  -9.123  54.211  1.00173.62           N  
ANISOU 3674  N   LYS B1059    22398  20882  22689   1094    407   4056       N  
ATOM   3675  CA  LYS B1059      69.360  -9.221  53.101  1.00172.83           C  
ANISOU 3675  CA  LYS B1059    22273  20676  22717   1301    535   4125       C  
ATOM   3676  C   LYS B1059      68.630  -9.135  51.765  1.00172.11           C  
ANISOU 3676  C   LYS B1059    22382  20299  22713   1026    633   3749       C  
ATOM   3677  O   LYS B1059      69.141  -8.537  50.811  1.00170.45           O  
ANISOU 3677  O   LYS B1059    22024  20154  22588   1032    552   3655       O  
ATOM   3678  CB  LYS B1059      70.191 -10.498  53.201  1.00176.68           C  
ANISOU 3678  CB  LYS B1059    22957  20927  23246   1701    884   4492       C  
ATOM   3679  CG  LYS B1059      71.251 -10.406  54.289  1.00178.51           C  
ANISOU 3679  CG  LYS B1059    22916  21492  23417   2033    753   4881       C  
ATOM   3680  CD  LYS B1059      72.232 -11.561  54.250  1.00182.23           C  
ANISOU 3680  CD  LYS B1059    23541  21752  23945   2455   1074   5243       C  
ATOM   3681  CE  LYS B1059      73.568 -11.122  54.841  1.00183.33           C  
ANISOU 3681  CE  LYS B1059    23310  22274  24071   2791    888   5569       C  
ATOM   3682  NZ  LYS B1059      74.442 -12.259  55.226  1.00187.22           N  
ANISOU 3682  NZ  LYS B1059    23936  22619  24579   3211   1158   5962       N  
ATOM   3683  N   ASP B1060      67.439  -9.730  51.671  1.00168.83           N  
ANISOU 3683  N   ASP B1060    22304  19565  22278    785    811   3531       N  
ATOM   3684  CA  ASP B1060      66.619  -9.505  50.487  1.00177.67           C  
ANISOU 3684  CA  ASP B1060    23586  20454  23466    481    852   3133       C  
ATOM   3685  C   ASP B1060      66.150  -8.055  50.429  1.00179.73           C  
ANISOU 3685  C   ASP B1060    23555  21047  23689    165    440   2832       C  
ATOM   3686  O   ASP B1060      65.863  -7.537  49.345  1.00187.30           O  
ANISOU 3686  O   ASP B1060    24522  21931  24715    -28    386   2542       O  
ATOM   3687  CB  ASP B1060      65.424 -10.455  50.476  1.00189.04           C  
ANISOU 3687  CB  ASP B1060    25443  21494  24892    289   1125   2963       C  
ATOM   3688  CG  ASP B1060      64.656 -10.409  49.170  1.00198.87           C  
ANISOU 3688  CG  ASP B1060    26896  22446  26219     21   1224   2576       C  
ATOM   3689  OD1 ASP B1060      65.121  -9.736  48.226  1.00202.78           O  
ANISOU 3689  OD1 ASP B1060    27236  23024  26788     15   1113   2467       O  
ATOM   3690  OD2 ASP B1060      63.584 -11.046  49.088  1.00202.77           O  
ANISOU 3690  OD2 ASP B1060    27709  22629  26704   -183   1412   2379       O  
ATOM   3691  N   PHE B1061      66.070  -7.391  51.585  1.00164.00           N  
ANISOU 3691  N   PHE B1061    21305  19420  21587    113    146   2897       N  
ATOM   3692  CA  PHE B1061      65.750  -5.967  51.616  1.00159.92           C  
ANISOU 3692  CA  PHE B1061    20472  19255  21033   -154   -270   2645       C  
ATOM   3693  C   PHE B1061      66.864  -5.161  50.959  1.00150.63           C  
ANISOU 3693  C   PHE B1061    18990  18310  19933     -3   -438   2719       C  
ATOM   3694  O   PHE B1061      66.626  -4.418  50.001  1.00148.49           O  
ANISOU 3694  O   PHE B1061    18659  18045  19717   -209   -569   2436       O  
ATOM   3695  CB  PHE B1061      65.518  -5.528  53.065  1.00163.06           C  
ANISOU 3695  CB  PHE B1061    20662  19995  21298   -201   -527   2739       C  
ATOM   3696  CG  PHE B1061      65.599  -4.042  53.285  1.00151.95           C  
ANISOU 3696  CG  PHE B1061    18846  19032  19854   -361   -980   2598       C  
ATOM   3697  CD1 PHE B1061      64.507  -3.226  53.040  1.00151.49           C  
ANISOU 3697  CD1 PHE B1061    18763  19025  19770   -759  -1204   2193       C  
ATOM   3698  CD2 PHE B1061      66.766  -3.466  53.759  1.00145.71           C  
ANISOU 3698  CD2 PHE B1061    17696  18609  19057   -109  -1184   2872       C  
ATOM   3699  CE1 PHE B1061      64.583  -1.862  53.256  1.00148.22           C  
ANISOU 3699  CE1 PHE B1061    17975  19016  19324   -903  -1624   2065       C  
ATOM   3700  CE2 PHE B1061      66.847  -2.104  53.974  1.00143.14           C  
ANISOU 3700  CE2 PHE B1061    16995  18691  18703   -254  -1601   2745       C  
ATOM   3701  CZ  PHE B1061      65.755  -1.301  53.721  1.00143.59           C  
ANISOU 3701  CZ  PHE B1061    17034  18790  18735   -652  -1821   2343       C  
ATOM   3702  N   ARG B1062      68.099  -5.309  51.450  1.00162.23           N  
ANISOU 3702  N   ARG B1062    20268  19966  21406    360   -433   3101       N  
ATOM   3703  CA  ARG B1062      69.219  -4.619  50.819  1.00162.56           C  
ANISOU 3703  CA  ARG B1062    20025  20214  21526    524   -565   3190       C  
ATOM   3704  C   ARG B1062      69.426  -5.098  49.388  1.00153.02           C  
ANISOU 3704  C   ARG B1062    19037  18663  20442    567   -293   3097       C  
ATOM   3705  O   ARG B1062      69.823  -4.313  48.519  1.00141.72           O  
ANISOU 3705  O   ARG B1062    17432  17340  19076    516   -431   2974       O  
ATOM   3706  CB  ARG B1062      70.499  -4.836  51.630  1.00162.14           C  
ANISOU 3706  CB  ARG B1062    19756  20393  21457    927   -571   3626       C  
ATOM   3707  CG  ARG B1062      71.032  -6.262  51.558  1.00160.52           C  
ANISOU 3707  CG  ARG B1062    19834  19859  21297   1256   -156   3915       C  
ATOM   3708  CD  ARG B1062      72.280  -6.468  52.404  1.00167.29           C  
ANISOU 3708  CD  ARG B1062    20475  20954  22133   1658   -175   4343       C  
ATOM   3709  NE  ARG B1062      72.697  -7.869  52.402  1.00167.45           N  
ANISOU 3709  NE  ARG B1062    20789  20647  22190   1962    220   4611       N  
ATOM   3710  CZ  ARG B1062      73.394  -8.445  51.426  1.00168.48           C  
ANISOU 3710  CZ  ARG B1062    21039  20544  22434   2171    476   4697       C  
ATOM   3711  NH1 ARG B1062      73.758  -7.746  50.359  1.00172.94           N  
ANISOU 3711  NH1 ARG B1062    21458  21166  23084   2107    387   4540       N  
ATOM   3712  NH2 ARG B1062      73.723  -9.726  51.514  1.00175.66           N  
ANISOU 3712  NH2 ARG B1062    22216  21158  23368   2444    824   4940       N  
ATOM   3713  N   HIS B1063      69.163  -6.381  49.125  1.00144.61           N  
ANISOU 3713  N   HIS B1063    18354  17182  19409    660     95   3154       N  
ATOM   3714  CA  HIS B1063      69.297  -6.906  47.771  1.00135.49           C  
ANISOU 3714  CA  HIS B1063    17431  15680  18369    697    371   3056       C  
ATOM   3715  C   HIS B1063      68.210  -6.362  46.854  1.00137.12           C  
ANISOU 3715  C   HIS B1063    17753  15751  18597    301    291   2605       C  
ATOM   3716  O   HIS B1063      68.458  -6.137  45.664  1.00134.62           O  
ANISOU 3716  O   HIS B1063    17454  15327  18367    276    339   2469       O  
ATOM   3717  CB  HIS B1063      69.252  -8.434  47.801  1.00138.45           C  
ANISOU 3717  CB  HIS B1063    18189  15646  18772    895    801   3232       C  
ATOM   3718  CG  HIS B1063      69.370  -9.071  46.452  1.00145.95           C  
ANISOU 3718  CG  HIS B1063    19395  16219  19838    946   1106   3138       C  
ATOM   3719  ND1 HIS B1063      70.585  -9.358  45.867  1.00156.94           N  
ANISOU 3719  ND1 HIS B1063    20722  17588  21319   1270   1250   3368       N  
ATOM   3720  CD2 HIS B1063      68.424  -9.478  45.572  1.00152.41           C  
ANISOU 3720  CD2 HIS B1063    20535  16673  20701    716   1295   2836       C  
ATOM   3721  CE1 HIS B1063      70.383  -9.916  44.687  1.00156.13           C  
ANISOU 3721  CE1 HIS B1063    20891  17125  21308   1237   1514   3213       C  
ATOM   3722  NE2 HIS B1063      69.080  -9.999  44.483  1.00158.91           N  
ANISOU 3722  NE2 HIS B1063    21481  17262  21635    905   1546   2890       N  
ATOM   3723  N   GLY B1064      67.006  -6.147  47.388  1.00132.55           N  
ANISOU 3723  N   GLY B1064    17253  15175  17937     -9    169   2369       N  
ATOM   3724  CA  GLY B1064      65.923  -5.630  46.571  1.00129.50           C  
ANISOU 3724  CA  GLY B1064    16977  14663  17565   -390     82   1930       C  
ATOM   3725  C   GLY B1064      66.255  -4.313  45.902  1.00124.81           C  
ANISOU 3725  C   GLY B1064    16080  14341  17002   -511   -234   1761       C  
ATOM   3726  O   GLY B1064      65.793  -4.044  44.790  1.00117.49           O  
ANISOU 3726  O   GLY B1064    15265  13246  16131   -713   -219   1461       O  
ATOM   3727  N   PHE B1065      67.059  -3.477  46.560  1.00135.86           N  
ANISOU 3727  N   PHE B1065    17093  16160  18366   -391   -524   1948       N  
ATOM   3728  CA  PHE B1065      67.445  -2.202  45.975  1.00136.06           C  
ANISOU 3728  CA  PHE B1065    16813  16461  18422   -493   -833   1811       C  
ATOM   3729  C   PHE B1065      68.627  -2.341  45.027  1.00129.97           C  
ANISOU 3729  C   PHE B1065    15991  15637  17756   -229   -685   1981       C  
ATOM   3730  O   PHE B1065      68.862  -1.444  44.210  1.00128.47           O  
ANISOU 3730  O   PHE B1065    15635  15567  17610   -335   -861   1823       O  
ATOM   3731  CB  PHE B1065      67.800  -1.201  47.076  1.00138.16           C  
ANISOU 3731  CB  PHE B1065    16676  17210  18610   -486  -1218   1927       C  
ATOM   3732  CG  PHE B1065      66.696  -0.973  48.066  1.00135.93           C  
ANISOU 3732  CG  PHE B1065    16404  17025  18218   -741  -1393   1767       C  
ATOM   3733  CD1 PHE B1065      65.711  -0.026  47.837  1.00137.49           C  
ANISOU 3733  CD1 PHE B1065    16543  17310  18385  -1120  -1665   1382       C  
ATOM   3734  CD2 PHE B1065      66.652  -1.706  49.238  1.00135.50           C  
ANISOU 3734  CD2 PHE B1065    16417  16979  18089   -597  -1287   2004       C  
ATOM   3735  CE1 PHE B1065      64.699   0.174  48.758  1.00145.27           C  
ANISOU 3735  CE1 PHE B1065    17534  18391  19270  -1352  -1824   1231       C  
ATOM   3736  CE2 PHE B1065      65.648  -1.511  50.159  1.00136.40           C  
ANISOU 3736  CE2 PHE B1065    16539  17187  18098   -830  -1440   1861       C  
ATOM   3737  CZ  PHE B1065      64.669  -0.569  49.922  1.00132.98           C  
ANISOU 3737  CZ  PHE B1065    16043  16845  17639  -1208  -1709   1471       C  
ATOM   3738  N   ASP B1066      69.375  -3.443  45.120  1.00127.08           N  
ANISOU 3738  N   ASP B1066    15763  15093  17427    111   -365   2297       N  
ATOM   3739  CA  ASP B1066      70.450  -3.694  44.167  1.00125.00           C  
ANISOU 3739  CA  ASP B1066    15485  14740  17267    363   -186   2446       C  
ATOM   3740  C   ASP B1066      69.900  -4.117  42.810  1.00124.99           C  
ANISOU 3740  C   ASP B1066    15803  14344  17342    219     53   2179       C  
ATOM   3741  O   ASP B1066      70.387  -3.663  41.768  1.00121.81           O  
ANISOU 3741  O   ASP B1066    15322  13951  17011    224     32   2099       O  
ATOM   3742  CB  ASP B1066      71.394  -4.757  44.724  1.00136.12           C  
ANISOU 3742  CB  ASP B1066    16946  16081  18692    775     76   2862       C  
ATOM   3743  CG  ASP B1066      72.094  -4.304  45.989  1.00134.06           C  
ANISOU 3743  CG  ASP B1066    16345  16230  18364    953   -164   3146       C  
ATOM   3744  OD1 ASP B1066      72.282  -3.080  46.160  1.00134.38           O  
ANISOU 3744  OD1 ASP B1066    16044  16636  18379    836   -523   3071       O  
ATOM   3745  OD2 ASP B1066      72.451  -5.169  46.815  1.00131.38           O  
ANISOU 3745  OD2 ASP B1066    16081  15844  17995   1209      3   3442       O  
ATOM   3746  N   ILE B1067      68.887  -4.987  42.802  1.00126.77           N  
ANISOU 3746  N   ILE B1067    16392  14222  17553     89    283   2036       N  
ATOM   3747  CA  ILE B1067      68.218  -5.325  41.549  1.00126.31           C  
ANISOU 3747  CA  ILE B1067    16637  13796  17560    -88    483   1739       C  
ATOM   3748  C   ILE B1067      67.638  -4.070  40.914  1.00120.54           C  
ANISOU 3748  C   ILE B1067    15765  13214  16820   -430    172   1373       C  
ATOM   3749  O   ILE B1067      67.663  -3.903  39.688  1.00122.06           O  
ANISOU 3749  O   ILE B1067    16039  13258  17081   -501    238   1191       O  
ATOM   3750  CB  ILE B1067      67.125  -6.383  41.790  1.00131.93           C  
ANISOU 3750  CB  ILE B1067    17740  14140  18249   -203    744   1628       C  
ATOM   3751  CG1 ILE B1067      67.727  -7.657  42.387  1.00135.66           C  
ANISOU 3751  CG1 ILE B1067    18366  14445  18732    146   1061   2000       C  
ATOM   3752  CG2 ILE B1067      66.399  -6.688  40.482  1.00136.17           C  
ANISOU 3752  CG2 ILE B1067    18582  14303  18853   -398    936   1299       C  
ATOM   3753  CD1 ILE B1067      66.694  -8.633  42.931  1.00132.57           C  
ANISOU 3753  CD1 ILE B1067    18312  13758  18299     42   1276   1940       C  
ATOM   3754  N   LEU B1068      67.111  -3.166  41.740  1.00108.25           N  
ANISOU 3754  N   LEU B1068    13996  11958  15178   -644   -173   1260       N  
ATOM   3755  CA  LEU B1068      66.506  -1.944  41.223  1.00103.52           C  
ANISOU 3755  CA  LEU B1068    13258  11512  14564   -978   -491    907       C  
ATOM   3756  C   LEU B1068      67.555  -1.060  40.561  1.00101.53           C  
ANISOU 3756  C   LEU B1068    12714  11498  14365   -876   -661    976       C  
ATOM   3757  O   LEU B1068      67.366  -0.594  39.431  1.00 99.05           O  
ANISOU 3757  O   LEU B1068    12443  11093  14097  -1036   -695    728       O  
ATOM   3758  CB  LEU B1068      65.810  -1.198  42.360  1.00104.08           C  
ANISOU 3758  CB  LEU B1068    13142  11873  14530  -1194   -826    807       C  
ATOM   3759  CG  LEU B1068      64.684  -0.238  41.981  1.00 98.91           C  
ANISOU 3759  CG  LEU B1068    12473  11265  13844  -1608  -1098    369       C  
ATOM   3760  CD1 LEU B1068      63.435  -1.008  41.583  1.00112.06           C  
ANISOU 3760  CD1 LEU B1068    14539  12527  15510  -1823   -867     88       C  
ATOM   3761  CD2 LEU B1068      64.394   0.706  43.134  1.00102.83           C  
ANISOU 3761  CD2 LEU B1068    12672  12155  14246  -1751  -1485    344       C  
ATOM   3762  N   VAL B1069      68.670  -0.816  41.254  1.00103.26           N  
ANISOU 3762  N   VAL B1069    12633  12025  14577   -611   -768   1310       N  
ATOM   3763  CA  VAL B1069      69.733   0.012  40.693  1.00 98.12           C  
ANISOU 3763  CA  VAL B1069    11687  11616  13977   -500   -926   1398       C  
ATOM   3764  C   VAL B1069      70.299  -0.630  39.433  1.00 99.30           C  
ANISOU 3764  C   VAL B1069    12028  11475  14227   -337   -607   1434       C  
ATOM   3765  O   VAL B1069      70.605   0.058  38.451  1.00 99.53           O  
ANISOU 3765  O   VAL B1069    11959  11554  14304   -410   -700   1303       O  
ATOM   3766  CB  VAL B1069      70.832   0.255  41.744  1.00 98.63           C  
ANISOU 3766  CB  VAL B1069    11411  12046  14018   -220  -1068   1769       C  
ATOM   3767  CG1 VAL B1069      72.034   0.949  41.113  1.00 97.67           C  
ANISOU 3767  CG1 VAL B1069    11006  12141  13963    -66  -1173   1891       C  
ATOM   3768  CG2 VAL B1069      70.289   1.074  42.906  1.00 97.43           C  
ANISOU 3768  CG2 VAL B1069    11032  12220  13767   -404  -1428   1703       C  
ATOM   3769  N   GLY B1070      70.449  -1.955  39.439  1.00100.68           N  
ANISOU 3769  N   GLY B1070    12479  11340  14433   -115   -228   1611       N  
ATOM   3770  CA  GLY B1070      70.953  -2.631  38.255  1.00115.41           C  
ANISOU 3770  CA  GLY B1070    14541  12914  16393     43     90   1640       C  
ATOM   3771  C   GLY B1070      70.104  -2.363  37.029  1.00114.41           C  
ANISOU 3771  C   GLY B1070    14617  12558  16297   -254    109   1246       C  
ATOM   3772  O   GLY B1070      70.627  -2.162  35.930  1.00113.90           O  
ANISOU 3772  O   GLY B1070    14541  12437  16298   -211    172   1200       O  
ATOM   3773  N   GLN B1071      68.781  -2.347  37.200  1.00116.81           N  
ANISOU 3773  N   GLN B1071    15107  12728  16549   -560     52    953       N  
ATOM   3774  CA  GLN B1071      67.894  -2.047  36.084  1.00114.89           C  
ANISOU 3774  CA  GLN B1071    15051  12275  16325   -860     45    557       C  
ATOM   3775  C   GLN B1071      67.887  -0.556  35.758  1.00103.61           C  
ANISOU 3775  C   GLN B1071    13330  11160  14876  -1082   -351    359       C  
ATOM   3776  O   GLN B1071      67.788  -0.177  34.585  1.00 96.48           O  
ANISOU 3776  O   GLN B1071    12489  10154  14014  -1208   -354    140       O  
ATOM   3777  CB  GLN B1071      66.477  -2.518  36.399  1.00118.01           C  
ANISOU 3777  CB  GLN B1071    15734  12431  16674  -1114    111    303       C  
ATOM   3778  CG  GLN B1071      66.293  -4.005  36.620  1.00120.18           C  
ANISOU 3778  CG  GLN B1071    16345  12347  16971   -946    513    442       C  
ATOM   3779  CD  GLN B1071      64.863  -4.337  37.023  1.00127.19           C  
ANISOU 3779  CD  GLN B1071    17479  13041  17805  -1226    536    179       C  
ATOM   3780  OE1 GLN B1071      64.251  -3.623  37.819  1.00127.75           O  
ANISOU 3780  OE1 GLN B1071    17398  13346  17797  -1436    245     62       O  
ATOM   3781  NE2 GLN B1071      64.321  -5.412  36.464  1.00128.59           N  
ANISOU 3781  NE2 GLN B1071    18035  12795  18028  -1234    882     77       N  
ATOM   3782  N   ILE B1072      67.982   0.305  36.777  1.00101.46           N  
ANISOU 3782  N   ILE B1072    12742  11269  14538  -1134   -690    429       N  
ATOM   3783  CA  ILE B1072      68.068   1.740  36.520  1.00 96.05           C  
ANISOU 3783  CA  ILE B1072    11757  10900  13837  -1324  -1076    269       C  
ATOM   3784  C   ILE B1072      69.341   2.057  35.751  1.00 91.38           C  
ANISOU 3784  C   ILE B1072    10985  10418  13317  -1113  -1051    444       C  
ATOM   3785  O   ILE B1072      69.376   2.996  34.947  1.00 87.28           O  
ANISOU 3785  O   ILE B1072    10349   9998  12814  -1274  -1242    254       O  
ATOM   3786  CB  ILE B1072      67.998   2.544  37.835  1.00 98.25           C  
ANISOU 3786  CB  ILE B1072    11721  11573  14035  -1391  -1434    338       C  
ATOM   3787  CG1 ILE B1072      66.617   2.403  38.480  1.00101.29           C  
ANISOU 3787  CG1 ILE B1072    12276  11864  14346  -1661  -1498     98       C  
ATOM   3788  CG2 ILE B1072      68.330   4.013  37.579  1.00 93.31           C  
ANISOU 3788  CG2 ILE B1072    10751  11296  13407  -1530  -1824    233       C  
ATOM   3789  CD1 ILE B1072      66.530   2.977  39.885  1.00 99.60           C  
ANISOU 3789  CD1 ILE B1072    11788  12008  14048  -1695  -1798    197       C  
ATOM   3790  N   ASP B1073      70.406   1.288  35.986  1.00 94.24           N  
ANISOU 3790  N   ASP B1073    11319  10766  13720   -750   -818    807       N  
ATOM   3791  CA  ASP B1073      71.643   1.497  35.244  1.00 80.68           C  
ANISOU 3791  CA  ASP B1073     9442   9139  12075   -533   -763    981       C  
ATOM   3792  C   ASP B1073      71.498   1.026  33.803  1.00 85.07           C  
ANISOU 3792  C   ASP B1073    10285   9340  12696   -567   -493    806       C  
ATOM   3793  O   ASP B1073      71.978   1.689  32.876  1.00 88.38           O  
ANISOU 3793  O   ASP B1073    10590   9835  13154   -600   -572    734       O  
ATOM   3794  CB  ASP B1073      72.795   0.769  35.936  1.00 98.63           C  
ANISOU 3794  CB  ASP B1073    11610  11491  14372   -130   -587   1411       C  
ATOM   3795  CG  ASP B1073      73.228   1.452  37.218  1.00101.76           C  
ANISOU 3795  CG  ASP B1073    11643  12308  14712    -63   -893   1608       C  
ATOM   3796  OD1 ASP B1073      72.971   2.666  37.362  1.00 96.53           O  
ANISOU 3796  OD1 ASP B1073    10739  11926  14013   -292  -1258   1443       O  
ATOM   3797  OD2 ASP B1073      73.827   0.776  38.083  1.00101.93           O  
ANISOU 3797  OD2 ASP B1073    11621  12379  14727    219   -771   1926       O  
ATOM   3798  N   ASP B1074      70.839  -0.116  33.594  1.00 91.76           N  
ANISOU 3798  N   ASP B1074    11509   9799  13557   -563   -174    735       N  
ATOM   3799  CA  ASP B1074      70.585  -0.579  32.234  1.00 93.59           C  
ANISOU 3799  CA  ASP B1074    12032   9681  13848   -616     79    539       C  
ATOM   3800  C   ASP B1074      69.767   0.443  31.455  1.00 79.71           C  
ANISOU 3800  C   ASP B1074    10275   7944  12067   -982   -165    144       C  
ATOM   3801  O   ASP B1074      70.002   0.660  30.261  1.00 78.62           O  
ANISOU 3801  O   ASP B1074    10190   7707  11974  -1012   -103     23       O  
ATOM   3802  CB  ASP B1074      69.868  -1.928  32.262  1.00101.59           C  
ANISOU 3802  CB  ASP B1074    13446  10281  14872   -585    432    502       C  
ATOM   3803  CG  ASP B1074      70.763  -3.054  32.740  1.00107.07           C  
ANISOU 3803  CG  ASP B1074    14190  10886  15606   -197    732    887       C  
ATOM   3804  OD1 ASP B1074      71.990  -2.841  32.831  1.00113.86           O  
ANISOU 3804  OD1 ASP B1074    14797  11970  16497     60    703   1166       O  
ATOM   3805  OD2 ASP B1074      70.240  -4.152  33.024  1.00105.07           O  
ANISOU 3805  OD2 ASP B1074    14228  10338  15354   -149    997    909       O  
ATOM   3806  N   ALA B1075      68.803   1.085  32.119  1.00 81.21           N  
ANISOU 3806  N   ALA B1075    10405   8266  12184  -1260   -447    -62       N  
ATOM   3807  CA  ALA B1075      68.005   2.108  31.454  1.00 78.84           C  
ANISOU 3807  CA  ALA B1075    10092   8006  11858  -1611   -709   -442       C  
ATOM   3808  C   ALA B1075      68.824   3.366  31.197  1.00 78.76           C  
ANISOU 3808  C   ALA B1075     9720   8351  11853  -1618  -1012   -394       C  
ATOM   3809  O   ALA B1075      68.695   3.992  30.138  1.00 81.88           O  
ANISOU 3809  O   ALA B1075    10135   8712  12266  -1780  -1096   -619       O  
ATOM   3810  CB  ALA B1075      66.771   2.436  32.295  1.00 77.10           C  
ANISOU 3810  CB  ALA B1075     9894   7840  11559  -1895   -931   -668       C  
ATOM   3811  N   LEU B1076      69.667   3.758  32.156  1.00 78.17           N  
ANISOU 3811  N   LEU B1076     9316   8621  11763  -1445  -1181   -106       N  
ATOM   3812  CA  LEU B1076      70.505   4.937  31.964  1.00 71.88           C  
ANISOU 3812  CA  LEU B1076     8162   8171  10977  -1438  -1464    -41       C  
ATOM   3813  C   LEU B1076      71.431   4.780  30.765  1.00 73.03           C  
ANISOU 3813  C   LEU B1076     8336   8213  11198  -1270  -1261     45       C  
ATOM   3814  O   LEU B1076      71.728   5.765  30.081  1.00 77.29           O  
ANISOU 3814  O   LEU B1076     8708   8909  11749  -1382  -1459    -61       O  
ATOM   3815  CB  LEU B1076      71.313   5.217  33.230  1.00 72.76           C  
ANISOU 3815  CB  LEU B1076     7932   8648  11066  -1241  -1634    282       C  
ATOM   3816  CG  LEU B1076      70.633   6.131  34.252  1.00 70.54           C  
ANISOU 3816  CG  LEU B1076     7444   8652  10706  -1472  -2025    157       C  
ATOM   3817  CD1 LEU B1076      71.286   6.008  35.616  1.00 72.02           C  
ANISOU 3817  CD1 LEU B1076     7387   9110  10865  -1243  -2098    492       C  
ATOM   3818  CD2 LEU B1076      70.662   7.577  33.779  1.00 78.44           C  
ANISOU 3818  CD2 LEU B1076     8195   9909  11701  -1696  -2393    -36       C  
ATOM   3819  N   LYS B1077      71.901   3.560  30.495  1.00 75.77           N  
ANISOU 3819  N   LYS B1077     8891   8300  11598  -1003   -867    235       N  
ATOM   3820  CA  LYS B1077      72.748   3.342  29.326  1.00 76.97           C  
ANISOU 3820  CA  LYS B1077     9088   8335  11822   -841   -653    306       C  
ATOM   3821  C   LYS B1077      71.984   3.634  28.041  1.00 82.56           C  
ANISOU 3821  C   LYS B1077    10017   8817  12534  -1110   -641    -62       C  
ATOM   3822  O   LYS B1077      72.497   4.301  27.135  1.00 79.58           O  
ANISOU 3822  O   LYS B1077     9531   8523  12183  -1140   -715   -114       O  
ATOM   3823  CB  LYS B1077      73.283   1.911  29.312  1.00 80.27           C  
ANISOU 3823  CB  LYS B1077     9715   8491  12294   -513   -227    558       C  
ATOM   3824  CG  LYS B1077      74.348   1.676  28.247  1.00 84.58           C  
ANISOU 3824  CG  LYS B1077    10256   8965  12915   -296     -8    688       C  
ATOM   3825  CD  LYS B1077      74.497   0.204  27.900  1.00 90.99           C  
ANISOU 3825  CD  LYS B1077    11386   9404  13782    -58    441    807       C  
ATOM   3826  CE  LYS B1077      74.882  -0.627  29.113  1.00 93.72           C  
ANISOU 3826  CE  LYS B1077    11703   9782  14125    211    563   1127       C  
ATOM   3827  NZ  LYS B1077      75.129  -2.049  28.745  1.00107.64           N  
ANISOU 3827  NZ  LYS B1077    13763  11187  15948    463   1000   1261       N  
ATOM   3828  N   LEU B1078      70.752   3.129  27.942  1.00 85.16           N  
ANISOU 3828  N   LEU B1078    10662   8857  12837  -1306   -546   -322       N  
ATOM   3829  CA  LEU B1078      69.940   3.391  26.759  1.00 84.43           C  
ANISOU 3829  CA  LEU B1078    10791   8543  12744  -1570   -543   -691       C  
ATOM   3830  C   LEU B1078      69.692   4.884  26.587  1.00 83.13           C  
ANISOU 3830  C   LEU B1078    10389   8659  12537  -1845   -963   -904       C  
ATOM   3831  O   LEU B1078      69.718   5.402  25.465  1.00 86.08           O  
ANISOU 3831  O   LEU B1078    10797   8983  12925  -1962  -1001  -1082       O  
ATOM   3832  CB  LEU B1078      68.615   2.636  26.859  1.00 85.88           C  
ANISOU 3832  CB  LEU B1078    11325   8400  12903  -1742   -400   -934       C  
ATOM   3833  CG  LEU B1078      68.727   1.112  26.919  1.00 84.78           C  
ANISOU 3833  CG  LEU B1078    11470   7934  12811  -1497     33   -764       C  
ATOM   3834  CD1 LEU B1078      67.432   0.493  27.421  1.00 93.78           C  
ANISOU 3834  CD1 LEU B1078    12879   8838  13914  -1673    106   -961       C  
ATOM   3835  CD2 LEU B1078      69.095   0.554  25.554  1.00 91.01           C  
ANISOU 3835  CD2 LEU B1078    12475   8440  13667  -1392    337   -805       C  
ATOM   3836  N   ALA B1079      69.449   5.594  27.690  1.00 81.72           N  
ANISOU 3836  N   ALA B1079     9970   8775  12304  -1952  -1285   -888       N  
ATOM   3837  CA  ALA B1079      69.220   7.031  27.603  1.00 82.47           C  
ANISOU 3837  CA  ALA B1079     9827   9148  12360  -2210  -1701  -1083       C  
ATOM   3838  C   ALA B1079      70.477   7.762  27.144  1.00 83.16           C  
ANISOU 3838  C   ALA B1079     9626   9486  12485  -2073  -1801   -898       C  
ATOM   3839  O   ALA B1079      70.393   8.742  26.396  1.00 86.58           O  
ANISOU 3839  O   ALA B1079     9978  10008  12911  -2266  -2013  -1094       O  
ATOM   3840  CB  ALA B1079      68.749   7.569  28.954  1.00 83.89           C  
ANISOU 3840  CB  ALA B1079     9801   9596  12476  -2327  -2011  -1083       C  
ATOM   3841  N   ASN B1080      71.651   7.299  27.582  1.00 85.77           N  
ANISOU 3841  N   ASN B1080     9799   9932  12856  -1740  -1651   -523       N  
ATOM   3842  CA  ASN B1080      72.897   7.933  27.166  1.00 79.90           C  
ANISOU 3842  CA  ASN B1080     8778   9427  12155  -1594  -1724   -333       C  
ATOM   3843  C   ASN B1080      73.181   7.707  25.687  1.00 78.92           C  
ANISOU 3843  C   ASN B1080     8841   9067  12077  -1572  -1494   -424       C  
ATOM   3844  O   ASN B1080      73.857   8.527  25.056  1.00 82.98           O  
ANISOU 3844  O   ASN B1080     9164   9754  12610  -1586  -1623   -410       O  
ATOM   3845  CB  ASN B1080      74.058   7.411  28.011  1.00 85.41           C  
ANISOU 3845  CB  ASN B1080     9276  10291  12885  -1232  -1602     85       C  
ATOM   3846  CG  ASN B1080      74.158   8.105  29.353  1.00 85.12           C  
ANISOU 3846  CG  ASN B1080     8912  10624  12804  -1247  -1931    207       C  
ATOM   3847  OD1 ASN B1080      74.792   9.154  29.475  1.00 86.13           O  
ANISOU 3847  OD1 ASN B1080     8706  11083  12935  -1265  -2208    273       O  
ATOM   3848  ND2 ASN B1080      73.525   7.527  30.368  1.00 84.50           N  
ANISOU 3848  ND2 ASN B1080     8929  10492  12685  -1243  -1903    234       N  
ATOM   3849  N   GLU B1081      72.681   6.613  25.120  1.00 85.51           N  
ANISOU 3849  N   GLU B1081     8009  15054   9426   -973  -3167   1816       N  
ATOM   3850  CA  GLU B1081      72.827   6.344  23.696  1.00 88.95           C  
ANISOU 3850  CA  GLU B1081     8270  15516  10010   -834  -3111   1837       C  
ATOM   3851  C   GLU B1081      71.775   7.054  22.853  1.00 83.46           C  
ANISOU 3851  C   GLU B1081     7533  14853   9324   -726  -3034   1612       C  
ATOM   3852  O   GLU B1081      71.724   6.836  21.638  1.00 80.17           O  
ANISOU 3852  O   GLU B1081     6988  14458   9016   -593  -2975   1597       O  
ATOM   3853  CB  GLU B1081      72.753   4.837  23.434  1.00 88.41           C  
ANISOU 3853  CB  GLU B1081     8125  15462  10004   -805  -2978   1876       C  
ATOM   3854  CG  GLU B1081      73.916   4.048  24.005  1.00 90.65           C  
ANISOU 3854  CG  GLU B1081     8419  15714  10309   -885  -3055   2120       C  
ATOM   3855  CD  GLU B1081      73.759   2.554  23.801  1.00 93.51           C  
ANISOU 3855  CD  GLU B1081     8714  16092  10725   -860  -2915   2145       C  
ATOM   3856  OE1 GLU B1081      72.646   2.115  23.442  1.00 87.70           O  
ANISOU 3856  OE1 GLU B1081     7944  15386   9992   -803  -2754   1956       O  
ATOM   3857  OE2 GLU B1081      74.749   1.819  24.000  1.00 95.83           O  
ANISOU 3857  OE2 GLU B1081     8984  16364  11066   -898  -2968   2350       O  
ATOM   3858  N   GLY B1082      70.946   7.898  23.464  1.00 85.26           N  
ANISOU 3858  N   GLY B1082     7871  15084   9440   -773  -3037   1438       N  
ATOM   3859  CA  GLY B1082      69.879   8.553  22.738  1.00 84.50           C  
ANISOU 3859  CA  GLY B1082     7742  15015   9349   -674  -2966   1209       C  
ATOM   3860  C   GLY B1082      68.705   7.660  22.422  1.00 85.41           C  
ANISOU 3860  C   GLY B1082     7808  15156   9490   -616  -2780   1016       C  
ATOM   3861  O   GLY B1082      67.932   7.969  21.510  1.00 85.26           O  
ANISOU 3861  O   GLY B1082     7719  15158   9519   -497  -2720    843       O  
ATOM   3862  N   LYS B1083      68.551   6.552  23.142  1.00 92.96           N  
ANISOU 3862  N   LYS B1083     8797  16104  10421   -692  -2690   1039       N  
ATOM   3863  CA  LYS B1083      67.453   5.616  22.911  1.00 94.31           C  
ANISOU 3863  CA  LYS B1083     8914  16287  10633   -645  -2505    860       C  
ATOM   3864  C   LYS B1083      66.359   5.858  23.951  1.00 96.35           C  
ANISOU 3864  C   LYS B1083     9298  16528  10780   -735  -2420    667       C  
ATOM   3865  O   LYS B1083      66.166   5.095  24.899  1.00 96.34           O  
ANISOU 3865  O   LYS B1083     9376  16504  10723   -831  -2336    680       O  
ATOM   3866  CB  LYS B1083      67.970   4.182  22.961  1.00 95.92           C  
ANISOU 3866  CB  LYS B1083     9062  16486  10897   -661  -2440   1009       C  
ATOM   3867  CG  LYS B1083      69.131   3.915  22.017  1.00 94.93           C  
ANISOU 3867  CG  LYS B1083     8819  16369  10880   -581  -2522   1218       C  
ATOM   3868  CD  LYS B1083      69.655   2.497  22.165  1.00 98.98           C  
ANISOU 3868  CD  LYS B1083     9286  16876  11445   -609  -2462   1369       C  
ATOM   3869  CE  LYS B1083      70.775   2.214  21.175  1.00 98.54           C  
ANISOU 3869  CE  LYS B1083     9108  16826  11507   -523  -2531   1571       C  
ATOM   3870  NZ  LYS B1083      71.509   0.961  21.505  1.00 98.53           N  
ANISOU 3870  NZ  LYS B1083     9081  16812  11542   -575  -2509   1757       N  
ATOM   3871  N   VAL B1084      65.627   6.955  23.744  1.00 97.15           N  
ANISOU 3871  N   VAL B1084     9422  16638  10852   -698  -2437    484       N  
ATOM   3872  CA  VAL B1084      64.629   7.371  24.725  1.00103.79           C  
ANISOU 3872  CA  VAL B1084    10390  17459  11586   -784  -2368    302       C  
ATOM   3873  C   VAL B1084      63.538   6.317  24.855  1.00105.98           C  
ANISOU 3873  C   VAL B1084    10632  17724  11912   -777  -2161    134       C  
ATOM   3874  O   VAL B1084      63.115   5.974  25.965  1.00106.28           O  
ANISOU 3874  O   VAL B1084    10786  17728  11867   -885  -2070     97       O  
ATOM   3875  CB  VAL B1084      64.050   8.750  24.352  1.00 99.22           C  
ANISOU 3875  CB  VAL B1084     9824  16892  10982   -732  -2427    133       C  
ATOM   3876  CG1 VAL B1084      63.358   8.702  22.997  1.00101.02           C  
ANISOU 3876  CG1 VAL B1084     9900  17144  11338   -569  -2363    -34       C  
ATOM   3877  CG2 VAL B1084      63.090   9.233  25.431  1.00 99.05           C  
ANISOU 3877  CG2 VAL B1084     9943  16846  10846   -828  -2362    -42       C  
ATOM   3878  N   LYS B1085      63.070   5.779  23.728  1.00115.14           N  
ANISOU 3878  N   LYS B1085    11634  18901  13212   -648  -2081     30       N  
ATOM   3879  CA  LYS B1085      61.980   4.811  23.778  1.00123.97           C  
ANISOU 3879  CA  LYS B1085    12699  19999  14403   -633  -1885   -149       C  
ATOM   3880  C   LYS B1085      62.441   3.486  24.373  1.00120.75           C  
ANISOU 3880  C   LYS B1085    12306  19573  14001   -708  -1804      7       C  
ATOM   3881  O   LYS B1085      61.696   2.845  25.123  1.00120.13           O  
ANISOU 3881  O   LYS B1085    12275  19456  13911   -775  -1647    -92       O  
ATOM   3882  CB  LYS B1085      61.406   4.599  22.377  1.00142.06           C  
ANISOU 3882  CB  LYS B1085    14817  22310  16848   -464  -1843   -302       C  
ATOM   3883  CG  LYS B1085      59.939   4.978  22.231  1.00135.51           C  
ANISOU 3883  CG  LYS B1085    13962  21462  16063   -416  -1741   -617       C  
ATOM   3884  CD  LYS B1085      59.695   6.453  22.509  1.00132.65           C  
ANISOU 3884  CD  LYS B1085    13698  21104  15597   -441  -1836   -704       C  
ATOM   3885  CE  LYS B1085      58.218   6.793  22.397  1.00121.27           C  
ANISOU 3885  CE  LYS B1085    12228  19640  14211   -397  -1730  -1022       C  
ATOM   3886  NZ  LYS B1085      57.743   7.609  23.550  1.00107.61           N  
ANISOU 3886  NZ  LYS B1085    10650  17883  12352   -521  -1713  -1103       N  
ATOM   3887  N   GLU B1086      63.663   3.057  24.052  1.00119.27           N  
ANISOU 3887  N   GLU B1086    12077  19403  13835   -696  -1901    250       N  
ATOM   3888  CA  GLU B1086      64.181   1.822  24.632  1.00115.93           C  
ANISOU 3888  CA  GLU B1086    11674  18962  13412   -768  -1839    412       C  
ATOM   3889  C   GLU B1086      64.382   1.958  26.136  1.00109.54           C  
ANISOU 3889  C   GLU B1086    11062  18115  12441   -925  -1850    491       C  
ATOM   3890  O   GLU B1086      64.147   1.006  26.889  1.00109.46           O  
ANISOU 3890  O   GLU B1086    11110  18072  12408   -994  -1721    506       O  
ATOM   3891  CB  GLU B1086      65.488   1.426  23.947  1.00119.87           C  
ANISOU 3891  CB  GLU B1086    12087  19486  13974   -720  -1954    657       C  
ATOM   3892  CG  GLU B1086      65.305   0.937  22.519  1.00129.62           C  
ANISOU 3892  CG  GLU B1086    13135  20748  15367   -562  -1911    597       C  
ATOM   3893  CD  GLU B1086      66.573   0.347  21.931  1.00125.54           C  
ANISOU 3893  CD  GLU B1086    12537  20246  14915   -522  -1992    847       C  
ATOM   3894  OE1 GLU B1086      67.091   0.909  20.943  1.00124.30           O  
ANISOU 3894  OE1 GLU B1086    12306  20111  14811   -419  -2092    903       O  
ATOM   3895  OE2 GLU B1086      67.053  -0.678  22.459  1.00123.80           O  
ANISOU 3895  OE2 GLU B1086    12331  20011  14695   -591  -1951    990       O  
ATOM   3896  N   ALA B1087      64.823   3.132  26.595  1.00108.50           N  
ANISOU 3896  N   ALA B1087    11045  17985  12196   -977  -2002    544       N  
ATOM   3897  CA  ALA B1087      64.991   3.344  28.029  1.00 92.64           C  
ANISOU 3897  CA  ALA B1087     9240  15936  10022  -1115  -2027    608       C  
ATOM   3898  C   ALA B1087      63.649   3.329  28.749  1.00 87.63           C  
ANISOU 3898  C   ALA B1087     8697  15267   9333  -1160  -1846    380       C  
ATOM   3899  O   ALA B1087      63.532   2.770  29.846  1.00 82.80           O  
ANISOU 3899  O   ALA B1087     8224  14609   8626  -1254  -1757    415       O  
ATOM   3900  CB  ALA B1087      65.719   4.663  28.283  1.00103.14           C  
ANISOU 3900  CB  ALA B1087    10660  17272  11257  -1150  -2239    696       C  
ATOM   3901  N   GLN B1088      62.625   3.937  28.146  1.00107.74           N  
ANISOU 3901  N   GLN B1088    11170  17827  11941  -1089  -1785    146       N  
ATOM   3902  CA  GLN B1088      61.298   3.928  28.752  1.00104.92           C  
ANISOU 3902  CA  GLN B1088    10878  17428  11559  -1125  -1602    -84       C  
ATOM   3903  C   GLN B1088      60.785   2.503  28.917  1.00104.12           C  
ANISOU 3903  C   GLN B1088    10728  17291  11540  -1133  -1391   -120       C  
ATOM   3904  O   GLN B1088      60.165   2.170  29.934  1.00100.56           O  
ANISOU 3904  O   GLN B1088    10403  16785  11022  -1215  -1241   -187       O  
ATOM   3905  CB  GLN B1088      60.336   4.757  27.902  1.00 93.25           C  
ANISOU 3905  CB  GLN B1088     9296  15970  10164  -1030  -1586   -329       C  
ATOM   3906  CG  GLN B1088      60.642   6.246  27.918  1.00 93.97           C  
ANISOU 3906  CG  GLN B1088     9461  16084  10158  -1036  -1766   -326       C  
ATOM   3907  CD  GLN B1088      59.813   7.028  26.920  1.00 97.54           C  
ANISOU 3907  CD  GLN B1088     9799  16560  10701   -924  -1769   -549       C  
ATOM   3908  OE1 GLN B1088      59.322   6.477  25.935  1.00103.36           O  
ANISOU 3908  OE1 GLN B1088    10375  17309  11589   -815  -1692   -660       O  
ATOM   3909  NE2 GLN B1088      59.660   8.324  27.165  1.00 99.87           N  
ANISOU 3909  NE2 GLN B1088    10181  16860  10904   -945  -1866   -619       N  
ATOM   3910  N   ALA B1089      61.028   1.649  27.920  1.00112.97           N  
ANISOU 3910  N   ALA B1089    11673  18439  12812  -1044  -1371    -77       N  
ATOM   3911  CA  ALA B1089      60.651   0.246  28.044  1.00122.03           C  
ANISOU 3911  CA  ALA B1089    12764  19552  14048  -1050  -1182    -91       C  
ATOM   3912  C   ALA B1089      61.384  -0.415  29.204  1.00117.84           C  
ANISOU 3912  C   ALA B1089    12394  18987  13391  -1167  -1170    119       C  
ATOM   3913  O   ALA B1089      60.792  -1.194  29.961  1.00117.48           O  
ANISOU 3913  O   ALA B1089    12418  18886  13335  -1226   -982     67       O  
ATOM   3914  CB  ALA B1089      60.948  -0.493  26.741  1.00116.38           C  
ANISOU 3914  CB  ALA B1089    11839  18876  13505   -929  -1196    -57       C  
ATOM   3915  N   ALA B1090      62.677  -0.119  29.357  1.00112.25           N  
ANISOU 3915  N   ALA B1090    11750  18306  12595  -1199  -1368    356       N  
ATOM   3916  CA  ALA B1090      63.424  -0.669  30.482  1.00112.01           C  
ANISOU 3916  CA  ALA B1090    11886  18240  12435  -1304  -1386    556       C  
ATOM   3917  C   ALA B1090      62.837  -0.191  31.802  1.00117.47           C  
ANISOU 3917  C   ALA B1090    12802  18873  12957  -1403  -1316    475       C  
ATOM   3918  O   ALA B1090      62.790  -0.944  32.781  1.00122.43           O  
ANISOU 3918  O   ALA B1090    13568  19447  13504  -1477  -1202    534       O  
ATOM   3919  CB  ALA B1090      64.898  -0.280  30.374  1.00 86.51           C  
ANISOU 3919  CB  ALA B1090     8674  15041   9156  -1314  -1634    806       C  
ATOM   3920  N   ALA B1091      62.379   1.063  31.845  1.00110.32           N  
ANISOU 3920  N   ALA B1091    11945  17977  11995  -1402  -1378    340       N  
ATOM   3921  CA  ALA B1091      61.695   1.556  33.033  1.00113.74           C  
ANISOU 3921  CA  ALA B1091    12586  18354  12276  -1486  -1294    237       C  
ATOM   3922  C   ALA B1091      60.348   0.874  33.231  1.00144.45           C  
ANISOU 3922  C   ALA B1091    16455  22191  16240  -1486  -1009     28       C  
ATOM   3923  O   ALA B1091      59.855   0.811  34.362  1.00146.02           O  
ANISOU 3923  O   ALA B1091    16840  22322  16317  -1564   -881    -15       O  
ATOM   3924  CB  ALA B1091      61.508   3.070  32.945  1.00102.03           C  
ANISOU 3924  CB  ALA B1091    11143  16895  10730  -1479  -1429    134       C  
ATOM   3925  N   GLU B1092      59.732   0.368  32.156  1.00147.36           N  
ANISOU 3925  N   GLU B1092    16601  22580  16811  -1395   -905   -107       N  
ATOM   3926  CA  GLU B1092      58.488  -0.381  32.310  1.00151.16           C  
ANISOU 3926  CA  GLU B1092    17038  23001  17396  -1393   -632   -303       C  
ATOM   3927  C   GLU B1092      58.713  -1.667  33.095  1.00144.65           C  
ANISOU 3927  C   GLU B1092    16301  22120  16539  -1456   -486   -172       C  
ATOM   3928  O   GLU B1092      57.880  -2.050  33.925  1.00147.94           O  
ANISOU 3928  O   GLU B1092    16822  22458  16931  -1510   -269   -273       O  
ATOM   3929  CB  GLU B1092      57.892  -0.689  30.937  1.00150.77           C  
ANISOU 3929  CB  GLU B1092    16724  22982  17579  -1272   -582   -464       C  
ATOM   3930  N   GLN B1093      59.834  -2.348  32.847  1.00130.64           N  
ANISOU 3930  N   GLN B1093    14489  20379  14769  -1449   -596     55       N  
ATOM   3931  CA  GLN B1093      60.169  -3.541  33.616  1.00130.76           C  
ANISOU 3931  CA  GLN B1093    14603  20343  14738  -1509   -481    201       C  
ATOM   3932  C   GLN B1093      60.531  -3.213  35.058  1.00133.38           C  
ANISOU 3932  C   GLN B1093    15228  20622  14828  -1613   -511    315       C  
ATOM   3933  O   GLN B1093      60.511  -4.111  35.907  1.00137.80           O  
ANISOU 3933  O   GLN B1093    15916  21116  15324  -1668   -366    388       O  
ATOM   3934  CB  GLN B1093      61.304  -4.312  32.939  1.00128.68           C  
ANISOU 3934  CB  GLN B1093    14217  20129  14545  -1469   -605    414       C  
ATOM   3935  CG  GLN B1093      61.020  -4.659  31.483  1.00127.81           C  
ANISOU 3935  CG  GLN B1093    13829  20070  14663  -1354   -588    314       C  
ATOM   3936  CD  GLN B1093      62.176  -5.371  30.809  1.00125.59           C  
ANISOU 3936  CD  GLN B1093    13436  19837  14446  -1313   -712    531       C  
ATOM   3937  OE1 GLN B1093      63.321  -5.282  31.252  1.00122.44           O  
ANISOU 3937  OE1 GLN B1093    13143  19450  13928  -1361   -873    757       O  
ATOM   3938  NE2 GLN B1093      61.877  -6.103  29.741  1.00122.58           N  
ANISOU 3938  NE2 GLN B1093    12838  19477  14260  -1219   -637    460       N  
ATOM   3939  N   LEU B1094      60.862  -1.954  35.355  1.00135.46           N  
ANISOU 3939  N   LEU B1094    15606  20908  14953  -1638   -695    330       N  
ATOM   3940  CA  LEU B1094      61.191  -1.587  36.727  1.00136.88           C  
ANISOU 3940  CA  LEU B1094    16077  21035  14898  -1728   -739    427       C  
ATOM   3941  C   LEU B1094      59.977  -1.725  37.633  1.00138.22           C  
ANISOU 3941  C   LEU B1094    16393  21115  15010  -1773   -473    256       C  
ATOM   3942  O   LEU B1094      60.097  -2.136  38.794  1.00139.66           O  
ANISOU 3942  O   LEU B1094    16806  21226  15034  -1838   -394    346       O  
ATOM   3943  CB  LEU B1094      61.705  -0.148  36.779  1.00136.62           C  
ANISOU 3943  CB  LEU B1094    16117  21041  14751  -1738   -991    452       C  
ATOM   3944  CG  LEU B1094      63.029   0.134  36.073  1.00135.58           C  
ANISOU 3944  CG  LEU B1094    15882  20981  14653  -1706  -1268    644       C  
ATOM   3945  CD1 LEU B1094      63.418   1.606  36.134  1.00135.41           C  
ANISOU 3945  CD1 LEU B1094    15926  20988  14536  -1715  -1496    645       C  
ATOM   3946  CD2 LEU B1094      64.094  -0.718  36.669  1.00136.26           C  
ANISOU 3946  CD2 LEU B1094    16071  21041  14660  -1748  -1340    887       C  
ATOM   3947  N   LYS B1095      58.798  -1.383  37.114  1.00140.03           N  
ANISOU 3947  N   LYS B1095    16493  21341  15370  -1735   -330      9       N  
ATOM   3948  CA  LYS B1095      57.577  -1.448  37.906  1.00142.19           C  
ANISOU 3948  CA  LYS B1095    16884  21524  15617  -1774    -65   -172       C  
ATOM   3949  C   LYS B1095      57.240  -2.873  38.322  1.00143.37           C  
ANISOU 3949  C   LYS B1095    17051  21596  15826  -1794    192   -146       C  
ATOM   3950  O   LYS B1095      56.676  -3.086  39.402  1.00144.88           O  
ANISOU 3950  O   LYS B1095    17443  21693  15913  -1851    390   -184       O  
ATOM   3951  CB  LYS B1095      56.438  -0.850  37.085  1.00142.31           C  
ANISOU 3951  CB  LYS B1095    16713  21554  15804  -1716     16   -445       C  
ATOM   3952  CG  LYS B1095      56.668   0.606  36.719  1.00142.16           C  
ANISOU 3952  CG  LYS B1095    16690  21602  15721  -1696   -218   -486       C  
ATOM   3953  CD  LYS B1095      55.435   1.237  36.105  1.00144.07           C  
ANISOU 3953  CD  LYS B1095    16791  21843  16107  -1646   -120   -771       C  
ATOM   3954  CE  LYS B1095      55.262   0.764  34.666  1.00145.43           C  
ANISOU 3954  CE  LYS B1095    16663  22069  16526  -1541   -127   -852       C  
ATOM   3955  NZ  LYS B1095      56.019   1.604  33.696  1.00146.59           N  
ANISOU 3955  NZ  LYS B1095    16701  22313  16681  -1476   -401   -791       N  
ATOM   3956  N   THR B1096      57.580  -3.860  37.490  1.00167.97           N  
ANISOU 3956  N   THR B1096    19966  24747  19108  -1745    201    -79       N  
ATOM   3957  CA  THR B1096      57.263  -5.247  37.820  1.00175.62           C  
ANISOU 3957  CA  THR B1096    20933  25642  20151  -1761    447    -55       C  
ATOM   3958  C   THR B1096      58.127  -5.761  38.966  1.00175.98           C  
ANISOU 3958  C   THR B1096    21239  25643  19983  -1830    423    182       C  
ATOM   3959  O   THR B1096      57.621  -6.409  39.889  1.00181.03           O  
ANISOU 3959  O   THR B1096    22036  26182  20564  -1875    658    169       O  
ATOM   3960  CB  THR B1096      57.429  -6.129  36.583  1.00175.68           C  
ANISOU 3960  CB  THR B1096    20655  25703  20393  -1685    443    -47       C  
ATOM   3961  OG1 THR B1096      56.572  -5.655  35.536  1.00193.97           O  
ANISOU 3961  OG1 THR B1096    22744  28052  22904  -1610    464   -281       O  
ATOM   3962  CG2 THR B1096      57.073  -7.573  36.905  1.00187.95           C  
ANISOU 3962  CG2 THR B1096    22196  27178  22039  -1701    702    -30       C  
ATOM   3963  N   THR B1097      59.432  -5.482  38.926  1.00142.36           N  
ANISOU 3963  N   THR B1097    17032  21449  15610  -1835    142    397       N  
ATOM   3964  CA  THR B1097      60.310  -5.900  40.014  1.00144.39           C  
ANISOU 3964  CA  THR B1097    17543  21661  15657  -1893     84    620       C  
ATOM   3965  C   THR B1097      60.075  -5.059  41.262  1.00145.82           C  
ANISOU 3965  C   THR B1097    18030  21777  15598  -1952     87    594       C  
ATOM   3966  O   THR B1097      60.309  -5.529  42.381  1.00147.42           O  
ANISOU 3966  O   THR B1097    18486  21901  15625  -1998    156    708       O  
ATOM   3967  CB  THR B1097      61.774  -5.824  39.587  1.00142.69           C  
ANISOU 3967  CB  THR B1097    17279  21524  15412  -1879   -227    848       C  
ATOM   3968  OG1 THR B1097      61.953  -6.549  38.365  1.00141.27           O  
ANISOU 3968  OG1 THR B1097    16812  21406  15458  -1816   -226    862       O  
ATOM   3969  CG2 THR B1097      62.668  -6.430  40.660  1.00144.00           C  
ANISOU 3969  CG2 THR B1097    17689  21637  15389  -1930   -281   1075       C  
ATOM   3970  N   ARG B1098      59.617  -3.817  41.085  1.00148.22           N  
ANISOU 3970  N   ARG B1098    18321  22109  15885  -1946     13    446       N  
ATOM   3971  CA  ARG B1098      59.276  -2.976  42.225  1.00151.45           C  
ANISOU 3971  CA  ARG B1098    19012  22455  16076  -1996     31    396       C  
ATOM   3972  C   ARG B1098      58.305  -3.688  43.155  1.00152.84           C  
ANISOU 3972  C   ARG B1098    19352  22510  16209  -2029    371    311       C  
ATOM   3973  O   ARG B1098      58.342  -3.482  44.374  1.00157.01           O  
ANISOU 3973  O   ARG B1098    20188  22962  16509  -2074    405    364       O  
ATOM   3974  CB  ARG B1098      58.651  -1.669  41.738  1.00151.47           C  
ANISOU 3974  CB  ARG B1098    18925  22502  16123  -1977    -35    201       C  
ATOM   3975  CG  ARG B1098      58.139  -0.764  42.846  1.00158.85           C  
ANISOU 3975  CG  ARG B1098    20132  23370  16852  -2025      9    117       C  
ATOM   3976  CD  ARG B1098      56.635  -0.906  43.001  1.00150.42           C  
ANISOU 3976  CD  ARG B1098    19043  22227  15882  -2027    342   -125       C  
ATOM   3977  NE  ARG B1098      55.882  -0.265  41.929  1.00152.49           N  
ANISOU 3977  NE  ARG B1098    19048  22546  16345  -1980    345   -339       N  
ATOM   3978  CZ  ARG B1098      54.656  -0.629  41.561  1.00154.59           C  
ANISOU 3978  CZ  ARG B1098    19163  22767  16805  -1957    609   -555       C  
ATOM   3979  NH1 ARG B1098      54.041  -1.632  42.176  1.00154.23           N  
ANISOU 3979  NH1 ARG B1098    19193  22618  16790  -1982    905   -582       N  
ATOM   3980  NH2 ARG B1098      54.044   0.005  40.572  1.00156.86           N  
ANISOU 3980  NH2 ARG B1098    19226  23108  17266  -1906    576   -746       N  
ATOM   3981  N   ASN B1099      57.426  -4.524  42.597  1.00150.56           N  
ANISOU 3981  N   ASN B1099    18868  22196  16143  -2003    628    177       N  
ATOM   3982  CA  ASN B1099      56.512  -5.304  43.423  1.00151.44           C  
ANISOU 3982  CA  ASN B1099    19112  22181  16247  -2032    974    102       C  
ATOM   3983  C   ASN B1099      57.269  -6.133  44.452  1.00156.00           C  
ANISOU 3983  C   ASN B1099    19948  22694  16631  -2068    994    328       C  
ATOM   3984  O   ASN B1099      56.760  -6.369  45.554  1.00157.97           O  
ANISOU 3984  O   ASN B1099    20449  22828  16744  -2102   1212    312       O  
ATOM   3985  CB  ASN B1099      55.664  -6.215  42.533  1.00151.71           C  
ANISOU 3985  CB  ASN B1099    18856  22202  16582  -1992   1208    -45       C  
ATOM   3986  CG  ASN B1099      54.781  -5.439  41.571  1.00149.15           C  
ANISOU 3986  CG  ASN B1099    18293  21925  16455  -1949   1212   -293       C  
ATOM   3987  OD1 ASN B1099      54.833  -4.211  41.517  1.00147.95           O  
ANISOU 3987  OD1 ASN B1099    18180  21821  16214  -1949   1036   -348       O  
ATOM   3988  ND2 ASN B1099      53.978  -6.158  40.794  1.00133.06           N  
ANISOU 3988  ND2 ASN B1099    16002  19868  14687  -1907   1403   -446       N  
ATOM   3989  N   ALA B1100      58.478  -6.584  44.113  1.00170.06           N  
ANISOU 3989  N   ALA B1100    21678  24540  18397  -2055    774    538       N  
ATOM   3990  CA  ALA B1100      59.278  -7.353  45.060  1.00170.91           C  
ANISOU 3990  CA  ALA B1100    22030  24589  18319  -2083    760    759       C  
ATOM   3991  C   ALA B1100      59.757  -6.498  46.229  1.00171.92           C  
ANISOU 3991  C   ALA B1100    22505  24678  18140  -2118    604    846       C  
ATOM   3992  O   ALA B1100      59.933  -7.014  47.338  1.00172.95           O  
ANISOU 3992  O   ALA B1100    22921  24712  18079  -2141    696    956       O  
ATOM   3993  CB  ALA B1100      60.474  -7.979  44.342  1.00145.39           C  
ANISOU 3993  CB  ALA B1100    18638  21440  15165  -2059    543    955       C  
ATOM   3994  N   TYR B1101      59.974  -5.199  46.004  1.00196.18           N  
ANISOU 3994  N   TYR B1101    25564  27816  21159  -2117    367    799       N  
ATOM   3995  CA  TYR B1101      60.504  -4.339  47.059  1.00209.15           C  
ANISOU 3995  CA  TYR B1101    27523  29425  22518  -2145    183    883       C  
ATOM   3996  C   TYR B1101      59.470  -4.093  48.151  1.00199.53           C  
ANISOU 3996  C   TYR B1101    26574  28091  21148  -2170    440    754       C  
ATOM   3997  O   TYR B1101      59.783  -4.171  49.345  1.00205.96           O  
ANISOU 3997  O   TYR B1101    27725  28819  21711  -2188    438    861       O  
ATOM   3998  CB  TYR B1101      60.974  -3.012  46.461  1.00231.29           C  
ANISOU 3998  CB  TYR B1101    30219  32330  25332  -2136   -129    858       C  
ATOM   3999  N   ILE B1102      58.229  -3.797  47.761  1.00174.68           N  
ANISOU 3999  N   ILE B1102    23288  24931  18151  -2166    665    522       N  
ATOM   4000  CA  ILE B1102      57.199  -3.453  48.737  1.00175.87           C  
ANISOU 4000  CA  ILE B1102    23675  24970  18176  -2190    914    384       C  
ATOM   4001  C   ILE B1102      56.860  -4.629  49.640  1.00174.46           C  
ANISOU 4001  C   ILE B1102    23701  24660  17925  -2201   1220    442       C  
ATOM   4002  O   ILE B1102      56.246  -4.438  50.696  1.00175.35           O  
ANISOU 4002  O   ILE B1102    24095  24660  17871  -2219   1412    387       O  
ATOM   4003  CB  ILE B1102      55.952  -2.902  48.023  1.00175.62           C  
ANISOU 4003  CB  ILE B1102    23416  24955  18358  -2180   1080    115       C  
ATOM   4004  CG1 ILE B1102      55.428  -3.882  46.973  1.00173.70           C  
ANISOU 4004  CG1 ILE B1102    22838  24733  18429  -2152   1265     28       C  
ATOM   4005  CG2 ILE B1102      56.277  -1.564  47.395  1.00173.34           C  
ANISOU 4005  CG2 ILE B1102    23013  24776  18071  -2170    777     62       C  
ATOM   4006  CD1 ILE B1102      54.118  -3.439  46.349  1.00170.27           C  
ANISOU 4006  CD1 ILE B1102    22192  24291  18211  -2137   1450   -250       C  
ATOM   4007  N   GLN B1103      57.239  -5.845  49.251  1.00190.10           N  
ANISOU 4007  N   GLN B1103    25553  26648  20029  -2189   1279    553       N  
ATOM   4008  CA  GLN B1103      57.043  -6.992  50.129  1.00213.33           C  
ANISOU 4008  CA  GLN B1103    28703  29463  22890  -2197   1552    634       C  
ATOM   4009  C   GLN B1103      57.943  -6.901  51.356  1.00206.82           C  
ANISOU 4009  C   GLN B1103    28275  28582  21725  -2205   1398    833       C  
ATOM   4010  O   GLN B1103      57.537  -7.286  52.459  1.00214.23           O  
ANISOU 4010  O   GLN B1103    29516  29387  22495  -2212   1631    850       O  
ATOM   4011  CB  GLN B1103      57.313  -8.288  49.365  1.00232.80           C  
ANISOU 4011  CB  GLN B1103    30924  31959  25571  -2180   1622    712       C  
ATOM   4012  N   LYS B1104      59.167  -6.394  51.188  1.00198.10           N  
ANISOU 4012  N   LYS B1104    27181  27568  20522  -2200   1007    983       N  
ATOM   4013  CA  LYS B1104      60.148  -6.465  52.265  1.00199.64           C  
ANISOU 4013  CA  LYS B1104    27725  27709  20420  -2199    829   1187       C  
ATOM   4014  C   LYS B1104      59.802  -5.522  53.413  1.00201.39           C  
ANISOU 4014  C   LYS B1104    28304  27846  20370  -2206    838   1130       C  
ATOM   4015  O   LYS B1104      59.842  -5.919  54.584  1.00203.50           O  
ANISOU 4015  O   LYS B1104    28925  27993  20402  -2199    950   1215       O  
ATOM   4016  CB  LYS B1104      61.539  -6.132  51.720  1.00198.33           C  
ANISOU 4016  CB  LYS B1104    27445  27657  20255  -2191    401   1349       C  
ATOM   4017  CG  LYS B1104      62.014  -7.026  50.583  1.00196.60           C  
ANISOU 4017  CG  LYS B1104    26887  27524  20290  -2178    361   1425       C  
ATOM   4018  CD  LYS B1104      61.933  -8.504  50.940  1.00197.59           C  
ANISOU 4018  CD  LYS B1104    27080  27566  20428  -2173    610   1517       C  
ATOM   4019  CE  LYS B1104      62.666  -8.822  52.236  1.00199.66           C  
ANISOU 4019  CE  LYS B1104    27740  27732  20389  -2170    530   1702       C  
ATOM   4020  NZ  LYS B1104      62.587 -10.270  52.574  1.00200.63           N  
ANISOU 4020  NZ  LYS B1104    27934  27773  20525  -2162    778   1795       N  
ATOM   4021  N   TYR B1105      59.460  -4.270  53.107  1.00186.96           N  
ANISOU 4021  N   TYR B1105    26399  26076  18562  -2216    724    988       N  
ATOM   4022  CA  TYR B1105      59.363  -3.260  54.155  1.00180.22           C  
ANISOU 4022  CA  TYR B1105    25882  25158  17434  -2220    652    958       C  
ATOM   4023  C   TYR B1105      58.061  -2.479  54.079  1.00181.28           C  
ANISOU 4023  C   TYR B1105    25968  25272  17638  -2234    871    714       C  
ATOM   4024  O   TYR B1105      57.524  -2.036  55.100  1.00172.09           O  
ANISOU 4024  O   TYR B1105    25111  24006  16269  -2236   1003    654       O  
ATOM   4025  CB  TYR B1105      60.546  -2.292  54.067  1.00178.84           C  
ANISOU 4025  CB  TYR B1105    25732  25070  17150  -2217    195   1066       C  
ATOM   4026  N   LEU B1106      57.558  -2.307  52.869  1.00205.26           N  
ANISOU 4026  N   LEU B1106    28626  28401  20963  -2237    906    571       N  
ATOM   4027  CA  LEU B1106      56.397  -1.480  52.648  1.00216.50           C  
ANISOU 4027  CA  LEU B1106    29961  29819  22479  -2248   1064    332       C  
ATOM   4028  C   LEU B1106      55.092  -2.260  52.787  1.00222.26           C  
ANISOU 4028  C   LEU B1106    30658  30442  23348  -2252   1521    184       C  
ATOM   4029  O   LEU B1106      54.149  -1.777  53.420  1.00193.52           O  
ANISOU 4029  O   LEU B1106    27180  26714  19637  -2263   1734     41       O  
ATOM   4030  CB  LEU B1106      56.501  -0.834  51.269  1.00224.82           C  
ANISOU 4030  CB  LEU B1106    30633  31020  23769  -2240    859    243       C  
ATOM   4031  CG  LEU B1106      55.328   0.099  51.048  1.00204.52           C  
ANISOU 4031  CG  LEU B1106    27977  28445  21286  -2246    995     -7       C  
ATOM   4032  CD1 LEU B1106      55.454   1.276  51.905  1.00215.34           C  
ANISOU 4032  CD1 LEU B1106    29629  29790  22400  -2260    845    -15       C  
ATOM   4033  CD2 LEU B1106      55.230   0.558  49.662  1.00195.44           C  
ANISOU 4033  CD2 LEU B1106    26447  27420  20392  -2228    863   -117       C  
ATOM   4034  N   LYS B  42      49.300 -22.018  54.019  1.00180.31           N  
ANISOU 4034  N   LYS B  42    19164  34688  14657   5298   -405    214       N  
ATOM   4035  CA  LYS B  42      47.953 -21.582  54.366  1.00176.66           C  
ANISOU 4035  CA  LYS B  42    18938  33967  14219   5202   -227    344       C  
ATOM   4036  C   LYS B  42      46.912 -22.516  53.756  1.00160.07           C  
ANISOU 4036  C   LYS B  42    17072  31414  12334   5344   -100    837       C  
ATOM   4037  O   LYS B  42      45.906 -22.067  53.206  1.00173.75           O  
ANISOU 4037  O   LYS B  42    18995  32791  14233   5145     47    861       O  
ATOM   4038  CB  LYS B  42      47.716 -20.147  53.892  1.00177.67           C  
ANISOU 4038  CB  LYS B  42    19120  33950  14437   4766   -157   -113       C  
ATOM   4039  N   HIS B  43      47.165 -23.818  53.855  1.00175.51           N  
ANISOU 4039  N   HIS B  43    19016  33365  14303   5683   -138   1229       N  
