HEADER    MEMBRANE PROTEIN                        03-DEC-19   6LFL              
TITLE     CRYSTAL STRUCTURE OF A CLASS A GPCR                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 2,GLGA GLYCOGEN SYNTHASE,C-X-
COMPND   3 C CHEMOKINE RECEPTOR TYPE 2;                                         
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: CXCR-2,CDW128B,GRO/MGSA RECEPTOR,HIGH AFFINITY INTERLEUKIN-8
COMPND   6 RECEPTOR B,IL-8R B,IL-8 RECEPTOR TYPE 2,GLYCOGEN SYNTHASE,CXCR-2,    
COMPND   7 CDW128B,GRO/MGSA RECEPTOR,HIGH AFFINITY INTERLEUKIN-8 RECEPTOR B,IL- 
COMPND   8 8R B,IL-8 RECEPTOR TYPE 2;                                           
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI (STRAIN GE5 /   
SOURCE   3 ORSAY);                                                              
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   6 STRAIN: GE5 / ORSAY;                                                 
SOURCE   7 GENE: CXCR2, IL8RB, PAB2292;                                         
SOURCE   8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    G PROTEIN-COUPLED RECEPTOR, MEMBRANE PROTEIN                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.J.LIU,T.HUA,K.W.LIU,L.J.WU                                          
REVDAT   2   16-SEP-20 6LFL    1       JRNL                                     
REVDAT   1   02-SEP-20 6LFL    0                                                
JRNL        AUTH   K.LIU,L.WU,S.YUAN,M.WU,Y.XU,Q.SUN,S.LI,S.ZHAO,T.HUA,Z.J.LIU  
JRNL        TITL   STRUCTURAL BASIS OF CXC CHEMOKINE RECEPTOR 2 ACTIVATION AND  
JRNL        TITL 2 SIGNALLING.                                                  
JRNL        REF    NATURE                        V. 585   135 2020              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   32610344                                                     
JRNL        DOI    10.1038/S41586-020-2492-5                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12047                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.233                          
REMARK   3   R VALUE            (WORKING SET)  : 0.231                          
REMARK   3   FREE R VALUE                      : 0.264                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.110                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 616                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.50                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.44                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2858                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2145                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2711                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2123                   
REMARK   3   BIN FREE R VALUE                        : 0.2562                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.14                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 147                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3706                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 110.7                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 132.5                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.54330                                             
REMARK   3    B22 (A**2) : -15.81650                                            
REMARK   3    B33 (A**2) : 16.35980                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -5.57590                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.520               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.449               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.902                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3823   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5173   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1316   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 613    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3823   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 497    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4388   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.93                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 23.04                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    40.412   -19.015   183.590           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1988 T22:    0.0881                                    
REMARK   3     T33:   -0.4302 T12:    0.0337                                    
REMARK   3     T13:   -0.0710 T23:    0.0018                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0383 L22:    2.1584                                    
REMARK   3     L33:    0.9676 L12:   -1.0940                                    
REMARK   3     L13:   -1.2712 L23:    1.5478                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0765 S12:    0.2724 S13:   -0.0327                     
REMARK   3     S21:   -0.1226 S22:   -0.1571 S23:   -0.0138                     
REMARK   3     S31:   -0.3108 S32:   -0.1083 S33:    0.0807                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6LFL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE DEPOSITION ID IS D_1300014707.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12047                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 10.78                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.03                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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: 5LWE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH7.0, 32% PEG 400, 50-150   
REMARK 280  MM SODIUM TARTRATE DIBASIC DIHYDRATE SALT, LIPIDIC CUBIC PHASE,     
REMARK 280  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       54.23000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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 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     ALA A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     CYS A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     LEU A    44                                                      
REMARK 465     GLU A    45                                                      
REMARK 465     MET A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     ASN A   202                                                      
REMARK 465     ASN A   203                                                      
REMARK 465     THR A   204                                                      
REMARK 465     GLN A   280                                                      
REMARK 465     VAL A   281                                                      
REMARK 465     ILE A   282                                                      
REMARK 465     GLN A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     THR A   285                                                      
REMARK 465     CYS A   286                                                      
REMARK 465     GLU A   287                                                      
REMARK 465     ARG A   288                                                      
REMARK 465     LYS A   337                                                      
REMARK 465     ASP A   338                                                      
REMARK 465     SER A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     PRO A   341                                                      
REMARK 465     LYS A   342                                                      
REMARK 465     ASP A   343                                                      
REMARK 465     SER A   344                                                      
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     TYR A  49    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 208    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 212    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 289    CG   CD   NE   CZ   NH1  NH2                        
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 A 158       73.36   -111.35                                   
REMARK 500    ASN A 191       -0.52     62.70                                   
REMARK 500    PHE A 220      -58.93   -133.06                                   
REMARK 500    GLN A1045      -64.88   -129.95                                   
REMARK 500    ILE A1117       77.97   -119.71                                   
REMARK 500    PRO A1118       37.35    -85.44                                   
REMARK 500    ILE A1139       79.33   -107.36                                   
REMARK 500    ALA A1142       87.52    -67.85                                   
REMARK 500    ASP A1180      102.71    -58.26                                   
REMARK 500    LEU A1181       31.50    -86.98                                   
REMARK 500    HIS A 247      -41.61    -20.51                                   
REMARK 500    HIS A 332      -80.98    -99.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EBX A 1201                
DBREF  6LFL A   37   241  UNP    P25025   CXCR2_HUMAN     37    241             
DBREF  6LFL A 1001  1196  UNP    Q9V2J8   Q9V2J8_PYRAB   218    413             
DBREF  6LFL A  244   344  UNP    P25025   CXCR2_HUMAN    244    344             
SEQADV 6LFL TRP A  135  UNP  P25025    LEU   135 ENGINEERED MUTATION            
SEQADV 6LFL GLU A  249  UNP  P25025    ALA   249 ENGINEERED MUTATION            
SEQADV 6LFL ALA A  303  UNP  P25025    GLY   303 ENGINEERED MUTATION            
SEQRES   1 A  502  ALA PRO CYS GLU PRO GLU SER LEU GLU ILE ASN LYS TYR          
SEQRES   2 A  502  PHE VAL VAL ILE ILE TYR ALA LEU VAL PHE LEU LEU SER          
SEQRES   3 A  502  LEU LEU GLY ASN SER LEU VAL MET LEU VAL ILE LEU TYR          
SEQRES   4 A  502  SER ARG VAL GLY ARG SER VAL THR ASP VAL TYR LEU LEU          
SEQRES   5 A  502  ASN LEU ALA LEU ALA ASP LEU LEU PHE ALA LEU THR LEU          
SEQRES   6 A  502  PRO ILE TRP ALA ALA SER LYS VAL ASN GLY TRP ILE PHE          
SEQRES   7 A  502  GLY THR PHE LEU CYS LYS VAL VAL SER LEU LEU LYS GLU          
SEQRES   8 A  502  VAL ASN PHE TYR SER GLY ILE TRP LEU LEU ALA CYS ILE          
SEQRES   9 A  502  SER VAL ASP ARG TYR LEU ALA ILE VAL HIS ALA THR ARG          
SEQRES  10 A  502  THR LEU THR GLN LYS ARG TYR LEU VAL LYS PHE ILE CYS          
SEQRES  11 A  502  LEU SER ILE TRP GLY LEU SER LEU LEU LEU ALA LEU PRO          
SEQRES  12 A  502  VAL LEU LEU PHE ARG ARG THR VAL TYR SER SER ASN VAL          
SEQRES  13 A  502  SER PRO ALA CYS TYR GLU ASP MET GLY ASN ASN THR ALA          
SEQRES  14 A  502  ASN TRP ARG MET LEU LEU ARG ILE LEU PRO GLN SER PHE          
SEQRES  15 A  502  GLY PHE ILE VAL PRO LEU LEU ILE MET LEU PHE CYS TYR          
SEQRES  16 A  502  GLY PHE THR LEU ARG THR LEU PHE LYS ALA GLY ILE ASP          
SEQRES  17 A  502  CYS SER PHE TRP ASN GLU SER TYR LEU THR GLY SER ARG          
SEQRES  18 A  502  ASP GLU ARG LYS LYS SER LEU LEU SER LYS PHE GLY MET          
SEQRES  19 A  502  ASP GLU GLY VAL THR PHE MET PHE ILE GLY ARG PHE ASP          
SEQRES  20 A  502  ARG GLY GLN LYS GLY VAL ASP VAL LEU LEU LYS ALA ILE          
SEQRES  21 A  502  GLU ILE LEU SER SER LYS LYS GLU PHE GLN GLU MET ARG          
SEQRES  22 A  502  PHE ILE ILE ILE GLY LYS GLY ASP PRO GLU LEU GLU GLY          
SEQRES  23 A  502  TRP ALA ARG SER LEU GLU GLU LYS HIS GLY ASN VAL LYS          
SEQRES  24 A  502  VAL ILE THR GLU MET LEU SER ARG GLU PHE VAL ARG GLU          
SEQRES  25 A  502  LEU TYR GLY SER VAL ASP PHE VAL ILE ILE PRO SER TYR          
SEQRES  26 A  502  PHE GLU PRO PHE GLY LEU VAL ALA LEU GLU ALA MET CYS          
SEQRES  27 A  502  LEU GLY ALA ILE PRO ILE ALA SER ALA VAL GLY GLY LEU          
SEQRES  28 A  502  ARG ASP ILE ILE THR ASN GLU THR GLY ILE LEU VAL LYS          
SEQRES  29 A  502  ALA GLY ASP PRO GLY GLU LEU ALA ASN ALA ILE LEU LYS          
SEQRES  30 A  502  ALA LEU GLU LEU SER ARG SER ASP LEU SER LYS PHE ARG          
SEQRES  31 A  502  GLU ASN CYS LYS LYS ARG ALA MET SER PHE SER GLY GLN          
SEQRES  32 A  502  LYS HIS ARG GLU MET ARG VAL ILE PHE ALA VAL VAL LEU          
SEQRES  33 A  502  ILE PHE LEU LEU CYS TRP LEU PRO TYR ASN LEU VAL LEU          
SEQRES  34 A  502  LEU ALA ASP THR LEU MET ARG THR GLN VAL ILE GLN GLU          
SEQRES  35 A  502  THR CYS GLU ARG ARG ASN HIS ILE ASP ARG ALA LEU ASP          
SEQRES  36 A  502  ALA THR GLU ILE LEU ALA ILE LEU HIS SER CYS LEU ASN          
SEQRES  37 A  502  PRO LEU ILE TYR ALA PHE ILE GLY GLN LYS PHE ARG HIS          
SEQRES  38 A  502  GLY LEU LEU LYS ILE LEU ALA ILE HIS GLY LEU ILE SER          
SEQRES  39 A  502  LYS ASP SER LEU PRO LYS ASP SER                              
HET    EBX  A1201      31                                                       
HETNAM     EBX 4-[[3,4-BIS(OXIDANYLIDENE)-2-[[(1~{R})-1-(4-PROPAN-2-            
HETNAM   2 EBX  YLFURAN-2-YL)PROPYL]AMINO]CYCLOBUTEN-1-YL]AMINO]-~{N},          
HETNAM   3 EBX  ~{N}-DIMETHYL-3-OXIDANYL-PYRIDINE-2-CARBOXAMIDE                 
FORMUL   2  EBX    C22 H26 N4 O5                                                
HELIX    1 AA1 ASN A   47  SER A   76  1                                  30    
HELIX    2 AA2 SER A   81  ASN A  110  1                                  30    
HELIX    3 AA3 GLY A  115  VAL A  149  1                                  35    
HELIX    4 AA4 TYR A  160  ALA A  177  1                                  18    
HELIX    5 AA5 PRO A  179  ARG A  184  1                                   6    
HELIX    6 AA6 ASN A  206  GLY A  219  1                                  14    
HELIX    7 AA7 PHE A  220  ALA A  241  1                                  22    
HELIX    8 AA8 SER A 1015  PHE A 1027  1                                  13    
HELIX    9 AA9 GLY A 1047  SER A 1059  1                                  13    
HELIX   10 AB1 LYS A 1061  GLN A 1065  5                                   5    
HELIX   11 AB2 ASP A 1076  HIS A 1090  1                                  15    
HELIX   12 AB3 SER A 1101  VAL A 1112  1                                  12    
HELIX   13 AB4 GLY A 1125  LEU A 1134  1                                  10    
HELIX   14 AB5 GLY A 1145  ILE A 1150  1                                   6    
HELIX   15 AB6 ASP A 1162  SER A 1177  1                                  16    
HELIX   16 AB7 LEU A 1181  GLY A  244  1                                  17    
HELIX   17 AB8 LYS A  246  THR A  279  1                                  34    
HELIX   18 AB9 ASN A  290  SER A  307  1                                  18    
HELIX   19 AC1 CYS A  308  ILE A  317  1                                  10    
HELIX   20 AC2 GLY A  318  HIS A  332  1                                  15    
SHEET    1 AA1 2 ARG A 185  VAL A 187  0                                        
SHEET    2 AA1 2 ALA A 195  TYR A 197 -1  O  ALA A 195   N  VAL A 187           
SHEET    1 AA2 6 VAL A1093  ILE A1096  0                                        
SHEET    2 AA2 6 MET A1067  ILE A1072  1  N  ILE A1071   O  LYS A1094           
SHEET    3 AA2 6 VAL A1033  PHE A1037  1  N  VAL A1033   O  ARG A1068           
SHEET    4 AA2 6 PHE A1114  ILE A1117  1  O  ILE A1116   N  MET A1036           
SHEET    5 AA2 6 ILE A1137  SER A1141  1  O  ILE A1139   N  VAL A1115           
SHEET    6 AA2 6 ILE A1156  VAL A1158  1  O  ILE A1156   N  PRO A1138           
SSBOND   1 CYS A  119    CYS A  196                          1555   1555  2.03  
SITE     1 AC1 14 VAL A  72  SER A  76  GLY A  79  SER A  81                    
SITE     2 AC1 14 THR A  83  ASP A  84  ARG A 144  GLU A 249                    
SITE     3 AC1 14 ILE A 253  TYR A 314  GLY A 318  GLN A 319                    
SITE     4 AC1 14 LYS A 320  PHE A 321                                          
CRYST1   41.300  108.460   82.600  90.00  91.16  90.00 P 1 21 1      2          
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      0.024213  0.000000  0.000490        0.00000                         
SCALE2      0.000000  0.009220  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012109        0.00000                         
ATOM      1  N   ILE A  46      69.330 -26.230 148.881  1.00164.21           N  
ANISOU    1  N   ILE A  46    23143  20329  18921  -1024   4962     94       N  
ATOM      2  CA  ILE A  46      68.391 -25.128 149.113  1.00164.58           C  
ANISOU    2  CA  ILE A  46    23433  20391  18709   -787   4937    211       C  
ATOM      3  C   ILE A  46      67.770 -25.215 150.542  1.00165.40           C  
ANISOU    3  C   ILE A  46    23197  20748  18899   -830   4554    164       C  
ATOM      4  O   ILE A  46      68.414 -25.765 151.441  1.00163.15           O  
ANISOU    4  O   ILE A  46    22537  20503  18951  -1077   4436     25       O  
ATOM      5  CB  ILE A  46      67.333 -24.997 147.963  1.00168.96           C  
ANISOU    5  CB  ILE A  46    24382  21050  18766   -426   4914    375       C  
ATOM      6  CG1 ILE A  46      66.503 -26.286 147.758  1.00167.42           C  
ANISOU    6  CG1 ILE A  46    23984  21239  18388   -334   4512    366       C  
ATOM      7  CG2 ILE A  46      67.980 -24.533 146.652  1.00172.46           C  
ANISOU    7  CG2 ILE A  46    25252  21165  19108   -352   5371    442       C  
ATOM      8  CD1 ILE A  46      65.015 -26.067 147.871  1.00172.48           C  
ANISOU    8  CD1 ILE A  46    24715  22158  18662    -27   4207    449       C  
ATOM      9  N   ASN A  47      66.539 -24.667 150.745  1.00161.42           N  
ANISOU    9  N   ASN A  47    22836  20408  18090   -578   4366    273       N  
ATOM     10  CA  ASN A  47      65.795 -24.658 152.018  1.00158.87           C  
ANISOU   10  CA  ASN A  47    22250  20317  17796   -577   4020    249       C  
ATOM     11  C   ASN A  47      65.542 -26.064 152.584  1.00158.97           C  
ANISOU   11  C   ASN A  47    21858  20641  17905   -684   3643    164       C  
ATOM     12  O   ASN A  47      65.229 -26.195 153.768  1.00156.39           O  
ANISOU   12  O   ASN A  47    21261  20462  17698   -754   3396    113       O  
ATOM     13  CB  ASN A  47      64.455 -23.914 151.862  1.00160.71           C  
ANISOU   13  CB  ASN A  47    22749  20671  17644   -256   3904    385       C  
ATOM     14  CG  ASN A  47      64.575 -22.453 151.492  1.00187.42           C  
ANISOU   14  CG  ASN A  47    26531  23757  20923   -129   4258    480       C  
ATOM     15  OD1 ASN A  47      65.085 -21.626 152.256  1.00182.05           O  
ANISOU   15  OD1 ASN A  47    25809  22888  20473   -267   4415    438       O  
ATOM     16  ND2 ASN A  47      64.083 -22.101 150.313  1.00181.70           N  
ANISOU   16  ND2 ASN A  47    26211  22987  19840    152   4393    607       N  
ATOM     17  N   LYS A  48      65.678 -27.103 151.732  1.00155.21           N  
ANISOU   17  N   LYS A  48    21352  20249  17372   -690   3620    150       N  
ATOM     18  CA  LYS A  48      65.487 -28.519 152.053  1.00152.84           C  
ANISOU   18  CA  LYS A  48    20702  20216  17152   -784   3320     73       C  
ATOM     19  C   LYS A  48      66.422 -29.030 153.156  1.00155.34           C  
ANISOU   19  C   LYS A  48    20644  20505  17871  -1075   3261    -58       C  
ATOM     20  O   LYS A  48      65.975 -29.787 154.019  1.00152.63           O  
ANISOU   20  O   LYS A  48    20011  20394  17586  -1114   2961   -104       O  
ATOM     21  CB  LYS A  48      65.595 -29.385 150.784  1.00155.88           C  
ANISOU   21  CB  LYS A  48    21176  20642  17408   -738   3382     82       C  
ATOM     22  CG  LYS A  48      64.398 -29.231 149.848  1.00171.85           C  
ANISOU   22  CG  LYS A  48    23475  22822  19000   -410   3292    178       C  
ATOM     23  CD  LYS A  48      64.502 -30.110 148.608  1.00182.44           C  
ANISOU   23  CD  LYS A  48    24897  24213  20208   -357   3343    171       C  
ATOM     24  CE  LYS A  48      63.326 -29.913 147.680  1.00191.80           C  
ANISOU   24  CE  LYS A  48    26361  25559  20954     -2   3245    242       C  
ATOM     25  NZ  LYS A  48      63.352 -30.868 146.540  1.00198.40           N  
ANISOU   25  NZ  LYS A  48    27237  26488  21657     58   3248    212       N  
ATOM     26  N   TYR A  49      67.704 -28.599 153.140  1.00153.44           N  
ANISOU   26  N   TYR A  49    20416  19977  17907  -1265   3553   -130       N  
ATOM     27  CA  TYR A  49      68.719 -28.981 154.133  1.00152.32           C  
ANISOU   27  CA  TYR A  49    19931  19785  18157  -1525   3517   -282       C  
ATOM     28  C   TYR A  49      68.328 -28.522 155.555  1.00151.61           C  
ANISOU   28  C   TYR A  49    19669  19793  18144  -1528   3304   -314       C  
ATOM     29  O   TYR A  49      68.478 -29.285 156.509  1.00149.47           O  
ANISOU   29  O   TYR A  49    19075  19668  18047  -1637   3071   -403       O  
ATOM     30  CB  TYR A  49      70.132 -28.495 153.698  1.00156.74           C  
ANISOU   30  CB  TYR A  49    20564  19997  18993  -1707   3905   -377       C  
ATOM     31  N   PHE A  50      67.792 -27.288 155.665  1.00146.47           N  
ANISOU   31  N   PHE A  50    19250  19059  17343  -1392   3388   -235       N  
ATOM     32  CA  PHE A  50      67.348 -26.639 156.899  1.00144.19           C  
ANISOU   32  CA  PHE A  50    18861  18835  17091  -1371   3227   -249       C  
ATOM     33  C   PHE A  50      66.183 -27.397 157.538  1.00141.39           C  
ANISOU   33  C   PHE A  50    18337  18812  16572  -1263   2836   -205       C  
ATOM     34  O   PHE A  50      66.194 -27.621 158.747  1.00139.42           O  
ANISOU   34  O   PHE A  50    17834  18665  16475  -1342   2634   -277       O  
ATOM     35  CB  PHE A  50      66.992 -25.162 156.610  1.00148.13           C  
ANISOU   35  CB  PHE A  50    19698  19151  17433  -1231   3452   -156       C  
ATOM     36  CG  PHE A  50      65.905 -24.527 157.452  1.00149.29           C  
ANISOU   36  CG  PHE A  50    19864  19440  17420  -1087   3244    -88       C  
ATOM     37  CD1 PHE A  50      66.203 -23.950 158.681  1.00152.23           C  
ANISOU   37  CD1 PHE A  50    20068  19766  18006  -1194   3200   -176       C  
ATOM     38  CD2 PHE A  50      64.593 -24.464 156.992  1.00151.64           C  
ANISOU   38  CD2 PHE A  50    20350  19912  17355   -835   3098     51       C  
ATOM     39  CE1 PHE A  50      65.202 -23.340 159.445  1.00152.69           C  
ANISOU   39  CE1 PHE A  50    20153  19944  17918  -1065   3022   -111       C  
ATOM     40  CE2 PHE A  50      63.590 -23.873 157.767  1.00154.00           C  
ANISOU   40  CE2 PHE A  50    20660  20334  17519   -707   2913    104       C  
ATOM     41  CZ  PHE A  50      63.900 -23.319 158.990  1.00151.63           C  
ANISOU   41  CZ  PHE A  50    20200  19979  17434   -828   2881     31       C  
ATOM     42  N   VAL A  51      65.189 -27.789 156.720  1.00134.40           N  
ANISOU   42  N   VAL A  51    17597  18087  15381  -1076   2741   -102       N  
ATOM     43  CA  VAL A  51      63.997 -28.520 157.145  1.00130.85           C  
ANISOU   43  CA  VAL A  51    17007  17941  14767   -960   2406    -76       C  
ATOM     44  C   VAL A  51      64.397 -29.806 157.874  1.00129.13           C  
ANISOU   44  C   VAL A  51    16431  17860  14774  -1129   2220   -177       C  
ATOM     45  O   VAL A  51      63.939 -30.019 158.998  1.00127.27           O  
ANISOU   45  O   VAL A  51    16007  17763  14586  -1136   1997   -202       O  
ATOM     46  CB  VAL A  51      63.016 -28.760 155.960  1.00135.33           C  
ANISOU   46  CB  VAL A  51    17784  18641  14995   -735   2370     10       C  
ATOM     47  CG1 VAL A  51      61.871 -29.695 156.345  1.00133.48           C  
ANISOU   47  CG1 VAL A  51    17355  18716  14645   -646   2043    -10       C  
ATOM     48  CG2 VAL A  51      62.465 -27.438 155.431  1.00136.95           C  
ANISOU   48  CG2 VAL A  51    18353  18736  14947   -521   2513    118       C  
ATOM     49  N   VAL A  52      65.303 -30.614 157.266  1.00122.94           N  
ANISOU   49  N   VAL A  52    15566  17013  14135  -1265   2331   -234       N  
ATOM     50  CA  VAL A  52      65.800 -31.885 157.821  1.00119.85           C  
ANISOU   50  CA  VAL A  52    14854  16726  13957  -1420   2189   -328       C  
ATOM     51  C   VAL A  52      66.496 -31.660 159.179  1.00120.68           C  
ANISOU   51  C   VAL A  52    14749  16772  14330  -1555   2125   -423       C  
ATOM     52  O   VAL A  52      66.280 -32.450 160.105  1.00118.48           O  
ANISOU   52  O   VAL A  52    14239  16655  14122  -1580   1901   -462       O  
ATOM     53  CB  VAL A  52      66.663 -32.703 156.819  1.00123.80           C  
ANISOU   53  CB  VAL A  52    15332  17149  14556  -1534   2346   -369       C  
ATOM     54  CG1 VAL A  52      66.959 -34.101 157.356  1.00121.96           C  
ANISOU   54  CG1 VAL A  52    14781  17059  14499  -1656   2176   -449       C  
ATOM     55  CG2 VAL A  52      65.976 -32.810 155.461  1.00124.37           C  
ANISOU   55  CG2 VAL A  52    15639  17274  14341  -1376   2413   -283       C  
ATOM     56  N   ILE A  53      67.265 -30.550 159.310  1.00116.82           N  
ANISOU   56  N   ILE A  53    14353  16054  13978  -1622   2326   -465       N  
ATOM     57  CA  ILE A  53      67.938 -30.152 160.556  1.00115.37           C  
ANISOU   57  CA  ILE A  53    13986  15806  14044  -1732   2277   -581       C  
ATOM     58  C   ILE A  53      66.895 -29.944 161.671  1.00115.71           C  
ANISOU   58  C   ILE A  53    13975  16025  13964  -1617   2021   -534       C  
ATOM     59  O   ILE A  53      66.981 -30.612 162.697  1.00113.11           O  
ANISOU   59  O   ILE A  53    13412  15815  13751  -1659   1817   -600       O  
ATOM     60  CB  ILE A  53      68.875 -28.919 160.345  1.00120.08           C  
ANISOU   60  CB  ILE A  53    14708  16109  14809  -1820   2580   -653       C  
ATOM     61  CG1 ILE A  53      70.211 -29.350 159.715  1.00121.16           C  
ANISOU   61  CG1 ILE A  53    14768  16070  15197  -1997   2794   -773       C  
ATOM     62  CG2 ILE A  53      69.103 -28.117 161.647  1.00120.86           C  
ANISOU   62  CG2 ILE A  53    14683  16169  15071  -1860   2509   -752       C  
ATOM     63  CD1 ILE A  53      71.114 -28.188 159.230  1.00131.21           C  
ANISOU   63  CD1 ILE A  53    16204  17020  16630  -2084   3164   -846       C  
ATOM     64  N   ILE A  54      65.893 -29.066 161.428  1.00112.12           N  
ANISOU   64  N   ILE A  54    13751  15586  13265  -1458   2036   -418       N  
ATOM     65  CA  ILE A  54      64.803 -28.731 162.355  1.00110.83           C  
ANISOU   65  CA  ILE A  54    13576  15570  12964  -1338   1823   -364       C  
ATOM     66  C   ILE A  54      64.001 -29.975 162.720  1.00112.94           C  
ANISOU   66  C   ILE A  54    13675  16089  13148  -1287   1561   -347       C  
ATOM     67  O   ILE A  54      63.651 -30.156 163.886  1.00111.06           O  
ANISOU   67  O   ILE A  54    13290  15956  12952  -1279   1371   -371       O  
ATOM     68  CB  ILE A  54      63.889 -27.588 161.801  1.00114.86           C  
ANISOU   68  CB  ILE A  54    14387  16039  13218  -1164   1913   -243       C  
ATOM     69  CG1 ILE A  54      64.696 -26.378 161.241  1.00117.45           C  
ANISOU   69  CG1 ILE A  54    14925  16082  13618  -1207   2239   -250       C  
ATOM     70  CG2 ILE A  54      62.837 -27.130 162.824  1.00114.37           C  
ANISOU   70  CG2 ILE A  54    14304  16107  13046  -1056   1708   -202       C  
ATOM     71  CD1 ILE A  54      65.823 -25.706 162.156  1.00127.09           C  
ANISOU   71  CD1 ILE A  54    16011  17123  15155  -1378   2345   -389       C  
ATOM     72  N   TYR A  55      63.732 -30.835 161.728  1.00110.03           N  
ANISOU   72  N   TYR A  55    13331  15806  12670  -1253   1569   -314       N  
ATOM     73  CA  TYR A  55      62.991 -32.075 161.924  1.00108.90           C  
ANISOU   73  CA  TYR A  55    13029  15885  12465  -1214   1366   -315       C  
ATOM     74  C   TYR A  55      63.750 -33.017 162.857  1.00110.90           C  
ANISOU   74  C   TYR A  55    13014  16166  12956  -1352   1270   -404       C  
ATOM     75  O   TYR A  55      63.151 -33.534 163.793  1.00109.09           O  
ANISOU   75  O   TYR A  55    12656  16075  12719  -1314   1086   -408       O  
ATOM     76  CB  TYR A  55      62.676 -32.743 160.574  1.00111.27           C  