ATOM   4040  CA  HIS B  43      46.349 -24.825  53.191  1.00173.77           C  
ANISOU 4040  CA  HIS B  43    19007  32688  14329   5805    -30   1697       C  
ATOM   4041  C   HIS B  43      45.202 -25.246  54.102  1.00172.06           C  
ANISOU 4041  C   HIS B  43    18960  32335  14078   5964    145   2084       C  
ATOM   4042  O   HIS B  43      45.423 -25.596  55.267  1.00175.63           O  
ANISOU 4042  O   HIS B  43    19349  33065  14316   6203    139   2191       O  
ATOM   4043  CB  HIS B  43      47.196 -26.040  52.810  1.00172.99           C  
ANISOU 4043  CB  HIS B  43    18842  32575  14311   6071   -123   1922       C  
ATOM   4044  N   LEU B  44      43.983 -25.212  53.571  1.00159.51           N  
ANISOU 4044  N   LEU B  44    17581  30326  12700   5829    307   2290       N  
ATOM   4045  CA  LEU B  44      42.803 -25.659  54.296  1.00153.48           C  
ANISOU 4045  CA  LEU B  44    16983  29371  11961   5951    495   2678       C  
ATOM   4046  C   LEU B  44      42.356 -27.016  53.767  1.00163.32           C  
ANISOU 4046  C   LEU B  44    18379  30207  13468   6112    583   3165       C  
ATOM   4047  O   LEU B  44      42.310 -27.237  52.553  1.00163.29           O  
ANISOU 4047  O   LEU B  44    18438  29893  13713   5985    565   3210       O  
ATOM   4048  CB  LEU B  44      41.658 -24.653  54.159  1.00159.49           C  
ANISOU 4048  CB  LEU B  44    17865  29939  12796   5676    653   2577       C  
ATOM   4049  CG  LEU B  44      41.962 -23.194  54.503  1.00155.93           C  
ANISOU 4049  CG  LEU B  44    17318  29765  12163   5441    614   2062       C  
ATOM   4050  CD1 LEU B  44      40.700 -22.351  54.387  1.00130.02           C  
ANISOU 4050  CD1 LEU B  44    14188  26214   8999   5213    820   2037       C  
ATOM   4051  CD2 LEU B  44      42.568 -23.068  55.891  1.00151.19           C  
ANISOU 4051  CD2 LEU B  44    16589  29612  11244   5611    530   1949       C  
ATOM   4052  N   ASP B  45      42.026 -27.922  54.688  1.00157.68           N  
ANISOU 4052  N   ASP B  45    17735  29474  12703   6378    687   3517       N  
ATOM   4053  CA  ASP B  45      41.494 -29.225  54.311  1.00172.12           C  
ANISOU 4053  CA  ASP B  45    19735  30869  14794   6504    818   3975       C  
ATOM   4054  C   ASP B  45      40.077 -29.144  53.761  1.00162.08           C  
ANISOU 4054  C   ASP B  45    18641  29148  13795   6287    999   4186       C  
ATOM   4055  O   ASP B  45      39.606 -30.118  53.164  1.00162.50           O  
ANISOU 4055  O   ASP B  45    18835  28779  14128   6297   1101   4514       O  
ATOM   4056  CB  ASP B  45      41.522 -30.169  55.516  1.00153.35           C  
ANISOU 4056  CB  ASP B  45    17394  28600  12270   6838    908   4262       C  
ATOM   4057  N   ALA B  46      39.391 -28.014  53.946  1.00152.52           N  
ANISOU 4057  N   ALA B  46    17424  28008  12518   6081   1056   3997       N  
ATOM   4058  CA  ALA B  46      37.990 -27.922  53.550  1.00150.39           C  
ANISOU 4058  CA  ALA B  46    17299  27347  12495   5893   1252   4209       C  
ATOM   4059  C   ALA B  46      37.836 -27.892  52.033  1.00147.95           C  
ANISOU 4059  C   ALA B  46    17020  26603  12591   5612   1226   4135       C  
ATOM   4060  O   ALA B  46      37.006 -28.617  51.472  1.00145.89           O  
ANISOU 4060  O   ALA B  46    16879  25894  12658   5533   1351   4437       O  
ATOM   4061  CB  ALA B  46      37.354 -26.679  54.177  1.00150.33           C  
ANISOU 4061  CB  ALA B  46    17269  27515  12335   5751   1335   3987       C  
ATOM   4062  N   ILE B  47      38.629 -27.060  51.352  1.00158.71           N  
ANISOU 4062  N   ILE B  47    18265  28040  13996   5421   1070   3695       N  
ATOM   4063  CA  ILE B  47      38.437 -26.853  49.914  1.00157.08           C  
ANISOU 4063  CA  ILE B  47    18082  27372  14229   5105   1052   3546       C  
ATOM   4064  C   ILE B  47      38.350 -28.176  49.155  1.00155.27           C  
ANISOU 4064  C   ILE B  47    17958  26738  14299   5156   1071   3887       C  
ATOM   4065  O   ILE B  47      37.382 -28.369  48.408  1.00150.89           O  
ANISOU 4065  O   ILE B  47    17500  25731  14100   4948   1180   4031       O  
ATOM   4066  CB  ILE B  47      39.521 -25.921  49.361  1.00159.70           C  
ANISOU 4066  CB  ILE B  47    18278  27880  14520   4946    879   3041       C  
ATOM   4067  CG1 ILE B  47      39.163 -24.454  49.629  1.00160.03           C  
ANISOU 4067  CG1 ILE B  47    18285  28065  14455   4734    934   2683       C  
ATOM   4068  CG2 ILE B  47      39.727 -26.152  47.866  1.00158.75           C  
ANISOU 4068  CG2 ILE B  47    18186  27319  14813   4734    819   2958       C  
ATOM   4069  CD1 ILE B  47      39.776 -23.894  50.891  1.00150.64           C  
ANISOU 4069  CD1 ILE B  47    16996  27461  12778   4895    882   2493       C  
ATOM   4070  N   PRO B  48      39.303 -29.104  49.282  1.00157.35           N  
ANISOU 4070  N   PRO B  48    18211  27138  14438   5420    977   4023       N  
ATOM   4071  CA  PRO B  48      39.153 -30.384  48.568  1.00156.06           C  
ANISOU 4071  CA  PRO B  48    18187  26547  14562   5463   1033   4361       C  
ATOM   4072  C   PRO B  48      37.848 -31.094  48.886  1.00153.91           C  
ANISOU 4072  C   PRO B  48    18078  25982  14420   5474   1254   4791       C  
ATOM   4073  O   PRO B  48      37.255 -31.723  48.001  1.00153.90           O  
ANISOU 4073  O   PRO B  48    18195  25499  14779   5306   1336   4968       O  
ATOM   4074  CB  PRO B  48      40.374 -31.190  49.036  1.00162.63           C  
ANISOU 4074  CB  PRO B  48    18980  27692  15122   5834    927   4467       C  
ATOM   4075  CG  PRO B  48      41.377 -30.159  49.437  1.00162.02           C  
ANISOU 4075  CG  PRO B  48    18691  28134  14735   5857    746   4040       C  
ATOM   4076  CD  PRO B  48      40.580 -29.023  50.014  1.00162.03           C  
ANISOU 4076  CD  PRO B  48    18662  28274  14629   5683    818   3864       C  
ATOM   4077  N   ILE B  49      37.383 -31.010  50.134  1.00137.91           N  
ANISOU 4077  N   ILE B  49    16060  24239  12101   5658   1358   4957       N  
ATOM   4078  CA  ILE B  49      36.103 -31.611  50.494  1.00138.78           C  
ANISOU 4078  CA  ILE B  49    16312  24090  12327   5655   1588   5353       C  
ATOM   4079  C   ILE B  49      34.961 -30.882  49.795  1.00135.86           C  
ANISOU 4079  C   ILE B  49    15935  23402  12285   5275   1671   5242       C  
ATOM   4080  O   ILE B  49      34.054 -31.506  49.232  1.00135.08           O  
ANISOU 4080  O   ILE B  49    15938  22882  12504   5119   1802   5488       O  
ATOM   4081  CB  ILE B  49      35.920 -31.608  52.022  1.00142.17           C  
ANISOU 4081  CB  ILE B  49    16727  24844  12448   5892   1679   5445       C  
ATOM   4082  N   LEU B  50      34.988 -29.547  49.824  1.00130.25           N  
ANISOU 4082  N   LEU B  50    15104  22895  11492   5122   1602   4867       N  
ATOM   4083  CA  LEU B  50      33.912 -28.772  49.216  1.00127.35           C  
ANISOU 4083  CA  LEU B  50    14724  22262  11400   4801   1688   4762       C  
ATOM   4084  C   LEU B  50      33.826 -29.024  47.715  1.00126.23           C  
ANISOU 4084  C   LEU B  50    14611  21665  11685   4533   1632   4702       C  
ATOM   4085  O   LEU B  50      32.729 -29.169  47.165  1.00125.32           O  
ANISOU 4085  O   LEU B  50    14540  21207  11869   4327   1746   4855       O  
ATOM   4086  CB  LEU B  50      34.124 -27.283  49.491  1.00133.14           C  
ANISOU 4086  CB  LEU B  50    15349  23295  11945   4709   1632   4346       C  
ATOM   4087  CG  LEU B  50      33.658 -26.723  50.837  1.00147.68           C  
ANISOU 4087  CG  LEU B  50    17179  25486  13447   4854   1752   4387       C  
ATOM   4088  CD1 LEU B  50      34.305 -27.435  52.013  1.00133.90           C  
ANISOU 4088  CD1 LEU B  50    15450  24110  11317   5216   1731   4581       C  
ATOM   4089  CD2 LEU B  50      33.952 -25.228  50.898  1.00149.92           C  
ANISOU 4089  CD2 LEU B  50    17380  26002  13582   4715   1699   3926       C  
ATOM   4090  N   TYR B  51      34.974 -29.079  47.036  1.00121.93           N  
ANISOU 4090  N   TYR B  51    14035  21123  11168   4531   1455   4477       N  
ATOM   4091  CA  TYR B  51      34.970 -29.298  45.590  1.00118.83           C  
ANISOU 4091  CA  TYR B  51    13683  20304  11162   4282   1396   4400       C  
ATOM   4092  C   TYR B  51      34.267 -30.601  45.234  1.00118.76           C  
ANISOU 4092  C   TYR B  51    13815  19903  11405   4261   1517   4810       C  
ATOM   4093  O   TYR B  51      33.492 -30.652  44.273  1.00118.41           O  
ANISOU 4093  O   TYR B  51    13808  19480  11701   3989   1558   4837       O  
ATOM   4094  CB  TYR B  51      36.409 -29.295  45.071  1.00122.94           C  
ANISOU 4094  CB  TYR B  51    14154  20925  11630   4340   1204   4135       C  
ATOM   4095  CG  TYR B  51      36.942 -27.910  44.779  1.00120.36           C  
ANISOU 4095  CG  TYR B  51    13707  20787  11239   4184   1091   3653       C  
ATOM   4096  CD1 TYR B  51      36.685 -26.855  45.646  1.00119.50           C  
ANISOU 4096  CD1 TYR B  51    13524  21001  10879   4192   1135   3481       C  
ATOM   4097  CD2 TYR B  51      37.739 -27.665  43.670  1.00121.85           C  
ANISOU 4097  CD2 TYR B  51    13870  20828  11598   4034    958   3366       C  
ATOM   4098  CE1 TYR B  51      37.174 -25.588  45.395  1.00118.85           C  
ANISOU 4098  CE1 TYR B  51    13356  21071  10730   4038   1061   3033       C  
ATOM   4099  CE2 TYR B  51      38.240 -26.402  43.415  1.00117.50           C  
ANISOU 4099  CE2 TYR B  51    13224  20435  10984   3884    880   2921       C  
ATOM   4100  CZ  TYR B  51      37.955 -25.368  44.282  1.00116.07           C  
ANISOU 4100  CZ  TYR B  51    12981  20561  10559   3882    936   2755       C  
ATOM   4101  OH  TYR B  51      38.450 -24.108  44.035  1.00115.40           O  
ANISOU 4101  OH  TYR B  51    12827  20612  10407   3719    886   2305       O  
ATOM   4102  N   TYR B  52      34.519 -31.665  46.001  1.00119.22           N  
ANISOU 4102  N   TYR B  52    13958  20049  11293   4543   1584   5131       N  
ATOM   4103  CA  TYR B  52      33.864 -32.938  45.723  1.00119.87           C  
ANISOU 4103  CA  TYR B  52    14201  19746  11600   4519   1733   5523       C  
ATOM   4104  C   TYR B  52      32.365 -32.851  45.983  1.00119.18           C  
ANISOU 4104  C   TYR B  52    14127  19514  11643   4355   1922   5728       C  
ATOM   4105  O   TYR B  52      31.570 -33.480  45.275  1.00115.26           O  
ANISOU 4105  O   TYR B  52    13713  18619  11460   4142   2019   5910       O  
ATOM   4106  CB  TYR B  52      34.494 -34.050  46.563  1.00122.47           C  
ANISOU 4106  CB  TYR B  52    14635  20214  11683   4892   1789   5826       C  
ATOM   4107  CG  TYR B  52      35.682 -34.719  45.906  1.00124.76           C  
ANISOU 4107  CG  TYR B  52    14981  20411  12012   5006   1668   5781       C  
ATOM   4108  CD1 TYR B  52      36.946 -34.147  45.956  1.00126.14           C  
ANISOU 4108  CD1 TYR B  52    15022  20933  11973   5146   1468   5472       C  
ATOM   4109  CD2 TYR B  52      35.537 -35.928  45.237  1.00124.08           C  
ANISOU 4109  CD2 TYR B  52    15082  19889  12172   4966   1767   6045       C  
ATOM   4110  CE1 TYR B  52      38.033 -34.758  45.354  1.00128.13           C  
ANISOU 4110  CE1 TYR B  52    15309  21111  12261   5262   1366   5439       C  
ATOM   4111  CE2 TYR B  52      36.617 -36.547  44.633  1.00125.09           C  
ANISOU 4111  CE2 TYR B  52    15274  19920  12335   5085   1676   6014       C  
ATOM   4112  CZ  TYR B  52      37.862 -35.958  44.695  1.00129.53           C  
ANISOU 4112  CZ  TYR B  52    15686  20844  12687   5243   1474   5716       C  
ATOM   4113  OH  TYR B  52      38.940 -36.570  44.095  1.00119.90           O  
ANISOU 4113  OH  TYR B  52    14514  19540  11502   5373   1391   5692       O  
ATOM   4114  N   ILE B  53      31.959 -32.082  46.995  1.00131.67           N  
ANISOU 4114  N   ILE B  53    15624  21422  12984   4445   1982   5697       N  
ATOM   4115  CA  ILE B  53      30.534 -31.878  47.239  1.00131.84           C  
ANISOU 4115  CA  ILE B  53    15631  21335  13127   4291   2164   5869       C  
ATOM   4116  C   ILE B  53      29.876 -31.276  46.004  1.00131.46           C  
ANISOU 4116  C   ILE B  53    15518  20996  13436   3924   2123   5680       C  
ATOM   4117  O   ILE B  53      28.869 -31.787  45.500  1.00130.49           O  
ANISOU 4117  O   ILE B  53    15429  20557  13595   3721   2236   5886       O  
ATOM   4118  CB  ILE B  53      30.320 -30.992  48.480  1.00133.22           C  
ANISOU 4118  CB  ILE B  53    15726  21926  12967   4452   2223   5809       C  
ATOM   4119  CG1 ILE B  53      30.692 -31.758  49.751  1.00136.79           C  
ANISOU 4119  CG1 ILE B  53    16261  22632  13080   4816   2307   6087       C  
ATOM   4120  CG2 ILE B  53      28.877 -30.504  48.541  1.00132.82           C  
ANISOU 4120  CG2 ILE B  53    15624  21769  13071   4258   2391   5903       C  
ATOM   4121  CD1 ILE B  53      30.726 -30.899  51.001  1.00138.38           C  
ANISOU 4121  CD1 ILE B  53    16393  23290  12893   5004   2333   5991       C  
ATOM   4122  N   ILE B  54      30.441 -30.177  45.499  1.00133.54           N  
ANISOU 4122  N   ILE B  54    15687  21370  13683   3832   1964   5281       N  
ATOM   4123  CA  ILE B  54      29.900 -29.547  44.299  1.00135.63           C  
ANISOU 4123  CA  ILE B  54    15899  21372  14260   3513   1918   5088       C  
ATOM   4124  C   ILE B  54      29.962 -30.507  43.119  1.00132.00           C  
ANISOU 4124  C   ILE B  54    15531  20502  14122   3344   1870   5183       C  
ATOM   4125  O   ILE B  54      29.070 -30.519  42.262  1.00133.44           O  
ANISOU 4125  O   ILE B  54    15702  20399  14602   3079   1904   5221       O  
ATOM   4126  CB  ILE B  54      30.655 -28.238  43.999  1.00137.42           C  
ANISOU 4126  CB  ILE B  54    16043  21787  14384   3471   1772   4637       C  
ATOM   4127  CG1 ILE B  54      30.369 -27.189  45.079  1.00132.67           C  
ANISOU 4127  CG1 ILE B  54    15367  21543  13497   3578   1853   4532       C  
ATOM   4128  CG2 ILE B  54      30.293 -27.716  42.614  1.00140.38           C  
ANISOU 4128  CG2 ILE B  54    16396  21857  15086   3169   1710   4440       C  
ATOM   4129  CD1 ILE B  54      28.918 -26.748  45.162  1.00131.04           C  
ANISOU 4129  CD1 ILE B  54    15119  21249  13422   3447   2022   4667       C  
ATOM   4130  N   PHE B  55      31.014 -31.325  43.053  1.00128.44           N  
ANISOU 4130  N   PHE B  55    15171  20025  13605   3497   1793   5221       N  
ATOM   4131  CA  PHE B  55      31.172 -32.234  41.923  1.00126.13           C  
ANISOU 4131  CA  PHE B  55    14990  19334  13601   3346   1755   5291       C  
ATOM   4132  C   PHE B  55      29.983 -33.178  41.809  1.00119.98           C  
ANISOU 4132  C   PHE B  55    14295  18250  13044   3199   1932   5648       C  
ATOM   4133  O   PHE B  55      29.285 -33.203  40.789  1.00120.91           O  
ANISOU 4133  O   PHE B  55    14409  18066  13465   2900   1928   5625       O  
ATOM   4134  CB  PHE B  55      32.463 -33.037  42.064  1.00122.13           C  
ANISOU 4134  CB  PHE B  55    14577  18877  12950   3594   1683   5329       C  
ATOM   4135  CG  PHE B  55      32.495 -34.270  41.208  1.00120.20           C  
ANISOU 4135  CG  PHE B  55    14500  18209  12960   3500   1720   5521       C  
ATOM   4136  CD1 PHE B  55      32.597 -34.170  39.830  1.00115.78           C  
ANISOU 4136  CD1 PHE B  55    13966  17338  12688   3234   1616   5327       C  
ATOM   4137  CD2 PHE B  55      32.396 -35.528  41.778  1.00119.89           C  
ANISOU 4137  CD2 PHE B  55    14615  18068  12869   3673   1876   5898       C  
ATOM   4138  CE1 PHE B  55      32.618 -35.302  39.038  1.00114.02           C  
ANISOU 4138  CE1 PHE B  55    13915  16716  12690   3133   1659   5494       C  
ATOM   4139  CE2 PHE B  55      32.415 -36.664  40.991  1.00119.61           C  
ANISOU 4139  CE2 PHE B  55    14763  17620  13065   3574   1935   6069       C  
ATOM   4140  CZ  PHE B  55      32.525 -36.550  39.619  1.00117.03           C  
ANISOU 4140  CZ  PHE B  55    14456  16990  13020   3297   1824   5861       C  
ATOM   4141  N   VAL B  56      29.726 -33.957  42.860  1.00123.56           N  
ANISOU 4141  N   VAL B  56    14821  18787  13338   3401   2095   5978       N  
ATOM   4142  CA  VAL B  56      28.667 -34.957  42.793  1.00121.85           C  
ANISOU 4142  CA  VAL B  56    14701  18271  13326   3257   2288   6324       C  
ATOM   4143  C   VAL B  56      27.303 -34.284  42.722  1.00119.89           C  
ANISOU 4143  C   VAL B  56    14313  18016  13225   3015   2370   6331       C  
ATOM   4144  O   VAL B  56      26.444 -34.676  41.923  1.00114.10           O  
ANISOU 4144  O   VAL B  56    13586  16979  12789   2723   2423   6420       O  
ATOM   4145  CB  VAL B  56      28.767 -35.915  43.994  1.00109.12           C  
ANISOU 4145  CB  VAL B  56    13217  16758  11484   3558   2464   6676       C  
ATOM   4146  CG1 VAL B  56      27.654 -36.951  43.950  1.00102.07           C  
ANISOU 4146  CG1 VAL B  56    12436  15543  10804   3388   2694   7029       C  
ATOM   4147  CG2 VAL B  56      30.128 -36.594  44.016  1.00106.95           C  
ANISOU 4147  CG2 VAL B  56    13073  16502  11061   3824   2383   6682       C  
ATOM   4148  N   ILE B  57      27.083 -33.256  43.543  1.00113.77           N  
ANISOU 4148  N   ILE B  57    13406  17585  12238   3132   2383   6232       N  
ATOM   4149  CA  ILE B  57      25.811 -32.539  43.507  1.00109.80           C  
ANISOU 4149  CA  ILE B  57    12760  17103  11857   2938   2469   6237       C  
ATOM   4150  C   ILE B  57      25.547 -32.012  42.102  1.00110.38           C  
ANISOU 4150  C   ILE B  57    12759  16956  12225   2629   2337   6000       C  
ATOM   4151  O   ILE B  57      24.460 -32.199  41.542  1.00110.39           O  
ANISOU 4151  O   ILE B  57    12703  16761  12479   2376   2408   6116       O  
ATOM   4152  CB  ILE B  57      25.804 -31.405  44.547  1.00110.18           C  
ANISOU 4152  CB  ILE B  57    12701  17554  11607   3131   2492   6113       C  
ATOM   4153  CG1 ILE B  57      25.790 -31.977  45.969  1.00112.73           C  
ANISOU 4153  CG1 ILE B  57    13095  18086  11650   3417   2655   6400       C  
ATOM   4154  CG2 ILE B  57      24.609 -30.488  44.327  1.00114.89           C  
ANISOU 4154  CG2 ILE B  57    13145  18167  12340   2939   2560   6060       C  
ATOM   4155  CD1 ILE B  57      24.495 -32.671  46.359  1.00120.90           C  
ANISOU 4155  CD1 ILE B  57    14140  18986  12812   3329   2896   6769       C  
ATOM   4156  N   GLY B  58      26.542 -31.351  41.508  1.00127.95           N  
ANISOU 4156  N   GLY B  58    14980  19222  14414   2644   2145   5665       N  
ATOM   4157  CA  GLY B  58      26.370 -30.834  40.161  1.00128.30           C  
ANISOU 4157  CA  GLY B  58    14975  19056  14717   2375   2021   5434       C  
ATOM   4158  C   GLY B  58      26.249 -31.931  39.122  1.00116.90           C  
ANISOU 4158  C   GLY B  58    13637  17221  13560   2159   1999   5555       C  
ATOM   4159  O   GLY B  58      25.433 -31.839  38.200  1.00108.72           O  
ANISOU 4159  O   GLY B  58    12544  15986  12780   1885   1984   5538       O  
ATOM   4160  N   PHE B  59      27.056 -32.985  39.252  1.00100.68           N  
ANISOU 4160  N   PHE B  59    11741  15056  11457   2285   2002   5679       N  
ATOM   4161  CA  PHE B  59      26.993 -34.084  38.297  1.00102.17           C  
ANISOU 4161  CA  PHE B  59    12067  14850  11903   2085   2004   5795       C  
ATOM   4162  C   PHE B  59      25.676 -34.839  38.393  1.00110.36           C  
ANISOU 4162  C   PHE B  59    13105  15715  13112   1890   2189   6107       C  
ATOM   4163  O   PHE B  59      25.267 -35.476  37.417  1.00112.60           O  
ANISOU 4163  O   PHE B  59    13451  15674  13658   1615   2188   6151       O  
ATOM   4164  CB  PHE B  59      28.162 -35.043  38.517  1.00108.46           C  
ANISOU 4164  CB  PHE B  59    13048  15577  12584   2307   1998   5881       C  
ATOM   4165  CG  PHE B  59      28.737 -35.596  37.245  1.00105.12           C  
ANISOU 4165  CG  PHE B  59    12757  14809  12375   2147   1895   5773       C  
ATOM   4166  CD1 PHE B  59      29.753 -34.925  36.583  1.00108.09           C  
ANISOU 4166  CD1 PHE B  59    13111  15227  12732   2177   1702   5442       C  
ATOM   4167  CD2 PHE B  59      28.265 -36.783  36.711  1.00 99.75           C  
ANISOU 4167  CD2 PHE B  59    12233  13755  11912   1958   2003   5995       C  
ATOM   4168  CE1 PHE B  59      30.288 -35.427  35.411  1.00109.62           C  
ANISOU 4168  CE1 PHE B  59    13435  15098  13118   2037   1616   5345       C  
ATOM   4169  CE2 PHE B  59      28.797 -37.290  35.539  1.00109.80           C  
ANISOU 4169  CE2 PHE B  59    13646  14701  13372   1809   1917   5891       C  
ATOM   4170  CZ  PHE B  59      29.809 -36.611  34.888  1.00109.53           C  
ANISOU 4170  CZ  PHE B  59    13587  14714  13315   1858   1722   5570       C  
ATOM   4171  N   LEU B  60      25.007 -34.782  39.547  1.00115.77           N  
ANISOU 4171  N   LEU B  60    13722  16615  13650   2016   2354   6316       N  
ATOM   4172  CA  LEU B  60      23.723 -35.452  39.707  1.00109.71           C  
ANISOU 4172  CA  LEU B  60    12933  15711  13040   1825   2549   6610       C  
ATOM   4173  C   LEU B  60      22.600 -34.661  39.046  1.00112.24           C  
ANISOU 4173  C   LEU B  60    13046  16042  13559   1544   2514   6507       C  
ATOM   4174  O   LEU B  60      21.805 -35.216  38.280  1.00112.76           O  
ANISOU 4174  O   LEU B  60    13096  15863  13883   1237   2550   6597       O  
ATOM   4175  CB  LEU B  60      23.428 -35.654  41.195  1.00104.59           C  
ANISOU 4175  CB  LEU B  60    12290  15296  12154   2077   2749   6872       C  
ATOM   4176  CG  LEU B  60      23.714 -37.039  41.780  1.00108.01           C  
ANISOU 4176  CG  LEU B  60    12947  15571  12522   2215   2922   7186       C  
ATOM   4177  CD1 LEU B  60      25.155 -37.457  41.548  1.00112.63           C  
ANISOU 4177  CD1 LEU B  60    13705  16088  12999   2417   2798   7087       C  
ATOM   4178  CD2 LEU B  60      23.391 -37.046  43.269  1.00103.14           C  
ANISOU 4178  CD2 LEU B  60    12319  15225  11644   2481   3113   7421       C  
ATOM   4179  N   VAL B  61      22.513 -33.361  39.338  1.00102.72           N  
ANISOU 4179  N   VAL B  61    11679  15125  12225   1647   2452   6319       N  
ATOM   4180  CA  VAL B  61      21.460 -32.547  38.740  1.00101.85           C  
ANISOU 4180  CA  VAL B  61    11370  15048  12280   1428   2429   6232       C  
ATOM   4181  C   VAL B  61      21.646 -32.426  37.231  1.00104.58           C  
ANISOU 4181  C   VAL B  61    11724  15156  12857   1181   2242   6008       C  
ATOM   4182  O   VAL B  61      20.663 -32.345  36.486  1.00111.01           O  
ANISOU 4182  O   VAL B  61    12413  15878  13886    918   2235   6026       O  
ATOM   4183  CB  VAL B  61      21.406 -31.161  39.412  1.00 98.21           C  
ANISOU 4183  CB  VAL B  61    10774  14932  11610   1623   2429   6075       C  
ATOM   4184  CG1 VAL B  61      20.971 -31.295  40.863  1.00 97.98           C  
ANISOU 4184  CG1 VAL B  61    10723  15132  11374   1828   2635   6324       C  
ATOM   4185  CG2 VAL B  61      22.756 -30.458  39.319  1.00105.15           C  
ANISOU 4185  CG2 VAL B  61    11731  15909  12312   1803   2262   5759       C  
ATOM   4186  N   ASN B  62      22.893 -32.417  36.751  1.00111.59           N  
ANISOU 4186  N   ASN B  62    12749  15951  13699   1261   2089   5795       N  
ATOM   4187  CA  ASN B  62      23.131 -32.249  35.321  1.00111.84           C  
ANISOU 4187  CA  ASN B  62    12805  15756  13933   1044   1916   5569       C  
ATOM   4188  C   ASN B  62      22.947 -33.546  34.543  1.00112.87           C  
ANISOU 4188  C   ASN B  62    13064  15529  14291    797   1930   5715       C  
ATOM   4189  O   ASN B  62      22.542 -33.506  33.376  1.00111.93           O  
ANISOU 4189  O   ASN B  62    12914  15228  14388    528   1834   5613       O  
ATOM   4190  CB  ASN B  62      24.533 -31.687  35.083  1.00110.32           C  
ANISOU 4190  CB  ASN B  62    12703  15605  13609   1215   1759   5271       C  
ATOM   4191  CG  ASN B  62      24.607 -30.189  35.318  1.00109.42           C  
ANISOU 4191  CG  ASN B  62    12461  15767  13349   1334   1711   5024       C  
ATOM   4192  OD1 ASN B  62      24.312 -29.395  34.425  1.00105.12           O  
ANISOU 4192  OD1 ASN B  62    11844  15173  12922   1191   1624   4830       O  
ATOM   4193  ND2 ASN B  62      25.000 -29.796  36.524  1.00111.30           N  
ANISOU 4193  ND2 ASN B  62    12681  16292  13317   1598   1778   5030       N  
ATOM   4194  N   ILE B  63      23.233 -34.698  35.156  1.00118.96           N  
ANISOU 4194  N   ILE B  63    13993  16193  15012    884   2058   5952       N  
ATOM   4195  CA  ILE B  63      22.928 -35.965  34.500  1.00119.83           C  
ANISOU 4195  CA  ILE B  63    14244  15948  15337    630   2120   6112       C  
ATOM   4196  C   ILE B  63      21.427 -36.213  34.462  1.00121.11           C  
ANISOU 4196  C   ILE B  63    14259  16089  15668    352   2246   6302       C  
ATOM   4197  O   ILE B  63      20.957 -37.034  33.666  1.00121.82           O  
ANISOU 4197  O   ILE B  63    14412  15898  15975     44   2268   6368       O  
ATOM   4198  CB  ILE B  63      23.680 -37.124  35.188  1.00120.81           C  
ANISOU 4198  CB  ILE B  63    14605  15950  15347    827   2251   6322       C  
ATOM   4199  CG1 ILE B  63      23.752 -38.345  34.261  1.00123.59           C  
ANISOU 4199  CG1 ILE B  63    15168  15877  15914    582   2283   6396       C  
ATOM   4200  CG2 ILE B  63      23.045 -37.483  36.524  1.00121.17           C  
ANISOU 4200  CG2 ILE B  63    14620  16160  15258    968   2479   6627       C  
ATOM   4201  CD1 ILE B  63      24.663 -38.173  33.065  1.00127.29           C  
ANISOU 4201  CD1 ILE B  63    15733  16161  16471    518   2079   6119       C  
ATOM   4202  N   VAL B  64      20.658 -35.520  35.303  1.00120.34           N  
ANISOU 4202  N   VAL B  64    13963  16289  15472    444   2334   6384       N  
ATOM   4203  CA  VAL B  64      19.204 -35.589  35.213  1.00121.44           C  
ANISOU 4203  CA  VAL B  64    13911  16459  15773    182   2438   6537       C  
ATOM   4204  C   VAL B  64      18.697 -34.741  34.053  1.00122.23           C  
ANISOU 4204  C   VAL B  64    13831  16579  16031    -36   2261   6314       C  
ATOM   4205  O   VAL B  64      17.748 -35.121  33.358  1.00122.14           O  
ANISOU 4205  O   VAL B  64    13718  16459  16230   -359   2269   6377       O  
ATOM   4206  CB  VAL B  64      18.574 -35.154  36.551  1.00123.09           C  
ANISOU 4206  CB  VAL B  64    13976  16981  15813    382   2613   6716       C  
ATOM   4207  CG1 VAL B  64      17.108 -34.786  36.363  1.00124.08           C  
ANISOU 4207  CG1 VAL B  64    13830  17226  16088    151   2674   6797       C  
ATOM   4208  CG2 VAL B  64      18.725 -36.254  37.592  1.00125.95           C  
ANISOU 4208  CG2 VAL B  64    14511  17273  16070    514   2831   7008       C  
ATOM   4209  N   VAL B  65      19.321 -33.583  33.823  1.00131.27           N  
ANISOU 4209  N   VAL B  65    14937  17869  17070    136   2104   6048       N  
ATOM   4210  CA  VAL B  65      18.883 -32.697  32.748  1.00135.78           C  
ANISOU 4210  CA  VAL B  65    15357  18468  17765    -24   1948   5839       C  
ATOM   4211  C   VAL B  65      19.015 -33.388  31.397  1.00133.94           C  
ANISOU 4211  C   VAL B  65    15232  17912  17749   -322   1820   5751       C  
ATOM   4212  O   VAL B  65      18.109 -33.320  30.558  1.00138.33           O  
ANISOU 4212  O   VAL B  65    15643  18437  18478   -590   1764   5738       O  
ATOM   4213  CB  VAL B  65      19.680 -31.379  32.785  1.00145.36           C  
ANISOU 4213  CB  VAL B  65    16565  19856  18810    227   1834   5562       C  
ATOM   4214  CG1 VAL B  65      19.392 -30.545  31.544  1.00151.23           C  
ANISOU 4214  CG1 VAL B  65    17211  20568  19681     76   1673   5337       C  
ATOM   4215  CG2 VAL B  65      19.348 -30.595  34.041  1.00138.26           C  
ANISOU 4215  CG2 VAL B  65    15541  19288  17705    479   1968   5636       C  
ATOM   4216  N   VAL B  66      20.140 -34.066  31.165  1.00116.52           N  
ANISOU 4216  N   VAL B  66    13277  15470  15527   -274   1774   5690       N  
ATOM   4217  CA  VAL B  66      20.374 -34.676  29.862  1.00113.84           C  
ANISOU 4217  CA  VAL B  66    13070  14808  15376   -539   1655   5583       C  
ATOM   4218  C   VAL B  66      19.415 -35.836  29.633  1.00115.76           C  
ANISOU 4218  C   VAL B  66    13315  14865  15803   -869   1769   5805       C  
ATOM   4219  O   VAL B  66      18.935 -36.050  28.513  1.00118.31           O  
ANISOU 4219  O   VAL B  66    13611  15032  16308  -1182   1674   5729       O  
ATOM   4220  CB  VAL B  66      21.842 -35.126  29.736  1.00109.36           C  
ANISOU 4220  CB  VAL B  66    12775  14042  14737   -378   1601   5477       C  
ATOM   4221  CG1 VAL B  66      22.778 -33.931  29.862  1.00105.60           C  
ANISOU 4221  CG1 VAL B  66    12275  13757  14089   -100   1480   5220       C  
ATOM   4222  CG2 VAL B  66      22.175 -36.190  30.777  1.00112.75           C  
ANISOU 4222  CG2 VAL B  66    13362  14409  15069   -231   1788   5734       C  
ATOM   4223  N   THR B  67      19.119 -36.607  30.681  1.00119.18           N  
ANISOU 4223  N   THR B  67    13786  15312  16184   -815   1982   6077       N  
ATOM   4224  CA  THR B  67      18.234 -37.752  30.503  1.00121.93           C  
ANISOU 4224  CA  THR B  67    14155  15465  16707  -1148   2123   6284       C  
ATOM   4225  C   THR B  67      16.789 -37.306  30.312  1.00123.09           C  
ANISOU 4225  C   THR B  67    13983  15816  16968  -1387   2129   6333       C  
ATOM   4226  O   THR B  67      16.055 -37.891  29.508  1.00126.22           O  
ANISOU 4226  O   THR B  67    14335  16066  17557  -1762   2118   6352       O  
ATOM   4227  CB  THR B  67      18.350 -38.697  31.698  1.00121.88           C  
ANISOU 4227  CB  THR B  67    14301  15403  16604  -1005   2374   6568       C  
ATOM   4228  OG1 THR B  67      18.155 -37.963  32.913  1.00122.10           O  
ANISOU 4228  OG1 THR B  67    14174  15776  16443   -709   2460   6662       O  
ATOM   4229  CG2 THR B  67      19.725 -39.356  31.723  1.00121.35           C  
ANISOU 4229  CG2 THR B  67    14562  15096  16450   -807   2375   6545       C  
ATOM   4230  N   LEU B  68      16.361 -36.267  31.034  1.00131.20           N  
ANISOU 4230  N   LEU B  68    14781  17194  17875  -1176   2149   6349       N  
ATOM   4231  CA  LEU B  68      15.023 -35.729  30.810  1.00138.63           C  
ANISOU 4231  CA  LEU B  68    15397  18362  18915  -1362   2144   6387       C  
ATOM   4232  C   LEU B  68      14.849 -35.291  29.361  1.00136.24           C  
ANISOU 4232  C   LEU B  68    15011  18004  18750  -1586   1913   6158       C  
ATOM   4233  O   LEU B  68      13.809 -35.549  28.743  1.00135.80           O  
ANISOU 4233  O   LEU B  68    14773  17969  18855  -1910   1895   6203       O  
ATOM   4234  CB  LEU B  68      14.765 -34.559  31.759  1.00137.21           C  
ANISOU 4234  CB  LEU B  68    15023  18549  18560  -1047   2196   6409       C  
ATOM   4235  CG  LEU B  68      14.246 -34.908  33.155  1.00135.78           C  
ANISOU 4235  CG  LEU B  68    14788  18517  18284   -923   2453   6693       C  
ATOM   4236  CD1 LEU B  68      14.360 -33.706  34.081  1.00139.15           C  
ANISOU 4236  CD1 LEU B  68    15110  19268  18494   -556   2486   6660       C  
ATOM   4237  CD2 LEU B  68      12.806 -35.393  33.095  1.00140.57           C  
ANISOU 4237  CD2 LEU B  68    15162  19185  19064  -1241   2579   6890       C  
ATOM   4238  N   PHE B  69      15.859 -34.627  28.806  1.00124.17           N  
ANISOU 4238  N   PHE B  69    13608  16418  17152  -1419   1738   5908       N  
ATOM   4239  CA  PHE B  69      15.832 -34.159  27.425  1.00123.56           C  
ANISOU 4239  CA  PHE B  69    13492  16274  17180  -1588   1519   5678       C  
ATOM   4240  C   PHE B  69      15.769 -35.314  26.432  1.00125.97           C  
ANISOU 4240  C   PHE B  69    13939  16255  17670  -1964   1471   5671       C  
ATOM   4241  O   PHE B  69      14.734 -35.575  25.819  1.00140.97           O  
ANISOU 4241  O   PHE B  69    15665  18186  19713  -2285   1442   5713       O  
ATOM   4242  CB  PHE B  69      17.067 -33.296  27.138  1.00124.15           C  
ANISOU 4242  CB  PHE B  69    13718  16319  17133  -1319   1378   5418       C  
ATOM   4243  CG  PHE B  69      17.182 -32.851  25.706  1.00118.81           C  
ANISOU 4243  CG  PHE B  69    13053  15536  16553  -1468   1165   5177       C  
ATOM   4244  CD1 PHE B  69      16.540 -31.704  25.269  1.00112.68           C  
ANISOU 4244  CD1 PHE B  69    12054  14990  15767  -1434   1075   5076       C  
ATOM   4245  CD2 PHE B  69      17.941 -33.574  24.799  1.00118.10           C  
ANISOU 4245  CD2 PHE B  69    13210  15111  16552  -1624   1068   5058       C  
ATOM   4246  CE1 PHE B  69      16.647 -31.291  23.954  1.00111.45           C  
ANISOU 4246  CE1 PHE B  69    11923  14739  15684  -1551    886   4865       C  
ATOM   4247  CE2 PHE B  69      18.050 -33.167  23.485  1.00102.45           C  
ANISOU 4247  CE2 PHE B  69    11252  13029  14647  -1756    878   4838       C  
ATOM   4248  CZ  PHE B  69      17.403 -32.024  23.062  1.00109.83           C  
ANISOU 4248  CZ  PHE B  69    11964  14201  15565  -1718    784   4742       C  
HETATM 4249  N   YCM B  70      16.902 -35.994  26.288  1.00145.16           N  
ANISOU 4249  N   YCM B  70    16685  18384  20085  -1917   1467   5614       N  
HETATM 4250  CA  YCM B  70      17.064 -37.084  25.358  1.00146.00           C  
ANISOU 4250  CA  YCM B  70    16995  18135  20342  -2233   1435   5584       C  
HETATM 4251  CB  YCM B  70      18.344 -37.857  25.684  1.00145.42           C  
ANISOU 4251  CB  YCM B  70    17271  17779  20204  -2064   1512   5602       C  
HETATM 4252  SG  YCM B  70      18.878 -39.014  24.461  1.00144.26           S  
ANISOU 4252  SG  YCM B  70    17443  17158  20210  -2367   1465   5510       S  
HETATM 4253  CD  YCM B  70      20.405 -38.315  23.907  1.00142.69           C  
ANISOU 4253  CD  YCM B  70    17429  16872  19915  -2078   1281   5231       C  
HETATM 4254  CE  YCM B  70      21.545 -38.601  24.852  1.00144.49           C  
ANISOU 4254  CE  YCM B  70    17851  17058  19993  -1723   1390   5306       C  
HETATM 4255  OZ1 YCM B  70      21.663 -37.949  25.912  1.00141.33           O  
ANISOU 4255  OZ1 YCM B  70    17322  16944  19431  -1422   1438   5363       O  
HETATM 4256  NZ2 YCM B  70      22.438 -39.590  24.536  1.00145.85           N  
ANISOU 4256  NZ2 YCM B  70    18339  16882  20194  -1729   1440   5315       N  
HETATM 4257  C   YCM B  70      15.928 -38.096  25.252  1.00146.83           C  
ANISOU 4257  C   YCM B  70    17021  18163  20605  -2630   1557   5767       C  
HETATM 4258  O   YCM B  70      15.494 -38.484  24.163  1.00147.43           O  
ANISOU 4258  O   YCM B  70    17091  18100  20827  -2984   1458   5680       O  
ATOM   4259  N   CYS B  71      15.445 -38.545  26.407  1.00137.01           N  
ANISOU 4259  N   CYS B  71    15721  17012  19325  -2581   1782   6020       N  
ATOM   4260  CA  CYS B  71      14.380 -39.542  26.434  1.00144.53           C  
ANISOU 4260  CA  CYS B  71    16605  17889  20420  -2958   1938   6199       C  
ATOM   4261  C   CYS B  71      13.223 -39.114  25.543  1.00142.31           C  
ANISOU 4261  C   CYS B  71    16010  17801  20260  -3271   1792   6102       C  
ATOM   4262  O   CYS B  71      12.626 -39.937  24.849  1.00146.73           O  
ANISOU 4262  O   CYS B  71    16611  18209  20932  -3635   1778   6006       O  
ATOM   4263  CB  CYS B  71      13.881 -39.766  27.863  1.00143.42           C  
ANISOU 4263  CB  CYS B  71    16392  17914  20189  -2797   2181   6429       C  
ATOM   4264  SG  CYS B  71      15.050 -40.627  28.938  1.00131.96           S  
ANISOU 4264  SG  CYS B  71    15334  16218  18587  -2478   2383   6559       S  
ATOM   4265  N   GLN B  72      12.912 -37.821  25.557  1.00152.35           N  
ANISOU 4265  N   GLN B  72    17005  19417  21464  -3079   1668   6037       N  
ATOM   4266  CA  GLN B  72      11.838 -37.319  24.717  1.00156.63           C  
ANISOU 4266  CA  GLN B  72    17226  20184  22101  -3323   1522   5964       C  
ATOM   4267  C   GLN B  72      12.291 -37.326  23.260  1.00152.53           C  
ANISOU 4267  C   GLN B  72    16843  19461  21652  -3506   1286   5713       C  
ATOM   4268  O   GLN B  72      13.452 -37.038  22.956  1.00156.35           O  
ANISOU 4268  O   GLN B  72    17575  19767  22064  -3293   1189   5550       O  
ATOM   4269  CB  GLN B  72      11.453 -35.900  25.130  1.00152.25           C  
ANISOU 4269  CB  GLN B  72    16383  20034  21433  -3010   1471   5951       C  
ATOM   4270  CG  GLN B  72      11.006 -35.758  26.580  1.00145.56           C  
ANISOU 4270  CG  GLN B  72    15396  19412  20496  -2797   1701   6188       C  
ATOM   4271  CD  GLN B  72       9.846 -36.657  26.952  1.00158.62           C  
ANISOU 4271  CD  GLN B  72    16875  21121  22274  -3122   1883   6417       C  
ATOM   4272  OE1 GLN B  72       8.814 -36.677  26.283  1.00157.10           O  
ANISOU 4272  OE1 GLN B  72    16434  21070  22185  -3402   1798   6369       O  
ATOM   4273  NE2 GLN B  72      10.010 -37.405  28.040  1.00166.64           N  
ANISOU 4273  NE2 GLN B  72    18062  22018  23234  -3029   2108   6565       N  
ATOM   4274  N   LYS B  73      11.363 -37.624  22.355  1.00143.11           N  
ANISOU 4274  N   LYS B  73    15473  18313  20588  -3901   1193   5677       N  
ATOM   4275  CA  LYS B  73      11.641 -37.653  20.925  1.00141.06           C  
ANISOU 4275  CA  LYS B  73    15321  17885  20390  -4110    967   5444       C  
ATOM   4276  C   LYS B  73      10.605 -36.784  20.226  1.00139.21           C  
ANISOU 4276  C   LYS B  73    14707  18015  20172  -4205    787   5376       C  
ATOM   4277  O   LYS B  73       9.493 -36.596  20.729  1.00129.30           O  
ANISOU 4277  O   LYS B  73    13109  17084  18935  -4264    864   5533       O  
ATOM   4278  CB  LYS B  73      11.626 -39.080  20.355  1.00148.43           C  
ANISOU 4278  CB  LYS B  73    16534  18462  21403  -4461   1010   5325       C  
ATOM   4279  CG  LYS B  73      13.016 -39.708  20.193  1.00147.31           C  
ANISOU 4279  CG  LYS B  73    16854  17883  21234  -4355   1043   5229       C  
ATOM   4280  CD  LYS B  73      13.750 -39.828  21.523  1.00148.74           C  
ANISOU 4280  CD  LYS B  73    17180  18005  21331  -4021   1248   5426       C  
ATOM   4281  CE  LYS B  73      15.053 -40.604  21.386  1.00146.13           C  
ANISOU 4281  CE  LYS B  73    17300  17254  20969  -3922   1300   5341       C  
ATOM   4282  NZ  LYS B  73      15.815 -40.639  22.668  1.00147.21           N  
ANISOU 4282  NZ  LYS B  73    17557  17378  20999  -3558   1477   5537       N  
ATOM   4283  N   GLY B  74      10.974 -36.256  19.063  1.00138.83           N  
ANISOU 4283  N   GLY B  74    14720  17918  20110  -4205    555   5149       N  
ATOM   4284  CA  GLY B  74      10.123 -35.320  18.372  1.00149.06           C  
ANISOU 4284  CA  GLY B  74    15683  19563  21389  -4216    376   5080       C  
ATOM   4285  C   GLY B  74      10.833 -34.001  18.158  1.00147.32           C  
ANISOU 4285  C   GLY B  74    15519  19417  21039  -3799    258   4925       C  
ATOM   4286  O   GLY B  74      12.016 -33.851  18.480  1.00148.85           O  
ANISOU 4286  O   GLY B  74    16004  19386  21164  -3539    298   4849       O  
ATOM   4287  N   PRO B  75      10.128 -33.014  17.604  1.00121.27           N  
ANISOU 4287  N   PRO B  75    11941  16437  17699  -3724    117   4875       N  
ATOM   4288  CA  PRO B  75      10.766 -31.711  17.363  1.00119.23           C  
ANISOU 4288  CA  PRO B  75    11752  16236  17314  -3332     29   4724       C  
ATOM   4289  C   PRO B  75      11.110 -31.037  18.683  1.00114.04           C  
ANISOU 4289  C   PRO B  75    11091  15692  16547  -2934    210   4822       C  
ATOM   4290  O   PRO B  75      10.230 -30.708  19.481  1.00113.63           O  
ANISOU 4290  O   PRO B  75    10753  15951  16470  -2844    327   5002       O  
ATOM   4291  CB  PRO B  75       9.699 -30.930  16.585  1.00119.51           C  
ANISOU 4291  CB  PRO B  75    11451  16626  17332  -3360   -123   4708       C  
ATOM   4292  CG  PRO B  75       8.405 -31.555  16.993  1.00118.82           C  
ANISOU 4292  CG  PRO B  75    11019  16797  17330  -3637    -47   4918       C  
ATOM   4293  CD  PRO B  75       8.702 -33.013  17.233  1.00122.98           C  
ANISOU 4293  CD  PRO B  75    11755  17000  17971  -3976     52   4966       C  
ATOM   4294  N   LYS B  76      12.405 -30.832  18.900  1.00130.19           N  
ANISOU 4294  N   LYS B  76    13454  17492  18519  -2699    234   4695       N  
ATOM   4295  CA  LYS B  76      12.906 -30.230  20.125  1.00125.01           C  
ANISOU 4295  CA  LYS B  76    12839  16919  17740  -2332    395   4750       C  
ATOM   4296  C   LYS B  76      12.788 -28.716  20.037  1.00117.41           C  
ANISOU 4296  C   LYS B  76    11755  16200  16657  -2011    360   4658       C  
ATOM   4297  O   LYS B  76      13.105 -28.115  19.006  1.00119.00           O  
ANISOU 4297  O   LYS B  76    12038  16335  16840  -1974    210   4464       O  
ATOM   4298  CB  LYS B  76      14.359 -30.636  20.367  1.00129.64           C  
ANISOU 4298  CB  LYS B  76    13796  17173  18288  -2221    426   4641       C  
ATOM   4299  N   LYS B  77      12.331 -28.096  21.120  1.00110.83           N  
ANISOU 4299  N   LYS B  77    10743  15634  15733  -1772    517   4798       N  
ATOM   4300  CA  LYS B  77      12.256 -26.646  21.130  1.00108.93           C  
ANISOU 4300  CA  LYS B  77    10423  15601  15366  -1447    525   4715       C  
ATOM   4301  C   LYS B  77      13.659 -26.060  21.084  1.00107.11           C  
ANISOU 4301  C   LYS B  77    10513  15152  15032  -1214    511   4481       C  
ATOM   4302  O   LYS B  77      14.620 -26.657  21.574  1.00107.09           O  
ANISOU 4302  O   LYS B  77    10735  14938  15015  -1205    556   4446       O  
ATOM   4303  CB  LYS B  77      11.568 -26.157  22.404  1.00107.86           C  
ANISOU 4303  CB  LYS B  77    10070  15768  15146  -1233    726   4913       C  
ATOM   4304  CG  LYS B  77      10.103 -26.512  22.550  1.00110.52           C  
ANISOU 4304  CG  LYS B  77    10039  16384  15568  -1412    769   5150       C  
ATOM   4305  CD  LYS B  77       9.595 -26.103  23.933  1.00110.77           C  
ANISOU 4305  CD  LYS B  77     9909  16670  15509  -1180    996   5345       C  
ATOM   4306  CE  LYS B  77       9.644 -24.594  24.143  1.00119.68           C  
ANISOU 4306  CE  LYS B  77    11017  17977  16480   -791   1059   5266       C  
ATOM   4307  NZ  LYS B  77       9.035 -24.189  25.443  1.00126.83           N  
ANISOU 4307  NZ  LYS B  77    11751  19142  17295   -578   1287   5464       N  
ATOM   4308  N   VAL B  78      13.772 -24.866  20.499  1.00107.83           N  
ANISOU 4308  N   VAL B  78    10621  15306  15043  -1015    459   4321       N  
ATOM   4309  CA  VAL B  78      15.076 -24.215  20.450  1.00107.54           C  
ANISOU 4309  CA  VAL B  78    10874  15079  14906   -803    462   4081       C  
ATOM   4310  C   VAL B  78      15.590 -23.984  21.863  1.00107.08           C  
ANISOU 4310  C   VAL B  78    10872  15090  14722   -573    644   4122       C  
ATOM   4311  O   VAL B  78      16.803 -24.004  22.105  1.00106.35           O  
ANISOU 4311  O   VAL B  78    11022  14817  14568   -482    655   3967       O  
ATOM   4312  CB  VAL B  78      14.987 -22.904  19.644  1.00107.82           C  
ANISOU 4312  CB  VAL B  78    10914  15183  14869   -620    416   3922       C  
ATOM   4313  CG1 VAL B  78      16.366 -22.285  19.458  1.00105.67           C  
ANISOU 4313  CG1 VAL B  78    10955  14685  14511   -453    420   3648       C  
ATOM   4314  CG2 VAL B  78      14.334 -23.162  18.290  1.00108.34           C  
ANISOU 4314  CG2 VAL B  78    10888  15236  15041   -842    231   3913       C  
ATOM   4315  N   SER B  79      14.682 -23.772  22.817  1.00 98.68           N  
ANISOU 4315  N   SER B  79     9579  14302  13612   -474    789   4330       N  
ATOM   4316  CA  SER B  79      15.088 -23.647  24.211  1.00 90.45           C  
ANISOU 4316  CA  SER B  79     8584  13343  12441   -272    965   4390       C  
ATOM   4317  C   SER B  79      15.684 -24.952  24.722  1.00 89.60           C  
ANISOU 4317  C   SER B  79     8604  13059  12380   -416    973   4470       C  
ATOM   4318  O   SER B  79      16.763 -24.963  25.324  1.00 93.65           O  
ANISOU 4318  O   SER B  79     9314  13478  12789   -274   1016   4371       O  
ATOM   4319  CB  SER B  79      13.892 -23.229  25.066  1.00101.61           C  
ANISOU 4319  CB  SER B  79     9720  15083  13806   -155   1124   4616       C  
ATOM   4320  OG  SER B  79      13.367 -21.985  24.632  1.00105.29           O  
ANISOU 4320  OG  SER B  79    10083  15711  14212     20   1140   4554       O  
ATOM   4321  N   SER B  80      14.999 -26.071  24.469  1.00 90.97           N  
ANISOU 4321  N   SER B  80     8672  13188  12706   -700    937   4646       N  
ATOM   4322  CA  SER B  80      15.493 -27.362  24.937  1.00 91.02           C  
ANISOU 4322  CA  SER B  80     8819  13005  12760   -836    975   4746       C  
ATOM   4323  C   SER B  80      16.856 -27.694  24.345  1.00 95.26           C  
ANISOU 4323  C   SER B  80     9662  13230  13302   -853    862   4533       C  
ATOM   4324  O   SER B  80      17.670 -28.355  24.999  1.00 94.34           O  
ANISOU 4324  O   SER B  80     9717  12989  13140   -797    924   4563       O  
ATOM   4325  CB  SER B  80      14.487 -28.461  24.598  1.00 96.01           C  
ANISOU 4325  CB  SER B  80     9301  13615  13565  -1179    962   4941       C  
ATOM   4326  OG  SER B  80      13.271 -28.265  25.296  1.00 96.32           O  
ANISOU 4326  OG  SER B  80     9046  13952  13599  -1161   1092   5160       O  
ATOM   4327  N   ILE B  81      17.123 -27.249  23.116  1.00 97.89           N  
ANISOU 4327  N   ILE B  81    10068  13440  13684   -915    705   4324       N  
ATOM   4328  CA  ILE B  81      18.435 -27.482  22.519  1.00 96.73           C  
ANISOU 4328  CA  ILE B  81    10209  13002  13541   -918    608   4109       C  
ATOM   4329  C   ILE B  81      19.511 -26.766  23.324  1.00 93.77           C  
ANISOU 4329  C   ILE B  81     9963  12673  12992   -610    683   3973       C  
ATOM   4330  O   ILE B  81      20.612 -27.292  23.524  1.00 94.12           O  
ANISOU 4330  O   ILE B  81    10209  12546  13006   -568    677   3902       O  
ATOM   4331  CB  ILE B  81      18.442 -27.041  21.043  1.00100.48           C  
ANISOU 4331  CB  ILE B  81    10732  13355  14090  -1030    438   3913       C  
ATOM   4332  CG1 ILE B  81      17.360 -27.781  20.251  1.00102.32           C  
ANISOU 4332  CG1 ILE B  81    10821  13576  14480  -1356    350   4038       C  
ATOM   4333  CG2 ILE B  81      19.812 -27.280  20.423  1.00 94.23           C  
ANISOU 4333  CG2 ILE B  81    10239  12257  13307  -1031    352   3691       C  
ATOM   4334  CD1 ILE B  81      17.470 -29.294  20.303  1.00102.60           C  
ANISOU 4334  CD1 ILE B  81    10963  13390  14629  -1619    364   4161       C  
ATOM   4335  N   TYR B  82      19.210 -25.555  23.796  1.00 95.69           N  
ANISOU 4335  N   TYR B  82    10091  13157  13111   -390    760   3931       N  
ATOM   4336  CA  TYR B  82      20.169 -24.831  24.622  1.00 93.27           C  
ANISOU 4336  CA  TYR B  82     9893  12922  12622   -121    843   3788       C  
ATOM   4337  C   TYR B  82      20.293 -25.451  26.008  1.00 91.02           C  
ANISOU 4337  C   TYR B  82     9591  12749  12244    -24    973   3974       C  
ATOM   4338  O   TYR B  82      21.373 -25.411  26.607  1.00 98.46           O  
ANISOU 4338  O   TYR B  82    10674  13679  13058    132    999   3868       O  
ATOM   4339  CB  TYR B  82      19.764 -23.361  24.732  1.00 97.81           C  
ANISOU 4339  CB  TYR B  82    10375  13703  13085     75    915   3690       C  
ATOM   4340  CG  TYR B  82      19.679 -22.639  23.403  1.00 98.47           C  
ANISOU 4340  CG  TYR B  82    10497  13685  13231     29    808   3508       C  
ATOM   4341  CD1 TYR B  82      20.465 -23.024  22.325  1.00 97.67           C  
ANISOU 4341  CD1 TYR B  82    10581  13308  13223   -109    661   3335       C  
ATOM   4342  CD2 TYR B  82      18.815 -21.565  23.231  1.00 94.39           C  
ANISOU 4342  CD2 TYR B  82     9843  13349  12673    142    866   3516       C  
ATOM   4343  CE1 TYR B  82      20.389 -22.364  21.112  1.00 95.61           C  
ANISOU 4343  CE1 TYR B  82    10369  12951  13006   -140    570   3173       C  
ATOM   4344  CE2 TYR B  82      18.734 -20.899  22.022  1.00 93.51           C  
ANISOU 4344  CE2 TYR B  82     9780  13149  12602    127    777   3363       C  
ATOM   4345  CZ  TYR B  82      19.523 -21.302  20.966  1.00 94.36           C  
ANISOU 4345  CZ  TYR B  82    10075  12980  12797    -18    627   3190       C  
ATOM   4346  OH  TYR B  82      19.443 -20.640  19.762  1.00 93.79           O  
ANISOU 4346  OH  TYR B  82    10064  12818  12753    -23    546   3043       O  
ATOM   4347  N   ILE B  83      19.208 -26.024  26.534  1.00 89.77           N  
ANISOU 4347  N   ILE B  83     9256  12714  12139   -111   1058   4251       N  
ATOM   4348  CA  ILE B  83      19.286 -26.707  27.823  1.00 93.56           C  
ANISOU 4348  CA  ILE B  83     9737  13280  12533    -25   1194   4451       C  
ATOM   4349  C   ILE B  83      20.244 -27.889  27.730  1.00 88.51           C  
ANISOU 4349  C   ILE B  83     9307  12386  11936   -105   1145   4456       C  
ATOM   4350  O   ILE B  83      21.094 -28.096  28.603  1.00 88.93           O  
ANISOU 4350  O   ILE B  83     9473  12470  11848     76   1205   4459       O  
ATOM   4351  CB  ILE B  83      17.889 -27.160  28.284  1.00 95.86           C  
ANISOU 4351  CB  ILE B  83     9801  13721  12899   -140   1305   4749       C  
ATOM   4352  CG1 ILE B  83      16.918 -25.981  28.356  1.00 91.19           C  
ANISOU 4352  CG1 ILE B  83     8990  13393  12263    -36   1362   4758       C  
ATOM   4353  CG2 ILE B  83      17.982 -27.846  29.641  1.00106.52           C  
ANISOU 4353  CG2 ILE B  83    11174  15150  14147    -33   1465   4961       C  
ATOM   4354  CD1 ILE B  83      17.328 -24.900  29.318  1.00 92.68           C  
ANISOU 4354  CD1 ILE B  83     9206  13777  12232    278   1477   4666       C  
ATOM   4355  N   PHE B  84      20.117 -28.682  26.665  1.00 84.12           N  
ANISOU 4355  N   PHE B  84     8811  11585  11565   -369   1041   4460       N  
ATOM   4356  CA  PHE B  84      20.978 -29.848  26.500  1.00 87.91           C  
ANISOU 4356  CA  PHE B  84     9511  11795  12097   -450   1013   4478       C  
ATOM   4357  C   PHE B  84      22.439 -29.434  26.397  1.00 98.61           C  
ANISOU 4357  C   PHE B  84    11055  13072  13342   -259    942   4228       C  
ATOM   4358  O   PHE B  84      23.300 -29.966  27.108  1.00104.75           O  
ANISOU 4358  O   PHE B  84    11957  13823  14019   -114    993   4269       O  
ATOM   4359  CB  PHE B  84      20.546 -30.637  25.264  1.00103.01           C  
ANISOU 4359  CB  PHE B  84    11462  13453  14222   -784    914   4489       C  
ATOM   4360  CG  PHE B  84      21.379 -31.857  24.998  1.00104.86           C  
ANISOU 4360  CG  PHE B  84    11947  13374  14522   -880    904   4510       C  
ATOM   4361  CD1 PHE B  84      21.128 -33.043  25.666  1.00110.20           C  
ANISOU 4361  CD1 PHE B  84    12673  13970  15228   -955   1043   4764       C  
ATOM   4362  CD2 PHE B  84      22.404 -31.821  24.067  1.00104.12           C  
ANISOU 4362  CD2 PHE B  84    12049  13054  14459   -889    776   4280       C  
ATOM   4363  CE1 PHE B  84      21.890 -34.168  25.418  1.00110.06           C  
ANISOU 4363  CE1 PHE B  84    12908  13647  15264  -1023   1059   4794       C  
ATOM   4364  CE2 PHE B  84      23.167 -32.942  23.815  1.00107.22           C  
ANISOU 4364  CE2 PHE B  84    12678  13153  14908   -959    783   4307       C  
ATOM   4365  CZ  PHE B  84      22.910 -34.118  24.491  1.00108.06           C  
ANISOU 4365  CZ  PHE B  84    12842  13176  15038  -1020    927   4568       C  
ATOM   4366  N   ASN B  85      22.740 -28.483  25.511  1.00 87.60           N  
ANISOU 4366  N   ASN B  85     9679  11647  11957   -252    829   3969       N  
ATOM   4367  CA  ASN B  85      24.117 -28.030  25.360  1.00 84.01           C  
ANISOU 4367  CA  ASN B  85     9389  11125  11406    -94    769   3710       C  
ATOM   4368  C   ASN B  85      24.636 -27.383  26.637  1.00 84.45           C  
ANISOU 4368  C   ASN B  85     9409  11442  11235    189    866   3675       C  
ATOM   4369  O   ASN B  85      25.828 -27.488  26.944  1.00 84.05           O  
ANISOU 4369  O   ASN B  85     9483  11372  11080    328    850   3556       O  
ATOM   4370  CB  ASN B  85      24.218 -27.055  24.188  1.00 82.11           C  
ANISOU 4370  CB  ASN B  85     9174  10808  11217   -145    658   3448       C  
ATOM   4371  CG  ASN B  85      24.207 -27.759  22.845  1.00 80.65           C  
ANISOU 4371  CG  ASN B  85     9100  10321  11221   -398    533   3410       C  
ATOM   4372  OD1 ASN B  85      25.256 -27.982  22.242  1.00 85.57           O  
ANISOU 4372  OD1 ASN B  85     9912  10732  11870   -406    460   3241       O  
ATOM   4373  ND2 ASN B  85      23.019 -28.116  22.372  1.00 81.87           N  
ANISOU 4373  ND2 ASN B  85     9135  10465  11505   -612    511   3563       N  
ATOM   4374  N   LEU B  86      23.762 -26.712  27.391  1.00 89.83           N  
ANISOU 4374  N   LEU B  86     9919  12382  11831    279    970   3774       N  
ATOM   4375  CA  LEU B  86      24.187 -26.116  28.653  1.00 89.77           C  
ANISOU 4375  CA  LEU B  86     9884  12632  11593    536   1073   3745       C  
ATOM   4376  C   LEU B  86      24.566 -27.186  29.668  1.00 92.39           C  
ANISOU 4376  C   LEU B  86    10265  12996  11841    625   1142   3951       C  
ATOM   4377  O   LEU B  86      25.518 -27.011  30.438  1.00 92.98           O  
ANISOU 4377  O   LEU B  86    10400  13201  11727    829   1161   3861       O  
ATOM   4378  CB  LEU B  86      23.077 -25.223  29.208  1.00 86.50           C  
ANISOU 4378  CB  LEU B  86     9286  12467  11112    607   1188   3829       C  
ATOM   4379  CG  LEU B  86      23.389 -24.481  30.510  1.00 93.80           C  
ANISOU 4379  CG  LEU B  86    10185  13669  11785    862   1310   3787       C  
ATOM   4380  CD1 LEU B  86      24.586 -23.557  30.337  1.00 89.42           C  
ANISOU 4380  CD1 LEU B  86     9751  13125  11101    977   1259   3439       C  
ATOM   4381  CD2 LEU B  86      22.175 -23.700  30.989  1.00 95.16           C  
ANISOU 4381  CD2 LEU B  86    10184  14056  11915    921   1442   3903       C  
ATOM   4382  N   ALA B  87      23.838 -28.305  29.681  1.00 94.29           N  
ANISOU 4382  N   ALA B  87    10485  13127  12213    475   1186   4226       N  
ATOM   4383  CA  ALA B  87      24.129 -29.363  30.642  1.00 98.35           C  
ANISOU 4383  CA  ALA B  87    11068  13650  12648    570   1280   4450       C  
ATOM   4384  C   ALA B  87      25.409 -30.103  30.277  1.00 96.91           C  
ANISOU 4384  C   ALA B  87    11091  13260  12470    603   1199   4362       C  
ATOM   4385  O   ALA B  87      26.199 -30.461  31.159  1.00 95.74           O  
ANISOU 4385  O   ALA B  87    11014  13208  12154    815   1245   4415       O  
ATOM   4386  CB  ALA B  87      22.952 -30.335  30.723  1.00105.96           C  
ANISOU 4386  CB  ALA B  87    11967  14533  13761    377   1379   4762       C  
ATOM   4387  N   VAL B  88      25.631 -30.346  28.984  1.00 95.83           N  
ANISOU 4387  N   VAL B  88    11049  12847  12513    408   1080   4234       N  
ATOM   4388  CA  VAL B  88      26.855 -31.017  28.555  1.00 92.86           C  
ANISOU 4388  CA  VAL B  88    10871  12259  12150    443   1011   4143       C  
ATOM   4389  C   VAL B  88      28.070 -30.193  28.957  1.00 91.77           C  
ANISOU 4389  C   VAL B  88    10750  12304  11813    691    960   3897       C  
ATOM   4390  O   VAL B  88      29.056 -30.721  29.485  1.00 97.87           O  
ANISOU 4390  O   VAL B  88    11615  13104  12468    869    970   3919       O  
ATOM   4391  CB  VAL B  88      26.821 -31.276  27.038  1.00 91.05           C  
ANISOU 4391  CB  VAL B  88    10740  11709  12144    181    894   4023       C  
ATOM   4392  CG1 VAL B  88      28.194 -31.700  26.539  1.00 82.15           C  
ANISOU 4392  CG1 VAL B  88     9811  10386  11015    248    820   3873       C  
ATOM   4393  CG2 VAL B  88      25.778 -32.332  26.706  1.00 95.38           C  
ANISOU 4393  CG2 VAL B  88    11298  12067  12874    -81    950   4271       C  
ATOM   4394  N   ALA B  89      28.018 -28.883  28.711  1.00 85.06           N  
ANISOU 4394  N   ALA B  89     9810  11591  10918    707    914   3656       N  
ATOM   4395  CA  ALA B  89      29.094 -28.006  29.158  1.00 82.44           C  
ANISOU 4395  CA  ALA B  89     9480  11457  10387    913    887   3402       C  
ATOM   4396  C   ALA B  89      29.272 -28.095  30.669  1.00 92.48           C  
ANISOU 4396  C   ALA B  89    10689  13029  11420   1152    985   3538       C  
ATOM   4397  O   ALA B  89      30.398 -28.196  31.169  1.00101.75           O  
ANISOU 4397  O   ALA B  89    11909  14319  12432   1332    959   3447       O  
ATOM   4398  CB  ALA B  89      28.804 -26.567  28.733  1.00 92.23           C  
ANISOU 4398  CB  ALA B  89    10645  12784  11614    880    869   3153       C  
ATOM   4399  N   ASP B  90      28.165 -28.056  31.414  1.00 89.93           N  
ANISOU 4399  N   ASP B  90    10254  12852  11064   1161   1100   3758       N  
ATOM   4400  CA  ASP B  90      28.242 -28.184  32.866  1.00 86.40           C  
ANISOU 4400  CA  ASP B  90     9760  12685  10384   1387   1206   3911       C  
ATOM   4401  C   ASP B  90      28.831 -29.529  33.273  1.00 94.02           C  
ANISOU 4401  C   ASP B  90    10840  13567  11318   1484   1226   4122       C  
ATOM   4402  O   ASP B  90      29.636 -29.605  34.209  1.00 98.01           O  
ANISOU 4402  O   ASP B  90    11358  14288  11593   1723   1241   4122       O  
ATOM   4403  CB  ASP B  90      26.854 -28.004  33.483  1.00 88.49           C  
ANISOU 4403  CB  ASP B  90     9893  13078  10652   1356   1341   4135       C  
ATOM   4404  CG  ASP B  90      26.371 -26.564  33.431  1.00 92.60           C  
ANISOU 4404  CG  ASP B  90    10301  13760  11122   1358   1361   3942       C  
ATOM   4405  OD1 ASP B  90      27.220 -25.647  33.448  1.00 91.29           O  