ANISOU   76  CB  TYR A  55    13408  16250  12621  -1160   1425   -287       C  
ATOM     77  CG  TYR A  55      61.401 -32.290 159.879  1.00114.80           C  
ANISOU   77  CG  TYR A  55    14055  16795  12768   -952   1388   -212       C  
ATOM     78  CD1 TYR A  55      60.933 -30.983 160.012  1.00117.68           C  
ANISOU   78  CD1 TYR A  55    14623  17088  13000   -835   1426   -148       C  
ATOM     79  CD2 TYR A  55      60.712 -33.143 159.022  1.00116.08           C  
ANISOU   79  CD2 TYR A  55    14206  17119  12782   -863   1323   -220       C  
ATOM     80  CE1 TYR A  55      59.780 -30.556 159.352  1.00119.80           C  
ANISOU   80  CE1 TYR A  55    15081  17452  12986   -621   1382    -88       C  
ATOM     81  CE2 TYR A  55      59.566 -32.724 158.346  1.00118.12           C  
ANISOU   81  CE2 TYR A  55    14640  17480  12762   -650   1272   -180       C  
ATOM     82  CZ  TYR A  55      59.102 -31.430 158.514  1.00127.34           C  
ANISOU   82  CZ  TYR A  55    16014  18579  13791   -521   1297   -111       C  
ATOM     83  OH  TYR A  55      57.974 -31.021 157.839  1.00129.29           O  
ANISOU   83  OH  TYR A  55    16437  18933  13755   -288   1235    -79       O  
ATOM     84  N   ALA A  56      65.072 -33.185 162.644  1.00107.86           N  
ANISOU   84  N   ALA A  56    12558  15639  12785  -1500   1404   -481       N  
ATOM     85  CA  ALA A  56      65.927 -34.036 163.480  1.00106.84           C  
ANISOU   85  CA  ALA A  56    12183  15525  12888  -1616   1319   -580       C  
ATOM     86  C   ALA A  56      66.136 -33.435 164.875  1.00109.99           C  
ANISOU   86  C   ALA A  56    12498  15900  13393  -1616   1210   -637       C  
ATOM     87  O   ALA A  56      66.215 -34.174 165.857  1.00108.67           O  
ANISOU   87  O   ALA A  56    12156  15827  13308  -1620   1048   -682       O  
ATOM     88  CB  ALA A  56      67.266 -34.257 162.800  1.00108.47           C  
ANISOU   88  CB  ALA A  56    12343  15577  13296  -1765   1499   -664       C  
ATOM     89  N   LEU A  57      66.211 -32.091 164.947  1.00107.02           N  
ANISOU   89  N   LEU A  57    12260  15396  13006  -1601   1309   -635       N  
ATOM     90  CA  LEU A  57      66.388 -31.295 166.159  1.00106.51           C  
ANISOU   90  CA  LEU A  57    12142  15296  13033  -1598   1231   -698       C  
ATOM     91  C   LEU A  57      65.149 -31.409 167.054  1.00107.29           C  
ANISOU   91  C   LEU A  57    12236  15568  12961  -1466   1014   -619       C  
ATOM     92  O   LEU A  57      65.293 -31.692 168.244  1.00107.13           O  
ANISOU   92  O   LEU A  57    12071  15608  13024  -1461    857   -678       O  
ATOM     93  CB  LEU A  57      66.649 -29.831 165.771  1.00108.28           C  
ANISOU   93  CB  LEU A  57    12543  15329  13269  -1613   1437   -703       C  
ATOM     94  CG  LEU A  57      67.110 -28.900 166.873  1.00114.07           C  
ANISOU   94  CG  LEU A  57    13206  15982  14152  -1645   1414   -810       C  
ATOM     95  CD1 LEU A  57      68.453 -28.285 166.525  1.00116.13           C  
ANISOU   95  CD1 LEU A  57    13443  16013  14666  -1788   1652   -958       C  
ATOM     96  CD2 LEU A  57      66.064 -27.829 167.145  1.00116.42           C  
ANISOU   96  CD2 LEU A  57    13680  16291  14262  -1527   1398   -708       C  
ATOM     97  N   VAL A  58      63.938 -31.210 166.481  1.00100.98           N  
ANISOU   97  N   VAL A  58    11597  14846  11923  -1351   1007   -498       N  
ATOM     98  CA  VAL A  58      62.669 -31.315 167.208  1.00 98.49           C  
ANISOU   98  CA  VAL A  58    11286  14686  11448  -1227    826   -432       C  
ATOM     99  C   VAL A  58      62.464 -32.759 167.684  1.00 99.34           C  
ANISOU   99  C   VAL A  58    11217  14939  11587  -1228    681   -451       C  
ATOM    100  O   VAL A  58      62.190 -32.963 168.863  1.00 97.76           O  
ANISOU  100  O   VAL A  58    10935  14806  11405  -1190    538   -463       O  
ATOM    101  CB  VAL A  58      61.468 -30.740 166.401  1.00102.25           C  
ANISOU  101  CB  VAL A  58    11966  15208  11676  -1095    857   -328       C  
ATOM    102  CG1 VAL A  58      60.124 -31.169 166.988  1.00100.91           C  
ANISOU  102  CG1 VAL A  58    11760  15216  11364   -980    674   -287       C  
ATOM    103  CG2 VAL A  58      61.548 -29.218 166.310  1.00103.07           C  
ANISOU  103  CG2 VAL A  58    12255  15168  11740  -1066    982   -298       C  
ATOM    104  N   PHE A  59      62.681 -33.747 166.785  1.00 95.69           N  
ANISOU  104  N   PHE A  59    10707  14511  11141  -1274    738   -456       N  
ATOM    105  CA  PHE A  59      62.572 -35.191 167.034  1.00 94.87           C  
ANISOU  105  CA  PHE A  59    10442  14523  11080  -1287    651   -476       C  
ATOM    106  C   PHE A  59      63.226 -35.609 168.343  1.00102.01           C  
ANISOU  106  C   PHE A  59    11195  15424  12139  -1316    545   -539       C  
ATOM    107  O   PHE A  59      62.628 -36.376 169.106  1.00100.87           O  
ANISOU  107  O   PHE A  59    10982  15383  11960  -1254    431   -523       O  
ATOM    108  CB  PHE A  59      63.199 -35.985 165.874  1.00 96.38           C  
ANISOU  108  CB  PHE A  59    10595  14695  11329  -1373    769   -498       C  
ATOM    109  CG  PHE A  59      63.425 -37.460 166.124  1.00 96.60           C  
ANISOU  109  CG  PHE A  59    10445  14804  11455  -1417    716   -534       C  
ATOM    110  CD1 PHE A  59      62.380 -38.369 166.012  1.00 98.11           C  
ANISOU  110  CD1 PHE A  59    10595  15138  11546  -1354    661   -507       C  
ATOM    111  CD2 PHE A  59      64.690 -37.943 166.441  1.00 98.58           C  
ANISOU  111  CD2 PHE A  59    10565  14982  11910  -1518    736   -608       C  
ATOM    112  CE1 PHE A  59      62.592 -39.733 166.213  1.00 98.15           C  
ANISOU  112  CE1 PHE A  59    10445  15199  11647  -1395    646   -539       C  
ATOM    113  CE2 PHE A  59      64.898 -39.308 166.662  1.00100.43           C  
ANISOU  113  CE2 PHE A  59    10649  15284  12227  -1545    698   -633       C  
ATOM    114  CZ  PHE A  59      63.850 -40.195 166.531  1.00 97.50           C  
ANISOU  114  CZ  PHE A  59    10254  15042  11749  -1486    665   -590       C  
ATOM    115  N   LEU A  60      64.472 -35.137 168.574  1.00101.47           N  
ANISOU  115  N   LEU A  60    11078  15232  12242  -1401    591   -623       N  
ATOM    116  CA  LEU A  60      65.254 -35.455 169.769  1.00102.04           C  
ANISOU  116  CA  LEU A  60    11006  15300  12464  -1410    480   -712       C  
ATOM    117  C   LEU A  60      64.726 -34.736 171.001  1.00105.30           C  
ANISOU  117  C   LEU A  60    11457  15741  12813  -1314    352   -703       C  
ATOM    118  O   LEU A  60      64.495 -35.382 172.024  1.00103.93           O  
ANISOU  118  O   LEU A  60    11215  15646  12626  -1240    217   -704       O  
ATOM    119  CB  LEU A  60      66.747 -35.192 169.540  1.00103.59           C  
ANISOU  119  CB  LEU A  60    11115  15361  12882  -1529    569   -842       C  
ATOM    120  CG  LEU A  60      67.387 -36.062 168.452  1.00109.60           C  
ANISOU  120  CG  LEU A  60    11820  16090  13734  -1631    690   -863       C  
ATOM    121  CD1 LEU A  60      68.647 -35.424 167.913  1.00111.81           C  
ANISOU  121  CD1 LEU A  60    12076  16197  14211  -1757    844   -983       C  
ATOM    122  CD2 LEU A  60      67.663 -37.485 168.945  1.00112.11           C  
ANISOU  122  CD2 LEU A  60    11979  16500  14117  -1619    587   -888       C  
ATOM    123  N   LEU A  61      64.462 -33.421 170.877  1.00102.28           N  
ANISOU  123  N   LEU A  61    11198  15289  12376  -1306    408   -684       N  
ATOM    124  CA  LEU A  61      63.906 -32.585 171.940  1.00102.12           C  
ANISOU  124  CA  LEU A  61    11229  15284  12289  -1224    306   -672       C  
ATOM    125  C   LEU A  61      62.527 -33.074 172.416  1.00106.02           C  
ANISOU  125  C   LEU A  61    11768  15911  12605  -1108    194   -569       C  
ATOM    126  O   LEU A  61      62.153 -32.832 173.566  1.00105.80           O  
ANISOU  126  O   LEU A  61    11740  15917  12542  -1033     77   -569       O  
ATOM    127  CB  LEU A  61      63.832 -31.131 171.474  1.00102.87           C  
ANISOU  127  CB  LEU A  61    11464  15267  12353  -1243    429   -658       C  
ATOM    128  CG  LEU A  61      65.077 -30.307 171.734  1.00108.88           C  
ANISOU  128  CG  LEU A  61    12168  15885  13317  -1333    504   -798       C  
ATOM    129  CD1 LEU A  61      65.329 -29.326 170.604  1.00110.11           C  
ANISOU  129  CD1 LEU A  61    12465  15889  13485  -1398    735   -786       C  
ATOM    130  CD2 LEU A  61      64.977 -29.578 173.061  1.00111.96           C  
ANISOU  130  CD2 LEU A  61    12534  16286  13722  -1276    381   -851       C  
ATOM    131  N   SER A  62      61.778 -33.756 171.533  1.00102.22           N  
ANISOU  131  N   SER A  62    11318  15500  12019  -1093    238   -499       N  
ATOM    132  CA  SER A  62      60.465 -34.313 171.855  1.00101.52           C  
ANISOU  132  CA  SER A  62    11250  15531  11793   -998    162   -434       C  
ATOM    133  C   SER A  62      60.611 -35.686 172.472  1.00104.99           C  
ANISOU  133  C   SER A  62    11565  16031  12295   -987    103   -455       C  
ATOM    134  O   SER A  62      59.941 -35.978 173.461  1.00103.97           O  
ANISOU  134  O   SER A  62    11437  15951  12114   -904     20   -433       O  
ATOM    135  CB  SER A  62      59.576 -34.374 170.619  1.00105.85           C  
ANISOU  135  CB  SER A  62    11876  16133  12211   -975    234   -383       C  
ATOM    136  OG  SER A  62      60.278 -34.902 169.509  1.00118.90           O  
ANISOU  136  OG  SER A  62    13493  17760  13924  -1057    338   -406       O  
ATOM    137  N   LEU A  63      61.504 -36.523 171.906  1.00102.08           N  
ANISOU  137  N   LEU A  63    11100  15646  12040  -1066    160   -497       N  
ATOM    138  CA  LEU A  63      61.773 -37.868 172.408  1.00101.52           C  
ANISOU  138  CA  LEU A  63    10918  15618  12038  -1054    127   -516       C  
ATOM    139  C   LEU A  63      62.198 -37.804 173.880  1.00105.35           C  
ANISOU  139  C   LEU A  63    11377  16086  12564   -980      8   -549       C  
ATOM    140  O   LEU A  63      61.440 -38.245 174.742  1.00103.66           O  
ANISOU  140  O   LEU A  63    11189  15920  12276   -883    -48   -509       O  
ATOM    141  CB  LEU A  63      62.852 -38.564 171.558  1.00101.68           C  
ANISOU  141  CB  LEU A  63    10841  15604  12190  -1160    210   -566       C  
ATOM    142  CG  LEU A  63      62.459 -39.893 170.928  1.00105.62           C  
ANISOU  142  CG  LEU A  63    11277  16172  12681  -1179    274   -544       C  
ATOM    143  CD1 LEU A  63      63.558 -40.402 170.038  1.00107.91           C  
ANISOU  143  CD1 LEU A  63    11484  16415  13101  -1294    362   -593       C  
ATOM    144  CD2 LEU A  63      62.145 -40.952 171.987  1.00105.49           C  
ANISOU  144  CD2 LEU A  63    11208  16204  12670  -1098    221   -532       C  
ATOM    145  N   LEU A  64      63.356 -37.171 174.160  1.00103.19           N  
ANISOU  145  N   LEU A  64    11062  15741  12406  -1019    -24   -633       N  
ATOM    146  CA  LEU A  64      63.900 -36.992 175.505  1.00103.70           C  
ANISOU  146  CA  LEU A  64    11093  15796  12513   -936   -155   -698       C  
ATOM    147  C   LEU A  64      62.887 -36.261 176.380  1.00106.77           C  
ANISOU  147  C   LEU A  64    11592  16209  12768   -837   -230   -642       C  
ATOM    148  O   LEU A  64      62.516 -36.776 177.438  1.00107.06           O  
ANISOU  148  O   LEU A  64    11647  16284  12745   -721   -317   -622       O  
ATOM    149  CB  LEU A  64      65.249 -36.234 175.478  1.00105.22           C  
ANISOU  149  CB  LEU A  64    11206  15903  12870  -1009   -161   -835       C  
ATOM    150  CG  LEU A  64      66.284 -36.631 174.394  1.00111.46           C  
ANISOU  150  CG  LEU A  64    11898  16635  13817  -1141    -51   -905       C  
ATOM    151  CD1 LEU A  64      67.439 -35.641 174.346  1.00113.20           C  
ANISOU  151  CD1 LEU A  64    12053  16749  14208  -1222    -23  -1057       C  
ATOM    152  CD2 LEU A  64      66.802 -38.067 174.570  1.00114.57           C  
ANISOU  152  CD2 LEU A  64    12184  17074  14273  -1114    -89   -928       C  
ATOM    153  N   GLY A  65      62.393 -35.124 175.881  1.00101.49           N  
ANISOU  153  N   GLY A  65    11007  15511  12042   -877   -179   -611       N  
ATOM    154  CA  GLY A  65      61.421 -34.271 176.555  1.00 99.90           C  
ANISOU  154  CA  GLY A  65    10913  15323  11721   -800   -234   -560       C  
ATOM    155  C   GLY A  65      60.231 -35.012 177.119  1.00100.68           C  
ANISOU  155  C   GLY A  65    11060  15495  11698   -702   -269   -478       C  
ATOM    156  O   GLY A  65      60.089 -35.105 178.339  1.00 99.88           O  
ANISOU  156  O   GLY A  65    10983  15405  11562   -603   -361   -479       O  
ATOM    157  N   ASN A  66      59.381 -35.559 176.228  1.00 95.64           N  
ANISOU  157  N   ASN A  66    10437  14903  11000   -724   -186   -422       N  
ATOM    158  CA  ASN A  66      58.160 -36.297 176.582  1.00 93.76           C  
ANISOU  158  CA  ASN A  66    10228  14724  10674   -650   -179   -371       C  
ATOM    159  C   ASN A  66      58.425 -37.587 177.356  1.00 95.52           C  
ANISOU  159  C   ASN A  66    10399  14954  10938   -594   -187   -377       C  
ATOM    160  O   ASN A  66      57.606 -37.940 178.203  1.00 94.56           O  
ANISOU  160  O   ASN A  66    10332  14843  10753   -505   -194   -345       O  
ATOM    161  CB  ASN A  66      57.291 -36.554 175.355  1.00 92.26           C  
ANISOU  161  CB  ASN A  66    10037  14586  10430   -686    -91   -352       C  
ATOM    162  CG  ASN A  66      56.711 -35.280 174.793  1.00117.97           C  
ANISOU  162  CG  ASN A  66    13387  17842  13596   -683    -90   -329       C  
ATOM    163  OD1 ASN A  66      55.703 -34.755 175.278  1.00113.38           O  
ANISOU  163  OD1 ASN A  66    12874  17278  12925   -614   -130   -303       O  
ATOM    164  ND2 ASN A  66      57.348 -34.736 173.769  1.00111.79           N  
ANISOU  164  ND2 ASN A  66    12619  17026  12832   -750    -33   -337       N  
ATOM    165  N   SER A  67      59.570 -38.271 177.097  1.00 91.03           N  
ANISOU  165  N   SER A  67     9740  14370  10476   -639   -176   -420       N  
ATOM    166  CA  SER A  67      59.957 -39.490 177.815  1.00 90.19           C  
ANISOU  166  CA  SER A  67     9599  14265  10407   -568   -181   -424       C  
ATOM    167  C   SER A  67      60.226 -39.147 179.275  1.00 94.16           C  
ANISOU  167  C   SER A  67    10163  14743  10869   -437   -302   -435       C  
ATOM    168  O   SER A  67      59.765 -39.864 180.172  1.00 94.11           O  
ANISOU  168  O   SER A  67    10218  14734  10805   -321   -295   -396       O  
ATOM    169  CB  SER A  67      61.193 -40.126 177.191  1.00 93.07           C  
ANISOU  169  CB  SER A  67     9848  14616  10897   -643   -155   -479       C  
ATOM    170  OG  SER A  67      60.913 -40.632 175.897  1.00 99.95           O  
ANISOU  170  OG  SER A  67    10669  15513  11794   -747    -36   -466       O  
ATOM    171  N   LEU A  68      60.929 -38.017 179.509  1.00 90.23           N  
ANISOU  171  N   LEU A  68     9659  14224  10401   -451   -398   -495       N  
ATOM    172  CA  LEU A  68      61.236 -37.514 180.841  1.00 90.26           C  
ANISOU  172  CA  LEU A  68     9710  14216  10369   -328   -532   -532       C  
ATOM    173  C   LEU A  68      59.944 -37.207 181.591  1.00 93.39           C  
ANISOU  173  C   LEU A  68    10239  14617  10628   -242   -534   -452       C  
ATOM    174  O   LEU A  68      59.803 -37.634 182.731  1.00 93.11           O  
ANISOU  174  O   LEU A  68    10278  14576  10523    -98   -585   -433       O  
ATOM    175  CB  LEU A  68      62.113 -36.265 180.742  1.00 90.91           C  
ANISOU  175  CB  LEU A  68     9737  14269  10535   -394   -600   -634       C  
ATOM    176  CG  LEU A  68      63.191 -36.134 181.803  1.00 97.02           C  
ANISOU  176  CG  LEU A  68    10460  15042  11361   -293   -747   -755       C  
ATOM    177  CD1 LEU A  68      64.394 -36.999 181.469  1.00 97.75           C  
ANISOU  177  CD1 LEU A  68    10425  15136  11581   -309   -757   -842       C  
ATOM    178  CD2 LEU A  68      63.630 -34.699 181.935  1.00100.78           C  
ANISOU  178  CD2 LEU A  68    10906  15483  11902   -350   -796   -856       C  
ATOM    179  N   VAL A  69      58.978 -36.541 180.914  1.00 89.66           N  
ANISOU  179  N   VAL A  69     9803  14150  10113   -320   -470   -405       N  
ATOM    180  CA  VAL A  69      57.647 -36.161 181.419  1.00 88.86           C  
ANISOU  180  CA  VAL A  69     9812  14051   9899   -263   -458   -341       C  
ATOM    181  C   VAL A  69      56.814 -37.408 181.808  1.00 93.48           C  
ANISOU  181  C   VAL A  69    10439  14638  10442   -188   -372   -291       C  
ATOM    182  O   VAL A  69      56.236 -37.426 182.897  1.00 92.94           O  
ANISOU  182  O   VAL A  69    10473  14543  10297    -78   -388   -259       O  
ATOM    183  CB  VAL A  69      56.918 -35.204 180.426  1.00 91.39           C  
ANISOU  183  CB  VAL A  69    10148  14385  10193   -354   -411   -320       C  
ATOM    184  CG1 VAL A  69      55.455 -34.985 180.801  1.00 90.43           C  
ANISOU  184  CG1 VAL A  69    10115  14272   9970   -299   -389   -269       C  
ATOM    185  CG2 VAL A  69      57.642 -33.866 180.332  1.00 91.48           C  
ANISOU  185  CG2 VAL A  69    10158  14364  10239   -404   -469   -364       C  
ATOM    186  N   MET A  70      56.804 -38.455 180.952  1.00 91.10           N  
ANISOU  186  N   MET A  70    10062  14355  10197   -247   -266   -290       N  
ATOM    187  CA  MET A  70      56.095 -39.715 181.216  1.00 91.69           C  
ANISOU  187  CA  MET A  70    10158  14416  10263   -195   -145   -261       C  
ATOM    188  C   MET A  70      56.691 -40.433 182.418  1.00 96.27           C  
ANISOU  188  C   MET A  70    10806  14950  10822    -53   -169   -245       C  
ATOM    189  O   MET A  70      55.938 -40.987 183.213  1.00 96.42           O  
ANISOU  189  O   MET A  70    10926  14923  10786     45    -88   -205       O  
ATOM    190  CB  MET A  70      56.108 -40.641 179.996  1.00 94.32           C  
ANISOU  190  CB  MET A  70    10378  14783  10678   -297    -30   -283       C  
ATOM    191  CG  MET A  70      55.215 -40.174 178.874  1.00 98.57           C  
ANISOU  191  CG  MET A  70    10876  15372  11204   -387     16   -302       C  
ATOM    192  SD  MET A  70      55.509 -41.097 177.347  1.00103.72           S  
ANISOU  192  SD  MET A  70    11389  16076  11943   -506    120   -346       S  
ATOM    193  CE  MET A  70      54.470 -42.567 177.663  1.00100.63           C  
ANISOU  193  CE  MET A  70    10976  15671  11589   -466    292   -365       C  
ATOM    194  N   LEU A  71      58.039 -40.397 182.565  1.00 92.70           N  
ANISOU  194  N   LEU A  71    10306  14505  10413    -31   -276   -285       N  
ATOM    195  CA  LEU A  71      58.770 -40.990 183.693  1.00 92.86           C  
ANISOU  195  CA  LEU A  71    10390  14497  10398    135   -338   -287       C  
ATOM    196  C   LEU A  71      58.360 -40.318 185.020  1.00 95.73           C  
ANISOU  196  C   LEU A  71    10899  14833  10639    281   -426   -266       C  
ATOM    197  O   LEU A  71      57.918 -41.013 185.927  1.00 95.04           O  
ANISOU  197  O   LEU A  71    10944  14696  10469    430   -367   -214       O  
ATOM    198  CB  LEU A  71      60.292 -40.884 183.462  1.00 93.41           C  
ANISOU  198  CB  LEU A  71    10344  14592  10556    116   -458   -374       C  
ATOM    199  CG  LEU A  71      61.193 -41.116 184.678  1.00 99.23           C  
ANISOU  199  CG  LEU A  71    11133  15323  11246    313   -594   -417       C  
ATOM    200  CD1 LEU A  71      61.820 -42.492 184.644  1.00 99.90           C  
ANISOU  200  CD1 LEU A  71    11194  15397  11365    385   -538   -411       C  
ATOM    201  CD2 LEU A  71      62.260 -40.048 184.768  1.00102.21           C  
ANISOU  201  CD2 LEU A  71    11416  15731  11687    291   -770   -542       C  
ATOM    202  N   VAL A  72      58.482 -38.972 185.099  1.00 92.23           N  
ANISOU  202  N   VAL A  72    10442  14413  10188    239   -548   -308       N  
ATOM    203  CA  VAL A  72      58.159 -38.128 186.260  1.00 92.36           C  
ANISOU  203  CA  VAL A  72    10579  14414  10102    355   -648   -304       C  
ATOM    204  C   VAL A  72      56.693 -38.319 186.701  1.00 96.47           C  
ANISOU  204  C   VAL A  72    11237  14886  10532    399   -526   -215       C  
ATOM    205  O   VAL A  72      56.429 -38.431 187.905  1.00 98.02           O  
ANISOU  205  O   VAL A  72    11580  15039  10623    561   -545   -184       O  
ATOM    206  CB  VAL A  72      58.543 -36.633 186.023  1.00 95.80           C  
ANISOU  206  CB  VAL A  72    10946  14876  10578    262   -766   -374       C  
ATOM    207  CG1 VAL A  72      58.163 -35.754 187.213  1.00 96.05           C  
ANISOU  207  CG1 VAL A  72    11094  14894  10507    372   -862   -374       C  
ATOM    208  CG2 VAL A  72      60.031 -36.485 185.730  1.00 96.09           C  
ANISOU  208  CG2 VAL A  72    10846  14940  10726    232   -870   -492       C  
ATOM    209  N   ILE A  73      55.758 -38.413 185.744  1.00 90.84           N  
ANISOU  209  N   ILE A  73    10477  14176   9860    267   -395   -188       N  
ATOM    210  CA  ILE A  73      54.349 -38.626 186.079  1.00 90.23           C  
ANISOU  210  CA  ILE A  73    10499  14052   9733    293   -265   -138       C  
ATOM    211  C   ILE A  73      54.103 -40.065 186.579  1.00 94.89           C  
ANISOU  211  C   ILE A  73    11168  14573  10313    396   -106   -100       C  
ATOM    212  O   ILE A  73      53.450 -40.237 187.615  1.00 95.25           O  
ANISOU  212  O   ILE A  73    11368  14542  10280    516    -39    -59       O  
ATOM    213  CB  ILE A  73      53.405 -38.205 184.914  1.00 92.34           C  
ANISOU  213  CB  ILE A  73    10678  14358  10049    141   -196   -153       C  
ATOM    214  CG1 ILE A  73      53.515 -36.686 184.646  1.00 92.29           C  
ANISOU  214  CG1 ILE A  73    10651  14392  10025     76   -329   -171       C  
ATOM    215  CG2 ILE A  73      51.942 -38.603 185.191  1.00 92.70           C  
ANISOU  215  CG2 ILE A  73    10791  14354  10078    163    -47   -139       C  
ATOM    216  CD1 ILE A  73      53.007 -36.229 183.307  1.00 96.43           C  
ANISOU  216  CD1 ILE A  73    11087  14967  10584    -52   -292   -190       C  
ATOM    217  N   LEU A  74      54.656 -41.079 185.871  1.00 91.26           N  
ANISOU  217  N   LEU A  74    10614  14128   9933    351    -32   -113       N  
ATOM    218  CA  LEU A  74      54.459 -42.497 186.199  1.00 91.71           C  
ANISOU  218  CA  LEU A  74    10737  14110   9998    436    151    -79       C  
ATOM    219  C   LEU A  74      55.240 -43.021 187.411  1.00 98.70           C  
ANISOU  219  C   LEU A  74    11770  14942  10790    649    107    -40       C  
ATOM    220  O   LEU A  74      54.832 -44.047 187.968  1.00 99.73           O  
ANISOU  220  O   LEU A  74    12027  14977  10890    760    285      8       O  
ATOM    221  CB  LEU A  74      54.731 -43.401 184.992  1.00 91.08           C  
ANISOU  221  CB  LEU A  74    10502  14065  10040    311    256   -110       C  
ATOM    222  CG  LEU A  74      53.733 -43.348 183.842  1.00 94.52           C  
ANISOU  222  CG  LEU A  74    10814  14540  10558    144    361   -157       C  
ATOM    223  CD1 LEU A  74      54.327 -43.962 182.602  1.00 94.29           C  
ANISOU  223  CD1 LEU A  74    10621  14572  10632     22    390   -196       C  
ATOM    224  CD2 LEU A  74      52.426 -44.034 184.197  1.00 96.84           C  
ANISOU  224  CD2 LEU A  74    11171  14752  10871    170    582   -163       C  
ATOM    225  N   TYR A  75      56.342 -42.343 187.818  1.00 96.18           N  
ANISOU  225  N   TYR A  75    11439  14679  10428    718   -118    -73       N  
ATOM    226  CA  TYR A  75      57.196 -42.727 188.959  1.00 97.55           C  
ANISOU  226  CA  TYR A  75    11740  14827  10497    950   -211    -64       C  
ATOM    227  C   TYR A  75      56.414 -42.866 190.279  1.00102.47           C  
ANISOU  227  C   TYR A  75    12611  15352  10971   1146   -132      7       C  
ATOM    228  O   TYR A  75      56.504 -43.909 190.938  1.00102.99           O  
ANISOU  228  O   TYR A  75    12828  15338  10964   1324    -20     61       O  
ATOM    229  CB  TYR A  75      58.367 -41.744 189.119  1.00 99.03           C  
ANISOU  229  CB  TYR A  75    11839  15102  10684    972   -478   -156       C  
ATOM    230  CG  TYR A  75      59.505 -42.262 189.970  1.00102.47           C  
ANISOU  230  CG  TYR A  75    12336  15548  11048   1199   -605   -192       C  
ATOM    231  CD1 TYR A  75      60.463 -43.123 189.439  1.00104.93           C  
ANISOU  231  CD1 TYR A  75    12542  15886  11442   1198   -607   -229       C  
ATOM    232  CD2 TYR A  75      59.663 -41.842 191.287  1.00104.59           C  
ANISOU  232  CD2 TYR A  75    12763  15811  11165   1424   -740   -204       C  
ATOM    233  CE1 TYR A  75      61.534 -43.579 190.210  1.00107.87           C  
ANISOU  233  CE1 TYR A  75    12963  16278  11746   1427   -743   -278       C  
ATOM    234  CE2 TYR A  75      60.732 -42.289 192.067  1.00107.34           C  
ANISOU  234  CE2 TYR A  75    13168  16185  11432   1664   -882   -258       C  
ATOM    235  CZ  TYR A  75      61.668 -43.155 191.524  1.00115.12           C  
ANISOU  235  CZ  TYR A  75    14042  17197  12501   1669   -888   -298       C  
ATOM    236  OH  TYR A  75      62.725 -43.592 192.290  1.00116.01           O  
ANISOU  236  OH  TYR A  75    14205  17343  12530   1926  -1044   -364       O  
ATOM    237  N   SER A  76      55.636 -41.829 190.645  1.00 98.35           N  
ANISOU  237  N   SER A  76    12143  14824  10403   1115   -172     11       N  
ATOM    238  CA  SER A  76      54.828 -41.869 191.860  1.00 98.84           C  
ANISOU  238  CA  SER A  76    12442  14781  10330   1283    -85     76       C  
ATOM    239  C   SER A  76      53.360 -41.583 191.565  1.00101.36           C  
ANISOU  239  C   SER A  76    12770  15044  10700   1145     85     97       C  
ATOM    240  O   SER A  76      53.022 -40.589 190.907  1.00100.67           O  
ANISOU  240  O   SER A  76    12551  15026  10675    979      3     55       O  
ATOM    241  CB  SER A  76      55.373 -40.924 192.929  1.00102.97           C  
ANISOU  241  CB  SER A  76    13060  15342  10722   1441   -317     48       C  
ATOM    242  OG  SER A  76      54.748 -41.123 194.188  1.00109.98           O  
ANISOU  242  OG  SER A  76    14211  16122  11456   1643   -230    117       O  
ATOM    243  N   ARG A  77      52.501 -42.495 192.046  1.00 96.26           N  
ANISOU  243  N   ARG A  77    12281  14262  10031   1225    337    152       N  
ATOM    244  CA  ARG A  77      51.048 -42.462 191.951  1.00 94.31           C  
ANISOU  244  CA  ARG A  77    12061  13930   9842   1129    543    151       C  
ATOM    245  C   ARG A  77      50.545 -41.403 192.928  1.00 95.84           C  
ANISOU  245  C   ARG A  77    12397  14092   9925   1204    456    170       C  
ATOM    246  O   ARG A  77      49.495 -40.802 192.695  1.00 94.85           O  
ANISOU  246  O   ARG A  77    12231  13951   9855   1085    514    143       O  
ATOM    247  CB  ARG A  77      50.508 -43.849 192.332  1.00 95.91           C  
ANISOU  247  CB  ARG A  77    12408  13972  10062   1219    861    191       C  
ATOM    248  CG  ARG A  77      49.002 -44.046 192.206  1.00109.10           C  
ANISOU  248  CG  ARG A  77    14086  15533  11834   1117   1124    155       C  
ATOM    249  CD  ARG A  77      48.599 -45.411 192.729  1.00123.51           C  
ANISOU  249  CD  ARG A  77    16082  17171  13677   1227   1464    190       C  
ATOM    250  NE  ARG A  77      48.959 -46.489 191.802  1.00135.65           N  
ANISOU  250  NE  ARG A  77    17472  18727  15340   1144   1590    158       N  
ATOM    251  CZ  ARG A  77      49.126 -47.763 192.147  1.00152.13           C  
ANISOU  251  CZ  ARG A  77    19693  20681  17428   1262   1835    204       C  
ATOM    252  NH1 ARG A  77      48.984 -48.141 193.411  1.00141.16           N  
ANISOU  252  NH1 ARG A  77    18608  19121  15904   1488   1987    291       N  
ATOM    253  NH2 ARG A  77      49.450 -48.666 191.233  1.00140.41           N  
ANISOU  253  NH2 ARG A  77    18051  19226  16071   1166   1938    166       N  
ATOM    254  N   VAL A  78      51.301 -41.189 194.025  1.00 92.02           N  
ANISOU  254  N   VAL A  78    12078  13602   9283   1413    311    207       N  
ATOM    255  CA  VAL A  78      51.015 -40.231 195.100  1.00 91.72           C  
ANISOU  255  CA  VAL A  78    12197  13538   9115   1522    208    225       C  
ATOM    256  C   VAL A  78      51.024 -38.801 194.556  1.00 95.84           C  
ANISOU  256  C   VAL A  78    12540  14185   9690   1354     -4    164       C  
ATOM    257  O   VAL A  78      51.910 -38.436 193.776  1.00 95.49           O  
ANISOU  257  O   VAL A  78    12310  14264   9708   1263   -175    110       O  
ATOM    258  CB  VAL A  78      51.985 -40.411 196.299  1.00 95.96           C  
ANISOU  258  CB  VAL A  78    12931  14065   9465   1807     78    255       C  
ATOM    259  CG1 VAL A  78      51.775 -39.333 197.356  1.00 95.81           C  
ANISOU  259  CG1 VAL A  78    13049  14044   9310   1915    -65    254       C  
ATOM    260  CG2 VAL A  78      51.855 -41.803 196.911  1.00 96.96           C  
ANISOU  260  CG2 VAL A  78    13286  14038   9514   2001    325    334       C  
ATOM    261  N   GLY A  79      50.003 -38.038 194.935  1.00 92.27           N  
ANISOU  261  N   GLY A  79    12150  13686   9223   1312     34    171       N  
ATOM    262  CA  GLY A  79      49.835 -36.648 194.533  1.00 91.21           C  
ANISOU  262  CA  GLY A  79    11886  13644   9127   1171   -132    126       C  
ATOM    263  C   GLY A  79      49.440 -36.415 193.089  1.00 94.11           C  
ANISOU  263  C   GLY A  79    12030  14083   9645    941   -104     82       C  
ATOM    264  O   GLY A  79      49.155 -35.272 192.724  1.00 93.30           O  
ANISOU  264  O   GLY A  79    11846  14037   9567    834   -205     55       O  
ATOM    265  N   ARG A  80      49.425 -37.482 192.255  1.00 90.88           N  
ANISOU  265  N   ARG A  80    11529  13671   9330    876     34     72       N  
ATOM    266  CA  ARG A  80      49.067 -37.418 190.832  1.00 90.02           C  
ANISOU  266  CA  ARG A  80    11216  13636   9353    683     68     21       C  
ATOM    267  C   ARG A  80      47.576 -37.151 190.682  1.00 95.00           C  
ANISOU  267  C   ARG A  80    11846  14218  10032    608    199     -7       C  
ATOM    268  O   ARG A  80      46.760 -37.892 191.227  1.00 95.56           O  
ANISOU  268  O   ARG A  80    12023  14168  10115    664    401     -2       O  
ATOM    269  CB  ARG A  80      49.485 -38.706 190.100  1.00 90.10           C  
ANISOU  269  CB  ARG A  80    11140  13650   9444    654    188      9       C  
ATOM    270  CG  ARG A  80      49.169 -38.725 188.607  1.00 97.28           C  
ANISOU  270  CG  ARG A  80    11840  14646  10476    471    213    -53       C  
ATOM    271  CD  ARG A  80      49.852 -39.876 187.904  1.00102.86           C  
ANISOU  271  CD  ARG A  80    12454  15374  11256    443    289    -65       C  
ATOM    272  NE  ARG A  80      49.162 -41.152 188.097  1.00106.33           N  
ANISOU  272  NE  ARG A  80    12942  15708  11749    476    544    -71       N  
ATOM    273  CZ  ARG A  80      49.782 -42.316 188.268  1.00118.05           C  
ANISOU  273  CZ  ARG A  80    14466  17143  13245    549    650    -43       C  
ATOM    274  NH1 ARG A  80      51.111 -42.375 188.289  1.00 94.98           N  
ANISOU  274  NH1 ARG A  80    11532  14276  10281    602    502    -12       N  
ATOM    275  NH2 ARG A  80      49.080 -43.430 188.430  1.00110.30           N  
ANISOU  275  NH2 ARG A  80    13536  16049  12326    571    917    -55       N  
ATOM    276  N   SER A  81      47.235 -36.079 189.955  1.00 91.80           N  
ANISOU  276  N   SER A  81    11327  13896   9657    491     93    -43       N  
ATOM    277  CA  SER A  81      45.859 -35.635 189.732  1.00 91.86           C  
ANISOU  277  CA  SER A  81    11310  13882   9710    426    174    -89       C  
ATOM    278  C   SER A  81      45.287 -36.037 188.353  1.00 95.78           C  
ANISOU  278  C   SER A  81    11624  14446  10323    304    250   -174       C  
ATOM    279  O   SER A  81      46.026 -36.501 187.477  1.00 94.91           O  
ANISOU  279  O   SER A  81    11404  14407  10250    254    225   -184       O  
ATOM    280  CB  SER A  81      45.761 -34.125 189.932  1.00 95.20           C  
ANISOU  280  CB  SER A  81    11752  14348  10071    408      6    -75       C  
ATOM    281  OG  SER A  81      46.431 -33.423 188.897  1.00101.74           O  
ANISOU  281  OG  SER A  81    12451  15293  10913    320   -138    -87       O  
ATOM    282  N   VAL A  82      43.958 -35.826 188.174  1.00 92.30           N  
ANISOU  282  N   VAL A  82    11147  13986   9938    263    336   -248       N  
ATOM    283  CA  VAL A  82      43.190 -36.088 186.953  1.00 91.81           C  
ANISOU  283  CA  VAL A  82    10910  13996   9978    173    394   -363       C  
ATOM    284  C   VAL A  82      43.849 -35.323 185.805  1.00 95.10           C  
ANISOU  284  C   VAL A  82    11220  14557  10359    111    211   -354       C  
ATOM    285  O   VAL A  82      43.983 -35.859 184.702  1.00 95.46           O  
ANISOU  285  O   VAL A  82    11131  14679  10460     54    232   -412       O  
ATOM    286  CB  VAL A  82      41.699 -35.691 187.135  1.00 96.28           C  
ANISOU  286  CB  VAL A  82    11466  14520  10595    165    470   -456       C  
ATOM    287  CG1 VAL A  82      40.881 -35.969 185.877  1.00 96.20           C  
ANISOU  287  CG1 VAL A  82    11262  14601  10690     96    511   -609       C  
ATOM    288  CG2 VAL A  82      41.078 -36.399 188.337  1.00 97.02           C  
ANISOU  288  CG2 VAL A  82    11693  14442  10730    225    682   -462       C  
ATOM    289  N   THR A  83      44.311 -34.093 186.089  1.00 90.17           N  
ANISOU  289  N   THR A  83    10664  13956   9641    127     47   -281       N  
ATOM    290  CA  THR A  83      45.005 -33.255 185.120  1.00 88.88           C  
ANISOU  290  CA  THR A  83    10436  13895   9439     77    -99   -262       C  
ATOM    291  C   THR A  83      46.354 -33.870 184.751  1.00 91.60           C  
ANISOU  291  C   THR A  83    10738  14266   9798     53   -123   -229       C  
ATOM    292  O   THR A  83      46.679 -33.895 183.568  1.00 91.47           O  
ANISOU  292  O   THR A  83    10623  14329   9803     -8   -149   -253       O  
ATOM    293  CB  THR A  83      45.129 -31.829 185.631  1.00 95.19           C  
ANISOU  293  CB  THR A  83    11323  14686  10157     97   -227   -206       C  
ATOM    294  OG1 THR A  83      43.909 -31.464 186.273  1.00 96.60           O  
ANISOU  294  OG1 THR A  83    11559  14815  10330    130   -185   -231       O  
ATOM    295  CG2 THR A  83      45.440 -30.851 184.527  1.00 91.22           C  
ANISOU  295  CG2 THR A  83    10768  14267   9623     48   -327   -201       C  
ATOM    296  N   ASP A  84      47.109 -34.408 185.744  1.00 87.28           N  
ANISOU  296  N   ASP A  84    10271  13654   9237    113   -111   -180       N  
ATOM    297  CA  ASP A  84      48.409 -35.053 185.519  1.00 86.67           C  
ANISOU  297  CA  ASP A  84    10153  13597   9182    107   -136   -160       C  
ATOM    298  C   ASP A  84      48.266 -36.262 184.589  1.00 89.76           C  
ANISOU  298  C   ASP A  84    10432  14014   9658     54    -10   -208       C  
ATOM    299  O   ASP A  84      49.142 -36.495 183.752  1.00 88.48           O  
ANISOU  299  O   ASP A  84    10184  13906   9529      0    -43   -212       O  
ATOM    300  CB  ASP A  84      49.092 -35.431 186.847  1.00 89.04           C  
ANISOU  300  CB  ASP A  84    10575  13824   9433    222   -152   -112       C  
ATOM    301  CG  ASP A  84      49.495 -34.248 187.720  1.00100.84           C  
ANISOU  301  CG  ASP A  84    12158  15309  10847    277   -302    -84       C  
ATOM    302  OD1 ASP A  84      49.948 -33.222 187.163  1.00102.14           O  
ANISOU  302  OD1 ASP A  84    12262  15531  11017    208   -413    -97       O  
ATOM    303  OD2 ASP A  84      49.376 -34.355 188.962  1.00105.52           O  
ANISOU  303  OD2 ASP A  84    12887  15831  11373    394   -295    -54       O  
ATOM    304  N   VAL A  85      47.115 -36.973 184.686  1.00 86.41           N  
ANISOU  304  N   VAL A  85    10000  13548   9282     62    145   -260       N  
ATOM    305  CA  VAL A  85      46.762 -38.116 183.836  1.00 85.97           C  
ANISOU  305  CA  VAL A  85     9824  13514   9326      8    289   -336       C  
ATOM    306  C   VAL A  85      46.549 -37.629 182.392  1.00 90.04           C  
ANISOU  306  C   VAL A  85    10202  14151   9856    -75    218   -401       C  
ATOM    307  O   VAL A  85      47.108 -38.221 181.469  1.00 89.83           O  
ANISOU  307  O   VAL A  85    10076  14181   9874   -130    236   -425       O  
ATOM    308  CB  VAL A  85      45.541 -38.905 184.375  1.00 89.85           C  
ANISOU  308  CB  VAL A  85    10338  13912   9889     36    494   -404       C  
ATOM    309  CG1 VAL A  85      45.214 -40.100 183.479  1.00 90.01           C  
ANISOU  309  CG1 VAL A  85    10212  13954  10032    -27    654   -507       C  
ATOM    310  CG2 VAL A  85      45.773 -39.366 185.809  1.00 90.04           C  
ANISOU  310  CG2 VAL A  85    10541  13799   9872    144    580   -324       C  
ATOM    311  N   TYR A  86      45.778 -36.532 182.206  1.00 86.30           N  
ANISOU  311  N   TYR A  86     9740  13717   9335    -72    137   -425       N  
ATOM    312  CA  TYR A  86      45.537 -35.948 180.887  1.00 85.80           C  
ANISOU  312  CA  TYR A  86     9585  13765   9248   -111     60   -477       C  
ATOM    313  C   TYR A  86      46.816 -35.427 180.251  1.00 87.81           C  
ANISOU  313  C   TYR A  86     9846  14063   9455   -148    -47   -405       C  
ATOM    314  O   TYR A  86      47.034 -35.687 179.075  1.00 87.29           O  
ANISOU  314  O   TYR A  86     9695  14072   9400   -189    -46   -444       O  
ATOM    315  CB  TYR A  86      44.472 -34.858 180.944  1.00 87.88           C  
ANISOU  315  CB  TYR A  86     9884  14049   9458    -73     -3   -510       C  
ATOM    316  CG  TYR A  86      43.086 -35.335 181.334  1.00 92.08           C  
ANISOU  316  CG  TYR A  86    10378  14547  10063    -48    110   -623       C  
ATOM    317  CD1 TYR A  86      42.604 -36.576 180.914  1.00 94.77           C  
ANISOU  317  CD1 TYR A  86    10593  14897  10518    -75    254   -747       C  
ATOM    318  CD2 TYR A  86      42.220 -34.509 182.043  1.00 93.70           C  
ANISOU  318  CD2 TYR A  86    10657  14707  10237     -4     83   -626       C  
ATOM    319  CE1 TYR A  86      41.316 -37.004 181.243  1.00 96.40           C  
ANISOU  319  CE1 TYR A  86    10747  15059  10822    -62    381   -883       C  
ATOM    320  CE2 TYR A  86      40.928 -34.921 182.371  1.00 95.54           C  
ANISOU  320  CE2 TYR A  86    10844  14899  10559     11    201   -752       C  
ATOM    321  CZ  TYR A  86      40.480 -36.168 181.967  1.00105.00           C  
ANISOU  321  CZ  TYR A  86    11913  16098  11885    -19    355   -888       C  
ATOM    322  OH  TYR A  86      39.204 -36.561 182.294  1.00109.43           O  
ANISOU  322  OH  TYR A  86    12415  16602  12560    -12    493  -1040       O  
ATOM    323  N   LEU A  87      47.687 -34.756 181.038  1.00 83.90           N  
ANISOU  323  N   LEU A  87     9447  13515   8917   -132   -127   -315       N  
ATOM    324  CA  LEU A  87      48.993 -34.243 180.595  1.00 83.45           C  
ANISOU  324  CA  LEU A  87     9390  13473   8846   -174   -209   -267       C  
ATOM    325  C   LEU A  87      49.952 -35.388 180.206  1.00 86.65           C  
ANISOU  325  C   LEU A  87     9715  13884   9323   -217   -156   -276       C  
ATOM    326  O   LEU A  87      50.778 -35.215 179.305  1.00 85.53           O  
ANISOU  326  O   LEU A  87     9528  13774   9196   -276   -181   -274       O  
ATOM    327  CB  LEU A  87      49.634 -33.321 181.657  1.00 83.55           C  
ANISOU  327  CB  LEU A  87     9500  13427   8819   -142   -302   -208       C  
ATOM    328  CG  LEU A  87      48.939 -31.965 181.928  1.00 88.42           C  
ANISOU  328  CG  LEU A  87    10197  14035   9365   -115   -363   -189       C  
ATOM    329  CD1 LEU A  87      49.375 -31.370 183.259  1.00 88.92           C  
ANISOU  329  CD1 LEU A  87    10350  14034   9402    -68   -432   -152       C  
ATOM    330  CD2 LEU A  87      49.173 -30.966 180.811  1.00 90.35           C  
ANISOU  330  CD2 LEU A  87    10437  14316   9575   -156   -400   -183       C  
ATOM    331  N   LEU A  88      49.815 -36.557 180.869  1.00 83.39           N  
ANISOU  331  N   LEU A  88     9296  13430   8959   -185    -65   -285       N  
ATOM    332  CA  LEU A  88      50.590 -37.770 180.594  1.00 83.59           C  
ANISOU  332  CA  LEU A  88     9252  13453   9057   -213      6   -294       C  
ATOM    333  C   LEU A  88      50.176 -38.336 179.234  1.00 88.09           C  
ANISOU  333  C   LEU A  88     9698  14097   9676   -284     80   -364       C  
ATOM    334  O   LEU A  88      51.031 -38.819 178.495  1.00 88.10           O  
ANISOU  334  O   LEU A  88     9628  14125   9723   -342     92   -368       O  
ATOM    335  CB  LEU A  88      50.357 -38.816 181.715  1.00 84.19           C  
ANISOU  335  CB  LEU A  88     9386  13447   9156   -136    113   -280       C  
ATOM    336  CG  LEU A  88      50.908 -40.252 181.539  1.00 89.06           C  
ANISOU  336  CG  LEU A  88     9945  14044   9851   -145    229   -290       C  
ATOM    337  CD1 LEU A  88      52.396 -40.325 181.843  1.00 89.44           C  
ANISOU  337  CD1 LEU A  88    10010  14080   9892   -118    136   -242       C  
ATOM    338  CD2 LEU A  88      50.172 -41.225 182.438  1.00 91.53           C  
ANISOU  338  CD2 LEU A  88    10325  14264  10187    -71    399   -294       C  
ATOM    339  N   ASN A  89      48.867 -38.280 178.910  1.00 84.99           N  
ANISOU  339  N   ASN A  89     9274  13740   9279   -275    127   -434       N  
ATOM    340  CA  ASN A  89      48.331 -38.762 177.636  1.00 84.98           C  
ANISOU  340  CA  ASN A  89     9149  13827   9315   -319    181   -532       C  
ATOM    341  C   ASN A  89      48.759 -37.855 176.485  1.00 89.66           C  
ANISOU  341  C   ASN A  89     9739  14494   9835   -346     77   -518       C  
ATOM    342  O   ASN A  89      49.085 -38.342 175.405  1.00 88.98           O  
ANISOU  342  O   ASN A  89     9570  14469   9771   -391    105   -559       O  
ATOM    343  CB  ASN A  89      46.823 -38.892 177.709  1.00 84.23           C  
ANISOU  343  CB  ASN A  89     9013  13748   9242   -284    246   -640       C  
ATOM    344  CG  ASN A  89      46.391 -40.160 178.377  1.00104.15           C  
ANISOU  344  CG  ASN A  89    11500  16198  11876   -283    422   -695       C  
ATOM    345  OD1 ASN A  89      46.287 -41.214 177.745  1.00 97.22           O  
ANISOU  345  OD1 ASN A  89    10500  15348  11090   -327    537   -785       O  
ATOM    346  ND2 ASN A  89      46.133 -40.091 179.671  1.00 97.65           N  
ANISOU  346  ND2 ASN A  89    10789  15268  11046   -229    464   -644       N  
ATOM    347  N   LEU A  90      48.807 -36.542 176.752  1.00 87.62           N  
ANISOU  347  N   LEU A  90     9583  14218   9488   -313    -27   -457       N  
ATOM    348  CA  LEU A  90      49.246 -35.493 175.841  1.00 88.36           C  
ANISOU  348  CA  LEU A  90     9723  14346   9503   -322   -102   -424       C  
ATOM    349  C   LEU A  90      50.722 -35.719 175.488  1.00 93.35           C  
ANISOU  349  C   LEU A  90    10339  14947  10182   -395    -93   -379       C  
ATOM    350  O   LEU A  90      51.099 -35.585 174.320  1.00 93.49           O  
ANISOU  350  O   LEU A  90    10342  15002  10178   -427    -82   -387       O  
ATOM    351  CB  LEU A  90      49.074 -34.135 176.536  1.00 88.69           C  
ANISOU  351  CB  LEU A  90     9886  14343   9470   -277   -184   -363       C  
ATOM    352  CG  LEU A  90      48.710 -32.965 175.640  1.00 94.26           C  
ANISOU  352  CG  LEU A  90    10658  15089  10068   -238   -233   -354       C  
ATOM    353  CD1 LEU A  90      47.205 -32.830 175.507  1.00 94.83           C  
ANISOU  353  CD1 LEU A  90    10717  15227  10087   -157   -252   -428       C  
ATOM    354  CD2 LEU A  90      49.279 -31.682 176.188  1.00 97.20           C  
ANISOU  354  CD2 LEU A  90    11146  15386  10400   -237   -285   -272       C  
ATOM    355  N   ALA A  91      51.544 -36.090 176.503  1.00 90.02           N  
ANISOU  355  N   ALA A  91     9924  14457   9824   -409    -95   -340       N  
ATOM    356  CA  ALA A  91      52.972 -36.397 176.372  1.00 89.66           C  
ANISOU  356  CA  ALA A  91     9844  14376   9848   -470    -94   -321       C  
ATOM    357  C   ALA A  91      53.167 -37.607 175.472  1.00 94.03           C  
ANISOU  357  C   ALA A  91    10290  14972  10467   -525     -7   -364       C  
ATOM    358  O   ALA A  91      54.095 -37.606 174.670  1.00 94.61           O  
ANISOU  358  O   ALA A  91    10331  15043  10576   -591      4   -364       O  
ATOM    359  CB  ALA A  91      53.590 -36.659 177.740  1.00 90.29           C  
ANISOU  359  CB  ALA A  91     9951  14391   9965   -432   -130   -294       C  
ATOM    360  N   LEU A  92      52.277 -38.621 175.578  1.00 90.04           N  
ANISOU  360  N   LEU A  92     9726  14497   9989   -503     70   -411       N  
ATOM    361  CA  LEU A  92      52.319 -39.822 174.745  1.00 89.75           C  
ANISOU  361  CA  LEU A  92     9573  14503  10023   -556    168   -468       C  
ATOM    362  C   LEU A  92      51.880 -39.495 173.311  1.00 94.19           C  
ANISOU  362  C   LEU A  92    10099  15154  10533   -576    164   -523       C  
ATOM    363  O   LEU A  92      52.483 -40.005 172.364  1.00 93.57           O  
ANISOU  363  O   LEU A  92     9956  15104  10491   -638    206   -543       O  
ATOM    364  CB  LEU A  92      51.468 -40.949 175.356  1.00 89.72           C  
ANISOU  364  CB  LEU A  92     9522  14487  10081   -525    278   -519       C  
ATOM    365  CG  LEU A  92      51.213 -42.193 174.490  1.00 94.45           C  
ANISOU  365  CG  LEU A  92     9984  15135  10766   -578    404   -609       C  
ATOM    366  CD1 LEU A  92      52.487 -43.002 174.263  1.00 94.19           C  
ANISOU  366  CD1 LEU A  92     9905  15074  10810   -639    447   -573       C  
ATOM    367  CD2 LEU A  92      50.145 -43.057 175.105  1.00 97.83           C  
ANISOU  367  CD2 LEU A  92    10374  15536  11259   -544    535   -682       C  
ATOM    368  N   ALA A  93      50.857 -38.625 173.156  1.00 91.60           N  
ANISOU  368  N   ALA A  93     9823  14871  10111   -511    110   -547       N  
ATOM    369  CA  ALA A  93      50.366 -38.186 171.848  1.00 92.50           C  
ANISOU  369  CA  ALA A  93     9933  15075  10136   -484     85   -600       C  
ATOM    370  C   ALA A  93      51.463 -37.434 171.069  1.00 98.74           C  
ANISOU  370  C   ALA A  93    10803  15837  10877   -519     63   -528       C  
ATOM    371  O   ALA A  93      51.614 -37.657 169.864  1.00 99.02           O  
ANISOU  371  O   ALA A  93    10813  15926  10882   -531     93   -564       O  
ATOM    372  CB  ALA A  93      49.127 -37.319 172.004  1.00 93.41           C  
ANISOU  372  CB  ALA A  93    10106  15231  10156   -386     18   -632       C  
ATOM    373  N   ASP A  94      52.256 -36.589 171.767  1.00 96.23           N  
ANISOU  373  N   ASP A  94    10578  15426  10561   -537     25   -441       N  
ATOM    374  CA  ASP A  94      53.373 -35.856 171.167  1.00 96.98           C  
ANISOU  374  CA  ASP A  94    10744  15459  10645   -585     36   -388       C  
ATOM    375  C   ASP A  94      54.559 -36.785 170.913  1.00100.31           C  
ANISOU  375  C   ASP A  94    11077  15848  11190   -686     98   -397       C  
ATOM    376  O   ASP A  94      55.289 -36.588 169.946  1.00 99.62           O  
ANISOU  376  O   ASP A  94    11013  15735  11104   -736    148   -391       O  
ATOM    377  CB  ASP A  94      53.793 -34.669 172.048  1.00 99.70           C  
ANISOU  377  CB  ASP A  94    11188  15713  10980   -576    -14   -327       C  
ATOM    378  CG  ASP A  94      52.964 -33.410 171.851  1.00117.74           C  
ANISOU  378  CG  ASP A  94    13600  18007  13131   -490    -52   -299       C  
ATOM    379  OD1 ASP A  94      52.799 -32.979 170.680  1.00120.29           O  
ANISOU  379  OD1 ASP A  94    13992  18353  13359   -456    -19   -296       O  
ATOM    380  OD2 ASP A  94      52.498 -32.839 172.867  1.00124.90           O  
ANISOU  380  OD2 ASP A  94    14547  18890  14018   -448   -110   -278       O  
ATOM    381  N   LEU A  95      54.734 -37.801 171.777  1.00 97.33           N  
ANISOU  381  N   LEU A  95    10607  15461  10911   -708    106   -412       N  
ATOM    382  CA  LEU A  95      55.794 -38.805 171.685  1.00 97.62           C  
ANISOU  382  CA  LEU A  95    10551  15470  11070   -788    159   -424       C  
ATOM    383  C   LEU A  95      55.614 -39.660 170.439  1.00102.81           C  
ANISOU  383  C   LEU A  95    11128  16196  11739   -830    239   -474       C  
ATOM    384  O   LEU A  95      56.608 -40.003 169.811  1.00102.74           O  
ANISOU  384  O   LEU A  95    11080  16159  11798   -910    288   -477       O  
ATOM    385  CB  LEU A  95      55.816 -39.683 172.962  1.00 97.50           C  
ANISOU  385  CB  LEU A  95    10490  15431  11126   -759    155   -421       C  
ATOM    386  CG  LEU A  95      57.040 -40.582 173.288  1.00102.44           C  
ANISOU  386  CG  LEU A  95    11042  16009  11872   -806    180   -422       C  
ATOM    387  CD1 LEU A  95      56.917 -41.964 172.656  1.00104.83           C  
ANISOU  387  CD1 LEU A  95    11237  16353  12240   -851    288   -460       C  
ATOM    388  CD2 LEU A  95      58.387 -39.904 172.981  1.00102.99           C  
ANISOU  388  CD2 LEU A  95    11116  16019  11997   -871    147   -423       C  
ATOM    389  N   LEU A  96      54.360 -39.999 170.081  1.00100.68           N  
ANISOU  389  N   LEU A  96    10825  16017  11411   -777    253   -531       N  
ATOM    390  CA  LEU A  96      54.043 -40.806 168.899  1.00101.42           C  
ANISOU  390  CA  LEU A  96    10831  16197  11509   -801    319   -608       C  
ATOM    391  C   LEU A  96      54.233 -40.023 167.598  1.00107.08           C  
ANISOU  391  C   LEU A  96    11630  16939  12117   -789    310   -602       C  
ATOM    392  O   LEU A  96      54.746 -40.578 166.625  1.00106.84           O  
ANISOU  392  O   LEU A  96    11552  16928  12112   -844    372   -629       O  
ATOM    393  CB  LEU A  96      52.617 -41.367 168.982  1.00101.65           C  
ANISOU  393  CB  LEU A  96    10782  16315  11526   -738    333   -707       C  
ATOM    394  CG  LEU A  96      52.437 -42.569 169.894  1.00106.39           C  
ANISOU  394  CG  LEU A  96    11284  16885  12255   -764    417   -738       C  
ATOM    395  CD1 LEU A  96      51.079 -42.541 170.567  1.00107.09           C  
ANISOU  395  CD1 LEU A  96    11362  16997  12330   -688    418   -804       C  
ATOM    396  CD2 LEU A  96      52.650 -43.874 169.143  1.00108.50           C  
ANISOU  396  CD2 LEU A  96    11411  17194  12622   -836    528   -815       C  
ATOM    397  N   PHE A  97      53.824 -38.735 167.587  1.00104.70           N  
ANISOU  397  N   PHE A  97    11465  16628  11690   -708    244   -561       N  
ATOM    398  CA  PHE A  97      53.950 -37.829 166.446  1.00105.62           C  
ANISOU  398  CA  PHE A  97    11710  16745  11675   -663    251   -537       C  
ATOM    399  C   PHE A  97      55.417 -37.524 166.156  1.00109.92           C  
ANISOU  399  C   PHE A  97    12310  17168  12287   -763    323   -474       C  
ATOM    400  O   PHE A  97      55.773 -37.317 164.998  1.00110.75           O  
ANISOU  400  O   PHE A  97    12486  17262  12331   -764    386   -469       O  
ATOM    401  CB  PHE A  97      53.152 -36.541 166.700  1.00108.15           C  
ANISOU  401  CB  PHE A  97    12169  17068  11855   -545    176   -504       C  
ATOM    402  CG  PHE A  97      53.374 -35.394 165.741  1.00111.18           C  
ANISOU  402  CG  PHE A  97    12736  17412  12094   -480    201   -449       C  
ATOM    403  CD1 PHE A  97      53.118 -35.539 164.382  1.00115.59           C  
ANISOU  403  CD1 PHE A  97    13339  18045  12533   -408    228   -490       C  
ATOM    404  CD2 PHE A  97      53.788 -34.152 166.204  1.00114.07           C  
ANISOU  404  CD2 PHE A  97    13243  17662  12435   -475    209   -363       C  
ATOM    405  CE1 PHE A  97      53.322 -34.475 163.498  1.00117.76           C  
ANISOU  405  CE1 PHE A  97    13821  18266  12656   -324    273   -428       C  
ATOM    406  CE2 PHE A  97      53.974 -33.083 165.322  1.00118.13           C  
ANISOU  406  CE2 PHE A  97    13950  18117  12818   -406    268   -308       C  
ATOM    407  CZ  PHE A  97      53.739 -33.252 163.976  1.00117.12           C  
ANISOU  407  CZ  PHE A  97    13890  18053  12559   -325    305   -333       C  
ATOM    408  N   ALA A  98      56.265 -37.521 167.204  1.00105.70           N  
ANISOU  408  N   ALA A  98    11741  16540  11882   -840    317   -439       N  
ATOM    409  CA  ALA A  98      57.711 -37.298 167.129  1.00105.45           C  
ANISOU  409  CA  ALA A  98    11720  16386  11961   -944    380   -416       C  
ATOM    410  C   ALA A  98      58.369 -38.394 166.323  1.00108.97           C  
ANISOU  410  C   ALA A  98    12064  16843  12495  -1033    461   -454       C  
ATOM    411  O   ALA A  98      59.271 -38.108 165.543  1.00109.47           O  
ANISOU  411  O   ALA A  98    12175  16826  12593  -1099    548   -448       O  
ATOM    412  CB  ALA A  98      58.303 -37.279 168.524  1.00105.90           C  
ANISOU  412  CB  ALA A  98    11724  16379  12136   -976    323   -408       C  
ATOM    413  N   LEU A  99      57.895 -39.643 166.490  1.00105.00           N  
ANISOU  413  N   LEU A  99    11428  16431  12037  -1037    453   -499       N  
ATOM    414  CA  LEU A  99      58.393 -40.832 165.795  1.00104.97           C  
ANISOU  414  CA  LEU A  99    11309  16450  12125  -1121    532   -541       C  
ATOM    415  C   LEU A  99      58.249 -40.758 164.267  1.00109.99           C  
ANISOU  415  C   LEU A  99    11997  17130  12664  -1114    597   -565       C  
ATOM    416  O   LEU A  99      59.059 -41.361 163.557  1.00110.60           O  
ANISOU  416  O   LEU A  99    12022  17181  12821  -1204    681   -584       O  
ATOM    417  CB  LEU A  99      57.714 -42.104 166.327  1.00104.41           C  
ANISOU  417  CB  LEU A  99    11097  16460  12114  -1111    531   -590       C  
ATOM    418  CG  LEU A  99      57.906 -42.430 167.809  1.00108.66           C  
ANISOU  418  CG  LEU A  99    11595  16951  12741  -1102    491   -564       C  
ATOM    419  CD1 LEU A  99      56.853 -43.420 168.281  1.00108.85           C  
ANISOU  419  CD1 LEU A  99    11535  17044  12780  -1057    517   -610       C  
ATOM    420  CD2 LEU A  99      59.315 -42.940 168.103  1.00109.86           C  
ANISOU  420  CD2 LEU A  99    11683  17019  13040  -1188    521   -553       C  
ATOM    421  N   THR A 100      57.231 -40.027 163.763  1.00105.82           N  
ANISOU  421  N   THR A 100    11579  16669  11959   -994    555   -568       N  
ATOM    422  CA  THR A 100      56.999 -39.881 162.325  1.00105.93           C  
ANISOU  422  CA  THR A 100    11674  16735  11838   -940    600   -593       C  
ATOM    423  C   THR A 100      57.902 -38.824 161.669  1.00110.79           C  
ANISOU  423  C   THR A 100    12475  17217  12404   -954    684   -521       C  
ATOM    424  O   THR A 100      58.069 -38.854 160.447  1.00111.36           O  
ANISOU  424  O   THR A 100    12625  17295  12393   -935    760   -530       O  
ATOM    425  CB  THR A 100      55.519 -39.637 162.015  1.00109.19           C  
ANISOU  425  CB  THR A 100    12118  17291  12080   -779    512   -651       C  
ATOM    426  OG1 THR A 100      55.088 -38.422 162.622  1.00105.87           O  
ANISOU  426  OG1 THR A 100    11829  16831  11565   -690    445   -591       O  
ATOM    427  CG2 THR A 100      54.637 -40.788 162.438  1.00106.86           C  
ANISOU  427  CG2 THR A 100    11625  17116  11859   -779    475   -758       C  
ATOM    428  N   LEU A 101      58.489 -37.909 162.469  1.00107.19           N  
ANISOU  428  N   LEU A 101    12092  16633  12002   -986    687   -459       N  