ANISOU 4405  OD1 ASP B  90    10162  13706  10819   1457   1312   3650       O  
ATOM   4406  OD2 ASP B  90      25.141 -26.350  33.379  1.00 88.32           O  
ANISOU 4406  OD2 ASP B  90     9646  13236  10674   1262   1437   4084       O  
ATOM   4407  N   LEU B  91      28.441 -30.604  32.584  1.00 93.05           N  
ANISOU 4407  N   LEU B  91    10807  13137  11411   1306   1233   4304       N  
ATOM   4408  CA  LEU B  91      28.966 -31.923  32.923  1.00 92.79           C  
ANISOU 4408  CA  LEU B  91    10917  12983  11356   1401   1283   4521       C  
ATOM   4409  C   LEU B  91      30.461 -32.013  32.650  1.00100.07           C  
ANISOU 4409  C   LEU B  91    11942  13883  12197   1548   1174   4324       C  
ATOM   4410  O   LEU B  91      31.215 -32.560  33.464  1.00105.17           O  
ANISOU 4410  O   LEU B  91    12641  14656  12662   1792   1210   4430       O  
ATOM   4411  CB  LEU B  91      28.223 -33.002  32.136  1.00 94.49           C  
ANISOU 4411  CB  LEU B  91    11228  12842  11832   1139   1328   4722       C  
ATOM   4412  CG  LEU B  91      26.820 -33.367  32.621  1.00 97.62           C  
ANISOU 4412  CG  LEU B  91    11538  13256  12297   1015   1477   5007       C  
ATOM   4413  CD1 LEU B  91      26.136 -34.284  31.619  1.00 95.64           C  
ANISOU 4413  CD1 LEU B  91    11370  12650  12320    693   1493   5124       C  
ATOM   4414  CD2 LEU B  91      26.875 -34.021  33.994  1.00 98.64           C  
ANISOU 4414  CD2 LEU B  91    11703  13540  12236   1251   1637   5281       C  
ATOM   4415  N   LEU B  92      30.910 -31.478  31.513  1.00104.48           N  
ANISOU 4415  N   LEU B  92    12526  14294  12878   1414   1044   4043       N  
ATOM   4416  CA  LEU B  92      32.318 -31.598  31.149  1.00102.38           C  
ANISOU 4416  CA  LEU B  92    12351  13987  12561   1530    946   3853       C  
ATOM   4417  C   LEU B  92      33.200 -30.750  32.057  1.00107.47           C  
ANISOU 4417  C   LEU B  92    12890  15018  12924   1781    913   3663       C  
ATOM   4418  O   LEU B  92      34.299 -31.173  32.434  1.00111.46           O  
ANISOU 4418  O   LEU B  92    13435  15626  13290   1987    884   3649       O  
ATOM   4419  CB  LEU B  92      32.509 -31.203  29.685  1.00 97.54           C  
ANISOU 4419  CB  LEU B  92    11796  13110  12154   1310    832   3598       C  
ATOM   4420  CG  LEU B  92      31.856 -32.143  28.668  1.00 88.22           C  
ANISOU 4420  CG  LEU B  92    10746  11536  11240   1054    842   3749       C  
ATOM   4421  CD1 LEU B  92      31.982 -31.583  27.262  1.00 68.38           C  
ANISOU 4421  CD1 LEU B  92     8278   8805   8899    848    723   3480       C  
ATOM   4422  CD2 LEU B  92      32.461 -33.538  28.743  1.00 94.25           C  
ANISOU 4422  CD2 LEU B  92    11687  12104  12021   1139    895   3952       C  
ATOM   4423  N   LEU B  93      32.738 -29.552  32.424  1.00111.64           N  
ANISOU 4423  N   LEU B  93    13284  15775  13360   1769    924   3514       N  
ATOM   4424  CA  LEU B  93      33.523 -28.710  33.321  1.00122.88           C  
ANISOU 4424  CA  LEU B  93    14612  17573  14503   1976    905   3316       C  
ATOM   4425  C   LEU B  93      33.481 -29.235  34.751  1.00127.70           C  
ANISOU 4425  C   LEU B  93    15186  18457  14877   2219    995   3570       C  
ATOM   4426  O   LEU B  93      34.481 -29.157  35.475  1.00127.56           O  
ANISOU 4426  O   LEU B  93    15134  18716  14619   2440    956   3482       O  
ATOM   4427  CB  LEU B  93      33.027 -27.265  33.248  1.00126.12           C  
ANISOU 4427  CB  LEU B  93    14925  18111  14884   1883    916   3075       C  
ATOM   4428  CG  LEU B  93      31.648 -26.928  33.820  1.00126.62           C  
ANISOU 4428  CG  LEU B  93    14906  18264  14941   1846   1038   3260       C  
ATOM   4429  CD1 LEU B  93      31.712 -26.599  35.306  1.00126.80           C  
ANISOU 4429  CD1 LEU B  93    14846  18671  14660   2071   1120   3313       C  
ATOM   4430  CD2 LEU B  93      31.026 -25.773  33.042  1.00116.10           C  
ANISOU 4430  CD2 LEU B  93    13535  16853  13726   1673   1037   3052       C  
ATOM   4431  N   LEU B  94      32.335 -29.774  35.179  1.00117.18           N  
ANISOU 4431  N   LEU B  94    13856  17066  13601   2182   1117   3886       N  
ATOM   4432  CA  LEU B  94      32.263 -30.383  36.504  1.00118.61           C  
ANISOU 4432  CA  LEU B  94    14031  17469  13567   2417   1222   4160       C  
ATOM   4433  C   LEU B  94      33.146 -31.621  36.605  1.00118.90           C  
ANISOU 4433  C   LEU B  94    14194  17421  13564   2586   1212   4326       C  
ATOM   4434  O   LEU B  94      33.593 -31.973  37.703  1.00120.40           O  
ANISOU 4434  O   LEU B  94    14377  17869  13500   2859   1256   4463       O  
ATOM   4435  CB  LEU B  94      30.817 -30.745  36.844  1.00119.38           C  
ANISOU 4435  CB  LEU B  94    14111  17483  13764   2315   1373   4466       C  
ATOM   4436  CG  LEU B  94      29.898 -29.592  37.247  1.00121.24           C  
ANISOU 4436  CG  LEU B  94    14206  17915  13944   2261   1433   4390       C  
ATOM   4437  CD1 LEU B  94      28.460 -30.075  37.359  1.00122.77           C  
ANISOU 4437  CD1 LEU B  94    14372  17983  14292   2124   1576   4699       C  
ATOM   4438  CD2 LEU B  94      30.355 -28.969  38.558  1.00123.25           C  
ANISOU 4438  CD2 LEU B  94    14391  18584  13853   2522   1465   4323       C  
ATOM   4439  N   ALA B  95      33.407 -32.291  35.481  1.00122.68           N  
ANISOU 4439  N   ALA B  95    14794  17543  14275   2443   1164   4323       N  
ATOM   4440  CA  ALA B  95      34.236 -33.489  35.505  1.00124.75           C  
ANISOU 4440  CA  ALA B  95    15199  17688  14512   2611   1177   4490       C  
ATOM   4441  C   ALA B  95      35.696 -33.179  35.803  1.00131.53           C  
ANISOU 4441  C   ALA B  95    16005  18825  15145   2860   1060   4276       C  
ATOM   4442  O   ALA B  95      36.450 -34.092  36.155  1.00131.09           O  
ANISOU 4442  O   ALA B  95    16033  18793  14981   3095   1082   4439       O  
ATOM   4443  CB  ALA B  95      34.124 -34.230  34.172  1.00123.85           C  
ANISOU 4443  CB  ALA B  95    15243  17106  14707   2375   1164   4518       C  
ATOM   4444  N   THR B  96      36.112 -31.920  35.671  1.00121.05           N  
ANISOU 4444  N   THR B  96    14541  17713  13741   2816    949   3917       N  
ATOM   4445  CA  THR B  96      37.483 -31.525  35.962  1.00117.11           C  
ANISOU 4445  CA  THR B  96    13959  17516  13022   3016    837   3676       C  
ATOM   4446  C   THR B  96      37.698 -31.125  37.417  1.00115.41           C  
ANISOU 4446  C   THR B  96    13615  17786  12450   3271    855   3694       C  
ATOM   4447  O   THR B  96      38.841 -30.870  37.809  1.00116.84           O  
ANISOU 4447  O   THR B  96    13705  18280  12409   3457    761   3514       O  
ATOM   4448  CB  THR B  96      37.901 -30.359  35.057  1.00114.07           C  
ANISOU 4448  CB  THR B  96    13505  17108  12728   2820    723   3251       C  
ATOM   4449  OG1 THR B  96      37.055 -29.228  35.304  1.00113.50           O  
ANISOU 4449  OG1 THR B  96    13342  17154  12629   2686    760   3120       O  
ATOM   4450  CG2 THR B  96      37.799 -30.756  33.590  1.00112.61           C  
ANISOU 4450  CG2 THR B  96    13455  16458  12874   2587    693   3218       C  
ATOM   4451  N   LEU B  97      36.637 -31.059  38.219  1.00120.30           N  
ANISOU 4451  N   LEU B  97    14217  18489  13001   3280    974   3899       N  
ATOM   4452  CA  LEU B  97      36.802 -30.697  39.623  1.00121.88           C  
ANISOU 4452  CA  LEU B  97    14314  19147  12849   3523   1000   3925       C  
ATOM   4453  C   LEU B  97      37.754 -31.624  40.369  1.00122.75           C  
ANISOU 4453  C   LEU B  97    14448  19471  12722   3866    984   4106       C  
ATOM   4454  O   LEU B  97      38.591 -31.115  41.135  1.00123.42           O  
ANISOU 4454  O   LEU B  97    14407  19988  12500   4061    902   3934       O  
ATOM   4455  CB  LEU B  97      35.432 -30.667  40.313  1.00119.94           C  
ANISOU 4455  CB  LEU B  97    14074  18900  12598   3483   1157   4174       C  
ATOM   4456  CG  LEU B  97      34.636 -29.367  40.181  1.00117.63           C  
ANISOU 4456  CG  LEU B  97    13689  18650  12355   3272   1177   3955       C  
ATOM   4457  CD1 LEU B  97      33.188 -29.582  40.594  1.00119.07           C  
ANISOU 4457  CD1 LEU B  97    13888  18733  12619   3203   1345   4254       C  
ATOM   4458  CD2 LEU B  97      35.270 -28.261  41.013  1.00118.33           C  
ANISOU 4458  CD2 LEU B  97    13654  19185  12121   3398   1125   3666       C  
ATOM   4459  N   PRO B  98      37.689 -32.950  40.213  1.00105.17           N  
ANISOU 4459  N   PRO B  98    12377  16980  10602   3960   1063   4441       N  
ATOM   4460  CA  PRO B  98      38.653 -33.809  40.920  1.00108.00           C  
ANISOU 4460  CA  PRO B  98    12764  17556  10716   4329   1057   4620       C  
ATOM   4461  C   PRO B  98      40.100 -33.451  40.638  1.00105.69           C  
ANISOU 4461  C   PRO B  98    12358  17499  10302   4443    879   4313       C  
ATOM   4462  O   PRO B  98      40.947 -33.587  41.530  1.00108.52           O  
ANISOU 4462  O   PRO B  98    12630  18264  10340   4761    829   4337       O  
ATOM   4463  CB  PRO B  98      38.309 -35.215  40.408  1.00107.35           C  
ANISOU 4463  CB  PRO B  98    12908  17020  10859   4325   1187   4975       C  
ATOM   4464  CG  PRO B  98      36.876 -35.128  40.005  1.00102.09           C  
ANISOU 4464  CG  PRO B  98    12302  16030  10457   4004   1300   5074       C  
ATOM   4465  CD  PRO B  98      36.689 -33.735  39.467  1.00110.18           C  
ANISOU 4465  CD  PRO B  98    13173  17127  11564   3744   1182   4686       C  
ATOM   4466  N   LEU B  99      40.413 -32.995  39.424  1.00118.31           N  
ANISOU 4466  N   LEU B  99    13945  18867  12138   4195    785   4025       N  
ATOM   4467  CA  LEU B  99      41.775 -32.565  39.130  1.00114.42           C  
ANISOU 4467  CA  LEU B  99    13328  18606  11542   4273    626   3704       C  
ATOM   4468  C   LEU B  99      42.168 -31.382  40.004  1.00114.72           C  
ANISOU 4468  C   LEU B  99    13151  19168  11269   4329    540   3410       C  
ATOM   4469  O   LEU B  99      43.291 -31.325  40.519  1.00118.93           O  
ANISOU 4469  O   LEU B  99    13549  20101  11539   4558    437   3289       O  
ATOM   4470  CB  LEU B  99      41.906 -32.205  37.651  1.00115.07           C  
ANISOU 4470  CB  LEU B  99    13454  18319  11948   3967    564   3443       C  
ATOM   4471  CG  LEU B  99      41.671 -33.339  36.653  1.00118.47           C  
ANISOU 4471  CG  LEU B  99    14102  18228  12685   3886    632   3676       C  
ATOM   4472  CD1 LEU B  99      41.765 -32.819  35.225  1.00112.34           C  
ANISOU 4472  CD1 LEU B  99    13360  17125  12200   3573    562   3383       C  
ATOM   4473  CD2 LEU B  99      42.660 -34.471  36.878  1.00115.11           C  
ANISOU 4473  CD2 LEU B  99    13738  17855  12143   4216    638   3883       C  
ATOM   4474  N   TRP B 100      41.253 -30.428  40.185  1.00110.42           N  
ANISOU 4474  N   TRP B 100    12573  18639  10744   4122    586   3288       N  
ATOM   4475  CA  TRP B 100      41.563 -29.243  40.973  1.00110.70           C  
ANISOU 4475  CA  TRP B 100    12435  19134  10493   4138    529   2986       C  
ATOM   4476  C   TRP B 100      41.540 -29.548  42.463  1.00112.65           C  
ANISOU 4476  C   TRP B 100    12631  19796  10374   4447    568   3207       C  
ATOM   4477  O   TRP B 100      42.239 -28.887  43.239  1.00114.92           O  
ANISOU 4477  O   TRP B 100    12763  20561  10343   4562    485   2980       O  
ATOM   4478  CB  TRP B 100      40.579 -28.121  40.639  1.00108.42           C  
ANISOU 4478  CB  TRP B 100    12153  18696  10347   3831    590   2794       C  
ATOM   4479  CG  TRP B 100      40.230 -28.068  39.181  1.00105.48           C  
ANISOU 4479  CG  TRP B 100    11880  17833  10365   3543    590   2709       C  
ATOM   4480  CD1 TRP B 100      38.987 -27.909  38.642  1.00103.26           C  
ANISOU 4480  CD1 TRP B 100    11688  17210  10335   3318    685   2808       C  
ATOM   4481  CD2 TRP B 100      41.132 -28.206  38.076  1.00102.13           C  
ANISOU 4481  CD2 TRP B 100    11472  17219  10112   3461    490   2517       C  
ATOM   4482  NE1 TRP B 100      39.060 -27.926  37.270  1.00101.11           N  
ANISOU 4482  NE1 TRP B 100    11492  16556  10368   3101    641   2685       N  
ATOM   4483  CE2 TRP B 100      40.366 -28.109  36.898  1.00 99.71           C  
ANISOU 4483  CE2 TRP B 100    11284  16451  10153   3182    528   2505       C  
ATOM   4484  CE3 TRP B 100      42.513 -28.398  37.970  1.00101.97           C  
ANISOU 4484  CE3 TRP B 100    11372  17392   9981   3602    374   2354       C  
ATOM   4485  CZ2 TRP B 100      40.935 -28.194  35.629  1.00 98.39           C  
ANISOU 4485  CZ2 TRP B 100    11176  15991  10217   3039    459   2336       C  
ATOM   4486  CZ3 TRP B 100      43.076 -28.483  36.710  1.00103.59           C  
ANISOU 4486  CZ3 TRP B 100    11629  17302  10430   3458    314   2189       C  
ATOM   4487  CH2 TRP B 100      42.288 -28.381  35.556  1.00 97.52           C  
ANISOU 4487  CH2 TRP B 100    10998  16055  10001   3179    359   2181       C  
ATOM   4488  N   ALA B 101      40.745 -30.536  42.878  1.00124.62           N  
ANISOU 4488  N   ALA B 101    14282  21143  11925   4575    701   3640       N  
ATOM   4489  CA  ALA B 101      40.783 -30.981  44.266  1.00128.56           C  
ANISOU 4489  CA  ALA B 101    14762  22013  12074   4907    750   3892       C  
ATOM   4490  C   ALA B 101      42.113 -31.657  44.578  1.00132.22           C  
ANISOU 4490  C   ALA B 101    15163  22766  12309   5239    642   3932       C  
ATOM   4491  O   ALA B 101      42.736 -31.382  45.610  1.00132.36           O  
ANISOU 4491  O   ALA B 101    15044  23300  11946   5476    570   3860       O  
ATOM   4492  CB  ALA B 101      39.617 -31.929  44.544  1.00134.41           C  
ANISOU 4492  CB  ALA B 101    15680  22453  12934   4949    943   4352       C  
ATOM   4493  N   THR B 102      42.562 -32.551  43.693  1.00135.24           N  
ANISOU 4493  N   THR B 102    15644  22831  12910   5268    631   4048       N  
ATOM   4494  CA  THR B 102      43.871 -33.170  43.871  1.00134.42           C  
ANISOU 4494  CA  THR B 102    15472  22992  12611   5590    530   4077       C  
ATOM   4495  C   THR B 102      44.988 -32.153  43.670  1.00131.59           C  
ANISOU 4495  C   THR B 102    14877  22999  12123   5522    337   3599       C  
ATOM   4496  O   THR B 102      45.984 -32.162  44.401  1.00137.53           O  
ANISOU 4496  O   THR B 102    15464  24251  12538   5802    228   3535       O  
ATOM   4497  CB  THR B 102      44.034 -34.341  42.902  1.00136.71           C  
ANISOU 4497  CB  THR B 102    15949  22808  13188   5618    591   4310       C  
ATOM   4498  OG1 THR B 102      42.941 -35.254  43.062  1.00126.56           O  
ANISOU 4498  OG1 THR B 102    14892  21161  12035   5631    790   4731       O  
ATOM   4499  CG2 THR B 102      45.346 -35.074  43.157  1.00139.98           C  
ANISOU 4499  CG2 THR B 102    16304  23499  13385   6007    514   4396       C  
ATOM   4500  N   TYR B 103      44.832 -31.259  42.691  1.00120.94           N  
ANISOU 4500  N   TYR B 103    13505  21418  11030   5150    297   3257       N  
ATOM   4501  CA  TYR B 103      45.833 -30.220  42.472  1.00122.04           C  
ANISOU 4501  CA  TYR B 103    13435  21873  11063   5041    143   2780       C  
ATOM   4502  C   TYR B 103      45.957 -29.303  43.680  1.00119.68           C  
ANISOU 4502  C   TYR B 103    12961  22135  10376   5105     94   2581       C  
ATOM   4503  O   TYR B 103      47.056 -28.827  43.989  1.00120.72           O  
ANISOU 4503  O   TYR B 103    12885  22720  10262   5182    -44   2290       O  
ATOM   4504  CB  TYR B 103      45.474 -29.415  41.221  1.00116.84           C  
ANISOU 4504  CB  TYR B 103    12826  20813  10753   4627    149   2481       C  
ATOM   4505  CG  TYR B 103      46.400 -28.255  40.939  1.00118.60           C  
ANISOU 4505  CG  TYR B 103    12862  21304  10895   4464     27   1969       C  
ATOM   4506  CD1 TYR B 103      47.750 -28.460  40.685  1.00124.18           C  
ANISOU 4506  CD1 TYR B 103    13428  22233  11522   4591    -99   1806       C  
ATOM   4507  CD2 TYR B 103      45.921 -26.952  40.920  1.00116.61           C  
ANISOU 4507  CD2 TYR B 103    12579  21078  10649   4182     56   1649       C  
ATOM   4508  CE1 TYR B 103      48.597 -27.399  40.423  1.00123.27           C  
ANISOU 4508  CE1 TYR B 103    13135  22362  11338   4416   -195   1326       C  
ATOM   4509  CE2 TYR B 103      46.759 -25.885  40.660  1.00115.78           C  
ANISOU 4509  CE2 TYR B 103    12326  21193  10472   4012    -27   1172       C  
ATOM   4510  CZ  TYR B 103      48.095 -26.114  40.413  1.00120.99           C  
ANISOU 4510  CZ  TYR B 103    12838  22075  11058   4118   -153   1006       C  
ATOM   4511  OH  TYR B 103      48.929 -25.051  40.154  1.00113.62           O  
ANISOU 4511  OH  TYR B 103    11751  21362  10057   3925   -221    520       O  
ATOM   4512  N   TYR B 104      44.850 -29.049  44.378  1.00127.24           N  
ANISOU 4512  N   TYR B 104    13995  23081  11269   5068    211   2728       N  
ATOM   4513  CA  TYR B 104      44.898 -28.212  45.570  1.00129.21           C  
ANISOU 4513  CA  TYR B 104    14110  23847  11139   5134    185   2559       C  
ATOM   4514  C   TYR B 104      45.429 -28.988  46.771  1.00136.56           C  
ANISOU 4514  C   TYR B 104    14974  25232  11680   5562    145   2820       C  
ATOM   4515  O   TYR B 104      46.198 -28.446  47.572  1.00137.37           O  
ANISOU 4515  O   TYR B 104    14887  25892  11415   5679     31   2589       O  
ATOM   4516  CB  TYR B 104      43.505 -27.652  45.867  1.00131.74           C  
ANISOU 4516  CB  TYR B 104    14544  23981  11532   4951    340   2631       C  
ATOM   4517  CG  TYR B 104      43.455 -26.722  47.058  1.00132.49           C  
ANISOU 4517  CG  TYR B 104    14533  24560  11248   4990    340   2444       C  
ATOM   4518  CD1 TYR B 104      43.277 -27.214  48.344  1.00133.67           C  
ANISOU 4518  CD1 TYR B 104    14684  25037  11066   5299    381   2728       C  
ATOM   4519  CD2 TYR B 104      43.581 -25.348  46.894  1.00131.91           C  
ANISOU 4519  CD2 TYR B 104    14378  24602  11141   4715    317   1984       C  
ATOM   4520  CE1 TYR B 104      43.231 -26.365  49.434  1.00136.19           C  
ANISOU 4520  CE1 TYR B 104    14921  25800  11026   5329    383   2550       C  
ATOM   4521  CE2 TYR B 104      43.535 -24.492  47.977  1.00134.05           C  
ANISOU 4521  CE2 TYR B 104    14574  25300  11059   4735    333   1799       C  
ATOM   4522  CZ  TYR B 104      43.359 -25.005  49.245  1.00136.89           C  
ANISOU 4522  CZ  TYR B 104    14931  25992  11088   5040    359   2081       C  
ATOM   4523  OH  TYR B 104      43.313 -24.157  50.327  1.00129.17           O  
ANISOU 4523  OH  TYR B 104    13892  25441   9746   5056    377   1892       O  
ATOM   4524  N   SER B 105      45.030 -30.255  46.910  1.00141.46           N  
ANISOU 4524  N   SER B 105    15756  25628  12366   5800    246   3296       N  
ATOM   4525  CA  SER B 105      45.460 -31.044  48.060  1.00145.50           C  
ANISOU 4525  CA  SER B 105    16237  26543  12503   6240    235   3589       C  
ATOM   4526  C   SER B 105      46.971 -31.240  48.076  1.00147.48           C  
ANISOU 4526  C   SER B 105    16290  27200  12546   6469     52   3430       C  
ATOM   4527  O   SER B 105      47.567 -31.372  49.151  1.00151.01           O  
ANISOU 4527  O   SER B 105    16612  28050  12715   6689     37   3395       O  
ATOM   4528  CB  SER B 105      44.750 -32.398  48.062  1.00146.34           C  
ANISOU 4528  CB  SER B 105    16588  26252  12763   6427    410   4127       C  
ATOM   4529  OG  SER B 105      45.137 -33.176  46.944  1.00145.07           O  
ANISOU 4529  OG  SER B 105    16520  25692  12908   6405    409   4215       O  
ATOM   4530  N   TYR B 106      47.607 -31.264  46.904  1.00147.82           N  
ANISOU 4530  N   TYR B 106    16299  27015  12852   6323    -24   3245       N  
ATOM   4531  CA  TYR B 106      49.055 -31.363  46.804  1.00155.25           C  
ANISOU 4531  CA  TYR B 106    17026  28340  13623   6508   -198   3060       C  
ATOM   4532  C   TYR B 106      49.732 -29.995  46.773  1.00144.71           C  
ANISOU 4532  C   TYR B 106    15437  27390  12158   6256   -349   2494       C  
ATOM   4533  O   TYR B 106      50.866 -29.884  46.294  1.00144.25           O  
ANISOU 4533  O   TYR B 106    15197  27524  12087   6264   -484   2246       O  
ATOM   4534  CB  TYR B 106      49.444 -32.164  45.558  1.00145.15           C  
ANISOU 4534  CB  TYR B 106    15850  26604  12695   6496   -181   3164       C  
ATOM   4535  CG  TYR B 106      49.257 -33.660  45.695  1.00137.77           C  
ANISOU 4535  CG  TYR B 106    15134  25364  11847   6784    -22   3653       C  
ATOM   4536  CD1 TYR B 106      48.039 -34.259  45.405  1.00152.86           C  
ANISOU 4536  CD1 TYR B 106    17328  26746  14005   6708    155   4005       C  
ATOM   4537  CD2 TYR B 106      50.304 -34.474  46.104  1.00158.18           C  
ANISOU 4537  CD2 TYR B 106    17655  28150  14297   7085    -14   3725       C  
ATOM   4538  CE1 TYR B 106      47.867 -35.627  45.525  1.00153.32           C  
ANISOU 4538  CE1 TYR B 106    17607  26471  14175   6905    340   4395       C  
ATOM   4539  CE2 TYR B 106      50.143 -35.842  46.227  1.00153.41           C  
ANISOU 4539  CE2 TYR B 106    17278  27221  13790   7313    171   4132       C  
ATOM   4540  CZ  TYR B 106      48.923 -36.414  45.937  1.00149.18           C  
ANISOU 4540  CZ  TYR B 106    17032  26147  13504   7213    351   4455       C  
ATOM   4541  OH  TYR B 106      48.761 -37.776  46.059  1.00127.08           O  
ANISOU 4541  OH  TYR B 106    14469  23012  10803   7412    553   4831       O  
ATOM   4542  N   ARG B 107      49.066 -28.960  47.281  1.00153.52           N  
ANISOU 4542  N   ARG B 107    16540  28617  13172   6032   -314   2285       N  
ATOM   4543  CA  ARG B 107      49.626 -27.614  47.373  1.00153.27           C  
ANISOU 4543  CA  ARG B 107    16300  28951  12985   5779   -422   1744       C  
ATOM   4544  C   ARG B 107      50.217 -27.167  46.035  1.00150.44           C  
ANISOU 4544  C   ARG B 107    15890  28325  12944   5481   -475   1398       C  
ATOM   4545  O   ARG B 107      51.405 -26.862  45.913  1.00151.59           O  
ANISOU 4545  O   ARG B 107    15808  28831  12960   5486   -619   1088       O  
ATOM   4546  CB  ARG B 107      50.675 -27.529  48.486  1.00157.49           C  
ANISOU 4546  CB  ARG B 107    16573  30229  13036   6048   -573   1617       C  
ATOM   4547  CG  ARG B 107      50.101 -27.460  49.894  1.00160.19           C  
ANISOU 4547  CG  ARG B 107    16943  30792  13128   6174   -476   1748       C  
ATOM   4548  CD  ARG B 107      49.525 -28.791  50.352  1.00161.73           C  
ANISOU 4548  CD  ARG B 107    17331  30729  13392   6492   -331   2298       C  
ATOM   4549  NE  ARG B 107      49.202 -28.771  51.778  1.00174.06           N  
ANISOU 4549  NE  ARG B 107    18878  32570  14688   6653   -258   2394       N  
ATOM   4550  CZ  ARG B 107      48.534 -29.729  52.413  1.00174.41           C  
ANISOU 4550  CZ  ARG B 107    19097  32427  14744   6895   -102   2830       C  
ATOM   4551  NH1 ARG B 107      48.289 -29.617  53.712  1.00173.08           N  
ANISOU 4551  NH1 ARG B 107    18900  32539  14323   7034    -49   2878       N  
ATOM   4552  NH2 ARG B 107      48.113 -30.801  51.754  1.00171.52           N  
ANISOU 4552  NH2 ARG B 107    18940  31579  14650   6986     11   3208       N  
ATOM   4553  N   TYR B 108      49.354 -27.130  45.023  1.00136.35           N  
ANISOU 4553  N   TYR B 108    14319  25910  11579   5217   -354   1454       N  
ATOM   4554  CA  TYR B 108      49.717 -26.626  43.700  1.00137.57           C  
ANISOU 4554  CA  TYR B 108    14473  25739  12060   4903   -374   1134       C  
ATOM   4555  C   TYR B 108      50.958 -27.336  43.161  1.00136.99           C  
ANISOU 4555  C   TYR B 108    14277  25757  12017   5080   -491   1129       C  
ATOM   4556  O   TYR B 108      51.928 -26.710  42.727  1.00141.47           O  
ANISOU 4556  O   TYR B 108    14665  26518  12571   4939   -589    732       O  
ATOM   4557  CB  TYR B 108      49.929 -25.112  43.740  1.00140.78           C  
ANISOU 4557  CB  TYR B 108    14756  26365  12369   4580   -398    601       C  
ATOM   4558  CG  TYR B 108      48.729 -24.341  44.241  1.00136.14           C  
ANISOU 4558  CG  TYR B 108    14296  25682  11750   4411   -266    588       C  
ATOM   4559  CD1 TYR B 108      47.698 -23.989  43.382  1.00134.82           C  
ANISOU 4559  CD1 TYR B 108    14332  24954  11940   4137   -132    602       C  
ATOM   4560  CD2 TYR B 108      48.626 -23.970  45.575  1.00144.17           C  
ANISOU 4560  CD2 TYR B 108    15228  27182  12369   4537   -272    567       C  
ATOM   4561  CE1 TYR B 108      46.598 -23.286  43.836  1.00134.02           C  
ANISOU 4561  CE1 TYR B 108    14335  24777  11808   4005     -2    604       C  
ATOM   4562  CE2 TYR B 108      47.530 -23.267  46.038  1.00145.73           C  
ANISOU 4562  CE2 TYR B 108    15549  27287  12535   4395   -135    562       C  
ATOM   4563  CZ  TYR B 108      46.519 -22.928  45.165  1.00134.72           C  
ANISOU 4563  CZ  TYR B 108    14347  25334  11509   4135      3    585       C  
ATOM   4564  OH  TYR B 108      45.426 -22.229  45.622  1.00123.09           O  
ANISOU 4564  OH  TYR B 108    12986  23779  10004   4016    149    592       O  
ATOM   4565  N   ASP B 109      50.923 -28.665  43.201  1.00129.24           N  
ANISOU 4565  N   ASP B 109    13401  24629  11074   5398   -462   1581       N  
ATOM   4566  CA  ASP B 109      51.973 -29.510  42.636  1.00121.42           C  
ANISOU 4566  CA  ASP B 109    12346  23642  10147   5607   -534   1661       C  
ATOM   4567  C   ASP B 109      51.311 -30.449  41.632  1.00123.63           C  
ANISOU 4567  C   ASP B 109    12918  23226  10831   5570   -405   1991       C  
ATOM   4568  O   ASP B 109      50.718 -31.461  42.017  1.00126.89           O  
ANISOU 4568  O   ASP B 109    13505  23468  11238   5803   -304   2440       O  
ATOM   4569  CB  ASP B 109      52.705 -30.282  43.729  1.00125.85           C  
ANISOU 4569  CB  ASP B 109    12757  24751  10311   6085   -615   1902       C  
ATOM   4570  CG  ASP B 109      53.900 -31.054  43.199  1.00127.23           C  
ANISOU 4570  CG  ASP B 109    12825  25003  10512   6327   -694   1953       C  
ATOM   4571  OD1 ASP B 109      54.198 -30.939  41.992  1.00128.53           O  
ANISOU 4571  OD1 ASP B 109    13028  24809  11000   6103   -689   1772       O  
ATOM   4572  OD2 ASP B 109      54.544 -31.772  43.993  1.00130.97           O  
ANISOU 4572  OD2 ASP B 109    13216  25816  10732   6683   -704   2140       O  
ATOM   4573  N   TRP B 110      51.408 -30.113  40.348  1.00122.76           N  
ANISOU 4573  N   TRP B 110    12869  22712  11064   5268   -397   1762       N  
ATOM   4574  CA  TRP B 110      50.760 -30.912  39.316  1.00122.87           C  
ANISOU 4574  CA  TRP B 110    13161  22058  11464   5179   -281   2026       C  
ATOM   4575  C   TRP B 110      51.488 -32.238  39.130  1.00120.82           C  
ANISOU 4575  C   TRP B 110    12951  21743  11211   5527   -276   2335       C  
ATOM   4576  O   TRP B 110      52.710 -32.269  38.956  1.00121.96           O  
ANISOU 4576  O   TRP B 110    12912  22167  11261   5664   -381   2168       O  
ATOM   4577  CB  TRP B 110      50.716 -30.144  37.997  1.00120.35           C  
ANISOU 4577  CB  TRP B 110    12894  21353  11482   4774   -280   1679       C  
ATOM   4578  CG  TRP B 110      49.831 -30.790  36.980  1.00120.51           C  
ANISOU 4578  CG  TRP B 110    13205  20695  11887   4620   -163   1918       C  
ATOM   4579  CD1 TRP B 110      50.219 -31.576  35.935  1.00118.74           C  
ANISOU 4579  CD1 TRP B 110    13113  20089  11914   4634   -141   2015       C  
ATOM   4580  CD2 TRP B 110      48.401 -30.721  36.920  1.00120.55           C  
ANISOU 4580  CD2 TRP B 110    13401  20342  12059   4425    -49   2088       C  
ATOM   4581  NE1 TRP B 110      49.121 -31.994  35.224  1.00118.19           N  
ANISOU 4581  NE1 TRP B 110    13309  19447  12152   4442    -27   2221       N  
ATOM   4582  CE2 TRP B 110      47.992 -31.483  35.809  1.00117.40           C  
ANISOU 4582  CE2 TRP B 110    13235  19363  12008   4312     27   2271       C  
ATOM   4583  CE3 TRP B 110      47.428 -30.085  37.697  1.00123.92           C  
ANISOU 4583  CE3 TRP B 110    13819  20893  12371   4335      1   2101       C  
ATOM   4584  CZ2 TRP B 110      46.653 -31.626  35.455  1.00113.38           C  
ANISOU 4584  CZ2 TRP B 110    12927  18424  11729   4103    137   2457       C  
ATOM   4585  CZ3 TRP B 110      46.100 -30.229  37.344  1.00120.48           C  
ANISOU 4585  CZ3 TRP B 110    13580  20023  12173   4146    119   2299       C  
ATOM   4586  CH2 TRP B 110      45.724 -30.993  36.233  1.00115.76           C  
ANISOU 4586  CH2 TRP B 110    13191  18878  11917   4027    179   2471       C  
ATOM   4587  N   LEU B 111      50.731 -33.337  39.170  1.00116.40           N  
ANISOU 4587  N   LEU B 111    12644  20820  10762   5669   -140   2789       N  
ATOM   4588  CA  LEU B 111      51.288 -34.674  39.036  1.00118.52           C  
ANISOU 4588  CA  LEU B 111    13020  20976  11038   6015    -88   3134       C  
ATOM   4589  C   LEU B 111      50.838 -35.404  37.778  1.00116.29           C  
ANISOU 4589  C   LEU B 111    13031  19986  11166   5846     34   3294       C  
ATOM   4590  O   LEU B 111      51.438 -36.428  37.432  1.00121.38           O  
ANISOU 4590  O   LEU B 111    13777  20483  11858   6091     83   3512       O  
ATOM   4591  CB  LEU B 111      50.916 -35.527  40.258  1.00121.89           C  
ANISOU 4591  CB  LEU B 111    13521  21598  11194   6394     -2   3574       C  
ATOM   4592  CG  LEU B 111      51.388 -35.004  41.614  1.00124.82           C  
ANISOU 4592  CG  LEU B 111    13621  22698  11106   6634   -120   3482       C  
ATOM   4593  CD1 LEU B 111      50.778 -35.827  42.739  1.00127.73           C  
ANISOU 4593  CD1 LEU B 111    14134  23118  11281   6915     21   3904       C  
ATOM   4594  CD2 LEU B 111      52.905 -35.022  41.695  1.00127.12           C  
ANISOU 4594  CD2 LEU B 111    13645  23474  11180   6892   -272   3308       C  
ATOM   4595  N   PHE B 112      49.811 -34.913  37.084  1.00114.48           N  
ANISOU 4595  N   PHE B 112    12944  19328  11225   5443     89   3192       N  
ATOM   4596  CA  PHE B 112      49.249 -35.640  35.954  1.00112.64           C  
ANISOU 4596  CA  PHE B 112    13002  18433  11364   5265    207   3361       C  
ATOM   4597  C   PHE B 112      50.048 -35.464  34.669  1.00111.91           C  
ANISOU 4597  C   PHE B 112    12906  18116  11499   5109    147   3087       C  
ATOM   4598  O   PHE B 112      49.790 -36.185  33.699  1.00114.19           O  
ANISOU 4598  O   PHE B 112    13439  17876  12071   5007    239   3229       O  
ATOM   4599  CB  PHE B 112      47.801 -35.199  35.717  1.00113.21           C  
ANISOU 4599  CB  PHE B 112    13208  18166  11642   4905    283   3370       C  
ATOM   4600  CG  PHE B 112      46.918 -35.342  36.924  1.00112.81           C  
ANISOU 4600  CG  PHE B 112    13171  18296  11395   5026    363   3638       C  
ATOM   4601  CD1 PHE B 112      46.796 -34.308  37.838  1.00110.37           C  
ANISOU 4601  CD1 PHE B 112    12654  18444  10838   5013    290   3444       C  
ATOM   4602  CD2 PHE B 112      46.207 -36.510  37.143  1.00111.44           C  
ANISOU 4602  CD2 PHE B 112    13234  17824  11285   5145    529   4080       C  
ATOM   4603  CE1 PHE B 112      45.984 -34.438  38.949  1.00111.88           C  
ANISOU 4603  CE1 PHE B 112    12866  18797  10845   5131    373   3692       C  
ATOM   4604  CE2 PHE B 112      45.393 -36.646  38.251  1.00116.20           C  
ANISOU 4604  CE2 PHE B 112    13854  18585  11711   5256    619   4329       C  
ATOM   4605  CZ  PHE B 112      45.282 -35.608  39.155  1.00115.09           C  
ANISOU 4605  CZ  PHE B 112    13499  18907  11321   5256    538   4139       C  
ATOM   4606  N   GLY B 113      50.999 -34.533  34.635  1.00135.29           N  
ANISOU 4606  N   GLY B 113    15605  21457  14342   5076      5   2695       N  
ATOM   4607  CA  GLY B 113      51.822 -34.326  33.468  1.00129.38           C  
ANISOU 4607  CA  GLY B 113    14838  20530  13792   4940    -44   2423       C  
ATOM   4608  C   GLY B 113      51.575 -32.982  32.815  1.00119.82           C  
ANISOU 4608  C   GLY B 113    13560  19239  12729   4523   -101   1987       C  
ATOM   4609  O   GLY B 113      50.552 -32.330  33.048  1.00120.54           O  
ANISOU 4609  O   GLY B 113    13685  19269  12844   4303    -76   1942       O  
ATOM   4610  N   PRO B 114      52.514 -32.540  31.973  1.00106.18           N  
ANISOU 4610  N   PRO B 114    11740  17503  11101   4416   -163   1663       N  
ATOM   4611  CA  PRO B 114      52.351 -31.231  31.321  1.00103.10           C  
ANISOU 4611  CA  PRO B 114    11302  17027  10843   4029   -196   1236       C  
ATOM   4612  C   PRO B 114      51.311 -31.227  30.214  1.00102.58           C  
ANISOU 4612  C   PRO B 114    11516  16332  11126   3714   -112   1276       C  
ATOM   4613  O   PRO B 114      50.765 -30.160  29.907  1.00 95.76           O  
ANISOU 4613  O   PRO B 114    10652  15388  10344   3415   -112   1016       O  
ATOM   4614  CB  PRO B 114      53.753 -30.939  30.771  1.00104.82           C  
ANISOU 4614  CB  PRO B 114    11347  17423  11056   4050   -268    920       C  
ATOM   4615  CG  PRO B 114      54.325 -32.292  30.504  1.00109.45           C  
ANISOU 4615  CG  PRO B 114    12031  17864  11691   4352   -233   1235       C  
ATOM   4616  CD  PRO B 114      53.763 -33.210  31.566  1.00115.88           C  
ANISOU 4616  CD  PRO B 114    12913  18792  12326   4651   -187   1677       C  
ATOM   4617  N   VAL B 115      51.018 -32.378  29.606  1.00113.67           N  
ANISOU 4617  N   VAL B 115    13165  17297  12729   3773    -34   1589       N  
ATOM   4618  CA  VAL B 115      50.018 -32.412  28.544  1.00110.57           C  
ANISOU 4618  CA  VAL B 115    13028  16330  12653   3464     34   1625       C  
ATOM   4619  C   VAL B 115      48.620 -32.279  29.133  1.00108.84           C  
ANISOU 4619  C   VAL B 115    12875  16058  12422   3357     84   1812       C  
ATOM   4620  O   VAL B 115      47.754 -31.605  28.563  1.00108.35           O  
ANISOU 4620  O   VAL B 115    12890  15752  12527   3055     99   1686       O  
ATOM   4621  CB  VAL B 115      50.166 -33.700  27.714  1.00122.73           C  
ANISOU 4621  CB  VAL B 115    14817  17419  14397   3541    110   1884       C  
ATOM   4622  CG1 VAL B 115      49.091 -33.770  26.639  1.00113.41           C  
ANISOU 4622  CG1 VAL B 115    13895  15669  13525   3208    169   1922       C  
ATOM   4623  CG2 VAL B 115      51.552 -33.773  27.090  1.00120.42           C  
ANISOU 4623  CG2 VAL B 115    14453  17177  14125   3647     70   1688       C  
ATOM   4624  N   MET B 116      48.377 -32.908  30.285  1.00104.31           N  
ANISOU 4624  N   MET B 116    12269  15723  11642   3615    118   2120       N  
ATOM   4625  CA  MET B 116      47.076 -32.787  30.932  1.00104.96           C  
ANISOU 4625  CA  MET B 116    12395  15789  11696   3531    178   2305       C  
ATOM   4626  C   MET B 116      46.878 -31.412  31.554  1.00104.68           C  
ANISOU 4626  C   MET B 116    12157  16123  11492   3419    121   2015       C  
ATOM   4627  O   MET B 116      45.736 -31.025  31.822  1.00104.14           O  
ANISOU 4627  O   MET B 116    12126  15988  11455   3270    172   2082       O  
ATOM   4628  CB  MET B 116      46.910 -33.870  31.999  1.00106.86           C  
ANISOU 4628  CB  MET B 116    12676  16171  11754   3853    251   2722       C  
ATOM   4629  CG  MET B 116      46.462 -35.215  31.445  1.00117.06           C  
ANISOU 4629  CG  MET B 116    14252  16971  13256   3870    375   3082       C  
ATOM   4630  SD  MET B 116      46.025 -36.429  32.710  1.00132.26           S  
ANISOU 4630  SD  MET B 116    16272  18999  14983   4209    511   3592       S  
ATOM   4631  CE  MET B 116      44.850 -35.514  33.709  1.00109.19           C  
ANISOU 4631  CE  MET B 116    13220  16342  11927   4083    515   3578       C  
ATOM   4632  N   CYS B 117      47.962 -30.672  31.794  1.00102.35           N  
ANISOU 4632  N   CYS B 117    11650  16220  11020   3482     29   1691       N  
ATOM   4633  CA  CYS B 117      47.832 -29.304  32.285  1.00104.31           C  
ANISOU 4633  CA  CYS B 117    11732  16783  11117   3338     -7   1370       C  
ATOM   4634  C   CYS B 117      47.319 -28.384  31.186  1.00102.28           C  
ANISOU 4634  C   CYS B 117    11570  16176  11114   2976     17   1100       C  
ATOM   4635  O   CYS B 117      46.381 -27.607  31.397  1.00 98.92           O  
ANISOU 4635  O   CYS B 117    11157  15737  10690   2811     62   1042       O  
ATOM   4636  CB  CYS B 117      49.179 -28.813  32.817  1.00104.71           C  
ANISOU 4636  CB  CYS B 117    11529  17352  10905   3484   -106   1083       C  
ATOM   4637  SG  CYS B 117      49.281 -27.027  33.068  1.00105.11           S  
ANISOU 4637  SG  CYS B 117    11408  17710  10819   3229   -133    572       S  
ATOM   4638  N   LYS B 118      47.927 -28.461  30.001  1.00107.24           N  
ANISOU 4638  N   LYS B 118    12273  16522  11951   2864     -3    942       N  
ATOM   4639  CA  LYS B 118      47.461 -27.664  28.872  1.00106.51           C  
ANISOU 4639  CA  LYS B 118    12298  16071  12102   2541     25    707       C  
ATOM   4640  C   LYS B 118      46.104 -28.152  28.379  1.00103.86           C  
ANISOU 4640  C   LYS B 118    12173  15300  11991   2405     91    989       C  
ATOM   4641  O   LYS B 118      45.260 -27.347  27.967  1.00 98.52           O  
ANISOU 4641  O   LYS B 118    11552  14458  11422   2176    125    873       O  
ATOM   4642  CB  LYS B 118      48.499 -27.708  27.749  1.00106.59           C  
ANISOU 4642  CB  LYS B 118    12343  15891  12267   2478     -7    485       C  
ATOM   4643  CG  LYS B 118      48.223 -26.763  26.591  1.00103.08           C  
ANISOU 4643  CG  LYS B 118    12006  15123  12035   2164     23    191       C  
ATOM   4644  CD  LYS B 118      49.306 -26.857  25.522  1.00102.51           C  
ANISOU 4644  CD  LYS B 118    11971  14873  12104   2119      3    -18       C  
ATOM   4645  CE  LYS B 118      50.612 -26.213  25.975  1.00105.29           C  
ANISOU 4645  CE  LYS B 118    12082  15668  12255   2193    -41   -349       C  
ATOM   4646  NZ  LYS B 118      50.483 -24.738  26.148  1.00108.88           N  
ANISOU 4646  NZ  LYS B 118    12456  16290  12624   1987     -8   -716       N  
ATOM   4647  N   VAL B 119      45.875 -29.464  28.415  1.00 98.06           N  
ANISOU 4647  N   VAL B 119    11557  14381  11321   2542    118   1359       N  
ATOM   4648  CA  VAL B 119      44.634 -30.054  27.926  1.00 94.79           C  
ANISOU 4648  CA  VAL B 119    11338  13556  11122   2395    183   1630       C  
ATOM   4649  C   VAL B 119      43.487 -29.701  28.863  1.00 94.46           C  
ANISOU 4649  C   VAL B 119    11236  13682  10971   2379    233   1776       C  
ATOM   4650  O   VAL B 119      42.633 -28.872  28.530  1.00 98.78           O  
ANISOU 4650  O   VAL B 119    11796  14126  11612   2162    252   1662       O  
ATOM   4651  CB  VAL B 119      44.771 -31.581  27.780  1.00 96.71           C  
ANISOU 4651  CB  VAL B 119    11740  13562  11445   2546    227   1978       C  
ATOM   4652  CG1 VAL B 119      43.403 -32.232  27.630  1.00 98.69           C  
ANISOU 4652  CG1 VAL B 119    12157  13484  11856   2408    309   2288       C  
ATOM   4653  CG2 VAL B 119      45.656 -31.924  26.590  1.00 99.21           C  
ANISOU 4653  CG2 VAL B 119    12169  13592  11935   2502    201   1844       C  
ATOM   4654  N   PHE B 120      43.458 -30.327  30.041  1.00 94.03           N  
ANISOU 4654  N   PHE B 120    11122  13890  10714   2625    263   2039       N  
ATOM   4655  CA  PHE B 120      42.357 -30.119  30.972  1.00 90.73           C  
ANISOU 4655  CA  PHE B 120    10660  13619  10192   2629    327   2217       C  
ATOM   4656  C   PHE B 120      42.299 -28.700  31.519  1.00 83.22           C  
ANISOU 4656  C   PHE B 120     9544  13004   9071   2571    307   1920       C  
ATOM   4657  O   PHE B 120      41.291 -28.335  32.132  1.00 91.43           O  
ANISOU 4657  O   PHE B 120    10558  14128  10055   2532    371   2025       O  
ATOM   4658  CB  PHE B 120      42.459 -31.115  32.129  1.00 96.70           C  
ANISOU 4658  CB  PHE B 120    11402  14592  10746   2933    374   2558       C  
ATOM   4659  CG  PHE B 120      42.103 -32.523  31.747  1.00 99.17           C  
ANISOU 4659  CG  PHE B 120    11920  14529  11230   2964    454   2919       C  
ATOM   4660  CD1 PHE B 120      43.061 -33.382  31.235  1.00101.66           C  
ANISOU 4660  CD1 PHE B 120    12330  14697  11599   3094    439   2968       C  
ATOM   4661  CD2 PHE B 120      40.808 -32.988  31.902  1.00104.16           C  
ANISOU 4661  CD2 PHE B 120    12654  14953  11968   2856    560   3206       C  
ATOM   4662  CE1 PHE B 120      42.732 -34.679  30.881  1.00104.80           C  
ANISOU 4662  CE1 PHE B 120    12947  14722  12149   3113    539   3294       C  
ATOM   4663  CE2 PHE B 120      40.473 -34.283  31.553  1.00109.68           C  
ANISOU 4663  CE2 PHE B 120    13557  15293  12823   2854    654   3521       C  
ATOM   4664  CZ  PHE B 120      41.437 -35.129  31.042  1.00106.32           C  
ANISOU 4664  CZ  PHE B 120    13251  14700  12445   2982    648   3564       C  
ATOM   4665  N   GLY B 121      43.337 -27.895  31.313  1.00 99.27           N  
ANISOU 4665  N   GLY B 121    11473  15223  11021   2556    236   1553       N  
ATOM   4666  CA  GLY B 121      43.281 -26.500  31.698  1.00105.55           C  
ANISOU 4666  CA  GLY B 121    12149  16279  11675   2457    241   1237       C  
ATOM   4667  C   GLY B 121      42.477 -25.679  30.712  1.00 96.44           C  
ANISOU 4667  C   GLY B 121    11095  14800  10747   2171    285   1081       C  
ATOM   4668  O   GLY B 121      41.645 -24.856  31.104  1.00102.72           O  
ANISOU 4668  O   GLY B 121    11865  15676  11488   2091    350   1037       O  
ATOM   4669  N   SER B 122      42.722 -25.901  29.421  1.00 99.69           N  
ANISOU 4669  N   SER B 122    11627  14843  11406   2030    257   1002       N  
ATOM   4670  CA  SER B 122      41.944 -25.229  28.386  1.00100.73           C  
ANISOU 4670  CA  SER B 122    11871  14645  11757   1776    293    884       C  
ATOM   4671  C   SER B 122      40.567 -25.861  28.231  1.00 88.76           C  
ANISOU 4671  C   SER B 122    10452  12875  10400   1705    338   1229       C  
ATOM   4672  O   SER B 122      39.584 -25.159  27.970  1.00 81.84           O  
ANISOU 4672  O   SER B 122     9596  11900   9599   1557    387   1200       O  
ATOM   4673  CB  SER B 122      42.703 -25.267  27.060  1.00 98.22           C  
ANISOU 4673  CB  SER B 122    11655  14030  11633   1656    247    680       C  
ATOM   4674  OG  SER B 122      44.032 -24.803  27.224  1.00 90.87           O  
ANISOU 4674  OG  SER B 122    10615  13350  10561   1724    209    376       O  
ATOM   4675  N   PHE B 123      40.481 -27.185  28.383  1.00 86.69           N  
ANISOU 4675  N   PHE B 123    10249  12506  10185   1808    333   1557       N  
ATOM   4676  CA  PHE B 123      39.193 -27.864  28.290  1.00 85.45           C  
ANISOU 4676  CA  PHE B 123    10175  12120  10172   1722    388   1886       C  
ATOM   4677  C   PHE B 123      38.189 -27.280  29.275  1.00 86.65           C  
ANISOU 4677  C   PHE B 123    10220  12511  10191   1744    460   1982       C  
ATOM   4678  O   PHE B 123      36.992 -27.193  28.977  1.00 82.88           O  
ANISOU 4678  O   PHE B 123     9771  11870   9850   1594    507   2111       O  
ATOM   4679  CB  PHE B 123      39.381 -29.362  28.536  1.00 85.70           C  
ANISOU 4679  CB  PHE B 123    10291  12049  10222   1861    405   2215       C  
ATOM   4680  CG  PHE B 123      38.157 -30.183  28.256  1.00 82.02           C  
ANISOU 4680  CG  PHE B 123     9936  11289   9939   1726    469   2531       C  
ATOM   4681  CD1 PHE B 123      37.708 -30.363  26.958  1.00 82.48           C  
ANISOU 4681  CD1 PHE B 123    10127  10954  10259   1480    447   2504       C  
ATOM   4682  CD2 PHE B 123      37.458 -30.779  29.292  1.00 84.04           C  
ANISOU 4682  CD2 PHE B 123    10163  11671  10097   1836    556   2850       C  
ATOM   4683  CE1 PHE B 123      36.580 -31.120  26.699  1.00 82.50           C  
ANISOU 4683  CE1 PHE B 123    10215  10710  10422   1328    503   2776       C  
ATOM   4684  CE2 PHE B 123      36.331 -31.537  29.041  1.00 87.14           C  
ANISOU 4684  CE2 PHE B 123    10647  11801  10661   1685    628   3128       C  
ATOM   4685  CZ  PHE B 123      35.891 -31.708  27.743  1.00 82.52           C  
ANISOU 4685  CZ  PHE B 123    10178  10840  10336   1422    597   3085       C  
ATOM   4686  N   LEU B 124      38.659 -26.870  30.454  1.00 92.20           N  
ANISOU 4686  N   LEU B 124    10793  13617  10621   1931    472   1920       N  
ATOM   4687  CA  LEU B 124      37.787 -26.200  31.413  1.00 88.26           C  
ANISOU 4687  CA  LEU B 124    10201  13360   9975   1960    552   1976       C  
ATOM   4688  C   LEU B 124      37.312 -24.859  30.868  1.00 86.35           C  
ANISOU 4688  C   LEU B 124     9951  13065   9795   1779    581   1705       C  
ATOM   4689  O   LEU B 124      36.107 -24.598  30.784  1.00 90.10           O  
ANISOU 4689  O   LEU B 124    10430  13443  10360   1680    650   1832       O  
ATOM   4690  CB  LEU B 124      38.520 -26.015  32.743  1.00 89.16           C  
ANISOU 4690  CB  LEU B 124    10189  13926   9760   2196    550   1927       C  
ATOM   4691  CG  LEU B 124      37.794 -25.191  33.809  1.00 91.91           C  
ANISOU 4691  CG  LEU B 124    10446  14564   9911   2240    638   1930       C  
ATOM   4692  CD1 LEU B 124      36.510 -25.880  34.248  1.00 97.42           C  
ANISOU 4692  CD1 LEU B 124    11171  15171  10673   2257    731   2327       C  
ATOM   4693  CD2 LEU B 124      38.706 -24.941  35.001  1.00 97.85           C  
ANISOU 4693  CD2 LEU B 124    11081  15776  10324   2454    612   1814       C  
ATOM   4694  N   THR B 125      38.255 -23.991  30.495  1.00 84.20           N  
ANISOU 4694  N   THR B 125     9664  12857   9469   1740    543   1333       N  
ATOM   4695  CA  THR B 125      37.890 -22.667  30.003  1.00 82.77           C  
ANISOU 4695  CA  THR B 125     9502  12619   9326   1588    598   1062       C  
ATOM   4696  C   THR B 125      36.954 -22.759  28.803  1.00 83.82           C  
ANISOU 4696  C   THR B 125     9744  12363   9742   1403    603   1157       C  
ATOM   4697  O   THR B 125      36.043 -21.937  28.652  1.00 80.49           O  
ANISOU 4697  O   THR B 125     9326  11903   9354   1321    679   1126       O  
ATOM   4698  CB  THR B 125      39.152 -21.885  29.636  1.00 80.83           C  
ANISOU 4698  CB  THR B 125     9252  12446   9013   1551    565    649       C  
ATOM   4699  OG1 THR B 125      40.109 -21.988  30.698  1.00 80.92           O  
ANISOU 4699  OG1 THR B 125     9142  12841   8764   1721    531    576       O  
ATOM   4700  CG2 THR B 125      38.823 -20.422  29.399  1.00 83.15           C  
ANISOU 4700  CG2 THR B 125     9575  12734   9283   1427    663    362       C  
ATOM   4701  N   LEU B 126      37.162 -23.755  27.940  1.00 85.09           N  
ANISOU 4701  N   LEU B 126     9996  12238  10096   1343    527   1273       N  
ATOM   4702  CA  LEU B 126      36.304 -23.923  26.772  1.00 74.61           C  
ANISOU 4702  CA  LEU B 126     8770  10554   9024   1156    515   1359       C  
ATOM   4703  C   LEU B 126      34.861 -24.183  27.188  1.00 76.94           C  
ANISOU 4703  C   LEU B 126     9014  10860   9359   1130    576   1669       C  
ATOM   4704  O   LEU B 126      33.946 -23.442  26.812  1.00 77.51           O  
ANISOU 4704  O   LEU B 126     9075  10877   9498   1031    620   1642       O  
ATOM   4705  CB  LEU B 126      36.834 -25.061  25.896  1.00 73.31           C  
ANISOU 4705  CB  LEU B 126     8723  10098   9034   1103    432   1441       C  
ATOM   4706  CG  LEU B 126      35.945 -25.477  24.724  1.00 69.98           C  
ANISOU 4706  CG  LEU B 126     8411   9310   8866    901    406   1565       C  
ATOM   4707  CD1 LEU B 126      35.666 -24.288  23.825  1.00 74.42           C  
ANISOU 4707  CD1 LEU B 126     9012   9763   9502    769    412   1310       C  
ATOM   4708  CD2 LEU B 126      36.591 -26.601  23.931  1.00 58.06           C  
ANISOU 4708  CD2 LEU B 126     7041   7517   7502    857    341   1624       C  
ATOM   4709  N   ASN B 127      34.639 -25.241  27.970  1.00 78.48           N  
ANISOU 4709  N   ASN B 127     9176  11132   9510   1227    591   1974       N  
ATOM   4710  CA  ASN B 127      33.283 -25.608  28.356  1.00 74.72           C  
ANISOU 4710  CA  ASN B 127     8648  10657   9087   1186    659   2282       C  
ATOM   4711  C   ASN B 127      32.638 -24.580  29.274  1.00 82.61           C  
ANISOU 4711  C   ASN B 127     9526  11944   9917   1265    757   2256       C  
ATOM   4712  O   ASN B 127      31.407 -24.496  29.317  1.00 83.92           O  
ANISOU 4712  O   ASN B 127     9637  12094  10156   1195    820   2436       O  
ATOM   4713  CB  ASN B 127      33.287 -26.974  29.040  1.00 76.03           C  
ANISOU 4713  CB  ASN B 127     8829  10831   9227   1284    681   2606       C  
ATOM   4714  CG  ASN B 127      33.636 -28.098  28.091  1.00 76.31           C  
ANISOU 4714  CG  ASN B 127     9010  10527   9457   1182    619   2691       C  
ATOM   4715  OD1 ASN B 127      32.759 -28.691  27.464  1.00 78.80           O  
ANISOU 4715  OD1 ASN B 127     9378  10598   9965   1004    628   2865       O  
ATOM   4716  ND2 ASN B 127      34.925 -28.396  27.977  1.00 76.28           N  
ANISOU 4716  ND2 ASN B 127     9069  10516   9398   1291    562   2562       N  
ATOM   4717  N   MET B 128      33.431 -23.797  30.008  1.00 89.59           N  
ANISOU 4717  N   MET B 128    10366  13100  10575   1402    778   2034       N  
ATOM   4718  CA  MET B 128      32.844 -22.799  30.894  1.00 90.92           C  
ANISOU 4718  CA  MET B 128    10445  13531  10571   1475    889   1996       C  
ATOM   4719  C   MET B 128      32.367 -21.582  30.110  1.00 89.88           C  
ANISOU 4719  C   MET B 128    10340  13290  10519   1355    933   1780       C  
ATOM   4720  O   MET B 128      31.291 -21.045  30.391  1.00 90.45           O  
ANISOU 4720  O   MET B 128    10357  13429  10582   1356   1033   1881       O  
ATOM   4721  CB  MET B 128      33.849 -22.384  31.969  1.00 93.87           C  
ANISOU 4721  CB  MET B 128    10769  14243  10655   1647    901   1819       C  
ATOM   4722  CG  MET B 128      33.281 -21.432  33.017  1.00 96.95           C  
ANISOU 4722  CG  MET B 128    11084  14916  10835   1734   1030   1789       C  
ATOM   4723  SD  MET B 128      31.777 -22.038  33.809  1.00 98.49           S  
ANISOU 4723  SD  MET B 128    11207  15167  11046   1789   1137   2233       S  
ATOM   4724  CE  MET B 128      32.457 -23.176  35.012  1.00105.01           C  
ANISOU 4724  CE  MET B 128    12003  16227  11669   1999   1108   2443       C  
ATOM   4725  N   PHE B 129      33.150 -21.134  29.126  1.00 89.33           N  
ANISOU 4725  N   PHE B 129    10361  13053  10528   1266    873   1490       N  
ATOM   4726  CA  PHE B 129      32.668 -20.086  28.233  1.00 88.88           C  
ANISOU 4726  CA  PHE B 129    10361  12841  10568   1157    921   1315       C  
ATOM   4727  C   PHE B 129      31.423 -20.544  27.484  1.00 87.68           C  
ANISOU 4727  C   PHE B 129    10202  12477  10635   1043    902   1570       C  
ATOM   4728  O   PHE B 129      30.444 -19.797  27.375  1.00 92.13           O  
ANISOU 4728  O   PHE B 129    10732  13058  11215   1030    987   1601       O  
ATOM   4729  CB  PHE B 129      33.761 -19.679  27.245  1.00 88.86           C  
ANISOU 4729  CB  PHE B 129    10474  12663  10626   1075    863    981       C  
ATOM   4730  CG  PHE B 129      34.702 -18.631  27.772  1.00 88.76           C  
ANISOU 4730  CG  PHE B 129    10466  12855  10405   1134    932    637       C  
ATOM   4731  CD1 PHE B 129      34.249 -17.352  28.052  1.00 91.43           C  
ANISOU 4731  CD1 PHE B 129    10818  13289  10633   1148   1078    484       C  
ATOM   4732  CD2 PHE B 129      36.041 -18.920  27.973  1.00 82.57           C  
ANISOU 4732  CD2 PHE B 129     9673  12169   9531   1170    860    460       C  
ATOM   4733  CE1 PHE B 129      35.112 -16.384  28.534  1.00 86.98           C  
ANISOU 4733  CE1 PHE B 129    10273  12901   9872   1171   1158    147       C  
ATOM   4734  CE2 PHE B 129      36.909 -17.956  28.453  1.00 79.94           C  
ANISOU 4734  CE2 PHE B 129     9328  12045   9002   1193    922    124       C  
ATOM   4735  CZ  PHE B 129      36.444 -16.687  28.734  1.00 85.65           C  
ANISOU 4735  CZ  PHE B 129    10080  12847   9616   1180   1074    -41       C  
ATOM   4736  N   ALA B 130      31.441 -21.772  26.961  1.00 84.00           N  
ANISOU 4736  N   ALA B 130     9767  11818  10332    959    798   1752       N  
ATOM   4737  CA  ALA B 130      30.260 -22.308  26.294  1.00 87.25           C  
ANISOU 4737  CA  ALA B 130    10157  12052  10941    823    773   1994       C  
ATOM   4738  C   ALA B 130      29.056 -22.297  27.228  1.00 88.17           C  
ANISOU 4738  C   ALA B 130    10129  12374  10997    881    876   2259       C  
ATOM   4739  O   ALA B 130      27.955 -21.893  26.837  1.00 88.57           O  
ANISOU 4739  O   ALA B 130    10118  12403  11134    814    911   2345       O  
ATOM   4740  CB  ALA B 130      30.542 -23.726  25.795  1.00 83.36           C  
ANISOU 4740  CB  ALA B 130     9734  11337  10600    726    671   2153       C  
ATOM   4741  N   SER B 131      29.250 -22.731  28.476  1.00 90.69           N  
ANISOU 4741  N   SER B 131    10390  12908  11159   1018    929   2396       N  
ATOM   4742  CA  SER B 131      28.155 -22.719  29.440  1.00 83.96           C  
ANISOU 4742  CA  SER B 131     9407  12258  10235   1086   1044   2648       C  
ATOM   4743  C   SER B 131      27.663 -21.300  29.696  1.00 80.02           C  
ANISOU 4743  C   SER B 131     8858  11922   9626   1158   1157   2506       C  
ATOM   4744  O   SER B 131      26.455 -21.064  29.813  1.00 78.81           O  
ANISOU 4744  O   SER B 131     8602  11829   9515   1147   1238   2683       O  
ATOM   4745  CB  SER B 131      28.597 -23.377  30.747  1.00 87.50           C  
ANISOU 4745  CB  SER B 131     9829  12912  10504   1246   1086   2794       C  
ATOM   4746  OG  SER B 131      27.557 -23.349  31.709  1.00 83.98           O  
ANISOU 4746  OG  SER B 131     9268  12660   9982   1317   1213   3035       O  
ATOM   4747  N   ILE B 132      28.585 -20.339  29.785  1.00 81.66           N  
ANISOU 4747  N   ILE B 132     9137  12202   9688   1232   1177   2185       N  
ATOM   4748  CA  ILE B 132      28.190 -18.957  30.035  1.00 80.17           C  
ANISOU 4748  CA  ILE B 132     8940  12142   9380   1304   1314   2031       C  
ATOM   4749  C   ILE B 132      27.536 -18.360  28.796  1.00 78.33           C  
ANISOU 4749  C   ILE B 132     8740  11702   9319   1200   1311   1971       C  
ATOM   4750  O   ILE B 132      26.594 -17.565  28.896  1.00 72.83           O  
ANISOU 4750  O   ILE B 132     7992  11082   8597   1252   1432   2022       O  
ATOM   4751  CB  ILE B 132      29.406 -18.127  30.489  1.00 80.05           C  
ANISOU 4751  CB  ILE B 132     9005  12257   9155   1384   1350   1684       C  
ATOM   4752  CG1 ILE B 132      29.943 -18.656  31.821  1.00 79.71           C  
ANISOU 4752  CG1 ILE B 132     8904  12481   8903   1515   1354   1762       C  
ATOM   4753  CG2 ILE B 132      29.027 -16.654  30.609  1.00 79.35           C  
ANISOU 4753  CG2 ILE B 132     8952  12243   8954   1436   1515   1497       C  
ATOM   4754  CD1 ILE B 132      31.313 -18.118  32.189  1.00 82.19           C  
ANISOU 4754  CD1 ILE B 132     9272  12937   9020   1564   1339   1421       C  
ATOM   4755  N   PHE B 133      28.021 -18.731  27.610  1.00 84.24           N  
ANISOU 4755  N   PHE B 133     9579  12193  10234   1067   1179   1869       N  
ATOM   4756  CA  PHE B 133      27.415 -18.226  26.385  1.00 78.77           C  
ANISOU 4756  CA  PHE B 133     8927  11309   9695    976   1163   1822       C  
ATOM   4757  C   PHE B 133      26.011 -18.785  26.192  1.00 80.60           C  
ANISOU 4757  C   PHE B 133     9017  11544  10065    911   1147   2151       C  
ATOM   4758  O   PHE B 133      25.142 -18.094  25.648  1.00 88.81           O  
ANISOU 4758  O   PHE B 133    10020  12571  11153    913   1194   2172       O  
ATOM   4759  CB  PHE B 133      28.287 -18.570  25.177  1.00 81.86           C  
ANISOU 4759  CB  PHE B 133     9457  11423  10224    846   1024   1643       C  
ATOM   4760  CG  PHE B 133      29.631 -17.886  25.172  1.00 85.83           C  
ANISOU 4760  CG  PHE B 133    10089  11910  10611    887   1048   1287       C  
ATOM   4761  CD1 PHE B 133      29.869 -16.762  25.950  1.00 88.33           C  
ANISOU 4761  CD1 PHE B 133    10418  12416  10727   1005   1198   1100       C  
ATOM   4762  CD2 PHE B 133      30.656 -18.368  24.377  1.00 81.88           C  
ANISOU 4762  CD2 PHE B 133     9700  11205  10204    795    931   1133       C  
ATOM   4763  CE1 PHE B 133      31.101 -16.137  25.932  1.00 87.18           C  
ANISOU 4763  CE1 PHE B 133    10381  12267  10478   1010   1226    755       C  
ATOM   4764  CE2 PHE B 133      31.890 -17.747  24.359  1.00 84.09           C  
ANISOU 4764  CE2 PHE B 133    10078  11487  10385    819    957    801       C  
ATOM   4765  CZ  PHE B 133      32.112 -16.630  25.138  1.00 83.32           C  
ANISOU 4765  CZ  PHE B 133     9979  11590  10090    916   1103    607       C  
ATOM   4766  N   PHE B 134      25.766 -20.023  26.631  1.00 79.86           N  
ANISOU 4766  N   PHE B 134     8841  11473  10029    855   1092   2410       N  
ATOM   4767  CA  PHE B 134      24.432 -20.599  26.512  1.00 79.57           C  
ANISOU 4767  CA  PHE B 134     8653  11456  10123    765   1089   2717       C  
ATOM   4768  C   PHE B 134      23.467 -20.020  27.539  1.00 75.94           C  
ANISOU 4768  C   PHE B 134     8044  11268   9544    904   1252   2876       C  
ATOM   4769  O   PHE B 134      22.273 -19.889  27.250  1.00 81.18           O  
ANISOU 4769  O   PHE B 134     8571  11981  10294    864   1282   3046       O  
ATOM   4770  CB  PHE B 134      24.494 -22.122  26.655  1.00 85.29           C  
ANISOU 4770  CB  PHE B 134     9366  12092  10950    646   1009   2937       C  
ATOM   4771  CG  PHE B 134      24.943 -22.830  25.406  1.00 81.79           C  