ATOM    429  CA  LEU A 101      59.348 -36.824 161.981  1.00108.14           C  
ANISOU  429  CA  LEU A 101    12385  16596  12107  -1010    798   -404       C  
ATOM    430  C   LEU A 101      60.598 -37.285 161.178  1.00113.88           C  
ANISOU  430  C   LEU A 101    13093  17221  12956  -1142    944   -421       C  
ATOM    431  O   LEU A 101      60.845 -36.659 160.145  1.00114.33           O  
ANISOU  431  O   LEU A 101    13326  17197  12916  -1110   1064   -390       O  
ATOM    432  CB  LEU A 101      59.749 -35.862 163.104  1.00107.89           C  
ANISOU  432  CB  LEU A 101    12388  16453  12151  -1035    774   -370       C  
ATOM    433  CG  LEU A 101      58.615 -35.038 163.710  1.00112.42           C  
ANISOU  433  CG  LEU A 101    13046  17085  12585   -901    667   -336       C  
ATOM    434  CD1 LEU A 101      59.034 -34.428 165.028  1.00112.40           C  
ANISOU  434  CD1 LEU A 101    13017  16995  12694   -947    624   -324       C  
ATOM    435  CD2 LEU A 101      58.133 -33.960 162.752  1.00115.96           C  
ANISOU  435  CD2 LEU A 101    13724  17509  12824   -770    725   -286       C  
ATOM    436  N   PRO A 102      61.377 -38.346 161.554  1.00110.97           N  
ANISOU  436  N   PRO A 102    12535  16843  12786  -1277    952   -467       N  
ATOM    437  CA  PRO A 102      62.526 -38.736 160.709  1.00111.51           C  
ANISOU  437  CA  PRO A 102    12591  16810  12970  -1400   1097   -489       C  
ATOM    438  C   PRO A 102      62.128 -39.331 159.342  1.00116.57           C  
ANISOU  438  C   PRO A 102    13271  17533  13486  -1361   1157   -503       C  
ATOM    439  O   PRO A 102      62.879 -39.200 158.369  1.00116.46           O  
ANISOU  439  O   PRO A 102    13348  17415  13485  -1416   1304   -498       O  
ATOM    440  CB  PRO A 102      63.298 -39.723 161.589  1.00112.32           C  
ANISOU  440  CB  PRO A 102    12475  16905  13298  -1521   1058   -538       C  
ATOM    441  CG  PRO A 102      62.280 -40.304 162.484  1.00115.89           C  
ANISOU  441  CG  PRO A 102    12824  17501  13706  -1445    915   -541       C  
ATOM    442  CD  PRO A 102      61.272 -39.223 162.741  1.00111.61           C  
ANISOU  442  CD  PRO A 102    12423  16992  12990  -1312    843   -498       C  
ATOM    443  N   ILE A 103      60.931 -39.954 159.267  1.00113.65           N  
ANISOU  443  N   ILE A 103    12834  17346  13000  -1262   1050   -533       N  
ATOM    444  CA  ILE A 103      60.359 -40.526 158.035  1.00114.04           C  
ANISOU  444  CA  ILE A 103    12902  17512  12917  -1196   1073   -577       C  
ATOM    445  C   ILE A 103      59.877 -39.358 157.152  1.00119.53           C  
ANISOU  445  C   ILE A 103    13860  18190  13368  -1034   1102   -532       C  
ATOM    446  O   ILE A 103      60.014 -39.417 155.933  1.00119.30           O  
ANISOU  446  O   ILE A 103    13941  18157  13231   -994   1191   -538       O  
ATOM    447  CB  ILE A 103      59.237 -41.567 158.346  1.00116.28           C  
ANISOU  447  CB  ILE A 103    13000  17990  13189  -1146    956   -661       C  
ATOM    448  CG1 ILE A 103      59.651 -42.508 159.519  1.00115.69           C  
ANISOU  448  CG1 ILE A 103    12713  17903  13341  -1274    936   -679       C  
ATOM    449  CG2 ILE A 103      58.870 -42.375 157.092  1.00116.55           C  
ANISOU  449  CG2 ILE A 103    12998  18145  13141  -1110    989   -743       C  
ATOM    450  CD1 ILE A 103      58.542 -42.908 160.505  1.00122.60           C  
ANISOU  450  CD1 ILE A 103    13476  18892  14216  -1207    826   -721       C  
ATOM    451  N   TRP A 104      59.359 -38.284 157.789  1.00117.75           N  
ANISOU  451  N   TRP A 104    13746  17942  13050   -934   1036   -482       N  
ATOM    452  CA  TRP A 104      58.922 -37.049 157.140  1.00119.59           C  
ANISOU  452  CA  TRP A 104    14248  18138  13052   -765   1068   -423       C  
ATOM    453  C   TRP A 104      60.128 -36.234 156.661  1.00124.07           C  
ANISOU  453  C   TRP A 104    15005  18474  13663   -838   1272   -352       C  
ATOM    454  O   TRP A 104      59.997 -35.467 155.709  1.00125.12           O  
ANISOU  454  O   TRP A 104    15389  18550  13601   -708   1370   -304       O  
ATOM    455  CB  TRP A 104      58.099 -36.183 158.102  1.00118.72           C  
ANISOU  455  CB  TRP A 104    14181  18057  12870   -662    949   -391       C  
ATOM    456  CG  TRP A 104      56.612 -36.386 158.069  1.00120.43           C  
ANISOU  456  CG  TRP A 104    14355  18479  12923   -491    785   -455       C  
ATOM    457  CD1 TRP A 104      55.787 -36.529 159.149  1.00122.63           C  
ANISOU  457  CD1 TRP A 104    14496  18852  13248   -473    645   -491       C  
ATOM    458  CD2 TRP A 104      55.756 -36.338 156.915  1.00121.80           C  
ANISOU  458  CD2 TRP A 104    14640  18781  12856   -295    746   -501       C  
ATOM    459  NE1 TRP A 104      54.474 -36.593 158.741  1.00122.94           N  
ANISOU  459  NE1 TRP A 104    14532  19065  13114   -295    529   -571       N  
ATOM    460  CE2 TRP A 104      54.427 -36.503 157.372  1.00126.01           C  
ANISOU  460  CE2 TRP A 104    15063  19490  13323   -176    574   -586       C  
ATOM    461  CE3 TRP A 104      55.982 -36.195 155.533  1.00124.59           C  
ANISOU  461  CE3 TRP A 104    15178  19118  13042   -197    841   -490       C  
ATOM    462  CZ2 TRP A 104      53.331 -36.540 156.495  1.00126.67           C  
ANISOU  462  CZ2 TRP A 104    15190  19748  13190     38    477   -682       C  
ATOM    463  CZ3 TRP A 104      54.899 -36.241 154.667  1.00127.32           C  
ANISOU  463  CZ3 TRP A 104    15587  19640  13148     29    740   -569       C  
ATOM    464  CH2 TRP A 104      53.592 -36.406 155.147  1.00127.79           C  
ANISOU  464  CH2 TRP A 104    15512  19887  13157    147    551   -673       C  
ATOM    465  N   ALA A 105      61.282 -36.361 157.352  1.00119.74           N  
ANISOU  465  N   ALA A 105    14342  17786  13368  -1032   1344   -357       N  
ATOM    466  CA  ALA A 105      62.524 -35.658 157.022  1.00120.49           C  
ANISOU  466  CA  ALA A 105    14566  17643  13571  -1135   1554   -328       C  
ATOM    467  C   ALA A 105      63.103 -36.174 155.709  1.00125.30           C  
ANISOU  467  C   ALA A 105    15247  18199  14163  -1174   1714   -340       C  
ATOM    468  O   ALA A 105      63.523 -35.369 154.872  1.00126.98           O  
ANISOU  468  O   ALA A 105    15705  18250  14292  -1135   1905   -292       O  
ATOM    469  CB  ALA A 105      63.538 -35.820 158.142  1.00120.45           C  
ANISOU  469  CB  ALA A 105    14369  17539  13856  -1320   1552   -374       C  
ATOM    470  N   ALA A 106      63.095 -37.512 155.517  1.00120.03           N  
ANISOU  470  N   ALA A 106    14379  17659  13567  -1245   1649   -402       N  
ATOM    471  CA  ALA A 106      63.566 -38.155 154.289  1.00119.99           C  
ANISOU  471  CA  ALA A 106    14413  17632  13547  -1285   1780   -423       C  
ATOM    472  C   ALA A 106      62.558 -37.912 153.156  1.00124.70           C  
ANISOU  472  C   ALA A 106    15217  18340  13822  -1061   1764   -400       C  
ATOM    473  O   ALA A 106      62.936 -37.901 151.985  1.00125.43           O  
ANISOU  473  O   ALA A 106    15474  18361  13824  -1035   1917   -387       O  
ATOM    474  CB  ALA A 106      63.764 -39.642 154.520  1.00119.28           C  
ANISOU  474  CB  ALA A 106    14036  17657  13629  -1416   1706   -500       C  
ATOM    475  N   SER A 107      61.283 -37.659 153.528  1.00120.95           N  
ANISOU  475  N   SER A 107    14747  18034  13173   -887   1581   -403       N  
ATOM    476  CA  SER A 107      60.173 -37.352 152.626  1.00121.84           C  
ANISOU  476  CA  SER A 107    15038  18285  12971   -635   1514   -406       C  
ATOM    477  C   SER A 107      60.313 -35.962 151.978  1.00128.37           C  
ANISOU  477  C   SER A 107    16233  18947  13596   -485   1664   -303       C  
ATOM    478  O   SER A 107      59.583 -35.672 151.027  1.00130.03           O  
ANISOU  478  O   SER A 107    16643  19242  13520   -253   1642   -297       O  
ATOM    479  CB  SER A 107      58.841 -37.467 153.365  1.00123.67           C  
ANISOU  479  CB  SER A 107    15133  18729  13127   -515   1279   -461       C  
ATOM    480  OG  SER A 107      57.761 -36.865 152.668  1.00131.24           O  
ANISOU  480  OG  SER A 107    16284  19800  13780   -246   1199   -467       O  
ATOM    481  N   LYS A 108      61.239 -35.113 152.472  1.00124.85           N  
ANISOU  481  N   LYS A 108    15878  18264  13295   -602   1823   -233       N  
ATOM    482  CA  LYS A 108      61.453 -33.770 151.925  1.00126.54           C  
ANISOU  482  CA  LYS A 108    16447  18281  13352   -480   2016   -134       C  
ATOM    483  C   LYS A 108      62.556 -33.765 150.872  1.00132.03           C  
ANISOU  483  C   LYS A 108    17315  18766  14086   -558   2297   -111       C  
ATOM    484  O   LYS A 108      62.463 -33.031 149.886  1.00133.13           O  
ANISOU  484  O   LYS A 108    17789  18803  13989   -382   2453    -39       O  
ATOM    485  CB  LYS A 108      61.743 -32.746 153.041  1.00128.80           C  
ANISOU  485  CB  LYS A 108    16745  18420  13774   -552   2051    -90       C  
ATOM    486  CG  LYS A 108      60.631 -32.599 154.093  1.00143.54           C  
ANISOU  486  CG  LYS A 108    18484  20469  15587   -462   1796   -101       C  
ATOM    487  CD  LYS A 108      59.425 -31.789 153.610  1.00155.21           C  
ANISOU  487  CD  LYS A 108    20207  22037  16727   -167   1724    -47       C  
ATOM    488  CE  LYS A 108      58.270 -31.875 154.576  1.00165.90           C  
ANISOU  488  CE  LYS A 108    21393  23592  18049    -92   1462    -85       C  
ATOM    489  NZ  LYS A 108      57.109 -31.061 154.124  1.00178.20           N  
ANISOU  489  NZ  LYS A 108    23177  25242  19289    203   1381    -49       N  
ATOM    490  N   VAL A 109      63.591 -34.598 151.086  1.00128.55           N  
ANISOU  490  N   VAL A 109    16651  18254  13936   -813   2364   -172       N  
ATOM    491  CA  VAL A 109      64.763 -34.774 150.216  1.00129.79           C  
ANISOU  491  CA  VAL A 109    16906  18206  14203   -941   2632   -176       C  
ATOM    492  C   VAL A 109      64.310 -35.381 148.874  1.00135.30           C  
ANISOU  492  C   VAL A 109    17733  19021  14653   -790   2636   -177       C  
ATOM    493  O   VAL A 109      64.561 -34.809 147.809  1.00136.91           O  
ANISOU  493  O   VAL A 109    18261  19073  14686   -678   2854   -116       O  
ATOM    494  CB  VAL A 109      65.835 -35.647 150.933  1.00132.27           C  
ANISOU  494  CB  VAL A 109    16894  18467  14898  -1237   2639   -264       C  
ATOM    495  CG1 VAL A 109      67.060 -35.868 150.051  1.00133.23           C  
ANISOU  495  CG1 VAL A 109    17094  18370  15158  -1383   2918   -285       C  
ATOM    496  CG2 VAL A 109      66.239 -35.038 152.275  1.00131.27           C  
ANISOU  496  CG2 VAL A 109    16636  18248  14993  -1353   2606   -284       C  
ATOM    497  N   ASN A 110      63.640 -36.540 148.957  1.00130.88           N  
ANISOU  497  N   ASN A 110    16921  18726  14080   -784   2405   -256       N  
ATOM    498  CA  ASN A 110      63.033 -37.300 147.862  1.00131.26           C  
ANISOU  498  CA  ASN A 110    17003  18954  13914   -642   2341   -301       C  
ATOM    499  C   ASN A 110      61.587 -37.473 148.308  1.00133.52           C  
ANISOU  499  C   ASN A 110    17167  19527  14038   -461   2046   -355       C  
ATOM    500  O   ASN A 110      61.319 -37.330 149.499  1.00132.04           O  
ANISOU  500  O   ASN A 110    16807  19380  13980   -526   1917   -360       O  
ATOM    501  CB  ASN A 110      63.701 -38.673 147.720  1.00131.77           C  
ANISOU  501  CB  ASN A 110    16799  19058  14209   -863   2358   -386       C  
ATOM    502  CG  ASN A 110      65.201 -38.646 147.870  1.00157.50           C  
ANISOU  502  CG  ASN A 110    20031  22048  17765  -1121   2592   -370       C  
ATOM    503  OD1 ASN A 110      65.740 -38.862 148.963  1.00150.16           O  
ANISOU  503  OD1 ASN A 110    18861  21076  17118  -1314   2550   -401       O  
ATOM    504  ND2 ASN A 110      65.903 -38.369 146.778  1.00151.43           N  
ANISOU  504  ND2 ASN A 110    19510  21089  16936  -1118   2846   -333       N  
ATOM    505  N   GLY A 111      60.678 -37.786 147.391  1.00129.87           N  
ANISOU  505  N   GLY A 111    16783  19256  13304   -238   1943   -409       N  
ATOM    506  CA  GLY A 111      59.263 -37.950 147.722  1.00128.84           C  
ANISOU  506  CA  GLY A 111    16529  19400  13024    -54   1670   -496       C  
ATOM    507  C   GLY A 111      58.902 -39.127 148.613  1.00129.18           C  
ANISOU  507  C   GLY A 111    16161  19622  13300   -215   1495   -615       C  
ATOM    508  O   GLY A 111      59.755 -39.686 149.309  1.00126.89           O  
ANISOU  508  O   GLY A 111    15670  19236  13305   -476   1560   -607       O  
ATOM    509  N   TRP A 112      57.623 -39.509 148.607  1.00125.22           N  
ANISOU  509  N   TRP A 112    15532  19377  12670    -51   1280   -738       N  
ATOM    510  CA  TRP A 112      57.172 -40.636 149.408  1.00123.24           C  
ANISOU  510  CA  TRP A 112    14907  19287  12631   -185   1142   -863       C  
ATOM    511  C   TRP A 112      57.423 -41.971 148.684  1.00128.11           C  
ANISOU  511  C   TRP A 112    15341  20000  13335   -284   1177   -979       C  
ATOM    512  O   TRP A 112      56.583 -42.440 147.908  1.00128.22           O  
ANISOU  512  O   TRP A 112    15311  20217  13191   -122   1075  -1120       O  
ATOM    513  CB  TRP A 112      55.716 -40.458 149.855  1.00121.80           C  
ANISOU  513  CB  TRP A 112    14639  19311  12329      3    922   -964       C  
ATOM    514  CG  TRP A 112      55.362 -41.349 151.002  1.00120.82           C  
ANISOU  514  CG  TRP A 112    14174  19274  12460   -159    832  -1052       C  
ATOM    515  CD1 TRP A 112      54.789 -42.583 150.932  1.00123.35           C  
ANISOU  515  CD1 TRP A 112    14216  19775  12878   -196    760  -1228       C  
ATOM    516  CD2 TRP A 112      55.641 -41.113 152.387  1.00119.08           C  
ANISOU  516  CD2 TRP A 112    13866  18944  12436   -306    829   -969       C  
ATOM    517  NE1 TRP A 112      54.656 -43.115 152.193  1.00121.17           N  
ANISOU  517  NE1 TRP A 112    13703  19497  12838   -349    728  -1249       N  
ATOM    518  CE2 TRP A 112      55.180 -42.238 153.105  1.00121.76           C  
ANISOU  518  CE2 TRP A 112    13895  19401  12969   -413    760  -1089       C  
ATOM    519  CE3 TRP A 112      56.211 -40.044 153.099  1.00119.95           C  
ANISOU  519  CE3 TRP A 112    14133  18867  12575   -349    885   -815       C  
ATOM    520  CZ2 TRP A 112      55.273 -42.328 154.498  1.00119.43           C  
ANISOU  520  CZ2 TRP A 112    13467  19042  12870   -542    740  -1046       C  
ATOM    521  CZ3 TRP A 112      56.306 -40.134 154.478  1.00119.81           C  
ANISOU  521  CZ3 TRP A 112    13959  18803  12759   -483    846   -788       C  
ATOM    522  CH2 TRP A 112      55.840 -41.265 155.163  1.00119.26           C  
ANISOU  522  CH2 TRP A 112    13605  18852  12855   -570    771   -895       C  
ATOM    523  N   ILE A 113      58.609 -42.560 148.933  1.00125.06           N  
ANISOU  523  N   ILE A 113    14845  19466  13206   -545   1322   -930       N  
ATOM    524  CA  ILE A 113      59.066 -43.834 148.349  1.00125.47           C  
ANISOU  524  CA  ILE A 113    14719  19566  13387   -685   1391  -1017       C  
ATOM    525  C   ILE A 113      58.760 -45.018 149.283  1.00129.81           C  
ANISOU  525  C   ILE A 113    14904  20230  14189   -841   1309  -1120       C  
ATOM    526  O   ILE A 113      58.579 -46.150 148.824  1.00129.45           O  
ANISOU  526  O   ILE A 113    14668  20311  14208   -889   1308  -1247       O  
ATOM    527  CB  ILE A 113      60.595 -43.811 148.038  1.00128.50           C  
ANISOU  527  CB  ILE A 113    15203  19706  13916   -879   1615   -910       C  
ATOM    528  CG1 ILE A 113      61.156 -42.390 147.862  1.00129.85           C  
ANISOU  528  CG1 ILE A 113    15712  19656  13968   -810   1743   -762       C  
ATOM    529  CG2 ILE A 113      60.937 -44.697 146.839  1.00130.28           C  
ANISOU  529  CG2 ILE A 113    15410  19974  14117   -910   1707   -982       C  
ATOM    530  CD1 ILE A 113      62.217 -42.051 148.857  1.00134.41           C  
ANISOU  530  CD1 ILE A 113    16244  20015  14812  -1026   1847   -675       C  
ATOM    531  N   PHE A 114      58.724 -44.732 150.594  1.00126.37           N  
ANISOU  531  N   PHE A 114    14388  19736  13891   -913   1258  -1062       N  
ATOM    532  CA  PHE A 114      58.569 -45.630 151.742  1.00125.06           C  
ANISOU  532  CA  PHE A 114    13935  19616  13966  -1054   1210  -1113       C  
ATOM    533  C   PHE A 114      57.401 -46.623 151.661  1.00131.27           C  
ANISOU  533  C   PHE A 114    14492  20628  14756   -995   1114  -1298       C  
ATOM    534  O   PHE A 114      57.467 -47.680 152.296  1.00130.13           O  
ANISOU  534  O   PHE A 114    14108  20503  14832  -1140   1145  -1353       O  
ATOM    535  CB  PHE A 114      58.505 -44.810 153.040  1.00125.70           C  
ANISOU  535  CB  PHE A 114    14054  19612  14094  -1054   1146  -1020       C  
ATOM    536  CG  PHE A 114      59.451 -43.630 153.009  1.00127.33           C  
ANISOU  536  CG  PHE A 114    14504  19612  14265  -1071   1236   -873       C  
ATOM    537  CD1 PHE A 114      60.829 -43.820 153.038  1.00129.51           C  
ANISOU  537  CD1 PHE A 114    14770  19710  14729  -1261   1379   -811       C  
ATOM    538  CD2 PHE A 114      58.966 -42.335 152.876  1.00130.34           C  
ANISOU  538  CD2 PHE A 114    15123  19970  14429   -893   1195   -812       C  
ATOM    539  CE1 PHE A 114      61.701 -42.732 152.957  1.00130.92           C  
ANISOU  539  CE1 PHE A 114    15160  19684  14899  -1284   1490   -707       C  
ATOM    540  CE2 PHE A 114      59.842 -41.247 152.802  1.00133.53           C  
ANISOU  540  CE2 PHE A 114    15756  20166  14815   -914   1315   -688       C  
ATOM    541  CZ  PHE A 114      61.201 -41.454 152.838  1.00131.03           C  
ANISOU  541  CZ  PHE A 114    15413  19668  14704  -1115   1468   -645       C  
ATOM    542  N   GLY A 115      56.376 -46.309 150.875  1.00130.61           N  
ANISOU  542  N   GLY A 115    14480  20705  14440   -779   1012  -1403       N  
ATOM    543  CA  GLY A 115      55.250 -47.213 150.694  1.00131.57           C  
ANISOU  543  CA  GLY A 115    14371  21046  14574   -713    926  -1621       C  
ATOM    544  C   GLY A 115      53.880 -46.607 150.879  1.00138.15           C  
ANISOU  544  C   GLY A 115    15218  22030  15241   -490    756  -1728       C  
ATOM    545  O   GLY A 115      53.710 -45.626 151.605  1.00137.49           O  
ANISOU  545  O   GLY A 115    15267  21876  15096   -426    697  -1620       O  
ATOM    546  N   THR A 116      52.889 -47.225 150.226  1.00137.15           N  
ANISOU  546  N   THR A 116    14937  22117  15057   -373    676  -1961       N  
ATOM    547  CA  THR A 116      51.475 -46.841 150.272  1.00138.59           C  
ANISOU  547  CA  THR A 116    15076  22480  15103   -151    504  -2131       C  
ATOM    548  C   THR A 116      50.940 -47.024 151.702  1.00140.10           C  
ANISOU  548  C   THR A 116    15089  22646  15498   -244    486  -2153       C  
ATOM    549  O   THR A 116      50.218 -46.163 152.205  1.00139.66           O  
ANISOU  549  O   THR A 116    15114  22610  15339   -107    373  -2143       O  
ATOM    550  CB  THR A 116      50.685 -47.651 149.223  1.00156.10           C  
ANISOU  550  CB  THR A 116    17119  24929  17263    -36    442  -2414       C  
ATOM    551  OG1 THR A 116      50.907 -49.046 149.451  1.00159.10           O  
ANISOU  551  OG1 THR A 116    17209  25315  17925   -260    565  -2519       O  
ATOM    552  CG2 THR A 116      51.086 -47.303 147.780  1.00157.67           C  
ANISOU  552  CG2 THR A 116    17547  25166  17193    122    433  -2395       C  
ATOM    553  N   PHE A 117      51.359 -48.127 152.362  1.00134.92           N  
ANISOU  553  N   PHE A 117    14212  21928  15124   -472    612  -2167       N  
ATOM    554  CA  PHE A 117      51.025 -48.522 153.737  1.00133.13           C  
ANISOU  554  CA  PHE A 117    13821  21645  15116   -585    647  -2175       C  
ATOM    555  C   PHE A 117      51.593 -47.545 154.768  1.00133.35           C  
ANISOU  555  C   PHE A 117    14038  21494  15136   -623    640  -1929       C  
ATOM    556  O   PHE A 117      50.870 -47.134 155.677  1.00132.38           O  
ANISOU  556  O   PHE A 117    13901  21371  15028   -570    575  -1940       O  
ATOM    557  CB  PHE A 117      51.512 -49.969 153.996  1.00134.36           C  
ANISOU  557  CB  PHE A 117    13744  21761  15546   -802    813  -2227       C  
ATOM    558  CG  PHE A 117      51.903 -50.338 155.410  1.00134.60           C  
ANISOU  558  CG  PHE A 117    13714  21634  15795   -962    912  -2105       C  
ATOM    559  CD1 PHE A 117      50.946 -50.771 156.324  1.00136.86           C  
ANISOU  559  CD1 PHE A 117    13840  21944  16216   -963    932  -2223       C  
ATOM    560  CD2 PHE A 117      53.234 -50.306 155.811  1.00136.86           C  
ANISOU  560  CD2 PHE A 117    14098  21745  16155  -1104    996  -1888       C  
ATOM    561  CE1 PHE A 117      51.312 -51.135 157.624  1.00138.67           C  
ANISOU  561  CE1 PHE A 117    14043  22023  16624  -1086   1033  -2104       C  
ATOM    562  CE2 PHE A 117      53.598 -50.658 157.114  1.00136.85           C  
ANISOU  562  CE2 PHE A 117    14051  21612  16333  -1219   1071  -1786       C  
ATOM    563  CZ  PHE A 117      52.636 -51.076 158.011  1.00135.88           C  
ANISOU  563  CZ  PHE A 117    13799  21512  16316  -1201   1090  -1885       C  
ATOM    564  N   LEU A 118      52.891 -47.187 154.628  1.00127.64           N  
ANISOU  564  N   LEU A 118    13480  20615  14401   -717    714  -1727       N  
ATOM    565  CA  LEU A 118      53.596 -46.258 155.512  1.00125.47           C  
ANISOU  565  CA  LEU A 118    13376  20165  14134   -764    719  -1513       C  
ATOM    566  C   LEU A 118      52.976 -44.861 155.517  1.00128.77           C  
ANISOU  566  C   LEU A 118    14000  20596  14330   -574    597  -1462       C  
ATOM    567  O   LEU A 118      53.142 -44.140 156.502  1.00127.57           O  
ANISOU  567  O   LEU A 118    13929  20334  14206   -595    577  -1338       O  
ATOM    568  CB  LEU A 118      55.082 -46.193 155.169  1.00124.91           C  
ANISOU  568  CB  LEU A 118    13417  19935  14109   -897    834  -1359       C  
ATOM    569  CG  LEU A 118      55.997 -46.722 156.250  1.00127.94           C  
ANISOU  569  CG  LEU A 118    13705  20176  14730  -1088    917  -1263       C  
ATOM    570  CD1 LEU A 118      56.614 -48.038 155.840  1.00127.91           C  
ANISOU  570  CD1 LEU A 118    13534  20173  14895  -1240   1036  -1317       C  
ATOM    571  CD2 LEU A 118      57.073 -45.718 156.583  1.00129.66           C  
ANISOU  571  CD2 LEU A 118    14112  20214  14937  -1132    939  -1086       C  
ATOM    572  N   CYS A 119      52.237 -44.489 154.439  1.00125.97           N  
ANISOU  572  N   CYS A 119    13730  20382  13752   -374    510  -1566       N  
ATOM    573  CA  CYS A 119      51.528 -43.210 154.374  1.00126.17           C  
ANISOU  573  CA  CYS A 119    13951  20438  13549   -161    388  -1536       C  
ATOM    574  C   CYS A 119      50.431 -43.235 155.415  1.00129.00           C  
ANISOU  574  C   CYS A 119    14162  20866  13985   -125    294  -1633       C  
ATOM    575  O   CYS A 119      50.384 -42.348 156.256  1.00128.21           O  
ANISOU  575  O   CYS A 119    14176  20676  13862   -105    258  -1513       O  
ATOM    576  CB  CYS A 119      50.958 -42.936 152.986  1.00128.11           C  
ANISOU  576  CB  CYS A 119    14309  20835  13532     71    309  -1649       C  
ATOM    577  SG  CYS A 119      50.431 -41.219 152.745  1.00133.16           S  
ANISOU  577  SG  CYS A 119    15279  21463  13852    350    198  -1550       S  
ATOM    578  N   LYS A 120      49.593 -44.294 155.389  1.00124.87           N  
ANISOU  578  N   LYS A 120    13377  20491  13577   -133    275  -1858       N  
ATOM    579  CA  LYS A 120      48.482 -44.525 156.312  1.00123.83           C  
ANISOU  579  CA  LYS A 120    13067  20424  13557   -114    220  -1998       C  
ATOM    580  C   LYS A 120      48.958 -44.600 157.763  1.00125.06           C  
ANISOU  580  C   LYS A 120    13200  20411  13906   -286    303  -1849       C  
ATOM    581  O   LYS A 120      48.290 -44.059 158.641  1.00124.46           O  
ANISOU  581  O   LYS A 120    13135  20319  13834   -234    242  -1846       O  
ATOM    582  CB  LYS A 120      47.692 -45.782 155.904  1.00126.63           C  
ANISOU  582  CB  LYS A 120    13133  20939  14040   -126    241  -2282       C  
ATOM    583  CG  LYS A 120      46.873 -45.574 154.635  1.00136.77           C  
ANISOU  583  CG  LYS A 120    14417  22434  15117    106    103  -2490       C  
ATOM    584  CD  LYS A 120      46.509 -46.861 153.920  1.00143.80           C  
ANISOU  584  CD  LYS A 120    15040  23472  16124     73    147  -2758       C  
ATOM    585  CE  LYS A 120      45.686 -46.564 152.688  1.00153.36           C  
ANISOU  585  CE  LYS A 120    16265  24902  17102    335    -17  -2974       C  
ATOM    586  NZ  LYS A 120      45.201 -47.803 152.027  1.00162.65           N  
ANISOU  586  NZ  LYS A 120    17147  26244  18409    313     13  -3284       N  
ATOM    587  N   VAL A 121      50.133 -45.220 158.002  1.00119.92           N  
ANISOU  587  N   VAL A 121    12529  19633  13402   -475    433  -1725       N  
ATOM    588  CA  VAL A 121      50.746 -45.341 159.332  1.00118.10           C  
ANISOU  588  CA  VAL A 121    12291  19243  13340   -620    506  -1581       C  
ATOM    589  C   VAL A 121      51.089 -43.948 159.878  1.00120.48           C  
ANISOU  589  C   VAL A 121    12820  19434  13524   -568    436  -1395       C  
ATOM    590  O   VAL A 121      50.627 -43.594 160.963  1.00119.75           O  
ANISOU  590  O   VAL A 121    12729  19299  13470   -555    400  -1366       O  
ATOM    591  CB  VAL A 121      51.981 -46.291 159.332  1.00121.29           C  
ANISOU  591  CB  VAL A 121    12625  19549  13910   -807    645  -1508       C  
ATOM    592  CG1 VAL A 121      52.704 -46.278 160.681  1.00119.77           C  
ANISOU  592  CG1 VAL A 121    12457  19196  13855   -917    693  -1355       C  
ATOM    593  CG2 VAL A 121      51.583 -47.713 158.954  1.00121.39           C  
ANISOU  593  CG2 VAL A 121    12398  19658  14066   -869    736  -1695       C  
ATOM    594  N   VAL A 122      51.863 -43.160 159.104  1.00116.12           N  
ANISOU  594  N   VAL A 122    12462  18829  12831   -536    433  -1281       N  
ATOM    595  CA  VAL A 122      52.301 -41.811 159.461  1.00115.37           C  
ANISOU  595  CA  VAL A 122    12590  18614  12630   -494    401  -1114       C  
ATOM    596  C   VAL A 122      51.120 -40.815 159.526  1.00119.94           C  
ANISOU  596  C   VAL A 122    13267  19273  13034   -300    273  -1151       C  
ATOM    597  O   VAL A 122      51.012 -40.081 160.510  1.00119.38           O  
ANISOU  597  O   VAL A 122    13262  19125  12973   -296    236  -1066       O  
ATOM    598  CB  VAL A 122      53.456 -41.337 158.542  1.00119.36           C  
ANISOU  598  CB  VAL A 122    13271  19021  13058   -522    481  -1003       C  
ATOM    599  CG1 VAL A 122      53.689 -39.835 158.650  1.00119.56           C  
ANISOU  599  CG1 VAL A 122    13547  18937  12944   -439    465   -866       C  
ATOM    600  CG2 VAL A 122      54.742 -42.099 158.853  1.00118.13           C  
ANISOU  600  CG2 VAL A 122    13026  18747  13111   -730    599   -943       C  
ATOM    601  N   SER A 123      50.233 -40.814 158.511  1.00117.13           N  
ANISOU  601  N   SER A 123    12911  19076  12518   -133    199  -1291       N  
ATOM    602  CA  SER A 123      49.063 -39.929 158.437  1.00117.46           C  
ANISOU  602  CA  SER A 123    13034  19215  12380     81     63  -1356       C  
ATOM    603  C   SER A 123      48.079 -40.115 159.588  1.00119.61           C  
ANISOU  603  C   SER A 123    13148  19525  12773     73      5  -1448       C  
ATOM    604  O   SER A 123      47.467 -39.136 160.012  1.00119.24           O  
ANISOU  604  O   SER A 123    13206  19478  12624    191    -83  -1420       O  