ANISOU 4771  CG  PHE B 134     9041  11350  10684    461    854   2866       C  
ATOM   4772  CD1 PHE B 134      24.209 -22.728  24.235  1.00 76.96           C  
ANISOU 4772  CD1 PHE B 134     8405  10607  10231    307    779   2873       C  
ATOM   4773  CD2 PHE B 134      26.095 -23.598  25.403  1.00 78.97           C  
ANISOU 4773  CD2 PHE B 134     8821  10858  10327    451    787   2795       C  
ATOM   4774  CE1 PHE B 134      24.617 -23.376  23.086  1.00 73.88           C  
ANISOU 4774  CE1 PHE B 134     8139   9941   9992    131    641   2801       C  
ATOM   4775  CE2 PHE B 134      26.510 -24.248  24.257  1.00 78.52           C  
ANISOU 4775  CE2 PHE B 134     8889  10514  10429    287    661   2731       C  
ATOM   4776  CZ  PHE B 134      25.770 -24.137  23.096  1.00 78.58           C  
ANISOU 4776  CZ  PHE B 134     8887  10379  10592    118    589   2729       C  
ATOM   4777  N   ILE B 135      23.954 -19.666  28.730  1.00 76.87           N  
ANISOU 4777  N   ILE B 135     8177  11576   9456   1068   1360   2823       N  
ATOM   4778  CA  ILE B 135      23.111 -18.947  29.681  1.00 74.73           C  
ANISOU 4778  CA  ILE B 135     7794  11551   9050   1217   1537   2934       C  
ATOM   4779  C   ILE B 135      22.584 -17.668  29.047  1.00 73.85           C  
ANISOU 4779  C   ILE B 135     7692  11429   8940   1268   1615   2802       C  
ATOM   4780  O   ILE B 135      21.437 -17.266  29.278  1.00 80.51           O  
ANISOU 4780  O   ILE B 135     8400  12406   9782   1334   1727   2977       O  
ATOM   4781  CB  ILE B 135      23.890 -18.655  30.976  1.00 73.34           C  
ANISOU 4781  CB  ILE B 135     7671  11572   8625   1381   1632   2834       C  
ATOM   4782  CG1 ILE B 135      24.045 -19.933  31.802  1.00 76.27           C  
ANISOU 4782  CG1 ILE B 135     7995  12011   8974   1382   1598   3067       C  
ATOM   4783  CG2 ILE B 135      23.185 -17.577  31.789  1.00 68.35           C  
ANISOU 4783  CG2 ILE B 135     6981  11158   7831   1542   1833   2851       C  
ATOM   4784  CD1 ILE B 135      25.089 -19.828  32.898  1.00 78.87           C  
ANISOU 4784  CD1 ILE B 135     8393  12518   9057   1532   1633   2938       C  
ATOM   4785  N   THR B 136      23.413 -17.008  28.237  1.00 78.88           N  
ANISOU 4785  N   THR B 136     8491  11904   9576   1250   1572   2499       N  
ATOM   4786  CA  THR B 136      22.964 -15.808  27.540  1.00 82.04           C  
ANISOU 4786  CA  THR B 136     8935  12258   9977   1309   1658   2373       C  
ATOM   4787  C   THR B 136      21.952 -16.153  26.455  1.00 78.69           C  
ANISOU 4787  C   THR B 136     8405  11739   9756   1201   1561   2553       C  
ATOM   4788  O   THR B 136      20.937 -15.464  26.303  1.00 81.29           O  
ANISOU 4788  O   THR B 136     8643  12161  10083   1289   1659   2652       O  
ATOM   4789  CB  THR B 136      24.162 -15.072  26.941  1.00 76.68           C  
ANISOU 4789  CB  THR B 136     8474  11412   9248   1303   1649   2000       C  
ATOM   4790  OG1 THR B 136      25.096 -14.754  27.980  1.00 62.24           O  
ANISOU 4790  OG1 THR B 136     6719   9712   7218   1386   1732   1821       O  
ATOM   4791  CG2 THR B 136      23.713 -13.794  26.251  1.00 84.52           C  
ANISOU 4791  CG2 THR B 136     9547  12340  10226   1386   1771   1874       C  
ATOM   4792  N   CYS B 137      22.214 -17.215  25.688  1.00 73.40           N  
ANISOU 4792  N   CYS B 137     7745  10892   9253   1012   1372   2595       N  
ATOM   4793  CA  CYS B 137      21.243 -17.661  24.697  1.00 77.36           C  
ANISOU 4793  CA  CYS B 137     8130  11325   9937    877   1264   2766       C  
ATOM   4794  C   CYS B 137      19.905 -17.993  25.342  1.00 76.88           C  
ANISOU 4794  C   CYS B 137     7822  11491   9899    890   1333   3093       C  
ATOM   4795  O   CYS B 137      18.851 -17.781  24.732  1.00 73.70           O  
ANISOU 4795  O   CYS B 137     7278  11145   9578    867   1319   3219       O  
ATOM   4796  CB  CYS B 137      21.784 -18.874  23.939  1.00 78.51           C  
ANISOU 4796  CB  CYS B 137     8343  11245  10242    656   1068   2764       C  
ATOM   4797  SG  CYS B 137      23.169 -18.502  22.837  1.00 69.08           S  
ANISOU 4797  SG  CYS B 137     7420   9761   9068    614    972   2398       S  
ATOM   4798  N   MET B 138      19.925 -18.507  26.574  1.00 78.99           N  
ANISOU 4798  N   MET B 138     8025  11901  10088    934   1411   3236       N  
ATOM   4799  CA  MET B 138      18.680 -18.818  27.265  1.00 75.15           C  
ANISOU 4799  CA  MET B 138     7305  11630   9618    949   1502   3547       C  
ATOM   4800  C   MET B 138      17.908 -17.550  27.610  1.00 75.16           C  
ANISOU 4800  C   MET B 138     7225  11829   9505   1160   1681   3564       C  
ATOM   4801  O   MET B 138      16.683 -17.499  27.448  1.00 81.04           O  
ANISOU 4801  O   MET B 138     7760  12710  10320   1157   1715   3775       O  
ATOM   4802  CB  MET B 138      18.971 -19.620  28.534  1.00 72.44           C  
ANISOU 4802  CB  MET B 138     6948  11379   9195    972   1563   3686       C  
ATOM   4803  CG  MET B 138      19.289 -21.088  28.298  1.00 72.70           C  
ANISOU 4803  CG  MET B 138     7006  11249   9367    763   1427   3796       C  
ATOM   4804  SD  MET B 138      17.959 -21.974  27.460  1.00 96.51           S  
ANISOU 4804  SD  MET B 138     9815  14229  12624    504   1339   4055       S  
ATOM   4805  CE  MET B 138      16.550 -21.564  28.492  1.00 94.69           C  
ANISOU 4805  CE  MET B 138     9318  14332  12330    631   1539   4329       C  
ATOM   4806  N   SER B 139      18.606 -16.518  28.088  1.00 74.38           N  
ANISOU 4806  N   SER B 139     7285  11752   9224   1342   1807   3342       N  
ATOM   4807  CA  SER B 139      17.931 -15.280  28.461  1.00 75.39           C  
ANISOU 4807  CA  SER B 139     7376  12043   9227   1557   2011   3349       C  
ATOM   4808  C   SER B 139      17.393 -14.540  27.243  1.00 76.52           C  
ANISOU 4808  C   SER B 139     7513  12112   9448   1584   1990   3298       C  
ATOM   4809  O   SER B 139      16.357 -13.871  27.336  1.00 83.95           O  
ANISOU 4809  O   SER B 139     8325  13215  10359   1730   2124   3438       O  
ATOM   4810  CB  SER B 139      18.882 -14.383  29.252  1.00 79.91           C  
ANISOU 4810  CB  SER B 139     8150  12635   9576   1714   2159   3094       C  
ATOM   4811  OG  SER B 139      19.238 -14.987  30.484  1.00 85.63           O  
ANISOU 4811  OG  SER B 139     8855  13487  10194   1730   2194   3171       O  
ATOM   4812  N   VAL B 140      18.072 -14.641  26.100  1.00 82.61           N  
ANISOU 4812  N   VAL B 140     8425  12650  10312   1462   1832   3107       N  
ATOM   4813  CA  VAL B 140      17.561 -14.010  24.887  1.00 89.97           C  
ANISOU 4813  CA  VAL B 140     9360  13513  11313   1491   1798   3071       C  
ATOM   4814  C   VAL B 140      16.329 -14.750  24.380  1.00 90.28           C  
ANISOU 4814  C   VAL B 140     9126  13666  11511   1371   1679   3360       C  
ATOM   4815  O   VAL B 140      15.357 -14.129  23.933  1.00 98.57           O  
ANISOU 4815  O   VAL B 140    10048  14838  12565   1484   1730   3467       O  
ATOM   4816  CB  VAL B 140      18.661 -13.940  23.812  1.00 95.70           C  
ANISOU 4816  CB  VAL B 140    10324  13950  12087   1390   1668   2784       C  
ATOM   4817  CG1 VAL B 140      18.067 -13.522  22.475  1.00 94.95           C  
ANISOU 4817  CG1 VAL B 140    10217  13783  12076   1395   1598   2787       C  
ATOM   4818  CG2 VAL B 140      19.754 -12.975  24.237  1.00 97.35           C  
ANISOU 4818  CG2 VAL B 140    10784  14075  12128   1517   1819   2480       C  
ATOM   4819  N   ASP B 141      16.349 -16.084  24.432  1.00 82.73           N  
ANISOU 4819  N   ASP B 141     8074  12677  10682   1141   1527   3488       N  
ATOM   4820  CA  ASP B 141      15.202 -16.853  23.957  1.00 87.66           C  
ANISOU 4820  CA  ASP B 141     8436  13410  11460    980   1415   3742       C  
ATOM   4821  C   ASP B 141      13.959 -16.537  24.779  1.00 86.01           C  
ANISOU 4821  C   ASP B 141     7965  13511  11203   1121   1581   4003       C  
ATOM   4822  O   ASP B 141      12.859 -16.401  24.229  1.00 80.27           O  
ANISOU 4822  O   ASP B 141     7017  12939  10541   1119   1553   4159       O  
ATOM   4823  CB  ASP B 141      15.513 -18.349  24.007  1.00 86.09           C  
ANISOU 4823  CB  ASP B 141     8222  13095  11392    705   1268   3824       C  
ATOM   4824  CG  ASP B 141      14.653 -19.155  23.050  1.00 89.56           C  
ANISOU 4824  CG  ASP B 141     8476  13541  12010    460   1100   3972       C  
ATOM   4825  OD1 ASP B 141      14.921 -19.114  21.829  1.00 87.59           O  
ANISOU 4825  OD1 ASP B 141     8326  13126  11828    363    947   3828       O  
ATOM   4826  OD2 ASP B 141      13.707 -19.826  23.516  1.00 92.37           O  
ANISOU 4826  OD2 ASP B 141     8591  14072  12434    355   1125   4226       O  
ATOM   4827  N   ARG B 142      14.113 -16.414  26.099  1.00 81.64           N  
ANISOU 4827  N   ARG B 142     7426  13066  10527   1249   1754   4053       N  
ATOM   4828  CA  ARG B 142      12.982 -16.036  26.939  1.00 87.01           C  
ANISOU 4828  CA  ARG B 142     7880  14033  11147   1408   1941   4292       C  
ATOM   4829  C   ARG B 142      12.530 -14.615  26.631  1.00 86.26           C  
ANISOU 4829  C   ARG B 142     7798  14029  10949   1674   2082   4235       C  
ATOM   4830  O   ARG B 142      11.330 -14.317  26.658  1.00 90.95           O  
ANISOU 4830  O   ARG B 142     8147  14852  11556   1774   2165   4451       O  
ATOM   4831  CB  ARG B 142      13.356 -16.171  28.414  1.00 87.96           C  
ANISOU 4831  CB  ARG B 142     8056  14231  11135   1500   2101   4334       C  
ATOM   4832  CG  ARG B 142      13.373 -17.601  28.926  1.00 89.63           C  
ANISOU 4832  CG  ARG B 142     8183  14433  11441   1286   2024   4506       C  
ATOM   4833  CD  ARG B 142      13.507 -17.641  30.441  1.00105.70           C  
ANISOU 4833  CD  ARG B 142    10237  16601  13322   1423   2209   4597       C  
ATOM   4834  NE  ARG B 142      13.418 -19.001  30.965  1.00111.47           N  
ANISOU 4834  NE  ARG B 142    10889  17327  14137   1243   2168   4796       N  
ATOM   4835  CZ  ARG B 142      13.496 -19.315  32.254  1.00113.21           C  
ANISOU 4835  CZ  ARG B 142    11118  17656  14241   1330   2308   4918       C  
ATOM   4836  NH1 ARG B 142      13.667 -18.366  33.164  1.00109.65           N  
ANISOU 4836  NH1 ARG B 142    10743  17338  13580   1580   2488   4850       N  
ATOM   4837  NH2 ARG B 142      13.404 -20.582  32.636  1.00114.86           N  
ANISOU 4837  NH2 ARG B 142    11275  17833  14535   1165   2280   5107       N  
ATOM   4838  N   TYR B 143      13.479 -13.723  26.336  1.00 86.23           N  
ANISOU 4838  N   TYR B 143     8080  13847  10838   1794   2127   3949       N  
ATOM   4839  CA  TYR B 143      13.123 -12.361  25.956  1.00 85.69           C  
ANISOU 4839  CA  TYR B 143     8074  13815  10668   2050   2281   3881       C  
ATOM   4840  C   TYR B 143      12.338 -12.341  24.651  1.00 90.11           C  
ANISOU 4840  C   TYR B 143     8485  14404  11348   2015   2141   3970       C  
ATOM   4841  O   TYR B 143      11.408 -11.543  24.491  1.00 91.25           O  
ANISOU 4841  O   TYR B 143     8505  14721  11443   2229   2265   4096       O  
ATOM   4842  CB  TYR B 143      14.389 -11.511  25.838  1.00 91.44           C  
ANISOU 4842  CB  TYR B 143     9162  14311  11272   2136   2355   3532       C  
ATOM   4843  CG  TYR B 143      14.158 -10.107  25.330  1.00 91.15           C  
ANISOU 4843  CG  TYR B 143     9257  14246  11132   2388   2530   3430       C  
ATOM   4844  CD1 TYR B 143      13.722  -9.102  26.183  1.00 93.00           C  
ANISOU 4844  CD1 TYR B 143     9516  14619  11200   2654   2819   3474       C  
ATOM   4845  CD2 TYR B 143      14.385  -9.782  23.999  1.00 88.53           C  
ANISOU 4845  CD2 TYR B 143     9045  13734  10857   2370   2423   3292       C  
ATOM   4846  CE1 TYR B 143      13.514  -7.816  25.725  1.00 94.53           C  
ANISOU 4846  CE1 TYR B 143     9858  14764  11293   2900   3008   3389       C  
ATOM   4847  CE2 TYR B 143      14.180  -8.498  23.532  1.00 91.97           C  
ANISOU 4847  CE2 TYR B 143     9625  14129  11189   2620   2604   3210       C  
ATOM   4848  CZ  TYR B 143      13.747  -7.518  24.400  1.00 91.55           C  
ANISOU 4848  CZ  TYR B 143     9603  14206  10976   2886   2903   3261       C  
ATOM   4849  OH  TYR B 143      13.537  -6.238  23.943  1.00108.90           O  
ANISOU 4849  OH  TYR B 143    11970  16342  13064   3151   3112   3188       O  
ATOM   4850  N   GLN B 144      12.698 -13.210  23.702  1.00 87.34           N  
ANISOU 4850  N   GLN B 144     8146  13895  11143   1757   1886   3909       N  
ATOM   4851  CA  GLN B 144      11.915 -13.312  22.474  1.00 88.27           C  
ANISOU 4851  CA  GLN B 144     8101  14070  11368   1694   1728   4001       C  
ATOM   4852  C   GLN B 144      10.510 -13.828  22.758  1.00 95.50           C  
ANISOU 4852  C   GLN B 144     8620  15307  12360   1649   1719   4332       C  
ATOM   4853  O   GLN B 144       9.540 -13.386  22.131  1.00 98.85           O  
ANISOU 4853  O   GLN B 144     8849  15919  12790   1757   1707   4459       O  
ATOM   4854  CB  GLN B 144      12.618 -14.224  21.468  1.00 84.65           C  
ANISOU 4854  CB  GLN B 144     7751  13367  11045   1401   1462   3863       C  
ATOM   4855  CG  GLN B 144      13.836 -13.605  20.803  1.00 94.57           C  
ANISOU 4855  CG  GLN B 144     9365  14322  12245   1451   1450   3541       C  
ATOM   4856  CD  GLN B 144      14.337 -14.425  19.627  1.00 93.75           C  
ANISOU 4856  CD  GLN B 144     9346  13997  12277   1187   1191   3431       C  
ATOM   4857  OE1 GLN B 144      13.550 -15.037  18.903  1.00 84.75           O  
ANISOU 4857  OE1 GLN B 144     8004  12949  11247   1031   1024   3576       O  
ATOM   4858  NE2 GLN B 144      15.651 -14.443  19.433  1.00 88.20           N  
ANISOU 4858  NE2 GLN B 144     8939  13010  11563   1128   1161   3168       N  
ATOM   4859  N   SER B 145      10.380 -14.763  23.702  1.00101.83           N  
ANISOU 4859  N   SER B 145     9291  16185  13214   1496   1730   4477       N  
ATOM   4860  CA  SER B 145       9.066 -15.317  24.009  1.00 99.96           C  
ANISOU 4860  CA  SER B 145     8672  16247  13060   1420   1736   4786       C  
ATOM   4861  C   SER B 145       8.170 -14.290  24.687  1.00101.35           C  
ANISOU 4861  C   SER B 145     8696  16699  13115   1747   1985   4945       C  
ATOM   4862  O   SER B 145       6.948 -14.318  24.501  1.00103.68           O  
ANISOU 4862  O   SER B 145     8658  17274  13461   1768   1985   5174       O  
ATOM   4863  CB  SER B 145       9.207 -16.555  24.894  1.00100.56           C  
ANISOU 4863  CB  SER B 145     8689  16305  13215   1186   1722   4899       C  
ATOM   4864  OG  SER B 145       9.999 -17.543  24.260  1.00107.55           O  
ANISOU 4864  OG  SER B 145     9721  16930  14215    895   1510   4769       O  
ATOM   4865  N   VAL B 146       8.751 -13.383  25.470  1.00 97.43           N  
ANISOU 4865  N   VAL B 146     8433  16135  12452   1999   2204   4826       N  
ATOM   4866  CA  VAL B 146       7.948 -12.401  26.189  1.00100.73           C  
ANISOU 4866  CA  VAL B 146     8744  16788  12741   2319   2472   4973       C  
ATOM   4867  C   VAL B 146       7.566 -11.247  25.273  1.00105.38           C  
ANISOU 4867  C   VAL B 146     9363  17414  13264   2573   2523   4931       C  
ATOM   4868  O   VAL B 146       6.409 -10.811  25.248  1.00106.10           O  
ANISOU 4868  O   VAL B 146     9193  17782  13339   2757   2621   5153       O  
ATOM   4869  CB  VAL B 146       8.709 -11.905  27.433  1.00100.50           C  
ANISOU 4869  CB  VAL B 146     8967  16675  12544   2474   2699   4854       C  
ATOM   4870  CG1 VAL B 146       7.985 -10.725  28.064  1.00 96.60           C  
ANISOU 4870  CG1 VAL B 146     8434  16374  11897   2830   3001   4963       C  
ATOM   4871  CG2 VAL B 146       8.881 -13.036  28.436  1.00104.94           C  
ANISOU 4871  CG2 VAL B 146     9457  17264  13152   2275   2675   4960       C  
ATOM   4872  N   ILE B 147       8.530 -10.732  24.505  1.00101.72           N  
ANISOU 4872  N   ILE B 147     9217  16675  12756   2599   2468   4654       N  
ATOM   4873  CA  ILE B 147       8.233  -9.615  23.617  1.00 99.33           C  
ANISOU 4873  CA  ILE B 147     8989  16375  12378   2858   2536   4609       C  
ATOM   4874  C   ILE B 147       7.388 -10.074  22.437  1.00 95.40           C  
ANISOU 4874  C   ILE B 147     8211  16032  12005   2750   2300   4755       C  
ATOM   4875  O   ILE B 147       6.563  -9.308  21.923  1.00103.72           O  
ANISOU 4875  O   ILE B 147     9141  17266  13001   3000   2370   4875       O  
ATOM   4876  CB  ILE B 147       9.534  -8.941  23.141  1.00 99.64           C  
ANISOU 4876  CB  ILE B 147     9463  16060  12334   2902   2564   4262       C  
ATOM   4877  CG1 ILE B 147      10.369  -8.464  24.333  1.00 90.11           C  
ANISOU 4877  CG1 ILE B 147     8516  14735  10987   2991   2795   4099       C  
ATOM   4878  CG2 ILE B 147       9.217  -7.775  22.215  1.00104.69           C  
ANISOU 4878  CG2 ILE B 147    10208  16683  12888   3186   2662   4227       C  
ATOM   4879  CD1 ILE B 147       9.699  -7.400  25.185  1.00 96.39           C  
ANISOU 4879  CD1 ILE B 147     9300  15703  11621   3331   3129   4217       C  
ATOM   4880  N   TYR B 148       7.572 -11.314  21.981  1.00102.16           N  
ANISOU 4880  N   TYR B 148     9217  12531  17068   2997  -2940  -2153       N  
ATOM   4881  CA  TYR B 148       6.846 -11.840  20.826  1.00110.21           C  
ANISOU 4881  CA  TYR B 148    10200  13481  18194   2817  -3124  -2034       C  
ATOM   4882  C   TYR B 148       6.191 -13.164  21.193  1.00118.94           C  
ANISOU 4882  C   TYR B 148    11020  14836  19335   2776  -2799  -2020       C  
ATOM   4883  O   TYR B 148       6.754 -14.241  20.951  1.00119.53           O  
ANISOU 4883  O   TYR B 148    11199  15007  19210   2544  -2564  -1891       O  
ATOM   4884  CB  TYR B 148       7.780 -12.009  19.628  1.00108.34           C  
ANISOU 4884  CB  TYR B 148    10342  13075  17748   2502  -3270  -1843       C  
ATOM   4885  CG  TYR B 148       8.602 -10.778  19.324  1.00 95.73           C  
ANISOU 4885  CG  TYR B 148     9054  11242  16076   2519  -3541  -1848       C  
ATOM   4886  CD1 TYR B 148       8.090  -9.756  18.537  1.00107.17           C  
ANISOU 4886  CD1 TYR B 148    10582  12445  17694   2570  -3973  -1862       C  
ATOM   4887  CD2 TYR B 148       9.886 -10.633  19.832  1.00104.99           C  
ANISOU 4887  CD2 TYR B 148    10437  12442  17011   2483  -3368  -1836       C  
ATOM   4888  CE1 TYR B 148       8.835  -8.626  18.258  1.00 93.65           C  
ANISOU 4888  CE1 TYR B 148     9163  10509  15910   2582  -4214  -1869       C  
ATOM   4889  CE2 TYR B 148      10.639  -9.507  19.560  1.00104.90           C  
ANISOU 4889  CE2 TYR B 148    10707  12216  16932   2487  -3614  -1842       C  
ATOM   4890  CZ  TYR B 148      10.108  -8.507  18.773  1.00101.31           C  
ANISOU 4890  CZ  TYR B 148    10339  11510  16644   2536  -4032  -1862       C  
ATOM   4891  OH  TYR B 148      10.855  -7.385  18.497  1.00103.72           O  
ANISOU 4891  OH  TYR B 148    10937  11594  16878   2535  -4269  -1870       O  
ATOM   4892  N   PRO B 149       4.993 -13.120  21.781  1.00122.92           N  
ANISOU 4892  N   PRO B 149    11162  15446  20095   2999  -2767  -2149       N  
ATOM   4893  CA  PRO B 149       4.280 -14.371  22.084  1.00131.38           C  
ANISOU 4893  CA  PRO B 149    11950  16749  21220   2952  -2472  -2138       C  
ATOM   4894  C   PRO B 149       3.852 -15.133  20.842  1.00132.32           C  
ANISOU 4894  C   PRO B 149    12106  16815  21356   2669  -2614  -1980       C  
ATOM   4895  O   PRO B 149       3.756 -16.366  20.890  1.00146.63           O  
ANISOU 4895  O   PRO B 149    13833  18795  23084   2515  -2328  -1913       O  
ATOM   4896  CB  PRO B 149       3.074 -13.902  22.911  1.00136.26           C  
ANISOU 4896  CB  PRO B 149    12187  17447  22138   3275  -2472  -2316       C  
ATOM   4897  CG  PRO B 149       3.489 -12.584  23.474  1.00121.59           C  
ANISOU 4897  CG  PRO B 149    10439  15464  20294   3511  -2602  -2440       C  
ATOM   4898  CD  PRO B 149       4.361 -11.956  22.428  1.00120.63           C  
ANISOU 4898  CD  PRO B 149    10707  15096  20030   3328  -2920  -2325       C  
ATOM   4899  N   PHE B 150       3.600 -14.441  19.727  1.00138.17           N  
ANISOU 4899  N   PHE B 150    12985  17321  22192   2591  -3047  -1915       N  
ATOM   4900  CA  PHE B 150       3.031 -15.112  18.561  1.00145.58           C  
ANISOU 4900  CA  PHE B 150    13934  18208  23172   2334  -3213  -1776       C  
ATOM   4901  C   PHE B 150       4.067 -15.965  17.835  1.00144.90           C  
ANISOU 4901  C   PHE B 150    14192  18085  22779   1993  -3086  -1598       C  
ATOM   4902  O   PHE B 150       3.769 -17.101  17.448  1.00156.04           O  
ANISOU 4902  O   PHE B 150    15557  19590  24139   1781  -2937  -1504       O  
ATOM   4903  CB  PHE B 150       2.413 -14.081  17.609  1.00149.17           C  
ANISOU 4903  CB  PHE B 150    14430  18423  23826   2367  -3725  -1760       C  
ATOM   4904  CG  PHE B 150       3.347 -12.964  17.218  1.00137.82           C  
ANISOU 4904  CG  PHE B 150    13347  16743  22275   2379  -3978  -1743       C  
ATOM   4905  CD1 PHE B 150       4.170 -13.083  16.109  1.00135.28           C  
ANISOU 4905  CD1 PHE B 150    13412  16244  21744   2087  -4127  -1580       C  
ATOM   4906  CD2 PHE B 150       3.392 -11.790  17.954  1.00140.33           C  
ANISOU 4906  CD2 PHE B 150    13622  17002  22696   2678  -4061  -1890       C  
ATOM   4907  CE1 PHE B 150       5.027 -12.058  15.749  1.00139.71           C  
ANISOU 4907  CE1 PHE B 150    14298  16580  22205   2092  -4352  -1564       C  
ATOM   4908  CE2 PHE B 150       4.247 -10.762  17.599  1.00143.75           C  
ANISOU 4908  CE2 PHE B 150    14387  17209  23024   2678  -4289  -1877       C  
ATOM   4909  CZ  PHE B 150       5.064 -10.896  16.494  1.00142.04           C  
ANISOU 4909  CZ  PHE B 150    14542  16824  22604   2385  -4437  -1714       C  
ATOM   4910  N   LEU B 151       5.283 -15.452  17.635  1.00158.75           N  
ANISOU 4910  N   LEU B 151    16294  19699  24325   1930  -3134  -1545       N  
ATOM   4911  CA  LEU B 151       6.289 -16.235  16.923  1.00161.35           C  
ANISOU 4911  CA  LEU B 151    16957  19982  24369   1614  -3006  -1366       C  
ATOM   4912  C   LEU B 151       6.790 -17.386  17.785  1.00159.54           C  
ANISOU 4912  C   LEU B 151    16655  20003  23960   1578  -2496  -1352       C  
ATOM   4913  O   LEU B 151       7.411 -18.319  17.264  1.00159.35           O  
ANISOU 4913  O   LEU B 151    16839  19985  23720   1316  -2315  -1198       O  
ATOM   4914  CB  LEU B 151       7.455 -15.357  16.475  1.00176.96           C  
ANISOU 4914  CB  LEU B 151    19314  21741  26183   1558  -3193  -1307       C  
ATOM   4915  CG  LEU B 151       8.409 -16.064  15.504  1.00162.45           C  
ANISOU 4915  CG  LEU B 151    17843  19803  24078   1218  -3126  -1102       C  
ATOM   4916  CD1 LEU B 151       8.964 -15.083  14.477  1.00147.77           C  
ANISOU 4916  CD1 LEU B 151    16334  17641  22170   1118  -3513  -1027       C  
ATOM   4917  CD2 LEU B 151       9.550 -16.767  16.235  1.00160.80           C  
ANISOU 4917  CD2 LEU B 151    17726  19757  23615   1174  -2686  -1055       C  
ATOM   4918  N   SER B 152       6.532 -17.319  19.097  1.00167.49           N  
ANISOU 4918  N   SER B 152    17382  21207  25050   1842  -2257  -1507       N  
ATOM   4919  CA  SER B 152       6.931 -18.376  20.017  1.00167.22           C  
ANISOU 4919  CA  SER B 152    17253  21423  24860   1841  -1769  -1507       C  
ATOM   4920  C   SER B 152       6.385 -19.726  19.571  1.00165.71           C  
ANISOU 4920  C   SER B 152    16977  21337  24648   1624  -1581  -1408       C  
ATOM   4921  O   SER B 152       6.981 -20.765  19.871  1.00165.94           O  
ANISOU 4921  O   SER B 152    17071  21508  24472   1506  -1202  -1330       O  
ATOM   4922  CB  SER B 152       6.446 -18.064  21.438  1.00165.57           C  
ANISOU 4922  CB  SER B 152    16719  21398  24792   2170  -1585  -1705       C  
ATOM   4923  OG  SER B 152       6.729 -16.726  21.811  1.00164.23           O  
ANISOU 4923  OG  SER B 152    16608  21111  24682   2381  -1803  -1816       O  
ATOM   4924  N   GLN B 153       5.257 -19.734  18.858  1.00215.27           N  
ANISOU 4924  N   GLN B 153    23113  27548  31133   1567  -1840  -1406       N  
ATOM   4925  CA  GLN B 153       4.689 -20.984  18.371  1.00227.93           C  
ANISOU 4925  CA  GLN B 153    24647  29238  32719   1339  -1692  -1313       C  
ATOM   4926  C   GLN B 153       5.643 -21.643  17.383  1.00218.67           C  
ANISOU 4926  C   GLN B 153    23871  27946  31266   1005  -1640  -1112       C  
ATOM   4927  O   GLN B 153       5.874 -21.127  16.285  1.00229.57           O  
ANISOU 4927  O   GLN B 153    25516  29092  32618    854  -1982  -1018       O  
ATOM   4928  CB  GLN B 153       3.333 -20.736  17.706  1.00239.83           C  
ANISOU 4928  CB  GLN B 153    25944  30677  34505   1329  -2041  -1339       C  
ATOM   4929  N   ARG B 154       6.211 -22.782  17.779  1.00145.03           N  
ANISOU 4929  N   ARG B 154    14599  18776  21730    895  -1201  -1042       N  
ATOM   4930  CA  ARG B 154       7.191 -23.576  17.048  1.00144.34           C  
ANISOU 4930  CA  ARG B 154    14873  18614  21355    602  -1038   -848       C  
ATOM   4931  C   ARG B 154       8.583 -22.971  17.137  1.00143.77           C  
ANISOU 4931  C   ARG B 154    15090  18446  21088    629  -1026   -793       C  
ATOM   4932  O   ARG B 154       9.551 -23.645  16.781  1.00141.41           O  
ANISOU 4932  O   ARG B 154    15068  18122  20538    432   -808   -637       O  
ATOM   4933  CB  ARG B 154       6.823 -23.782  15.566  1.00141.84           C  
ANISOU 4933  CB  ARG B 154    14766  18091  21036    304  -1332   -715       C  
ATOM   4934  CG  ARG B 154       7.182 -25.161  15.033  1.00144.55           C  
ANISOU 4934  CG  ARG B 154    15316  18458  21149     -1  -1028   -549       C  
ATOM   4935  CD  ARG B 154       8.156 -25.160  13.862  1.00148.99           C  
ANISOU 4935  CD  ARG B 154    16344  18778  21486   -268  -1142   -362       C  
ATOM   4936  NE  ARG B 154       7.504 -24.638  12.660  1.00139.09           N  
ANISOU 4936  NE  ARG B 154    15196  17301  20349   -413  -1613   -327       N  
ATOM   4937  CZ  ARG B 154       8.042 -24.637  11.443  1.00136.18           C  
ANISOU 4937  CZ  ARG B 154    15223  16693  19825   -675  -1786   -169       C  
ATOM   4938  NH1 ARG B 154       9.242 -25.165  11.237  1.00141.71           N  
ANISOU 4938  NH1 ARG B 154    16249  17345  20249   -826  -1512    -25       N  
ATOM   4939  NH2 ARG B 154       7.365 -24.125  10.423  1.00139.43           N  
ANISOU 4939  NH2 ARG B 154    15705  16915  20357   -786  -2229   -149       N  
ATOM   4940  N   ARG B 155       8.735 -21.730  17.607  1.00158.68           N  
ANISOU 4940  N   ARG B 155    16928  20282  23081    864  -1241   -912       N  
ATOM   4941  CA  ARG B 155      10.054 -21.115  17.580  1.00157.02           C  
ANISOU 4941  CA  ARG B 155    17008  19963  22687    858  -1268   -851       C  
ATOM   4942  C   ARG B 155      10.483 -21.104  16.111  1.00153.21           C  
ANISOU 4942  C   ARG B 155    16898  19223  22092    566  -1508   -674       C  
ATOM   4943  O   ARG B 155       9.621 -21.089  15.222  1.00153.92           O  
ANISOU 4943  O   ARG B 155    16982  19191  22310    451  -1783   -654       O  
ATOM   4944  CB  ARG B 155      11.013 -21.862  18.510  1.00154.06           C  
ANISOU 4944  CB  ARG B 155    16649  19794  22093    886   -794   -811       C  
ATOM   4945  N   ASN B 156      11.777 -20.999  15.835  1.00137.60           N  
ANISOU 4945  N   ASN B 156    15240  17150  19891    456  -1442   -550       N  
ATOM   4946  CA  ASN B 156      12.292 -21.111  14.479  1.00129.42           C  
ANISOU 4946  CA  ASN B 156    14582  15875  18717    168  -1602   -368       C  
ATOM   4947  C   ASN B 156      13.231 -22.304  14.340  1.00125.73           C  
ANISOU 4947  C   ASN B 156    14323  15471  17976    -39  -1192   -187       C  
ATOM   4948  O   ASN B 156      14.191 -22.414  15.113  1.00120.02           O  
ANISOU 4948  O   ASN B 156    13619  14873  17110     44   -910   -165       O  
ATOM   4949  CB  ASN B 156      13.019 -19.815  14.107  1.00119.40           C  
ANISOU 4949  CB  ASN B 156    13546  14387  17434    207  -1927   -365       C  
ATOM   4950  CG  ASN B 156      13.753 -19.915  12.798  1.00118.54           C  
ANISOU 4950  CG  ASN B 156    13856  14032  17151    -82  -2045   -169       C  
ATOM   4951  OD1 ASN B 156      14.977 -19.792  12.751  1.00116.82           O  
ANISOU 4951  OD1 ASN B 156    13881  13759  16747   -146  -1932    -68       O  
ATOM   4952  ND2 ASN B 156      13.014 -20.146  11.722  1.00119.81           N  
ANISOU 4952  ND2 ASN B 156    14108  14044  17371   -265  -2271   -110       N  
ATOM   4953  N   PRO B 157      12.993 -23.223  13.393  1.00120.08           N  
ANISOU 4953  N   PRO B 157    13769  14678  17178   -307  -1140    -51       N  
ATOM   4954  CA  PRO B 157      13.899 -24.379  13.266  1.00118.90           C  
ANISOU 4954  CA  PRO B 157    13832  14580  16764   -496   -722    128       C  
ATOM   4955  C   PRO B 157      15.328 -23.991  12.925  1.00113.56           C  
ANISOU 4955  C   PRO B 157    13493  13764  15890   -572   -702    267       C  
ATOM   4956  O   PRO B 157      16.265 -24.705  13.308  1.00103.80           O  
ANISOU 4956  O   PRO B 157    12344  12638  14456   -609   -313    380       O  
ATOM   4957  CB  PRO B 157      13.258 -25.210  12.145  1.00119.49           C  
ANISOU 4957  CB  PRO B 157    14054  14537  16811   -779   -770    234       C  
ATOM   4958  CG  PRO B 157      12.484 -24.220  11.347  1.00121.99           C  
ANISOU 4958  CG  PRO B 157    14386  14648  17316   -791  -1299    169       C  
ATOM   4959  CD  PRO B 157      11.950 -23.235  12.350  1.00126.06           C  
ANISOU 4959  CD  PRO B 157    14552  15282  18064   -462  -1462    -41       C  
ATOM   4960  N   TRP B 158      15.522 -22.875  12.212  1.00112.79           N  
ANISOU 4960  N   TRP B 158    13583  13426  15844   -595  -1109    267       N  
ATOM   4961  CA  TRP B 158      16.848 -22.462  11.772  1.00111.54           C  
ANISOU 4961  CA  TRP B 158    13760  13111  15509   -689  -1119    405       C  
ATOM   4962  C   TRP B 158      17.704 -21.869  12.883  1.00110.30           C  
ANISOU 4962  C   TRP B 158    13495  13095  15320   -471   -995    340       C  
ATOM   4963  O   TRP B 158      18.934 -21.862  12.759  1.00108.74           O  
ANISOU 4963  O   TRP B 158    13527  12849  14941   -550   -858    478       O  
ATOM   4964  CB  TRP B 158      16.733 -21.397  10.667  1.00112.61           C  
ANISOU 4964  CB  TRP B 158    14130  12937  15718   -778  -1610    413       C  
ATOM   4965  CG  TRP B 158      16.403 -21.890   9.299  1.00113.19           C  
ANISOU 4965  CG  TRP B 158    14476  12796  15734  -1066  -1743    547       C  
ATOM   4966  CD1 TRP B 158      15.168 -22.000   8.727  1.00115.12           C  
ANISOU 4966  CD1 TRP B 158    14636  12981  16124  -1134  -1989    495       C  
ATOM   4967  CD2 TRP B 158      17.348 -22.260   8.290  1.00120.52           C  
ANISOU 4967  CD2 TRP B 158    15827  13525  16441  -1329  -1661    760       C  
ATOM   4968  NE1 TRP B 158      15.287 -22.460   7.435  1.00115.16           N  
ANISOU 4968  NE1 TRP B 158    14993  12766  15998  -1435  -2061    660       N  
ATOM   4969  CE2 TRP B 158      16.616 -22.622   7.143  1.00113.25           C  
ANISOU 4969  CE2 TRP B 158    15073  12427  15528  -1556  -1856    823       C  
ATOM   4970  CE3 TRP B 158      18.745 -22.335   8.253  1.00110.53           C  
ANISOU 4970  CE3 TRP B 158    14810  12216  14970  -1397  -1435    908       C  
ATOM   4971  CZ2 TRP B 158      17.234 -23.057   5.972  1.00112.61           C  
ANISOU 4971  CZ2 TRP B 158    15420  12118  15250  -1846  -1820   1022       C  
ATOM   4972  CZ3 TRP B 158      19.355 -22.767   7.094  1.00109.44           C  
ANISOU 4972  CZ3 TRP B 158    15079  11855  14650  -1674  -1391   1110       C  
ATOM   4973  CH2 TRP B 158      18.601 -23.122   5.968  1.00110.69           C  
ANISOU 4973  CH2 TRP B 158    15417  11829  14812  -1896  -1579   1163       C  
ATOM   4974  N   GLN B 159      17.091 -21.381  13.960  1.00103.15           N  
ANISOU 4974  N   GLN B 159    12249  12361  14583   -204  -1036    140       N  
ATOM   4975  CA  GLN B 159      17.851 -20.667  14.981  1.00 94.37           C  
ANISOU 4975  CA  GLN B 159    11053  11358  13446      0   -979     63       C  
ATOM   4976  C   GLN B 159      18.863 -21.584  15.663  1.00 85.02           C  
ANISOU 4976  C   GLN B 159     9878  10378  12046    -18   -503    182       C  
ATOM   4977  O   GLN B 159      20.050 -21.253  15.763  1.00 84.85           O  
ANISOU 4977  O   GLN B 159    10023  10332  11884    -38   -444    273       O  
ATOM   4978  CB  GLN B 159      16.882 -20.050  15.992  1.00 97.58           C  
ANISOU 4978  CB  GLN B 159    11097  11903  14075    286  -1095   -178       C  
ATOM   4979  CG  GLN B 159      17.519 -19.078  16.967  1.00 95.91           C  
ANISOU 4979  CG  GLN B 159    10820  11759  13864    499  -1128   -287       C  
ATOM   4980  CD  GLN B 159      16.514 -18.410  17.907  1.00105.13           C  
ANISOU 4980  CD  GLN B 159    11657  13031  15256    784  -1254   -528       C  
ATOM   4981  OE1 GLN B 159      16.904 -17.797  18.900  1.00 91.45           O  
ANISOU 4981  OE1 GLN B 159     9828  11399  13518    974  -1212   -636       O  
ATOM   4982  NE2 GLN B 159      15.224 -18.514  17.590  1.00112.22           N  
ANISOU 4982  NE2 GLN B 159    12387  13902  16352    811  -1410   -609       N  
ATOM   4983  N   ALA B 160      18.410 -22.749  16.133  1.00 91.37           N  
ANISOU 4983  N   ALA B 160    10505  11387  12825    -13   -157    188       N  
ATOM   4984  CA  ALA B 160      19.297 -23.656  16.854  1.00 86.44           C  
ANISOU 4984  CA  ALA B 160     9866  10973  12004     -6    309    297       C  
ATOM   4985  C   ALA B 160      20.358 -24.280  15.955  1.00 83.68           C  
ANISOU 4985  C   ALA B 160     9866  10497  11430   -258    480    553       C  
ATOM   4986  O   ALA B 160      21.473 -24.549  16.417  1.00 80.37           O  
ANISOU 4986  O   ALA B 160     9509  10185  10843   -245    753    668       O  
ATOM   4987  CB  ALA B 160      18.480 -24.757  17.533  1.00 90.00           C  
ANISOU 4987  CB  ALA B 160    10050  11658  12486     58    634    238       C  
ATOM   4988  N   SER B 161      20.043 -24.523  14.680  1.00 90.15           N  
ANISOU 4988  N   SER B 161    10920  11092  12242   -487    328    650       N  
ATOM   4989  CA  SER B 161      21.017 -25.160  13.798  1.00 83.80           C  
ANISOU 4989  CA  SER B 161    10466  10153  11222   -729    514    897       C  
ATOM   4990  C   SER B 161      22.228 -24.272  13.542  1.00 73.82           C  
ANISOU 4990  C   SER B 161     9424   8750   9873   -751    374    986       C  
ATOM   4991  O   SER B 161      23.320 -24.783  13.265  1.00 67.42           O  
ANISOU 4991  O   SER B 161     8831   7915   8869   -876    631   1189       O  
ATOM   4992  CB  SER B 161      20.354 -25.532  12.471  1.00 86.87           C  
ANISOU 4992  CB  SER B 161    11074  10312  11622   -975    348    967       C  
ATOM   4993  OG  SER B 161      19.271 -26.421  12.672  1.00 86.66           O  
ANISOU 4993  OG  SER B 161    10849  10414  11662   -983    493    899       O  
ATOM   4994  N   TYR B 162      22.061 -22.955  13.625  1.00 71.84           N  
ANISOU 4994  N   TYR B 162     9126   8405   9765   -632    -21    842       N  
ATOM   4995  CA  TYR B 162      23.149 -22.006  13.426  1.00 64.91           C  
ANISOU 4995  CA  TYR B 162     8446   7393   8823   -646   -183    904       C  
ATOM   4996  C   TYR B 162      23.758 -21.513  14.730  1.00 64.55           C  
ANISOU 4996  C   TYR B 162     8192   7565   8768   -426    -80    818       C  
ATOM   4997  O   TYR B 162      24.981 -21.372  14.823  1.00 60.04           O  
ANISOU 4997  O   TYR B 162     7756   7000   8056   -466     37    947       O  
ATOM   4998  CB  TYR B 162      22.647 -20.806  12.613  1.00 67.34           C  
ANISOU 4998  CB  TYR B 162     8879   7428   9278   -672   -698    810       C  
ATOM   4999  CG  TYR B 162      23.599 -19.634  12.573  1.00 63.11           C  
ANISOU 4999  CG  TYR B 162     8497   6765   8716   -645   -913    819       C  
ATOM   5000  CD1 TYR B 162      24.589 -19.553  11.605  1.00 62.33           C  
ANISOU 5000  CD1 TYR B 162     8755   6453   8475   -854   -934   1014       C  
ATOM   5001  CD2 TYR B 162      23.499 -18.603  13.496  1.00 63.86           C  
ANISOU 5001  CD2 TYR B 162     8391   6946   8928   -417  -1092    631       C  
ATOM   5002  CE1 TYR B 162      25.459 -18.481  11.563  1.00 62.29           C  
ANISOU 5002  CE1 TYR B 162     8889   6331   8448   -840  -1128   1023       C  
ATOM   5003  CE2 TYR B 162      24.364 -17.529  13.463  1.00 63.84           C  
ANISOU 5003  CE2 TYR B 162     8537   6824   8896   -406  -1288    635       C  
ATOM   5004  CZ  TYR B 162      25.341 -17.472  12.494  1.00 63.05           C  
ANISOU 5004  CZ  TYR B 162     8779   6519   8658   -620  -1309    832       C  
ATOM   5005  OH  TYR B 162      26.204 -16.401  12.457  1.00 63.11           O  
ANISOU 5005  OH  TYR B 162     8933   6407   8638   -619  -1502    837       O  
ATOM   5006  N   ILE B 163      22.928 -21.252  15.740  1.00 68.59           N  
ANISOU 5006  N   ILE B 163     8378   8256   9428   -198   -119    604       N  
ATOM   5007  CA  ILE B 163      23.417 -20.649  16.976  1.00 65.44           C  
ANISOU 5007  CA  ILE B 163     7795   8042   9028     14    -71    497       C  
ATOM   5008  C   ILE B 163      24.331 -21.608  17.729  1.00 60.38           C  
ANISOU 5008  C   ILE B 163     7099   7647   8197     24    395    634       C  
ATOM   5009  O   ILE B 163      25.386 -21.207  18.236  1.00 59.52           O  
ANISOU 5009  O   ILE B 163     7020   7608   7986     65    453    685       O  
ATOM   5010  CB  ILE B 163      22.227 -20.201  17.846  1.00 73.13           C  
ANISOU 5010  CB  ILE B 163     8446   9135  10206    255   -204    237       C  
ATOM   5011  CG1 ILE B 163      21.470 -19.053  17.169  1.00 65.28           C  
ANISOU 5011  CG1 ILE B 163     7509   7893   9402    274   -692    108       C  
ATOM   5012  CG2 ILE B 163      22.702 -19.797  19.235  1.00 72.69           C  
ANISOU 5012  CG2 ILE B 163     8195   9303  10122    471    -80    130       C  
ATOM   5013  CD1 ILE B 163      22.181 -17.716  17.229  1.00 75.52           C  
ANISOU 5013  CD1 ILE B 163     8935   9059  10701    327   -973     61       C  
ATOM   5014  N   VAL B 164      23.949 -22.884  17.820  1.00 64.69           N  
ANISOU 5014  N   VAL B 164     7561   8328   8690    -16    732    698       N  
ATOM   5015  CA  VAL B 164      24.717 -23.827  18.634  1.00 61.96           C  
ANISOU 5015  CA  VAL B 164     7135   8235   8174     24   1190    817       C  
ATOM   5016  C   VAL B 164      26.149 -23.980  18.133  1.00 63.12           C  
ANISOU 5016  C   VAL B 164     7548   8310   8127   -133   1327   1066       C  
ATOM   5017  O   VAL B 164      27.080 -23.849  18.945  1.00 60.51           O  
ANISOU 5017  O   VAL B 164     7149   8144   7697    -43   1479   1113       O  
ATOM   5018  CB  VAL B 164      23.976 -25.174  18.721  1.00 72.24           C  
ANISOU 5018  CB  VAL B 164     8324   9667   9458     -4   1520    841       C  
ATOM   5019  CG1 VAL B 164      24.895 -26.254  19.282  1.00 69.83           C  
ANISOU 5019  CG1 VAL B 164     8014   9570   8946     -9   2009   1021       C  
ATOM   5020  CG2 VAL B 164      22.731 -25.033  19.582  1.00 76.28           C  
ANISOU 5020  CG2 VAL B 164     8505  10326  10151    201   1458    592       C  
ATOM   5021  N   PRO B 165      26.404 -24.260  16.850  1.00 65.51           N  
ANISOU 5021  N   PRO B 165     8150   8376   8365   -366   1290   1237       N  
ATOM   5022  CA  PRO B 165      27.805 -24.327  16.398  1.00 55.30           C  
ANISOU 5022  CA  PRO B 165     7105   7008   6898   -502   1421   1476       C  
ATOM   5023  C   PRO B 165      28.589 -23.058  16.680  1.00 55.52           C  
ANISOU 5023  C   PRO B 165     7156   6996   6943   -438   1161   1435       C  
ATOM   5024  O   PRO B 165      29.772 -23.128  17.035  1.00 54.57           O  
ANISOU 5024  O   PRO B 165     7070   6977   6689   -443   1350   1582       O  
ATOM   5025  CB  PRO B 165      27.674 -24.588  14.890  1.00 55.40           C  
ANISOU 5025  CB  PRO B 165     7445   6720   6883   -753   1321   1609       C  
ATOM   5026  CG  PRO B 165      26.342 -25.228  14.730  1.00 64.67           C  
ANISOU 5026  CG  PRO B 165     8515   7905   8151   -763   1332   1501       C  
ATOM   5027  CD  PRO B 165      25.457 -24.612  15.775  1.00 59.19           C  
ANISOU 5027  CD  PRO B 165     7479   7376   7633   -521   1160   1234       C  
ATOM   5028  N   LEU B 166      27.959 -21.892  16.529  1.00 56.86           N  
ANISOU 5028  N   LEU B 166     7308   7020   7274   -379    729   1242       N  
ATOM   5029  CA  LEU B 166      28.659 -20.636  16.769  1.00 57.22           C  
ANISOU 5029  CA  LEU B 166     7396   7008   7337   -327    466   1191       C  
ATOM   5030  C   LEU B 166      29.103 -20.519  18.222  1.00 60.17           C  
ANISOU 5030  C   LEU B 166     7513   7680   7670   -130    632   1116       C  
ATOM   5031  O   LEU B 166      30.205 -20.035  18.505  1.00 66.04           O  
ANISOU 5031  O   LEU B 166     8313   8459   8323   -141    632   1197       O  
ATOM   5032  CB  LEU B 166      27.761 -19.460  16.388  1.00 58.87           C  
ANISOU 5032  CB  LEU B 166     7622   7010   7735   -279    -11    983       C  
ATOM   5033  CG  LEU B 166      28.376 -18.065  16.494  1.00 59.49           C  
ANISOU 5033  CG  LEU B 166     7784   6976   7841   -242   -327    915       C  
ATOM   5034  CD1 LEU B 166      29.277 -17.782  15.305  1.00 59.05           C  
ANISOU 5034  CD1 LEU B 166     8080   6659   7696   -468   -438   1109       C  
ATOM   5035  CD2 LEU B 166      27.285 -17.016  16.607  1.00 61.27           C  
ANISOU 5035  CD2 LEU B 166     7911   7098   8272    -99   -720    659       C  
ATOM   5036  N   VAL B 167      28.257 -20.955  19.159  1.00 60.68           N  
ANISOU 5036  N   VAL B 167     7296   7960   7799     46    774    964       N  
ATOM   5037  CA  VAL B 167      28.579 -20.806  20.577  1.00 60.16           C  
ANISOU 5037  CA  VAL B 167     6990   8172   7697    242    914    872       C  
ATOM   5038  C   VAL B 167      29.836 -21.593  20.920  1.00 62.24           C  
ANISOU 5038  C   VAL B 167     7279   8614   7754    188   1291   1107       C  
ATOM   5039  O   VAL B 167      30.778 -21.062  21.520  1.00 69.11           O  
ANISOU 5039  O   VAL B 167     8129   9582   8547    229   1278   1138       O  
ATOM   5040  CB  VAL B 167      27.387 -21.242  21.448  1.00 64.51           C  
ANISOU 5040  CB  VAL B 167     7248   8910   8353    431   1028    678       C  
ATOM   5041  CG1 VAL B 167      27.802 -21.328  22.911  1.00 70.24           C  
ANISOU 5041  CG1 VAL B 167     7747   9939   9001    616   1250    619       C  
ATOM   5042  CG2 VAL B 167      26.226 -20.277  21.278  1.00 61.29           C  
ANISOU 5042  CG2 VAL B 167     6779   8346   8162    522    634    437       C  
ATOM   5043  N   TRP B 168      29.870 -22.875  20.548  1.00 57.52           N  
ANISOU 5043  N   TRP B 168     6728   8063   7064     93   1634   1279       N  
ATOM   5044  CA  TRP B 168      31.056 -23.679  20.823  1.00 62.57           C  
ANISOU 5044  CA  TRP B 168     7397   8866   7512     48   2013   1522       C  
ATOM   5045  C   TRP B 168      32.283 -23.113  20.122  1.00 59.01           C  
ANISOU 5045  C   TRP B 168     7189   8255   6979   -108   1896   1707       C  
ATOM   5046  O   TRP B 168      33.395 -23.192  20.655  1.00 63.81           O  
ANISOU 5046  O   TRP B 168     7763   9020   7462    -92   2071   1848       O  
ATOM   5047  CB  TRP B 168      30.823 -25.129  20.402  1.00 58.13           C  
ANISOU 5047  CB  TRP B 168     6884   8335   6869    -40   2392   1678       C  
ATOM   5048  CG  TRP B 168      29.950 -25.891  21.348  1.00 60.52           C  
ANISOU 5048  CG  TRP B 168     6921   8874   7200    122   2630   1549       C  
ATOM   5049  CD1 TRP B 168      28.639 -26.221  21.169  1.00 64.02           C  
ANISOU 5049  CD1 TRP B 168     7284   9275   7766    141   2588   1399       C  
ATOM   5050  CD2 TRP B 168      30.326 -26.418  22.627  1.00 66.66           C  
ANISOU 5050  CD2 TRP B 168     7476   9970   7882    286   2950   1561       C  
ATOM   5051  NE1 TRP B 168      28.175 -26.922  22.257  1.00 65.94           N  
ANISOU 5051  NE1 TRP B 168     7270   9785   7998    306   2871   1314       N  
ATOM   5052  CE2 TRP B 168      29.191 -27.056  23.166  1.00 70.36           C  
ANISOU 5052  CE2 TRP B 168     7746  10567   8421    400   3097   1410       C  
ATOM   5053  CE3 TRP B 168      31.511 -26.411  23.369  1.00 68.75           C  
ANISOU 5053  CE3 TRP B 168     7713  10387   8021    326   3047   1641       C  
ATOM   5054  CZ2 TRP B 168      29.207 -27.682  24.411  1.00 69.70           C  
ANISOU 5054  CZ2 TRP B 168     7532  10651   8300    492   3161   1237       C  
ATOM   5055  CZ3 TRP B 168      31.524 -27.033  24.605  1.00 68.06           C  
ANISOU 5055  CZ3 TRP B 168     7509  10429   7921    406   3045   1428       C  
ATOM   5056  CH2 TRP B 168      30.380 -27.659  25.113  1.00 62.87           C  
ANISOU 5056  CH2 TRP B 168     6722   9830   7338    475   3097   1234       C  
ATOM   5057  N   CYS B 169      32.102 -22.538  18.931  1.00 53.47           N  
ANISOU 5057  N   CYS B 169     6728   7243   6346   -260   1599   1712       N  
ATOM   5058  CA  CYS B 169      33.226 -21.929  18.227  1.00 55.29           C  
ANISOU 5058  CA  CYS B 169     7199   7299   6510   -411   1470   1876       C  
ATOM   5059  C   CYS B 169      33.706 -20.672  18.942  1.00 61.48           C  
ANISOU 5059  C   CYS B 169     7897   8135   7328   -315   1203   1753       C  
ATOM   5060  O   CYS B 169      34.915 -20.469  19.106  1.00 65.57           O  
ANISOU 5060  O   CYS B 169     8463   8712   7741   -365   1274   1907       O  
ATOM   5061  CB  CYS B 169      32.825 -21.602  16.790  1.00 53.68           C  
ANISOU 5061  CB  CYS B 169     7282   6741   6372   -592   1207   1895       C  
ATOM   5062  SG  CYS B 169      33.970 -20.496  15.934  1.00 62.11           S  
ANISOU 5062  SG  CYS B 169     8644   7549   7407   -757    931   2019       S  
ATOM   5063  N   MET B 170      32.777 -19.816  19.372  1.00 59.53           N  
ANISOU 5063  N   MET B 170     7525   7866   7228   -179    899   1479       N  
ATOM   5064  CA  MET B 170      33.165 -18.636  20.137  1.00 65.12           C  
ANISOU 5064  CA  MET B 170     8154   8628   7963    -79    659   1343       C  
ATOM   5065  C   MET B 170      33.878 -19.032  21.424  1.00 65.65           C  
ANISOU 5065  C   MET B 170     8006   9031   7908     38    944   1390       C  
ATOM   5066  O   MET B 170      34.856 -18.390  21.824  1.00 66.84           O  
ANISOU 5066  O   MET B 170     8169   9239   7988     24    872   1436       O  
ATOM   5067  CB  MET B 170      31.938 -17.777  20.442  1.00 65.25           C  
ANISOU 5067  CB  MET B 170     8060   8573   8159     71    334   1040       C  
ATOM   5068  CG  MET B 170      31.347 -17.093  19.218  1.00 60.74           C  
ANISOU 5068  CG  MET B 170     7708   7659   7713    -36    -27    984       C  
ATOM   5069  SD  MET B 170      30.013 -15.947  19.621  1.00 70.39           S  
ANISOU 5069  SD  MET B 170     8796   8796   9154    160   -423    641       S  
ATOM   5070  CE  MET B 170      28.806 -17.061  20.338  1.00 66.77           C  
ANISOU 5070  CE  MET B 170     8036   8571   8760    322   -146    533       C  
ATOM   5071  N   ALA B 171      33.398 -20.085  22.089  1.00 63.42           N  
ANISOU 5071  N   ALA B 171     7526   8975   7596    150   1266   1380       N  
ATOM   5072  CA  ALA B 171      34.087 -20.583  23.274  1.00 69.49           C  
ANISOU 5072  CA  ALA B 171     8101  10068   8234    257   1565   1450       C  
ATOM   5073  C   ALA B 171      35.481 -21.092  22.924  1.00 72.19           C  
ANISOU 5073  C   ALA B 171     8565  10451   8414    113   1799   1764       C  
ATOM   5074  O   ALA B 171      36.437 -20.876  23.679  1.00 69.61           O  
ANISOU 5074  O   ALA B 171     8153  10308   7987    147   1863   1837       O  
ATOM   5075  CB  ALA B 171      33.261 -21.686  23.934  1.00 72.70           C  
ANISOU 5075  CB  ALA B 171     8299  10682   8640    393   1881   1391       C  
ATOM   5076  N   CYS B 172      35.616 -21.770  21.781  1.00 67.56           N  
ANISOU 5076  N   CYS B 172     8180   9693   7798    -52   1929   1957       N  
ATOM   5077  CA  CYS B 172      36.931 -22.219  21.338  1.00 55.58           C  
ANISOU 5077  CA  CYS B 172     6798   8180   6138   -192   2150   2266       C  
ATOM   5078  C   CYS B 172      37.866 -21.035  21.133  1.00 62.79           C  
ANISOU 5078  C   CYS B 172     7826   8982   7048   -281   1860   2300       C  
ATOM   5079  O   CYS B 172      39.003 -21.032  21.618  1.00 67.33           O  
ANISOU 5079  O   CYS B 172     8346   9722   7516   -291   1987   2459       O  
ATOM   5080  CB  CYS B 172      36.804 -23.027  20.047  1.00 50.99           C  
ANISOU 5080  CB  CYS B 172     6454   7381   5537   -361   2301   2441       C  
ATOM   5081  SG  CYS B 172      36.361 -24.758  20.294  1.00 66.89           S  
ANISOU 5081  SG  CYS B 172     8397   9498   7522   -333   2583   2318       S  
ATOM   5082  N   LEU B 173      37.400 -20.015  20.412  1.00 63.47           N  
ANISOU 5082  N   LEU B 173     8073   8790   7254   -349   1465   2155       N  
ATOM   5083  CA  LEU B 173      38.221 -18.829  20.203  1.00 64.98           C  
ANISOU 5083  CA  LEU B 173     8387   8857   7448   -437   1172   2167       C  
ATOM   5084  C   LEU B 173      38.530 -18.132  21.520  1.00 62.45           C  
ANISOU 5084  C   LEU B 173     7854   8768   7108   -298   1074   2029       C  
ATOM   5085  O   LEU B 173      39.621 -17.576  21.687  1.00 62.27           O  
ANISOU 5085  O   LEU B 173     7862   8782   7015   -369   1009   2133       O  
ATOM   5086  CB  LEU B 173      37.514 -17.872  19.245  1.00 61.41           C  
ANISOU 5086  CB  LEU B 173     8139   8061   7131   -511    763   2012       C  
ATOM   5087  CG  LEU B 173      37.769 -18.104  17.756  1.00 61.50           C  
ANISOU 5087  CG  LEU B 173     8461   7778   7129   -725    757   2201       C  
ATOM   5088  CD1 LEU B 173      37.363 -19.506  17.333  1.00 59.75           C  
ANISOU 5088  CD1 LEU B 173     8260   7583   6861   -757   1105   2333       C  
ATOM   5089  CD2 LEU B 173      37.023 -17.063  16.934  1.00 69.49           C  
ANISOU 5089  CD2 LEU B 173     9656   8469   8278   -775    322   2025       C  
ATOM   5090  N   SER B 174      37.587 -18.152  22.464  1.00 69.41           N  
ANISOU 5090  N   SER B 174     8521   9805   8046   -106   1065   1798       N  
ATOM   5091  CA  SER B 174      37.797 -17.466  23.733  1.00 70.44           C  
ANISOU 5091  CA  SER B 174     8468  10141   8153     29    966   1647       C  
ATOM   5092  C   SER B 174      38.842 -18.164  24.594  1.00 74.56           C  
ANISOU 5092  C   SER B 174     8837  10982   8511     55   1295   1841       C  
ATOM   5093  O   SER B 174      39.510 -17.511  25.403  1.00 71.37           O  
ANISOU 5093  O   SER B 174     8352  10719   8047     83   1195   1810       O  
ATOM   5094  CB  SER B 174      36.475 -17.364  24.493  1.00 70.23           C  
ANISOU 5094  CB  SER B 174     8263  10189   8233    232    898   1355       C  
ATOM   5095  OG  SER B 174      35.527 -16.607  23.763  1.00 69.85           O  
ANISOU 5095  OG  SER B 174     8338   9856   8345    222    565   1172       O  
ATOM   5096  N   SER B 175      39.000 -19.477  24.437  1.00 73.59           N  
ANISOU 5096  N   SER B 175     6866  13819   7276   -622    264   1354       N  
ATOM   5097  CA  SER B 175      39.942 -20.253  25.231  1.00 75.34           C  
ANISOU 5097  CA  SER B 175     7242  14110   7274   -485    251   1587       C  
ATOM   5098  C   SER B 175      41.266 -20.501  24.522  1.00 73.94           C  
ANISOU 5098  C   SER B 175     7197  13670   7227   -311    135   1658       C  
ATOM   5099  O   SER B 175      42.113 -21.221  25.060  1.00 75.31           O  
ANISOU 5099  O   SER B 175     7517  13858   7238   -186    115   1864       O  
ATOM   5100  CB  SER B 175      39.316 -21.597  25.623  1.00 77.58           C  
ANISOU 5100  CB  SER B 175     7736  14351   7389   -632    393   1900       C  
ATOM   5101  OG  SER B 175      38.970 -22.354  24.476  1.00 76.52           O  
ANISOU 5101  OG  SER B 175     7782  13840   7454   -757    434   2035       O  
ATOM   5102  N   LEU B 176      41.467 -19.933  23.333  1.00 71.34           N  
ANISOU 5102  N   LEU B 176     6820  13104   7183   -300     58   1494       N  
ATOM   5103  CA  LEU B 176      42.739 -20.125  22.639  1.00 70.04           C  
ANISOU 5103  CA  LEU B 176     6765  12703   7143   -134    -49   1550       C  
ATOM   5104  C   LEU B 176      43.916 -19.599  23.447  1.00 70.56           C  
ANISOU 5104  C   LEU B 176     6736  13006   7068     91   -164   1487       C  
ATOM   5105  O   LEU B 176      44.933 -20.308  23.549  1.00 71.21           O  
ANISOU 5105  O   LEU B 176     6972  13002   7082    235   -204   1677       O  
ATOM   5106  CB  LEU B 176      42.679 -19.467  21.257  1.00 67.16           C  
ANISOU 5106  CB  LEU B 176     6342  12074   7104   -175   -112   1354       C  
ATOM   5107  CG  LEU B 176      42.138 -20.335  20.121  1.00 66.32           C  
ANISOU 5107  CG  LEU B 176     6433  11583   7180   -324    -38   1503       C  
ATOM   5108  CD1 LEU B 176      41.856 -19.482  18.897  1.00 63.60           C  
ANISOU 5108  CD1 LEU B 176     5987  11038   7138   -393    -96   1262       C  
ATOM   5109  CD2 LEU B 176      43.114 -21.453  19.779  1.00 66.66           C  
ANISOU 5109  CD2 LEU B 176     6734  11380   7215   -210    -52   1769       C  
ATOM   5110  N   PRO B 177      43.865 -18.397  24.028  1.00 70.37           N  
ANISOU 5110  N   PRO B 177     6470  13273   6993    137   -228   1230       N  
ATOM   5111  CA  PRO B 177      44.980 -17.959  24.886  1.00 71.11           C  
ANISOU 5111  CA  PRO B 177     6486  13604   6930    347   -338   1191       C  
ATOM   5112  C   PRO B 177      45.335 -18.968  25.964  1.00 73.78           C  
ANISOU 5112  C   PRO B 177     6976  14073   6984    414   -287   1464       C  
ATOM   5113  O   PRO B 177      46.519 -19.152  26.271  1.00 74.23           O  
ANISOU 5113  O   PRO B 177     7086  14153   6966    600   -377   1548       O  
ATOM   5114  CB  PRO B 177      44.460 -16.644  25.481  1.00 70.99           C  
ANISOU 5114  CB  PRO B 177     6206  13901   6864    330   -376    895       C  
ATOM   5115  CG  PRO B 177      43.502 -16.129  24.459  1.00 69.07           C  
ANISOU 5115  CG  PRO B 177     5884  13491   6867    167   -350    715       C  
ATOM   5116  CD  PRO B 177      42.843 -17.346  23.867  1.00 69.37           C  
ANISOU 5116  CD  PRO B 177     6133  13259   6966     11   -217    954       C  
ATOM   5117  N   THR B 178      44.336 -19.634  26.547  1.00 78.18           N  
ANISOU 5117  N   THR B 178     7606  14717   7380    263   -148   1606       N  
ATOM   5118  CA  THR B 178      44.621 -20.650  27.554  1.00 80.80           C  
ANISOU 5118  CA  THR B 178     8106  15159   7437    308    -99   1878       C  
ATOM   5119  C   THR B 178      45.419 -21.801  26.956  1.00 80.79           C  
ANISOU 5119  C   THR B 178     8364  14840   7492    383   -116   2139       C  
ATOM   5120  O   THR B 178      46.365 -22.300  27.575  1.00 83.44           O  
ANISOU 5120  O   THR B 178     8803  15233   7668    541   -170   2295       O  
ATOM   5121  CB  THR B 178      43.317 -21.167  28.164  1.00 82.70           C  
ANISOU 5121  CB  THR B 178     8383  15528   7513    102     61   1983       C  
ATOM   5122  OG1 THR B 178      42.544 -20.064  28.654  1.00 88.01           O  
ANISOU 5122  OG1 THR B 178     8803  16491   8145     38     80   1722       O  
ATOM   5123  CG2 THR B 178      43.604 -22.131  29.309  1.00 86.79           C  
ANISOU 5123  CG2 THR B 178     9065  16190   7721    144    104   2250       C  
ATOM   5124  N   PHE B 179      45.058 -22.232  25.746  1.00 77.18           N  
ANISOU 5124  N   PHE B 179     8019  14044   7263    277    -77   2188       N  
ATOM   5125  CA  PHE B 179      45.754 -23.358  25.135  1.00 77.91           C  
ANISOU 5125  CA  PHE B 179     8371  13822   7411    347    -89   2435       C  
ATOM   5126  C   PHE B 179      47.173 -22.979  24.730  1.00 80.08           C  
ANISOU 5126  C   PHE B 179     8612  14021   7794    579   -235   2365       C  
ATOM   5127  O   PHE B 179      48.062 -23.838  24.715  1.00 82.36           O  
ANISOU 5127  O   PHE B 179     9085  14176   8031    713   -271   2571       O  
ATOM   5128  CB  PHE B 179      44.972 -23.867  23.924  1.00 77.10           C  
ANISOU 5128  CB  PHE B 179     8394  13374   7526    170    -13   2493       C  
ATOM   5129  CG  PHE B 179      45.393 -25.235  23.467  1.00 84.92           C  
ANISOU 5129  CG  PHE B 179     9691  14056   8519    199      7   2792       C  
ATOM   5130  CD1 PHE B 179      46.468 -25.400  22.607  1.00 89.38           C  
ANISOU 5130  CD1 PHE B 179    10344  14371   9248    360    -84   2814       C  
ATOM   5131  CD2 PHE B 179      44.710 -26.359  23.902  1.00 79.78           C  
ANISOU 5131  CD2 PHE B 179     9244  13369   7701     65    114   3050       C  
ATOM   5132  CE1 PHE B 179      46.855 -26.665  22.192  1.00 86.38           C  
ANISOU 5132  CE1 PHE B 179    10251  13705   8864    399    -70   3085       C  
ATOM   5133  CE2 PHE B 179      45.090 -27.624  23.490  1.00 80.61           C  
ANISOU 5133  CE2 PHE B 179     9644  13182   7801     94    122   3326       C  
ATOM   5134  CZ  PHE B 179      46.164 -27.778  22.634  1.00 86.15           C  
ANISOU 5134  CZ  PHE B 179    10433  13632   8667    268     29   3340       C  
ATOM   5135  N   TYR B 180      47.406 -21.705  24.404  1.00 80.82           N  
ANISOU 5135  N   TYR B 180     8472  14201   8034    628   -324   2076       N  
ATOM   5136  CA  TYR B 180      48.735 -21.285  23.978  1.00 73.48           C  
ANISOU 5136  CA  TYR B 180     7496  13209   7216    832   -463   1999       C  