ATOM    605  CB  SER A 123      48.344 -40.074 157.100  1.00122.57           C  
ANISOU  605  CB  SER A 123    13681  20044  12846    272    -15  -1523       C  
ATOM    606  OG  SER A 123      49.174 -39.665 156.025  1.00132.59           O  
ANISOU  606  OG  SER A 123    15161  21262  13956    320     42  -1417       O  
ATOM    607  N   LEU A 124      47.929 -41.355 160.095  1.00115.13           N  
ANISOU  607  N   LEU A 124    12342  18978  12423    -63     72  -1558       N  
ATOM    608  CA  LEU A 124      47.030 -41.640 161.214  1.00114.58           C  
ANISOU  608  CA  LEU A 124    12129  18917  12491    -83     61  -1650       C  
ATOM    609  C   LEU A 124      47.599 -41.096 162.523  1.00115.62           C  
ANISOU  609  C   LEU A 124    12364  18877  12690   -176     92  -1453       C  
ATOM    610  O   LEU A 124      46.862 -40.483 163.287  1.00115.18           O  
ANISOU  610  O   LEU A 124    12340  18812  12613   -110     28  -1457       O  
ATOM    611  CB  LEU A 124      46.713 -43.143 161.327  1.00114.91           C  
ANISOU  611  CB  LEU A 124    11904  19009  12748   -193    164  -1829       C  
ATOM    612  CG  LEU A 124      45.733 -43.571 162.434  1.00120.17           C  
ANISOU  612  CG  LEU A 124    12417  19667  13576   -215    198  -1952       C  
ATOM    613  CD1 LEU A 124      44.281 -43.262 162.062  1.00121.74           C  
ANISOU  613  CD1 LEU A 124    12529  20024  13703    -43     82  -2187       C  
ATOM    614  CD2 LEU A 124      45.893 -45.043 162.750  1.00123.32           C  
ANISOU  614  CD2 LEU A 124    12612  20032  14212   -370    369  -2042       C  
ATOM    615  N   LEU A 125      48.904 -41.288 162.765  1.00109.98           N  
ANISOU  615  N   LEU A 125    11701  18033  12054   -320    181  -1296       N  
ATOM    616  CA  LEU A 125      49.545 -40.790 163.978  1.00108.08           C  
ANISOU  616  CA  LEU A 125    11550  17639  11877   -398    198  -1129       C  
ATOM    617  C   LEU A 125      49.481 -39.259 164.087  1.00112.53           C  
ANISOU  617  C   LEU A 125    12323  18156  12277   -295    111  -1016       C  
ATOM    618  O   LEU A 125      49.101 -38.769 165.147  1.00112.22           O  
ANISOU  618  O   LEU A 125    12314  18062  12261   -285     75   -971       O  
ATOM    619  CB  LEU A 125      50.991 -41.309 164.142  1.00106.98           C  
ANISOU  619  CB  LEU A 125    11405  17382  11859   -556    297  -1016       C  
ATOM    620  CG  LEU A 125      51.247 -42.830 164.111  1.00110.74           C  
ANISOU  620  CG  LEU A 125    11691  17875  12510   -670    405  -1096       C  
ATOM    621  CD1 LEU A 125      52.628 -43.146 164.609  1.00109.86           C  
ANISOU  621  CD1 LEU A 125    11594  17632  12515   -802    476   -971       C  
ATOM    622  CD2 LEU A 125      50.240 -43.612 164.944  1.00113.36           C  
ANISOU  622  CD2 LEU A 125    11878  18237  12958   -667    441  -1209       C  
ATOM    623  N   LYS A 126      49.780 -38.514 162.990  1.00109.60           N  
ANISOU  623  N   LYS A 126    12105  17801  11737   -210     91   -975       N  
ATOM    624  CA  LYS A 126      49.752 -37.041 162.984  1.00109.78           C  
ANISOU  624  CA  LYS A 126    12349  17766  11597   -103     40   -864       C  
ATOM    625  C   LYS A 126      48.345 -36.450 163.194  1.00115.35           C  
ANISOU  625  C   LYS A 126    13066  18570  12191     65    -79   -948       C  
ATOM    626  O   LYS A 126      48.220 -35.378 163.797  1.00114.87           O  
ANISOU  626  O   LYS A 126    13137  18440  12068    113   -117   -855       O  
ATOM    627  CB  LYS A 126      50.432 -36.444 161.736  1.00112.46           C  
ANISOU  627  CB  LYS A 126    12874  18071  11784    -45     88   -794       C  
ATOM    628  CG  LYS A 126      49.673 -36.552 160.420  1.00123.26           C  
ANISOU  628  CG  LYS A 126    14268  19593  12971    129     35   -912       C  
ATOM    629  CD  LYS A 126      50.304 -35.625 159.392  1.00134.83           C  
ANISOU  629  CD  LYS A 126    16000  20984  14245    225     94   -800       C  
ATOM    630  CE  LYS A 126      49.646 -35.677 158.038  1.00144.27           C  
ANISOU  630  CE  LYS A 126    17263  22329  15223    434     35   -907       C  
ATOM    631  NZ  LYS A 126      50.309 -34.753 157.081  1.00150.30           N  
ANISOU  631  NZ  LYS A 126    18327  22989  15790    538    126   -779       N  
ATOM    632  N   GLU A 127      47.302 -37.155 162.713  1.00113.18           N  
ANISOU  632  N   GLU A 127    12641  18456  11906    149   -134  -1140       N  
ATOM    633  CA  GLU A 127      45.899 -36.759 162.853  1.00114.05           C  
ANISOU  633  CA  GLU A 127    12718  18677  11938    310   -251  -1270       C  
ATOM    634  C   GLU A 127      45.383 -37.131 164.251  1.00116.16           C  
ANISOU  634  C   GLU A 127    12848  18900  12387    218   -237  -1308       C  
ATOM    635  O   GLU A 127      44.725 -36.306 164.891  1.00115.34           O  
ANISOU  635  O   GLU A 127    12811  18779  12234    294   -305  -1288       O  
ATOM    636  CB  GLU A 127      45.033 -37.401 161.752  1.00117.04           C  
ANISOU  636  CB  GLU A 127    12969  19250  12253    440   -315  -1499       C  
ATOM    637  CG  GLU A 127      45.112 -36.712 160.398  1.00131.92           C  
ANISOU  637  CG  GLU A 127    15043  21203  13879    629   -375  -1480       C  
ATOM    638  CD  GLU A 127      44.152 -35.552 160.218  1.00159.84           C  
ANISOU  638  CD  GLU A 127    18717  24809  17207    870   -513  -1510       C  
ATOM    639  OE1 GLU A 127      44.443 -34.449 160.737  1.00157.53           O  
ANISOU  639  OE1 GLU A 127    18618  24392  16844    885   -505  -1331       O  
ATOM    640  OE2 GLU A 127      43.107 -35.745 159.556  1.00156.19           O  
ANISOU  640  OE2 GLU A 127    18161  24528  16656   1050   -629  -1726       O  
ATOM    641  N   VAL A 128      45.706 -38.366 164.726  1.00111.56           N  
ANISOU  641  N   VAL A 128    12093  18287  12008     60   -133  -1353       N  
ATOM    642  CA  VAL A 128      45.330 -38.876 166.051  1.00110.27           C  
ANISOU  642  CA  VAL A 128    11820  18055  12021    -29    -78  -1378       C  
ATOM    643  C   VAL A 128      45.946 -37.989 167.132  1.00113.41           C  
ANISOU  643  C   VAL A 128    12378  18305  12408    -73    -84  -1175       C  
ATOM    644  O   VAL A 128      45.223 -37.565 168.031  1.00112.69           O  
ANISOU  644  O   VAL A 128    12299  18185  12333    -38   -117  -1185       O  
ATOM    645  CB  VAL A 128      45.608 -40.399 166.238  1.00113.36           C  
ANISOU  645  CB  VAL A 128    12024  18432  12616   -169     59  -1457       C  
ATOM    646  CG1 VAL A 128      45.718 -40.795 167.708  1.00112.19           C  
ANISOU  646  CG1 VAL A 128    11856  18151  12622   -267    149  -1391       C  
ATOM    647  CG2 VAL A 128      44.538 -41.237 165.544  1.00114.08           C  
ANISOU  647  CG2 VAL A 128    11911  18669  12763   -117     70  -1721       C  
ATOM    648  N   ASN A 129      47.240 -37.629 166.991  1.00110.17           N  
ANISOU  648  N   ASN A 129    12089  17802  11967   -142    -56  -1010       N  
ATOM    649  CA  ASN A 129      47.934 -36.727 167.919  1.00109.88           C  
ANISOU  649  CA  ASN A 129    12194  17630  11924   -182    -65   -840       C  
ATOM    650  C   ASN A 129      47.183 -35.387 168.080  1.00114.40           C  
ANISOU  650  C   ASN A 129    12902  18210  12355    -54   -160   -811       C  
ATOM    651  O   ASN A 129      47.132 -34.858 169.199  1.00114.00           O  
ANISOU  651  O   ASN A 129    12901  18077  12335    -72   -177   -741       O  
ATOM    652  CB  ASN A 129      49.407 -36.515 167.502  1.00111.84           C  
ANISOU  652  CB  ASN A 129    12531  17790  12172   -267    -13   -716       C  
ATOM    653  CG  ASN A 129      49.957 -35.116 167.713  1.00139.19           C  
ANISOU  653  CG  ASN A 129    16182  21152  15552   -247    -36   -582       C  
ATOM    654  OD1 ASN A 129      50.078 -34.325 166.768  1.00138.45           O  
ANISOU  654  OD1 ASN A 129    16223  21057  15323   -176    -34   -545       O  
ATOM    655  ND2 ASN A 129      50.292 -34.775 168.954  1.00127.71           N  
ANISOU  655  ND2 ASN A 129    14748  19603  14173   -300    -46   -512       N  
ATOM    656  N   PHE A 130      46.585 -34.860 166.975  1.00110.71           N  
ANISOU  656  N   PHE A 130    12498  17842  11725     88   -222   -868       N  
ATOM    657  CA  PHE A 130      45.830 -33.608 167.017  1.00110.32           C  
ANISOU  657  CA  PHE A 130    12584  17806  11526    234   -311   -845       C  
ATOM    658  C   PHE A 130      44.493 -33.768 167.724  1.00114.10           C  
ANISOU  658  C   PHE A 130    12948  18349  12055    290   -372   -977       C  
ATOM    659  O   PHE A 130      44.266 -33.092 168.727  1.00112.91           O  
ANISOU  659  O   PHE A 130    12859  18123  11918    286   -394   -910       O  
ATOM    660  CB  PHE A 130      45.654 -32.979 165.625  1.00112.96           C  
ANISOU  660  CB  PHE A 130    13050  18221  11650    399   -356   -860       C  
ATOM    661  CG  PHE A 130      44.889 -31.672 165.639  1.00114.80           C  
ANISOU  661  CG  PHE A 130    13440  18464  11715    571   -442   -830       C  
ATOM    662  CD1 PHE A 130      45.509 -30.488 166.019  1.00117.26           C  
ANISOU  662  CD1 PHE A 130    13948  18637  11970    561   -405   -655       C  
ATOM    663  CD2 PHE A 130      43.551 -31.627 165.274  1.00117.87           C  
ANISOU  663  CD2 PHE A 130    13769  19001  12014    746   -557   -993       C  
ATOM    664  CE1 PHE A 130      44.802 -29.283 166.039  1.00118.75           C  
ANISOU  664  CE1 PHE A 130    14287  18827  12005    720   -471   -622       C  
ATOM    665  CE2 PHE A 130      42.842 -30.423 165.305  1.00121.45           C  
ANISOU  665  CE2 PHE A 130    14369  19464  12312    915   -640   -965       C  
ATOM    666  CZ  PHE A 130      43.474 -29.259 165.684  1.00119.06           C  
ANISOU  666  CZ  PHE A 130    14277  19015  11945    901   -592   -769       C  
ATOM    667  N   TYR A 131      43.612 -34.648 167.203  1.00111.77           N  
ANISOU  667  N   TYR A 131    12482  18187  11799    340   -391  -1179       N  
ATOM    668  CA  TYR A 131      42.274 -34.879 167.759  1.00112.04           C  
ANISOU  668  CA  TYR A 131    12380  18283  11908    393   -430  -1351       C  
ATOM    669  C   TYR A 131      42.305 -35.346 169.217  1.00113.83           C  
ANISOU  669  C   TYR A 131    12543  18388  12318    255   -340  -1315       C  
ATOM    670  O   TYR A 131      41.474 -34.888 169.997  1.00113.37           O  
ANISOU  670  O   TYR A 131    12489  18306  12279    296   -371  -1350       O  
ATOM    671  CB  TYR A 131      41.429 -35.819 166.872  1.00114.74           C  
ANISOU  671  CB  TYR A 131    12522  18786  12286    459   -448  -1608       C  
ATOM    672  CG  TYR A 131      41.172 -35.290 165.474  1.00118.75           C  
ANISOU  672  CG  TYR A 131    13104  19435  12580    650   -565  -1673       C  
ATOM    673  CD1 TYR A 131      40.521 -34.076 165.273  1.00121.57           C  
ANISOU  673  CD1 TYR A 131    13600  19836  12756    839   -691  -1665       C  
ATOM    674  CD2 TYR A 131      41.547 -36.021 164.350  1.00120.53           C  
ANISOU  674  CD2 TYR A 131    13269  19752  12775    660   -547  -1749       C  
ATOM    675  CE1 TYR A 131      40.284 -33.582 163.990  1.00123.98           C  
ANISOU  675  CE1 TYR A 131    14003  20266  12836   1049   -796  -1719       C  
ATOM    676  CE2 TYR A 131      41.304 -35.545 163.060  1.00123.16           C  
ANISOU  676  CE2 TYR A 131    13695  20214  12888    862   -654  -1809       C  
ATOM    677  CZ  TYR A 131      40.667 -34.326 162.884  1.00132.28           C  
ANISOU  677  CZ  TYR A 131    15004  21407  13847   1067   -780  -1793       C  
ATOM    678  OH  TYR A 131      40.422 -33.852 161.615  1.00135.55           O  
ANISOU  678  OH  TYR A 131    15537  21947  14019   1300   -884  -1848       O  
ATOM    679  N   SER A 132      43.282 -36.196 169.597  1.00109.03           N  
ANISOU  679  N   SER A 132    11897  17697  11834    106   -230  -1238       N  
ATOM    680  CA  SER A 132      43.420 -36.658 170.980  1.00108.12           C  
ANISOU  680  CA  SER A 132    11758  17458  11865      2   -139  -1186       C  
ATOM    681  C   SER A 132      43.904 -35.510 171.871  1.00110.89           C  
ANISOU  681  C   SER A 132    12288  17699  12146      1   -189  -1001       C  
ATOM    682  O   SER A 132      43.306 -35.267 172.918  1.00109.89           O  
ANISOU  682  O   SER A 132    12180  17513  12060     10   -185  -1001       O  
ATOM    683  CB  SER A 132      44.371 -37.849 171.078  1.00111.79           C  
ANISOU  683  CB  SER A 132    12148  17870  12456   -126    -19  -1154       C  
ATOM    684  OG  SER A 132      45.693 -37.501 170.693  1.00120.45           O  
ANISOU  684  OG  SER A 132    13348  18926  13490   -174    -36   -999       O  
ATOM    685  N   GLY A 133      44.950 -34.806 171.422  1.00106.99           N  
ANISOU  685  N   GLY A 133    11921  17175  11555     -9   -223   -861       N  
ATOM    686  CA  GLY A 133      45.546 -33.668 172.117  1.00106.00           C  
ANISOU  686  CA  GLY A 133    11955  16946  11372    -17   -260   -702       C  
ATOM    687  C   GLY A 133      44.586 -32.515 172.336  1.00109.30           C  
ANISOU  687  C   GLY A 133    12463  17379  11687     94   -343   -705       C  
ATOM    688  O   GLY A 133      44.575 -31.922 173.416  1.00108.39           O  
ANISOU  688  O   GLY A 133    12418  17178  11588     78   -356   -629       O  
ATOM    689  N   ILE A 134      43.754 -32.204 171.328  1.00106.12           N  
ANISOU  689  N   ILE A 134    12057  17088  11174    219   -405   -800       N  
ATOM    690  CA  ILE A 134      42.778 -31.126 171.433  1.00106.13           C  
ANISOU  690  CA  ILE A 134    12141  17117  11069    348   -492   -817       C  
ATOM    691  C   ILE A 134      41.620 -31.529 172.355  1.00109.14           C  
ANISOU  691  C   ILE A 134    12404  17506  11559    351   -494   -942       C  
ATOM    692  O   ILE A 134      41.129 -30.672 173.086  1.00109.16           O  
ANISOU  692  O   ILE A 134    12483  17460  11532    390   -534   -902       O  
ATOM    693  CB  ILE A 134      42.322 -30.583 170.049  1.00110.71           C  
ANISOU  693  CB  ILE A 134    12782  17813  11469    515   -569   -875       C  
ATOM    694  CG1 ILE A 134      41.802 -29.135 170.169  1.00111.80           C  
ANISOU  694  CG1 ILE A 134    13087  17932  11461    646   -643   -807       C  
ATOM    695  CG2 ILE A 134      41.322 -31.517 169.333  1.00112.35           C  
ANISOU  695  CG2 ILE A 134    12807  18176  11703    593   -607  -1105       C  
ATOM    696  CD1 ILE A 134      41.883 -28.272 168.917  1.00122.80           C  
ANISOU  696  CD1 ILE A 134    14647  19374  12638    812   -683   -766       C  
ATOM    697  N   TRP A 135      41.210 -32.826 172.348  1.00104.83           N  
ANISOU  697  N   TRP A 135    11677  17004  11151    302   -428  -1094       N  
ATOM    698  CA  TRP A 135      40.130 -33.343 173.206  1.00104.12           C  
ANISOU  698  CA  TRP A 135    11469  16896  11197    291   -382  -1233       C  
ATOM    699  C   TRP A 135      40.563 -33.495 174.657  1.00103.65           C  
ANISOU  699  C   TRP A 135    11465  16682  11235    185   -294  -1114       C  
ATOM    700  O   TRP A 135      39.753 -33.256 175.549  1.00102.40           O  
ANISOU  700  O   TRP A 135    11311  16471  11127    200   -279  -1153       O  
ATOM    701  CB  TRP A 135      39.537 -34.651 172.667  1.00103.97           C  
ANISOU  701  CB  TRP A 135    11236  16962  11305    276   -312  -1456       C  
ATOM    702  CG  TRP A 135      38.378 -34.436 171.742  1.00106.84           C  
ANISOU  702  CG  TRP A 135    11502  17480  11613    421   -413  -1670       C  
ATOM    703  CD1 TRP A 135      38.379 -34.559 170.384  1.00110.73           C  
ANISOU  703  CD1 TRP A 135    11947  18117  12008    512   -486  -1766       C  
ATOM    704  CD2 TRP A 135      37.056 -34.005 172.106  1.00107.72           C  
ANISOU  704  CD2 TRP A 135    11554  17620  11754    510   -462  -1827       C  
ATOM    705  NE1 TRP A 135      37.132 -34.260 169.880  1.00111.72           N  
ANISOU  705  NE1 TRP A 135    11983  18373  12095    667   -592  -1983       N  
ATOM    706  CE2 TRP A 135      36.300 -33.922 170.916  1.00113.13           C  
ANISOU  706  CE2 TRP A 135    12142  18481  12360    663   -578  -2030       C  
ATOM    707  CE3 TRP A 135      36.431 -33.696 173.328  1.00108.77           C  
ANISOU  707  CE3 TRP A 135    11708  17646  11975    482   -418  -1824       C  
ATOM    708  CZ2 TRP A 135      34.963 -33.510 170.908  1.00113.62           C  
ANISOU  708  CZ2 TRP A 135    12116  18620  12433    791   -663  -2238       C  
ATOM    709  CZ3 TRP A 135      35.099 -33.313 173.320  1.00111.23           C  
ANISOU  709  CZ3 TRP A 135    11932  18020  12309    589   -484  -2024       C  
ATOM    710  CH2 TRP A 135      34.380 -33.221 172.123  1.00113.30           C  
ANISOU  710  CH2 TRP A 135    12085  18463  12499    742   -610  -2233       C  
ATOM    711  N   LEU A 136      41.845 -33.874 174.891  1.00 98.00           N  
ANISOU  711  N   LEU A 136    10798  15895  10543     89   -241   -975       N  
ATOM    712  CA  LEU A 136      42.443 -34.012 176.222  1.00 96.24           C  
ANISOU  712  CA  LEU A 136    10646  15537  10385     17   -179   -856       C  
ATOM    713  C   LEU A 136      42.512 -32.650 176.890  1.00 99.20           C  
ANISOU  713  C   LEU A 136    11174  15853  10666     53   -265   -736       C  
ATOM    714  O   LEU A 136      42.314 -32.563 178.103  1.00 99.33           O  
ANISOU  714  O   LEU A 136    11241  15777  10724     41   -234   -698       O  
ATOM    715  CB  LEU A 136      43.855 -34.608 176.152  1.00 95.53           C  
ANISOU  715  CB  LEU A 136    10567  15407  10325    -67   -136   -754       C  
ATOM    716  CG  LEU A 136      43.972 -36.111 175.941  1.00 99.98           C  
ANISOU  716  CG  LEU A 136    10996  15979  11012   -126    -13   -839       C  
ATOM    717  CD1 LEU A 136      45.333 -36.463 175.407  1.00 99.87           C  
ANISOU  717  CD1 LEU A 136    10984  15966  10996   -191     -8   -756       C  
ATOM    718  CD2 LEU A 136      43.679 -36.884 177.215  1.00102.11           C  
ANISOU  718  CD2 LEU A 136    11265  16139  11393   -149    109   -848       C  
ATOM    719  N   LEU A 137      42.782 -31.586 176.095  1.00 94.41           N  
ANISOU  719  N   LEU A 137    10650  15292   9929    104   -358   -677       N  
ATOM    720  CA  LEU A 137      42.830 -30.205 176.573  1.00 93.42           C  
ANISOU  720  CA  LEU A 137    10668  15114   9713    142   -427   -571       C  
ATOM    721  C   LEU A 137      41.449 -29.721 177.001  1.00 96.45           C  
ANISOU  721  C   LEU A 137    11050  15513  10083    221   -464   -651       C  
ATOM    722  O   LEU A 137      41.349 -28.935 177.940  1.00 95.21           O  
ANISOU  722  O   LEU A 137    10989  15281   9906    224   -487   -576       O  
ATOM    723  CB  LEU A 137      43.439 -29.260 175.527  1.00 93.74           C  
ANISOU  723  CB  LEU A 137    10809  15183   9625    183   -474   -496       C  
ATOM    724  CG  LEU A 137      44.967 -29.235 175.446  1.00 97.99           C  
ANISOU  724  CG  LEU A 137    11396  15654  10181     92   -436   -386       C  
ATOM    725  CD1 LEU A 137      45.424 -28.411 174.279  1.00 98.61           C  
ANISOU  725  CD1 LEU A 137    11575  15749  10143    140   -442   -336       C  
ATOM    726  CD2 LEU A 137      45.598 -28.694 176.724  1.00100.14           C  
ANISOU  726  CD2 LEU A 137    11740  15814  10495     36   -439   -291       C  
ATOM    727  N   ALA A 138      40.390 -30.218 176.339  1.00 93.85           N  
ANISOU  727  N   ALA A 138    10602  15282   9776    283   -469   -819       N  
ATOM    728  CA  ALA A 138      39.007 -29.888 176.671  1.00 94.52           C  
ANISOU  728  CA  ALA A 138    10649  15390   9876    360   -500   -941       C  
ATOM    729  C   ALA A 138      38.596 -30.556 177.989  1.00 97.84           C  
ANISOU  729  C   ALA A 138    11024  15704  10445    288   -394   -980       C  
ATOM    730  O   ALA A 138      37.804 -29.986 178.741  1.00 97.50           O  
ANISOU  730  O   ALA A 138    11016  15614  10415    319   -404  -1002       O  
ATOM    731  CB  ALA A 138      38.075 -30.313 175.545  1.00 96.42           C  
ANISOU  731  CB  ALA A 138    10749  15774  10111    454   -540  -1145       C  
ATOM    732  N   CYS A 139      39.150 -31.751 178.271  1.00 94.03           N  
ANISOU  732  N   CYS A 139    10480  15176  10070    200   -280   -983       N  
ATOM    733  CA  CYS A 139      38.880 -32.516 179.488  1.00 93.79           C  
ANISOU  733  CA  CYS A 139    10439  15026  10171    144   -143  -1004       C  
ATOM    734  C   CYS A 139      39.524 -31.868 180.690  1.00 96.37           C  
ANISOU  734  C   CYS A 139    10932  15235  10448    124   -157   -825       C  
ATOM    735  O   CYS A 139      38.972 -31.937 181.789  1.00 95.41           O  
ANISOU  735  O   CYS A 139    10856  15013  10385    122    -81   -834       O  
ATOM    736  CB  CYS A 139      39.313 -33.966 179.325  1.00 94.41           C  
ANISOU  736  CB  CYS A 139    10419  15092  10361     76    -10  -1054       C  
ATOM    737  SG  CYS A 139      38.396 -34.860 178.048  1.00 99.45           S  
ANISOU  737  SG  CYS A 139    10828  15860  11097     94     35  -1316       S  
ATOM    738  N   ILE A 140      40.673 -31.208 180.469  1.00 93.18           N  
ANISOU  738  N   ILE A 140    10619  14842   9942    112   -248   -678       N  
ATOM    739  CA  ILE A 140      41.377 -30.435 181.484  1.00 93.35           C  
ANISOU  739  CA  ILE A 140    10783  14773   9912    101   -287   -531       C  
ATOM    740  C   ILE A 140      40.491 -29.224 181.823  1.00100.20           C  
ANISOU  740  C   ILE A 140    11720  15629  10724    155   -353   -530       C  
ATOM    741  O   ILE A 140      40.270 -28.972 183.003  1.00100.07           O  
ANISOU  741  O   ILE A 140    11780  15520  10721    156   -329   -492       O  
ATOM    742  CB  ILE A 140      42.815 -30.042 181.028  1.00 96.11           C  
ANISOU  742  CB  ILE A 140    11179  15138  10200     66   -351   -417       C  
ATOM    743  CG1 ILE A 140      43.735 -31.293 180.975  1.00 95.74           C  
ANISOU  743  CG1 ILE A 140    11072  15079  10224     11   -281   -411       C  
ATOM    744  CG2 ILE A 140      43.410 -28.950 181.943  1.00 97.16           C  
ANISOU  744  CG2 ILE A 140    11440  15198  10279     66   -414   -304       C  
ATOM    745  CD1 ILE A 140      45.133 -31.138 180.327  1.00 95.42           C  
ANISOU  745  CD1 ILE A 140    11036  15062  10159    -34   -323   -342       C  
ATOM    746  N   SER A 141      39.924 -28.539 180.795  1.00 99.07           N  
ANISOU  746  N   SER A 141    11550  15579  10512    213   -429   -581       N  
ATOM    747  CA  SER A 141      39.017 -27.390 180.954  1.00100.09           C  
ANISOU  747  CA  SER A 141    11736  15714  10581    283   -496   -594       C  
ATOM    748  C   SER A 141      37.806 -27.753 181.813  1.00106.24           C  
ANISOU  748  C   SER A 141    12467  16441  11458    292   -432   -707       C  
ATOM    749  O   SER A 141      37.529 -27.049 182.780  1.00106.25           O  
ANISOU  749  O   SER A 141    12557  16367  11446    299   -443   -657       O  
ATOM    750  CB  SER A 141      38.525 -26.870 179.606  1.00104.76           C  
ANISOU  750  CB  SER A 141    12295  16428  11082    376   -577   -663       C  
ATOM    751  OG  SER A 141      39.377 -27.172 178.517  1.00115.74           O  
ANISOU  751  OG  SER A 141    13680  17879  12419    370   -589   -625       O  
ATOM    752  N   VAL A 142      37.109 -28.862 181.476  1.00104.22           N  
ANISOU  752  N   VAL A 142    12067  16218  11313    286   -349   -871       N  
ATOM    753  CA  VAL A 142      35.931 -29.374 182.191  1.00105.21           C  
ANISOU  753  CA  VAL A 142    12125  16280  11569    284   -245  -1016       C  
ATOM    754  C   VAL A 142      36.242 -29.621 183.680  1.00109.91           C  
ANISOU  754  C   VAL A 142    12837  16713  12209    231   -137   -913       C  
ATOM    755  O   VAL A 142      35.459 -29.215 184.544  1.00109.31           O  
ANISOU  755  O   VAL A 142    12812  16555  12166    244   -102   -937       O  
ATOM    756  CB  VAL A 142      35.337 -30.616 181.466  1.00109.94           C  
ANISOU  756  CB  VAL A 142    12534  16939  12300    275   -151  -1226       C  
ATOM    757  CG1 VAL A 142      34.405 -31.431 182.369  1.00110.18           C  
ANISOU  757  CG1 VAL A 142    12504  16851  12508    238     31  -1368       C  
ATOM    758  CG2 VAL A 142      34.625 -30.205 180.178  1.00110.56           C  
ANISOU  758  CG2 VAL A 142    12497  17180  12329    368   -276  -1376       C  
ATOM    759  N   ASP A 143      37.405 -30.242 183.964  1.00107.24           N  
ANISOU  759  N   ASP A 143    12553  16334  11861    185    -93   -799       N  
ATOM    760  CA  ASP A 143      37.862 -30.535 185.323  1.00107.34           C  
ANISOU  760  CA  ASP A 143    12694  16206  11884    168     -8   -696       C  
ATOM    761  C   ASP A 143      38.163 -29.261 186.102  1.00110.30           C  
ANISOU  761  C   ASP A 143    13216  16540  12152    190   -115   -563       C  
ATOM    762  O   ASP A 143      37.700 -29.126 187.233  1.00109.74           O  
ANISOU  762  O   ASP A 143    13241  16359  12098    204    -52   -545       O  
ATOM    763  CB  ASP A 143      39.089 -31.465 185.307  1.00109.40           C  
ANISOU  763  CB  ASP A 143    12964  16456  12147    138     37   -620       C  
ATOM    764  CG  ASP A 143      38.885 -32.748 186.088  1.00124.40           C  
ANISOU  764  CG  ASP A 143    14882  18235  14148    133    238   -659       C  
ATOM    765  OD1 ASP A 143      38.066 -33.596 185.642  1.00126.43           O  
ANISOU  765  OD1 ASP A 143    15015  18494  14530    112    370   -813       O  
ATOM    766  OD2 ASP A 143      39.541 -32.911 187.144  1.00130.64           O  
ANISOU  766  OD2 ASP A 143    15815  18928  14893    161    270   -546       O  
ATOM    767  N   ARG A 144      38.903 -28.320 185.482  1.00106.42           N  
ANISOU  767  N   ARG A 144    12746  16129  11560    192   -259   -479       N  
ATOM    768  CA  ARG A 144      39.293 -27.050 186.098  1.00105.80           C  
ANISOU  768  CA  ARG A 144    12790  16016  11392    204   -354   -366       C  
ATOM    769  C   ARG A 144      38.124 -26.072 186.264  1.00111.43           C  
ANISOU  769  C   ARG A 144    13527  16721  12090    240   -386   -406       C  
ATOM    770  O   ARG A 144      38.136 -25.310 187.230  1.00111.54           O  
ANISOU  770  O   ARG A 144    13648  16663  12067    246   -411   -336       O  
ATOM    771  CB  ARG A 144      40.482 -26.390 185.366  1.00103.19           C  
ANISOU  771  CB  ARG A 144    12474  15749  10984    186   -455   -279       C  
ATOM    772  CG  ARG A 144      41.759 -27.245 185.237  1.00106.35           C  
ANISOU  772  CG  ARG A 144    12849  16154  11404    148   -437   -240       C  
ATOM    773  CD  ARG A 144      42.432 -27.601 186.551  1.00114.17           C  
ANISOU  773  CD  ARG A 144    13922  17056  12401    153   -417   -182       C  
ATOM    774  NE  ARG A 144      42.002 -28.909 187.048  1.00122.03           N  
ANISOU  774  NE  ARG A 144    14906  17998  13463    169   -292   -229       N  
ATOM    775  CZ  ARG A 144      41.657 -29.164 188.307  1.00132.51           C  
ANISOU  775  CZ  ARG A 144    16334  19222  14793    211   -224   -214       C  
ATOM    776  NH1 ARG A 144      41.698 -28.202 189.223  1.00111.62           N  
ANISOU  776  NH1 ARG A 144    13798  16529  12084    240   -290   -158       N  
ATOM    777  NH2 ARG A 144      41.285 -30.385 188.664  1.00122.27           N  
ANISOU  777  NH2 ARG A 144    15039  17859  13561    229    -75   -257       N  
ATOM    778  N   TYR A 145      37.114 -26.101 185.356  1.00108.72           N  
ANISOU  778  N   TYR A 145    13080  16454  11776    273   -392   -531       N  
ATOM    779  CA  TYR A 145      35.917 -25.244 185.427  1.00109.01           C  
ANISOU  779  CA  TYR A 145    13118  16492  11808    322   -429   -597       C  
ATOM    780  C   TYR A 145      35.078 -25.629 186.658  1.00111.59           C  
ANISOU  780  C   TYR A 145    13469  16694  12234    305   -312   -655       C  
ATOM    781  O   TYR A 145      34.817 -24.792 187.522  1.00109.97           O  