ATOM   5137  C   TYR B 180      49.716 -21.268  25.144  1.00 74.13           C  
ANISOU 5137  C   TYR B 180     7547  13556   7062   1027   -542   2058       C  
ATOM   5138  O   TYR B 180      50.893 -21.609  24.977  1.00 86.25           O  
ANISOU 5138  O   TYR B 180     9159  14999   8613   1208   -626   2152       O  
ATOM   5139  CB  TYR B 180      48.677 -19.891  23.349  1.00 69.95           C  
ANISOU 5139  CB  TYR B 180     6810  12792   6977    815   -543   1671       C  
ATOM   5140  CG  TYR B 180      47.865 -19.768  22.079  1.00 67.90           C  
ANISOU 5140  CG  TYR B 180     6564  12253   6981    645   -493   1581       C  
ATOM   5141  CD1 TYR B 180      47.662 -20.855  21.242  1.00 67.68           C  
ANISOU 5141  CD1 TYR B 180     6770  11889   7058    572   -419   1786       C  
ATOM   5142  CD2 TYR B 180      47.311 -18.548  21.713  1.00 66.19           C  
ANISOU 5142  CD2 TYR B 180     6136  12103   6909    560   -531   1286       C  
ATOM   5143  CE1 TYR B 180      46.923 -20.730  20.078  1.00 65.81           C  
ANISOU 5143  CE1 TYR B 180     6550  11392   7063    415   -379   1702       C  
ATOM   5144  CE2 TYR B 180      46.573 -18.415  20.554  1.00 64.33           C  
ANISOU 5144  CE2 TYR B 180     5915  11609   6917    404   -495   1199       C  
ATOM   5145  CZ  TYR B 180      46.382 -19.508  19.741  1.00 64.13           C  
ANISOU 5145  CZ  TYR B 180     6121  11254   6993    330   -417   1409       C  
ATOM   5146  OH  TYR B 180      45.647 -19.380  18.585  1.00 62.30           O  
ANISOU 5146  OH  TYR B 180     5911  10760   7002    174   -385   1325       O  
ATOM   5147  N   PHE B 181      49.253 -20.875  26.331  1.00 75.68           N  
ANISOU 5147  N   PHE B 181     7632  14084   7039    996   -518   2003       N  
ATOM   5148  CA  PHE B 181      50.135 -20.609  27.459  1.00 80.53           C  
ANISOU 5148  CA  PHE B 181     8178  14981   7439   1174   -609   2006       C  
ATOM   5149  C   PHE B 181      50.036 -21.620  28.590  1.00 82.00           C  
ANISOU 5149  C   PHE B 181     8530  15297   7330   1179   -541   2265       C  
ATOM   5150  O   PHE B 181      51.047 -21.889  29.242  1.00 87.43           O  
ANISOU 5150  O   PHE B 181     9266  16080   7872   1357   -622   2370       O  
ATOM   5151  CB  PHE B 181      49.850 -19.212  28.025  1.00 76.72           C  
ANISOU 5151  CB  PHE B 181     7424  14809   6918   1166   -663   1713       C  
ATOM   5152  CG  PHE B 181      50.083 -18.106  27.037  1.00 76.99           C  
ANISOU 5152  CG  PHE B 181     7286  14749   7218   1180   -759   1445       C  
ATOM   5153  CD1 PHE B 181      51.348 -17.869  26.527  1.00 88.84           C  
ANISOU 5153  CD1 PHE B 181     8768  16150   8838   1351   -890   1414       C  
ATOM   5154  CD2 PHE B 181      49.036 -17.307  26.614  1.00 82.24           C  
ANISOU 5154  CD2 PHE B 181     7810  15426   8011   1021   -721   1225       C  
ATOM   5155  CE1 PHE B 181      51.566 -16.854  25.615  1.00 76.43           C  
ANISOU 5155  CE1 PHE B 181     7045  14491   7503   1352   -980   1171       C  
ATOM   5156  CE2 PHE B 181      49.248 -16.290  25.703  1.00 88.53           C  
ANISOU 5156  CE2 PHE B 181     8462  16127   9047   1028   -818    979       C  
ATOM   5157  CZ  PHE B 181      50.515 -16.064  25.204  1.00 84.85           C  
ANISOU 5157  CZ  PHE B 181     7985  15562   8694   1189   -947    954       C  
ATOM   5158  N   ARG B 182      48.856 -22.181  28.846  1.00 86.88           N  
ANISOU 5158  N   ARG B 182     9234  15922   7853    986   -399   2370       N  
ATOM   5159  CA  ARG B 182      48.683 -23.097  29.967  1.00 89.74           C  
ANISOU 5159  CA  ARG B 182     9752  16425   7920    968   -333   2609       C  
ATOM   5160  C   ARG B 182      49.678 -24.249  29.892  1.00 91.26           C  
ANISOU 5160  C   ARG B 182    10192  16420   8064   1111   -379   2881       C  
ATOM   5161  O   ARG B 182      49.594 -25.096  28.997  1.00 92.22           O  
ANISOU 5161  O   ARG B 182    10501  16220   8318   1062   -338   3032       O  
ATOM   5162  CB  ARG B 182      47.250 -23.637  29.995  1.00 90.60           C  
ANISOU 5162  CB  ARG B 182     9938  16507   7978    716   -168   2700       C  
ATOM   5163  CG  ARG B 182      46.930 -24.518  31.196  1.00 93.66           C  
ANISOU 5163  CG  ARG B 182    10475  17066   8046    663    -89   2934       C  
ATOM   5164  CD  ARG B 182      46.909 -23.718  32.491  1.00 95.03           C  
ANISOU 5164  CD  ARG B 182    10466  17653   7989    712   -110   2799       C  
ATOM   5165  NE  ARG B 182      45.838 -22.724  32.504  1.00102.16           N  
ANISOU 5165  NE  ARG B 182    11138  18735   8943    568    -45   2549       N  
ATOM   5166  CZ  ARG B 182      45.538 -21.956  33.547  1.00 99.33           C  
ANISOU 5166  CZ  ARG B 182    10605  18738   8400    572    -38   2401       C  
ATOM   5167  NH1 ARG B 182      46.227 -22.061  34.676  1.00 97.89           N  
ANISOU 5167  NH1 ARG B 182    10452  18775   7965    706    -93   2481       N  
ATOM   5168  NH2 ARG B 182      44.545 -21.080  33.461  1.00 94.58           N  
ANISOU 5168  NH2 ARG B 182     9799  18274   7863    445     20   2169       N  
ATOM   5169  N   ASP B 183      50.624 -24.283  30.827  1.00 96.62           N  
ANISOU 5169  N   ASP B 183    10876  17286   8551   1293   -469   2941       N  
ATOM   5170  CA  ASP B 183      51.630 -25.336  30.871  1.00 96.73           C  
ANISOU 5170  CA  ASP B 183    11113  17141   8498   1452   -528   3191       C  
ATOM   5171  C   ASP B 183      52.273 -25.326  32.250  1.00 96.40           C  
ANISOU 5171  C   ASP B 183    11061  17395   8172   1592   -597   3253       C  
ATOM   5172  O   ASP B 183      52.207 -24.330  32.976  1.00 95.62           O  
ANISOU 5172  O   ASP B 183    10752  17597   7981   1609   -631   3063       O  
ATOM   5173  CB  ASP B 183      52.684 -25.154  29.774  1.00 95.58           C  
ANISOU 5173  CB  ASP B 183    10949  16762   8605   1615   -635   3127       C  
ATOM   5174  CG  ASP B 183      53.422 -26.440  29.455  1.00 98.11           C  
ANISOU 5174  CG  ASP B 183    11542  16820   8916   1731   -658   3401       C  
ATOM   5175  OD1 ASP B 183      52.879 -27.527  29.744  1.00 99.26           O  
ANISOU 5175  OD1 ASP B 183    11917  16876   8922   1633   -573   3638       O  
ATOM   5176  OD2 ASP B 183      54.546 -26.364  28.916  1.00 98.90           O  
ANISOU 5176  OD2 ASP B 183    11628  16806   9144   1920   -765   3379       O  
ATOM   5177  N   VAL B 184      52.895 -26.447  32.603  1.00109.19           N  
ANISOU 5177  N   VAL B 184    12916  18918   9651   1694   -623   3519       N  
ATOM   5178  CA  VAL B 184      53.519 -26.590  33.915  1.00 98.75           C  
ANISOU 5178  CA  VAL B 184    11623  17849   8050   1826   -692   3611       C  
ATOM   5179  C   VAL B 184      54.832 -25.819  33.925  1.00 93.31           C  
ANISOU 5179  C   VAL B 184    10772  17250   7431   2067   -857   3468       C  
ATOM   5180  O   VAL B 184      55.657 -25.960  33.014  1.00 91.97           O  
ANISOU 5180  O   VAL B 184    10630  16856   7459   2196   -930   3475       O  
ATOM   5181  CB  VAL B 184      53.741 -28.074  34.250  1.00 96.48           C  
ANISOU 5181  CB  VAL B 184    11655  17409   7594   1853   -675   3947       C  
ATOM   5182  CG1 VAL B 184      54.578 -28.216  35.508  1.00120.99           C  
ANISOU 5182  CG1 VAL B 184    14794  20743  10433   2022   -773   4040       C  
ATOM   5183  CG2 VAL B 184      52.406 -28.788  34.408  1.00109.99           C  
ANISOU 5183  CG2 VAL B 184    13516  19077   9197   1597   -516   4091       C  
ATOM   5184  N   ARG B 185      55.030 -25.000  34.957  1.00 94.12           N  
ANISOU 5184  N   ARG B 185    10707  17686   7370   2126   -916   3338       N  
ATOM   5185  CA  ARG B 185      56.249 -24.222  35.113  1.00 93.54           C  
ANISOU 5185  CA  ARG B 185    10472  17737   7334   2344  -1080   3203       C  
ATOM   5186  C   ARG B 185      56.696 -24.229  36.567  1.00114.00           C  
ANISOU 5186  C   ARG B 185    13071  20622   9621   2448  -1146   3271       C  
ATOM   5187  O   ARG B 185      55.876 -24.311  37.486  1.00120.72           O  
ANISOU 5187  O   ARG B 185    13950  21667  10253   2323  -1061   3308       O  
ATOM   5188  CB  ARG B 185      56.059 -22.774  34.647  1.00 91.17           C  
ANISOU 5188  CB  ARG B 185     9884  17542   7216   2309  -1115   2876       C  
ATOM   5189  CG  ARG B 185      55.871 -22.625  33.151  1.00108.88           C  
ANISOU 5189  CG  ARG B 185    12097  19492   9780   2243  -1087   2782       C  
ATOM   5190  CD  ARG B 185      57.156 -22.927  32.396  1.00112.27           C  
ANISOU 5190  CD  ARG B 185    12576  19714  10368   2438  -1197   2844       C  
ATOM   5191  NE  ARG B 185      56.987 -22.784  30.952  1.00116.41           N  
ANISOU 5191  NE  ARG B 185    13079  19955  11195   2373  -1168   2754       N  
ATOM   5192  CZ  ARG B 185      56.577 -23.755  30.139  1.00107.83           C  
ANISOU 5192  CZ  ARG B 185    12195  18565  10212   2290  -1075   2916       C  
ATOM   5193  NH1 ARG B 185      56.284 -24.957  30.619  1.00103.57           N  
ANISOU 5193  NH1 ARG B 185    11896  17958   9497   2257  -1003   3179       N  
ATOM   5194  NH2 ARG B 185      56.457 -23.520  28.840  1.00119.18           N  
ANISOU 5194  NH2 ARG B 185    13599  19758  11925   2236  -1058   2814       N  
ATOM   5195  N   THR B 186      58.010 -24.143  36.765  1.00108.40           N  
ANISOU 5195  N   THR B 186    12338  19947   8902   2677  -1299   3288       N  
ATOM   5196  CA  THR B 186      58.582 -24.142  38.105  1.00109.28           C  
ANISOU 5196  CA  THR B 186    12460  20322   8739   2799  -1385   3353       C  
ATOM   5197  C   THR B 186      58.507 -22.730  38.677  1.00111.19           C  
ANISOU 5197  C   THR B 186    12432  20877   8939   2800  -1443   3080       C  
ATOM   5198  O   THR B 186      59.095 -21.797  38.118  1.00111.27           O  
ANISOU 5198  O   THR B 186    12248  20895   9136   2886  -1543   2879       O  
ATOM   5199  CB  THR B 186      60.034 -24.618  38.073  1.00108.85           C  
ANISOU 5199  CB  THR B 186    12483  20178   8696   3048  -1533   3480       C  
ATOM   5200  OG1 THR B 186      60.846 -23.636  37.418  1.00128.76           O  
ANISOU 5200  OG1 THR B 186    14784  22705  11435   3170  -1650   3268       O  
ATOM   5201  CG2 THR B 186      60.167 -25.943  37.329  1.00111.63           C  
ANISOU 5201  CG2 THR B 186    13094  20191   9129   3066  -1488   3723       C  
ATOM   5202  N   ILE B 187      57.790 -22.569  39.785  1.00113.44           N  
ANISOU 5202  N   ILE B 187    12708  21419   8975   2703  -1382   3073       N  
ATOM   5203  CA  ILE B 187      57.751 -21.304  40.513  1.00116.71           C  
ANISOU 5203  CA  ILE B 187    12892  22151   9301   2722  -1445   2834       C  
ATOM   5204  C   ILE B 187      58.814 -21.369  41.607  1.00120.08           C  
ANISOU 5204  C   ILE B 187    13350  22766   9510   2915  -1586   2919       C  
ATOM   5205  O   ILE B 187      58.730 -22.186  42.528  1.00118.59           O  
ANISOU 5205  O   ILE B 187    13340  22651   9068   2912  -1554   3124       O  
ATOM   5206  CB  ILE B 187      56.352 -21.009  41.074  1.00119.20           C  
ANISOU 5206  CB  ILE B 187    13163  22653   9476   2512  -1298   2754       C  
ATOM   5207  CG1 ILE B 187      56.358 -19.690  41.850  1.00127.92           C  
ANISOU 5207  CG1 ILE B 187    14036  24087  10479   2550  -1374   2501       C  
ATOM   5208  CG2 ILE B 187      55.831 -22.152  41.942  1.00117.05           C  
ANISOU 5208  CG2 ILE B 187    13123  22420   8930   2425  -1190   3018       C  
ATOM   5209  CD1 ILE B 187      54.974 -19.125  42.079  1.00131.16           C  
ANISOU 5209  CD1 ILE B 187    14339  24660  10837   2352  -1237   2344       C  
ATOM   5210  N   GLU B 188      59.832 -20.515  41.493  1.00127.49           N  
ANISOU 5210  N   GLU B 188    14118  23777  10546   3081  -1750   2765       N  
ATOM   5211  CA  GLU B 188      61.016 -20.660  42.334  1.00122.58           C  
ANISOU 5211  CA  GLU B 188    13546  23186   9844   3246  -1865   2821       C  
ATOM   5212  C   GLU B 188      60.717 -20.333  43.793  1.00124.85           C  
ANISOU 5212  C   GLU B 188    13824  23749   9864   3211  -1854   2783       C  
ATOM   5213  O   GLU B 188      61.047 -21.117  44.690  1.00123.76           O  
ANISOU 5213  O   GLU B 188    13860  23625   9538   3257  -1861   2967       O  
ATOM   5214  CB  GLU B 188      62.140 -19.768  41.806  1.00126.70           C  
ANISOU 5214  CB  GLU B 188    13898  23596  10646   3357  -1984   2605       C  
ATOM   5215  N   TYR B 189      60.094 -19.182  44.058  1.00124.31           N  
ANISOU 5215  N   TYR B 189    13560  23892   9779   3128  -1838   2540       N  
ATOM   5216  CA  TYR B 189      59.902 -18.777  45.448  1.00132.65           C  
ANISOU 5216  CA  TYR B 189    14596  25203  10600   3110  -1834   2480       C  
ATOM   5217  C   TYR B 189      58.994 -19.737  46.208  1.00128.69           C  
ANISOU 5217  C   TYR B 189    14282  24821   9792   3001  -1709   2704       C  
ATOM   5218  O   TYR B 189      59.084 -19.811  47.439  1.00130.99           O  
ANISOU 5218  O   TYR B 189    14636  25265   9870   3013  -1714   2743       O  
ATOM   5219  CB  TYR B 189      59.357 -17.345  45.529  1.00138.58           C  
ANISOU 5219  CB  TYR B 189    15108  26137  11407   3041  -1833   2165       C  
ATOM   5220  CG  TYR B 189      57.900 -17.163  45.167  1.00133.18           C  
ANISOU 5220  CG  TYR B 189    14358  25584  10659   2870  -1707   2104       C  
ATOM   5221  CD1 TYR B 189      56.904 -17.327  46.123  1.00126.72           C  
ANISOU 5221  CD1 TYR B 189    13584  25009   9554   2757  -1595   2149       C  
ATOM   5222  CD2 TYR B 189      57.520 -16.787  43.886  1.00134.76           C  
ANISOU 5222  CD2 TYR B 189    14446  25666  11090   2813  -1697   1987       C  
ATOM   5223  CE1 TYR B 189      55.572 -17.149  45.807  1.00127.39           C  
ANISOU 5223  CE1 TYR B 189    13608  25172   9624   2577  -1453   2070       C  
ATOM   5224  CE2 TYR B 189      56.187 -16.603  43.561  1.00140.19           C  
ANISOU 5224  CE2 TYR B 189    15082  26379  11804   2623  -1549   1895       C  
ATOM   5225  CZ  TYR B 189      55.218 -16.786  44.526  1.00131.67           C  
ANISOU 5225  CZ  TYR B 189    14048  25510  10472   2503  -1422   1932       C  
ATOM   5226  OH  TYR B 189      53.891 -16.608  44.210  1.00129.27           O  
ANISOU 5226  OH  TYR B 189    13685  25214  10216   2306  -1263   1832       O  
ATOM   5227  N   LEU B 190      58.127 -20.475  45.512  1.00125.80           N  
ANISOU 5227  N   LEU B 190    14016  24376   9407   2883  -1593   2853       N  
ATOM   5228  CA  LEU B 190      57.319 -21.509  46.148  1.00124.44           C  
ANISOU 5228  CA  LEU B 190    14054  24241   8986   2751  -1454   3083       C  
ATOM   5229  C   LEU B 190      57.949 -22.893  46.060  1.00123.05           C  
ANISOU 5229  C   LEU B 190    14148  23829   8778   2824  -1475   3389       C  
ATOM   5230  O   LEU B 190      57.576 -23.778  46.839  1.00113.64           O  
ANISOU 5230  O   LEU B 190    13157  22658   7361   2746  -1398   3589       O  
ATOM   5231  CB  LEU B 190      55.920 -21.550  45.520  1.00123.10           C  
ANISOU 5231  CB  LEU B 190    13862  23993   8917   2512  -1262   3027       C  
ATOM   5232  CG  LEU B 190      54.852 -20.688  46.195  1.00124.18           C  
ANISOU 5232  CG  LEU B 190    13841  24426   8915   2375  -1168   2832       C  
ATOM   5233  CD1 LEU B 190      53.674 -20.450  45.265  1.00125.09           C  
ANISOU 5233  CD1 LEU B 190    13866  24433   9228   2178  -1021   2709       C  
ATOM   5234  CD2 LEU B 190      54.382 -21.341  47.488  1.00131.68           C  
ANISOU 5234  CD2 LEU B 190    14947  25576   9508   2298  -1084   3009       C  
ATOM   5235  N   GLY B 191      58.889 -23.098  45.141  1.00123.66           N  
ANISOU 5235  N   GLY B 191    14237  23656   9093   2961  -1572   3415       N  
ATOM   5236  CA  GLY B 191      59.574 -24.373  45.031  1.00111.03           C  
ANISOU 5236  CA  GLY B 191    12888  21798   7501   3046  -1601   3674       C  
ATOM   5237  C   GLY B 191      58.724 -25.516  44.525  1.00111.40           C  
ANISOU 5237  C   GLY B 191    13154  21664   7509   2901  -1462   3906       C  
ATOM   5238  O   GLY B 191      59.013 -26.675  44.833  1.00113.30           O  
ANISOU 5238  O   GLY B 191    13649  21753   7648   2927  -1464   4149       O  
ATOM   5239  N   VAL B 192      57.681 -25.223  43.749  1.00121.42           N  
ANISOU 5239  N   VAL B 192    14341  22853   8940   2713  -1326   3790       N  
ATOM   5240  CA  VAL B 192      56.776 -26.238  43.225  1.00124.80           C  
ANISOU 5240  CA  VAL B 192    14966  23057   9395   2531  -1173   3967       C  
ATOM   5241  C   VAL B 192      56.560 -25.961  41.743  1.00119.72           C  
ANISOU 5241  C   VAL B 192    14230  22162   9098   2482  -1135   3844       C  
ATOM   5242  O   VAL B 192      56.746 -24.840  41.267  1.00121.95           O  
ANISOU 5242  O   VAL B 192    14270  22504   9563   2526  -1188   3589       O  
ATOM   5243  CB  VAL B 192      55.429 -26.249  43.985  1.00125.89           C  
ANISOU 5243  CB  VAL B 192    15118  23395   9319   2296  -1011   3974       C  
ATOM   5244  CG1 VAL B 192      54.603 -25.017  43.631  1.00122.24           C  
ANISOU 5244  CG1 VAL B 192    14381  23071   8994   2177   -941   3674       C  
ATOM   5245  CG2 VAL B 192      54.654 -27.528  43.701  1.00120.78           C  
ANISOU 5245  CG2 VAL B 192    14731  22531   8628   2122   -876   4226       C  
ATOM   5246  N   ASN B 193      56.182 -27.005  41.002  1.00123.62           N  
ANISOU 5246  N   ASN B 193    14929  22361   9678   2390  -1050   4030       N  
ATOM   5247  CA  ASN B 193      55.807 -26.858  39.598  1.00120.98           C  
ANISOU 5247  CA  ASN B 193    14539  21771   9657   2310   -992   3935       C  
ATOM   5248  C   ASN B 193      54.287 -26.855  39.496  1.00121.20           C  
ANISOU 5248  C   ASN B 193    14557  21822   9670   2034   -812   3904       C  
ATOM   5249  O   ASN B 193      53.640 -27.897  39.650  1.00124.33           O  
ANISOU 5249  O   ASN B 193    15177  22118   9946   1896   -709   4126       O  
ATOM   5250  CB  ASN B 193      56.399 -27.942  38.701  1.00120.70           C  
ANISOU 5250  CB  ASN B 193    14724  21374   9761   2396  -1022   4138       C  
ATOM   5251  CG  ASN B 193      57.902 -27.918  38.680  1.00120.69           C  
ANISOU 5251  CG  ASN B 193    14711  21342   9803   2673  -1198   4154       C  
ATOM   5252  OD1 ASN B 193      58.527 -27.026  39.250  1.00125.96           O  
ANISOU 5252  OD1 ASN B 193    15191  22248  10423   2797  -1303   4000       O  
ATOM   5253  ND2 ASN B 193      58.491 -28.842  37.934  1.00120.57           N  
ANISOU 5253  ND2 ASN B 193    14882  21027   9902   2772  -1232   4323       N  
ATOM   5254  N   ALA B 194      53.730 -25.684  39.228  1.00109.35           N  
ANISOU 5254  N   ALA B 194    12801  20453   8294   1955   -780   3629       N  
ATOM   5255  CA  ALA B 194      52.297 -25.465  39.162  1.00125.56           C  
ANISOU 5255  CA  ALA B 194    14790  22573  10345   1707   -618   3550       C  
ATOM   5256  C   ALA B 194      51.832 -25.449  37.712  1.00126.22           C  
ANISOU 5256  C   ALA B 194    14852  22361  10743   1605   -561   3481       C  
ATOM   5257  O   ALA B 194      52.601 -25.174  36.788  1.00110.20           O  
ANISOU 5257  O   ALA B 194    12772  20147   8953   1732   -654   3401       O  
ATOM   5258  CB  ALA B 194      51.922 -24.151  39.851  1.00133.95           C  
ANISOU 5258  CB  ALA B 194    15582  23983  11328   1687   -623   3278       C  
ATOM   5259  N   CYS B 195      50.551 -25.759  37.524  1.00116.29           N  
ANISOU 5259  N   CYS B 195    13637  21065   9483   1368   -404   3517       N  
ATOM   5260  CA  CYS B 195      49.917 -25.689  36.208  1.00109.35           C  
ANISOU 5260  CA  CYS B 195    12729  19928   8891   1239   -336   3440       C  
ATOM   5261  C   CYS B 195      49.343 -24.287  36.072  1.00107.54           C  
ANISOU 5261  C   CYS B 195    12198  19887   8776   1179   -325   3110       C  
ATOM   5262  O   CYS B 195      48.229 -24.002  36.511  1.00108.22           O  
ANISOU 5262  O   CYS B 195    12198  20158   8765   1005   -210   3037       O  
ATOM   5263  CB  CYS B 195      48.839 -26.754  36.066  1.00112.30           C  
ANISOU 5263  CB  CYS B 195    13305  20158   9205   1013   -182   3653       C  
ATOM   5264  SG  CYS B 195      47.908 -26.661  34.519  1.00113.39           S  
ANISOU 5264  SG  CYS B 195    13408  19995   9680    827    -90   3558       S  
ATOM   5265  N   ILE B 196      50.120 -23.401  35.446  1.00 93.56           N  
ANISOU 5265  N   ILE B 196    10266  18070   7213   1324   -448   2907       N  
ATOM   5266  CA  ILE B 196      49.831 -21.979  35.384  1.00 98.32           C  
ANISOU 5266  CA  ILE B 196    10583  18860   7914   1313   -482   2581       C  
ATOM   5267  C   ILE B 196      49.884 -21.531  33.927  1.00 97.23           C  
ANISOU 5267  C   ILE B 196    10367  18452   8123   1299   -514   2431       C  
ATOM   5268  O   ILE B 196      50.215 -22.303  33.028  1.00 98.40           O  
ANISOU 5268  O   ILE B 196    10677  18285   8424   1313   -513   2578       O  
ATOM   5269  CB  ILE B 196      50.806 -21.149  36.244  1.00102.70           C  
ANISOU 5269  CB  ILE B 196    10996  19683   8343   1513   -628   2453       C  
ATOM   5270  CG1 ILE B 196      52.256 -21.386  35.807  1.00 97.42           C  
ANISOU 5270  CG1 ILE B 196    10393  18843   7778   1730   -775   2528       C  
ATOM   5271  CG2 ILE B 196      50.648 -21.498  37.715  1.00115.31           C  
ANISOU 5271  CG2 ILE B 196    12659  21566   9589   1511   -590   2579       C  
ATOM   5272  CD1 ILE B 196      52.859 -20.236  35.026  1.00 89.22           C  
ANISOU 5272  CD1 ILE B 196     9146  17769   6985   1827   -899   2267       C  
ATOM   5273  N   MET B 197      49.551 -20.263  33.706  1.00 89.82           N  
ANISOU 5273  N   MET B 197     9185  17639   7305   1272   -547   2133       N  
ATOM   5274  CA  MET B 197      49.627 -19.663  32.379  1.00 90.41           C  
ANISOU 5274  CA  MET B 197     9163  17486   7703   1261   -595   1956       C  
ATOM   5275  C   MET B 197      51.066 -19.221  32.140  1.00 86.77           C  
ANISOU 5275  C   MET B 197     8646  16991   7331   1484   -768   1892       C  
ATOM   5276  O   MET B 197      51.523 -18.227  32.715  1.00 87.37           O  
ANISOU 5276  O   MET B 197     8545  17309   7344   1588   -875   1709       O  
ATOM   5277  CB  MET B 197      48.658 -18.490  32.273  1.00 93.17           C  
ANISOU 5277  CB  MET B 197     9283  17985   8134   1138   -567   1662       C  
ATOM   5278  CG  MET B 197      47.192 -18.892  32.347  1.00 86.80           C  
ANISOU 5278  CG  MET B 197     8511  17193   7277    907   -393   1710       C  
ATOM   5279  SD  MET B 197      46.604 -19.705  30.850  1.00 84.91           S  
ANISOU 5279  SD  MET B 197     8429  16522   7313    747   -300   1827       S  
ATOM   5280  CE  MET B 197      46.523 -18.314  29.721  1.00 83.44           C  
ANISOU 5280  CE  MET B 197     8011  16243   7449    740   -391   1473       C  
ATOM   5281  N   ALA B 198      51.783 -19.962  31.295  1.00 94.53           N  
ANISOU 5281  N   ALA B 198     9781  17677   8458   1558   -798   2044       N  
ATOM   5282  CA  ALA B 198      53.209 -19.726  31.067  1.00 86.47           C  
ANISOU 5282  CA  ALA B 198     8727  16615   7511   1775   -953   2024       C  
ATOM   5283  C   ALA B 198      53.365 -18.621  30.027  1.00 81.28           C  
ANISOU 5283  C   ALA B 198     7884  15867   7132   1772  -1032   1755       C  
ATOM   5284  O   ALA B 198      53.668 -18.853  28.854  1.00 79.00           O  
ANISOU 5284  O   ALA B 198     7653  15289   7074   1777  -1042   1771       O  
ATOM   5285  CB  ALA B 198      53.900 -21.012  30.630  1.00 87.20           C  
ANISOU 5285  CB  ALA B 198     9063  16439   7629   1862   -948   2300       C  
ATOM   5286  N   PHE B 199      53.145 -17.388  30.476  1.00 84.28           N  
ANISOU 5286  N   PHE B 199     8043  16499   7482   1762  -1091   1501       N  
ATOM   5287  CA  PHE B 199      53.312 -16.237  29.609  1.00 83.57           C  
ANISOU 5287  CA  PHE B 199     7769  16353   7630   1761  -1185   1230       C  
ATOM   5288  C   PHE B 199      54.794 -15.942  29.394  1.00 89.71           C  
ANISOU 5288  C   PHE B 199     8499  17112   8475   1963  -1347   1210       C  
ATOM   5289  O   PHE B 199      55.642 -16.350  30.192  1.00 95.85           O  
ANISOU 5289  O   PHE B 199     9330  18011   9075   2115  -1404   1351       O  
ATOM   5290  CB  PHE B 199      52.630 -15.008  30.207  1.00 89.88           C  
ANISOU 5290  CB  PHE B 199     8356  17433   8362   1697  -1210    964       C  
ATOM   5291  CG  PHE B 199      51.146 -15.155  30.377  1.00 88.54           C  
ANISOU 5291  CG  PHE B 199     8194  17304   8141   1497  -1055    948       C  
ATOM   5292  CD1 PHE B 199      50.323 -15.339  29.279  1.00 84.24           C  
ANISOU 5292  CD1 PHE B 199     7690  16504   7815   1336   -966    923       C  
ATOM   5293  CD2 PHE B 199      50.572 -15.092  31.635  1.00 89.19           C  
ANISOU 5293  CD2 PHE B 199     8241  17688   7958   1467   -998    954       C  
ATOM   5294  CE1 PHE B 199      48.958 -15.468  29.434  1.00 85.98           C  
ANISOU 5294  CE1 PHE B 199     7906  16770   7992   1150   -825    908       C  
ATOM   5295  CE2 PHE B 199      49.206 -15.220  31.795  1.00 88.11           C  
ANISOU 5295  CE2 PHE B 199     8100  17606   7773   1281   -851    938       C  
ATOM   5296  CZ  PHE B 199      48.399 -15.407  30.693  1.00 86.00           C  
ANISOU 5296  CZ  PHE B 199     7864  17084   7728   1122   -766    915       C  
ATOM   5297  N   PRO B 200      55.133 -15.237  28.318  1.00 98.12           N  
ANISOU 5297  N   PRO B 200     9463  18026   9794   1965  -1426   1036       N  
ATOM   5298  CA  PRO B 200      56.514 -14.768  28.145  1.00 98.92           C  
ANISOU 5298  CA  PRO B 200     9479  18150   9958   2145  -1588    980       C  
ATOM   5299  C   PRO B 200      56.953 -13.937  29.338  1.00100.80           C  
ANISOU 5299  C   PRO B 200     9566  18739   9996   2248  -1705    865       C  
ATOM   5300  O   PRO B 200      56.352 -12.893  29.631  1.00103.06           O  
ANISOU 5300  O   PRO B 200     9694  19199  10264   2174  -1735    636       O  
ATOM   5301  CB  PRO B 200      56.449 -13.921  26.862  1.00105.95           C  
ANISOU 5301  CB  PRO B 200    10257  18860  11140   2071  -1639    759       C  
ATOM   5302  CG  PRO B 200      54.987 -13.694  26.593  1.00106.84           C  
ANISOU 5302  CG  PRO B 200    10354  18927  11312   1862  -1525    651       C  
ATOM   5303  CD  PRO B 200      54.277 -14.871  27.176  1.00102.79           C  
ANISOU 5303  CD  PRO B 200    10019  18407  10628   1798  -1370    891       C  
ATOM   5304  N   PRO B 201      57.995 -14.366  30.057  1.00103.58           N  
ANISOU 5304  N   PRO B 201     9965  19200  10191   2424  -1778   1016       N  
ATOM   5305  CA  PRO B 201      58.368 -13.650  31.289  1.00100.85           C  
ANISOU 5305  CA  PRO B 201     9521  19144   9654   2498  -1859    916       C  
ATOM   5306  C   PRO B 201      58.666 -12.173  31.088  1.00102.49           C  
ANISOU 5306  C   PRO B 201     9643  19236  10062   2416  -1886    587       C  
ATOM   5307  O   PRO B 201      58.474 -11.387  32.024  1.00104.46           O  
ANISOU 5307  O   PRO B 201     9834  19660  10195   2392  -1892    444       O  
ATOM   5308  CB  PRO B 201      59.613 -14.410  31.772  1.00102.15           C  
ANISOU 5308  CB  PRO B 201     9805  19284   9724   2672  -1906   1121       C  
ATOM   5309  CG  PRO B 201      59.491 -15.765  31.171  1.00104.16           C  
ANISOU 5309  CG  PRO B 201    10231  19353   9991   2693  -1834   1392       C  
ATOM   5310  CD  PRO B 201      58.841 -15.555  29.836  1.00 98.73           C  
ANISOU 5310  CD  PRO B 201     9527  18409   9574   2546  -1767   1279       C  
ATOM   5311  N   GLU B 202      59.128 -11.764  29.903  1.00108.22           N  
ANISOU 5311  N   GLU B 202    10383  19661  11076   2368  -1900    474       N  
ATOM   5312  CA  GLU B 202      59.508 -10.369  29.711  1.00109.29           C  
ANISOU 5312  CA  GLU B 202    10488  19653  11385   2284  -1928    199       C  
ATOM   5313  C   GLU B 202      58.321  -9.424  29.853  1.00111.62           C  
ANISOU 5313  C   GLU B 202    10706  20020  11684   2142  -1886    -18       C  
ATOM   5314  O   GLU B 202      58.516  -8.245  30.167  1.00113.20           O  
ANISOU 5314  O   GLU B 202    10894  20186  11930   2094  -1909   -220       O  
ATOM   5315  CB  GLU B 202      60.159 -10.176  28.335  1.00110.21           C  
ANISOU 5315  CB  GLU B 202    10654  19424  11795   2240  -1945    144       C  
ATOM   5316  CG  GLU B 202      59.215 -10.353  27.145  1.00118.40           C  
ANISOU 5316  CG  GLU B 202    11685  20300  13002   2124  -1894    113       C  
ATOM   5317  CD  GLU B 202      59.154 -11.777  26.636  1.00121.95           C  
ANISOU 5317  CD  GLU B 202    12179  20728  13428   2210  -1871    375       C  
ATOM   5318  OE1 GLU B 202      59.590 -12.693  27.366  1.00126.32           O  
ANISOU 5318  OE1 GLU B 202    12776  21436  13784   2355  -1884    598       O  
ATOM   5319  OE2 GLU B 202      58.653 -11.983  25.509  1.00117.20           O  
ANISOU 5319  OE2 GLU B 202    11586  19943  13002   2131  -1839    368       O  
ATOM   5320  N   LYS B 203      57.103  -9.912  29.633  1.00131.84           N  
ANISOU 5320  N   LYS B 203    13222  22676  14197   2073  -1826     26       N  
ATOM   5321  CA  LYS B 203      55.888  -9.117  29.758  1.00134.72           C  
ANISOU 5321  CA  LYS B 203    13508  23119  14561   1938  -1778   -174       C  
ATOM   5322  C   LYS B 203      54.828  -9.879  30.537  1.00127.41           C  
ANISOU 5322  C   LYS B 203    12512  22528  13372   1935  -1727    -39       C  
ATOM   5323  O   LYS B 203      53.646  -9.874  30.183  1.00127.34           O  
ANISOU 5323  O   LYS B 203    12435  22558  13390   1814  -1669    -98       O  
ATOM   5324  CB  LYS B 203      55.343  -8.708  28.391  1.00141.78           C  
ANISOU 5324  CB  LYS B 203    14412  23722  15738   1795  -1750   -312       C  
ATOM   5325  CG  LYS B 203      56.288  -7.873  27.548  1.00148.73           C  
ANISOU 5325  CG  LYS B 203    15375  24264  16872   1765  -1796   -443       C  
ATOM   5326  CD  LYS B 203      55.527  -7.122  26.462  1.00154.49           C  
ANISOU 5326  CD  LYS B 203    16123  24736  17840   1600  -1765   -629       C  
ATOM   5327  CE  LYS B 203      56.459  -6.602  25.380  1.00178.70           C  
ANISOU 5327  CE  LYS B 203    19288  27451  21160   1563  -1806   -684       C  
ATOM   5328  NZ  LYS B 203      57.680  -5.965  25.947  1.00147.81           N  
ANISOU 5328  NZ  LYS B 203    15412  23534  17214   1634  -1867   -711       N  
ATOM   5329  N   TYR B 204      55.232 -10.549  31.618  1.00109.65           N  
ANISOU 5329  N   TYR B 204    10285  20522  10854   2059  -1746    151       N  
ATOM   5330  CA  TYR B 204      54.278 -11.357  32.369  1.00114.16           C  
ANISOU 5330  CA  TYR B 204    10852  21364  11158   2032  -1675    318       C  
ATOM   5331  C   TYR B 204      53.194 -10.479  32.980  1.00110.46           C  
ANISOU 5331  C   TYR B 204    10247  21133  10589   1933  -1644    102       C  
ATOM   5332  O   TYR B 204      52.010 -10.839  32.967  1.00103.32           O  
ANISOU 5332  O   TYR B 204     9382  20208   9665   1782  -1490    126       O  
ATOM   5333  CB  TYR B 204      54.995 -12.159  33.454  1.00101.16           C  
ANISOU 5333  CB  TYR B 204     9321  19860   9257   2166  -1682    554       C  
ATOM   5334  CG  TYR B 204      54.176 -13.323  33.962  1.00 96.13           C  
ANISOU 5334  CG  TYR B 204     8856  19214   8453   2071  -1502    785       C  
ATOM   5335  CD1 TYR B 204      53.231 -13.152  34.964  1.00102.08           C  
ANISOU 5335  CD1 TYR B 204     9575  20220   8991   1988  -1418    743       C  
ATOM   5336  CD2 TYR B 204      54.341 -14.595  33.429  1.00 98.96           C  
ANISOU 5336  CD2 TYR B 204     9417  19314   8869   2061  -1419   1046       C  
ATOM   5337  CE1 TYR B 204      52.475 -14.216  35.422  1.00101.64           C  
ANISOU 5337  CE1 TYR B 204     9676  20162   8779   1887  -1253    959       C  
ATOM   5338  CE2 TYR B 204      53.591 -15.663  33.880  1.00100.00           C  
ANISOU 5338  CE2 TYR B 204     9718  19431   8847   1964  -1263   1262       C  
ATOM   5339  CZ  TYR B 204      52.659 -15.470  34.876  1.00 98.85           C  
ANISOU 5339  CZ  TYR B 204     9529  19543   8486   1871  -1180   1220       C  
ATOM   5340  OH  TYR B 204      51.911 -16.533  35.328  1.00 98.48           O  
ANISOU 5340  OH  TYR B 204     9650  19488   8279   1761  -1024   1440       O  
ATOM   5341  N   ALA B 205      53.579  -9.322  33.522  1.00111.23           N  
ANISOU 5341  N   ALA B 205    10315  21235  10712   1956  -1676   -120       N  
ATOM   5342  CA  ALA B 205      52.596  -8.433  34.129  1.00111.87           C  
ANISOU 5342  CA  ALA B 205    10299  21493  10714   1873  -1628   -336       C  
ATOM   5343  C   ALA B 205      51.584  -7.953  33.096  1.00113.24           C  
ANISOU 5343  C   ALA B 205    10419  21498  11111   1717  -1575   -513       C  
ATOM   5344  O   ALA B 205      50.385  -7.861  33.387  1.00115.19           O  
ANISOU 5344  O   ALA B 205    10569  21941  11258   1624  -1508   -585       O  
ATOM   5345  CB  ALA B 205      53.299  -7.243  34.783  1.00126.98           C  
ANISOU 5345  CB  ALA B 205    12228  23370  12647   1931  -1673   -528       C  
ATOM   5346  N   GLN B 206      52.045  -7.640  31.882  1.00109.05           N  
ANISOU 5346  N   GLN B 206     9956  20598  10881   1680  -1601   -585       N  
ATOM   5347  CA  GLN B 206      51.128  -7.156  30.856  1.00109.50           C  
ANISOU 5347  CA  GLN B 206     9993  20449  11165   1530  -1553   -752       C  
ATOM   5348  C   GLN B 206      50.183  -8.260  30.396  1.00 97.88           C  
ANISOU 5348  C   GLN B 206     8454  19075   9663   1449  -1495   -592       C  
ATOM   5349  O   GLN B 206      49.000  -8.007  30.144  1.00105.87           O  
ANISOU 5349  O   GLN B 206     9390  20114  10723   1316  -1428   -713       O  
ATOM   5350  CB  GLN B 206      51.907  -6.590  29.669  1.00113.79           C  
ANISOU 5350  CB  GLN B 206    10648  20568  12019   1505  -1599   -842       C  
ATOM   5351  CG  GLN B 206      52.704  -5.337  29.988  1.00123.87           C  
ANISOU 5351  CG  GLN B 206    11990  21719  13354   1542  -1651  -1012       C  
ATOM   5352  CD  GLN B 206      54.031  -5.643  30.647  1.00117.33           C  
ANISOU 5352  CD  GLN B 206    11200  20966  12415   1686  -1717   -876       C  
ATOM   5353  OE1 GLN B 206      54.878  -6.320  30.068  1.00115.65           O  
ANISOU 5353  OE1 GLN B 206    11043  20614  12286   1737  -1753   -727       O  
ATOM   5354  NE2 GLN B 206      54.217  -5.152  31.866  1.00126.29           N  
ANISOU 5354  NE2 GLN B 206    12305  22319  13362   1755  -1734   -928       N  
ATOM   5355  N   TRP B 207      50.686  -9.490  30.279  1.00103.20           N  
ANISOU 5355  N   TRP B 207     9193  19749  10269   1514  -1497   -309       N  
ATOM   5356  CA  TRP B 207      49.830 -10.599  29.873  1.00 99.98           C  
ANISOU 5356  CA  TRP B 207     8935  19152   9899   1373  -1313   -116       C  
ATOM   5357  C   TRP B 207      48.819 -10.939  30.961  1.00102.21           C  
ANISOU 5357  C   TRP B 207     9228  19671   9935   1293  -1174    -54       C  
ATOM   5358  O   TRP B 207      47.617 -11.047  30.692  1.00103.04           O  
ANISOU 5358  O   TRP B 207     9325  19734  10091   1129  -1049    -91       O  
ATOM   5359  CB  TRP B 207      50.683 -11.820  29.529  1.00102.25           C  
ANISOU 5359  CB  TRP B 207     9420  19221  10208   1444  -1286    177       C  
ATOM   5360  CG  TRP B 207      51.149 -11.830  28.109  1.00101.29           C  
ANISOU 5360  CG  TRP B 207     9334  18770  10381   1437  -1336    155       C  
ATOM   5361  CD1 TRP B 207      52.368 -11.434  27.640  1.00104.80           C  
ANISOU 5361  CD1 TRP B 207     9738  19142  10938   1570  -1484    105       C  
ATOM   5362  CD2 TRP B 207      50.398 -12.255  26.966  1.00102.55           C  
ANISOU 5362  CD2 TRP B 207     9576  18632  10757   1283  -1236    181       C  
ATOM   5363  NE1 TRP B 207      52.422 -11.589  26.276  1.00 99.32           N  
ANISOU 5363  NE1 TRP B 207     9098  18125  10514   1510  -1478     98       N  
ATOM   5364  CE2 TRP B 207      51.225 -12.090  25.838  1.00 95.35           C  
ANISOU 5364  CE2 TRP B 207     8676  17473  10080   1336  -1329    144       C  
ATOM   5365  CE3 TRP B 207      49.106 -12.759  26.787  1.00 97.26           C  
ANISOU 5365  CE3 TRP B 207     8970  17881  10103   1102  -1078    235       C  
ATOM   5366  CZ2 TRP B 207      50.803 -12.414  24.552  1.00 80.41           C  
ANISOU 5366  CZ2 TRP B 207     6866  15252   8433   1217  -1271    157       C  
ATOM   5367  CZ3 TRP B 207      48.688 -13.078  25.508  1.00 78.58           C  
ANISOU 5367  CZ3 TRP B 207     6683  15187   7985    984  -1025    249       C  
ATOM   5368  CH2 TRP B 207      49.534 -12.904  24.408  1.00 69.76           C  
ANISOU 5368  CH2 TRP B 207     5585  13823   7096   1043  -1122    210       C  
ATOM   5369  N   SER B 208      49.288 -11.116  32.198  1.00104.38           N  
ANISOU 5369  N   SER B 208     9519  20200   9938   1404  -1193     43       N  
ATOM   5370  CA  SER B 208      48.372 -11.401  33.297  1.00 98.57           C  
ANISOU 5370  CA  SER B 208     8790  19714   8948   1331  -1064     98       C  
ATOM   5371  C   SER B 208      47.299 -10.326  33.405  1.00 98.43           C  
ANISOU 5371  C   SER B 208     8584  19867   8949   1236  -1049   -190       C  
ATOM   5372  O   SER B 208      46.119 -10.631  33.613  1.00 90.31           O  
ANISOU 5372  O   SER B 208     7558  18900   7857   1090   -896   -170       O  
ATOM   5373  CB  SER B 208      49.144 -11.515  34.611  1.00100.44           C  
ANISOU 5373  CB  SER B 208     9051  20216   8898   1481  -1122    197       C  
ATOM   5374  OG  SER B 208      50.063 -12.591  34.571  1.00101.54           O  
ANISOU 5374  OG  SER B 208     9373  20204   9004   1569  -1128    475       O  
ATOM   5375  N   ALA B 209      47.690  -9.059  33.256  1.00100.96           N  
ANISOU 5375  N   ALA B 209     8740  20264   9357   1316  -1211   -462       N  
ATOM   5376  CA  ALA B 209      46.716  -7.976  33.317  1.00 97.17           C  
ANISOU 5376  CA  ALA B 209     8082  19935   8904   1242  -1217   -754       C  
ATOM   5377  C   ALA B 209      45.754  -8.033  32.139  1.00102.42           C  
ANISOU 5377  C   ALA B 209     8740  20351   9824   1072  -1133   -822       C  
ATOM   5378  O   ALA B 209      44.545  -7.836  32.308  1.00102.72           O  
ANISOU 5378  O   ALA B 209     8703  20494   9833    951  -1029   -925       O  
ATOM   5379  CB  ALA B 209      47.436  -6.628  33.356  1.00106.95           C  
ANISOU 5379  CB  ALA B 209     9300  21090  10247   1339  -1337  -1006       C  
ATOM   5380  N   GLY B 210      46.267  -8.305  30.938  1.00107.72           N  
ANISOU 5380  N   GLY B 210     9490  20694  10746   1060  -1177   -767       N  
ATOM   5381  CA  GLY B 210      45.403  -8.340  29.770  1.00111.57           C  
ANISOU 5381  CA  GLY B 210     9979  20926  11485    900  -1110   -833       C  
ATOM   5382  C   GLY B 210      44.474  -9.540  29.754  1.00102.04           C  
ANISOU 5382  C   GLY B 210     8905  19632  10233    750   -903   -604       C  
ATOM   5383  O   GLY B 210      43.284  -9.409  29.455  1.00 97.74           O  
ANISOU 5383  O   GLY B 210     8304  19070   9762    599   -808   -699       O  
ATOM   5384  N   ILE B 211      45.001 -10.723  30.073  1.00 89.90           N  
ANISOU 5384  N   ILE B 211     7547  18036   8573    787   -835   -300       N  
ATOM   5385  CA  ILE B 211      44.176 -11.927  30.055  1.00 88.07           C  
ANISOU 5385  CA  ILE B 211     7464  17706   8291    640   -647    -61       C  
ATOM   5386  C   ILE B 211      43.128 -11.877  31.161  1.00 97.88           C  
ANISOU 5386  C   ILE B 211     8629  19266   9293    558   -527    -87       C  
ATOM   5387  O   ILE B 211      42.001 -12.358  30.989  1.00 89.99           O  
ANISOU 5387  O   ILE B 211     7657  18226   8309    384   -378    -29       O  
ATOM   5388  CB  ILE B 211      45.061 -13.181  30.169  1.00 87.80           C  
ANISOU 5388  CB  ILE B 211     7652  17536   8172    714   -623    268       C  
ATOM   5389  CG1 ILE B 211      46.003 -13.283  28.965  1.00100.77           C  
ANISOU 5389  CG1 ILE B 211     9370  18849  10069    783   -723    294       C  
ATOM   5390  CG2 ILE B 211      44.204 -14.433  30.287  1.00 86.91           C  
ANISOU 5390  CG2 ILE B 211     7705  17348   7971    559   -436    524       C  
ATOM   5391  CD1 ILE B 211      45.295 -13.345  27.620  1.00 84.95           C  
ANISOU 5391  CD1 ILE B 211     7391  16535   8349    629   -673    240       C  
ATOM   5392  N   ALA B 212      43.477 -11.299  32.313  1.00 94.99           N  
ANISOU 5392  N   ALA B 212     8167  19224   8699    678   -589   -174       N  
ATOM   5393  CA  ALA B 212      42.512 -11.198  33.401  1.00 92.76           C  
ANISOU 5393  CA  ALA B 212     7804  19265   8177    609   -475   -213       C  
ATOM   5394  C   ALA B 212      41.332 -10.318  33.010  1.00 92.25           C  
ANISOU 5394  C   ALA B 212     7558  19252   8239    491   -444   -487       C  
ATOM   5395  O   ALA B 212      40.183 -10.614  33.358  1.00 92.55           O  
ANISOU 5395  O   ALA B 212     7569  19413   8184    350   -289   -463       O  
ATOM   5396  CB  ALA B 212      43.193 -10.652  34.657  1.00 94.16           C  
ANISOU 5396  CB  ALA B 212     7912  19768   8098    775   -568   -275       C  
ATOM   5397  N   LEU B 213      41.594  -9.232  32.280  1.00 92.11           N  
ANISOU 5397  N   LEU B 213     7415  19146   8436    545   -593   -750       N  
ATOM   5398  CA  LEU B 213      40.520  -8.314  31.917  1.00 85.31           C  
ANISOU 5398  CA  LEU B 213     6380  18337   7698    451   -586  -1031       C  
ATOM   5399  C   LEU B 213      39.614  -8.890  30.837  1.00 84.83           C  
ANISOU 5399  C   LEU B 213     6376  17997   7857    261   -471   -967       C  
ATOM   5400  O   LEU B 213      38.408  -8.616  30.840  1.00 96.87           O  
ANISOU 5400  O   LEU B 213     7793  19615   9398    137   -380  -1093       O  
ATOM   5401  CB  LEU B 213      41.110  -6.979  31.466  1.00 85.66           C  
ANISOU 5401  CB  LEU B 213     6289  18359   7898    564   -796  -1328       C  
ATOM   5402  CG  LEU B 213      41.860  -6.220  32.564  1.00 89.28           C  
ANISOU 5402  CG  LEU B 213     6662  19121   8140    742   -923  -1440       C  
ATOM   5403  CD1 LEU B 213      42.625  -5.043  31.984  1.00101.12           C  
ANISOU 5403  CD1 LEU B 213     8289  20273   9860    826  -1030  -1644       C  
ATOM   5404  CD2 LEU B 213      40.899  -5.750  33.647  1.00 95.26           C  
ANISOU 5404  CD2 LEU B 213     7285  20238   8672    722   -846  -1579       C  
ATOM   5405  N   MET B 214      40.153  -9.690  29.913  1.00 83.92           N  
ANISOU 5405  N   MET B 214     6432  17545   7911    237   -471   -772       N  
ATOM   5406  CA  MET B 214      39.286 -10.319  28.923  1.00 79.97           C  
ANISOU 5406  CA  MET B 214     6007  16775   7604     52   -358   -689       C  
ATOM   5407  C   MET B 214      38.443 -11.426  29.540  1.00 82.70           C  
ANISOU 5407  C   MET B 214     6446  17213   7763    -83   -156   -447       C  
ATOM   5408  O   MET B 214      37.406 -11.788  28.975  1.00 78.94           O  
ANISOU 5408  O   MET B 214     5982  16612   7400   -261    -44   -421       O  
ATOM   5409  CB  MET B 214      40.100 -10.874  27.750  1.00 71.43           C  
ANISOU 5409  CB  MET B 214     5090  15300   6749     68   -415   -550       C  
ATOM   5410  CG  MET B 214      40.820 -12.186  28.021  1.00 82.78           C  
ANISOU 5410  CG  MET B 214     6750  16642   8060    109   -355   -201       C  
ATOM   5411  SD  MET B 214      41.478 -12.926  26.511  1.00 83.45           S  
ANISOU 5411  SD  MET B 214     7033  16242   8432     94   -388    -41       S  
ATOM   5412  CE  MET B 214      39.997 -13.620  25.788  1.00 70.22           C  
ANISOU 5412  CE  MET B 214     5426  14367   6886   -163   -217     42       C  
ATOM   5413  N   LYS B 215      38.865 -11.969  30.684  1.00 88.98           N  
ANISOU 5413  N   LYS B 215     7312  18222   8272    -10   -113   -268       N  
ATOM   5414  CA  LYS B 215      38.017 -12.919  31.394  1.00 88.48           C  
ANISOU 5414  CA  LYS B 215     7324  18293   8002   -146     75    -58       C  
ATOM   5415  C   LYS B 215      36.779 -12.219  31.937  1.00 89.53           C  
ANISOU 5415  C   LYS B 215     7251  18717   8049   -239    156   -269       C  
ATOM   5416  O   LYS B 215      35.674 -12.772  31.895  1.00 90.51           O  
ANISOU 5416  O   LYS B 215     7386  18849   8156   -422    313   -184       O  
ATOM   5417  CB  LYS B 215      38.792 -13.580  32.534  1.00 92.76           C  
ANISOU 5417  CB  LYS B 215     7987  19009   8248    -39     87    166       C  
ATOM   5418  CG  LYS B 215      39.518 -14.864  32.155  1.00101.03           C  
ANISOU 5418  CG  LYS B 215     9295  19777   9313    -31    105    495       C  
ATOM   5419  CD  LYS B 215      40.176 -15.488  33.381  1.00100.13           C  
ANISOU 5419  CD  LYS B 215     9294  19863   8887     68    118    704       C  
ATOM   5420  CE  LYS B 215      41.672 -15.242  33.437  1.00 92.51           C  
ANISOU 5420  CE  LYS B 215     8366  18854   7928    293    -55    706       C  
ATOM   5421  NZ  LYS B 215      42.231 -15.670  34.752  1.00 95.03           N  
ANISOU 5421  NZ  LYS B 215     8763  19417   7928    394    -52    867       N  
ATOM   5422  N   ASN B 216      36.948 -10.996  32.445  1.00 82.67           N  
ANISOU 5422  N   ASN B 216     6193  18092   7124   -114     48   -548       N  
ATOM   5423  CA  ASN B 216      35.812 -10.232  32.948  1.00 83.01           C  
ANISOU 5423  CA  ASN B 216     6030  18420   7091   -177    111   -779       C  
ATOM   5424  C   ASN B 216      34.870  -9.839  31.817  1.00 88.64           C  
ANISOU 5424  C   ASN B 216     6650  18940   8089   -314    125   -950       C  
ATOM   5425  O   ASN B 216      33.648  -9.997  31.928  1.00 92.47           O  
ANISOU 5425  O   ASN B 216     7059  19530   8546   -468    266   -970       O  
ATOM   5426  CB  ASN B 216      36.305  -8.982  33.682  1.00 85.04           C  
ANISOU 5426  CB  ASN B 216     6123  18952   7236      5    -33  -1046       C  
ATOM   5427  CG  ASN B 216      37.094  -9.308  34.935  1.00 85.79           C  
ANISOU 5427  CG  ASN B 216     6290  19283   7022    132    -39   -895       C  
ATOM   5428  OD1 ASN B 216      36.879 -10.340  35.570  1.00 88.46           O  
ANISOU 5428  OD1 ASN B 216     6749  19702   7161     59    105   -636       O  
ATOM   5429  ND2 ASN B 216      38.009  -8.419  35.304  1.00 86.51           N  
ANISOU 5429  ND2 ASN B 216     6313  19488   7069    318   -211  -1056       N  
ATOM   5430  N   ILE B 217      35.421  -9.334  30.712  1.00 82.50           N  
ANISOU 5430  N   ILE B 217     5878  17881   7589   -264    -22  -1073       N  
ATOM   5431  CA  ILE B 217      34.585  -8.831  29.625  1.00 79.19           C  
ANISOU 5431  CA  ILE B 217     5366  17276   7448   -380    -35  -1265       C  
ATOM   5432  C   ILE B 217      33.825  -9.977  28.969  1.00 78.50           C  
ANISOU 5432  C   ILE B 217     5410  16955   7460   -583    123  -1033       C  
ATOM   5433  O   ILE B 217      32.589 -10.009  28.969  1.00 80.09           O  
ANISOU 5433  O   ILE B 217     5520  17241   7671   -734    242  -1086       O  
ATOM   5434  CB  ILE B 217      35.437  -8.060  28.601  1.00 78.00           C  
ANISOU 5434  CB  ILE B 217     5210  16868   7558   -282   -235  -1434       C  
ATOM   5435  CG1 ILE B 217      36.052  -6.822  29.258  1.00 81.61           C  
ANISOU 5435  CG1 ILE B 217     5520  17572   7917    -98   -399  -1690       C  
ATOM   5436  CG2 ILE B 217      34.595  -7.674  27.393  1.00 85.88           C  
ANISOU 5436  CG2 ILE B 217     6148  17630   8854   -415   -248  -1600       C  
ATOM   5437  CD1 ILE B 217      37.068  -6.099  28.393  1.00 81.97           C  
ANISOU 5437  CD1 ILE B 217     5662  17303   8180     11   -583  -1812       C  
ATOM   5438  N   LEU B 218      34.555 -10.937  28.400  1.00 77.52           N  
ANISOU 5438  N   LEU B 218     5505  16538   7412   -589    123   -774       N  
ATOM   5439  CA  LEU B 218      33.898 -12.039  27.708  1.00 75.20           C  
ANISOU 5439  CA  LEU B 218     5358  15991   7222   -779    256   -548       C  
ATOM   5440  C   LEU B 218      33.136 -12.931  28.678  1.00 80.37           C  
ANISOU 5440  C   LEU B 218     6053  16868   7614   -898    446   -336       C  
ATOM   5441  O   LEU B 218      32.163 -13.584  28.284  1.00 82.18           O  
ANISOU 5441  O   LEU B 218     6327  16992   7904  -1092    575   -224       O  
ATOM   5442  CB  LEU B 218      34.927 -12.866  26.940  1.00 77.05           C  
ANISOU 5442  CB  LEU B 218     5829  15870   7577   -736    206   -317       C  
ATOM   5443  CG  LEU B 218      35.689 -12.140  25.831  1.00 73.74           C  
ANISOU 5443  CG  LEU B 218     5398  15185   7436   -644     32   -490       C  
ATOM   5444  CD1 LEU B 218      36.770 -13.040  25.256  1.00 70.19           C  
ANISOU 5444  CD1 LEU B 218     5181  14434   7055   -583     -3   -240       C  
ATOM   5445  CD2 LEU B 218      34.739 -11.676  24.747  1.00 81.08           C  
ANISOU 5445  CD2 LEU B 218     6245  15922   8638   -788     30   -671       C  
ATOM   5446  N   GLY B 219      33.555 -12.967  29.941  1.00 80.18           N  
ANISOU 5446  N   GLY B 219     6017  17151   7295   -793    462   -278       N  
ATOM   5447  CA  GLY B 219      33.020 -13.922  30.888  1.00 83.03           C  
ANISOU 5447  CA  GLY B 219     6454  17708   7386   -899    633    -39       C  
ATOM   5448  C   GLY B 219      32.037 -13.356  31.891  1.00 85.06           C  
ANISOU 5448  C   GLY B 219     6502  18374   7444   -945    728   -200       C  
ATOM   5449  O   GLY B 219      31.417 -14.119  32.638  1.00 87.52           O  
ANISOU 5449  O   GLY B 219     6858  18859   7536  -1064    886    -15       O  
ATOM   5450  N   PHE B 220      31.880 -12.032  31.936  1.00 84.18           N  
ANISOU 5450  N   PHE B 220     6167  18423   7396   -852    631   -542       N  
ATOM   5451  CA  PHE B 220      30.980 -11.443  32.919  1.00 86.19           C  
ANISOU 5451  CA  PHE B 220     6217  19080   7452   -874    716   -713       C  
ATOM   5452  C   PHE B 220      30.251 -10.217  32.382  1.00 84.77           C  
ANISOU 5452  C   PHE B 220     5805  18936   7469   -877    650  -1075       C  
ATOM   5453  O   PHE B 220      29.020 -10.227  32.273  1.00 85.51           O  
ANISOU 5453  O   PHE B 220     5785  19109   7594  -1032    770  -1138       O  
ATOM   5454  CB  PHE B 220      31.758 -11.076  34.187  1.00 87.75           C  
ANISOU 5454  CB  PHE B 220     6388  19590   7363   -691    661   -740       C  
ATOM   5455  CG  PHE B 220      30.885 -10.780  35.371  1.00 90.42           C  
ANISOU 5455  CG  PHE B 220     6566  20357   7432   -724    782   -833       C  
ATOM   5456  CD1 PHE B 220      30.245 -11.806  36.046  1.00 93.00           C  
ANISOU 5456  CD1 PHE B 220     6970  20829   7539   -876    976   -585       C  
ATOM   5457  CD2 PHE B 220      30.709  -9.480  35.813  1.00 90.42           C  
ANISOU 5457  CD2 PHE B 220     6345  20619   7392   -603    700  -1168       C  
ATOM   5458  CE1 PHE B 220      29.440 -11.542  37.138  1.00 95.56           C  
ANISOU 5458  CE1 PHE B 220     7143  21558   7608   -910   1096   -670       C  
ATOM   5459  CE2 PHE B 220      29.905  -9.209  36.906  1.00 99.35           C  
ANISOU 5459  CE2 PHE B 220     7328  22151   8269   -625    816  -1259       C  
ATOM   5460  CZ  PHE B 220      29.270 -10.241  37.569  1.00 98.24           C  
ANISOU 5460  CZ  PHE B 220     7257  22159   7910   -780   1019  -1009       C  
ATOM   5461  N   ILE B 221      30.989  -9.158  32.048  1.00 81.72           N  
ANISOU 5461  N   ILE B 221     9033  15688   6329   1731    377  -1217       N  
ATOM   5462  CA  ILE B 221      30.371  -7.905  31.627  1.00 84.15           C  
ANISOU 5462  CA  ILE B 221     9540  15819   6616   1546    357  -1493       C  
ATOM   5463  C   ILE B 221      29.461  -8.142  30.429  1.00 78.64           C  
ANISOU 5463  C   ILE B 221     9079  14582   6219   1403    351  -1398       C  
ATOM   5464  O   ILE B 221      28.239  -7.985  30.530  1.00 78.99           O  
ANISOU 5464  O   ILE B 221     9168  14512   6331   1430    344  -1268       O  
ATOM   5465  CB  ILE B 221      31.422  -6.824  31.309  1.00 86.16           C  
ANISOU 5465  CB  ILE B 221     9862  16120   6755   1356    335  -1937       C  
ATOM   5466  CG1 ILE B 221      32.162  -6.406  32.582  1.00 79.13           C  
ANISOU 5466  CG1 ILE B 221     8738  15594   5734   1437    280  -1984       C  
ATOM   5467  CG2 ILE B 221      30.759  -5.616  30.653  1.00 86.18           C  
ANISOU 5467  CG2 ILE B 221    10139  15707   6899   1129    317  -2139       C  
ATOM   5468  CD1 ILE B 221      33.445  -7.151  32.827  1.00 87.53           C  
ANISOU 5468  CD1 ILE B 221     9576  16964   6718   1542    262  -1979       C  
ATOM   5469  N   ILE B 222      30.043  -8.517  29.287  1.00 78.13           N  
ANISOU 5469  N   ILE B 222     9169  14180   6339   1251    353  -1468       N  
ATOM   5470  CA  ILE B 222      29.237  -8.713  28.082  1.00 73.90           C  
ANISOU 5470  CA  ILE B 222     8901  13113   6066   1098    321  -1405       C  
ATOM   5471  C   ILE B 222      28.092  -9.687  28.334  1.00 78.11           C  
ANISOU 5471  C   ILE B 222     9352  13560   6768   1225    316   -997       C  
ATOM   5472  O   ILE B 222      26.943  -9.344  28.028  1.00 77.19           O  
ANISOU 5472  O   ILE B 222     9343  13223   6764   1169    260   -962       O  
ATOM   5473  CB  ILE B 222      30.134  -9.134  26.906  1.00 67.95           C  
ANISOU 5473  CB  ILE B 222     8334  12022   5463    939    351  -1507       C  
ATOM   5474  CG1 ILE B 222      31.021  -7.958  26.484  1.00 71.10           C  
ANISOU 5474  CG1 ILE B 222     8873  12410   5733    759    373  -1952       C  
ATOM   5475  CG2 ILE B 222      29.282  -9.626  25.739  1.00 65.25           C  
ANISOU 5475  CG2 ILE B 222     8268  11138   5386    812    304  -1368       C  
ATOM   5476  CD1 ILE B 222      32.032  -8.299  25.413  1.00 76.34           C  
ANISOU 5476  CD1 ILE B 222     9707  12771   6529    606    447  -2082       C  
ATOM   5477  N   PRO B 223      28.318 -10.886  28.878  1.00 80.09           N  
ANISOU 5477  N   PRO B 223     9414  13965   7051   1396    378   -685       N  
ATOM   5478  CA  PRO B 223      27.172 -11.728  29.260  1.00 75.91           C  
ANISOU 5478  CA  PRO B 223     8796  13382   6665   1514    404   -308       C  
ATOM   5479  C   PRO B 223      26.163 -11.003  30.136  1.00 73.53           C  
ANISOU 5479  C   PRO B 223     8386  13294   6258   1604    405   -293       C  
ATOM   5480  O   PRO B 223      24.970 -10.976  29.815  1.00 82.63           O  
ANISOU 5480  O   PRO B 223     9592  14202   7600   1550    374   -186       O  
ATOM   5481  CB  PRO B 223      27.838 -12.902  29.991  1.00 75.00           C  
ANISOU 5481  CB  PRO B 223     8486  13519   6493   1724    498    -34       C  
ATOM   5482  CG  PRO B 223      29.185 -13.004  29.373  1.00 73.40           C  
ANISOU 5482  CG  PRO B 223     8345  13265   6277   1650    499   -217       C  
ATOM   5483  CD  PRO B 223      29.603 -11.593  29.041  1.00 74.31           C  
ANISOU 5483  CD  PRO B 223     8565  13406   6264   1482    435   -651       C  
ATOM   5484  N   LEU B 224      26.618 -10.392  31.234  1.00 78.95           N  
ANISOU 5484  N   LEU B 224     8921  14429   6646   1738    438   -406       N  
ATOM   5485  CA  LEU B 224      25.689  -9.761  32.165  1.00 79.38           C  
ANISOU 5485  CA  LEU B 224     8883  14698   6581   1846    476   -371       C  
ATOM   5486  C   LEU B 224      24.914  -8.622  31.514  1.00 77.02           C  
ANISOU 5486  C   LEU B 224     8756  14148   6358   1683    409   -605       C  
ATOM   5487  O   LEU B 224      23.809  -8.293  31.959  1.00 80.87           O  
ANISOU 5487  O   LEU B 224     9190  14656   6883   1750    444   -509       O  
ATOM   5488  CB  LEU B 224      26.445  -9.250  33.392  1.00 81.85           C  
ANISOU 5488  CB  LEU B 224     9055  15520   6524   1998    510   -493       C  
ATOM   5489  CG  LEU B 224      25.587  -8.674  34.520  1.00 78.36           C  
ANISOU 5489  CG  LEU B 224     8530  15337   5908   2141    585   -437       C  
ATOM   5490  CD1 LEU B 224      24.625  -9.723  35.058  1.00 80.00           C  
ANISOU 5490  CD1 LEU B 224     8616  15522   6258   2308    698    -12       C  
ATOM   5491  CD2 LEU B 224      26.468  -8.130  35.637  1.00 82.83           C  
ANISOU 5491  CD2 LEU B 224     9005  16389   6078   2262    589   -601       C  
ATOM   5492  N   ILE B 225      25.470  -8.003  30.469  1.00 78.48           N  
ANISOU 5492  N   ILE B 225     9158  14090   6570   1480    327   -907       N  
ATOM   5493  CA  ILE B 225      24.726  -6.964  29.766  1.00 77.16           C  
ANISOU 5493  CA  ILE B 225     9197  13645   6477   1339    256  -1115       C  
ATOM   5494  C   ILE B 225      23.504  -7.558  29.079  1.00 80.58           C  
ANISOU 5494  C   ILE B 225     9677  13699   7242   1300    191   -874       C  
ATOM   5495  O   ILE B 225      22.460  -6.902  28.974  1.00 83.63           O  
ANISOU 5495  O   ILE B 225    10104  13964   7709   1291    147   -903       O  
ATOM   5496  CB  ILE B 225      25.632  -6.232  28.760  1.00 74.28           C  
ANISOU 5496  CB  ILE B 225     9095  13070   6060   1128    204  -1485       C  
ATOM   5497  CG1 ILE B 225      26.656  -5.366  29.498  1.00 78.46           C  
ANISOU 5497  CG1 ILE B 225     9564  13983   6263   1141    261  -1778       C  
ATOM   5498  CG2 ILE B 225      24.796  -5.375  27.820  1.00 81.36           C  
ANISOU 5498  CG2 ILE B 225    10261  13579   7072    989    114  -1647       C  
ATOM   5499  CD1 ILE B 225      27.755  -4.815  28.610  1.00 76.85           C  
ANISOU 5499  CD1 ILE B 225     9572  13611   6015    933    254  -2130       C  
ATOM   5500  N   PHE B 226      23.605  -8.800  28.603  1.00 78.87           N  
ANISOU 5500  N   PHE B 226     9452  13290   7228   1277    183   -637       N  
ATOM   5501  CA  PHE B 226      22.472  -9.444  27.950  1.00 75.38           C  
ANISOU 5501  CA  PHE B 226     9044  12487   7108   1218    109   -409       C  
ATOM   5502  C   PHE B 226      21.430  -9.897  28.965  1.00 85.29           C  
ANISOU 5502  C   PHE B 226    10025  13939   8444   1391    200   -102       C  