ANISOU  781  O   TYR A 145    13366  16417  12001    311   -329   -598       O  
ATOM    782  CB  TYR A 145      35.097 -25.327 184.118  1.00111.53           C  
ANISOU  782  CB  TYR A 145    13306  16938  12132    386   -476   -745       C  
ATOM    783  CG  TYR A 145      33.891 -24.412 184.066  1.00115.32           C  
ANISOU  783  CG  TYR A 145    13778  17439  12599    461   -537   -828       C  
ATOM    784  CD1 TYR A 145      33.995 -23.115 183.567  1.00117.85           C  
ANISOU  784  CD1 TYR A 145    14182  17812  12784    532   -655   -745       C  
ATOM    785  CD2 TYR A 145      32.630 -24.861 184.457  1.00116.84           C  
ANISOU  785  CD2 TYR A 145    13874  17596  12923    468   -463  -1005       C  
ATOM    786  CE1 TYR A 145      32.882 -22.272 183.504  1.00119.69           C  
ANISOU  786  CE1 TYR A 145    14411  18067  12998    617   -716   -822       C  
ATOM    787  CE2 TYR A 145      31.512 -24.027 184.402  1.00118.27           C  
ANISOU  787  CE2 TYR A 145    14034  17801  13102    543   -526  -1100       C  
ATOM    788  CZ  TYR A 145      31.645 -22.730 183.930  1.00126.23           C  
ANISOU  788  CZ  TYR A 145    15133  18870  13960    623   -662  -1003       C  
ATOM    789  OH  TYR A 145      30.548 -21.904 183.877  1.00128.49           O  
ANISOU  789  OH  TYR A 145    15403  19179  14238    712   -729  -1094       O  
ATOM    790  N   LEU A 146      34.731 -26.918 186.767  1.00108.67           N  
ANISOU  790  N   LEU A 146    13019  16286  11985    279   -173   -765       N  
ATOM    791  CA  LEU A 146      33.973 -27.461 187.888  1.00108.83           C  
ANISOU  791  CA  LEU A 146    13074  16161  12115    262    -10   -829       C  
ATOM    792  C   LEU A 146      34.739 -27.358 189.202  1.00113.34           C  
ANISOU  792  C   LEU A 146    13830  16609  12625    255     26   -667       C  
ATOM    793  O   LEU A 146      34.114 -27.419 190.254  1.00113.78           O  
ANISOU  793  O   LEU A 146    13969  16533  12729    259    138   -684       O  
ATOM    794  CB  LEU A 146      33.592 -28.931 187.633  1.00109.27           C  
ANISOU  794  CB  LEU A 146    13009  16190  12320    235    163   -980       C  
ATOM    795  CG  LEU A 146      32.567 -29.209 186.539  1.00114.31           C  
ANISOU  795  CG  LEU A 146    13439  16933  13060    250    159  -1207       C  
ATOM    796  CD1 LEU A 146      32.679 -30.628 186.062  1.00114.83           C  
ANISOU  796  CD1 LEU A 146    13382  17005  13245    212    301  -1322       C  
ATOM    797  CD2 LEU A 146      31.148 -28.937 187.018  1.00117.25           C  
ANISOU  797  CD2 LEU A 146    13765  17236  13548    263    229  -1372       C  
ATOM    798  N   ALA A 147      36.073 -27.202 189.151  1.00109.84           N  
ANISOU  798  N   ALA A 147    13450  16205  12077    252    -66   -524       N  
ATOM    799  CA  ALA A 147      36.904 -27.127 190.348  1.00109.92           C  
ANISOU  799  CA  ALA A 147    13622  16125  12019    268    -62   -392       C  
ATOM    800  C   ALA A 147      37.270 -25.717 190.813  1.00114.41           C  
ANISOU  800  C   ALA A 147    14287  16700  12484    280   -201   -291       C  
ATOM    801  O   ALA A 147      37.350 -25.507 192.027  1.00114.46           O  
ANISOU  801  O   ALA A 147    14428  16608  12454    307   -176   -232       O  
ATOM    802  CB  ALA A 147      38.163 -27.954 190.167  1.00110.60           C  
ANISOU  802  CB  ALA A 147    13707  16239  12079    266    -65   -331       C  
ATOM    803  N   ILE A 148      37.492 -24.755 189.896  1.00111.22           N  
ANISOU  803  N   ILE A 148    13828  16399  12029    267   -331   -271       N  
ATOM    804  CA  ILE A 148      37.901 -23.428 190.356  1.00111.38           C  
ANISOU  804  CA  ILE A 148    13940  16412  11968    270   -435   -181       C  
ATOM    805  C   ILE A 148      36.701 -22.437 190.405  1.00117.39           C  
ANISOU  805  C   ILE A 148    14711  17159  12733    285   -451   -218       C  
ATOM    806  O   ILE A 148      36.414 -21.935 191.494  1.00117.23           O  
ANISOU  806  O   ILE A 148    14790  17052  12698    291   -439   -184       O  
ATOM    807  CB  ILE A 148      39.170 -22.856 189.636  1.00114.22           C  
ANISOU  807  CB  ILE A 148    14282  16851  12265    249   -540   -110       C  
ATOM    808  CG1 ILE A 148      38.889 -22.213 188.274  1.00114.59           C  
ANISOU  808  CG1 ILE A 148    14261  16989  12288    253   -591   -132       C  
ATOM    809  CG2 ILE A 148      40.278 -23.901 189.506  1.00115.14           C  
ANISOU  809  CG2 ILE A 148    14367  16986  12395    235   -525    -95       C  
ATOM    810  CD1 ILE A 148      39.030 -20.753 188.315  1.00120.61           C  
ANISOU  810  CD1 ILE A 148    15093  17745  12989    257   -655    -69       C  
ATOM    811  N   VAL A 149      36.002 -22.180 189.272  1.00115.55           N  
ANISOU  811  N   VAL A 149    14382  17011  12512    303   -483   -292       N  
ATOM    812  CA  VAL A 149      34.863 -21.246 189.202  1.00116.40           C  
ANISOU  812  CA  VAL A 149    14490  17119  12619    337   -514   -339       C  
ATOM    813  C   VAL A 149      33.642 -21.833 189.970  1.00122.78           C  
ANISOU  813  C   VAL A 149    15279  17834  13536    336   -400   -451       C  
ATOM    814  O   VAL A 149      32.915 -21.082 190.627  1.00123.01           O  
ANISOU  814  O   VAL A 149    15365  17799  13574    344   -396   -455       O  
ATOM    815  CB  VAL A 149      34.556 -20.756 187.752  1.00120.70           C  
ANISOU  815  CB  VAL A 149    14956  17787  13116    393   -597   -385       C  
ATOM    816  CG1 VAL A 149      34.403 -21.905 186.776  1.00120.76           C  
ANISOU  816  CG1 VAL A 149    14828  17878  13175    407   -570   -501       C  
ATOM    817  CG2 VAL A 149      33.355 -19.818 187.686  1.00121.07           C  
ANISOU  817  CG2 VAL A 149    15005  17839  13158    452   -637   -444       C  
ATOM    818  N   HIS A 150      33.478 -23.166 189.949  1.00120.52           N  
ANISOU  818  N   HIS A 150    14924  17526  13344    319   -287   -541       N  
ATOM    819  CA  HIS A 150      32.470 -23.883 190.735  1.00121.35           C  
ANISOU  819  CA  HIS A 150    15023  17511  13574    307   -126   -652       C  
ATOM    820  C   HIS A 150      33.244 -24.687 191.782  1.00126.43           C  
ANISOU  820  C   HIS A 150    15790  18041  14208    291    -17   -561       C  
ATOM    821  O   HIS A 150      34.385 -25.055 191.516  1.00126.35           O  
ANISOU  821  O   HIS A 150    15791  18082  14135    289    -62   -478       O  
ATOM    822  CB  HIS A 150      31.608 -24.772 189.837  1.00122.88           C  
ANISOU  822  CB  HIS A 150    15035  17758  13895    311    -56   -852       C  
ATOM    823  CG  HIS A 150      30.719 -23.975 188.936  1.00126.87           C  
ANISOU  823  CG  HIS A 150    15431  18373  14403    362   -171   -965       C  
ATOM    824  ND1 HIS A 150      31.225 -23.295 187.841  1.00128.55           N  
ANISOU  824  ND1 HIS A 150    15619  18732  14493    411   -336   -911       N  
ATOM    825  CD2 HIS A 150      29.392 -23.732 189.024  1.00129.46           C  
ANISOU  825  CD2 HIS A 150    15685  18673  14832    385   -140  -1128       C  
ATOM    826  CE1 HIS A 150      30.193 -22.673 187.295  1.00128.60           C  
ANISOU  826  CE1 HIS A 150    15548  18804  14512    479   -408  -1033       C  
ATOM    827  NE2 HIS A 150      29.069 -22.907 187.970  1.00129.51           N  
ANISOU  827  NE2 HIS A 150    15617  18824  14766    464   -305  -1175       N  
ATOM    828  N   ALA A 151      32.703 -24.875 192.990  1.00123.64           N  
ANISOU  828  N   ALA A 151    15546  17532  13899    294    118   -569       N  
ATOM    829  CA  ALA A 151      33.460 -25.593 194.023  1.00123.85           C  
ANISOU  829  CA  ALA A 151    15726  17447  13883    316    217   -473       C  
ATOM    830  C   ALA A 151      33.106 -27.085 194.052  1.00128.56           C  
ANISOU  830  C   ALA A 151    16290  17956  14600    312    436   -572       C  
ATOM    831  O   ALA A 151      32.443 -27.566 194.980  1.00129.28           O  
ANISOU  831  O   ALA A 151    16481  17880  14762    323    633   -613       O  
ATOM    832  CB  ALA A 151      33.261 -24.938 195.385  1.00124.81           C  
ANISOU  832  CB  ALA A 151    16030  17442  13951    343    246   -401       C  
ATOM    833  N   THR A 152      33.547 -27.815 193.011  1.00124.30           N  
ANISOU  833  N   THR A 152    15617  17520  14092    293    421   -613       N  
ATOM    834  CA  THR A 152      33.250 -29.242 192.865  1.00124.35           C  
ANISOU  834  CA  THR A 152    15566  17456  14227    279    634   -720       C  
ATOM    835  C   THR A 152      34.430 -30.061 192.314  1.00126.73           C  
ANISOU  835  C   THR A 152    15836  17832  14483    284    606   -655       C  
ATOM    836  O   THR A 152      34.843 -29.892 191.163  1.00125.54           O  
ANISOU  836  O   THR A 152    15546  17840  14314    258    465   -671       O  
ATOM    837  CB  THR A 152      31.961 -29.450 192.038  1.00131.16           C  
ANISOU  837  CB  THR A 152    16223  18349  15262    236    707   -946       C  
ATOM    838  OG1 THR A 152      31.683 -28.279 191.265  1.00127.31           O  
ANISOU  838  OG1 THR A 152    15636  18011  14726    239    491   -971       O  
ATOM    839  CG2 THR A 152      30.762 -29.772 192.911  1.00131.70           C  
ANISOU  839  CG2 THR A 152    16336  18228  15477    225    942  -1068       C  
ATOM    840  N   ARG A 153      34.959 -30.967 193.151  1.00123.01           N  
ANISOU  840  N   ARG A 153    15509  17238  13990    327    752   -582       N  
ATOM    841  CA  ARG A 153      36.034 -31.872 192.757  1.00122.29           C  
ANISOU  841  CA  ARG A 153    15401  17194  13868    340    755   -527       C  
ATOM    842  C   ARG A 153      35.400 -33.008 191.954  1.00125.10           C  
ANISOU  842  C   ARG A 153    15590  17544  14396    286    936   -690       C  
ATOM    843  O   ARG A 153      34.293 -33.453 192.273  1.00125.42           O  
ANISOU  843  O   ARG A 153    15618  17459  14577    269   1149   -821       O  
ATOM    844  CB  ARG A 153      36.800 -32.401 193.979  1.00123.29           C  
ANISOU  844  CB  ARG A 153    15757  17191  13895    437    841   -396       C  
ATOM    845  N   THR A 154      36.077 -33.435 190.887  1.00119.93           N  
ANISOU  845  N   THR A 154    14798  17025  13746    254    855   -701       N  
ATOM    846  CA  THR A 154      35.574 -34.465 189.991  1.00119.44           C  
ANISOU  846  CA  THR A 154    14553  16987  13843    200   1000   -868       C  
ATOM    847  C   THR A 154      36.493 -35.681 189.937  1.00123.23           C  
ANISOU  847  C   THR A 154    15056  17439  14328    210   1109   -812       C  
ATOM    848  O   THR A 154      37.719 -35.528 189.870  1.00122.42           O  
ANISOU  848  O   THR A 154    15007  17411  14098    237    956   -670       O  
ATOM    849  CB  THR A 154      35.332 -33.875 188.594  1.00124.02           C  
ANISOU  849  CB  THR A 154    14920  17764  14436    157    815   -970       C  
ATOM    850  OG1 THR A 154      35.509 -32.453 188.605  1.00120.29           O  
ANISOU  850  OG1 THR A 154    14502  17372  13831    179    586   -876       O  
ATOM    851  CG2 THR A 154      33.967 -34.219 188.058  1.00123.67           C  
ANISOU  851  CG2 THR A 154    14695  17721  14574    122    937  -1218       C  
ATOM    852  N   LEU A 155      35.887 -36.891 189.967  1.00120.16           N  
ANISOU  852  N   LEU A 155    14619  16935  14100    188   1387   -940       N  
ATOM    853  CA  LEU A 155      36.527 -38.218 189.865  1.00120.15           C  
ANISOU  853  CA  LEU A 155    14626  16883  14144    193   1555   -922       C  
ATOM    854  C   LEU A 155      37.620 -38.512 190.906  1.00124.12           C  
ANISOU  854  C   LEU A 155    15376  17287  14496    297   1572   -714       C  
ATOM    855  O   LEU A 155      38.464 -39.377 190.664  1.00123.09           O  
ANISOU  855  O   LEU A 155    15246  17169  14354    313   1615   -662       O  
ATOM    856  CB  LEU A 155      37.096 -38.465 188.447  1.00119.44           C  
ANISOU  856  CB  LEU A 155    14324  16986  14073    130   1419   -970       C  
ATOM    857  CG  LEU A 155      36.200 -38.158 187.259  1.00123.73           C  
ANISOU  857  CG  LEU A 155    14620  17669  14724     61   1347  -1174       C  
ATOM    858  CD1 LEU A 155      36.999 -37.484 186.157  1.00125.00           C  
ANISOU  858  CD1 LEU A 155    14689  18040  14765     48   1064  -1112       C  
ATOM    859  CD2 LEU A 155      35.510 -39.414 186.757  1.00124.56           C  
ANISOU  859  CD2 LEU A 155    14554  17730  15041      4   1598  -1387       C  
ATOM    860  N   THR A 156      37.600 -37.824 192.059  1.00121.92           N  
ANISOU  860  N   THR A 156    15307  16914  14101    378   1539   -606       N  
ATOM    861  CA  THR A 156      38.608 -38.033 193.104  1.00122.46           C  
ANISOU  861  CA  THR A 156    15620  16903  14007    509   1530   -427       C  
ATOM    862  C   THR A 156      38.369 -39.350 193.855  1.00128.89           C  
ANISOU  862  C   THR A 156    16597  17498  14876    585   1877   -427       C  
ATOM    863  O   THR A 156      39.321 -40.097 194.086  1.00129.15           O  
ANISOU  863  O   THR A 156    16737  17506  14828    676   1908   -326       O  
ATOM    864  CB  THR A 156      38.742 -36.817 194.037  1.00128.61           C  
ANISOU  864  CB  THR A 156    16562  17675  14627    582   1353   -320       C  
ATOM    865  OG1 THR A 156      37.640 -36.772 194.939  1.00128.56           O  
ANISOU  865  OG1 THR A 156    16690  17489  14669    607   1555   -362       O  
ATOM    866  CG2 THR A 156      38.888 -35.493 193.282  1.00125.16           C  
ANISOU  866  CG2 THR A 156    15975  17430  14149    505   1051   -325       C  
ATOM    867  N   GLN A 157      37.104 -39.642 194.208  1.00127.02           N  
ANISOU  867  N   GLN A 157    16382  17096  14785    553   2149   -547       N  
ATOM    868  CA  GLN A 157      36.735 -40.869 194.914  1.00128.80           C  
ANISOU  868  CA  GLN A 157    16773  17077  15089    617   2538   -564       C  
ATOM    869  C   GLN A 157      36.805 -42.099 194.000  1.00133.19           C  
ANISOU  869  C   GLN A 157    17157  17641  15807    544   2720   -669       C  
ATOM    870  O   GLN A 157      37.259 -43.158 194.438  1.00134.16           O  
ANISOU  870  O   GLN A 157    17436  17627  15910    633   2941   -599       O  
ATOM    871  CB  GLN A 157      35.347 -40.739 195.565  1.00131.32           C  
ANISOU  871  CB  GLN A 157    17157  17201  15538    589   2791   -681       C  
ATOM    872  CG  GLN A 157      35.310 -41.183 197.026  1.00153.70           C  
ANISOU  872  CG  GLN A 157    20352  19768  18278    746   3058   -565       C  
ATOM    873  CD  GLN A 157      35.213 -42.684 197.188  1.00179.13           C  
ANISOU  873  CD  GLN A 157    23665  22782  21613    783   3466   -601       C  
ATOM    874  OE1 GLN A 157      34.120 -43.262 197.197  1.00177.53           O  
ANISOU  874  OE1 GLN A 157    23412  22403  21639    704   3812   -774       O  
ATOM    875  NE2 GLN A 157      36.353 -43.348 197.333  1.00171.35           N  
ANISOU  875  NE2 GLN A 157    22815  21807  20482    908   3445   -450       N  
ATOM    876  N   LYS A 158      36.366 -41.955 192.737  1.00128.60           N  
ANISOU  876  N   LYS A 158    16264  17221  15376    396   2628   -839       N  
ATOM    877  CA  LYS A 158      36.380 -43.035 191.750  1.00128.53           C  
ANISOU  877  CA  LYS A 158    16053  17251  15533    312   2773   -968       C  
ATOM    878  C   LYS A 158      37.413 -42.705 190.669  1.00130.79           C  
ANISOU  878  C   LYS A 158    16174  17795  15727    272   2443   -911       C  
ATOM    879  O   LYS A 158      37.065 -42.330 189.542  1.00129.55           O  
ANISOU  879  O   LYS A 158    15764  17808  15651    168   2298  -1049       O  
ATOM    880  CB  LYS A 158      34.971 -43.272 191.165  1.00131.74           C  
ANISOU  880  CB  LYS A 158    16227  17622  16205    186   2969  -1252       C  
ATOM    881  CG  LYS A 158      33.983 -43.929 192.129  1.00145.22           C  
ANISOU  881  CG  LYS A 158    18077  19035  18065    205   3390  -1345       C  
ATOM    882  CD  LYS A 158      32.562 -43.930 191.564  1.00153.82           C  
ANISOU  882  CD  LYS A 158    18906  20112  19427     78   3533  -1659       C  
ATOM    883  CE  LYS A 158      32.106 -45.299 191.120  1.00162.09           C  
ANISOU  883  CE  LYS A 158    19805  21045  20737      2   3902  -1871       C  
ATOM    884  NZ  LYS A 158      30.849 -45.241 190.325  1.00167.91           N  
ANISOU  884  NZ  LYS A 158    20218  21840  21742   -121   3960  -2218       N  
ATOM    885  N   ARG A 159      38.700 -42.833 191.034  1.00127.05           N  
ANISOU  885  N   ARG A 159    15852  17343  15077    369   2325   -713       N  
ATOM    886  CA  ARG A 159      39.832 -42.533 190.150  1.00125.52           C  
ANISOU  886  CA  ARG A 159    15536  17363  14792    340   2032   -643       C  
ATOM    887  C   ARG A 159      40.034 -43.546 189.003  1.00128.04           C  
ANISOU  887  C   ARG A 159    15647  17754  15250    249   2125   -746       C  
ATOM    888  O   ARG A 159      40.799 -43.262 188.073  1.00126.38           O  
ANISOU  888  O   ARG A 159    15299  17726  14994    199   1897   -724       O  
ATOM    889  CB  ARG A 159      41.131 -42.348 190.961  1.00125.67           C  
ANISOU  889  CB  ARG A 159    15771  17378  14601    479   1880   -433       C  
ATOM    890  CG  ARG A 159      41.415 -40.894 191.369  1.00131.52           C  
ANISOU  890  CG  ARG A 159    16582  18206  15185    516   1584   -345       C  
ATOM    891  CD  ARG A 159      41.717 -39.976 190.187  1.00132.29           C  
ANISOU  891  CD  ARG A 159    16465  18522  15278    406   1301   -381       C  
ATOM    892  NE  ARG A 159      43.000 -40.280 189.553  1.00131.41           N  
ANISOU  892  NE  ARG A 159    16283  18523  15122    400   1165   -320       N  
ATOM    893  CZ  ARG A 159      44.115 -39.591 189.767  1.00139.38           C  
ANISOU  893  CZ  ARG A 159    17349  19611  15998    451    929   -215       C  
ATOM    894  NH1 ARG A 159      44.112 -38.549 190.589  1.00125.12           N  
ANISOU  894  NH1 ARG A 159    15667  17793  14081    513    795   -155       N  
ATOM    895  NH2 ARG A 159      45.240 -39.935 189.156  1.00122.77           N  
ANISOU  895  NH2 ARG A 159    15167  17598  13883    436    831   -184       N  
ATOM    896  N   TYR A 160      39.342 -44.706 189.060  1.00124.75           N  
ANISOU  896  N   TYR A 160    15205  17186  15008    223   2474   -867       N  
ATOM    897  CA  TYR A 160      39.418 -45.750 188.034  1.00124.22           C  
ANISOU  897  CA  TYR A 160    14933  17168  15095    133   2605   -989       C  
ATOM    898  C   TYR A 160      38.749 -45.303 186.728  1.00124.68           C  
ANISOU  898  C   TYR A 160    14690  17415  15269      3   2467  -1191       C  
ATOM    899  O   TYR A 160      39.149 -45.751 185.654  1.00123.72           O  
ANISOU  899  O   TYR A 160    14384  17423  15199    -67   2415  -1254       O  
ATOM    900  CB  TYR A 160      38.821 -47.081 188.552  1.00127.49           C  
ANISOU  900  CB  TYR A 160    15417  17344  15679    144   3051  -1075       C  
ATOM    901  CG  TYR A 160      37.307 -47.138 188.570  1.00130.95           C  
ANISOU  901  CG  TYR A 160    15745  17679  16332     67   3285  -1312       C  
ATOM    902  CD1 TYR A 160      36.580 -46.605 189.632  1.00133.56           C  
ANISOU  902  CD1 TYR A 160    16254  17852  16639    125   3379  -1296       C  
ATOM    903  CD2 TYR A 160      36.600 -47.745 187.536  1.00132.47           C  
ANISOU  903  CD2 TYR A 160    15646  17928  16759    -62   3417  -1572       C  
ATOM    904  CE1 TYR A 160      35.185 -46.647 189.648  1.00135.26           C  
ANISOU  904  CE1 TYR A 160    16355  17966  17073     48   3599  -1535       C  
ATOM    905  CE2 TYR A 160      35.206 -47.787 187.537  1.00134.56           C  
ANISOU  905  CE2 TYR A 160    15780  18105  17241   -131   3624  -1828       C  
ATOM    906  CZ  TYR A 160      34.502 -47.244 188.600  1.00142.18           C  
ANISOU  906  CZ  TYR A 160    16923  18906  18194    -79   3720  -1810       C  
ATOM    907  OH  TYR A 160      33.128 -47.292 188.601  1.00144.24           O  
ANISOU  907  OH  TYR A 160    17043  19072  18691   -153   3932  -2082       O  
ATOM    908  N   LEU A 161      37.731 -44.420 186.835  1.00119.22           N  
ANISOU  908  N   LEU A 161    13956  16735  14606    -16   2406  -1294       N  
ATOM    909  CA  LEU A 161      36.949 -43.889 185.715  1.00117.83           C  
ANISOU  909  CA  LEU A 161    13518  16732  14519   -100   2266  -1499       C  
ATOM    910  C   LEU A 161      37.726 -42.960 184.789  1.00118.24           C  
ANISOU  910  C   LEU A 161    13496  17019  14411   -106   1897  -1411       C  
ATOM    911  O   LEU A 161      37.353 -42.828 183.623  1.00117.56           O  
ANISOU  911  O   LEU A 161    13191  17093  14383   -160   1794  -1569       O  
ATOM    912  CB  LEU A 161      35.670 -43.198 186.218  1.00118.39           C  
ANISOU  912  CB  LEU A 161    13588  16733  14661    -97   2311  -1628       C  
ATOM    913  CG  LEU A 161      34.581 -44.105 186.799  1.00124.65           C  
ANISOU  913  CG  LEU A 161    14371  17305  15685   -125   2708  -1815       C  
ATOM    914  CD1 LEU A 161      33.617 -43.311 187.640  1.00127.62           C  
ANISOU  914  CD1 LEU A 161    14837  17572  16079   -100   2740  -1858       C  
ATOM    915  CD2 LEU A 161      33.811 -44.832 185.702  1.00125.62           C  
ANISOU  915  CD2 LEU A 161    14181  17500  16048   -221   2836  -2124       C  
ATOM    916  N   VAL A 162      38.794 -42.316 185.303  1.00112.70           N  
ANISOU  916  N   VAL A 162    12978  16333  13512    -44   1708  -1174       N  
ATOM    917  CA  VAL A 162      39.646 -41.391 184.545  1.00110.69           C  
ANISOU  917  CA  VAL A 162    12685  16264  13108    -50   1390  -1074       C  
ATOM    918  C   VAL A 162      40.279 -42.122 183.365  1.00114.06           C  
ANISOU  918  C   VAL A 162    12951  16808  13579   -110   1374  -1118       C  
ATOM    919  O   VAL A 162      40.267 -41.589 182.258  1.00113.35           O  
ANISOU  919  O   VAL A 162    12725  16884  13458   -145   1196  -1177       O  
ATOM    920  CB  VAL A 162      40.711 -40.674 185.419  1.00113.57           C  
ANISOU  920  CB  VAL A 162    13264  16601  13287     25   1228   -843       C  
ATOM    921  CG1 VAL A 162      41.375 -39.536 184.650  1.00112.22           C  
ANISOU  921  CG1 VAL A 162    13046  16599  12992      7    932   -776       C  
ATOM    922  CG2 VAL A 162      40.111 -40.152 186.722  1.00113.75           C  
ANISOU  922  CG2 VAL A 162    13467  16484  13268     93   1284   -797       C  
ATOM    923  N   LYS A 163      40.781 -43.360 183.598  1.00111.01           N  
ANISOU  923  N   LYS A 163    12591  16327  13262   -114   1575  -1092       N  
ATOM    924  CA  LYS A 163      41.415 -44.234 182.595  1.00110.60           C  
ANISOU  924  CA  LYS A 163    12396  16358  13269   -175   1603  -1129       C  
ATOM    925  C   LYS A 163      40.499 -44.484 181.397  1.00113.97           C  
ANISOU  925  C   LYS A 163    12571  16900  13834   -252   1637  -1371       C  
ATOM    926  O   LYS A 163      40.960 -44.439 180.257  1.00112.39           O  
ANISOU  926  O   LYS A 163    12241  16854  13607   -294   1500  -1398       O  
ATOM    927  CB  LYS A 163      41.868 -45.568 183.220  1.00114.15           C  
ANISOU  927  CB  LYS A 163    12934  16651  13789   -152   1865  -1077       C  
ATOM    928  CG  LYS A 163      42.992 -45.416 184.251  1.00134.24           C  
ANISOU  928  CG  LYS A 163    15715  19117  16174    -48   1791   -845       C  
ATOM    929  CD  LYS A 163      42.512 -45.651 185.698  1.00144.48           C  
ANISOU  929  CD  LYS A 163    17233  20201  17460     54   2000   -792       C  
ATOM    930  CE  LYS A 163      43.377 -44.980 186.746  1.00150.96           C  
ANISOU  930  CE  LYS A 163    18287  20987  18083    181   1833   -592       C  
ATOM    931  NZ  LYS A 163      44.775 -45.490 186.750  1.00159.00           N  
ANISOU  931  NZ  LYS A 163    19358  22034  19020    236   1754   -466       N  
ATOM    932  N   PHE A 164      39.195 -44.690 181.661  1.00111.67           N  
ANISOU  932  N   PHE A 164    12210  16533  13687   -262   1813  -1559       N  
ATOM    933  CA  PHE A 164      38.183 -44.913 180.634  1.00112.17           C  
ANISOU  933  CA  PHE A 164    12018  16704  13899   -316   1847  -1837       C  
ATOM    934  C   PHE A 164      37.898 -43.654 179.821  1.00113.01           C  
ANISOU  934  C   PHE A 164    12049  17003  13886   -288   1542  -1879       C  
ATOM    935  O   PHE A 164      37.610 -43.770 178.630  1.00113.36           O  
ANISOU  935  O   PHE A 164    11895  17205  13973   -308   1469  -2052       O  
ATOM    936  CB  PHE A 164      36.896 -45.478 181.245  1.00116.06           C  
ANISOU  936  CB  PHE A 164    12458  17040  14600   -333   2139  -2044       C  
ATOM    937  CG  PHE A 164      37.086 -46.784 181.983  1.00119.50           C  
ANISOU  937  CG  PHE A 164    12976  17264  15165   -352   2491  -2022       C  
ATOM    938  CD1 PHE A 164      37.195 -47.986 181.289  1.00123.97           C  
ANISOU  938  CD1 PHE A 164    13377  17840  15888   -421   2678  -2156       C  
ATOM    939  CD2 PHE A 164      37.136 -46.815 183.373  1.00122.68           C  
ANISOU  939  CD2 PHE A 164    13633  17452  15529   -289   2651  -1870       C  
ATOM    940  CE1 PHE A 164      37.365 -49.195 181.975  1.00126.02           C  
ANISOU  940  CE1 PHE A 164    13729  17888  16265   -429   3029  -2129       C  
ATOM    941  CE2 PHE A 164      37.305 -48.025 184.057  1.00126.70           C  
ANISOU  941  CE2 PHE A 164    14252  17751  16138   -280   2996  -1840       C  
ATOM    942  CZ  PHE A 164      37.418 -49.206 183.354  1.00125.52           C  
ANISOU  942  CZ  PHE A 164    13940  17605  16148   -351   3190  -1966       C  
ATOM    943  N   ILE A 165      37.998 -42.458 180.447  1.00106.45           N  
ANISOU  943  N   ILE A 165    11385  16161  12900   -229   1368  -1723       N  
ATOM    944  CA  ILE A 165      37.785 -41.170 179.774  1.00104.96           C  
ANISOU  944  CA  ILE A 165    11169  16132  12579   -186   1091  -1729       C  
ATOM    945  C   ILE A 165      38.809 -40.977 178.642  1.00109.75           C  
ANISOU  945  C   ILE A 165    11743  16895  13063   -193    906  -1642       C  
ATOM    946  O   ILE A 165      38.411 -40.771 177.495  1.00109.05           O  
ANISOU  946  O   ILE A 165    11512  16963  12960   -176    795  -1784       O  
ATOM    947  CB  ILE A 165      37.757 -39.979 180.774  1.00106.51           C  
ANISOU  947  CB  ILE A 165    11562  16259  12649   -130    979  -1572       C  
ATOM    948  CG1 ILE A 165      36.533 -40.069 181.702  1.00107.42           C  
ANISOU  948  CG1 ILE A 165    11685  16235  12895   -121   1156  -1701       C  
ATOM    949  CG2 ILE A 165      37.797 -38.627 180.046  1.00105.66           C  
ANISOU  949  CG2 ILE A 165    11458  16305  12381    -80    701  -1534       C  
ATOM    950  CD1 ILE A 165      36.718 -39.438 183.068  1.00111.14           C  
ANISOU  950  CD1 ILE A 165    12390  16562  13277    -81   1160  -1517       C  
ATOM    951  N   CYS A 166      40.116 -41.081 178.963  1.00107.27           N  
ANISOU  951  N   CYS A 166    11560  16533  12664   -211    882  -1426       N  
ATOM    952  CA  CYS A 166      41.194 -40.925 177.982  1.00107.10           C  
ANISOU  952  CA  CYS A 166    11522  16628  12544   -230    738  -1336       C  
ATOM    953  C   CYS A 166      41.255 -42.080 176.977  1.00111.36           C  
ANISOU  953  C   CYS A 166    11880  17237  13193   -287    841  -1476       C  
ATOM    954  O   CYS A 166      41.650 -41.859 175.830  1.00110.51           O  
ANISOU  954  O   CYS A 166    11708  17264  13016   -292    715  -1488       O  
ATOM    955  CB  CYS A 166      42.542 -40.670 178.650  1.00106.87           C  
ANISOU  955  CB  CYS A 166    11664  16526  12416   -231    679  -1099       C  
ATOM    956  SG  CYS A 166      42.864 -41.695 180.104  1.00111.09           S  
ANISOU  956  SG  CYS A 166    12315  16865  13030   -223    897  -1016       S  
ATOM    957  N   LEU A 167      40.807 -43.289 177.386  1.00108.68           N  