ATOM   5503  O   PHE B 226      20.253  -9.534  28.859  1.00 97.63           O  
ANISOU 5503  O   PHE B 226    11555  15366  10173   1379    149    -59       O  
ATOM   5504  CB  PHE B 226      22.955 -10.632  27.115  1.00 82.51           C  
ANISOU 5504  CB  PHE B 226    10058  13106   8188   1122     91   -265       C  
ATOM   5505  CG  PHE B 226      23.605 -10.239  25.819  1.00 84.90           C  
ANISOU 5505  CG  PHE B 226    10694  13057   8509    913     -5   -537       C  
ATOM   5506  CD1 PHE B 226      24.887  -9.720  25.800  1.00 77.65           C  
ANISOU 5506  CD1 PHE B 226     9851  12280   7372    880     51   -805       C  
ATOM   5507  CD2 PHE B 226      22.934 -10.396  24.618  1.00 82.70           C  
ANISOU 5507  CD2 PHE B 226    10659  12298   8466    745   -148   -527       C  
ATOM   5508  CE1 PHE B 226      25.487  -9.358  24.609  1.00 78.61           C  
ANISOU 5508  CE1 PHE B 226    10297  12055   7515    683      3  -1057       C  
ATOM   5509  CE2 PHE B 226      23.528 -10.037  23.424  1.00 78.53           C  
ANISOU 5509  CE2 PHE B 226    10484  11422   7931    559   -219   -774       C  
ATOM   5510  CZ  PHE B 226      24.807  -9.518  23.420  1.00 77.19           C  
ANISOU 5510  CZ  PHE B 226    10398  11383   7547    528   -124  -1037       C  
ATOM   5511  N   ILE B 227      21.842 -10.689  29.958  1.00 81.84           N  
ANISOU 5511  N   ILE B 227     9390  13812   7893   1561    343    116       N  
ATOM   5512  CA  ILE B 227      20.889 -11.176  30.951  1.00 87.01           C  
ANISOU 5512  CA  ILE B 227     9810  14637   8614   1727    471    419       C  
ATOM   5513  C   ILE B 227      20.196 -10.008  31.640  1.00 90.47           C  
ANISOU 5513  C   ILE B 227    10175  15269   8931   1806    507    291       C  
ATOM   5514  O   ILE B 227      18.983 -10.040  31.882  1.00 91.69           O  
ANISOU 5514  O   ILE B 227    10204  15355   9277   1848    554    454       O  
ATOM   5515  CB  ILE B 227      21.588 -12.097  31.968  1.00 89.67           C  
ANISOU 5515  CB  ILE B 227     9997  15299   8774   1922    625    643       C  
ATOM   5516  CG1 ILE B 227      22.161 -13.329  31.263  1.00 87.03           C  
ANISOU 5516  CG1 ILE B 227     9738  14734   8594   1859    614    803       C  
ATOM   5517  CG2 ILE B 227      20.613 -12.520  33.061  1.00 92.15           C  
ANISOU 5517  CG2 ILE B 227    10104  15787   9121   2100    795    942       C  
ATOM   5518  CD1 ILE B 227      23.675 -13.377  31.221  1.00 89.25           C  
ANISOU 5518  CD1 ILE B 227    10076  15179   8655   1885    601    651       C  
ATOM   5519  N   ALA B 228      20.952  -8.960  31.973  1.00 88.83           N  
ANISOU 5519  N   ALA B 228    10040  15299   8414   1822    500     -6       N  
ATOM   5520  CA  ALA B 228      20.352  -7.795  32.613  1.00 89.12           C  
ANISOU 5520  CA  ALA B 228    10046  15505   8310   1893    550   -147       C  
ATOM   5521  C   ALA B 228      19.376  -7.104  31.670  1.00 89.36           C  
ANISOU 5521  C   ALA B 228    10193  15177   8582   1764    429   -262       C  
ATOM   5522  O   ALA B 228      18.233  -6.815  32.044  1.00 90.66           O  
ANISOU 5522  O   ALA B 228    10239  15334   8871   1845    486   -157       O  
ATOM   5523  CB  ALA B 228      21.443  -6.825  33.066  1.00 89.10           C  
ANISOU 5523  CB  ALA B 228    10129  15802   7924   1902    557   -469       C  
ATOM   5524  N   THR B 229      19.808  -6.835  30.436  1.00 99.24           N  
ANISOU 5524  N   THR B 229    11685  16119   9904   1574    266   -474       N  
ATOM   5525  CA  THR B 229      18.918  -6.212  29.463  1.00 96.35           C  
ANISOU 5525  CA  THR B 229    11467  15389   9754   1462    117   -580       C  
ATOM   5526  C   THR B 229      17.710  -7.097  29.184  1.00 94.64           C  
ANISOU 5526  C   THR B 229    11098  14942   9918   1463     69   -269       C  
ATOM   5527  O   THR B 229      16.580  -6.605  29.084  1.00102.35           O  
ANISOU 5527  O   THR B 229    12014  15800  11073   1488     19   -249       O  
ATOM   5528  CB  THR B 229      19.676  -5.917  28.167  1.00 97.80           C  
ANISOU 5528  CB  THR B 229    11977  15255   9928   1257    -36   -840       C  
ATOM   5529  OG1 THR B 229      20.753  -5.010  28.436  1.00 92.33           O  
ANISOU 5529  OG1 THR B 229    11408  14772   8902   1237     26  -1154       O  
ATOM   5530  CG2 THR B 229      18.748  -5.302  27.129  1.00101.04           C  
ANISOU 5530  CG2 THR B 229    12577  15270  10541   1158   -215   -940       C  
ATOM   5531  N   CYS B 230      17.927  -8.408  29.059  1.00 86.54           N  
ANISOU 5531  N   CYS B 230    10001  13848   9033   1436     88    -25       N  
ATOM   5532  CA  CYS B 230      16.816  -9.313  28.790  1.00 89.75           C  
ANISOU 5532  CA  CYS B 230    10263  14028   9811   1409     50    265       C  
ATOM   5533  C   CYS B 230      15.818  -9.321  29.942  1.00 87.92           C  
ANISOU 5533  C   CYS B 230     9724  14036   9648   1586    227    474       C  
ATOM   5534  O   CYS B 230      14.602  -9.310  29.718  1.00 90.86           O  
ANISOU 5534  O   CYS B 230     9968  14232  10323   1568    172    579       O  
ATOM   5535  CB  CYS B 230      17.339 -10.726  28.529  1.00 85.78           C  
ANISOU 5535  CB  CYS B 230     9768  13421   9405   1352     80    483       C  
ATOM   5536  SG  CYS B 230      18.164 -10.948  26.936  1.00 80.84           S  
ANISOU 5536  SG  CYS B 230     9513  12372   8829   1113   -124    303       S  
ATOM   5537  N   TYR B 231      16.308  -9.335  31.183  1.00 89.22           N  
ANISOU 5537  N   TYR B 231     9768  14598   9535   1761    441    533       N  
ATOM   5538  CA  TYR B 231      15.403  -9.328  32.326  1.00 86.64           C  
ANISOU 5538  CA  TYR B 231     9186  14491   9241   1938    648    729       C  
ATOM   5539  C   TYR B 231      14.613  -8.028  32.377  1.00 89.28           C  
ANISOU 5539  C   TYR B 231     9512  14820   9591   1974    624    547       C  
ATOM   5540  O   TYR B 231      13.377  -8.033  32.383  1.00 94.92           O  
ANISOU 5540  O   TYR B 231    10047  15410  10607   1998    646    683       O  
ATOM   5541  CB  TYR B 231      16.176  -9.530  33.629  1.00 91.83           C  
ANISOU 5541  CB  TYR B 231     9780  15570   9541   2124    864    803       C  
ATOM   5542  CG  TYR B 231      15.332  -9.238  34.849  1.00 93.00           C  
ANISOU 5542  CG  TYR B 231     9738  15955   9642   2314   1098    939       C  
ATOM   5543  CD1 TYR B 231      14.345 -10.124  35.260  1.00 95.02           C  
ANISOU 5543  CD1 TYR B 231     9780  16150  10174   2376   1262   1270       C  
ATOM   5544  CD2 TYR B 231      15.507  -8.069  35.578  1.00 90.32           C  
ANISOU 5544  CD2 TYR B 231     9450  15881   8988   2421   1174    731       C  
ATOM   5545  CE1 TYR B 231      13.564  -9.861  36.367  1.00 95.82           C  
ANISOU 5545  CE1 TYR B 231     9720  16445  10243   2549   1511   1396       C  
ATOM   5546  CE2 TYR B 231      14.731  -7.797  36.688  1.00 92.46           C  
ANISOU 5546  CE2 TYR B 231     9577  16345   9206   2598   1413    855       C  
ATOM   5547  CZ  TYR B 231      13.760  -8.697  37.077  1.00 96.25           C  
ANISOU 5547  CZ  TYR B 231     9843  16756   9970   2665   1587   1191       C  
ATOM   5548  OH  TYR B 231      12.981  -8.433  38.181  1.00106.12           O  
ANISOU 5548  OH  TYR B 231    10963  18180  11179   2841   1860   1317       O  
ATOM   5549  N   PHE B 232      15.317  -6.894  32.417  1.00 89.23           N  
ANISOU 5549  N   PHE B 232     9691  14944   9268   1978    588    234       N  
ATOM   5550  CA  PHE B 232      14.625  -5.611  32.445  1.00 92.48           C  
ANISOU 5550  CA  PHE B 232    10136  15335   9668   2021    578     49       C  
ATOM   5551  C   PHE B 232      13.790  -5.419  31.188  1.00 97.27           C  
ANISOU 5551  C   PHE B 232    10804  15527  10626   1891    344      4       C  
ATOM   5552  O   PHE B 232      12.805  -4.672  31.203  1.00 94.09           O  
ANISOU 5552  O   PHE B 232    10331  15056  10361   1957    338    -30       O  
ATOM   5553  CB  PHE B 232      15.631  -4.471  32.597  1.00 94.31           C  
ANISOU 5553  CB  PHE B 232    10600  15741   9490   2014    577   -301       C  
ATOM   5554  CG  PHE B 232      16.243  -4.383  33.967  1.00 90.99           C  
ANISOU 5554  CG  PHE B 232    10109  15758   8705   2168    793   -288       C  
ATOM   5555  CD1 PHE B 232      15.527  -3.849  35.026  1.00 93.42           C  
ANISOU 5555  CD1 PHE B 232    10298  16275   8923   2341    996   -230       C  
ATOM   5556  CD2 PHE B 232      17.535  -4.827  34.194  1.00 91.47           C  
ANISOU 5556  CD2 PHE B 232    10228  16017   8509   2146    789   -337       C  
ATOM   5557  CE1 PHE B 232      16.085  -3.765  36.288  1.00 91.91           C  
ANISOU 5557  CE1 PHE B 232    10080  16474   8365   2483   1181   -221       C  
ATOM   5558  CE2 PHE B 232      18.100  -4.745  35.454  1.00 92.16           C  
ANISOU 5558  CE2 PHE B 232    10258  16514   8246   2294    950   -329       C  
ATOM   5559  CZ  PHE B 232      17.373  -4.213  36.502  1.00 90.17           C  
ANISOU 5559  CZ  PHE B 232     9921  16460   7881   2459   1141   -273       C  
ATOM   5560  N   GLY B 233      14.167  -6.082  30.095  1.00105.10           N  
ANISOU 5560  N   GLY B 233    11937  16235  11761   1715    146      5       N  
ATOM   5561  CA  GLY B 233      13.320  -6.077  28.915  1.00109.98           C  
ANISOU 5561  CA  GLY B 233    12614  16451  12724   1591   -100      1       C  
ATOM   5562  C   GLY B 233      12.071  -6.917  29.099  1.00106.44           C  
ANISOU 5562  C   GLY B 233    11842  15921  12679   1622    -74    318       C  
ATOM   5563  O   GLY B 233      10.995  -6.562  28.612  1.00112.22           O  
ANISOU 5563  O   GLY B 233    12493  16448  13698   1611   -218    323       O  
ATOM   5564  N   ILE B 234      12.197  -8.046  29.799  1.00103.36           N  
ANISOU 5564  N   ILE B 234    11262  15684  12324   1662    111    585       N  
ATOM   5565  CA  ILE B 234      11.022  -8.843  30.133  1.00 98.58           C  
ANISOU 5565  CA  ILE B 234    10333  15030  12093   1692    201    888       C  
ATOM   5566  C   ILE B 234      10.163  -8.114  31.157  1.00 98.12           C  
ANISOU 5566  C   ILE B 234    10036  15196  12049   1885    410    927       C  
ATOM   5567  O   ILE B 234       8.929  -8.110  31.067  1.00100.53           O  
ANISOU 5567  O   ILE B 234    10103  15373  12721   1897    390   1042       O  
ATOM   5568  CB  ILE B 234      11.452 -10.230  30.648  1.00 94.53           C  
ANISOU 5568  CB  ILE B 234     9727  14613  11577   1694    380   1161       C  
ATOM   5569  CG1 ILE B 234      11.978 -11.088  29.496  1.00 93.93           C  
ANISOU 5569  CG1 ILE B 234     9851  14226  11611   1486    172   1171       C  
ATOM   5570  CG2 ILE B 234      10.294 -10.916  31.366  1.00105.71           C  
ANISOU 5570  CG2 ILE B 234    10793  16066  13305   1766    586   1469       C  
ATOM   5571  CD1 ILE B 234      12.677 -12.358  29.944  1.00 96.81           C  
ANISOU 5571  CD1 ILE B 234    10202  14687  11894   1504    349   1397       C  
ATOM   5572  N   ARG B 235      10.799  -7.487  32.146  1.00 85.36           N  
ANISOU 5572  N   ARG B 235     8479  13915  10040   2038    616    828       N  
ATOM   5573  CA  ARG B 235      10.051  -6.845  33.221  1.00 86.93           C  
ANISOU 5573  CA  ARG B 235     8486  14335  10211   2233    863    877       C  
ATOM   5574  C   ARG B 235       9.251  -5.660  32.693  1.00 93.80           C  
ANISOU 5574  C   ARG B 235     9369  15045  11226   2249    723    690       C  
ATOM   5575  O   ARG B 235       8.121  -5.422  33.135  1.00100.57           O  
ANISOU 5575  O   ARG B 235     9973  15913  12327   2363    854    806       O  
ATOM   5576  CB  ARG B 235      11.008  -6.435  34.343  1.00 89.81           C  
ANISOU 5576  CB  ARG B 235     8964  15080  10078   2376   1083    790       C  
ATOM   5577  CG  ARG B 235      10.337  -5.862  35.588  1.00100.03           C  
ANISOU 5577  CG  ARG B 235    10105  16619  11283   2587   1387    857       C  
ATOM   5578  CD  ARG B 235      11.336  -5.793  36.749  1.00 90.80           C  
ANISOU 5578  CD  ARG B 235     9051  15830   9620   2716   1593    828       C  
ATOM   5579  NE  ARG B 235      10.757  -5.247  37.977  1.00109.91           N  
ANISOU 5579  NE  ARG B 235    11379  18477  11904   2918   1901    886       N  
ATOM   5580  CZ  ARG B 235      10.726  -3.959  38.307  1.00119.45           C  
ANISOU 5580  CZ  ARG B 235    12712  19791  12883   2997   1958    653       C  
ATOM   5581  NH1 ARG B 235      10.170  -3.590  39.454  1.00127.88           N  
ANISOU 5581  NH1 ARG B 235    13704  21047  13837   3184   2269    738       N  
ATOM   5582  NH2 ARG B 235      11.253  -3.042  37.507  1.00117.01           N  
ANISOU 5582  NH2 ARG B 235    12626  19386  12447   2889   1729    335       N  
ATOM   5583  N   LYS B 236       9.813  -4.906  31.742  1.00 93.82           N  
ANISOU 5583  N   LYS B 236     9671  14887  11090   2147    471    404       N  
ATOM   5584  CA  LYS B 236       9.112  -3.731  31.233  1.00 89.21           C  
ANISOU 5584  CA  LYS B 236     9147  14143  10604   2185    336    219       C  
ATOM   5585  C   LYS B 236       7.894  -4.124  30.405  1.00 90.79           C  
ANISOU 5585  C   LYS B 236     9145  14031  11320   2120    122    359       C  
ATOM   5586  O   LYS B 236       6.845  -3.473  30.486  1.00102.11           O  
ANISOU 5586  O   LYS B 236    10409  15420  12970   2235    129    365       O  
ATOM   5587  CB  LYS B 236      10.063  -2.866  30.398  1.00 87.91           C  
ANISOU 5587  CB  LYS B 236     9395  13859  10146   2083    137   -122       C  
ATOM   5588  CG  LYS B 236      10.540  -3.494  29.081  1.00102.16           C  
ANISOU 5588  CG  LYS B 236    11408  15345  12062   1864   -161   -166       C  
ATOM   5589  CD  LYS B 236      11.438  -2.527  28.300  1.00107.11           C  
ANISOU 5589  CD  LYS B 236    12462  15840  12394   1773   -308   -517       C  
ATOM   5590  CE  LYS B 236      11.999  -3.137  27.012  1.00 98.87           C  
ANISOU 5590  CE  LYS B 236    11673  14467  11424   1556   -566   -570       C  
ATOM   5591  NZ  LYS B 236      10.944  -3.545  26.043  1.00106.10           N  
ANISOU 5591  NZ  LYS B 236    12531  15029  12752   1483   -838   -448       N  
ATOM   5592  N   HIS B 237       8.007  -5.187  29.606  1.00106.59           N  
ANISOU 5592  N   HIS B 237    11157  15814  13529   1939    -71    472       N  
ATOM   5593  CA  HIS B 237       6.883  -5.617  28.780  1.00113.12           C  
ANISOU 5593  CA  HIS B 237    11798  16339  14845   1850   -310    594       C  
ATOM   5594  C   HIS B 237       5.710  -6.078  29.636  1.00115.03           C  
ANISOU 5594  C   HIS B 237    11574  16696  15436   1959    -84    868       C  
ATOM   5595  O   HIS B 237       4.560  -5.693  29.397  1.00122.88           O  
ANISOU 5595  O   HIS B 237    12343  17568  16778   2010   -185    895       O  
ATOM   5596  CB  HIS B 237       7.330  -6.734  27.836  1.00115.35           C  
ANISOU 5596  CB  HIS B 237    12218  16372  15238   1620   -527    662       C  
ATOM   5597  CG  HIS B 237       6.266  -7.186  26.884  1.00120.05           C  
ANISOU 5597  CG  HIS B 237    12669  16637  16307   1494   -823    757       C  
ATOM   5598  ND1 HIS B 237       6.136  -6.670  25.612  1.00121.34           N  
ANISOU 5598  ND1 HIS B 237    13090  16481  16534   1393  -1205    568       N  
ATOM   5599  CD2 HIS B 237       5.284  -8.109  27.017  1.00123.40           C  
ANISOU 5599  CD2 HIS B 237    12726  16999  17162   1443   -799   1015       C  
ATOM   5600  CE1 HIS B 237       5.119  -7.254  25.004  1.00126.99           C  
ANISOU 5600  CE1 HIS B 237    13596  16963  17694   1291  -1433    704       C  
ATOM   5601  NE2 HIS B 237       4.585  -8.131  25.835  1.00126.93           N  
ANISOU 5601  NE2 HIS B 237    13194  17106  17929   1309  -1189    971       N  
ATOM   5602  N   LEU B 238       5.984  -6.907  30.645  1.00100.56           N  
ANISOU 5602  N   LEU B 238     9593  15093  13521   2003    232   1076       N  
ATOM   5603  CA  LEU B 238       4.911  -7.456  31.467  1.00106.13           C  
ANISOU 5603  CA  LEU B 238     9878  15884  14562   2089    491   1349       C  
ATOM   5604  C   LEU B 238       4.198  -6.378  32.278  1.00106.33           C  
ANISOU 5604  C   LEU B 238     9738  16082  14581   2313    708   1305       C  
ATOM   5605  O   LEU B 238       2.981  -6.457  32.481  1.00116.96           O  
ANISOU 5605  O   LEU B 238    10722  17374  16342   2369    792   1455       O  
ATOM   5606  CB  LEU B 238       5.470  -8.533  32.398  1.00102.14           C  
ANISOU 5606  CB  LEU B 238     9326  15581  13900   2107    803   1572       C  
ATOM   5607  CG  LEU B 238       5.968  -9.821  31.741  1.00 97.33           C  
ANISOU 5607  CG  LEU B 238     8808  14792  13381   1903    666   1693       C  
ATOM   5608  CD1 LEU B 238       6.747 -10.657  32.742  1.00 99.84           C  
ANISOU 5608  CD1 LEU B 238     9161  15353  13422   1978    982   1871       C  
ATOM   5609  CD2 LEU B 238       4.806 -10.622  31.175  1.00100.83           C  
ANISOU 5609  CD2 LEU B 238     8959  14965  14387   1756    551   1879       C  
ATOM   5610  N   LEU B 239       4.927  -5.364  32.749  1.00105.93           N  
ANISOU 5610  N   LEU B 239     9941  16230  14077   2440    811   1098       N  
ATOM   5611  CA  LEU B 239       4.301  -4.347  33.587  1.00108.83           C  
ANISOU 5611  CA  LEU B 239    10190  16760  14401   2660   1058   1058       C  
ATOM   5612  C   LEU B 239       3.439  -3.362  32.808  1.00108.93           C  
ANISOU 5612  C   LEU B 239    10159  16559  14669   2701    823    912       C  
ATOM   5613  O   LEU B 239       2.543  -2.750  33.400  1.00113.04           O  
ANISOU 5613  O   LEU B 239    10459  17148  15342   2882   1025    954       O  
ATOM   5614  CB  LEU B 239       5.375  -3.581  34.364  1.00110.21           C  
ANISOU 5614  CB  LEU B 239    10672  17215  13990   2767   1244    872       C  
ATOM   5615  CG  LEU B 239       5.715  -4.134  35.751  1.00115.53           C  
ANISOU 5615  CG  LEU B 239    11274  18202  14420   2881   1637   1054       C  
ATOM   5616  CD1 LEU B 239       6.277  -5.545  35.672  1.00107.51           C  
ANISOU 5616  CD1 LEU B 239    10238  17180  13429   2751   1614   1246       C  
ATOM   5617  CD2 LEU B 239       6.692  -3.210  36.463  1.00110.38           C  
ANISOU 5617  CD2 LEU B 239    10925  17819  13197   2985   1771    831       C  
ATOM   5618  N   LYS B 240       3.676  -3.192  31.507  1.00115.86           N  
ANISOU 5618  N   LYS B 240    11255  17172  15596   2554    414    746       N  
ATOM   5619  CA  LYS B 240       2.848  -2.309  30.696  1.00117.46           C  
ANISOU 5619  CA  LYS B 240    11439  17150  16042   2605    152    619       C  
ATOM   5620  C   LYS B 240       1.738  -3.050  29.967  1.00121.90           C  
ANISOU 5620  C   LYS B 240    11663  17466  17188   2507    -96    794       C  
ATOM   5621  O   LYS B 240       0.743  -2.428  29.578  1.00124.06           O  
ANISOU 5621  O   LYS B 240    11765  17604  17767   2603   -249    765       O  
ATOM   5622  CB  LYS B 240       3.706  -1.575  29.662  1.00117.52           C  
ANISOU 5622  CB  LYS B 240    11928  16983  15743   2516   -160    318       C  
ATOM   5623  CG  LYS B 240       4.523  -0.430  30.220  1.00126.32           C  
ANISOU 5623  CG  LYS B 240    13361  18287  16346   2633     33     77       C  
ATOM   5624  CD  LYS B 240       5.595   0.007  29.230  1.00123.41           C  
ANISOU 5624  CD  LYS B 240    13481  17751  15660   2487   -228   -202       C  
ATOM   5625  CE  LYS B 240       5.005   0.369  27.872  1.00121.50           C  
ANISOU 5625  CE  LYS B 240    13363  17133  15670   2435   -634   -299       C  
ATOM   5626  NZ  LYS B 240       4.796  -0.825  27.000  1.00112.71           N  
ANISOU 5626  NZ  LYS B 240    12152  15788  14883   2238   -920   -145       N  
ATOM   5627  N   THR B 241       1.891  -4.363  29.796  1.00129.55           N  
ANISOU 5627  N   THR B 241    12529  18376  18317   2321   -134    974       N  
ATOM   5628  CA  THR B 241       0.954  -5.175  29.034  1.00130.51           C  
ANISOU 5628  CA  THR B 241    12364  18248  18974   2175   -395   1124       C  
ATOM   5629  C   THR B 241      -0.293  -5.513  29.836  1.00133.81           C  
ANISOU 5629  C   THR B 241    12237  18760  19843   2275   -130   1365       C  
ATOM   5630  O   THR B 241      -1.353  -5.749  29.246  1.00136.28           O  
ANISOU 5630  O   THR B 241    12240  18882  20659   2215   -358   1441       O  
ATOM   5631  CB  THR B 241       1.626  -6.465  28.564  1.00128.52           C  
ANISOU 5631  CB  THR B 241    12244  17882  18707   1928   -503   1221       C  
ATOM   5632  N   ASN B 242      -0.188  -5.556  31.164  1.00138.70           N  
ANISOU 5632  N   ASN B 242    12736  19663  20298   2422    346   1484       N  
ATOM   5633  CA  ASN B 242      -1.248  -6.118  31.983  1.00148.01           C  
ANISOU 5633  CA  ASN B 242    13425  20920  21892   2484    667   1743       C  
ATOM   5634  C   ASN B 242      -1.286  -5.425  33.335  1.00142.14           C  
ANISOU 5634  C   ASN B 242    12638  20464  20907   2742   1145   1765       C  
ATOM   5635  O   ASN B 242      -0.312  -4.809  33.775  1.00139.31           O  
ANISOU 5635  O   ASN B 242    12638  20281  20012   2834   1262   1617       O  
ATOM   5636  CB  ASN B 242      -1.006  -7.630  32.154  1.00150.92           C  
ANISOU 5636  CB  ASN B 242    13708  21270  22364   2294    784   1971       C  
ATOM   5637  CG  ASN B 242      -1.602  -8.192  33.431  1.00144.59           C  
ANISOU 5637  CG  ASN B 242    12559  20644  21735   2394   1296   2231       C  
ATOM   5638  OD1 ASN B 242      -1.055  -8.017  34.521  1.00144.85           O  
ANISOU 5638  OD1 ASN B 242    12728  20929  21380   2550   1674   2265       O  
ATOM   5639  ND2 ASN B 242      -2.721  -8.891  33.297  1.00145.49           N  
ANISOU 5639  ND2 ASN B 242    12234  20615  22430   2296   1312   2414       N  
ATOM   5640  N   SER B 243      -2.452  -5.533  33.987  1.00148.26           N  
ANISOU 5640  N   SER B 243    12962  21274  22098   2849   1428   1948       N  
ATOM   5641  CA  SER B 243      -2.638  -4.954  35.312  1.00149.96           C  
ANISOU 5641  CA  SER B 243    13113  21733  22133   3095   1927   2000       C  
ATOM   5642  C   SER B 243      -3.663  -5.735  36.132  1.00153.94           C  
ANISOU 5642  C   SER B 243    13144  22267  23081   3125   2327   2289       C  
ATOM   5643  O   SER B 243      -4.159  -5.205  37.134  1.00163.82           O  
ANISOU 5643  O   SER B 243    14256  23661  24326   3340   2742   2347       O  
ATOM   5644  CB  SER B 243      -3.084  -3.488  35.201  1.00150.72           C  
ANISOU 5644  CB  SER B 243    13234  21821  22210   3303   1871   1806       C  
ATOM   5645  OG  SER B 243      -4.389  -3.391  34.654  1.00153.86           O  
ANISOU 5645  OG  SER B 243    13198  22035  23227   3322   1707   1866       O  
ATOM   5646  N   TYR B 244      -3.998  -6.963  35.740  1.00163.92           N  
ANISOU 5646  N   TYR B 244    14171  23385  24726   2911   2238   2467       N  
ATOM   5647  CA  TYR B 244      -5.061  -7.699  36.411  1.00161.18           C  
ANISOU 5647  CA  TYR B 244    13348  23027  24867   2911   2609   2730       C  
ATOM   5648  C   TYR B 244      -4.759  -7.881  37.893  1.00149.75           C  
ANISOU 5648  C   TYR B 244    11990  21820  23090   3073   3209   2880       C  
ATOM   5649  O   TYR B 244      -3.601  -7.937  38.317  1.00148.43           O  
ANISOU 5649  O   TYR B 244    12239  21813  22343   3105   3287   2836       O  
ATOM   5650  CB  TYR B 244      -5.257  -9.066  35.751  1.00149.32           C  
ANISOU 5650  CB  TYR B 244    11668  21327  23741   2619   2420   2880       C  
ATOM   5651  N   GLY B 245      -5.830  -7.980  38.686  1.00155.31           N  
ANISOU 5651  N   GLY B 245    12294  22542  24176   3180   3636   3060       N  
ATOM   5652  CA  GLY B 245      -5.667  -8.224  40.110  1.00145.83           C  
ANISOU 5652  CA  GLY B 245    11178  21536  22696   3334   4236   3227       C  
ATOM   5653  C   GLY B 245      -5.286  -9.658  40.418  1.00156.29           C  
ANISOU 5653  C   GLY B 245    12551  22845  23989   3174   4412   3450       C  
ATOM   5654  O   GLY B 245      -4.498  -9.918  41.329  1.00141.70           O  
ANISOU 5654  O   GLY B 245    11020  21176  21644   3271   4715   3524       O  
ATOM   5655  N   LYS B 246      -5.848 -10.611  39.671  1.00143.73           N  
ANISOU 5655  N   LYS B 246    10656  21033  22920   2931   4223   3559       N  
ATOM   5656  CA  LYS B 246      -5.503 -12.014  39.870  1.00153.29           C  
ANISOU 5656  CA  LYS B 246    11928  22193  24122   2764   4379   3770       C  
ATOM   5657  C   LYS B 246      -4.203 -12.376  39.161  1.00148.84           C  
ANISOU 5657  C   LYS B 246    11803  21622  23127   2632   3980   3663       C  
ATOM   5658  O   LYS B 246      -3.318 -13.008  39.750  1.00148.74           O  
ANISOU 5658  O   LYS B 246    12097  21724  22694   2659   4180   3767       O  
ATOM   5659  CB  LYS B 246      -6.643 -12.907  39.377  1.00154.51           C  
ANISOU 5659  CB  LYS B 246    11586  22102  25020   2536   4363   3925       C  
ATOM   5660  N   ASN B 247      -4.076 -11.991  37.889  1.00151.36           N  
ANISOU 5660  N   ASN B 247    12164  21800  23548   2498   3419   3459       N  
ATOM   5661  CA  ASN B 247      -2.865 -12.286  37.132  1.00147.94           C  
ANISOU 5661  CA  ASN B 247    12144  21330  22735   2366   3044   3342       C  
ATOM   5662  C   ASN B 247      -1.616 -11.661  37.739  1.00145.55           C  
ANISOU 5662  C   ASN B 247    12297  21288  21718   2553   3131   3217       C  
ATOM   5663  O   ASN B 247      -0.510 -12.134  37.458  1.00144.55           O  
ANISOU 5663  O   ASN B 247    12507  21181  21236   2472   2973   3185       O  
ATOM   5664  CB  ASN B 247      -3.019 -11.812  35.686  1.00148.70           C  
ANISOU 5664  CB  ASN B 247    12232  21217  23051   2216   2448   3126       C  
ATOM   5665  CG  ASN B 247      -4.145 -12.518  34.958  1.00149.59           C  
ANISOU 5665  CG  ASN B 247    11921  21064  23851   1994   2273   3231       C  
ATOM   5666  OD1 ASN B 247      -4.587 -13.592  35.366  1.00150.99           O  
ANISOU 5666  OD1 ASN B 247    11875  21183  24312   1885   2555   3462       O  
ATOM   5667  ND2 ASN B 247      -4.613 -11.918  33.869  1.00156.58           N  
ANISOU 5667  ND2 ASN B 247    12706  21783  25005   1923   1800   3056       N  
ATOM   5668  N   ARG B 248      -1.753 -10.612  38.555  1.00134.01           N  
ANISOU 5668  N   ARG B 248    10854  20022  20041   2796   3377   3141       N  
ATOM   5669  CA  ARG B 248      -0.572 -10.034  39.193  1.00135.41           C  
ANISOU 5669  CA  ARG B 248    11457  20457  19534   2958   3464   3016       C  
ATOM   5670  C   ARG B 248       0.183 -11.075  40.011  1.00132.86           C  
ANISOU 5670  C   ARG B 248    11325  20268  18887   2977   3751   3215       C  
ATOM   5671  O   ARG B 248       1.420 -11.088  40.014  1.00126.92           O  
ANISOU 5671  O   ARG B 248    10937  19649  17637   2989   3620   3117       O  
ATOM   5672  CB  ARG B 248      -0.955  -8.813  40.036  1.00131.41           C  
ANISOU 5672  CB  ARG B 248    10935  20123  18872   3210   3739   2925       C  
ATOM   5673  CG  ARG B 248       0.264  -8.094  40.616  1.00138.88           C  
ANISOU 5673  CG  ARG B 248    12329  21330  19108   3354   3776   2751       C  
ATOM   5674  CD  ARG B 248      -0.089  -7.042  41.670  1.00121.02           C  
ANISOU 5674  CD  ARG B 248    10092  19248  16641   3607   4142   2701       C  
ATOM   5675  NE  ARG B 248      -0.885  -7.561  42.778  1.00132.00           N  
ANISOU 5675  NE  ARG B 248    11261  20684  18211   3725   4671   2971       N  
ATOM   5676  CZ  ARG B 248      -2.179  -7.288  42.953  1.00142.10           C  
ANISOU 5676  CZ  ARG B 248    12164  21854  19974   3796   4901   3059       C  
ATOM   5677  NH1 ARG B 248      -2.817  -6.470  42.121  1.00149.19           N  
ANISOU 5677  NH1 ARG B 248    12869  22612  21205   3784   4629   2900       N  
ATOM   5678  NH2 ARG B 248      -2.835  -7.806  43.981  1.00151.04           N  
ANISOU 5678  NH2 ARG B 248    13179  22978  21232   3857   5367   3275       N  
ATOM   5679  N   ILE B 249      -0.533 -11.955  40.713  1.00136.08           N  
ANISOU 5679  N   ILE B 249    11494  20639  19571   2986   4150   3494       N  
ATOM   5680  CA  ILE B 249       0.143 -13.041  41.419  1.00130.19           C  
ANISOU 5680  CA  ILE B 249    10944  19983  18540   3005   4412   3706       C  
ATOM   5681  C   ILE B 249       0.883 -13.920  40.417  1.00124.80           C  
ANISOU 5681  C   ILE B 249    10411  19150  17858   2785   4045   3700       C  
ATOM   5682  O   ILE B 249       2.044 -14.292  40.622  1.00121.11           O  
ANISOU 5682  O   ILE B 249    10275  18812  16930   2824   4013   3704       O  
ATOM   5683  CB  ILE B 249      -0.865 -13.855  42.250  1.00130.19           C  
ANISOU 5683  CB  ILE B 249    10659  19914  18895   3030   4919   4008       C  
ATOM   5684  N   THR B 250       0.213 -14.260  39.312  1.00136.44           N  
ANISOU 5684  N   THR B 250    11642  20344  19854   2552   3757   3688       N  
ATOM   5685  CA  THR B 250       0.845 -15.047  38.258  1.00135.89           C  
ANISOU 5685  CA  THR B 250    11730  20091  19810   2326   3395   3667       C  
ATOM   5686  C   THR B 250       1.908 -14.238  37.523  1.00134.50           C  
ANISOU 5686  C   THR B 250    11887  19973  19245   2324   2975   3375       C  
ATOM   5687  O   THR B 250       2.887 -14.809  37.030  1.00126.62           O  
ANISOU 5687  O   THR B 250    11156  18930  18023   2226   2785   3354       O  
ATOM   5688  CB  THR B 250      -0.211 -15.555  37.275  1.00141.28           C  
ANISOU 5688  CB  THR B 250    12076  20454  21151   2072   3184   3713       C  
ATOM   5689  OG1 THR B 250      -1.224 -16.276  37.990  1.00144.17           O  
ANISOU 5689  OG1 THR B 250    12107  20765  21906   2061   3607   3973       O  
ATOM   5690  CG2 THR B 250       0.418 -16.471  36.232  1.00142.71           C  
ANISOU 5690  CG2 THR B 250    12453  20419  21350   1829   2854   3712       C  
ATOM   5691  N   ARG B 251       1.732 -12.916  37.435  1.00135.61           N  
ANISOU 5691  N   ARG B 251    12022  20196  19308   2431   2848   3149       N  
ATOM   5692  CA  ARG B 251       2.713 -12.082  36.747  1.00136.29           C  
ANISOU 5692  CA  ARG B 251    12434  20321  19029   2421   2481   2858       C  
ATOM   5693  C   ARG B 251       3.987 -11.953  37.571  1.00133.21           C  
ANISOU 5693  C   ARG B 251    12380  20225  18011   2577   2639   2816       C  
ATOM   5694  O   ARG B 251       5.092 -11.919  37.018  1.00134.43           O  
ANISOU 5694  O   ARG B 251    12827  20390  17860   2511   2382   2663       O  
ATOM   5695  CB  ARG B 251       2.115 -10.702  36.468  1.00135.62           C  
ANISOU 5695  CB  ARG B 251    12262  20228  19039   2502   2335   2637       C  
ATOM   5696  CG  ARG B 251       3.048  -9.735  35.752  1.00137.01           C  
ANISOU 5696  CG  ARG B 251    12787  20420  18852   2490   1985   2320       C  
ATOM   5697  CD  ARG B 251       2.464  -8.329  35.711  1.00137.73           C  
ANISOU 5697  CD  ARG B 251    12823  20531  18978   2621   1932   2123       C  
ATOM   5698  NE  ARG B 251       2.567  -7.650  37.001  1.00142.46           N  
ANISOU 5698  NE  ARG B 251    13466  21421  19242   2859   2317   2118       N  
ATOM   5699  CZ  ARG B 251       2.092  -6.433  37.248  1.00140.60           C  
ANISOU 5699  CZ  ARG B 251    13203  21243  18975   3015   2384   1973       C  
ATOM   5700  NH1 ARG B 251       1.471  -5.749  36.296  1.00140.31           N  
ANISOU 5700  NH1 ARG B 251    13082  20999  19229   2976   2084   1829       N  
ATOM   5701  NH2 ARG B 251       2.236  -5.898  38.453  1.00142.10           N  
ANISOU 5701  NH2 ARG B 251    13472  21689  18832   3220   2752   1975       N  
ATOM   5702  N   ASP B 252       3.852 -11.881  38.897  1.00120.08           N  
ANISOU 5702  N   ASP B 252    10679  18796  16149   2785   3062   2947       N  
ATOM   5703  CA  ASP B 252       5.027 -11.870  39.758  1.00112.93           C  
ANISOU 5703  CA  ASP B 252    10078  18181  14651   2939   3207   2933       C  
ATOM   5704  C   ASP B 252       5.753 -13.207  39.706  1.00110.72           C  
ANISOU 5704  C   ASP B 252     9919  17868  14283   2865   3216   3120       C  
ATOM   5705  O   ASP B 252       6.982 -13.251  39.824  1.00108.79           O  
ANISOU 5705  O   ASP B 252     9952  17789  13594   2914   3122   3038       O  
ATOM   5706  CB  ASP B 252       4.626 -11.531  41.193  1.00115.30           C  
ANISOU 5706  CB  ASP B 252    10333  18712  14764   3179   3663   3046       C  
ATOM   5707  CG  ASP B 252       4.197 -10.084  41.351  1.00120.20           C  
ANISOU 5707  CG  ASP B 252    10929  19412  15330   3290   3669   2826       C  
ATOM   5708  OD1 ASP B 252       4.323  -9.316  40.375  1.00120.80           O  
ANISOU 5708  OD1 ASP B 252    11056  19384  15459   3193   3309   2575       O  
ATOM   5709  OD2 ASP B 252       3.729  -9.716  42.450  1.00130.22           O  
ANISOU 5709  OD2 ASP B 252    12154  20830  16493   3479   4049   2906       O  
ATOM   5710  N   GLN B 253       5.009 -14.304  39.536  1.00112.21           N  
ANISOU 5710  N   GLN B 253     9895  17841  14898   2748   3336   3370       N  
ATOM   5711  CA  GLN B 253       5.634 -15.617  39.437  1.00111.71           C  
ANISOU 5711  CA  GLN B 253     9958  17707  14781   2675   3362   3561       C  
ATOM   5712  C   GLN B 253       6.569 -15.703  38.238  1.00112.02           C  
ANISOU 5712  C   GLN B 253    10208  17619  14734   2508   2929   3381       C  
ATOM   5713  O   GLN B 253       7.583 -16.407  38.291  1.00110.03           O  
ANISOU 5713  O   GLN B 253    10174  17424  14206   2526   2919   3448       O  
ATOM   5714  CB  GLN B 253       4.555 -16.695  39.333  1.00118.27           C  
ANISOU 5714  CB  GLN B 253    10515  18280  16141   2537   3552   3829       C  
ATOM   5715  CG  GLN B 253       3.899 -17.065  40.652  1.00118.98           C  
ANISOU 5715  CG  GLN B 253    10472  18481  16253   2705   4078   4086       C  
ATOM   5716  CD  GLN B 253       3.013 -18.291  40.533  1.00120.31           C  
ANISOU 5716  CD  GLN B 253    10411  18384  16917   2542   4285   4356       C  
ATOM   5717  OE1 GLN B 253       2.062 -18.309  39.751  1.00115.28           O  
ANISOU 5717  OE1 GLN B 253     9485  17506  16809   2341   4136   4328       O  
ATOM   5718  NE2 GLN B 253       3.324 -19.324  41.307  1.00124.32           N  
ANISOU 5718  NE2 GLN B 253    11053  18929  17253   2628   4624   4616       N  
ATOM   5719  N   VAL B 254       6.244 -15.003  37.149  1.00115.77           N  
ANISOU 5719  N   VAL B 254    10634  17913  15440   2354   2580   3159       N  
ATOM   5720  CA  VAL B 254       7.147 -14.958  36.004  1.00112.27           C  
ANISOU 5720  CA  VAL B 254    10434  17337  14886   2202   2187   2963       C  
ATOM   5721  C   VAL B 254       8.361 -14.094  36.319  1.00117.85           C  
ANISOU 5721  C   VAL B 254    11414  18319  15046   2340   2118   2734       C  
ATOM   5722  O   VAL B 254       9.502 -14.467  36.022  1.00115.11           O  
ANISOU 5722  O   VAL B 254    11299  18000  14436   2310   1997   2683       O  
ATOM   5723  CB  VAL B 254       6.399 -14.449  34.758  1.00123.44           C  
ANISOU 5723  CB  VAL B 254    11748  18459  16694   2007   1834   2795       C  
ATOM   5724  CG1 VAL B 254       7.352 -14.312  33.579  1.00120.59           C  
ANISOU 5724  CG1 VAL B 254    11691  17946  16183   1857   1450   2576       C  
ATOM   5725  CG2 VAL B 254       5.245 -15.381  34.414  1.00122.42           C  
ANISOU 5725  CG2 VAL B 254    11333  18060  17121   1843   1870   3013       C  
ATOM   5726  N   LEU B 255       8.136 -12.925  36.924  1.00118.16           N  
ANISOU 5726  N   LEU B 255    11422  18559  14913   2490   2203   2587       N  
ATOM   5727  CA  LEU B 255       9.249 -12.067  37.315  1.00112.20           C  
ANISOU 5727  CA  LEU B 255    10915  18080  13635   2611   2160   2359       C  
ATOM   5728  C   LEU B 255      10.162 -12.773  38.308  1.00104.41           C  
ANISOU 5728  C   LEU B 255    10049  17358  12264   2763   2378   2515       C  
ATOM   5729  O   LEU B 255      11.388 -12.626  38.249  1.00113.12           O  
ANISOU 5729  O   LEU B 255    11371  18611  12999   2783   2244   2366       O  
ATOM   5730  CB  LEU B 255       8.715 -10.763  37.906  1.00116.20           C  
ANISOU 5730  CB  LEU B 255    11367  18743  14042   2750   2270   2206       C  
ATOM   5731  CG  LEU B 255       8.117  -9.786  36.892  1.00116.65           C  
ANISOU 5731  CG  LEU B 255    11389  18582  14350   2640   1997   1976       C  
ATOM   5732  CD1 LEU B 255       7.330  -8.693  37.599  1.00119.22           C  
ANISOU 5732  CD1 LEU B 255    11602  19032  14663   2804   2190   1907       C  
ATOM   5733  CD2 LEU B 255       9.203  -9.184  36.017  1.00111.01           C  
ANISOU 5733  CD2 LEU B 255    10973  17832  13374   2534   1672   1671       C  
ATOM   5734  N   LYS B 256       9.581 -13.538  39.236  1.00104.02           N  
ANISOU 5734  N   LYS B 256     9861  17366  12296   2877   2718   2813       N  
ATOM   5735  CA  LYS B 256      10.394 -14.310  40.169  1.00101.72           C  
ANISOU 5735  CA  LYS B 256     9702  17301  11646   3040   2922   2995       C  
ATOM   5736  C   LYS B 256      11.350 -15.230  39.422  1.00100.54           C  
ANISOU 5736  C   LYS B 256     9694  17037  11468   2930   2722   3029       C  
ATOM   5737  O   LYS B 256      12.522 -15.359  39.796  1.00101.45           O  
ANISOU 5737  O   LYS B 256     9992  17375  11179   3043   2691   2993       O  
ATOM   5738  CB  LYS B 256       9.487 -15.122  41.096  1.00106.07           C  
ANISOU 5738  CB  LYS B 256    10095  17838  12368   3146   3328   3334       C  
ATOM   5739  CG  LYS B 256      10.199 -16.190  41.926  1.00105.48           C  
ANISOU 5739  CG  LYS B 256    10168  17913  11996   3303   3542   3583       C  
ATOM   5740  CD  LYS B 256       9.200 -17.086  42.654  1.00109.82           C  
ANISOU 5740  CD  LYS B 256    10574  18363  12789   3363   3953   3926       C  
ATOM   5741  CE  LYS B 256       8.563 -18.106  41.716  1.00114.08           C  
ANISOU 5741  CE  LYS B 256    10958  18529  13859   3126   3909   4083       C  
ATOM   5742  NZ  LYS B 256       9.506 -19.201  41.342  1.00111.25           N  
ANISOU 5742  NZ  LYS B 256    10785  18099  13385   3092   3814   4200       N  
ATOM   5743  N   MET B 257      10.867 -15.877  38.363  1.00 92.94           N  
ANISOU 5743  N   MET B 257     8651  15727  10935   2712   2582   3095       N  
ATOM   5744  CA  MET B 257      11.703 -16.788  37.593  1.00 92.80           C  
ANISOU 5744  CA  MET B 257     8784  15554  10920   2598   2416   3137       C  
ATOM   5745  C   MET B 257      12.660 -16.040  36.675  1.00 95.56           C  
ANISOU 5745  C   MET B 257     9321  15891  11097   2497   2068   2810       C  
ATOM   5746  O   MET B 257      13.777 -16.513  36.436  1.00102.69           O  
ANISOU 5746  O   MET B 257    10396  16828  11793   2501   1980   2793       O  
ATOM   5747  CB  MET B 257      10.812 -17.738  36.791  1.00 96.55           C  
ANISOU 5747  CB  MET B 257     9132  15644  11907   2383   2398   3316       C  
ATOM   5748  CG  MET B 257       9.892 -18.581  37.671  1.00115.56           C  
ANISOU 5748  CG  MET B 257    11358  18036  14513   2458   2778   3646       C  
ATOM   5749  SD  MET B 257       8.422 -19.196  36.826  1.00133.84           S  
ANISOU 5749  SD  MET B 257    13409  19930  17514   2183   2752   3775       S  
ATOM   5750  CE  MET B 257       9.151 -20.356  35.675  1.00136.68           C  
ANISOU 5750  CE  MET B 257    13985  19986  17963   1971   2536   3827       C  
ATOM   5751  N   ALA B 258      12.252 -14.878  36.160  1.00104.79           N  
ANISOU 5751  N   ALA B 258    10465  17002  12349   2414   1883   2550       N  
ATOM   5752  CA  ALA B 258      13.159 -14.074  35.350  1.00105.63           C  
ANISOU 5752  CA  ALA B 258    10776  17093  12265   2323   1591   2224       C  
ATOM   5753  C   ALA B 258      14.200 -13.371  36.211  1.00103.48           C  
ANISOU 5753  C   ALA B 258    10621  17210  11487   2501   1649   2064       C  
ATOM   5754  O   ALA B 258      15.332 -13.158  35.762  1.00105.91           O  
ANISOU 5754  O   ALA B 258    11107  17562  11571   2454   1478   1868       O  
ATOM   5755  CB  ALA B 258      12.370 -13.050  34.535  1.00107.50           C  
ANISOU 5755  CB  ALA B 258    10979  17128  12738   2193   1384   2004       C  
ATOM   5756  N   ALA B 259      13.839 -12.999  37.438  1.00105.37           N  
ANISOU 5756  N   ALA B 259    10768  17725  11544   2698   1891   2136       N  
ATOM   5757  CA  ALA B 259      14.778 -12.361  38.350  1.00107.36           C  
ANISOU 5757  CA  ALA B 259    11135  18359  11299   2868   1944   1993       C  
ATOM   5758  C   ALA B 259      15.744 -13.349  38.990  1.00116.11           C  
ANISOU 5758  C   ALA B 259    12307  19669  12139   3007   2038   2176       C  
ATOM   5759  O   ALA B 259      16.730 -12.919  39.596  1.00113.87           O  
ANISOU 5759  O   ALA B 259    12127  19699  11439   3127   2012   2037       O  
ATOM   5760  CB  ALA B 259      14.016 -11.612  39.446  1.00114.46           C  
ANISOU 5760  CB  ALA B 259    11949  19461  12079   3032   2180   2008       C  
ATOM   5761  N   ALA B 260      15.490 -14.653  38.870  1.00105.23           N  
ANISOU 5761  N   ALA B 260    10875  18117  10991   2996   2141   2480       N  
ATOM   5762  CA  ALA B 260      16.370 -15.641  39.482  1.00101.49           C  
ANISOU 5762  CA  ALA B 260    10475  17817  10269   3156   2242   2680       C  
ATOM   5763  C   ALA B 260      17.611 -15.894  38.635  1.00107.13           C  
ANISOU 5763  C   ALA B 260    11319  18484  10903   3066   1999   2539       C  
ATOM   5764  O   ALA B 260      18.722 -15.983  39.171  1.00104.54           O  
ANISOU 5764  O   ALA B 260    11066  18437  10218   3216   1978   2508       O  
ATOM   5765  CB  ALA B 260      15.608 -16.947  39.710  1.00100.36           C  
ANISOU 5765  CB  ALA B 260    10249  17488  10396   3184   2484   3065       C  
ATOM   5766  N   VAL B 261      17.446 -16.013  37.316  1.00111.42           N  
ANISOU 5766  N   VAL B 261    11891  18669  11774   2824   1816   2452       N  
ATOM   5767  CA  VAL B 261      18.592 -16.275  36.449  1.00112.09           C  
ANISOU 5767  CA  VAL B 261    12116  18663  11808   2728   1619   2321       C  
ATOM   5768  C   VAL B 261      19.611 -15.148  36.558  1.00111.83           C  
ANISOU 5768  C   VAL B 261    12160  18902  11429   2755   1468   1975       C  
ATOM   5769  O   VAL B 261      20.825 -15.387  36.576  1.00111.96           O  
ANISOU 5769  O   VAL B 261    12243  19069  11229   2815   1402   1914       O  
ATOM   5770  CB  VAL B 261      18.127 -16.480  34.993  1.00112.88           C  
ANISOU 5770  CB  VAL B 261    12274  18305  12309   2452   1449   2266       C  
ATOM   5771  CG1 VAL B 261      17.239 -17.714  34.887  1.00114.70           C  
ANISOU 5771  CG1 VAL B 261    12431  18271  12878   2406   1595   2607       C  
ATOM   5772  CG2 VAL B 261      17.401 -15.244  34.475  1.00112.85           C  
ANISOU 5772  CG2 VAL B 261    12257  18190  12432   2312   1302   2006       C  
ATOM   5773  N   VAL B 262      19.137 -13.903  36.639  1.00101.52           N  
ANISOU 5773  N   VAL B 262    10840  17659  10074   2712   1420   1741       N  
ATOM   5774  CA  VAL B 262      20.053 -12.771  36.724  1.00 96.88           C  
ANISOU 5774  CA  VAL B 262    10339  17306   9165   2708   1290   1391       C  
ATOM   5775  C   VAL B 262      20.724 -12.729  38.091  1.00 94.52           C  
ANISOU 5775  C   VAL B 262    10005  17463   8444   2953   1402   1433       C  
ATOM   5776  O   VAL B 262      21.901 -12.367  38.209  1.00 96.35           O  
ANISOU 5776  O   VAL B 262    10290  17925   8394   2977   1290   1226       O  
ATOM   5777  CB  VAL B 262      19.312 -11.457  36.412  1.00 97.34           C  
ANISOU 5777  CB  VAL B 262    10423  17275   9289   2598   1224   1137       C  
ATOM   5778  CG1 VAL B 262      18.225 -11.187  37.443  1.00 99.25           C  
ANISOU 5778  CG1 VAL B 262    10538  17655   9518   2747   1433   1286       C  
ATOM   5779  CG2 VAL B 262      20.294 -10.296  36.350  1.00 93.35           C  
ANISOU 5779  CG2 VAL B 262    10041  16957   8473   2552   1094    752       C  
ATOM   5780  N   LEU B 263      19.993 -13.094  39.146  1.00 99.47           N  
ANISOU 5780  N   LEU B 263    10549  18227   9020   3135   1624   1695       N  
ATOM   5781  CA  LEU B 263      20.576 -13.082  40.483  1.00 93.06           C  
ANISOU 5781  CA  LEU B 263     9743  17837   7780   3383   1727   1751       C  
ATOM   5782  C   LEU B 263      21.525 -14.257  40.683  1.00 95.99           C  
ANISOU 5782  C   LEU B 263    10122  18310   8038   3518   1722   1954       C  
ATOM   5783  O   LEU B 263      22.607 -14.094  41.258  1.00100.40           O  
ANISOU 5783  O   LEU B 263    10708  19201   8239   3648   1638   1849       O  
ATOM   5784  CB  LEU B 263      19.470 -13.100  41.539  1.00 97.34           C  
ANISOU 5784  CB  LEU B 263    10230  18459   8295   3540   1997   1972       C  
ATOM   5785  CG  LEU B 263      19.107 -11.748  42.161  1.00105.13           C  
ANISOU 5785  CG  LEU B 263    11246  19635   9062   3572   2041   1743       C  
ATOM   5786  CD1 LEU B 263      18.696 -10.738  41.097  1.00 91.89           C  
ANISOU 5786  CD1 LEU B 263     9576  17714   7623   3338   1888   1453       C  
ATOM   5787  CD2 LEU B 263      18.001 -11.916  43.197  1.00 96.29           C  
ANISOU 5787  CD2 LEU B 263    10077  18561   7946   3739   2355   1999       C  
ATOM   5788  N   ALA B 264      21.143 -15.446  40.212  1.00102.19           N  
ANISOU 5788  N   ALA B 264    10887  18812   9128   3490   1806   2241       N  
ATOM   5789  CA  ALA B 264      22.026 -16.599  40.344  1.00102.75           C  
ANISOU 5789  CA  ALA B 264    10984  18945   9109   3629   1817   2448       C  
ATOM   5790  C   ALA B 264      23.324 -16.397  39.575  1.00104.29           C  
ANISOU 5790  C   ALA B 264    11217  19170   9240   3536   1578   2194       C  
ATOM   5791  O   ALA B 264      24.349 -16.998  39.916  1.00100.76           O  
ANISOU 5791  O   ALA B 264    10772  18918   8595   3701   1548   2273       O  
ATOM   5792  CB  ALA B 264      21.317 -17.863  39.859  1.00101.35           C  
ANISOU 5792  CB  ALA B 264    10803  18404   9300   3576   1963   2780       C  
ATOM   5793  N   PHE B 265      23.302 -15.556  38.540  1.00 99.75           N  
ANISOU 5793  N   PHE B 265    10675  18395   8830   3283   1416   1889       N  
ATOM   5794  CA  PHE B 265      24.507 -15.298  37.762  1.00 93.13           C  
ANISOU 5794  CA  PHE B 265     9883  17552   7950   3171   1222   1625       C  
ATOM   5795  C   PHE B 265      25.460 -14.370  38.506  1.00 93.19           C  
ANISOU 5795  C   PHE B 265     9858  17994   7556   3267   1122   1354       C  
ATOM   5796  O   PHE B 265      26.674 -14.602  38.514  1.00 96.83           O  
ANISOU 5796  O   PHE B 265    10290  18631   7871   3332   1025   1278       O  
ATOM   5797  CB  PHE B 265      24.131 -14.703  36.405  1.00 94.53           C  
ANISOU 5797  CB  PHE B 265    10151  17343   8422   2869   1100   1392       C  
ATOM   5798  CG  PHE B 265      25.296 -14.526  35.476  1.00 95.04           C  
ANISOU 5798  CG  PHE B 265    10295  17323   8492   2730    945   1138       C  
ATOM   5799  CD1 PHE B 265      25.790 -15.598  34.753  1.00 93.17           C  
ANISOU 5799  CD1 PHE B 265    10110  16851   8439   2698    949   1287       C  
ATOM   5800  CD2 PHE B 265      25.896 -13.287  35.323  1.00 93.21           C  
ANISOU 5800  CD2 PHE B 265    10100  17228   8087   2625    821    747       C  
ATOM   5801  CE1 PHE B 265      26.862 -15.440  33.896  1.00 92.01           C  
ANISOU 5801  CE1 PHE B 265    10040  16609   8312   2573    840   1055       C  
ATOM   5802  CE2 PHE B 265      26.969 -13.122  34.467  1.00 89.37           C  
ANISOU 5802  CE2 PHE B 265     9686  16648   7623   2487    712    507       C  
ATOM   5803  CZ  PHE B 265      27.452 -14.200  33.753  1.00 93.12           C  
ANISOU 5803  CZ  PHE B 265    10202  16890   8291   2464    726    663       C  
ATOM   5804  N   ILE B 266      24.932 -13.319  39.135  1.00 91.34           N  
ANISOU 5804  N   ILE B 266     9624  17933   7148   3275   1145   1201       N  
ATOM   5805  CA  ILE B 266      25.791 -12.375  39.841  1.00 96.79           C  
ANISOU 5805  CA  ILE B 266    10303  19025   7448   3337   1046    919       C  
ATOM   5806  C   ILE B 266      26.274 -12.957  41.164  1.00 97.28           C  
ANISOU 5806  C   ILE B 266    10309  19485   7169   3641   1100   1128       C  
ATOM   5807  O   ILE B 266      27.406 -12.690  41.586  1.00 91.36           O  
ANISOU 5807  O   ILE B 266     9515  19012   6185   3700    946    952       O  
ATOM   5808  CB  ILE B 266      25.049 -11.045  40.062  1.00 92.49           C  
ANISOU 5808  CB  ILE B 266     9814  18509   6820   3244   1069    685       C  
ATOM   5809  CG1 ILE B 266      24.736 -10.380  38.719  1.00 96.29           C  
ANISOU 5809  CG1 ILE B 266    10377  18613   7594   2958    977    442       C  
ATOM   5810  CG2 ILE B 266      25.874 -10.115  40.944  1.00100.69           C  
ANISOU 5810  CG2 ILE B 266    10858  19868   7533   3278    952    413       C  
ATOM   5811  CD1 ILE B 266      23.807  -9.187  38.827  1.00 95.84           C  
ANISOU 5811  CD1 ILE B 266    10383  18509   7523   2883   1024    266       C  
ATOM   5812  N   ILE B 267      25.442 -13.755  41.834  1.00100.55           N  
ANISOU 5812  N   ILE B 267    10725  19871   7608   3819   1298   1495       N  
ATOM   5813  CA  ILE B 267      25.845 -14.341  43.108  1.00105.36           C  
ANISOU 5813  CA  ILE B 267    11326  20774   7930   4107   1340   1705       C  
ATOM   5814  C   ILE B 267      27.005 -15.310  42.910  1.00100.81           C  
ANISOU 5814  C   ILE B 267    10701  20302   7301   4234   1246   1817       C  
ATOM   5815  O   ILE B 267      27.916 -15.387  43.744  1.00 97.68           O  
ANISOU 5815  O   ILE B 267    10263  20164   6686   4401   1116   1783       O  
ATOM   5816  CB  ILE B 267      24.642 -15.029  43.778  1.00 99.77           C  
ANISOU 5816  CB  ILE B 267    10658  19961   7288   4255   1617   2082       C  
ATOM   5817  CG1 ILE B 267      23.586 -13.993  44.169  1.00 88.13           C  
ANISOU 5817  CG1 ILE B 267     9218  18436   5833   4171   1712   1959       C  
ATOM   5818  CG2 ILE B 267      25.085 -15.818  45.000  1.00 91.45           C  
ANISOU 5818  CG2 ILE B 267     9638  19088   6023   4542   1646   2319       C  
ATOM   5819  N   CYS B 268      26.997 -16.059  41.810  1.00 99.14           N  
ANISOU 5819  N   CYS B 268    10486  19757   7428   4114   1264   1924       N  
ATOM   5820  CA  CYS B 268      28.005 -17.088  41.597  1.00 99.07           C  
ANISOU 5820  CA  CYS B 268    10440  19769   7433   4241   1209   2070       C  
ATOM   5821  C   CYS B 268      29.284 -16.550  40.975  1.00 98.07           C  
ANISOU 5821  C   CYS B 268    10238  19752   7273   4125    981   1724       C  
ATOM   5822  O   CYS B 268      30.373 -17.043  41.293  1.00102.68           O  
ANISOU 5822  O   CYS B 268    10741  20574   7698   4310    890   1766       O  
ATOM   5823  CB  CYS B 268      27.437 -18.201  40.709  1.00100.51           C  
ANISOU 5823  CB  CYS B 268    10678  19495   8018   4155   1347   2345       C  
ATOM   5824  SG  CYS B 268      26.101 -19.159  41.467  1.00 87.18           S  
ANISOU 5824  SG  CYS B 268     9056  17672   6398   4316   1652   2807       S  
ATOM   5825  N   TRP B 269      29.189 -15.541  40.109  1.00 95.11           N  
ANISOU 5825  N   TRP B 269     9885  19207   7045   3831    893   1383       N  
ATOM   5826  CA  TRP B 269      30.327 -15.113  39.307  1.00 93.00           C  
ANISOU 5826  CA  TRP B 269     9569  18941   6826   3674    726   1062       C  
ATOM   5827  C   TRP B 269      30.954 -13.804  39.756  1.00 93.00           C  
ANISOU 5827  C   TRP B 269     9512  19290   6534   3613    575    665       C  
ATOM   5828  O   TRP B 269      32.151 -13.609  39.539  1.00 96.16           O  
ANISOU 5828  O   TRP B 269     9812  19850   6874   3582    437    442       O  
ATOM   5829  CB  TRP B 269      29.915 -14.977  37.836  1.00 83.16           C  
ANISOU 5829  CB  TRP B 269     8434  17196   5965   3365    738    944       C  
ATOM   5830  CG  TRP B 269      29.723 -16.295  37.163  1.00 85.06           C  
ANISOU 5830  CG  TRP B 269     8730  17087   6502   3381    841   1260       C  
ATOM   5831  CD1 TRP B 269      28.551 -16.820  36.705  1.00 91.44           C  
ANISOU 5831  CD1 TRP B 269     9640  17520   7583   3294    963   1486       C  
ATOM   5832  CD2 TRP B 269      30.735 -17.271  36.886  1.00 91.93           C  
ANISOU 5832  CD2 TRP B 269     9557  17944   7428   3493    838   1385       C  
ATOM   5833  NE1 TRP B 269      28.771 -18.058  36.151  1.00 91.72           N  
ANISOU 5833  NE1 TRP B 269     9723  17300   7827   3327   1037   1736       N  
ATOM   5834  CE2 TRP B 269      30.104 -18.359  36.251  1.00 91.89           C  
ANISOU 5834  CE2 TRP B 269     9665  17532   7718   3459    973   1687       C  
ATOM   5835  CE3 TRP B 269      32.114 -17.328  37.111  1.00 91.68           C  
ANISOU 5835  CE3 TRP B 269     9392  18206   7238   3619    734   1268       C  
ATOM   5836  CZ2 TRP B 269      30.804 -19.490  35.838  1.00 92.59           C  
ANISOU 5836  CZ2 TRP B 269     9768  17482   7929   3554   1028   1879       C  
ATOM   5837  CZ3 TRP B 269      32.807 -18.452  36.700  1.00 96.59           C  
ANISOU 5837  CZ3 TRP B 269     9998  18701   8001   3728    783   1464       C  
ATOM   5838  CH2 TRP B 269      32.152 -19.518  36.071  1.00 94.58           C  
ANISOU 5838  CH2 TRP B 269     9889  18023   8023   3698    939   1769       C  
ATOM   5839  N   LEU B 270      30.191 -12.905  40.374  1.00 93.84           N  
ANISOU 5839  N   LEU B 270     9676  19511   6467   3590    608    564       N  
ATOM   5840  CA  LEU B 270      30.784 -11.653  40.832  1.00 91.47           C  
ANISOU 5840  CA  LEU B 270     9336  19357   6059   3465    444    181       C  
ATOM   5841  C   LEU B 270      31.937 -11.877  41.801  1.00 94.05           C  
ANISOU 5841  C   LEU B 270     9512  20056   6168   3659    304    168       C  
ATOM   5842  O   LEU B 270      32.925 -11.127  41.724  1.00101.61           O  
ANISOU 5842  O   LEU B 270    10380  21140   7089   3527    148   -170       O  
ATOM   5843  CB  LEU B 270      29.710 -10.763  41.469  1.00 95.78           C  
ANISOU 5843  CB  LEU B 270     9982  19825   6583   3409    510    133       C  
ATOM   5844  CG  LEU B 270      30.183  -9.365  41.876  1.00 87.08           C  
ANISOU 5844  CG  LEU B 270     8889  18791   5407   3239    375   -255       C  
ATOM   5845  CD1 LEU B 270      30.656  -8.577  40.661  1.00 97.63           C  
ANISOU 5845  CD1 LEU B 270    10265  19911   6920   2936    297   -608       C  
ATOM   5846  CD2 LEU B 270      29.082  -8.610  42.604  1.00 92.39           C  
ANISOU 5846  CD2 LEU B 270     9679  19391   6033   3231    473   -244       C  
ATOM   5847  N   PRO B 271      31.893 -12.854  42.712  1.00 93.87           N  
ANISOU 5847  N   PRO B 271     9455  20210   6002   3963    354    511       N  
ATOM   5848  CA  PRO B 271      33.060 -13.066  43.589  1.00 97.39           C  
ANISOU 5848  CA  PRO B 271     9754  21019   6232   4161    198    482       C  
ATOM   5849  C   PRO B 271      34.337 -13.355  42.818  1.00 99.58           C  
ANISOU 5849  C   PRO B 271     9873  21416   6546   4138     69    342       C  
ATOM   5850  O   PRO B 271      35.373 -12.728  43.075  1.00 98.16           O  
ANISOU 5850  O   PRO B 271     9548  21476   6272   4084   -107     44       O  
ATOM   5851  CB  PRO B 271      32.626 -14.255  44.461  1.00 99.42           C  
ANISOU 5851  CB  PRO B 271    10057  21338   6381   4495    321    930       C  
ATOM   5852  CG  PRO B 271      31.136 -14.220  44.444  1.00 98.08           C  
ANISOU 5852  CG  PRO B 271    10052  20891   6322   4435    532   1107       C  
ATOM   5853  CD  PRO B 271      30.761 -13.726  43.077  1.00103.79           C  
ANISOU 5853  CD  PRO B 271    10814  21337   7285   4137    562    924       C  
ATOM   5854  N   PHE B 272      34.292 -14.296  41.871  1.00100.82           N  
ANISOU 5854  N   PHE B 272    10057  21408   6841   4173    165    553       N  
ATOM   5855  CA  PHE B 272      35.496 -14.642  41.124  1.00100.07           C  
ANISOU 5855  CA  PHE B 272     9818  21369   6836   4156     68    442       C  
ATOM   5856  C   PHE B 272      35.983 -13.472  40.280  1.00 98.14           C  
ANISOU 5856  C   PHE B 272     9544  21042   6701   3811    -14    -36       C  
ATOM   5857  O   PHE B 272      37.186 -13.194  40.228  1.00104.64           O  
ANISOU 5857  O   PHE B 272    10182  22097   7478   3785   -162   -287       O  
ATOM   5858  CB  PHE B 272      35.234 -15.862  40.241  1.00 97.20           C  
ANISOU 5858  CB  PHE B 272     9524  20577   6831   4176    227    758       C  
ATOM   5859  CG  PHE B 272      36.273 -16.071  39.174  1.00 95.73           C  
ANISOU 5859  CG  PHE B 272     9240  20227   6905   4048    186    598       C  
ATOM   5860  CD1 PHE B 272      37.452 -16.738  39.458  1.00 99.85           C  
ANISOU 5860  CD1 PHE B 272     9563  21002   7373   4280     93    672       C  
ATOM   5861  CD2 PHE B 272      36.068 -15.600  37.888  1.00 94.38           C  
ANISOU 5861  CD2 PHE B 272     9186  19641   7034   3709    247    376       C  
ATOM   5862  CE1 PHE B 272      38.408 -16.929  38.480  1.00 93.71           C  
ANISOU 5862  CE1 PHE B 272     8687  20064   6856   4168     88    525       C  
ATOM   5863  CE2 PHE B 272      37.022 -15.789  36.906  1.00 91.28           C  
ANISOU 5863  CE2 PHE B 272     8733  19074   6876   3590    244    228       C  
ATOM   5864  CZ  PHE B 272      38.193 -16.455  37.202  1.00 85.33           C  
ANISOU 5864  CZ  PHE B 272     7762  18573   6087   3816    177    302       C  
ATOM   5865  N   HIS B 273      35.064 -12.773  39.611  1.00 93.53           N  
ANISOU 5865  N   HIS B 273     9142  20125   6271   3545     84   -171       N  
ATOM   5866  CA  HIS B 273      35.478 -11.728  38.681  1.00103.21           C  
ANISOU 5866  CA  HIS B 273    10396  21197   7624   3213     40   -605       C  
ATOM   5867  C   HIS B 273      35.964 -10.483  39.411  1.00103.08           C  
ANISOU 5867  C   HIS B 273    10295  21386   7484   3095   -104   -951       C  
ATOM   5868  O   HIS B 273      36.833  -9.768  38.898  1.00100.24           O  