ANISOU  957  N   LEU A 167    11463  16801  13029   -327   1086  -1591       N  
ATOM    958  CA  LEU A 167      40.711 -44.465 176.513  1.00109.02           C  
ANISOU  958  CA  LEU A 167    11315  16898  13211   -388   1222  -1757       C  
ATOM    959  C   LEU A 167      39.680 -44.141 175.427  1.00113.17           C  
ANISOU  959  C   LEU A 167    11651  17588  13759   -362   1126  -2001       C  
ATOM    960  O   LEU A 167      39.912 -44.415 174.251  1.00112.22           O  
ANISOU  960  O   LEU A 167    11403  17604  13630   -378   1065  -2087       O  
ATOM    961  CB  LEU A 167      40.256 -45.686 177.328  1.00109.89           C  
ANISOU  961  CB  LEU A 167    11399  16839  13514   -426   1538  -1843       C  
ATOM    962  CG  LEU A 167      40.415 -47.049 176.674  1.00115.18           C  
ANISOU  962  CG  LEU A 167    11904  17518  14340   -501   1729  -1971       C  
ATOM    963  CD1 LEU A 167      41.811 -47.619 176.909  1.00116.58           C  
ANISOU  963  CD1 LEU A 167    12198  17630  14467   -523   1767  -1753       C  
ATOM    964  CD2 LEU A 167      39.361 -48.004 177.182  1.00116.83           C  
ANISOU  964  CD2 LEU A 167    12017  17593  14779   -533   2044  -2180       C  
ATOM    965  N   SER A 168      38.570 -43.497 175.838  1.00110.97           N  
ANISOU  965  N   SER A 168    11367  17300  13497   -309   1098  -2109       N  
ATOM    966  CA  SER A 168      37.498 -43.021 174.975  1.00112.11           C  
ANISOU  966  CA  SER A 168    11352  17599  13647   -248    977  -2348       C  
ATOM    967  C   SER A 168      38.036 -41.903 174.073  1.00115.70           C  
ANISOU  967  C   SER A 168    11881  18209  13869   -173    692  -2230       C  
ATOM    968  O   SER A 168      37.692 -41.869 172.891  1.00115.43           O  
ANISOU  968  O   SER A 168    11713  18343  13802   -120    585  -2395       O  
ATOM    969  CB  SER A 168      36.325 -42.526 175.819  1.00117.05           C  
ANISOU  969  CB  SER A 168    11985  18145  14341   -208   1019  -2455       C  
ATOM    970  OG  SER A 168      35.329 -41.865 175.054  1.00129.42           O  
ANISOU  970  OG  SER A 168    13420  19870  15885   -121    858  -2670       O  
ATOM    971  N   ILE A 169      38.904 -41.015 174.626  1.00112.23           N  
ANISOU  971  N   ILE A 169    11662  17709  13272   -161    584  -1954       N  
ATOM    972  CA  ILE A 169      39.537 -39.907 173.898  1.00112.14           C  
ANISOU  972  CA  ILE A 169    11759  17801  13048    -99    358  -1815       C  
ATOM    973  C   ILE A 169      40.362 -40.447 172.727  1.00117.28           C  
ANISOU  973  C   ILE A 169    12346  18550  13666   -129    336  -1812       C  
ATOM    974  O   ILE A 169      40.186 -39.975 171.605  1.00117.65           O  
ANISOU  974  O   ILE A 169    12360  18742  13602    -51    199  -1885       O  
ATOM    975  CB  ILE A 169      40.348 -38.956 174.837  1.00114.31           C  
ANISOU  975  CB  ILE A 169    12262  17967  13203    -99    286  -1546       C  
ATOM    976  CG1 ILE A 169      39.436 -38.127 175.781  1.00114.84           C  
ANISOU  976  CG1 ILE A 169    12402  17970  13262    -46    260  -1555       C  
ATOM    977  CG2 ILE A 169      41.326 -38.054 174.072  1.00115.12           C  
ANISOU  977  CG2 ILE A 169    12476  18138  13125    -70    120  -1390       C  
ATOM    978  CD1 ILE A 169      38.322 -37.233 175.120  1.00124.82           C  
ANISOU  978  CD1 ILE A 169    13611  19358  14459     65    119  -1708       C  
ATOM    979  N   TRP A 170      41.217 -41.459 172.986  1.00113.86           N  
ANISOU  979  N   TRP A 170    11899  18035  13326   -230    479  -1738       N  
ATOM    980  CA  TRP A 170      42.053 -42.110 171.976  1.00113.76           C  
ANISOU  980  CA  TRP A 170    11819  18094  13311   -280    489  -1733       C  
ATOM    981  C   TRP A 170      41.214 -42.816 170.905  1.00118.87           C  
ANISOU  981  C   TRP A 170    12246  18879  14040   -262    521  -2008       C  
ATOM    982  O   TRP A 170      41.585 -42.786 169.730  1.00118.95           O  
ANISOU  982  O   TRP A 170    12221  19011  13963   -239    433  -2034       O  
ATOM    983  CB  TRP A 170      43.015 -43.100 172.635  1.00112.05           C  
ANISOU  983  CB  TRP A 170    11627  17748  13198   -382    650  -1614       C  
ATOM    984  CG  TRP A 170      44.212 -42.458 173.275  1.00112.25           C  
ANISOU  984  CG  TRP A 170    11844  17685  13120   -393    575  -1359       C  
ATOM    985  CD1 TRP A 170      44.392 -42.198 174.601  1.00114.69           C  
ANISOU  985  CD1 TRP A 170    12287  17861  13427   -383    603  -1231       C  
ATOM    986  CD2 TRP A 170      45.419 -42.051 172.618  1.00111.70           C  
ANISOU  986  CD2 TRP A 170    11843  17650  12950   -417    472  -1223       C  
ATOM    987  NE1 TRP A 170      45.629 -41.635 174.811  1.00113.35           N  
ANISOU  987  NE1 TRP A 170    12249  17656  13165   -393    505  -1041       N  
ATOM    988  CE2 TRP A 170      46.284 -41.538 173.612  1.00114.86           C  
ANISOU  988  CE2 TRP A 170    12397  17939  13305   -423    434  -1035       C  
ATOM    989  CE3 TRP A 170      45.861 -42.076 171.282  1.00113.25           C  
ANISOU  989  CE3 TRP A 170    11986  17953  13092   -430    416  -1254       C  
ATOM    990  CZ2 TRP A 170      47.561 -41.045 173.313  1.00113.93           C  
ANISOU  990  CZ2 TRP A 170    12361  17811  13115   -452    350   -896       C  
ATOM    991  CZ3 TRP A 170      47.131 -41.598 170.989  1.00114.39           C  
ANISOU  991  CZ3 TRP A 170    12233  18072  13157   -463    349  -1095       C  
ATOM    992  CH2 TRP A 170      47.964 -41.086 171.995  1.00114.45           C  
ANISOU  992  CH2 TRP A 170    12375  17966  13146   -479    319   -928       C  
ATOM    993  N   GLY A 171      40.096 -43.420 171.323  1.00116.05           N  
ANISOU  993  N   GLY A 171    11746  18497  13852   -268    654  -2221       N  
ATOM    994  CA  GLY A 171      39.158 -44.131 170.455  1.00116.99           C  
ANISOU  994  CA  GLY A 171    11620  18740  14089   -251    700  -2536       C  
ATOM    995  C   GLY A 171      38.422 -43.218 169.496  1.00121.41           C  
ANISOU  995  C   GLY A 171    12139  19484  14506   -106    477  -2678       C  
ATOM    996  O   GLY A 171      38.380 -43.489 168.293  1.00121.23           O  
ANISOU  996  O   GLY A 171    12001  19618  14444    -61    406  -2822       O  
ATOM    997  N   LEU A 172      37.853 -42.115 170.029  1.00118.61           N  
ANISOU  997  N   LEU A 172    11893  19112  14061    -19    361  -2635       N  
ATOM    998  CA  LEU A 172      37.144 -41.077 169.271  1.00119.77           C  
ANISOU  998  CA  LEU A 172    12046  19417  14044    149    138  -2738       C  
ATOM    999  C   LEU A 172      38.122 -40.380 168.310  1.00124.59           C  
ANISOU  999  C   LEU A 172    12816  20110  14411    214    -23  -2548       C  
ATOM   1000  O   LEU A 172      37.728 -39.994 167.207  1.00125.16           O  
ANISOU 1000  O   LEU A 172    12854  20349  14351    356   -173  -2676       O  
ATOM   1001  CB  LEU A 172      36.534 -40.049 170.238  1.00119.64           C  
ANISOU 1001  CB  LEU A 172    12147  19322  13988    205     78  -2672       C  
ATOM   1002  CG  LEU A 172      35.688 -38.933 169.621  1.00125.40           C  
ANISOU 1002  CG  LEU A 172    12893  20196  14556    393   -142  -2780       C  
ATOM   1003  CD1 LEU A 172      34.217 -39.308 169.606  1.00127.32           C  
ANISOU 1003  CD1 LEU A 172    12895  20513  14967    451   -121  -3146       C  
ATOM   1004  CD2 LEU A 172      35.890 -37.624 170.363  1.00126.55           C  
ANISOU 1004  CD2 LEU A 172    13274  20252  14558    434   -235  -2539       C  
ATOM   1005  N   SER A 173      39.396 -40.236 168.745  1.00120.61           N  
ANISOU 1005  N   SER A 173    12489  19482  13855    118     18  -2256       N  
ATOM   1006  CA  SER A 173      40.508 -39.646 167.994  1.00120.14           C  
ANISOU 1006  CA  SER A 173    12592  19449  13606    142    -78  -2058       C  
ATOM   1007  C   SER A 173      40.866 -40.520 166.789  1.00124.24           C  
ANISOU 1007  C   SER A 173    12992  20077  14136    125    -52  -2166       C  
ATOM   1008  O   SER A 173      41.239 -39.988 165.743  1.00123.60           O  
ANISOU 1008  O   SER A 173    13004  20084  13874    216   -161  -2121       O  
ATOM   1009  CB  SER A 173      41.725 -39.490 168.900  1.00122.71           C  
ANISOU 1009  CB  SER A 173    13079  19605  13939     23    -12  -1779       C  
ATOM   1010  OG  SER A 173      42.735 -38.704 168.292  1.00133.30           O  
ANISOU 1010  OG  SER A 173    14588  20948  15111     46    -95  -1597       O  
ATOM   1011  N   LEU A 174      40.751 -41.857 166.945  1.00121.56           N  
ANISOU 1011  N   LEU A 174    12457  19722  14007     14    110  -2310       N  
ATOM   1012  CA  LEU A 174      41.024 -42.837 165.895  1.00122.25           C  
ANISOU 1012  CA  LEU A 174    12400  19908  14141    -21    159  -2439       C  
ATOM   1013  C   LEU A 174      39.897 -42.842 164.860  1.00128.16           C  
ANISOU 1013  C   LEU A 174    12990  20858  14846    130     47  -2742       C  
ATOM   1014  O   LEU A 174      40.177 -42.919 163.662  1.00128.05           O  
ANISOU 1014  O   LEU A 174    12964  20971  14718    195    -27  -2794       O  
ATOM   1015  CB  LEU A 174      41.229 -44.238 166.495  1.00122.02           C  
ANISOU 1015  CB  LEU A 174    12221  19779  14362   -186    390  -2493       C  
ATOM   1016  CG  LEU A 174      41.951 -45.248 165.598  1.00127.08           C  
ANISOU 1016  CG  LEU A 174    12761  20469  15055   -268    471  -2529       C  
ATOM   1017  CD1 LEU A 174      43.468 -45.130 165.732  1.00125.92           C  
ANISOU 1017  CD1 LEU A 174    12790  20212  14843   -359    489  -2231       C  
ATOM   1018  CD2 LEU A 174      41.507 -46.662 165.908  1.00130.27           C  
ANISOU 1018  CD2 LEU A 174    12940  20834  15722   -376    694  -2727       C  
ATOM   1019  N   LEU A 175      38.631 -42.740 165.322  1.00126.39           N  
ANISOU 1019  N   LEU A 175    12647  20664  14712    195     33  -2952       N  
ATOM   1020  CA  LEU A 175      37.447 -42.677 164.460  1.00128.37           C  
ANISOU 1020  CA  LEU A 175    12726  21112  14935    360    -93  -3281       C  
ATOM   1021  C   LEU A 175      37.405 -41.368 163.662  1.00132.95           C  
ANISOU 1021  C   LEU A 175    13493  21812  15210    575   -338  -3204       C  
ATOM   1022  O   LEU A 175      37.036 -41.389 162.488  1.00134.19           O  
ANISOU 1022  O   LEU A 175    13576  22155  15254    730   -465  -3397       O  
ATOM   1023  CB  LEU A 175      36.161 -42.880 165.270  1.00129.25           C  
ANISOU 1023  CB  LEU A 175    12662  21197  15251    358    -24  -3527       C  
ATOM   1024  CG  LEU A 175      35.574 -44.297 165.236  1.00135.09           C  
ANISOU 1024  CG  LEU A 175    13095  21949  16283    254    173  -3844       C  
ATOM   1025  CD1 LEU A 175      36.313 -45.249 166.185  1.00136.35           C  
ANISOU 1025  CD1 LEU A 175    13274  21896  16637     35    446  -3681       C  
ATOM   1026  CD2 LEU A 175      34.093 -44.275 165.544  1.00136.78           C  
ANISOU 1026  CD2 LEU A 175    13106  22209  16653    325    174  -4186       C  
ATOM   1027  N   LEU A 176      37.840 -40.248 164.284  1.00128.35           N  
ANISOU 1027  N   LEU A 176    13163  21116  14488    591   -393  -2921       N  
ATOM   1028  CA  LEU A 176      37.956 -38.917 163.670  1.00128.60           C  
ANISOU 1028  CA  LEU A 176    13426  21208  14228    782   -580  -2788       C  
ATOM   1029  C   LEU A 176      39.004 -38.950 162.543  1.00132.92           C  
ANISOU 1029  C   LEU A 176    14097  21798  14608    805   -599  -2661       C  
ATOM   1030  O   LEU A 176      38.833 -38.293 161.514  1.00133.23           O  
ANISOU 1030  O   LEU A 176    14245  21961  14414   1011   -744  -2693       O  
ATOM   1031  CB  LEU A 176      38.390 -37.892 164.743  1.00127.23           C  
ANISOU 1031  CB  LEU A 176    13478  20862  14001    733   -572  -2499       C  
ATOM   1032  CG  LEU A 176      37.421 -36.781 165.200  1.00132.38           C  
ANISOU 1032  CG  LEU A 176    14204  21528  14568    879   -696  -2528       C  
ATOM   1033  CD1 LEU A 176      35.976 -37.038 164.781  1.00137.47           C  
ANISOU 1033  CD1 LEU A 176    14634  22347  15251   1037   -798  -2888       C  
ATOM   1034  CD2 LEU A 176      37.481 -36.602 166.697  1.00130.93           C  
ANISOU 1034  CD2 LEU A 176    14055  21163  14528    735   -594  -2396       C  
ATOM   1035  N   ALA A 177      40.085 -39.729 162.752  1.00129.31           N  
ANISOU 1035  N   ALA A 177    13630  21230  14271    603   -444  -2521       N  
ATOM   1036  CA  ALA A 177      41.194 -39.899 161.815  1.00129.36           C  
ANISOU 1036  CA  ALA A 177    13739  21242  14172    575   -419  -2394       C  
ATOM   1037  C   ALA A 177      41.040 -41.150 160.937  1.00134.67           C  
ANISOU 1037  C   ALA A 177    14185  22043  14940    550   -372  -2629       C  
ATOM   1038  O   ALA A 177      41.956 -41.472 160.175  1.00134.40           O  
ANISOU 1038  O   ALA A 177    14207  22008  14852    503   -329  -2542       O  
ATOM   1039  CB  ALA A 177      42.516 -39.934 162.571  1.00128.30           C  
ANISOU 1039  CB  ALA A 177    13727  20908  14114    377   -289  -2108       C  
ATOM   1040  N   LEU A 178      39.881 -41.844 161.016  1.00132.05           N  
ANISOU 1040  N   LEU A 178    13592  21820  14762    579   -372  -2942       N  
ATOM   1041  CA  LEU A 178      39.630 -43.022 160.178  1.00132.72           C  
ANISOU 1041  CA  LEU A 178    13434  22039  14955    562   -326  -3210       C  
ATOM   1042  C   LEU A 178      39.515 -42.674 158.666  1.00137.92           C  
ANISOU 1042  C   LEU A 178    14150  22895  15359    784   -498  -3319       C  
ATOM   1043  O   LEU A 178      40.058 -43.439 157.870  1.00137.34           O  
ANISOU 1043  O   LEU A 178    14013  22872  15298    732   -441  -3361       O  
ATOM   1044  CB  LEU A 178      38.431 -43.853 160.663  1.00133.44           C  
ANISOU 1044  CB  LEU A 178    13218  22178  15304    525   -254  -3543       C  
ATOM   1045  CG  LEU A 178      38.364 -45.282 160.115  1.00138.66           C  
ANISOU 1045  CG  LEU A 178    13603  22916  16166    426   -123  -3797       C  
ATOM   1046  CD1 LEU A 178      39.221 -46.241 160.939  1.00136.97           C  
ANISOU 1046  CD1 LEU A 178    13357  22507  16177    164    131  -3638       C  
ATOM   1047  CD2 LEU A 178      36.936 -45.764 160.036  1.00143.38           C  
ANISOU 1047  CD2 LEU A 178    13900  23646  16931    502   -136  -4223       C  
ATOM   1048  N   PRO A 179      38.893 -41.537 158.231  1.00135.76           N  
ANISOU 1048  N   PRO A 179    14019  22724  14840   1040   -698  -3348       N  
ATOM   1049  CA  PRO A 179      38.840 -41.237 156.788  1.00137.18           C  
ANISOU 1049  CA  PRO A 179    14288  23082  14751   1279   -850  -3437       C  
ATOM   1050  C   PRO A 179      40.201 -41.120 156.098  1.00139.67           C  
ANISOU 1050  C   PRO A 179    14839  23318  14910   1233   -786  -3168       C  
ATOM   1051  O   PRO A 179      40.319 -41.550 154.949  1.00140.34           O  
ANISOU 1051  O   PRO A 179    14903  23537  14884   1333   -827  -3288       O  
ATOM   1052  CB  PRO A 179      38.066 -39.917 156.730  1.00140.19           C  
ANISOU 1052  CB  PRO A 179    14838  23528  14898   1547  -1045  -3438       C  
ATOM   1053  CG  PRO A 179      37.257 -39.909 157.972  1.00144.17           C  
ANISOU 1053  CG  PRO A 179    15189  23970  15621   1458  -1016  -3527       C  
ATOM   1054  CD  PRO A 179      38.167 -40.499 158.995  1.00137.48           C  
ANISOU 1054  CD  PRO A 179    14325  22907  15005   1143   -793  -3314       C  
ATOM   1055  N   VAL A 180      41.234 -40.585 156.795  1.00133.96           N  
ANISOU 1055  N   VAL A 180    14328  22379  14193   1080   -678  -2825       N  
ATOM   1056  CA  VAL A 180      42.579 -40.462 156.211  1.00133.08           C  
ANISOU 1056  CA  VAL A 180    14430  22164  13970   1013   -591  -2577       C  
ATOM   1057  C   VAL A 180      43.217 -41.848 156.004  1.00135.92           C  
ANISOU 1057  C   VAL A 180    14594  22514  14536    800   -444  -2638       C  
ATOM   1058  O   VAL A 180      44.067 -41.995 155.133  1.00135.53           O  
ANISOU 1058  O   VAL A 180    14653  22455  14389    790   -398  -2551       O  
ATOM   1059  CB  VAL A 180      43.535 -39.463 156.922  1.00135.66           C  
ANISOU 1059  CB  VAL A 180    15028  22269  14248    924   -521  -2230       C  
ATOM   1060  CG1 VAL A 180      42.900 -38.081 157.065  1.00136.35           C  
ANISOU 1060  CG1 VAL A 180    15315  22364  14127   1140   -652  -2171       C  
ATOM   1061  CG2 VAL A 180      44.037 -39.989 158.263  1.00133.41           C  
ANISOU 1061  CG2 VAL A 180    14627  21820  14241    651   -383  -2122       C  
ATOM   1062  N   LEU A 181      42.759 -42.867 156.758  1.00131.95           N  
ANISOU 1062  N   LEU A 181    13806  22013  14314    642   -360  -2801       N  
ATOM   1063  CA  LEU A 181      43.210 -44.256 156.621  1.00131.04           C  
ANISOU 1063  CA  LEU A 181    13479  21893  14416    448   -207  -2889       C  
ATOM   1064  C   LEU A 181      42.633 -44.873 155.323  1.00135.33           C  
ANISOU 1064  C   LEU A 181    13863  22660  14897    585   -282  -3189       C  
ATOM   1065  O   LEU A 181      43.105 -45.920 154.874  1.00134.66           O  
ANISOU 1065  O   LEU A 181    13639  22592  14934    457   -169  -3257       O  
ATOM   1066  CB  LEU A 181      42.767 -45.073 157.852  1.00130.24           C  
ANISOU 1066  CB  LEU A 181    13150  21714  14621    273    -77  -2981       C  
ATOM   1067  CG  LEU A 181      43.616 -46.280 158.230  1.00133.82           C  
ANISOU 1067  CG  LEU A 181    13482  22050  15312     23    135  -2920       C  
ATOM   1068  CD1 LEU A 181      44.776 -45.875 159.139  1.00132.07           C  
ANISOU 1068  CD1 LEU A 181    13458  21613  15110   -117    214  -2579       C  
ATOM   1069  CD2 LEU A 181      42.766 -47.336 158.915  1.00136.58           C  
ANISOU 1069  CD2 LEU A 181    13547  22404  15942    -72    264  -3160       C  
ATOM   1070  N   LEU A 182      41.630 -44.200 154.718  1.00132.71           N  
ANISOU 1070  N   LEU A 182    13555  22503  14366    858   -478  -3371       N  
ATOM   1071  CA  LEU A 182      40.967 -44.630 153.488  1.00134.25           C  
ANISOU 1071  CA  LEU A 182    13609  22936  14463   1045   -594  -3685       C  
ATOM   1072  C   LEU A 182      41.416 -43.830 152.263  1.00138.36           C  
ANISOU 1072  C   LEU A 182    14425  23524  14621   1275   -714  -3570       C  
ATOM   1073  O   LEU A 182      41.588 -44.420 151.197  1.00139.18           O  
ANISOU 1073  O   LEU A 182    14475  23750  14657   1333   -726  -3703       O  
ATOM   1074  CB  LEU A 182      39.426 -44.545 153.606  1.00135.97           C  
ANISOU 1074  CB  LEU A 182    13613  23330  14721   1223   -742  -4040       C  
ATOM   1075  CG  LEU A 182      38.762 -44.725 154.981  1.00139.80           C  
ANISOU 1075  CG  LEU A 182    13921  23716  15479   1081   -659  -4107       C  
ATOM   1076  CD1 LEU A 182      37.324 -44.255 154.947  1.00141.65           C  
ANISOU 1076  CD1 LEU A 182    14038  24117  15667   1316   -846  -4407       C  
ATOM   1077  CD2 LEU A 182      38.818 -46.173 155.452  1.00142.16           C  
ANISOU 1077  CD2 LEU A 182    13915  23962  16137    820   -438  -4261       C  
ATOM   1078  N   PHE A 183      41.578 -42.495 152.400  1.00133.86           N  
ANISOU 1078  N   PHE A 183    14172  22870  13817   1416   -792  -3331       N  
ATOM   1079  CA  PHE A 183      41.918 -41.609 151.279  1.00134.52           C  
ANISOU 1079  CA  PHE A 183    14582  22994  13537   1669   -885  -3212       C  
ATOM   1080  C   PHE A 183      43.399 -41.170 151.190  1.00135.90           C  
ANISOU 1080  C   PHE A 183    15059  22944  13635   1537   -725  -2839       C  
ATOM   1081  O   PHE A 183      43.789 -40.607 150.164  1.00136.57           O  
ANISOU 1081  O   PHE A 183    15411  23039  13438   1723   -751  -2748       O  
ATOM   1082  CB  PHE A 183      40.997 -40.370 151.263  1.00137.73           C  
ANISOU 1082  CB  PHE A 183    15156  23477  13699   1975  -1078  -3239       C  
ATOM   1083  CG  PHE A 183      39.521 -40.617 151.502  1.00140.60           C  
ANISOU 1083  CG  PHE A 183    15231  24039  14152   2109  -1240  -3604       C  
ATOM   1084  CD1 PHE A 183      38.807 -41.505 150.704  1.00145.49           C  
ANISOU 1084  CD1 PHE A 183    15582  24893  14804   2219  -1334  -3981       C  
ATOM   1085  CD2 PHE A 183      38.834 -39.920 152.489  1.00142.54           C  
ANISOU 1085  CD2 PHE A 183    15471  24238  14448   2135  -1300  -3589       C  
ATOM   1086  CE1 PHE A 183      37.442 -41.722 150.919  1.00147.77           C  
ANISOU 1086  CE1 PHE A 183    15583  25361  15202   2339  -1475  -4353       C  
ATOM   1087  CE2 PHE A 183      37.468 -40.136 152.701  1.00146.58           C  
ANISOU 1087  CE2 PHE A 183    15709  24923  15062   2255  -1438  -3945       C  
ATOM   1088  CZ  PHE A 183      36.782 -41.034 151.914  1.00146.45           C  
ANISOU 1088  CZ  PHE A 183    15413  25133  15097   2356  -1523  -4333       C  
ATOM   1089  N   ARG A 184      44.223 -41.418 152.225  1.00129.77           N  
ANISOU 1089  N   ARG A 184    14247  21961  13099   1234   -558  -2638       N  
ATOM   1090  CA  ARG A 184      45.634 -41.017 152.162  1.00128.40           C  
ANISOU 1090  CA  ARG A 184    14326  21574  12887   1101   -405  -2322       C  
ATOM   1091  C   ARG A 184      46.562 -42.155 151.731  1.00131.70           C  
ANISOU 1091  C   ARG A 184    14622  21956  13461    890   -257  -2324       C  
ATOM   1092  O   ARG A 184      46.656 -43.180 152.411  1.00130.10           O  
ANISOU 1092  O   ARG A 184    14155  21734  13544    665   -172  -2396       O  
ATOM   1093  CB  ARG A 184      46.130 -40.352 153.460  1.00125.29           C  
ANISOU 1093  CB  ARG A 184    14026  20967  12612    939   -329  -2080       C  
ATOM   1094  CG  ARG A 184      45.699 -38.903 153.588  1.00131.67           C  
ANISOU 1094  CG  ARG A 184    15095  21744  13190   1153   -427  -1969       C  
ATOM   1095  CD  ARG A 184      46.750 -38.063 154.269  1.00137.80           C  
ANISOU 1095  CD  ARG A 184    16089  22273  13995   1014   -300  -1667       C  
ATOM   1096  NE  ARG A 184      46.656 -36.660 153.870  1.00150.49           N  
ANISOU 1096  NE  ARG A 184    18025  23830  15324   1241   -341  -1535       N  
ATOM   1097  CZ  ARG A 184      47.597 -35.748 154.102  1.00168.70           C  
ANISOU 1097  CZ  ARG A 184    20582  25922  17595   1177   -215  -1286       C  
ATOM   1098  NH1 ARG A 184      48.718 -36.086 154.731  1.00156.93           N  
ANISOU 1098  NH1 ARG A 184    19038  24259  16327    898    -64  -1155       N  
ATOM   1099  NH2 ARG A 184      47.430 -34.496 153.698  1.00157.77           N  
ANISOU 1099  NH2 ARG A 184    19500  24491  15955   1399   -233  -1178       N  
ATOM   1100  N   ARG A 185      47.243 -41.956 150.583  1.00128.61           N  
ANISOU 1100  N   ARG A 185    14443  21547  12875    973   -215  -2241       N  
ATOM   1101  CA  ARG A 185      48.198 -42.898 149.983  1.00127.37           C  
ANISOU 1101  CA  ARG A 185    14223  21349  12822    800    -72  -2225       C  
ATOM   1102  C   ARG A 185      49.230 -42.180 149.094  1.00129.75           C  
ANISOU 1102  C   ARG A 185    14877  21514  12907    864     24  -2010       C  
ATOM   1103  O   ARG A 185      49.263 -40.945 149.069  1.00129.74           O  
ANISOU 1103  O   ARG A 185    15168  21425  12704   1017      5  -1854       O  
ATOM   1104  CB  ARG A 185      47.481 -44.045 149.223  1.00128.94           C  
ANISOU 1104  CB  ARG A 185    14151  21783  13056    860   -140  -2543       C  
ATOM   1105  CG  ARG A 185      46.350 -43.620 148.272  1.00140.76           C  
ANISOU 1105  CG  ARG A 185    15706  23514  14262   1221   -346  -2763       C  
ATOM   1106  CD  ARG A 185      46.086 -44.631 147.163  1.00151.47           C  
ANISOU 1106  CD  ARG A 185    16891  25070  15591   1292   -382  -3028       C  
ATOM   1107  NE  ARG A 185      45.716 -45.961 147.661  1.00161.65           N  
ANISOU 1107  NE  ARG A 185    17767  26438  17215   1080   -330  -3259       N  
ATOM   1108  CZ  ARG A 185      46.511 -47.030 147.619  1.00177.16           C  
ANISOU 1108  CZ  ARG A 185    19584  28331  19399    821   -157  -3237       C  
ATOM   1109  NH1 ARG A 185      47.732 -46.939 147.103  1.00162.43           N  
ANISOU 1109  NH1 ARG A 185    17934  26318  17465    730    -31  -3004       N  
ATOM   1110  NH2 ARG A 185      46.091 -48.195 148.093  1.00165.86           N  
ANISOU 1110  NH2 ARG A 185    17790  26963  18267    650    -94  -3453       N  
ATOM   1111  N   THR A 186      50.081 -42.955 148.383  1.00124.77           N  
ANISOU 1111  N   THR A 186    14223  20852  12332    740    148  -2003       N  
ATOM   1112  CA  THR A 186      51.098 -42.425 147.472  1.00124.61           C  
ANISOU 1112  CA  THR A 186    14523  20688  12135    780    276  -1822       C  
ATOM   1113  C   THR A 186      50.412 -41.880 146.207  1.00128.47           C  
ANISOU 1113  C   THR A 186    15238  21329  12245   1147    158  -1916       C  
ATOM   1114  O   THR A 186      49.714 -42.626 145.515  1.00128.95           O  
ANISOU 1114  O   THR A 186    15133  21614  12247   1267     47  -2160       O  
ATOM   1115  CB  THR A 186      52.199 -43.475 147.190  1.00132.13           C  
ANISOU 1115  CB  THR A 186    15357  21552  13294    516    450  -1794       C  
ATOM   1116  OG1 THR A 186      52.698 -43.997 148.427  1.00129.69           O  
ANISOU 1116  OG1 THR A 186    14830  21127  13317    221    529  -1730       O  
ATOM   1117  CG2 THR A 186      53.357 -42.908 146.379  1.00130.85           C  
ANISOU 1117  CG2 THR A 186    15522  21195  13001    514    621  -1596       C  
ATOM   1118  N   VAL A 187      50.588 -40.570 145.939  1.00124.29           N  
ANISOU 1118  N   VAL A 187    15087  20677  11460   1336    185  -1732       N  
ATOM   1119  CA  VAL A 187      50.009 -39.872 144.785  1.00125.89           C  
ANISOU 1119  CA  VAL A 187    15580  20990  11262   1723     88  -1778       C  
ATOM   1120  C   VAL A 187      51.117 -39.478 143.779  1.00129.01           C  
ANISOU 1120  C   VAL A 187    16338  21193  11486   1755    298  -1589       C  
ATOM   1121  O   VAL A 187      51.989 -38.660 144.090  1.00127.80           O  
ANISOU 1121  O   VAL A 187    16426  20777  11357   1655    482  -1345       O  
ATOM   1122  CB  VAL A 187      49.056 -38.693 145.176  1.00130.53           C  
ANISOU 1122  CB  VAL A 187    16326  21624  11645   1992    -65  -1761       C  
ATOM   1123  CG1 VAL A 187      49.636 -37.820 146.281  1.00128.85           C  
ANISOU 1123  CG1 VAL A 187    16236  21160  11562   1822     59  -1510       C  
ATOM   1124  CG2 VAL A 187      48.663 -37.846 143.968  1.00133.34           C  
ANISOU 1124  CG2 VAL A 187    17054  22051  11558   2412   -132  -1761       C  
ATOM   1125  N   TYR A 188      51.076 -40.101 142.580  1.00125.81           N  
ANISOU 1125  N   TYR A 188    15957  20922  10924   1888    279  -1722       N  
ATOM   1126  CA  TYR A 188      52.024 -39.885 141.482  1.00126.13           C  
ANISOU 1126  CA  TYR A 188    16331  20809  10784   1945    475  -1585       C  
ATOM   1127  C   TYR A 188      51.522 -38.809 140.524  1.00132.35           C  
ANISOU 1127  C   TYR A 188    17546  21630  11111   2388    419  -1545       C  
ATOM   1128  O   TYR A 188      50.328 -38.769 140.218  1.00133.56           O  
ANISOU 1128  O   TYR A 188    17646  22045  11054   2693    168  -1745       O  
ATOM   1129  CB  TYR A 188      52.267 -41.190 140.711  1.00126.83           C  
ANISOU 1129  CB  TYR A 188    16212  21027  10952   1851    487  -1755       C  
ATOM   1130  CG  TYR A 188      52.933 -42.276 141.522  1.00125.11           C  
ANISOU 1130  CG  TYR A 188    15623  20741  11171   1421    587  -1767       C  
ATOM   1131  CD1 TYR A 188      54.298 -42.239 141.785  1.00125.91           C  
ANISOU 1131  CD1 TYR A 188    15811  20557  11472   1132    840  -1552       C  
ATOM   1132  CD2 TYR A 188      52.211 -43.372 141.981  1.00124.56           C  
ANISOU 1132  CD2 TYR A 188    15118  20890  11320   1314    441  -2008       C  
ATOM   1133  CE1 TYR A 188      54.922 -43.242 142.527  1.00124.73           C  
ANISOU 1133  CE1 TYR A 188    15332  20352  11709    765    921  -1564       C  