ANISOU 5868  O   HIS B 273     9867  21025   7196   2880   -176  -1310       O  
ATOM   5869  CB  HIS B 273      34.329 -11.385  37.735  1.00104.29           C  
ANISOU 5869  CB  HIS B 273    10770  20844   8011   2975    170   -619       C  
ATOM   5870  CG  HIS B 273      34.082 -12.429  36.691  1.00 93.42           C  
ANISOU 5870  CG  HIS B 273     9479  19019   6996   2938    275   -374       C  
ATOM   5871  ND1 HIS B 273      34.842 -12.529  35.546  1.00 77.36           N  
ANISOU 5871  ND1 HIS B 273     7465  16723   5204   2760    278   -538       N  
ATOM   5872  CD2 HIS B 273      33.168 -13.425  36.624  1.00 97.60           C  
ANISOU 5872  CD2 HIS B 273    10093  19305   7684   3047    393     18       C  
ATOM   5873  CE1 HIS B 273      34.404 -13.540  34.817  1.00 86.15           C  
ANISOU 5873  CE1 HIS B 273     8692  17450   6593   2764    383   -257       C  
ATOM   5874  NE2 HIS B 273      33.388 -14.100  35.448  1.00 88.77           N  
ANISOU 5874  NE2 HIS B 273     9056  17789   6885   2929    448     80       N  
ATOM   5875  N   VAL B 274      35.431 -10.210  40.602  1.00105.54           N  
ANISOU 5875  N   VAL B 274    10623  21825   7652   3213   -123   -846       N  
ATOM   5876  CA  VAL B 274      35.947  -9.102  41.402  1.00111.01           C  
ANISOU 5876  CA  VAL B 274    11247  22693   8238   3113   -245  -1140       C  
ATOM   5877  C   VAL B 274      37.390  -9.378  41.804  1.00102.26           C  
ANISOU 5877  C   VAL B 274     9876  21989   6988   3239   -408  -1249       C  
ATOM   5878  O   VAL B 274      38.260  -8.504  41.706  1.00103.40           O  
ANISOU 5878  O   VAL B 274     9914  22220   7152   3042   -507  -1610       O  
ATOM   5879  CB  VAL B 274      35.052  -8.859  42.629  1.00108.75           C  
ANISOU 5879  CB  VAL B 274    11065  22456   7799   3241   -206   -979       C  
ATOM   5880  CG1 VAL B 274      35.722  -7.886  43.589  1.00 91.65           C  
ANISOU 5880  CG1 VAL B 274     8833  20520   5472   3183   -336  -1241       C  
ATOM   5881  CG2 VAL B 274      33.697  -8.323  42.193  1.00111.47           C  
ANISOU 5881  CG2 VAL B 274    11637  22421   8297   3077    -61   -955       C  
ATOM   5882  N   LEU B 275      37.666 -10.600  42.267  1.00101.03           N  
ANISOU 5882  N   LEU B 275     9610  22077   6698   3573   -432   -930       N  
ATOM   5883  CA  LEU B 275      39.038 -10.968  42.597  1.00104.00           C  
ANISOU 5883  CA  LEU B 275     9720  22843   6953   3729   -600  -1006       C  
ATOM   5884  C   LEU B 275      39.930 -10.916  41.363  1.00102.54           C  
ANISOU 5884  C   LEU B 275     9406  22632   6923   3551   -632  -1256       C  
ATOM   5885  O   LEU B 275      41.090 -10.495  41.442  1.00104.50           O  
ANISOU 5885  O   LEU B 275     9426  23138   7140   3486   -777  -1549       O  
ATOM   5886  CB  LEU B 275      39.074 -12.366  43.215  1.00108.16           C  
ANISOU 5886  CB  LEU B 275    10199  23550   7349   4135   -598   -565       C  
ATOM   5887  CG  LEU B 275      38.354 -12.551  44.551  1.00112.46           C  
ANISOU 5887  CG  LEU B 275    10867  24158   7707   4350   -559   -314       C  
ATOM   5888  CD1 LEU B 275      38.365 -14.014  44.964  1.00111.44           C  
ANISOU 5888  CD1 LEU B 275    10731  24109   7502   4731   -511    136       C  
ATOM   5889  CD2 LEU B 275      38.995 -11.690  45.626  1.00111.73           C  
ANISOU 5889  CD2 LEU B 275    10685  24348   7420   4329   -725   -576       C  
ATOM   5890  N   THR B 276      39.403 -11.339  40.212  1.00100.02           N  
ANISOU 5890  N   THR B 276     9239  21994   6771   3463   -483  -1156       N  
ATOM   5891  CA  THR B 276      40.176 -11.279  38.975  1.00 92.61           C  
ANISOU 5891  CA  THR B 276     8233  20850   6105   3246   -446  -1389       C  
ATOM   5892  C   THR B 276      40.495  -9.839  38.593  1.00 89.64           C  
ANISOU 5892  C   THR B 276     7880  20449   5731   2887   -476  -1899       C  
ATOM   5893  O   THR B 276      41.616  -9.534  38.172  1.00 94.27           O  
ANISOU 5893  O   THR B 276     8280  21143   6397   2755   -534  -2204       O  
ATOM   5894  CB  THR B 276      39.412 -11.973  37.846  1.00 92.36           C  
ANISOU 5894  CB  THR B 276     8423  20243   6425   3162   -234  -1151       C  
ATOM   5895  OG1 THR B 276      39.264 -13.367  38.149  1.00 96.62           O  
ANISOU 5895  OG1 THR B 276     8931  20769   7011   3477   -187   -687       O  
ATOM   5896  CG2 THR B 276      40.147 -11.820  36.522  1.00 98.73           C  
ANISOU 5896  CG2 THR B 276     9224  20728   7560   2900   -159  -1404       C  
ATOM   5897  N   PHE B 277      39.520  -8.938  38.733  1.00 99.70           N  
ANISOU 5897  N   PHE B 277     9376  21419   7085   2695   -413  -1956       N  
ATOM   5898  CA  PHE B 277      39.749  -7.543  38.372  1.00102.11           C  
ANISOU 5898  CA  PHE B 277     9749  21511   7538   2331   -412  -2362       C  
ATOM   5899  C   PHE B 277      40.811  -6.909  39.261  1.00102.69           C  
ANISOU 5899  C   PHE B 277     9573  21971   7474   2320   -569  -2612       C  
ATOM   5900  O   PHE B 277      41.670  -6.161  38.778  1.00104.71           O  
ANISOU 5900  O   PHE B 277     9741  22202   7843   2069   -584  -2972       O  
ATOM   5901  CB  PHE B 277      38.434  -6.764  38.459  1.00 97.50           C  
ANISOU 5901  CB  PHE B 277     9457  20552   7036   2188   -324  -2311       C  
ATOM   5902  CG  PHE B 277      38.558  -5.315  38.083  1.00 94.69           C  
ANISOU 5902  CG  PHE B 277     9230  19912   6835   1833   -303  -2662       C  
ATOM   5903  CD1 PHE B 277      38.783  -4.945  36.767  1.00100.08           C  
ANISOU 5903  CD1 PHE B 277    10046  20217   7761   1562   -215  -2866       C  
ATOM   5904  CD2 PHE B 277      38.439  -4.323  39.041  1.00 84.43           C  
ANISOU 5904  CD2 PHE B 277     7957  18688   5436   1776   -351  -2766       C  
ATOM   5905  CE1 PHE B 277      38.895  -3.613  36.416  1.00 99.19           C  
ANISOU 5905  CE1 PHE B 277    10088  19803   7795   1251   -176  -3142       C  
ATOM   5906  CE2 PHE B 277      38.549  -2.990  38.696  1.00 93.67           C  
ANISOU 5906  CE2 PHE B 277     9276  19573   6743   1463   -311  -3049       C  
ATOM   5907  CZ  PHE B 277      38.777  -2.634  37.382  1.00 96.34           C  
ANISOU 5907  CZ  PHE B 277     9744  19531   7330   1207   -222  -3224       C  
ATOM   5908  N   LEU B 278      40.772  -7.196  40.564  1.00108.60           N  
ANISOU 5908  N   LEU B 278    10219  23057   7985   2582   -675  -2428       N  
ATOM   5909  CA  LEU B 278      41.768  -6.641  41.475  1.00106.25           C  
ANISOU 5909  CA  LEU B 278     9701  23130   7539   2586   -833  -2654       C  
ATOM   5910  C   LEU B 278      43.159  -7.183  41.168  1.00113.53           C  
ANISOU 5910  C   LEU B 278    10288  24397   8451   2662   -952  -2797       C  
ATOM   5911  O   LEU B 278      44.135  -6.426  41.122  1.00116.40           O  
ANISOU 5911  O   LEU B 278    10474  24897   8855   2464  -1024  -3162       O  
ATOM   5912  CB  LEU B 278      41.379  -6.946  42.922  1.00117.04           C  
ANISOU 5912  CB  LEU B 278    11084  24741   8646   2871   -909  -2397       C  
ATOM   5913  CG  LEU B 278      40.072  -6.321  43.412  1.00 97.11           C  
ANISOU 5913  CG  LEU B 278     8860  21938   6100   2805   -803  -2291       C  
ATOM   5914  CD1 LEU B 278      39.688  -6.893  44.765  1.00 99.92           C  
ANISOU 5914  CD1 LEU B 278     9243  22531   6193   3128   -848  -1994       C  
ATOM   5915  CD2 LEU B 278      40.192  -4.806  43.485  1.00 97.20           C  
ANISOU 5915  CD2 LEU B 278     8964  21801   6168   2475   -804  -2644       C  
ATOM   5916  N   ASP B 279      43.269  -8.498  40.957  1.00107.34           N  
ANISOU 5916  N   ASP B 279     9409  23751   7626   2952   -971  -2501       N  
ATOM   5917  CA  ASP B 279      44.558  -9.086  40.607  1.00103.03           C  
ANISOU 5917  CA  ASP B 279     8529  23513   7104   3051  -1098  -2600       C  
ATOM   5918  C   ASP B 279      45.166  -8.394  39.394  1.00102.18           C  
ANISOU 5918  C   ASP B 279     8372  23243   7209   2688  -1027  -3029       C  
ATOM   5919  O   ASP B 279      46.379  -8.165  39.342  1.00107.00           O  
ANISOU 5919  O   ASP B 279     8665  24121   7870   2615  -1147  -3320       O  
ATOM   5920  CB  ASP B 279      44.391 -10.583  40.344  1.00102.63           C  
ANISOU 5920  CB  ASP B 279     8451  23475   7069   3390  -1087  -2156       C  
ATOM   5921  CG  ASP B 279      45.706 -11.276  40.048  1.00106.23           C  
ANISOU 5921  CG  ASP B 279     8551  24060   7752   3511  -1162  -2160       C  
ATOM   5922  OD1 ASP B 279      46.765 -10.622  40.144  1.00115.10           O  
ANISOU 5922  OD1 ASP B 279     9389  25476   8869   3378  -1314  -2539       O  
ATOM   5923  OD2 ASP B 279      45.679 -12.481  39.720  1.00107.15           O  
ANISOU 5923  OD2 ASP B 279     8668  23981   8063   3739  -1059  -1786       O  
ATOM   5924  N   ALA B 280      44.336  -8.053  38.407  1.00100.66           N  
ANISOU 5924  N   ALA B 280     8500  22565   7180   2447   -812  -3071       N  
ATOM   5925  CA  ALA B 280      44.834  -7.303  37.260  1.00102.32           C  
ANISOU 5925  CA  ALA B 280     8752  22497   7627   2073   -681  -3476       C  
ATOM   5926  C   ALA B 280      45.326  -5.925  37.683  1.00105.42           C  
ANISOU 5926  C   ALA B 280     9074  22909   8073   1791   -731  -3841       C  
ATOM   5927  O   ALA B 280      46.358  -5.448  37.196  1.00104.09           O  
ANISOU 5927  O   ALA B 280     8720  22803   8027   1574   -721  -4211       O  
ATOM   5928  CB  ALA B 280      43.743  -7.181  36.198  1.00105.50           C  
ANISOU 5928  CB  ALA B 280     9568  22269   8248   1882   -443  -3385       C  
ATOM   5929  N   LEU B 281      44.597  -5.269  38.590  1.00110.06           N  
ANISOU 5929  N   LEU B 281     9817  23434   8568   1788   -760  -3742       N  
ATOM   5930  CA  LEU B 281      45.041  -3.983  39.113  1.00116.14           C  
ANISOU 5930  CA  LEU B 281    10547  24238   9341   1552   -799  -4046       C  
ATOM   5931  C   LEU B 281      46.353  -4.102  39.877  1.00116.49           C  
ANISOU 5931  C   LEU B 281    10183  24845   9234   1665   -992  -4230       C  
ATOM   5932  O   LEU B 281      47.070  -3.104  40.015  1.00118.61           O  
ANISOU 5932  O   LEU B 281    10349  25167   9550   1421  -1010  -4570       O  
ATOM   5933  CB  LEU B 281      43.959  -3.389  40.014  1.00113.08           C  
ANISOU 5933  CB  LEU B 281    10422  23701   8840   1577   -794  -3870       C  
ATOM   5934  CG  LEU B 281      42.677  -2.957  39.299  1.00103.92           C  
ANISOU 5934  CG  LEU B 281     9666  21957   7862   1411   -618  -3750       C  
ATOM   5935  CD1 LEU B 281      41.617  -2.545  40.306  1.00102.32           C  
ANISOU 5935  CD1 LEU B 281     9671  21694   7513   1499   -624  -3559       C  
ATOM   5936  CD2 LEU B 281      42.959  -1.824  38.324  1.00113.03           C  
ANISOU 5936  CD2 LEU B 281    10973  22702   9273   1018   -495  -4058       C  
ATOM   5937  N   ALA B 282      46.679  -5.293  40.381  1.00108.45           N  
ANISOU 5937  N   ALA B 282     8942  24218   8047   2033  -1140  -3990       N  
ATOM   5938  CA  ALA B 282      47.981  -5.501  41.005  1.00118.09           C  
ANISOU 5938  CA  ALA B 282     9768  25927   9174   2157  -1346  -4136       C  
ATOM   5939  C   ALA B 282      49.080  -5.556  39.951  1.00113.56           C  
ANISOU 5939  C   ALA B 282     8912  25408   8826   1982  -1330  -4456       C  
ATOM   5940  O   ALA B 282      50.086  -4.844  40.049  1.00110.62           O  
ANISOU 5940  O   ALA B 282     8308  25201   8521   1781  -1384  -4824       O  
ATOM   5941  CB  ALA B 282      47.966  -6.783  41.838  1.00120.37           C  
ANISOU 5941  CB  ALA B 282     9948  26518   9270   2620  -1502  -3716       C  
ATOM   5942  N   TRP B 283      48.903  -6.401  38.931  1.00116.12           N  
ANISOU 5942  N   TRP B 283     9252  25587   9282   2045  -1251  -4325       N  
ATOM   5943  CA  TRP B 283      49.899  -6.505  37.870  1.00108.43           C  
ANISOU 5943  CA  TRP B 283     8022  24564   8613   1870  -1188  -4597       C  
ATOM   5944  C   TRP B 283      50.121  -5.171  37.168  1.00110.99           C  
ANISOU 5944  C   TRP B 283     8474  24651   9046   1387  -1020  -5114       C  
ATOM   5945  O   TRP B 283      51.209  -4.928  36.632  1.00109.28           O  
ANISOU 5945  O   TRP B 283     7980  24465   9075   1190   -976  -5442       O  
ATOM   5946  CB  TRP B 283      49.475  -7.567  36.854  1.00111.71           C  
ANISOU 5946  CB  TRP B 283     8629  24461   9355   1980   -934  -4226       C  
ATOM   5947  CG  TRP B 283      49.498  -8.966  37.391  1.00108.88           C  
ANISOU 5947  CG  TRP B 283     8113  24276   8983   2441  -1044  -3729       C  
ATOM   5948  CD1 TRP B 283      48.421  -9.732  37.732  1.00110.59           C  
ANISOU 5948  CD1 TRP B 283     8588  24376   9056   2707  -1021  -3269       C  
ATOM   5949  CD2 TRP B 283      50.658  -9.767  37.651  1.00107.75           C  
ANISOU 5949  CD2 TRP B 283     7519  24443   8979   2697  -1181  -3640       C  
ATOM   5950  NE1 TRP B 283      48.838 -10.960  38.186  1.00112.28           N  
ANISOU 5950  NE1 TRP B 283     8573  24794   9294   3109  -1122  -2898       N  
ATOM   5951  CE2 TRP B 283      50.207 -11.007  38.146  1.00108.12           C  
ANISOU 5951  CE2 TRP B 283     7610  24535   8936   3125  -1231  -3111       C  
ATOM   5952  CE3 TRP B 283      52.033  -9.556  37.512  1.00111.11           C  
ANISOU 5952  CE3 TRP B 283     7498  25108   9609   2610  -1259  -3958       C  
ATOM   5953  CZ2 TRP B 283      51.082 -12.030  38.504  1.00111.68           C  
ANISOU 5953  CZ2 TRP B 283     7699  25257   9476   3485  -1361  -2883       C  
ATOM   5954  CZ3 TRP B 283      52.900 -10.574  37.867  1.00114.70           C  
ANISOU 5954  CZ3 TRP B 283     7557  25847  10175   2969  -1401  -3733       C  
ATOM   5955  CH2 TRP B 283      52.421 -11.795  38.357  1.00114.93           C  
ANISOU 5955  CH2 TRP B 283     7683  25893  10093   3405  -1447  -3193       C  
ATOM   5956  N   MET B 284      49.113  -4.297  37.155  1.00110.04           N  
ANISOU 5956  N   MET B 284     8781  24098   8933   1196   -850  -5077       N  
ATOM   5957  CA  MET B 284      49.258  -2.987  36.532  1.00111.07           C  
ANISOU 5957  CA  MET B 284     9081  23823   9296    758   -658  -5414       C  
ATOM   5958  C   MET B 284      49.899  -1.958  37.454  1.00117.35           C  
ANISOU 5958  C   MET B 284     9700  24868  10020    626   -759  -5660       C  
ATOM   5959  O   MET B 284      50.279  -0.881  36.982  1.00121.50           O  
ANISOU 5959  O   MET B 284    10291  25136  10737    268   -614  -5963       O  
ATOM   5960  CB  MET B 284      47.894  -2.471  36.066  1.00112.12           C  
ANISOU 5960  CB  MET B 284     9743  23314   9544    617   -481  -5195       C  
ATOM   5961  CG  MET B 284      47.426  -3.078  34.753  1.00127.38           C  
ANISOU 5961  CG  MET B 284    11936  24787  11675    571   -291  -5080       C  
ATOM   5962  SD  MET B 284      45.877  -2.379  34.151  1.00117.15           S  
ANISOU 5962  SD  MET B 284    11251  22714  10547    391   -128  -4837       S  
ATOM   5963  CE  MET B 284      44.691  -3.285  35.139  1.00110.29           C  
ANISOU 5963  CE  MET B 284    10433  22068   9405    790   -264  -4385       C  
ATOM   5964  N   GLY B 285      50.030  -2.258  38.742  1.00123.89           N  
ANISOU 5964  N   GLY B 285    10345  26147  10580    903   -989  -5516       N  
ATOM   5965  CA  GLY B 285      50.691  -1.369  39.670  1.00120.67           C  
ANISOU 5965  CA  GLY B 285     9785  25990  10072    796  -1100  -5746       C  
ATOM   5966  C   GLY B 285      49.800  -0.359  40.354  1.00133.88           C  
ANISOU 5966  C   GLY B 285    11806  27419  11642    690  -1062  -5658       C  
ATOM   5967  O   GLY B 285      50.319   0.553  41.008  1.00150.00           O  
ANISOU 5967  O   GLY B 285    13780  29596  13615    538  -1124  -5884       O  
ATOM   5968  N   VAL B 286      48.482  -0.486  40.228  1.00134.23           N  
ANISOU 5968  N   VAL B 286    12221  27102  11679    763   -968  -5341       N  
ATOM   5969  CA  VAL B 286      47.573   0.429  40.911  1.00134.00           C  
ANISOU 5969  CA  VAL B 286    12524  26835  11554    689   -939  -5238       C  
ATOM   5970  C   VAL B 286      47.306  -0.034  42.337  1.00134.83           C  
ANISOU 5970  C   VAL B 286    12584  27312  11335   1011  -1133  -5008       C  
ATOM   5971  O   VAL B 286      47.306   0.776  43.268  1.00141.20           O  
ANISOU 5971  O   VAL B 286    13469  28195  11986    948  -1202  -5088       O  
ATOM   5972  CB  VAL B 286      46.262   0.579  40.114  1.00132.56           C  
ANISOU 5972  CB  VAL B 286    12767  26063  11536    606   -750  -5017       C  
ATOM   5973  CG1 VAL B 286      45.403   1.683  40.717  1.00136.81           C  
ANISOU 5973  CG1 VAL B 286    13647  26327  12008    494   -704  -4963       C  
ATOM   5974  CG2 VAL B 286      46.561   0.873  38.653  1.00140.30           C  
ANISOU 5974  CG2 VAL B 286    13826  26646  12834    321   -565  -5202       C  
ATOM   5975  N   ILE B 287      47.071  -1.329  42.527  1.00121.99           N  
ANISOU 5975  N   ILE B 287    10863  25893   9596   1358  -1215  -4708       N  
ATOM   5976  CA  ILE B 287      46.828  -1.904  43.844  1.00129.71           C  
ANISOU 5976  CA  ILE B 287    11821  27190  10273   1694  -1383  -4445       C  
ATOM   5977  C   ILE B 287      48.127  -2.588  44.257  1.00138.13           C  
ANISOU 5977  C   ILE B 287    12481  28767  11235   1884  -1598  -4529       C  
ATOM   5978  O   ILE B 287      48.386  -3.738  43.891  1.00137.60           O  
ANISOU 5978  O   ILE B 287    12242  28844  11196   2120  -1639  -4354       O  
ATOM   5979  CB  ILE B 287      45.649  -2.879  43.832  1.00121.05           C  
ANISOU 5979  CB  ILE B 287    10926  25940   9129   1965  -1314  -4012       C  
ATOM   5980  N   ASN B 288      48.947  -1.873  45.025  1.00151.44           N  
ANISOU 5980  N   ASN B 288    14024  30708  12807   1783  -1746  -4784       N  
ATOM   5981  CA  ASN B 288      50.211  -2.387  45.532  1.00155.47           C  
ANISOU 5981  CA  ASN B 288    14156  31688  13228   1947  -1986  -4879       C  
ATOM   5982  C   ASN B 288      50.147  -2.772  47.002  1.00164.54           C  
ANISOU 5982  C   ASN B 288    15336  33130  14050   2255  -2210  -4648       C  
ATOM   5983  O   ASN B 288      51.175  -3.141  47.577  1.00175.23           O  
ANISOU 5983  O   ASN B 288    16408  34858  15314   2402  -2447  -4704       O  
ATOM   5984  CB  ASN B 288      51.321  -1.354  45.315  1.00158.03           C  
ANISOU 5984  CB  ASN B 288    14263  32107  13676   1602  -2016  -5356       C  
ATOM   5985  CG  ASN B 288      51.591  -1.093  43.848  1.00154.91           C  
ANISOU 5985  CG  ASN B 288    13797  31451  13611   1314  -1798  -5604       C  
ATOM   5986  OD1 ASN B 288      51.744  -2.026  43.059  1.00153.26           O  
ANISOU 5986  OD1 ASN B 288    13450  31243  13539   1439  -1759  -5506       O  
ATOM   5987  ND2 ASN B 288      51.653   0.179  43.473  1.00154.24           N  
ANISOU 5987  ND2 ASN B 288    13830  31114  13658    924  -1646  -5916       N  
ATOM   5988  N   SER B 289      48.972  -2.701  47.622  1.00160.95           N  
ANISOU 5988  N   SER B 289    15226  32498  13430   2355  -2142  -4389       N  
ATOM   5989  CA  SER B 289      48.847  -3.026  49.037  1.00163.21           C  
ANISOU 5989  CA  SER B 289    15595  33027  13392   2634  -2331  -4177       C  
ATOM   5990  C   SER B 289      49.099  -4.515  49.243  1.00158.53           C  
ANISOU 5990  C   SER B 289    14844  32662  12727   3052  -2447  -3840       C  
ATOM   5991  O   SER B 289      48.425  -5.358  48.643  1.00160.29           O  
ANISOU 5991  O   SER B 289    15151  32706  13047   3208  -2295  -3555       O  
ATOM   5992  CB  SER B 289      47.463  -2.636  49.546  1.00155.53           C  
ANISOU 5992  CB  SER B 289    15038  31765  12290   2634  -2189  -3976       C  
ATOM   5993  OG  SER B 289      47.270  -3.069  50.880  1.00156.45           O  
ANISOU 5993  OG  SER B 289    15266  32092  12086   2925  -2345  -3744       O  
ATOM   5994  N   CYS B 290      50.071  -4.835  50.102  1.00165.86           N  
ANISOU 5994  N   CYS B 290    15561  33966  13491   3234  -2722  -3862       N  
ATOM   5995  CA  CYS B 290      50.414  -6.230  50.350  1.00169.00           C  
ANISOU 5995  CA  CYS B 290    15817  34563  13833   3643  -2846  -3532       C  
ATOM   5996  C   CYS B 290      49.284  -6.972  51.050  1.00169.32           C  
ANISOU 5996  C   CYS B 290    16177  34495  13663   3955  -2768  -3087       C  
ATOM   5997  O   CYS B 290      49.090  -8.170  50.814  1.00152.19           O  
ANISOU 5997  O   CYS B 290    13995  32297  11534   4248  -2713  -2745       O  
ATOM   5998  CB  CYS B 290      51.689  -6.307  51.190  1.00160.31           C  
ANISOU 5998  CB  CYS B 290    14442  33862  12605   3757  -3180  -3661       C  
ATOM   5999  SG  CYS B 290      53.211  -6.405  50.227  1.00169.31           S  
ANISOU 5999  SG  CYS B 290    15076  35180  14073   3624  -3287  -3968       S  
ATOM   6000  N   GLU B 291      48.532  -6.282  51.909  1.00171.57           N  
ANISOU 6000  N   GLU B 291    16758  34699  13732   3893  -2747  -3082       N  
ATOM   6001  CA  GLU B 291      47.419  -6.923  52.600  1.00170.98           C  
ANISOU 6001  CA  GLU B 291    16997  34503  13465   4167  -2648  -2680       C  
ATOM   6002  C   GLU B 291      46.359  -7.410  51.621  1.00165.35           C  
ANISOU 6002  C   GLU B 291    16422  33445  12961   4172  -2353  -2449       C  
ATOM   6003  O   GLU B 291      45.732  -8.451  51.849  1.00164.87           O  
ANISOU 6003  O   GLU B 291    16490  33322  12832   4475  -2268  -2056       O  
ATOM   6004  CB  GLU B 291      46.808  -5.946  53.606  1.00172.40           C  
ANISOU 6004  CB  GLU B 291    17477  34623  13403   4045  -2659  -2764       C  
ATOM   6005  CG  GLU B 291      45.760  -6.554  54.521  1.00172.91           C  
ANISOU 6005  CG  GLU B 291    17868  34601  13230   4333  -2578  -2376       C  
ATOM   6006  CD  GLU B 291      45.243  -5.564  55.548  1.00174.81           C  
ANISOU 6006  CD  GLU B 291    18412  34792  13217   4209  -2599  -2477       C  
ATOM   6007  OE1 GLU B 291      45.783  -4.440  55.615  1.00176.14           O  
ANISOU 6007  OE1 GLU B 291    18533  35015  13377   3915  -2703  -2839       O  
ATOM   6008  OE2 GLU B 291      44.299  -5.910  56.290  1.00175.14           O  
ANISOU 6008  OE2 GLU B 291    18753  34726  13065   4401  -2498  -2194       O  
ATOM   6009  N   VAL B 292      46.147  -6.677  50.527  1.00173.23           N  
ANISOU 6009  N   VAL B 292    17405  34201  14212   3836  -2195  -2684       N  
ATOM   6010  CA  VAL B 292      45.121  -7.055  49.560  1.00172.50           C  
ANISOU 6010  CA  VAL B 292    17460  33761  14322   3810  -1938  -2487       C  
ATOM   6011  C   VAL B 292      45.529  -8.308  48.792  1.00168.07           C  
ANISOU 6011  C   VAL B 292    16704  33252  13903   4023  -1925  -2280       C  
ATOM   6012  O   VAL B 292      44.731  -9.238  48.627  1.00169.03           O  
ANISOU 6012  O   VAL B 292    16965  33215  14042   4235  -1786  -1913       O  
ATOM   6013  CB  VAL B 292      44.833  -5.881  48.606  1.00185.08           C  
ANISOU 6013  CB  VAL B 292    19121  35056  16146   3386  -1792  -2806       C  
ATOM   6014  CG1 VAL B 292      43.924  -6.328  47.469  1.00185.03           C  
ANISOU 6014  CG1 VAL B 292    19236  34697  16370   3350  -1567  -2626       C  
ATOM   6015  CG2 VAL B 292      44.217  -4.718  49.368  1.00187.03           C  
ANISOU 6015  CG2 VAL B 292    19629  35173  16262   3204  -1765  -2929       C  
ATOM   6016  N   ILE B 293      46.772  -8.354  48.308  1.00152.12           N  
ANISOU 6016  N   ILE B 293    14364  31437  11998   3965  -2060  -2507       N  
ATOM   6017  CA  ILE B 293      47.201  -9.486  47.489  1.00150.23           C  
ANISOU 6017  CA  ILE B 293    13943  31211  11927   4144  -2039  -2323       C  
ATOM   6018  C   ILE B 293      47.081 -10.790  48.268  1.00145.50           C  
ANISOU 6018  C   ILE B 293    13395  30724  11165   4590  -2089  -1870       C  
ATOM   6019  O   ILE B 293      46.754 -11.840  47.702  1.00139.81           O  
ANISOU 6019  O   ILE B 293    12708  29857  10556   4779  -1966  -1552       O  
ATOM   6020  CB  ILE B 293      48.636  -9.266  46.976  1.00147.79           C  
ANISOU 6020  CB  ILE B 293    13260  31116  11777   4011  -2190  -2659       C  
ATOM   6021  CG1 ILE B 293      48.694  -8.035  46.070  1.00145.66           C  
ANISOU 6021  CG1 ILE B 293    12973  30676  11696   3556  -2084  -3097       C  
ATOM   6022  CG2 ILE B 293      49.123 -10.501  46.226  1.00144.98           C  
ANISOU 6022  CG2 ILE B 293    12716  30758  11610   4230  -2178  -2431       C  
ATOM   6023  CD1 ILE B 293      50.098  -7.613  45.692  1.00146.08           C  
ANISOU 6023  CD1 ILE B 293    12663  30940  11902   3373  -2217  -3488       C  
ATOM   6024  N   ALA B 294      47.346 -10.749  49.575  1.00150.85           N  
ANISOU 6024  N   ALA B 294    14100  31639  11576   4762  -2266  -1830       N  
ATOM   6025  CA  ALA B 294      47.171 -11.947  50.390  1.00153.44           C  
ANISOU 6025  CA  ALA B 294    14529  32042  11729   5185  -2296  -1400       C  
ATOM   6026  C   ALA B 294      45.703 -12.350  50.453  1.00150.26           C  
ANISOU 6026  C   ALA B 294    14467  31343  11283   5280  -2042  -1060       C  
ATOM   6027  O   ALA B 294      45.375 -13.540  50.378  1.00149.94           O  
ANISOU 6027  O   ALA B 294    14501  31206  11263   5563  -1934   -671       O  
ATOM   6028  CB  ALA B 294      47.730 -11.717  51.793  1.00159.11           C  
ANISOU 6028  CB  ALA B 294    15242  33064  12148   5325  -2553  -1458       C  
ATOM   6029  N   VAL B 295      44.805 -11.371  50.591  1.00165.78           N  
ANISOU 6029  N   VAL B 295    16644  33139  13208   5042  -1934  -1196       N  
ATOM   6030  CA  VAL B 295      43.375 -11.666  50.596  1.00165.12           C  
ANISOU 6030  CA  VAL B 295    16862  32752  13125   5098  -1688   -900       C  
ATOM   6031  C   VAL B 295      42.960 -12.291  49.270  1.00158.51           C  
ANISOU 6031  C   VAL B 295    16006  31655  12567   5060  -1496   -748       C  
ATOM   6032  O   VAL B 295      42.191 -13.259  49.235  1.00157.86           O  
ANISOU 6032  O   VAL B 295    16076  31401  12501   5271  -1332   -362       O  
ATOM   6033  CB  VAL B 295      42.569 -10.389  50.900  1.00163.00           C  
ANISOU 6033  CB  VAL B 295    16800  32327  12804   4817  -1618  -1112       C  
ATOM   6034  CG1 VAL B 295      41.079 -10.644  50.727  1.00170.53           C  
ANISOU 6034  CG1 VAL B 295    18030  32939  13823   4837  -1355   -833       C  
ATOM   6035  CG2 VAL B 295      42.872  -9.892  52.306  1.00152.61           C  
ANISOU 6035  CG2 VAL B 295    15564  31244  11176   4890  -1796  -1200       C  
ATOM   6036  N   ILE B 296      43.455 -11.744  48.157  1.00148.98           N  
ANISOU 6036  N   ILE B 296    14628  30399  11579   4780  -1509  -1049       N  
ATOM   6037  CA  ILE B 296      43.160 -12.323  46.850  1.00142.00           C  
ANISOU 6037  CA  ILE B 296    13734  29273  10946   4734  -1355   -926       C  
ATOM   6038  C   ILE B 296      43.579 -13.787  46.822  1.00141.73           C  
ANISOU 6038  C   ILE B 296    13612  29310  10929   5092  -1361   -557       C  
ATOM   6039  O   ILE B 296      42.842 -14.658  46.347  1.00135.46           O  
ANISOU 6039  O   ILE B 296    12959  28277  10234   5215  -1184   -217       O  
ATOM   6040  CB  ILE B 296      43.861 -11.526  45.735  1.00149.80           C  
ANISOU 6040  CB  ILE B 296    14535  30240  12142   4395  -1397  -1342       C  
ATOM   6041  CG1 ILE B 296      43.373 -10.076  45.715  1.00142.95           C  
ANISOU 6041  CG1 ILE B 296    13804  29219  11290   4031  -1351  -1682       C  
ATOM   6042  CG2 ILE B 296      43.628 -12.188  44.379  1.00144.41           C  
ANISOU 6042  CG2 ILE B 296    13856  29315  11696   4365  -1262  -1209       C  
ATOM   6043  CD1 ILE B 296      44.165  -9.175  44.781  1.00145.62           C  
ANISOU 6043  CD1 ILE B 296    13974  29541  11813   3681  -1386  -2133       C  
ATOM   6044  N   ASP B 297      44.776 -14.076  47.337  1.00140.57           N  
ANISOU 6044  N   ASP B 297    13238  29468  10703   5258  -1564   -612       N  
ATOM   6045  CA  ASP B 297      45.292 -15.438  47.298  1.00138.98           C  
ANISOU 6045  CA  ASP B 297    12948  29305  10552   5596  -1573   -274       C  
ATOM   6046  C   ASP B 297      44.483 -16.383  48.178  1.00137.37           C  
ANISOU 6046  C   ASP B 297    13001  29019  10172   5925  -1456    176       C  
ATOM   6047  O   ASP B 297      44.325 -17.560  47.835  1.00136.93           O  
ANISOU 6047  O   ASP B 297    13001  28804  10221   6149  -1324    538       O  
ATOM   6048  CB  ASP B 297      46.757 -15.442  47.734  1.00140.66           C  
ANISOU 6048  CB  ASP B 297    12860  29858  10727   5691  -1836   -457       C  
ATOM   6049  CG  ASP B 297      47.650 -14.655  46.796  1.00145.47           C  
ANISOU 6049  CG  ASP B 297    13183  30530  11559   5377  -1925   -886       C  
ATOM   6050  OD1 ASP B 297      47.177 -14.270  45.705  1.00145.65           O  
ANISOU 6050  OD1 ASP B 297    13249  30317  11775   5121  -1776  -1007       O  
ATOM   6051  OD2 ASP B 297      48.826 -14.424  47.150  1.00153.13           O  
ANISOU 6051  OD2 ASP B 297    13886  31779  12518   5385  -2146  -1108       O  
ATOM   6052  N   LEU B 298      43.970 -15.897  49.310  1.00138.57           N  
ANISOU 6052  N   LEU B 298    13324  29254  10071   5954  -1485    162       N  
ATOM   6053  CA  LEU B 298      43.234 -16.763  50.225  1.00143.88           C  
ANISOU 6053  CA  LEU B 298    14247  29854  10567   6266  -1368    567       C  
ATOM   6054  C   LEU B 298      41.802 -17.024  49.774  1.00137.23           C  
ANISOU 6054  C   LEU B 298    13657  28649   9836   6210  -1073    815       C  
ATOM   6055  O   LEU B 298      41.278 -18.119  50.005  1.00141.23           O  
ANISOU 6055  O   LEU B 298    14323  29007  10329   6468   -908   1216       O  
ATOM   6056  CB  LEU B 298      43.226 -16.151  51.628  1.00132.75           C  
ANISOU 6056  CB  LEU B 298    12943  28654   8840   6322  -1512    462       C  
ATOM   6057  N   ALA B 299      41.157 -16.048  49.135  1.00135.85           N  
ANISOU 6057  N   ALA B 299    13526  28310   9782   5874   -999    585       N  
ATOM   6058  CA  ALA B 299      39.749 -16.163  48.778  1.00133.67           C  
ANISOU 6058  CA  ALA B 299    13485  27692   9613   5797   -743    790       C  
ATOM   6059  C   ALA B 299      39.510 -16.719  47.381  1.00131.13           C  
ANISOU 6059  C   ALA B 299    13140  27107   9575   5709   -603    915       C  
ATOM   6060  O   ALA B 299      38.363 -17.042  47.052  1.00129.95           O  
ANISOU 6060  O   ALA B 299    13184  26660   9532   5679   -389   1145       O  
ATOM   6061  CB  ALA B 299      39.066 -14.794  48.892  1.00132.65           C  
ANISOU 6061  CB  ALA B 299    13456  27482   9464   5486   -731    495       C  
ATOM   6062  N   LEU B 300      40.546 -16.845  46.556  1.00135.20           N  
ANISOU 6062  N   LEU B 300    13433  27712  10223   5664   -719    773       N  
ATOM   6063  CA  LEU B 300      40.329 -17.287  45.182  1.00133.57           C  
ANISOU 6063  CA  LEU B 300    13230  27239  10283   5560   -600    870       C  
ATOM   6064  C   LEU B 300      39.735 -18.688  45.092  1.00129.84           C  
ANISOU 6064  C   LEU B 300    12915  26528   9889   5819   -396   1374       C  
ATOM   6065  O   LEU B 300      38.828 -18.890  44.265  1.00127.45           O  
ANISOU 6065  O   LEU B 300    12766  25905   9754   5694   -222   1519       O  
ATOM   6066  CB  LEU B 300      41.646 -17.207  44.399  1.00130.84           C  
ANISOU 6066  CB  LEU B 300    12597  27041  10076   5494   -764    629       C  
ATOM   6067  CG  LEU B 300      41.491 -17.001  42.891  1.00132.61           C  
ANISOU 6067  CG  LEU B 300    12806  27018  10561   5240   -704    511       C  
ATOM   6068  CD1 LEU B 300      41.132 -15.552  42.587  1.00128.40           C  
ANISOU 6068  CD1 LEU B 300    12333  26453  10000   4850   -729     81       C  
ATOM   6069  CD2 LEU B 300      42.758 -17.405  42.156  1.00120.67           C  
ANISOU 6069  CD2 LEU B 300    11013  25542   9295   5271   -783    418       C  
ATOM   6070  N   PRO B 301      40.174 -19.677  45.876  1.00125.13           N  
ANISOU 6070  N   PRO B 301    12314  26043   9188   6160   -396   1648       N  
ATOM   6071  CA  PRO B 301      39.590 -21.022  45.736  1.00128.28           C  
ANISOU 6071  CA  PRO B 301    12890  26163   9689   6382   -164   2122       C  
ATOM   6072  C   PRO B 301      38.105 -21.072  46.043  1.00138.90           C  
ANISOU 6072  C   PRO B 301    14503  27256  11015   6336     62   2331       C  
ATOM   6073  O   PRO B 301      37.394 -21.912  45.477  1.00135.20           O  
ANISOU 6073  O   PRO B 301    14185  26461  10724   6363    282   2646       O  
ATOM   6074  CB  PRO B 301      40.400 -21.866  46.731  1.00120.89           C  
ANISOU 6074  CB  PRO B 301    11912  25435   8585   6745   -231   2304       C  
ATOM   6075  CG  PRO B 301      41.652 -21.087  46.979  1.00145.11           C  
ANISOU 6075  CG  PRO B 301    14710  28872  11553   6694   -527   1923       C  
ATOM   6076  CD  PRO B 301      41.259 -19.647  46.871  1.00141.55           C  
ANISOU 6076  CD  PRO B 301    14238  28483  11061   6351   -607   1537       C  
ATOM   6077  N   PHE B 302      37.611 -20.203  46.927  1.00141.88           N  
ANISOU 6077  N   PHE B 302    14946  27756  11205   6262     23   2166       N  
ATOM   6078  CA  PHE B 302      36.183 -20.194  47.227  1.00140.68           C  
ANISOU 6078  CA  PHE B 302    15028  27357  11068   6211    245   2349       C  
ATOM   6079  C   PHE B 302      35.383 -19.565  46.092  1.00136.51           C  
ANISOU 6079  C   PHE B 302    14542  26565  10761   5868    329   2218       C  
ATOM   6080  O   PHE B 302      34.311 -20.063  45.729  1.00134.39           O  
ANISOU 6080  O   PHE B 302    14437  25981  10646   5828    557   2475       O  
ATOM   6081  CB  PHE B 302      35.924 -19.442  48.532  1.00143.19           C  
ANISOU 6081  CB  PHE B 302    15414  27866  11125   6247    180   2216       C  
ATOM   6082  CG  PHE B 302      36.508 -20.106  49.745  1.00148.00           C  
ANISOU 6082  CG  PHE B 302    16053  28693  11486   6594    119   2382       C  
ATOM   6083  CD1 PHE B 302      37.816 -19.857  50.126  1.00150.78           C  
ANISOU 6083  CD1 PHE B 302    16221  29386  11683   6680   -147   2165       C  
ATOM   6084  CD2 PHE B 302      35.746 -20.973  50.510  1.00155.69           C  
ANISOU 6084  CD2 PHE B 302    17249  29522  12386   6827    330   2746       C  
ATOM   6085  CE1 PHE B 302      38.354 -20.465  51.246  1.00155.51           C  
ANISOU 6085  CE1 PHE B 302    16865  30179  12041   7003   -222   2315       C  
ATOM   6086  CE2 PHE B 302      36.279 -21.584  51.630  1.00154.64           C  
ANISOU 6086  CE2 PHE B 302    17179  29572  12005   7152    274   2894       C  
ATOM   6087  CZ  PHE B 302      37.584 -21.329  51.999  1.00157.41           C  
ANISOU 6087  CZ  PHE B 302    17354  30266  12189   7245    -13   2681       C  
ATOM   6088  N   ALA B 303      35.889 -18.471  45.517  1.00125.65           N  
ANISOU 6088  N   ALA B 303    13032  25300   9410   5609    156   1811       N  
ATOM   6089  CA  ALA B 303      35.186 -17.828  44.413  1.00119.36           C  
ANISOU 6089  CA  ALA B 303    12302  24241   8809   5277    229   1654       C  
ATOM   6090  C   ALA B 303      35.173 -18.708  43.169  1.00118.60           C  
ANISOU 6090  C   ALA B 303    12241  23886   8934   5253    337   1862       C  
ATOM   6091  O   ALA B 303      34.169 -18.757  42.449  1.00118.83           O  
ANISOU 6091  O   ALA B 303    12412  23497   9240   5039    517   1927       O  
ATOM   6092  CB  ALA B 303      35.827 -16.475  44.104  1.00115.70           C  
ANISOU 6092  CB  ALA B 303    11708  23933   8320   5005     32   1152       C  
ATOM   6093  N   ILE B 304      36.276 -19.410  42.898  1.00124.61           N  
ANISOU 6093  N   ILE B 304    12860  24714   9772   5400    252   1918       N  
ATOM   6094  CA  ILE B 304      36.308 -20.310  41.749  1.00122.69           C  
ANISOU 6094  CA  ILE B 304    12661  24025   9929   5318    404   2078       C  
ATOM   6095  C   ILE B 304      35.309 -21.442  41.931  1.00116.74           C  
ANISOU 6095  C   ILE B 304    12113  22993   9250   5470    653   2541       C  
ATOM   6096  O   ILE B 304      34.785 -21.983  40.949  1.00101.10           O  
ANISOU 6096  O   ILE B 304    10253  20546   7616   5298    825   2660       O  
ATOM   6097  CB  ILE B 304      37.738 -20.844  41.528  1.00123.57           C  
ANISOU 6097  CB  ILE B 304    12567  24293  10092   5487    280   2056       C  
ATOM   6098  CG1 ILE B 304      38.617 -19.746  40.923  1.00120.75           C  
ANISOU 6098  CG1 ILE B 304    12019  24047   9815   5218    103   1565       C  
ATOM   6099  CG2 ILE B 304      37.714 -22.080  40.634  1.00115.32           C  
ANISOU 6099  CG2 ILE B 304    11621  22809   9386   5518    483   2347       C  
ATOM   6100  CD1 ILE B 304      40.090 -20.091  40.860  1.00121.00           C  
ANISOU 6100  CD1 ILE B 304    11783  24316   9875   5386    -43   1490       C  
ATOM   6101  N   LEU B 305      35.023 -21.817  43.178  1.00113.56           N  
ANISOU 6101  N   LEU B 305    11771  22856   8522   5783    685   2802       N  
ATOM   6102  CA  LEU B 305      34.048 -22.871  43.425  1.00111.43           C  
ANISOU 6102  CA  LEU B 305    11705  22321   8311   5922    954   3239       C  
ATOM   6103  C   LEU B 305      32.626 -22.363  43.235  1.00114.46           C  
ANISOU 6103  C   LEU B 305    12225  22434   8833   5655   1118   3215       C  
ATOM   6104  O   LEU B 305      31.760 -23.111  42.767  1.00112.30           O  
ANISOU 6104  O   LEU B 305    12087  21758   8825   5578   1346   3468       O  
ATOM   6105  CB  LEU B 305      34.226 -23.434  44.835  1.00110.64           C  
ANISOU 6105  CB  LEU B 305    11629  22410   8000   6255    980   3421       C  
ATOM   6106  CG  LEU B 305      33.344 -24.633  45.187  1.00111.96           C  
ANISOU 6106  CG  LEU B 305    12005  22274   8261   6410   1279   3852       C  
ATOM   6107  CD1 LEU B 305      33.600 -25.791  44.235  1.00111.23           C  
ANISOU 6107  CD1 LEU B 305    11968  21883   8412   6456   1412   4117       C  
ATOM   6108  CD2 LEU B 305      33.577 -25.060  46.627  1.00116.37           C  
ANISOU 6108  CD2 LEU B 305    12611  23037   8566   6735   1289   3981       C  
ATOM   6109  N   LEU B 306      32.369 -21.101  43.586  1.00120.75           N  
ANISOU 6109  N   LEU B 306    12980  23429   9472   5509   1006   2908       N  
ATOM   6110  CA  LEU B 306      31.056 -20.521  43.331  1.00118.95           C  
ANISOU 6110  CA  LEU B 306    12853  22952   9391   5258   1148   2859       C  
ATOM   6111  C   LEU B 306      30.752 -20.501  41.839  1.00116.95           C  
ANISOU 6111  C   LEU B 306    12616  22229   9593   4912   1181   2740       C  
ATOM   6112  O   LEU B 306      29.594 -20.661  41.439  1.00115.51           O  
ANISOU 6112  O   LEU B 306    12532  21700   9656   4752   1350   2862       O  
ATOM   6113  CB  LEU B 306      30.988 -19.109  43.911  1.00120.22           C  
ANISOU 6113  CB  LEU B 306    12961  23349   9369   5141   1003   2494       C  
ATOM   6114  CG  LEU B 306      31.020 -19.017  45.439  1.00126.88           C  
ANISOU 6114  CG  LEU B 306    13818  24433   9958   5372    977   2540       C  
ATOM   6115  CD1 LEU B 306      31.146 -17.569  45.888  1.00122.10           C  
ANISOU 6115  CD1 LEU B 306    13164  24022   9207   5216    809   2137       C  
ATOM   6116  CD2 LEU B 306      29.787 -19.661  46.057  1.00123.36           C  
ANISOU 6116  CD2 LEU B 306    13532  23782   9558   5483   1249   2888       C  
ATOM   6117  N   GLY B 307      31.776 -20.304  41.006  1.00121.68           N  
ANISOU 6117  N   GLY B 307    13121  22804  10308   4792   1023   2498       N  
ATOM   6118  CA  GLY B 307      31.581 -20.420  39.571  1.00109.44           C  
ANISOU 6118  CA  GLY B 307    11634  20783   9166   4492   1063   2412       C  
ATOM   6119  C   GLY B 307      31.121 -21.807  39.166  1.00109.46           C  
ANISOU 6119  C   GLY B 307    11759  20415   9417   4551   1266   2803       C  
ATOM   6120  O   GLY B 307      30.189 -21.961  38.374  1.00116.64           O  
ANISOU 6120  O   GLY B 307    12784  20907  10627   4319   1373   2855       O  
ATOM   6121  N   PHE B 308      31.772 -22.839  39.709  1.00107.96           N  
ANISOU 6121  N   PHE B 308    11552  20367   9100   4867   1318   3081       N  
ATOM   6122  CA  PHE B 308      31.321 -24.203  39.460  1.00105.09           C  
ANISOU 6122  CA  PHE B 308    11333  19663   8935   4950   1542   3477       C  
ATOM   6123  C   PHE B 308      29.907 -24.423  39.977  1.00105.87           C  
ANISOU 6123  C   PHE B 308    11543  19627   9058   4938   1742   3715       C  
ATOM   6124  O   PHE B 308      29.163 -25.241  39.424  1.00103.52           O  
ANISOU 6124  O   PHE B 308    11372  18920   9041   4830   1928   3942       O  
ATOM   6125  CB  PHE B 308      32.271 -25.208  40.114  1.00106.70           C  
ANISOU 6125  CB  PHE B 308    11509  20087   8944   5342   1566   3741       C  
ATOM   6126  CG  PHE B 308      33.571 -25.388  39.383  1.00108.40           C  
ANISOU 6126  CG  PHE B 308    11625  20297   9264   5354   1449   3601       C  
ATOM   6127  CD1 PHE B 308      33.644 -26.201  38.263  1.00109.16           C  
ANISOU 6127  CD1 PHE B 308    11838  19942   9696   5228   1579   3708       C  
ATOM   6128  CD2 PHE B 308      34.725 -24.761  39.824  1.00110.98           C  
ANISOU 6128  CD2 PHE B 308    11742  21067   9359   5490   1218   3361       C  
ATOM   6129  CE1 PHE B 308      34.840 -26.376  37.590  1.00108.64           C  
ANISOU 6129  CE1 PHE B 308    11687  19852   9737   5246   1508   3584       C  
ATOM   6130  CE2 PHE B 308      35.925 -24.934  39.155  1.00111.38           C  
ANISOU 6130  CE2 PHE B 308    11670  21110   9537   5502   1133   3230       C  
ATOM   6131  CZ  PHE B 308      35.981 -25.742  38.037  1.00104.61           C  
ANISOU 6131  CZ  PHE B 308    10938  19789   9021   5386   1291   3346       C  
ATOM   6132  N   THR B 309      29.518 -23.706  41.035  1.00112.87           N  
ANISOU 6132  N   THR B 309    12385  20842   9658   5041   1719   3664       N  
ATOM   6133  CA  THR B 309      28.195 -23.907  41.614  1.00113.72           C  
ANISOU 6133  CA  THR B 309    12584  20838   9785   5051   1942   3895       C  
ATOM   6134  C   THR B 309      27.094 -23.440  40.671  1.00110.86           C  
ANISOU 6134  C   THR B 309    12239  20091   9792   4677   1982   3765       C  
ATOM   6135  O   THR B 309      25.994 -24.005  40.679  1.00111.24           O  
ANISOU 6135  O   THR B 309    12357  19870  10038   4620   2197   4007       O  
ATOM   6136  CB  THR B 309      28.086 -23.177  42.952  1.00115.80           C  
ANISOU 6136  CB  THR B 309    12817  21538   9641   5248   1915   3846       C  
ATOM   6137  OG1 THR B 309      29.176 -23.561  43.798  1.00118.67           O  
ANISOU 6137  OG1 THR B 309    13159  22252   9678   5586   1816   3925       O  
ATOM   6138  CG2 THR B 309      26.772 -23.525  43.639  1.00117.25           C  
ANISOU 6138  CG2 THR B 309    13106  21604   9841   5302   2200   4128       C  
ATOM   6139  N   ASN B 310      27.361 -22.415  39.857  1.00110.37           N  
ANISOU 6139  N   ASN B 310    12114  19992   9828   4421   1778   3386       N  
ATOM   6140  CA  ASN B 310      26.366 -21.976  38.887  1.00101.66           C  
ANISOU 6140  CA  ASN B 310    11043  18512   9070   4081   1781   3259       C  
ATOM   6141  C   ASN B 310      25.978 -23.093  37.932  1.00101.23           C  
ANISOU 6141  C   ASN B 310    11098  17981   9384   3945   1899   3481       C  
ATOM   6142  O   ASN B 310      24.873 -23.068  37.379  1.00102.68           O  
ANISOU 6142  O   ASN B 310    11315  17840   9859   3718   1957   3506       O  
ATOM   6143  CB  ASN B 310      26.891 -20.775  38.100  1.00105.48           C  
ANISOU 6143  CB  ASN B 310    11489  19012   9576   3850   1545   2820       C  
ATOM   6144  CG  ASN B 310      25.808 -20.095  37.280  1.00106.18           C  
ANISOU 6144  CG  ASN B 310    11617  18777   9949   3539   1519   2663       C  
ATOM   6145  OD1 ASN B 310      25.955 -19.909  36.071  1.00109.17           O  
ANISOU 6145  OD1 ASN B 310    12069  18853  10558   3294   1410   2481       O  
ATOM   6146  ND2 ASN B 310      24.708 -19.736  37.932  1.00104.87           N  
ANISOU 6146  ND2 ASN B 310    11414  18665   9769   3557   1623   2738       N  
ATOM   6147  N   SER B 311      26.858 -24.074  37.728  1.00103.30           N  
ANISOU 6147  N   SER B 311    11417  18192   9641   4080   1933   3640       N  
ATOM   6148  CA  SER B 311      26.485 -25.263  36.975  1.00104.70           C  
ANISOU 6148  CA  SER B 311    11731  17923  10127   3985   2086   3894       C  
ATOM   6149  C   SER B 311      25.540 -26.161  37.761  1.00103.77           C  
ANISOU 6149  C   SER B 311    11661  17739  10028   4123   2354   4280       C  
ATOM   6150  O   SER B 311      24.826 -26.968  37.158  1.00105.06           O  
ANISOU 6150  O   SER B 311    11927  17496  10495   3965   2496   4466       O  
ATOM   6151  CB  SER B 311      27.736 -26.041  36.571  1.00101.02           C  
ANISOU 6151  CB  SER B 311    11322  17422   9639   4114   2072   3957       C  
ATOM   6152  OG  SER B 311      28.627 -25.219  35.836  1.00 98.74           O  
ANISOU 6152  OG  SER B 311    10985  17179   9354   3976   1857   3595       O  
ATOM   6153  N   CYS B 312      25.524 -26.040  39.092  1.00104.43           N  
ANISOU 6153  N   CYS B 312    11689  18201   9787   4405   2434   4397       N  
ATOM   6154  CA  CYS B 312      24.571 -26.788  39.902  1.00104.27           C  
ANISOU 6154  CA  CYS B 312    11729  18119   9770   4531   2721   4747       C  
ATOM   6155  C   CYS B 312      23.214 -26.100  39.965  1.00105.94           C  
ANISOU 6155  C   CYS B 312    11865  18229  10157   4321   2784   4674       C  
ATOM   6156  O   CYS B 312      22.195 -26.768  40.172  1.00 92.85           O  
ANISOU 6156  O   CYS B 312    10245  16351   8685   4286   3034   4933       O  
ATOM   6157  CB  CYS B 312      25.117 -26.968  41.320  1.00111.84           C  
ANISOU 6157  CB  CYS B 312    12702  19507  10284   4939   2794   4915       C  
ATOM   6158  SG  CYS B 312      26.687 -27.855  41.416  1.00116.17           S  
ANISOU 6158  SG  CYS B 312    13312  20213  10614   5259   2726   5049       S  
ATOM   6159  N   VAL B 313      23.180 -24.780  39.785  1.00104.64           N  
ANISOU 6159  N   VAL B 313    11592  18216   9951   4180   2576   4326       N  
ATOM   6160  CA  VAL B 313      21.921 -24.046  39.825  1.00 95.16           C  
ANISOU 6160  CA  VAL B 313    10305  16929   8922   4000   2624   4241       C  
ATOM   6161  C   VAL B 313      21.249 -23.965  38.459  1.00 99.12           C  
ANISOU 6161  C   VAL B 313    10799  16993   9870   3635   2526   4120       C  
ATOM   6162  O   VAL B 313      20.023 -23.794  38.392  1.00 98.57           O  
ANISOU 6162  O   VAL B 313    10656  16746  10051   3483   2617   4159       O  
ATOM   6163  CB  VAL B 313      22.147 -22.627  40.379  1.00 95.00           C  
ANISOU 6163  CB  VAL B 313    10198  17283   8615   4047   2467   3933       C  
ATOM   6164  CG1 VAL B 313      20.823 -21.891  40.523  1.00 99.04           C  
ANISOU 6164  CG1 VAL B 313    10622  17716   9294   3906   2552   3873       C  
ATOM   6165  CG2 VAL B 313      22.882 -22.687  41.709  1.00103.06           C  
ANISOU 6165  CG2 VAL B 313    11247  18746   9164   4404   2519   4032       C  
ATOM   6166  N   ASN B 314      22.011 -24.083  37.372  1.00102.13           N  
ANISOU 6166  N   ASN B 314    11256  17191  10357   3493   2344   3974       N  
ATOM   6167  CA  ASN B 314      21.411 -24.010  36.043  1.00104.14           C  
ANISOU 6167  CA  ASN B 314    11550  17016  11004   3149   2229   3853       C  
ATOM   6168  C   ASN B 314      20.328 -25.059  35.831  1.00106.30           C  
ANISOU 6168  C   ASN B 314    11850  16927  11613   3033   2429   4150       C  
ATOM   6169  O   ASN B 314      19.273 -24.712  35.269  1.00105.49           O  
ANISOU 6169  O   ASN B 314    11684  16584  11813   2789   2373   4074       O  
ATOM   6170  CB  ASN B 314      22.504 -24.143  34.976  1.00 99.89           C  
ANISOU 6170  CB  ASN B 314    11141  16320  10493   3048   2054   3690       C  
ATOM   6171  CG  ASN B 314      23.384 -22.912  34.885  1.00 98.51           C  
ANISOU 6171  CG  ASN B 314    10926  16414  10090   3050   1830   3319       C  
ATOM   6172  OD1 ASN B 314      22.966 -21.808  35.236  1.00 99.55           O  
ANISOU 6172  OD1 ASN B 314    10963  16730  10132   3020   1753   3122       O  
ATOM   6173  ND2 ASN B 314      24.614 -23.097  34.417  1.00 96.13           N  
ANISOU 6173  ND2 ASN B 314    10697  16126   9701   3082   1744   3219       N  
ATOM   6174  N   PRO B 315      20.507 -26.321  36.229  1.00110.94           N  
ANISOU 6174  N   PRO B 315    12525  17450  12175   3189   2656   4479       N  
ATOM   6175  CA  PRO B 315      19.416 -27.297  36.071  1.00118.72           C  
ANISOU 6175  CA  PRO B 315    13533  18085  13490   3054   2871   4752       C  
ATOM   6176  C   PRO B 315      18.099 -26.844  36.677  1.00124.07           C  
ANISOU 6176  C   PRO B 315    14032  18806  14302   3005   2996   4792       C  
ATOM   6177  O   PRO B 315      17.039 -27.048  36.073  1.00123.67           O  
ANISOU 6177  O   PRO B 315    13924  18429  14637   2745   3013   4824       O  
ATOM   6178  CB  PRO B 315      19.968 -28.543  36.779  1.00120.70           C  
ANISOU 6178  CB  PRO B 315    13912  18386  13561   3327   3133   5095       C  
ATOM   6179  CG  PRO B 315      21.442 -28.418  36.653  1.00120.28           C  
ANISOU 6179  CG  PRO B 315    13936  18536  13228   3497   2970   4970       C  
ATOM   6180  CD  PRO B 315      21.737 -26.946  36.748  1.00116.00           C  
ANISOU 6180  CD  PRO B 315    13259  18306  12510   3482   2718   4612       C  
ATOM   6181  N   PHE B 316      18.136 -26.228  37.861  1.00111.15           N  
ANISOU 6181  N   PHE B 316    12307  17564  12361   3247   3083   4788       N  
ATOM   6182  CA  PHE B 316      16.901 -25.800  38.504  1.00112.61           C  
ANISOU 6182  CA  PHE B 316    12328  17792  12666   3224   3246   4837       C  
ATOM   6183  C   PHE B 316      16.261 -24.623  37.777  1.00109.77           C  
ANISOU 6183  C   PHE B 316    11825  17353  12530   2977   3004   4526       C  
ATOM   6184  O   PHE B 316      15.033 -24.483  37.786  1.00110.61           O  
ANISOU 6184  O   PHE B 316    11778  17314  12936   2843   3100   4570       O  
ATOM   6185  CB  PHE B 316      17.175 -25.393  39.953  1.00114.33           C  
ANISOU 6185  CB  PHE B 316    12534  18447  12458   3556   3400   4896       C  
ATOM   6186  CG  PHE B 316      17.692 -26.505  40.822  1.00113.02           C  
ANISOU 6186  CG  PHE B 316    12520  18380  12041   3843   3654   5224       C  
ATOM   6187  CD1 PHE B 316      17.237 -27.804  40.673  1.00121.16           C  
ANISOU 6187  CD1 PHE B 316    13633  19090  13311   3793   3903   5534       C  
ATOM   6188  CD2 PHE B 316      18.637 -26.241  41.800  1.00111.73           C  
ANISOU 6188  CD2 PHE B 316    12431  18629  11392   4166   3638   5218       C  
ATOM   6189  CE1 PHE B 316      17.717 -28.818  41.482  1.00122.32           C  
ANISOU 6189  CE1 PHE B 316    13952  19316  13209   4078   4149   5842       C  
ATOM   6190  CE2 PHE B 316      19.120 -27.248  42.610  1.00114.43           C  
ANISOU 6190  CE2 PHE B 316    12930  19065  11482   4458   3851   5525       C  
ATOM   6191  CZ  PHE B 316      18.661 -28.538  42.451  1.00116.09           C  
ANISOU 6191  CZ  PHE B 316    13240  18942  11927   4423   4117   5843       C  
ATOM   6192  N   LEU B 317      17.071 -23.774  37.146  1.00101.89           N  
ANISOU 6192  N   LEU B 317    10875  16440  11399   2919   2700   4214       N  
ATOM   6193  CA  LEU B 317      16.590 -22.501  36.626  1.00101.02           C  
ANISOU 6193  CA  LEU B 317    10663  16316  11403   2748   2477   3903       C  
ATOM   6194  C   LEU B 317      15.991 -22.580  35.230  1.00102.61           C  
ANISOU 6194  C   LEU B 317    10875  16086  12027   2417   2283   3805       C  
ATOM   6195  O   LEU B 317      15.144 -21.746  34.890  1.00107.34           O  
ANISOU 6195  O   LEU B 317    11353  16606  12823   2275   2163   3643       O  
ATOM   6196  CB  LEU B 317      17.730 -21.477  36.612  1.00105.05           C  
ANISOU 6196  CB  LEU B 317    11241  17112  11561   2829   2256   3592       C  
ATOM   6197  CG  LEU B 317      18.093 -20.858  37.961  1.00107.36           C  
ANISOU 6197  CG  LEU B 317    11490  17867  11436   3109   2362   3568       C  
ATOM   6198  CD1 LEU B 317      19.363 -20.035  37.838  1.00102.94           C  
ANISOU 6198  CD1 LEU B 317    11002  17559  10552   3157   2132   3264       C  
ATOM   6199  CD2 LEU B 317      16.950 -20.002  38.484  1.00118.44           C  
ANISOU 6199  CD2 LEU B 317    12747  19341  12916   3099   2455   3517       C  
ATOM   6200  N   TYR B 318      16.407 -23.538  34.407  1.00104.16           N  
ANISOU 6200  N   TYR B 318    11226  15994  12355   2297   2240   3895       N  
ATOM   6201  CA  TYR B 318      16.000 -23.522  33.007  1.00105.41           C  
ANISOU 6201  CA  TYR B 318    11451  15745  12853   1980   2006   3758       C  
ATOM   6202  C   TYR B 318      15.295 -24.796  32.552  1.00112.18           C  
ANISOU 6202  C   TYR B 318    12337  16220  14065   1809   2125   4017       C  
ATOM   6203  O   TYR B 318      14.541 -24.774  31.578  1.00130.17           O  
ANISOU 6203  O   TYR B 318    14609  18167  16683   1536   1954   3940       O  
ATOM   6204  CB  TYR B 318      17.226 -23.279  32.119  1.00100.77           C  
ANISOU 6204  CB  TYR B 318    11083  15098  12108   1925   1779   3531       C  
ATOM   6205  CG  TYR B 318      18.031 -22.059  32.504  1.00 98.48           C  
ANISOU 6205  CG  TYR B 318    10777  15169  11471   2065   1662   3254       C  
ATOM   6206  CD1 TYR B 318      17.629 -20.787  32.122  1.00 99.20           C  
ANISOU 6206  CD1 TYR B 318    10824  15270  11599   1950   1460   2963       C  
ATOM   6207  CD2 TYR B 318      19.199 -22.182  33.245  1.00 97.72           C  
ANISOU 6207  CD2 TYR B 318    10716  15401  11014   2312   1747   3281       C  
ATOM   6208  CE1 TYR B 318      18.364 -19.671  32.472  1.00 98.92           C  
ANISOU 6208  CE1 TYR B 318    10792  15547  11245   2058   1370   2701       C  
ATOM   6209  CE2 TYR B 318      19.941 -21.072  33.599  1.00 98.20           C  
ANISOU 6209  CE2 TYR B 318    10754  15793  10766   2416   1633   3013       C  
ATOM   6210  CZ  TYR B 318      19.519 -19.820  33.210  1.00 96.33           C  
ANISOU 6210  CZ  TYR B 318    10487  15545  10569   2278   1456   2720       C  
ATOM   6211  OH  TYR B 318      20.256 -18.713  33.561  1.00101.64           O  
ANISOU 6211  OH  TYR B 318    11155  16532  10933   2363   1359   2444       O  
HETATM 6212  N   YCM B 319      15.531 -25.901  33.248  1.00120.87           N  
ANISOU 6212  N   YCM B 319    13096  17690  15141    442   3329   3051       N  
HETATM 6213  CA  YCM B 319      14.966 -27.166  32.843  1.00125.03           C  
ANISOU 6213  CA  YCM B 319    13799  17967  15739    640   3226   3044       C  
HETATM 6214  CB  YCM B 319      15.965 -28.311  33.043  1.00127.11           C  
ANISOU 6214  CB  YCM B 319    14079  18476  15742    807   3387   3277       C  
HETATM 6215  SG  YCM B 319      15.311 -29.941  32.875  1.00101.58           S  
ANISOU 6215  SG  YCM B 319    10996  14999  12600   1014   3301   3280       S  
HETATM 6216  CD  YCM B 319      15.653 -30.423  31.204  1.00114.92           C  
ANISOU 6216  CD  YCM B 319    13071  16470  14124   1341   3167   3365       C  
HETATM 6217  CE  YCM B 319      14.424 -30.613  30.352  1.00125.41           C  
ANISOU 6217  CE  YCM B 319    14613  17341  15697   1434   2917   3183       C  
HETATM 6218  OZ1 YCM B 319      13.333 -30.942  30.867  1.00122.08           O  
ANISOU 6218  OZ1 YCM B 319    14116  16727  15541   1347   2835   3033       O  
HETATM 6219  NZ2 YCM B 319      14.528 -30.420  28.999  1.00128.98           N  
ANISOU 6219  NZ2 YCM B 319    15342  17593  16073   1616   2780   3187       N  
HETATM 6220  C   YCM B 319      13.669 -27.542  33.550  1.00122.54           C  
ANISOU 6220  C   YCM B 319    13375  17443  15743    522   3141   2864       C  
HETATM 6221  O   YCM B 319      12.714 -28.080  32.982  1.00125.71           O  
ANISOU 6221  O   YCM B 319    13947  17494  16325    630   2962   2749       O  
ATOM   6222  N   PHE B 320      13.640 -27.242  34.843  1.00125.92           N  
ANISOU 6222  N   PHE B 320    13506  18097  16240    291   3275   2839       N  
ATOM   6223  CA  PHE B 320      12.532 -27.654  35.695  1.00125.62           C  
ANISOU 6223  CA  PHE B 320    13328  17922  16481    167   3230   2693       C  
ATOM   6224  C   PHE B 320      11.446 -26.589  35.712  1.00125.23           C  
ANISOU 6224  C   PHE B 320    13221  17643  16718    -26   3082   2451       C  
ATOM   6225  O   PHE B 320      10.261 -26.902  35.827  1.00125.15           O  
ANISOU 6225  O   PHE B 320    13222  17351  16978    -59   2947   2286       O  
ATOM   6226  CB  PHE B 320      13.032 -27.932  37.111  1.00125.29           C  
ANISOU 6226  CB  PHE B 320    12993  18241  16372     20   3452   2790       C  
ATOM   6227  CG  PHE B 320      14.123 -28.966  37.172  1.00129.20           C  
ANISOU 6227  CG  PHE B 320    13525  18981  16583    198   3609   3030       C  
ATOM   6228  CD1 PHE B 320      14.272 -29.903  36.161  1.00129.10           C  
ANISOU 6228  CD1 PHE B 320    13787  18799  16464    474   3527   3115       C  
ATOM   6229  CD2 PHE B 320      15.009 -28.993  38.234  1.00125.50           C  
ANISOU 6229  CD2 PHE B 320    12818  18914  15951     88   3838   3170       C  
ATOM   6230  CE1 PHE B 320      15.280 -30.847  36.212  1.00126.56           C  
ANISOU 6230  CE1 PHE B 320    13502  18704  15882    638   3671   3335       C  
ATOM   6231  CE2 PHE B 320      16.019 -29.936  38.291  1.00125.74           C  
ANISOU 6231  CE2 PHE B 320    12883  19173  15720    251   3983   3391       C  
ATOM   6232  CZ  PHE B 320      16.153 -30.863  37.279  1.00126.31           C  
ANISOU 6232  CZ  PHE B 320    13230  19073  15690    525   3899   3474       C  
ATOM   6233  N   VAL B 321      11.855 -25.326  35.590  1.00146.02           N  
ANISOU 6233  N   VAL B 321    15794  20395  19292   -152   3107   2431       N  
ATOM   6234  CA  VAL B 321      10.912 -24.219  35.513  1.00147.41           C  
ANISOU 6234  CA  VAL B 321    15930  20361  19719   -329   2966   2209       C  
ATOM   6235  C   VAL B 321      10.717 -23.750  34.076  1.00144.84           C  
ANISOU 6235  C   VAL B 321    15884  19752  19395   -190   2779   2148       C  
ATOM   6236  O   VAL B 321      10.106 -22.702  33.846  1.00144.06           O  
ANISOU 6236  O   VAL B 321    15777  19497  19463   -321   2664   1982       O  
ATOM   6237  CB  VAL B 321      11.360 -23.049  36.405  1.00157.21           C  
ANISOU 6237  CB  VAL B 321    16899  21904  20932   -590   3106   2201       C  
ATOM   6238  CG1 VAL B 321      11.777 -23.553  37.781  1.00161.15           C  
ANISOU 6238  CG1 VAL B 321    17128  22728  21372   -704   3314   2299       C  
ATOM   6239  CG2 VAL B 321      12.483 -22.272  35.739  1.00150.89           C  
ANISOU 6239  CG2 VAL B 321    16174  21286  19870   -540   3167   2327       C  
ATOM   6240  N   GLY B 322      11.220 -24.508  33.100  1.00149.48           N  
ANISOU 6240  N   GLY B 322    16724  20271  19802     76   2746   2278       N  
ATOM   6241  CA  GLY B 322      10.995 -24.149  31.711  1.00149.82           C  
ANISOU 6241  CA  GLY B 322    17046  20029  19852    223   2562   2219       C  
ATOM   6242  C   GLY B 322       9.577 -24.457  31.273  1.00149.88           C  
ANISOU 6242  C   GLY B 322    17187  19602  20160    260   2336   2016       C  
ATOM   6243  O   GLY B 322       8.968 -23.693  30.518  1.00149.87           O  
ANISOU 6243  O   GLY B 322    17308  19344  20293    242   2167   1869       O  
ATOM   6244  N   ASN B 323       9.033 -25.582  31.742  1.00137.28           N  
ANISOU 6244  N   ASN B 323    15569  17917  18674    311   2329   2004       N  
ATOM   6245  CA  ASN B 323       7.656 -25.932  31.418  1.00142.66           C  
ANISOU 6245  CA  ASN B 323    16362  18192  19652    338   2120   1810       C  
ATOM   6246  C   ASN B 323       6.680 -24.974  32.086  1.00143.13           C  
ANISOU 6246  C   ASN B 323    16229  18157  19995     68   2058   1594       C  
ATOM   6247  O   ASN B 323       5.655 -24.610  31.497  1.00146.84           O  
ANISOU 6247  O   ASN B 323    16818  18284  20692     58   1859   1408       O  
ATOM   6248  CB  ASN B 323       7.379 -27.371  31.853  1.00154.35           C  
ANISOU 6248  CB  ASN B 323    17844  19632  21171    448   2146   1862       C  
ATOM   6249  CG  ASN B 323       8.191 -28.383  31.069  1.00148.98           C  
ANISOU 6249  CG  ASN B 323    17386  18982  20237    735   2173   2056       C  
ATOM   6250  OD1 ASN B 323       8.993 -28.020  30.209  1.00153.36           O  
ANISOU 6250  OD1 ASN B 323    18092  19598  20579    854   2179   2157       O  
ATOM   6251  ND2 ASN B 323       8.000 -29.661  31.377  1.00152.29           N  
ANISOU 6251  ND2 ASN B 323    17823  19366  20675    846   2194   2111       N  
ATOM   6252  N   ARG B 324       6.982 -24.551  33.316  1.00134.15           N  
ANISOU 6252  N   ARG B 324    14797  17322  18851   -153   2227   1614       N  
ATOM   6253  CA  ARG B 324       6.112 -23.630  34.032  1.00132.09           C  
ANISOU 6253  CA  ARG B 324    14336  17002  18851   -419   2185   1416       C  
ATOM   6254  C   ARG B 324       6.239 -22.198  33.531  1.00123.70           C  
ANISOU 6254  C   ARG B 324    13288  15929  17784   -525   2130   1339       C  
ATOM   6255  O   ARG B 324       5.305 -21.408  33.706  1.00125.60           O  
ANISOU 6255  O   ARG B 324    13453  15995  18272   -697   2021   1140       O  
ATOM   6256  CB  ARG B 324       6.413 -23.656  35.531  1.00131.34           C  
ANISOU 6256  CB  ARG B 324    13915  17242  18745   -619   2387   1465       C  
ATOM   6257  CG  ARG B 324       5.970 -24.925  36.238  1.00140.48           C  
ANISOU 6257  CG  ARG B 324    15008  18375  19995   -579   2423   1482       C  
ATOM   6258  CD  ARG B 324       6.388 -24.904  37.701  1.00137.98           C  
ANISOU 6258  CD  ARG B 324    14369  18417  19639   -774   2636   1547       C  
ATOM   6259  NE  ARG B 324       5.770 -23.787  38.415  1.00137.39           N  
ANISOU 6259  NE  ARG B 324    14078  18352  19771  -1050   2623   1375       N  
ATOM   6260  CZ  ARG B 324       6.399 -22.679  38.805  1.00131.35           C  
ANISOU 6260  CZ  ARG B 324    13152  17846  18910  -1219   2732   1397       C  
ATOM   6261  NH1 ARG B 324       7.692 -22.504  38.562  1.00122.23           N  
ANISOU 6261  NH1 ARG B 324    12020  16969  17451  -1146   2867   1587       N  
ATOM   6262  NH2 ARG B 324       5.721 -21.737  39.447  1.00122.54           N  
ANISOU 6262  NH2 ARG B 324    11847  16706  18005  -1464   2704   1227       N  
ATOM   6263  N   PHE B 325       7.370 -21.846  32.918  1.00131.39           N  
ANISOU 6263  N   PHE B 325    14356  17085  18482   -427   2204   1494       N  
ATOM   6264  CA  PHE B 325       7.560 -20.482  32.437  1.00133.52           C  
ANISOU 6264  CA  PHE B 325    14639  17361  18732   -525   2160   1434       C  
ATOM   6265  C   PHE B 325       6.601 -20.178  31.295  1.00132.45           C  
ANISOU 6265  C   PHE B 325    14743  16801  18782   -443   1910   1262       C  
ATOM   6266  O   PHE B 325       5.792 -19.248  31.378  1.00130.35           O  
ANISOU 6266  O   PHE B 325    14411  16379  18736   -615   1805   1073       O  
ATOM   6267  CB  PHE B 325       9.015 -20.291  31.998  1.00133.95           C  
ANISOU 6267  CB  PHE B 325    14755  17703  18439   -416   2296   1652       C  
ATOM   6268  CG  PHE B 325       9.425 -18.853  31.844  1.00135.85           C  
ANISOU 6268  CG  PHE B 325    14929  18061  18626   -562   2315   1622       C  
ATOM   6269  CD1 PHE B 325       9.737 -18.085  32.954  1.00131.26           C  
ANISOU 6269  CD1 PHE B 325    14057  17773  18045   -809   2464   1619       C  
ATOM   6270  CD2 PHE B 325       9.521 -18.276  30.591  1.00124.08           C  
ANISOU 6270  CD2 PHE B 325    13669  16395  17081   -448   2185   1601       C  
ATOM   6271  CE1 PHE B 325      10.122 -16.765  32.817  1.00123.20           C  
ANISOU 6271  CE1 PHE B 325    12974  16861  16975   -942   2482   1593       C  
ATOM   6272  CE2 PHE B 325       9.907 -16.957  30.448  1.00128.74           C  
ANISOU 6272  CE2 PHE B 325    14198  17094  17621   -581   2202   1576       C  
ATOM   6273  CZ  PHE B 325      10.207 -16.201  31.562  1.00120.93           C  
ANISOU 6273  CZ  PHE B 325    12917  16395  16636   -829   2350   1572       C  
ATOM   6274  N   GLN B 326       6.653 -20.979  30.229  1.00127.14           N  
ANISOU 6274  N   GLN B 326    14350  15930  18027   -180   1810   1324       N  
ATOM   6275  CA  GLN B 326       5.778 -20.742  29.086  1.00127.04           C  
ANISOU 6275  CA  GLN B 326    14581  15512  18178    -84   1571   1171       C  
ATOM   6276  C   GLN B 326       4.311 -20.770  29.491  1.00128.83           C  
ANISOU 6276  C   GLN B 326    14742  15446  18760   -210   1427    940       C  
ATOM   6277  O   GLN B 326       3.493 -20.055  28.902  1.00127.35           O  
ANISOU 6277  O   GLN B 326    14648  14978  18762   -255   1250    763       O  
ATOM   6278  CB  GLN B 326       6.061 -21.769  27.991  1.00129.50           C  
ANISOU 6278  CB  GLN B 326    15189  15670  18344    226   1498   1283       C  
ATOM   6279  CG  GLN B 326       7.483 -21.695  27.464  1.00131.95           C  
ANISOU 6279  CG  GLN B 326    15588  16243  18305    363   1623   1504       C  
ATOM   6280  CD  GLN B 326       7.731 -20.430  26.661  1.00137.65           C  
ANISOU 6280  CD  GLN B 326    16397  16927  18976    329   1555   1462       C  
ATOM   6281  OE1 GLN B 326       6.821 -19.900  26.022  1.00138.00           O  
ANISOU 6281  OE1 GLN B 326    16559  16654  19222    311   1363   1283       O  
ATOM   6282  NE2 GLN B 326       8.960 -19.929  26.706  1.00139.45           N  
ANISOU 6282  NE2 GLN B 326    16564  17482  18937    315   1713   1625       N  
ATOM   6283  N   GLN B 327       3.956 -21.587  30.484  1.00134.49           N  
ANISOU 6283  N   GLN B 327    15303  16223  19576   -267   1498    938       N  
ATOM   6284  CA  GLN B 327       2.561 -21.661  30.904  1.00135.24           C  
ANISOU 6284  CA  GLN B 327    15332  16045  20010   -386   1366    724       C  
ATOM   6285  C   GLN B 327       2.107 -20.347  31.528  1.00138.11           C  
ANISOU 6285  C   GLN B 327    15483  16448  20545   -669   1362    565       C  
ATOM   6286  O   GLN B 327       1.022 -19.842  31.216  1.00146.12           O  
ANISOU 6286  O   GLN B 327    16547  17157  21814   -741   1184    360       O  
ATOM   6287  CB  GLN B 327       2.370 -22.815  31.888  1.00130.55           C  
ANISOU 6287  CB  GLN B 327    14600  15538  19464   -389   1462    772       C  
ATOM   6288  CG  GLN B 327       0.946 -22.947  32.390  1.00156.75           C  
ANISOU 6288  CG  GLN B 327    17838  18590  23132   -514   1336    558       C  
ATOM   6289  CD  GLN B 327      -0.049 -23.142  31.265  1.00159.85           C  
ANISOU 6289  CD  GLN B 327    18498  18534  23705   -371   1087    414       C  
ATOM   6290  OE1 GLN B 327       0.172 -23.942  30.356  1.00163.35           O  
ANISOU 6290  OE1 GLN B 327    19184  18845  24035   -124   1023    500       O  
ATOM   6291  NE2 GLN B 327      -1.143 -22.391  31.307  1.00166.19           N  
ANISOU 6291  NE2 GLN B 327    19259  19100  24788   -527    944    192       N  
ATOM   6292  N   LYS B 328       2.924 -19.776  32.413  1.00156.00           N  
ANISOU 6292  N   LYS B 328    17512  19088  22675   -834   1557    655       N  
ATOM   6293  CA  LYS B 328       2.563 -18.529  33.073  1.00162.17           C  
ANISOU 6293  CA  LYS B 328    18076  19934  23605  -1108   1568    514       C  
ATOM   6294  C   LYS B 328       2.743 -17.319  32.169  1.00161.27           C  
ANISOU 6294  C   LYS B 328    18078  19745  23452  -1125   1478    461       C  
ATOM   6295  O   LYS B 328       2.227 -16.243  32.491  1.00165.50           O  
ANISOU 6295  O   LYS B 328    18483  20244  24155  -1336   1433    307       O  
ATOM   6296  CB  LYS B 328       3.381 -18.347  34.353  1.00169.24           C  
ANISOU 6296  CB  LYS B 328    18674  21261  24369  -1279   1809    630       C  
ATOM   6297  CG  LYS B 328       3.097 -19.404  35.409  1.00164.16           C  
ANISOU 6297  CG  LYS B 328    17875  20700  23800  -1308   1901    657       C  
ATOM   6298  CD  LYS B 328       3.723 -19.047  36.747  1.00156.67           C  
ANISOU 6298  CD  LYS B 328    16608  20150  22770  -1518   2122    731       C  
ATOM   6299  CE  LYS B 328       3.565 -20.179  37.752  1.00150.12           C  
ANISOU 6299  CE  LYS B 328    15635  19423  21980  -1524   2226    783       C  
ATOM   6300  NZ  LYS B 328       2.142 -20.457  38.091  1.00128.36           N  
ANISOU 6300  NZ  LYS B 328    12842  16370  19558  -1604   2086    581       N  
ATOM   6301  N   LEU B 329       3.459 -17.465  31.052  1.00142.32           N  
ANISOU 6301  N   LEU B 329    15917  17321  20837   -909   1450    585       N  
ATOM   6302  CA  LEU B 329       3.524 -16.388  30.073  1.00142.11           C  
ANISOU 6302  CA  LEU B 329    16031  17174  20791   -903   1339    524       C  
ATOM   6303  C   LEU B 329       2.247 -16.322  29.246  1.00143.38           C  
ANISOU 6303  C   LEU B 329    16384  16879  21214   -851   1085    318       C  
ATOM   6304  O   LEU B 329       1.716 -15.233  29.004  1.00143.70           O  
ANISOU 6304  O   LEU B 329    16415  16781  21404   -983    977    162       O  
ATOM   6305  CB  LEU B 329       4.721 -16.591  29.146  1.00142.52           C  
ANISOU 6305  CB  LEU B 329    16278  17352  20521   -684   1394    729       C  
ATOM   6306  CG  LEU B 329       6.121 -16.590  29.756  1.00142.48           C  
ANISOU 6306  CG  LEU B 329    16121  17797  20218   -707   1639    951       C  
ATOM   6307  CD1 LEU B 329       7.135 -16.985  28.689  1.00143.05           C  
ANISOU 6307  CD1 LEU B 329    16432  17922  19998   -450   1659   1140       C  
ATOM   6308  CD2 LEU B 329       6.462 -15.243  30.359  1.00142.00           C  
ANISOU 6308  CD2 LEU B 329    15839  17966  20150   -955   1731    915       C  
ATOM   6309  N   ARG B 330       1.745 -17.477  28.801  1.00139.18           N  
ANISOU 6309  N   ARG B 330    16028  16109  20743   -660    986    315       N  
ATOM   6310  CA  ARG B 330       0.478 -17.499  28.084  1.00132.20           C  
ANISOU 6310  CA  ARG B 330    15318  14789  20123   -612    745    116       C  
ATOM   6311  C   ARG B 330      -0.698 -17.190  29.005  1.00133.27           C  
ANISOU 6311  C   ARG B 330    15252  14805  20579   -843    692    -90       C  
ATOM   6312  O   ARG B 330      -1.781 -16.849  28.518  1.00137.34           O  
ANISOU 6312  O   ARG B 330    15866  14981  21337   -867    496   -284       O  
ATOM   6313  CB  ARG B 330       0.257 -18.853  27.407  1.00136.36           C  
ANISOU 6313  CB  ARG B 330    16080  15100  20631   -346    658    171       C  
ATOM   6314  CG  ARG B 330       1.303 -19.194  26.355  1.00141.36           C  
ANISOU 6314  CG  ARG B 330    16948  15798  20966    -96    681    359       C  
ATOM   6315  CD  ARG B 330       1.141 -20.617  25.841  1.00138.08           C  
ANISOU 6315  CD  ARG B 330    16736  15207  20523    158    618    426       C  
ATOM   6316  NE  ARG B 330      -0.189 -20.783  25.255  1.00136.38           N  
ANISOU 6316  NE  ARG B 330    16675  14555  20587    203    384    226       N  
ATOM   6317  CZ  ARG B 330      -0.761 -21.948  24.966  1.00132.50           C  
ANISOU 6317  CZ  ARG B 330    16328  13834  20182    371    289    212       C  
ATOM   6318  NH1 ARG B 330      -1.973 -21.966  24.427  1.00135.33           N  
ANISOU 6318  NH1 ARG B 330    16821  13798  20801    395     73     21       N  
ATOM   6319  NH2 ARG B 330      -0.133 -23.090  25.213  1.00131.96           N  
ANISOU 6319  NH2 ARG B 330    16271  13926  19943    513    407    387       N  
ATOM   6320  N   SER B 331      -0.505 -17.304  30.321  1.00137.60           N  
ANISOU 6320  N   SER B 331    15522  15627  21133  -1012    861    -52       N  
ATOM   6321  CA  SER B 331      -1.586 -17.061  31.269  1.00137.68           C  
ANISOU 6321  CA  SER B 331    15327  15546  21440  -1233    824   -238       C  
ATOM   6322  C   SER B 331      -1.877 -15.573  31.429  1.00137.28           C  
ANISOU 6322  C   SER B 331    15151  15498  21509  -1462    786   -385       C  
ATOM   6323  O   SER B 331      -3.034 -15.148  31.335  1.00137.50           O  
ANISOU 6323  O   SER B 331    15189  15240  21815  -1558    623   -596       O  
ATOM   6324  CB  SER B 331      -1.227 -17.681  32.622  1.00137.85           C  
ANISOU 6324  CB  SER B 331    15091  15873  21413  -1332   1025   -139       C  
ATOM   6325  OG  SER B 331      -2.208 -17.394  33.602  1.00137.89           O  
ANISOU 6325  OG  SER B 331    14880  15819  21693  -1557   1004   -312       O  
ATOM   6326  N   VAL B 332      -0.840 -14.763  31.668  1.00131.05           N  
ANISOU 6326  N   VAL B 332    14246  15031  20516  -1553    934   -276       N  
ATOM   6327  CA  VAL B 332      -1.031 -13.323  31.824  1.00132.77           C  
ANISOU 6327  CA  VAL B 332    14342  15274  20830  -1771    908   -404       C  
ATOM   6328  C   VAL B 332      -1.238 -12.599  30.504  1.00134.25           C  
ANISOU 6328  C   VAL B 332    14770  15202  21036  -1683    729   -484       C  
ATOM   6329  O   VAL B 332      -1.476 -11.384  30.511  1.00137.51           O  
ANISOU 6329  O   VAL B 332    15108  15596  21544  -1853    683   -604       O  
ATOM   6330  CB  VAL B 332       0.167 -12.677  32.553  1.00135.20           C  
ANISOU 6330  CB  VAL B 332    14435  16023  20912  -1903   1130   -259       C  
ATOM   6331  CG1 VAL B 332       0.393 -13.346  33.903  1.00134.29           C  
ANISOU 6331  CG1 VAL B 332    14069  16178  20775  -2001   1314   -179       C  
ATOM   6332  CG2 VAL B 332       1.424 -12.748  31.694  1.00138.66           C  
ANISOU 6332  CG2 VAL B 332    15044  16616  21024  -1711   1199    -54       C  
ATOM   6333  N   PHE B 333      -1.160 -13.298  29.374  1.00142.22           N  
ANISOU 6333  N   PHE B 333    16066  16012  21959  -1424    626   -424       N  
ATOM   6334  CA  PHE B 333      -1.347 -12.666  28.070  1.00151.71           C  
ANISOU 6334  CA  PHE B 333    17511  16960  23172  -1325    452   -495       C  
ATOM   6335  C   PHE B 333      -0.371 -11.505  27.896  1.00152.79           C  
ANISOU 6335  C   PHE B 333    17597  17342  23115  -1404    543   -417       C  
ATOM   6336  O   PHE B 333       0.686 -11.468  28.526  1.00150.65           O  
ANISOU 6336  O   PHE B 333    17172  17441  22627  -1451    746   -252       O  
ATOM   6337  CB  PHE B 333      -2.786 -12.167  27.899  1.00154.15           C  
ANISOU 6337  CB  PHE B 333    17845  16901  23822  -1433    243   -757       C  
ATOM   6338  CG  PHE B 333      -3.816 -13.265  27.800  1.00146.35           C  
ANISOU 6338  CG  PHE B 333    16963  15609  23034  -1324    114   -847       C  
ATOM   6339  CD1 PHE B 333      -3.483 -14.521  27.315  1.00144.45           C  
ANISOU 6339  CD1 PHE B 333    16902  15326  22657  -1074    119   -710       C  
ATOM   6340  CD2 PHE B 333      -5.125 -13.033  28.189  1.00142.98           C  
ANISOU 6340  CD2 PHE B 333    16456  14936  22933  -1473    -14  -1070       C  
ATOM   6341  CE1 PHE B 333      -4.434 -15.521  27.223  1.00114.09           C  
ANISOU 6341  CE1 PHE B 333    13153  11199  18997   -976     -1   -794       C  
ATOM   6342  CE2 PHE B 333      -6.079 -14.029  28.099  1.00120.66           C  
ANISOU 6342  CE2 PHE B 333    13725  11828  20294  -1376   -134  -1153       C  
ATOM   6343  CZ  PHE B 333      -5.733 -15.274  27.616  1.00109.57           C  
ANISOU 6343  CZ  PHE B 333    12498  10384  18751  -1128   -128  -1015       C  
TER    6344      PHE B 333                                                      
HETATM 6345  N   VFD A1900      27.348  -4.074   6.615  1.00 52.32           N  
HETATM 6346  CA  VFD A1900      26.914  -4.115   5.198  1.00 52.32           C  
HETATM 6347  C   VFD A1900      26.197  -2.801   4.783  1.00 58.48           C  
HETATM 6348  O   VFD A1900      25.288  -2.878   3.908  1.00 60.98           O  
HETATM 6349  CB  VFD A1900      26.022  -5.327   4.909  1.00 56.42           C  
HETATM 6350  CG  VFD A1900      25.008  -5.676   5.968  1.00 61.67           C  
HETATM 6351  CD1 VFD A1900      23.891  -6.474   5.670  1.00 58.72           C  
HETATM 6352  CD2 VFD A1900      25.174  -5.212   7.277  1.00 59.65           C  
HETATM 6353  CAA VFD A1900      20.862  -7.970   7.162  1.00 58.42           C  
HETATM 6354  CAC VFD A1900      22.940  -6.814   6.641  1.00 59.81           C  
HETATM 6355  CAG VFD A1900      26.348  -4.357   7.657  1.00 54.49           C  
HETATM 6356  CAN VFD A1900      28.652  -3.759   7.063  1.00 54.89           C  
HETATM 6357  CAP VFD A1900      29.734  -3.437   6.013  1.00 52.32           C  
HETATM 6358  CAQ VFD A1900      30.843  -2.528   6.525  1.00 52.32           C  
HETATM 6359  CAR VFD A1900      31.534  -2.754   7.729  1.00 53.19           C  
HETATM 6360  CAS VFD A1900      32.542  -1.891   8.149  1.00 56.17           C  
HETATM 6361  CAT VFD A1900      32.882  -0.789   7.373  1.00 60.63           C  
HETATM 6362  CAU VFD A1900      32.213  -0.550   6.177  1.00 57.20           C  
HETATM 6363  CAV VFD A1900      31.206  -1.411   5.757  1.00 52.32           C  
HETATM 6364  CAW VFD A1900      30.276  -4.652   5.265  1.00 52.32           C  
HETATM 6365  CAX VFD A1900      30.494  -4.546   3.884  1.00 52.32           C  
HETATM 6366  CAY VFD A1900      30.984  -5.615   3.143  1.00 52.32           C  
HETATM 6367  CAZ VFD A1900      31.269  -6.819   3.772  1.00 52.32           C  
HETATM 6368  CBA VFD A1900      31.062  -6.949   5.139  1.00 52.32           C  
HETATM 6369  CBB VFD A1900      30.570  -5.879   5.883  1.00 52.32           C  
HETATM 6370  CBC VFD A1900      24.225  -5.546   8.252  1.00 59.28           C  
HETATM 6371  CBD VFD A1900      23.122  -6.336   7.947  1.00 62.18           C  
HETATM 6372  CBF VFD A1900      24.460  -8.174   4.192  1.00 64.21           C  
HETATM 6373  CBG VFD A1900      23.820  -8.989   3.097  1.00 59.64           C  
HETATM 6374  CBH VFD A1900      22.432  -8.971   2.909  1.00 59.85           C  
HETATM 6375  CBI VFD A1900      21.846  -9.720   1.892  1.00 62.44           C  
HETATM 6376  CBJ VFD A1900      22.638 -10.494   1.049  1.00 57.91           C  
HETATM 6377  CBK VFD A1900      24.017 -10.519   1.225  1.00 52.32           C  
HETATM 6378  CBL VFD A1900      24.604  -9.771   2.240  1.00 59.66           C  
HETATM 6379  OAB VFD A1900      21.874  -7.619   6.199  1.00 58.61           O  
HETATM 6380  OAO VFD A1900      28.929  -3.739   8.257  1.00 52.32           O  
HETATM 6381  OBE VFD A1900      23.726  -6.944   4.366  1.00 67.00           O  
HETATM 6382  OXX VFD A1900      26.624  -1.770   5.381  1.00 52.60           O  
HETATM 6383  C10 OLC A1201      40.785   8.515  -1.246  1.00 61.66           C  
HETATM 6384  C9  OLC A1201      41.452   8.895  -0.156  1.00 61.06           C  
HETATM 6385  C11 OLC A1201      40.487   7.067  -1.545  1.00 63.82           C  
HETATM 6386  C8  OLC A1201      41.970   7.917   0.875  1.00 52.32           C  
HETATM 6387  C24 OLC A1201      54.630   9.349   2.349  1.00 69.95           C  
HETATM 6388  C7  OLC A1201      43.472   7.673   0.698  1.00 57.06           C  
HETATM 6389  C6  OLC A1201      44.293   8.964   0.718  1.00 58.75           C  
HETATM 6390  C5  OLC A1201      45.713   8.723   0.204  1.00 61.61           C  
HETATM 6391  C4  OLC A1201      46.762   9.014   1.276  1.00 56.54           C  
HETATM 6392  C3  OLC A1201      48.124   9.245   0.627  1.00 60.98           C  
HETATM 6393  C2  OLC A1201      49.266   9.182   1.641  1.00 55.48           C  
HETATM 6394  C21 OLC A1201      52.503  10.441   1.590  1.00 63.04           C  
HETATM 6395  C1  OLC A1201      50.604   9.362   0.924  1.00 62.96           C  
HETATM 6396  C22 OLC A1201      53.967  10.169   1.243  1.00 68.71           C  
HETATM 6397  O19 OLC A1201      50.613   9.606  -0.271  1.00 67.22           O  
HETATM 6398  O25 OLC A1201      56.020   9.505   2.270  1.00 71.80           O  
HETATM 6399  O23 OLC A1201      54.041   9.470   0.033  1.00 64.87           O  
HETATM 6400  O20 OLC A1201      51.757   9.256   1.580  1.00 68.91           O  
HETATM 6401  C1  OLA A1202      52.818  -7.561  -5.759  1.00 80.10           C  
HETATM 6402  O1  OLA A1202      53.410  -8.227  -6.638  1.00 86.31           O  
HETATM 6403  O2  OLA A1202      53.322  -6.481  -5.372  1.00 72.56           O  
HETATM 6404  C2  OLA A1202      51.499  -8.058  -5.165  1.00 70.02           C  
HETATM 6405  C3  OLA A1202      50.529  -8.525  -6.251  1.00 74.75           C  
HETATM 6406  C4  OLA A1202      49.113  -8.825  -5.739  1.00 76.20           C  
HETATM 6407  C5  OLA A1202      48.949  -8.715  -4.221  1.00 74.47           C  
HETATM 6408  C6  OLA A1202      47.683  -9.420  -3.734  1.00 68.75           C  
HETATM 6409  C7  OLA A1202      46.423  -8.788  -4.316  1.00 73.95           C  
HETATM 6410  C8  OLA A1202      45.521  -9.863  -4.895  1.00 76.21           C  
HETATM 6411  C9  OLA A1202      44.799 -10.565  -3.774  1.00 67.59           C  
HETATM 6412  C10 OLA A1202      43.476 -10.726  -3.779  1.00 72.74           C  
HETATM 6413  C11 OLA A1202      42.619 -10.214  -4.911  1.00 71.72           C  
HETATM 6414  C12 OLA A1202      41.144 -10.474  -4.662  1.00 67.89           C  
HETATM 6415  C13 OLA A1202      40.837 -11.967  -4.571  1.00 58.25           C  
HETATM 6416  C14 OLA A1202      40.223 -12.480  -5.872  1.00 52.32           C  
HETATM 6417  C1  OLA A1203      53.311 -11.413  -1.274  1.00 77.00           C  
HETATM 6418  O1  OLA A1203      54.555 -11.282  -1.353  1.00 70.79           O  
HETATM 6419  O2  OLA A1203      52.712 -10.937  -0.281  1.00 77.28           O  
HETATM 6420  C2  OLA A1203      52.539 -12.141  -2.378  1.00 72.50           C  
HETATM 6421  C3  OLA A1203      51.058 -11.767  -2.374  1.00 68.74           C  
HETATM 6422  C4  OLA A1203      50.182 -12.915  -1.875  1.00 74.40           C  
HETATM 6423  C5  OLA A1203      48.810 -12.865  -2.544  1.00 68.99           C  
HETATM 6424  C6  OLA A1203      47.836 -13.877  -1.944  1.00 63.12           C  
HETATM 6425  C7  OLA A1203      46.446 -13.668  -2.544  1.00 64.37           C  
HETATM 6426  C8  OLA A1203      45.625 -14.946  -2.543  1.00 52.32           C  
HETATM 6427  C9  OLA A1203      44.973 -15.148  -1.199  1.00 52.32           C  
HETATM 6428  C10 OLA A1203      43.680 -15.459  -1.068  1.00 60.07           C  
HETATM 6429  C11 OLA A1203      42.770 -15.634  -2.260  1.00 69.60           C  
HETATM 6430  C12 OLA A1203      41.375 -16.066  -1.839  1.00 66.47           C  
HETATM 6431  C13 OLA A1203      41.427 -17.291  -0.927  1.00 60.83           C  
HETATM 6432  C18 OLC A1204      40.975  -0.991  -8.789  1.00 84.11           C  
HETATM 6433  C10 OLC A1204      43.554   5.741  -4.549  1.00 75.95           C  
HETATM 6434  C9  OLC A1204      44.758   5.980  -4.031  1.00 72.58           C  
HETATM 6435  C17 OLC A1204      42.245  -0.179  -8.973  1.00 76.20           C  
HETATM 6436  C11 OLC A1204      42.657   4.617  -4.089  1.00 71.81           C  
HETATM 6437  C8  OLC A1204      45.358   5.150  -2.922  1.00 68.86           C  
HETATM 6438  C24 OLC A1204      57.609   9.106  -3.449  1.00 92.29           C  
HETATM 6439  C16 OLC A1204      41.878   1.293  -9.169  1.00 78.50           C  
HETATM 6440  C12 OLC A1204      41.870   4.109  -5.297  1.00 70.77           C  
HETATM 6441  C7  OLC A1204      46.885   5.236  -2.967  1.00 72.79           C  
HETATM 6442  C15 OLC A1204      42.891   2.230  -8.509  1.00 95.64           C  
HETATM 6443  C13 OLC A1204      42.781   3.334  -6.248  1.00 72.14           C  
HETATM 6444  C6  OLC A1204      47.396   6.665  -2.793  1.00 69.14           C  
HETATM 6445  C14 OLC A1204      42.211   3.310  -7.665  1.00 78.99           C  
HETATM 6446  C5  OLC A1204      48.363   7.024  -3.920  1.00 70.03           C  
HETATM 6447  C4  OLC A1204      49.039   8.367  -3.651  1.00 71.77           C  
HETATM 6448  C3  OLC A1204      50.440   8.423  -4.253  1.00 69.76           C  
HETATM 6449  C2  OLC A1204      51.460   8.868  -3.207  1.00 71.73           C  
HETATM 6450  C21 OLC A1204      55.142   9.073  -3.709  1.00 74.82           C  
HETATM 6451  C1  OLC A1204      52.861   8.925  -3.810  1.00 72.25           C  
HETATM 6452  C22 OLC A1204      56.286   8.943  -2.707  1.00 78.97           C  
HETATM 6453  O19 OLC A1204      53.002   8.828  -5.018  1.00 80.17           O  
HETATM 6454  O25 OLC A1204      58.321  10.187  -2.915  1.00112.23           O  
HETATM 6455  O23 OLC A1204      56.162   9.931  -1.724  1.00 84.63           O  
HETATM 6456  O20 OLC A1204      53.923   9.074  -3.023  1.00 69.03           O  
HETATM 6457  C18 OLC A1205      36.958  11.047  14.088  1.00 90.02           C  
HETATM 6458  C10 OLC A1205      30.904  12.974   8.223  1.00 91.69           C  
HETATM 6459  C9  OLC A1205      30.311  13.768   7.329  1.00 77.68           C  
HETATM 6460  C17 OLC A1205      36.460  11.590  12.762  1.00 74.34           C  
HETATM 6461  C11 OLC A1205      30.437  11.567   8.513  1.00 79.57           C  
HETATM 6462  C8  OLC A1205      29.114  13.338   6.519  1.00 74.58           C  
HETATM 6463  C24 OLC A1205      18.163  14.996   0.969  1.00 82.21           C  
HETATM 6464  C16 OLC A1205      35.284  10.744  12.278  1.00 79.05           C  
HETATM 6465  C12 OLC A1205      30.890  11.157   9.915  1.00 68.60           C  
HETATM 6466  C7  OLC A1205      27.908  14.195   6.902  1.00 76.85           C  
HETATM 6467  C15 OLC A1205      34.463  11.478  11.218  1.00 82.99           C  
HETATM 6468  C13 OLC A1205      32.380  10.820   9.944  1.00 69.82           C  
HETATM 6469  C6  OLC A1205      26.633  13.660   6.254  1.00 70.25           C  
HETATM 6470  C14 OLC A1205      32.983  11.105  11.319  1.00 74.59           C  
HETATM 6471  C5  OLC A1205      25.403  14.406   6.770  1.00 77.56           C  
HETATM 6472  C4  OLC A1205      24.554  14.942   5.619  1.00 78.92           C  
HETATM 6473  C3  OLC A1205      23.591  13.871   5.112  1.00 72.06           C  
HETATM 6474  C2  OLC A1205      22.999  14.251   3.757  1.00 70.44           C  
HETATM 6475  C21 OLC A1205      20.277  14.717   2.281  1.00 72.18           C  
HETATM 6476  C1  OLC A1205      21.818  15.208   3.903  1.00 80.25           C  
HETATM 6477  C22 OLC A1205      19.667  15.273   0.995  1.00 78.47           C  
HETATM 6478  O19 OLC A1205      21.457  15.571   5.010  1.00 83.40           O  
HETATM 6479  O25 OLC A1205      17.706  14.981  -0.356  1.00 68.19           O  
HETATM 6480  O23 OLC A1205      19.894  16.653   0.922  1.00 89.11           O  
HETATM 6481  O20 OLC A1205      21.176  15.645   2.821  1.00 86.97           O  
HETATM 6482  C1  OLA A1206      24.352  17.827   1.336  1.00103.48           C  
HETATM 6483  O1  OLA A1206      24.969  18.271   0.339  1.00 97.00           O  
HETATM 6484  O2  OLA A1206      23.105  17.949   1.391  1.00 88.16           O  
HETATM 6485  C2  OLA A1206      25.110  17.144   2.477  1.00 83.28           C  
HETATM 6486  C3  OLA A1206      26.610  17.411   2.386  1.00 75.69           C  
HETATM 6487  C4  OLA A1206      27.347  16.303   1.633  1.00 75.56           C  
HETATM 6488  C5  OLA A1206      28.192  15.409   2.545  1.00 80.55           C  
HETATM 6489  C6  OLA A1206      29.184  16.202   3.399  1.00 75.31           C  
HETATM 6490  C7  OLA A1206      30.649  15.817   3.181  1.00 72.73           C  
HETATM 6491  C8  OLA A1206      30.880  14.320   3.060  1.00 74.30           C  
HETATM 6492  C9  OLA A1206      32.239  13.956   3.602  1.00 78.85           C  
HETATM 6493  C10 OLA A1206      33.078  13.152   2.948  1.00 79.24           C  
HETATM 6494  C11 OLA A1206      32.736  12.541   1.612  1.00 74.62           C  
HETATM 6495  C12 OLA A1206      33.952  11.827   1.054  1.00 77.51           C  
HETATM 6496  C13 OLA A1206      33.764  11.401  -0.401  1.00 71.90           C  
HETATM 6497  C14 OLA A1206      35.039  10.720  -0.897  1.00 69.79           C  
HETATM 6498  C15 OLA A1206      34.759   9.630  -1.930  1.00 67.32           C  
HETATM 6499  C16 OLA A1206      34.781   8.243  -1.289  1.00 70.06           C  
HETATM 6500  C17 OLA A1206      35.086   7.153  -2.316  1.00 69.87           C  
HETATM 6501  C18 OLA A1206      35.156   5.790  -1.652  1.00 52.32           C  
HETATM 6502  C   FMT A1207      38.568  -6.567   6.061  1.00 60.41           C  
HETATM 6503  O1  FMT A1207      39.759  -6.784   6.392  1.00 59.37           O  
HETATM 6504  O2  FMT A1207      37.832  -7.530   5.722  1.00 64.71           O  
HETATM 6505  O1  HEZ A1208      10.511   2.537   6.758  1.00107.25           O  
HETATM 6506  C1  HEZ A1208      11.525   1.844   6.084  1.00 87.69           C  
HETATM 6507  C2  HEZ A1208      11.377   2.085   4.584  1.00100.16           C  
HETATM 6508  C3  HEZ A1208      12.427   1.293   3.805  1.00 80.96           C  
HETATM 6509  C4  HEZ A1208      12.672   1.975   2.459  1.00 86.33           C  
HETATM 6510  C5  HEZ A1208      13.549   1.088   1.576  1.00102.79           C  
HETATM 6511  C6  HEZ A1208      13.993   1.869   0.339  1.00110.74           C  
HETATM 6512  O6  HEZ A1208      15.169   1.307  -0.181  1.00 97.95           O  
HETATM 6513  N   VFD B1900      40.015 -20.868  34.779  1.00 97.25           N  
HETATM 6514  CA  VFD B1900      40.388 -20.361  36.118  1.00 97.01           C  
HETATM 6515  C   VFD B1900      41.121 -18.994  36.022  1.00 97.14           C  
HETATM 6516  O   VFD B1900      41.349 -18.559  34.857  1.00 96.58           O  
HETATM 6517  CB  VFD B1900      41.268 -21.319  36.936  1.00 99.52           C  
HETATM 6518  CG  VFD B1900      41.896 -22.505  36.247  1.00 99.45           C  
HETATM 6519  CD1 VFD B1900      42.630 -23.465  36.972  1.00104.55           C  
HETATM 6520  CD2 VFD B1900      41.766 -22.667  34.865  1.00 95.99           C  
HETATM 6521  CAA VFD B1900      45.244 -25.046  37.583  1.00117.44           C  
HETATM 6522  CAC VFD B1900      43.224 -24.568  36.341  1.00105.16           C  
HETATM 6523  CAG VFD B1900      40.999 -21.675  34.045  1.00101.08           C  
HETATM 6524  CAN VFD B1900      38.784 -20.624  34.124  1.00 91.91           C  
HETATM 6525  CAP VFD B1900      37.697 -19.782  34.827  1.00 94.44           C  
HETATM 6526  CAQ VFD B1900      36.874 -18.957  33.845  1.00 92.06           C  
HETATM 6527  CAR VFD B1900      37.011 -17.562  33.736  1.00 90.48           C  
HETATM 6528  CAS VFD B1900      36.245 -16.833  32.829  1.00 90.34           C  
HETATM 6529  CAT VFD B1900      35.327 -17.481  32.012  1.00 87.90           C  
HETATM 6530  CAU VFD B1900      35.176 -18.859  32.103  1.00 85.59           C  
HETATM 6531  CAV VFD B1900      35.941 -19.588  33.009  1.00 90.63           C  
HETATM 6532  CAW VFD B1900      36.828 -20.628  35.755  1.00 94.79           C  
HETATM 6533  CAX VFD B1900      36.228 -20.036  36.876  1.00 95.84           C  
HETATM 6534  CAY VFD B1900      35.432 -20.781  37.739  1.00101.76           C  
HETATM 6535  CAZ VFD B1900      35.218 -22.134  37.501  1.00 92.73           C  
HETATM 6536  CBA VFD B1900      35.803 -22.741  36.398  1.00 95.70           C  
HETATM 6537  CBB VFD B1900      36.600 -21.998  35.532  1.00 96.56           C  
HETATM 6538  CBC VFD B1900      42.356 -23.766  34.233  1.00 95.29           C  
HETATM 6539  CBD VFD B1900      43.076 -24.710  34.955  1.00100.93           C  
HETATM 6540  CBF VFD B1900      41.983 -24.282  39.079  1.00110.18           C  
HETATM 6541  CBG VFD B1900      42.129 -24.023  40.557  1.00116.26           C  
HETATM 6542  CBH VFD B1900      43.154 -23.196  41.038  1.00118.89           C  
HETATM 6543  CBI VFD B1900      43.292 -22.956  42.403  1.00121.71           C  
HETATM 6544  CBJ VFD B1900      42.406 -23.538  43.306  1.00120.59           C  
HETATM 6545  CBK VFD B1900      41.384 -24.359  42.842  1.00117.82           C  
HETATM 6546  CBL VFD B1900      41.246 -24.599  41.478  1.00115.38           C  
HETATM 6547  OAB VFD B1900      43.930 -25.460  37.164  1.00106.33           O  
HETATM 6548  OAO VFD B1900      38.551 -21.079  33.009  1.00 87.96           O  
HETATM 6549  OBE VFD B1900      42.775 -23.316  38.356  1.00110.15           O  
HETATM 6550  OXX VFD B1900      41.411 -18.462  37.130  1.00101.44           O  
HETATM 6551  C1  OLA B1201      19.146 -16.521  20.380  1.00 85.83           C  
HETATM 6552  O1  OLA B1201      18.401 -15.756  19.725  1.00 84.70           O  
HETATM 6553  O2  OLA B1201      18.646 -17.523  20.937  1.00 89.63           O  
HETATM 6554  C2  OLA B1201      20.644 -16.246  20.508  1.00 80.04           C  
HETATM 6555  C3  OLA B1201      20.992 -14.833  20.051  1.00 81.49           C  
HETATM 6556  C4  OLA B1201      22.234 -14.331  20.781  1.00 81.03           C  
HETATM 6557  C5  OLA B1201      23.498 -15.043  20.298  1.00 76.77           C  
HETATM 6558  C6  OLA B1201      24.547 -15.191  21.404  1.00 77.75           C  
HETATM 6559  C7  OLA B1201      24.549 -14.018  22.385  1.00 78.70           C  
HETATM 6560  C8  OLA B1201      25.962 -13.688  22.825  1.00 87.88           C  
HETATM 6561  C9  OLA B1201      26.562 -14.844  23.579  1.00 79.85           C  
HETATM 6562  C10 OLA B1201      27.812 -14.811  24.042  1.00 74.81           C  
HETATM 6563  C11 OLA B1201      28.725 -13.625  23.853  1.00 76.30           C  
HETATM 6564  C12 OLA B1201      29.959 -14.054  23.075  1.00 89.55           C  
HETATM 6565  C13 OLA B1201      31.056 -12.991  23.111  1.00 82.36           C  
HETATM 6566  C14 OLA B1201      31.562 -12.657  21.708  1.00 80.21           C  
HETATM 6567  C15 OLA B1201      33.088 -12.585  21.659  1.00 75.99           C  
HETATM 6568  C16 OLA B1201      33.698 -13.967  21.432  1.00 72.23           C  
HETATM 6569  C17 OLA B1201      35.208 -13.950  21.662  1.00 72.76           C  
HETATM 6570  C18 OLA B1201      35.913 -14.900  20.712  1.00 67.35           C  
HETATM 6571  O   HOH A1301      35.338  -1.174   4.547  1.00 52.32           O  
HETATM 6572  O   HOH A1302      33.905  -4.691  -2.387  1.00 52.32           O  
HETATM 6573  O   HOH A1303      19.777  -4.827   4.924  1.00 66.54           O  
HETATM 6574  O   HOH A1304      25.413  -0.439   9.136  1.00 52.32           O  
CONECT  848 2882                                                                
CONECT 1091 1100                                                                
CONECT 1100 1091 1101                                                           
CONECT 1101 1100 1102 1108                                                      
CONECT 1102 1101 1103                                                           
CONECT 1103 1102 1104                                                           
CONECT 1104 1103 1105                                                           
CONECT 1105 1104 1106 1107                                                      
CONECT 1106 1105                                                                
CONECT 1107 1105                                                                
CONECT 1108 1101 1109 1110                                                      
CONECT 1109 1108                                                                
CONECT 1110 1108                                                                
CONECT 1492 2133                                                                
CONECT 2133 1492                                                                
CONECT 2882  848                                                                
CONECT 3088 3098                                                                
CONECT 3098 3088 3099                                                           
CONECT 3099 3098 3100 3106                                                      
CONECT 3100 3099 3101                                                           
CONECT 3101 3100 3102                                                           
CONECT 3102 3101 3103                                                           
CONECT 3103 3102 3104 3105                                                      
CONECT 3104 3103                                                                
CONECT 3105 3103                                                                
CONECT 3106 3099 3107 3108                                                      
CONECT 3107 3106                                                                
CONECT 3108 3106                                                                
CONECT 4240 4249                                                                
CONECT 4249 4240 4250                                                           
CONECT 4250 4249 4251 4257                                                      
CONECT 4251 4250 4252                                                           
CONECT 4252 4251 4253                                                           
CONECT 4253 4252 4254                                                           
CONECT 4254 4253 4255 4256                                                      
CONECT 4255 4254                                                                
CONECT 4256 4254                                                                
CONECT 4257 4250 4258 4259                                                      
CONECT 4258 4257                                                                
CONECT 4259 4257                                                                
CONECT 4637 5264                                                                
CONECT 5264 4637                                                                
CONECT 6202 6212                                                                
CONECT 6212 6202 6213                                                           
CONECT 6213 6212 6214 6220                                                      
CONECT 6214 6213 6215                                                           
CONECT 6215 6214 6216                                                           
CONECT 6216 6215 6217                                                           
CONECT 6217 6216 6218 6219                                                      
CONECT 6218 6217                                                                
CONECT 6219 6217                                                                
CONECT 6220 6213 6221 6222                                                      
CONECT 6221 6220                                                                
CONECT 6222 6220                                                                
CONECT 6345 6346 6355 6356                                                      
CONECT 6346 6345 6347 6349                                                      
CONECT 6347 6346 6348 6382                                                      
CONECT 6348 6347                                                                
CONECT 6349 6346 6350                                                           
CONECT 6350 6349 6351 6352                                                      
CONECT 6351 6350 6354 6381                                                      
CONECT 6352 6350 6355 6370                                                      
CONECT 6353 6379                                                                
CONECT 6354 6351 6371 6379                                                      
CONECT 6355 6345 6352                                                           
CONECT 6356 6345 6357 6380                                                      
CONECT 6357 6356 6358 6364                                                      
CONECT 6358 6357 6359 6363                                                      
CONECT 6359 6358 6360                                                           
CONECT 6360 6359 6361                                                           
CONECT 6361 6360 6362                                                           
CONECT 6362 6361 6363                                                           
CONECT 6363 6358 6362                                                           
CONECT 6364 6357 6365 6369                                                      
CONECT 6365 6364 6366                                                           
CONECT 6366 6365 6367                                                           
CONECT 6367 6366 6368                                                           
CONECT 6368 6367 6369                                                           
CONECT 6369 6364 6368                                                           
CONECT 6370 6352 6371                                                           
CONECT 6371 6354 6370                                                           
CONECT 6372 6373 6381                                                           
CONECT 6373 6372 6374 6378                                                      
CONECT 6374 6373 6375                                                           
CONECT 6375 6374 6376                                                           
CONECT 6376 6375 6377                                                           
CONECT 6377 6376 6378                                                           
CONECT 6378 6373 6377                                                           
CONECT 6379 6353 6354                                                           
CONECT 6380 6356                                                                
CONECT 6381 6351 6372                                                           
CONECT 6382 6347                                                                
CONECT 6383 6384 6385                                                           
CONECT 6384 6383 6386                                                           
CONECT 6385 6383                                                                
CONECT 6386 6384 6388                                                           
CONECT 6387 6396 6398                                                           
CONECT 6388 6386 6389                                                           
CONECT 6389 6388 6390                                                           
CONECT 6390 6389 6391                                                           
CONECT 6391 6390 6392                                                           
CONECT 6392 6391 6393                                                           
CONECT 6393 6392 6395                                                           
CONECT 6394 6396 6400                                                           
CONECT 6395 6393 6397 6400                                                      
CONECT 6396 6387 6394 6399                                                      
CONECT 6397 6395                                                                
CONECT 6398 6387                                                                
CONECT 6399 6396                                                                
CONECT 6400 6394 6395                                                           
CONECT 6401 6402 6403 6404                                                      
CONECT 6402 6401                                                                
CONECT 6403 6401                                                                
CONECT 6404 6401 6405                                                           
CONECT 6405 6404 6406                                                           
CONECT 6406 6405 6407                                                           
CONECT 6407 6406 6408                                                           
CONECT 6408 6407 6409                                                           
CONECT 6409 6408 6410                                                           
CONECT 6410 6409 6411                                                           
CONECT 6411 6410 6412                                                           
CONECT 6412 6411 6413                                                           
CONECT 6413 6412 6414                                                           
CONECT 6414 6413 6415                                                           
CONECT 6415 6414 6416                                                           
CONECT 6416 6415                                                                
CONECT 6417 6418 6419 6420                                                      
CONECT 6418 6417                                                                
CONECT 6419 6417                                                                
CONECT 6420 6417 6421                                                           
CONECT 6421 6420 6422                                                           
CONECT 6422 6421 6423                                                           
CONECT 6423 6422 6424                                                           
CONECT 6424 6423 6425                                                           
CONECT 6425 6424 6426                                                           
CONECT 6426 6425 6427                                                           
CONECT 6427 6426 6428                                                           
CONECT 6428 6427 6429                                                           
CONECT 6429 6428 6430                                                           
CONECT 6430 6429 6431                                                           
CONECT 6431 6430                                                                
CONECT 6432 6435                                                                
CONECT 6433 6434 6436                                                           
CONECT 6434 6433 6437                                                           
CONECT 6435 6432 6439                                                           
CONECT 6436 6433 6440                                                           
CONECT 6437 6434 6441                                                           
CONECT 6438 6452 6454                                                           
CONECT 6439 6435 6442                                                           
CONECT 6440 6436 6443                                                           
CONECT 6441 6437 6444                                                           
CONECT 6442 6439 6445                                                           
CONECT 6443 6440 6445                                                           
CONECT 6444 6441 6446                                                           
CONECT 6445 6442 6443                                                           
CONECT 6446 6444 6447                                                           
CONECT 6447 6446 6448                                                           
CONECT 6448 6447 6449                                                           
CONECT 6449 6448 6451                                                           
CONECT 6450 6452 6456                                                           
CONECT 6451 6449 6453 6456                                                      
CONECT 6452 6438 6450 6455                                                      
CONECT 6453 6451                                                                
CONECT 6454 6438                                                                
CONECT 6455 6452                                                                
CONECT 6456 6450 6451                                                           
CONECT 6457 6460                                                                
CONECT 6458 6459 6461                                                           
CONECT 6459 6458 6462                                                           
CONECT 6460 6457 6464                                                           
CONECT 6461 6458 6465                                                           
CONECT 6462 6459 6466                                                           
CONECT 6463 6477 6479                                                           
CONECT 6464 6460 6467                                                           
CONECT 6465 6461 6468                                                           
CONECT 6466 6462 6469                                                           
CONECT 6467 6464 6470                                                           
CONECT 6468 6465 6470                                                           
CONECT 6469 6466 6471                                                           
CONECT 6470 6467 6468                                                           
CONECT 6471 6469 6472                                                           
CONECT 6472 6471 6473                                                           
CONECT 6473 6472 6474                                                           
CONECT 6474 6473 6476                                                           
CONECT 6475 6477 6481                                                           
CONECT 6476 6474 6478 6481                                                      
CONECT 6477 6463 6475 6480                                                      
CONECT 6478 6476                                                                
CONECT 6479 6463                                                                
CONECT 6480 6477                                                                
CONECT 6481 6475 6476                                                           
CONECT 6482 6483 6484 6485                                                      
CONECT 6483 6482                                                                
CONECT 6484 6482                                                                
CONECT 6485 6482 6486                                                           
CONECT 6486 6485 6487                                                           
CONECT 6487 6486 6488                                                           
CONECT 6488 6487 6489                                                           
CONECT 6489 6488 6490                                                           
CONECT 6490 6489 6491                                                           
CONECT 6491 6490 6492                                                           
CONECT 6492 6491 6493                                                           
CONECT 6493 6492 6494                                                           
CONECT 6494 6493 6495                                                           
CONECT 6495 6494 6496                                                           
CONECT 6496 6495 6497                                                           
CONECT 6497 6496 6498                                                           
CONECT 6498 6497 6499                                                           
CONECT 6499 6498 6500                                                           
CONECT 6500 6499 6501                                                           
CONECT 6501 6500                                                                
CONECT 6502 6503 6504                                                           
CONECT 6503 6502                                                                
CONECT 6504 6502                                                                
CONECT 6505 6506                                                                
CONECT 6506 6505 6507                                                           
CONECT 6507 6506 6508                                                           
CONECT 6508 6507 6509                                                           
CONECT 6509 6508 6510                                                           
CONECT 6510 6509 6511                                                           
CONECT 6511 6510 6512                                                           
CONECT 6512 6511                                                                
CONECT 6513 6514 6523 6524                                                      
CONECT 6514 6513 6515 6517                                                      
CONECT 6515 6514 6516 6550                                                      
CONECT 6516 6515                                                                
CONECT 6517 6514 6518                                                           
CONECT 6518 6517 6519 6520                                                      
CONECT 6519 6518 6522 6549                                                      
CONECT 6520 6518 6523 6538                                                      
CONECT 6521 6547                                                                
CONECT 6522 6519 6539 6547                                                      
CONECT 6523 6513 6520                                                           
CONECT 6524 6513 6525 6548                                                      
CONECT 6525 6524 6526 6532                                                      
CONECT 6526 6525 6527 6531                                                      
CONECT 6527 6526 6528                                                           
CONECT 6528 6527 6529                                                           
CONECT 6529 6528 6530                                                           
CONECT 6530 6529 6531                                                           
CONECT 6531 6526 6530                                                           
CONECT 6532 6525 6533 6537                                                      
CONECT 6533 6532 6534                                                           
CONECT 6534 6533 6535                                                           
CONECT 6535 6534 6536                                                           
CONECT 6536 6535 6537                                                           
CONECT 6537 6532 6536                                                           
CONECT 6538 6520 6539                                                           
CONECT 6539 6522 6538                                                           
CONECT 6540 6541 6549                                                           
CONECT 6541 6540 6542 6546                                                      
CONECT 6542 6541 6543                                                           
CONECT 6543 6542 6544                                                           
CONECT 6544 6543 6545                                                           
CONECT 6545 6544 6546                                                           
CONECT 6546 6541 6545                                                           
CONECT 6547 6521 6522                                                           
CONECT 6548 6524                                                                
CONECT 6549 6519 6540                                                           
CONECT 6550 6515                                                                
CONECT 6551 6552 6553 6554                                                      
CONECT 6552 6551                                                                
CONECT 6553 6551                                                                
CONECT 6554 6551 6555                                                           
CONECT 6555 6554 6556                                                           
CONECT 6556 6555 6557                                                           
CONECT 6557 6556 6558                                                           
CONECT 6558 6557 6559                                                           
CONECT 6559 6558 6560                                                           
CONECT 6560 6559 6561                                                           
CONECT 6561 6560 6562                                                           
CONECT 6562 6561 6563                                                           
CONECT 6563 6562 6564                                                           
CONECT 6564 6563 6565                                                           
CONECT 6565 6564 6566                                                           
CONECT 6566 6565 6567                                                           
CONECT 6567 6566 6568                                                           
CONECT 6568 6567 6569                                                           
CONECT 6569 6568 6570                                                           
CONECT 6570 6569                                                                
MASTER      601    0   15   36    4    0    0    6 6572    2  280   64          
END