ATOM   1134  CE2 TYR A 188      52.823 -44.386 142.719  1.00123.05           C  
ANISOU 1134  CE2 TYR A 188    14612  20627  11514    942    548  -2008       C  
ATOM   1135  CZ  TYR A 188      54.181 -44.318 142.988  1.00128.53           C  
ANISOU 1135  CZ  TYR A 188    15408  21048  12380    678    777  -1782       C  
ATOM   1136  OH  TYR A 188      54.800 -45.313 143.707  1.00125.51           O  
ANISOU 1136  OH  TYR A 188    14729  20599  12362    339    873  -1783       O  
ATOM   1137  N   SER A 189      52.434 -37.943 140.048  1.00129.38           N  
ANISOU 1137  N   SER A 189    17595  20981  10581   2433    661  -1299       N  
ATOM   1138  CA  SER A 189      52.101 -36.853 139.128  1.00132.29           C  
ANISOU 1138  CA  SER A 189    18441  21326  10498   2861    667  -1218       C  
ATOM   1139  C   SER A 189      53.158 -36.644 138.040  1.00136.87           C  
ANISOU 1139  C   SER A 189    19410  21681  10913   2901    953  -1059       C  
ATOM   1140  O   SER A 189      54.231 -37.247 138.099  1.00135.08           O  
ANISOU 1140  O   SER A 189    19074  21294  10955   2565   1154  -1000       O  
ATOM   1141  CB  SER A 189      51.839 -35.560 139.894  1.00136.90           C  
ANISOU 1141  CB  SER A 189    19222  21775  11020   2951    680  -1054       C  
ATOM   1142  OG  SER A 189      50.547 -35.562 140.480  1.00148.05           O  
ANISOU 1142  OG  SER A 189    20396  23447  12410   3099    375  -1233       O  
ATOM   1143  N   SER A 190      52.843 -35.793 137.044  1.00135.76           N  
ANISOU 1143  N   SER A 190    19732  21524  10325   3326    974   -996       N  
ATOM   1144  CA  SER A 190      53.709 -35.481 135.911  1.00137.50           C  
ANISOU 1144  CA  SER A 190    20392  21527  10326   3436   1255   -847       C  
ATOM   1145  C   SER A 190      54.993 -34.739 136.307  1.00141.70           C  
ANISOU 1145  C   SER A 190    21169  21631  11039   3175   1643   -567       C  
ATOM   1146  O   SER A 190      54.931 -33.604 136.782  1.00141.84           O  
ANISOU 1146  O   SER A 190    21431  21485  10977   3273   1729   -412       O  
ATOM   1147  CB  SER A 190      52.934 -34.713 134.844  1.00143.83           C  
ANISOU 1147  CB  SER A 190    21634  22436  10576   4001   1161   -862       C  
ATOM   1148  OG  SER A 190      53.725 -34.470 133.694  1.00151.88           O  
ANISOU 1148  OG  SER A 190    23122  23221  11363   4127   1461   -704       O  
ATOM   1149  N   ASN A 191      56.157 -35.411 136.120  1.00138.01           N  
ANISOU 1149  N   ASN A 191    20621  20984  10832   2840   1880   -524       N  
ATOM   1150  CA  ASN A 191      57.541 -34.959 136.383  1.00137.42           C  
ANISOU 1150  CA  ASN A 191    20715  20504  10996   2540   2270   -314       C  
ATOM   1151  C   ASN A 191      57.868 -34.638 137.869  1.00140.03           C  
ANISOU 1151  C   ASN A 191    20788  20705  11713   2206   2295   -245       C  
ATOM   1152  O   ASN A 191      59.017 -34.296 138.172  1.00139.49           O  
ANISOU 1152  O   ASN A 191    20804  20313  11883   1940   2599   -107       O  
ATOM   1153  CB  ASN A 191      57.934 -33.769 135.486  1.00139.30           C  
ANISOU 1153  CB  ASN A 191    21578  20462  10887   2830   2570   -118       C  
ATOM   1154  CG  ASN A 191      57.871 -34.048 134.009  1.00152.21           C  
ANISOU 1154  CG  ASN A 191    23519  22157  12156   3132   2615   -156       C  
ATOM   1155  OD1 ASN A 191      57.003 -33.540 133.299  1.00144.16           O  
ANISOU 1155  OD1 ASN A 191    22812  21273  10687   3596   2489   -171       O  
ATOM   1156  ND2 ASN A 191      58.795 -34.851 133.508  1.00143.48           N  
ANISOU 1156  ND2 ASN A 191    22338  20951  11227   2888   2794   -175       N  
ATOM   1157  N   VAL A 192      56.891 -34.780 138.785  1.00135.29           N  
ANISOU 1157  N   VAL A 192    19863  20351  11188   2213   1983   -357       N  
ATOM   1158  CA  VAL A 192      57.083 -34.501 140.213  1.00132.62           C  
ANISOU 1158  CA  VAL A 192    19281  19923  11187   1932   1972   -305       C  
ATOM   1159  C   VAL A 192      57.263 -35.802 141.012  1.00134.59           C  
ANISOU 1159  C   VAL A 192    18996  20308  11833   1569   1841   -443       C  
ATOM   1160  O   VAL A 192      56.806 -36.864 140.583  1.00133.66           O  
ANISOU 1160  O   VAL A 192    18652  20435  11698   1595   1673   -614       O  
ATOM   1161  CB  VAL A 192      55.969 -33.589 140.809  1.00136.66           C  
ANISOU 1161  CB  VAL A 192    19857  20546  11521   2179   1773   -295       C  
ATOM   1162  CG1 VAL A 192      56.456 -32.881 142.069  1.00134.81           C  
ANISOU 1162  CG1 VAL A 192    19559  20097  11567   1929   1887   -169       C  
ATOM   1163  CG2 VAL A 192      55.480 -32.560 139.795  1.00139.75           C  
ANISOU 1163  CG2 VAL A 192    20758  20904  11436   2635   1824   -211       C  
ATOM   1164  N   SER A 193      57.948 -35.702 142.171  1.00130.46           N  
ANISOU 1164  N   SER A 193    18286  19618  11667   1241   1932   -371       N  
ATOM   1165  CA  SER A 193      58.234 -36.780 143.124  1.00128.01           C  
ANISOU 1165  CA  SER A 193    17508  19381  11749    894   1842   -464       C  
ATOM   1166  C   SER A 193      56.941 -37.344 143.752  1.00131.75           C  
ANISOU 1166  C   SER A 193    17656  20177  12226    971   1508   -628       C  
ATOM   1167  O   SER A 193      55.972 -36.588 143.889  1.00131.94           O  
ANISOU 1167  O   SER A 193    17802  20301  12028   1229   1362   -632       O  
ATOM   1168  CB  SER A 193      59.136 -36.257 144.241  1.00130.13           C  
ANISOU 1168  CB  SER A 193    17724  19394  12325    613   1999   -345       C  
ATOM   1169  OG  SER A 193      60.384 -35.792 143.757  1.00140.26           O  
ANISOU 1169  OG  SER A 193    19262  20364  13666    505   2328   -226       O  
ATOM   1170  N   PRO A 194      56.910 -38.637 144.185  1.00127.54           N  
ANISOU 1170  N   PRO A 194    16713  19791  11953    751   1401   -767       N  
ATOM   1171  CA  PRO A 194      55.692 -39.169 144.830  1.00127.11           C  
ANISOU 1171  CA  PRO A 194    16349  20014  11935    808   1124   -936       C  
ATOM   1172  C   PRO A 194      55.312 -38.386 146.090  1.00132.46           C  
ANISOU 1172  C   PRO A 194    16987  20645  12698    782   1047   -866       C  
ATOM   1173  O   PRO A 194      56.195 -37.872 146.776  1.00131.12           O  
ANISOU 1173  O   PRO A 194    16870  20243  12705    590   1198   -718       O  
ATOM   1174  CB  PRO A 194      56.071 -40.615 145.169  1.00126.75           C  
ANISOU 1174  CB  PRO A 194    15915  20039  12206    519   1122  -1049       C  
ATOM   1175  CG  PRO A 194      57.210 -40.939 144.294  1.00131.34           C  
ANISOU 1175  CG  PRO A 194    16624  20463  12814    405   1341   -984       C  
ATOM   1176  CD  PRO A 194      57.966 -39.668 144.123  1.00127.78           C  
ANISOU 1176  CD  PRO A 194    16549  19734  12266    443   1543   -781       C  
ATOM   1177  N   ALA A 195      54.005 -38.269 146.382  1.00131.21           N  
ANISOU 1177  N   ALA A 195    16736  20703  12416    982    814   -985       N  
ATOM   1178  CA  ALA A 195      53.541 -37.503 147.541  1.00131.02           C  
ANISOU 1178  CA  ALA A 195    16685  20647  12449    981    731   -927       C  
ATOM   1179  C   ALA A 195      52.511 -38.230 148.425  1.00135.76           C  
ANISOU 1179  C   ALA A 195    16917  21465  13201    939    516  -1107       C  
ATOM   1180  O   ALA A 195      52.045 -39.311 148.063  1.00135.14           O  
ANISOU 1180  O   ALA A 195    16603  21578  13165    939    425  -1297       O  
ATOM   1181  CB  ALA A 195      53.006 -36.154 147.084  1.00133.76           C  
ANISOU 1181  CB  ALA A 195    17401  20967  12457   1306    708   -843       C  
ATOM   1182  N   CYS A 196      52.187 -37.639 149.600  1.00133.10           N  
ANISOU 1182  N   CYS A 196    16529  21080  12962    891    459  -1050       N  
ATOM   1183  CA  CYS A 196      51.210 -38.165 150.553  1.00132.52           C  
ANISOU 1183  CA  CYS A 196    16146  21169  13034    855    287  -1200       C  
ATOM   1184  C   CYS A 196      50.117 -37.156 150.838  1.00137.80           C  
ANISOU 1184  C   CYS A 196    16927  21915  13514   1099    134  -1216       C  
ATOM   1185  O   CYS A 196      50.279 -36.315 151.727  1.00136.69           O  
ANISOU 1185  O   CYS A 196    16876  21635  13426   1044    165  -1076       O  
ATOM   1186  CB  CYS A 196      51.879 -38.633 151.843  1.00130.81           C  
ANISOU 1186  CB  CYS A 196    15717  20827  13159    535    364  -1133       C  
ATOM   1187  SG  CYS A 196      52.123 -40.422 151.947  1.00133.68           S  
ANISOU 1187  SG  CYS A 196    15707  21281  13803    298    396  -1285       S  
ATOM   1188  N   TYR A 197      49.008 -37.229 150.082  1.00136.63           N  
ANISOU 1188  N   TYR A 197    16772  21993  13150   1376    -35  -1400       N  
ATOM   1189  CA  TYR A 197      47.834 -36.388 150.311  1.00137.99           C  
ANISOU 1189  CA  TYR A 197    17013  22272  13145   1631   -209  -1460       C  
ATOM   1190  C   TYR A 197      46.551 -37.044 149.795  1.00143.42           C  
ANISOU 1190  C   TYR A 197    17488  23255  13749   1837   -422  -1766       C  
ATOM   1191  O   TYR A 197      46.603 -38.044 149.071  1.00142.73           O  
ANISOU 1191  O   TYR A 197    17253  23288  13689   1819   -427  -1922       O  
ATOM   1192  CB  TYR A 197      47.992 -34.928 149.818  1.00141.30           C  
ANISOU 1192  CB  TYR A 197    17861  22566  13259   1870   -160  -1271       C  
ATOM   1193  CG  TYR A 197      48.452 -34.731 148.390  1.00145.97           C  
ANISOU 1193  CG  TYR A 197    18752  23136  13576   2064    -73  -1222       C  
ATOM   1194  CD1 TYR A 197      47.543 -34.757 147.335  1.00150.68           C  
ANISOU 1194  CD1 TYR A 197    19423  23954  13874   2412   -240  -1394       C  
ATOM   1195  CD2 TYR A 197      49.766 -34.368 148.106  1.00146.74           C  
ANISOU 1195  CD2 TYR A 197    19091  22976  13687   1931    179  -1003       C  
ATOM   1196  CE1 TYR A 197      47.948 -34.514 146.021  1.00154.18           C  
ANISOU 1196  CE1 TYR A 197    20184  24369  14030   2625   -156  -1337       C  
ATOM   1197  CE2 TYR A 197      50.180 -34.107 146.799  1.00149.90           C  
ANISOU 1197  CE2 TYR A 197    19807  23327  13821   2122    288   -944       C  
ATOM   1198  CZ  TYR A 197      49.271 -34.194 145.757  1.00160.91           C  
ANISOU 1198  CZ  TYR A 197    21285  24947  14905   2474    120  -1104       C  
ATOM   1199  OH  TYR A 197      49.679 -33.960 144.463  1.00164.73           O  
ANISOU 1199  OH  TYR A 197    22103  25381  15106   2682    230  -1043       O  
ATOM   1200  N   GLU A 198      45.399 -36.500 150.230  1.00141.69           N  
ANISOU 1200  N   GLU A 198    17232  23150  13454   2020   -596  -1871       N  
ATOM   1201  CA  GLU A 198      44.053 -36.959 149.883  1.00143.33           C  
ANISOU 1201  CA  GLU A 198    17221  23637  13600   2234   -815  -2194       C  
ATOM   1202  C   GLU A 198      43.665 -36.653 148.420  1.00150.27           C  
ANISOU 1202  C   GLU A 198    18312  24677  14108   2611   -931  -2298       C  
ATOM   1203  O   GLU A 198      44.484 -36.133 147.654  1.00150.78           O  
ANISOU 1203  O   GLU A 198    18711  24617  13961   2696   -814  -2101       O  
ATOM   1204  CB  GLU A 198      43.025 -36.379 150.873  1.00144.51           C  
ANISOU 1204  CB  GLU A 198    17280  23830  13800   2301   -948  -2260       C  
ATOM   1205  CG  GLU A 198      42.864 -37.223 152.123  1.00153.42           C  
ANISOU 1205  CG  GLU A 198    18050  24934  15307   1997   -907  -2348       C  
ATOM   1206  CD  GLU A 198      42.123 -36.560 153.266  1.00173.88           C  
ANISOU 1206  CD  GLU A 198    20600  27491  17975   2000   -977  -2337       C  
ATOM   1207  OE1 GLU A 198      42.777 -35.855 154.068  1.00164.34           O  
ANISOU 1207  OE1 GLU A 198    19558  26075  16807   1869   -873  -2074       O  
ATOM   1208  OE2 GLU A 198      40.889 -36.754 153.367  1.00171.13           O  
ANISOU 1208  OE2 GLU A 198    20044  27321  17658   2130  -1133  -2606       O  
ATOM   1209  N   ASP A 199      42.420 -36.998 148.035  1.00148.29           N  
ANISOU 1209  N   ASP A 199    17863  24698  13783   2843  -1154  -2624       N  
ATOM   1210  CA  ASP A 199      41.899 -36.791 146.686  1.00175.53           C  
ANISOU 1210  CA  ASP A 199    21473  28346  16876   3240  -1309  -2781       C  
ATOM   1211  C   ASP A 199      40.556 -36.065 146.719  1.00192.64           C  
ANISOU 1211  C   ASP A 199    23647  30692  18857   3585  -1558  -2963       C  
ATOM   1212  O   ASP A 199      40.460 -34.964 147.261  1.00147.71           O  
ANISOU 1212  O   ASP A 199    18173  24877  13071   3660  -1553  -2773       O  
ATOM   1213  CB  ASP A 199      41.775 -38.138 145.950  1.00177.95           C  
ANISOU 1213  CB  ASP A 199    21486  28848  17277   3202  -1352  -3070       C  
ATOM   1214  CG  ASP A 199      43.068 -38.938 145.829  1.00185.56           C  
ANISOU 1214  CG  ASP A 199    22427  29655  18421   2877  -1117  -2918       C  
ATOM   1215  OD1 ASP A 199      44.149 -38.315 145.702  1.00184.81           O  
ANISOU 1215  OD1 ASP A 199    22655  29325  18240   2802   -935  -2595       O  
ATOM   1216  OD2 ASP A 199      42.996 -40.185 145.842  1.00191.36           O  
ANISOU 1216  OD2 ASP A 199    22818  30499  19390   2703  -1105  -3134       O  
ATOM   1217  N   ALA A 205      34.504 -37.980 146.072  1.00184.54           N  
ANISOU 1217  N   ALA A 205    21158  30952  18007   4486  -2650  -4943       N  
ATOM   1218  CA  ALA A 205      33.050 -37.917 145.919  1.00187.10           C  
ANISOU 1218  CA  ALA A 205    21237  31548  18306   4788  -2928  -5385       C  
ATOM   1219  C   ALA A 205      32.389 -37.081 147.038  1.00189.80           C  
ANISOU 1219  C   ALA A 205    21573  31797  18746   4772  -2968  -5324       C  
ATOM   1220  O   ALA A 205      33.101 -36.462 147.833  1.00186.79           O  
ANISOU 1220  O   ALA A 205    21421  31148  18402   4561  -2790  -4919       O  
ATOM   1221  CB  ALA A 205      32.472 -39.327 145.886  1.00188.36           C  
ANISOU 1221  CB  ALA A 205    20868  31888  18812   4632  -2945  -5847       C  
ATOM   1222  N   ASN A 206      31.035 -37.042 147.079  1.00188.70           N  
ANISOU 1222  N   ASN A 206    21169  31880  18647   5003  -3204  -5738       N  
ATOM   1223  CA  ASN A 206      30.258 -36.306 148.084  1.00187.97           C  
ANISOU 1223  CA  ASN A 206    21029  31731  18658   5013  -3265  -5748       C  
ATOM   1224  C   ASN A 206      30.498 -36.830 149.505  1.00187.66           C  
ANISOU 1224  C   ASN A 206    20758  31464  19079   4518  -3015  -5641       C  
ATOM   1225  O   ASN A 206      30.527 -36.034 150.446  1.00184.84           O  
ANISOU 1225  O   ASN A 206    20546  30926  18758   4425  -2952  -5391       O  
ATOM   1226  CB  ASN A 206      28.768 -36.322 147.746  1.00191.37           C  
ANISOU 1226  CB  ASN A 206    21173  32464  19074   5353  -3566  -6277       C  
ATOM   1227  CG  ASN A 206      28.321 -35.171 146.881  1.00205.65           C  
ANISOU 1227  CG  ASN A 206    23883  33217  21040   4870  -3412  -5344       C  
ATOM   1228  OD1 ASN A 206      28.165 -35.302 145.664  1.00201.59           O  
ANISOU 1228  OD1 ASN A 206    23453  32846  20296   5113  -3552  -5476       O  
ATOM   1229  ND2 ASN A 206      28.092 -34.015 147.489  1.00198.83           N  
ANISOU 1229  ND2 ASN A 206    22963  32830  19755   5449  -3646  -5584       N  
ATOM   1230  N   TRP A 207      30.682 -38.164 149.650  1.00183.64           N  
ANISOU 1230  N   TRP A 207    19905  30962  18910   4216  -2865  -5826       N  
ATOM   1231  CA  TRP A 207      30.959 -38.845 150.921  1.00180.54           C  
ANISOU 1231  CA  TRP A 207    19292  30355  18949   3758  -2606  -5741       C  
ATOM   1232  C   TRP A 207      32.358 -38.484 151.437  1.00181.25           C  
ANISOU 1232  C   TRP A 207    19716  30150  19001   3497  -2377  -5193       C  
ATOM   1233  O   TRP A 207      32.546 -38.358 152.648  1.00178.24           O  
ANISOU 1233  O   TRP A 207    19326  29560  18836   3233  -2223  -5000       O  
ATOM   1234  CB  TRP A 207      30.831 -40.372 150.768  1.00179.39           C  
ANISOU 1234  CB  TRP A 207    18725  30298  19136   3547  -2497  -6085       C  
ATOM   1235  CG  TRP A 207      29.447 -40.846 150.431  1.00183.13           C  
ANISOU 1235  CG  TRP A 207    18801  31040  19742   3741  -2681  -6673       C  
ATOM   1236  CD1 TRP A 207      28.966 -41.157 149.193  1.00188.89           C  
ANISOU 1236  CD1 TRP A 207    19408  32059  20305   4045  -2893  -7040       C  
ATOM   1237  CD2 TRP A 207      28.367 -41.070 151.350  1.00183.26           C  
ANISOU 1237  CD2 TRP A 207    18478  31055  20099   3644  -2662  -6985       C  
ATOM   1238  NE1 TRP A 207      27.652 -41.558 149.281  1.00189.39           N  
ANISOU 1238  NE1 TRP A 207    19134  32190  20637   4077  -2984  -7470       N  
ATOM   1239  CE2 TRP A 207      27.258 -41.514 150.594  1.00189.99           C  
ANISOU 1239  CE2 TRP A 207    19011  32175  21002   3880  -2860  -7530       C  
ATOM   1240  CE3 TRP A 207      28.224 -40.932 152.743  1.00182.57           C  
ANISOU 1240  CE3 TRP A 207    18343  30739  20288   3376  -2486  -6846       C  
ATOM   1241  CZ2 TRP A 207      26.025 -41.823 151.183  1.00189.83           C  
ANISOU 1241  CZ2 TRP A 207    18706  32063  21358   3774  -2836  -7818       C  
ATOM   1242  CZ3 TRP A 207      27.002 -41.237 153.324  1.00185.55           C  
ANISOU 1242  CZ3 TRP A 207    18354  31172  20973   3356  -2498  -7265       C  
ATOM   1243  CH2 TRP A 207      25.920 -41.679 152.549  1.00189.46           C  
ANISOU 1243  CH2 TRP A 207    18506  31955  21527   3593  -2690  -7840       C  
ATOM   1244  N   ARG A 208      33.329 -38.309 150.511  1.00178.54           N  
ANISOU 1244  N   ARG A 208    19666  29789  18381   3583  -2355  -4959       N  
ATOM   1245  CA  ARG A 208      34.721 -37.945 150.801  1.00176.16           C  
ANISOU 1245  CA  ARG A 208    19687  29221  18022   3368  -2145  -4471       C  
ATOM   1246  C   ARG A 208      34.833 -36.554 151.432  1.00178.76           C  
ANISOU 1246  C   ARG A 208    20344  29387  18190   3441  -2152  -4149       C  
ATOM   1247  O   ARG A 208      35.723 -36.340 152.254  1.00175.90           O  
ANISOU 1247  O   ARG A 208    20114  28778  17943   3168  -1959  -3814       O  
ATOM   1248  CB  ARG A 208      35.587 -38.043 149.535  1.00178.02           C  
ANISOU 1248  CB  ARG A 208    20156  29494  17990   3489  -2128  -4354       C  
ATOM   1249  N   MET A 209      33.934 -35.618 151.050  1.00177.30           N  
ANISOU 1249  N   MET A 209    20284  29341  17741   3817  -2377  -4263       N  
ATOM   1250  CA  MET A 209      33.881 -34.263 151.607  1.00176.79           C  
ANISOU 1250  CA  MET A 209    20516  29140  17517   3920  -2397  -3997       C  
ATOM   1251  C   MET A 209      33.215 -34.309 152.988  1.00178.92           C  
ANISOU 1251  C   MET A 209    20535  29336  18110   3709  -2368  -4078       C  
ATOM   1252  O   MET A 209      33.653 -33.596 153.891  1.00176.59           O  
ANISOU 1252  O   MET A 209    20417  28825  17853   3557  -2252  -3770       O  
ATOM   1253  CB  MET A 209      33.145 -33.287 150.665  1.00182.31           C  
ANISOU 1253  CB  MET A 209    21448  30016  17806   4420  -2644  -4095       C  
ATOM   1254  CG  MET A 209      33.142 -31.827 151.148  1.00185.80           C  
ANISOU 1254  CG  MET A 209    22237  30305  18054   4547  -2644  -3796       C  
ATOM   1255  SD  MET A 209      34.682 -30.908 150.859  1.00189.05           S  
ANISOU 1255  SD  MET A 209    23185  30434  18211   4505  -2413  -3256       S  
ATOM   1256  CE  MET A 209      35.466 -31.032 152.445  1.00181.73           C  
ANISOU 1256  CE  MET A 209    22159  29214  17677   3985  -2158  -2985       C  
ATOM   1257  N   LEU A 210      32.171 -35.157 153.148  1.00175.90           N  
ANISOU 1257  N   LEU A 210    19741  29124  17969   3698  -2458  -4502       N  
ATOM   1258  CA  LEU A 210      31.445 -35.359 154.409  1.00174.28           C  
ANISOU 1258  CA  LEU A 210    19267  28852  18100   3498  -2409  -4635       C  
ATOM   1259  C   LEU A 210      32.376 -35.936 155.465  1.00174.41           C  
ANISOU 1259  C   LEU A 210    19243  28615  18409   3059  -2128  -4378       C  
ATOM   1260  O   LEU A 210      32.307 -35.534 156.624  1.00172.67           O  
ANISOU 1260  O   LEU A 210    19050  28227  18328   2901  -2044  -4225       O  
ATOM   1261  CB  LEU A 210      30.253 -36.309 154.214  1.00176.16           C  
ANISOU 1261  CB  LEU A 210    19058  29313  18561   3558  -2518  -5173       C  
ATOM   1262  CG  LEU A 210      29.034 -35.750 153.497  1.00184.24           C  
ANISOU 1262  CG  LEU A 210    20032  30596  19374   3988  -2822  -5514       C  
ATOM   1263  CD1 LEU A 210      28.226 -36.867 152.875  1.00186.57           C  
ANISOU 1263  CD1 LEU A 210    19910  31140  19839   4062  -2919  -6047       C  
ATOM   1264  CD2 LEU A 210      28.170 -34.916 154.436  1.00187.02           C  
ANISOU 1264  CD2 LEU A 210    20368  30894  19796   4038  -2890  -5542       C  
ATOM   1265  N   LEU A 211      33.262 -36.861 155.049  1.00169.53           N  
ANISOU 1265  N   LEU A 211    18576  27970  17867   2879  -1989  -4326       N  
ATOM   1266  CA  LEU A 211      34.262 -37.506 155.898  1.00166.29           C  
ANISOU 1266  CA  LEU A 211    18138  27334  17709   2491  -1731  -4088       C  
ATOM   1267  C   LEU A 211      35.443 -36.559 156.211  1.00167.18           C  
ANISOU 1267  C   LEU A 211    18638  27227  17656   2415  -1634  -3612       C  
ATOM   1268  O   LEU A 211      36.309 -36.908 157.013  1.00164.57           O  
ANISOU 1268  O   LEU A 211    18317  26703  17511   2117  -1440  -3392       O  
ATOM   1269  CB  LEU A 211      34.731 -38.828 155.252  1.00166.47           C  
ANISOU 1269  CB  LEU A 211    17963  27423  17864   2353  -1630  -4228       C  
ATOM   1270  CG  LEU A 211      34.092 -40.134 155.780  1.00171.12           C  
ANISOU 1270  CG  LEU A 211    18128  28047  18844   2150  -1520  -4561       C  
ATOM   1271  CD1 LEU A 211      32.617 -40.267 155.383  1.00176.23           C  
ANISOU 1271  CD1 LEU A 211    18499  28935  19527   2385  -1708  -5039       C  
ATOM   1272  CD2 LEU A 211      34.857 -41.349 155.294  1.00170.71           C  
ANISOU 1272  CD2 LEU A 211    17945  27995  18923   1963  -1368  -4589       C  
ATOM   1273  N   ARG A 212      35.450 -35.351 155.599  1.00163.99           N  
ANISOU 1273  N   ARG A 212    18549  26851  16909   2696  -1764  -3472       N  
ATOM   1274  CA  ARG A 212      36.446 -34.295 155.809  1.00162.27           C  
ANISOU 1274  CA  ARG A 212    18707  26427  16520   2666  -1671  -3058       C  
ATOM   1275  C   ARG A 212      35.841 -33.111 156.587  1.00165.29           C  
ANISOU 1275  C   ARG A 212    19220  26747  16835   2773  -1747  -2969       C  
ATOM   1276  O   ARG A 212      36.566 -32.428 157.311  1.00163.42           O  
ANISOU 1276  O   ARG A 212    19188  26302  16602   2635  -1628  -2659       O  
ATOM   1277  CB  ARG A 212      37.036 -33.820 154.473  1.00163.68           C  
ANISOU 1277  CB  ARG A 212    19190  26646  16356   2895  -1703  -2936       C  
ATOM   1278  N   ILE A 213      34.512 -32.887 156.443  1.00162.59           N  
ANISOU 1278  N   ILE A 213    18744  26587  16444   3016  -1944  -3259       N  
ATOM   1279  CA  ILE A 213      33.728 -31.833 157.106  1.00162.02           C  
ANISOU 1279  CA  ILE A 213    18754  26489  16316   3145  -2041  -3236       C  
ATOM   1280  C   ILE A 213      33.349 -32.246 158.545  1.00162.35           C  
ANISOU 1280  C   ILE A 213    18548  26422  16717   2858  -1944  -3289       C  
ATOM   1281  O   ILE A 213      33.390 -31.408 159.452  1.00160.85           O  
ANISOU 1281  O   ILE A 213    18496  26079  16540   2792  -1902  -3085       O  
ATOM   1282  CB  ILE A 213      32.501 -31.427 156.217  1.00168.13           C  
ANISOU 1282  CB  ILE A 213    19503  27515  16861   3563  -2307  -3538       C  
ATOM   1283  CG1 ILE A 213      32.913 -30.516 155.022  1.00170.37           C  
ANISOU 1283  CG1 ILE A 213    20184  27837  16711   3897  -2385  -3364       C  
ATOM   1284  CG2 ILE A 213      31.331 -30.822 157.001  1.00169.15           C  
ANISOU 1284  CG2 ILE A 213    19528  27674  17069   3652  -2425  -3684       C  
ATOM   1285  CD1 ILE A 213      33.691 -29.161 155.329  1.00176.60           C  
ANISOU 1285  CD1 ILE A 213    21401  28390  17308   3903  -2266  -2926       C  
ATOM   1286  N   LEU A 214      32.981 -33.533 158.741  1.00157.32           N  
ANISOU 1286  N   LEU A 214    17555  25855  16366   2695  -1895  -3566       N  
ATOM   1287  CA  LEU A 214      32.614 -34.117 160.035  1.00155.05           C  
ANISOU 1287  CA  LEU A 214    17025  25457  16431   2426  -1767  -3646       C  
ATOM   1288  C   LEU A 214      33.743 -33.950 161.092  1.00155.32           C  
ANISOU 1288  C   LEU A 214    17224  25226  16565   2134  -1563  -3263       C  
ATOM   1289  O   LEU A 214      33.455 -33.382 162.150  1.00153.58           O  
ANISOU 1289  O   LEU A 214    17042  24887  16426   2065  -1536  -3171       O  
ATOM   1290  CB  LEU A 214      32.204 -35.590 159.864  1.00155.46           C  
ANISOU 1290  CB  LEU A 214    16702  25614  16753   2309  -1706  -3995       C  
ATOM   1291  CG  LEU A 214      31.253 -36.155 160.896  1.00159.76           C  
ANISOU 1291  CG  LEU A 214    16951  26117  17635   2162  -1625  -4240       C  
ATOM   1292  CD1 LEU A 214      30.127 -36.905 160.224  1.00162.09           C  
ANISOU 1292  CD1 LEU A 214    16903  26636  18050   2299  -1727  -4737       C  
ATOM   1293  CD2 LEU A 214      31.985 -37.050 161.882  1.00159.90           C  
ANISOU 1293  CD2 LEU A 214    16896  25928  17930   1807  -1357  -4090       C  
ATOM   1294  N   PRO A 215      35.028 -34.343 160.835  1.00150.24           N  
ANISOU 1294  N   PRO A 215    16691  24487  15906   1976  -1431  -3039       N  
ATOM   1295  CA  PRO A 215      36.068 -34.106 161.852  1.00147.43           C  
ANISOU 1295  CA  PRO A 215    16483  23894  15640   1729  -1265  -2706       C  
ATOM   1296  C   PRO A 215      36.550 -32.651 161.908  1.00150.28           C  
ANISOU 1296  C   PRO A 215    17187  24150  15764   1832  -1300  -2408       C  
ATOM   1297  O   PRO A 215      37.288 -32.300 162.823  1.00148.47           O  
ANISOU 1297  O   PRO A 215    17072  23733  15608   1652  -1186  -2163       O  
ATOM   1298  CB  PRO A 215      37.186 -35.069 161.446  1.00148.32           C  
ANISOU 1298  CB  PRO A 215    16562  23964  15828   1550  -1127  -2626       C  
ATOM   1299  CG  PRO A 215      37.047 -35.207 159.982  1.00154.67           C  
ANISOU 1299  CG  PRO A 215    17376  24953  16436   1763  -1238  -2773       C  
ATOM   1300  CD  PRO A 215      35.597 -35.010 159.640  1.00152.30           C  
ANISOU 1300  CD  PRO A 215    16943  24849  16074   2017  -1427  -3088       C  
ATOM   1301  N   GLN A 216      36.151 -31.809 160.932  1.00147.80           N  
ANISOU 1301  N   GLN A 216    17042  23952  15165   2130  -1449  -2437       N  
ATOM   1302  CA  GLN A 216      36.525 -30.391 160.895  1.00147.17           C  
ANISOU 1302  CA  GLN A 216    17301  23770  14848   2259  -1465  -2173       C  
ATOM   1303  C   GLN A 216      35.754 -29.612 161.956  1.00149.26           C  
ANISOU 1303  C   GLN A 216    17568  23976  15168   2272  -1512  -2161       C  
ATOM   1304  O   GLN A 216      36.304 -28.680 162.544  1.00147.88           O  
ANISOU 1304  O   GLN A 216    17610  23637  14941   2216  -1441  -1900       O  
ATOM   1305  CB  GLN A 216      36.295 -29.783 159.499  1.00150.77           C  
ANISOU 1305  CB  GLN A 216    17957  24363  14965   2604  -1595  -2213       C  
ATOM   1306  CG  GLN A 216      37.580 -29.549 158.708  1.00160.64           C  
ANISOU 1306  CG  GLN A 216    19474  25517  16046   2597  -1476  -1973       C  
ATOM   1307  CD  GLN A 216      37.315 -28.929 157.357  1.00175.77           C  
ANISOU 1307  CD  GLN A 216    21627  27553  17605   2966  -1589  -2001       C  
ATOM   1308  OE1 GLN A 216      37.153 -29.620 156.345  1.00170.79           O  
ANISOU 1308  OE1 GLN A 216    20923  27086  16884   3099  -1663  -2182       O  
ATOM   1309  NE2 GLN A 216      37.273 -27.608 157.312  1.00166.85           N  
ANISOU 1309  NE2 GLN A 216    20800  26339  16254   3150  -1598  -1823       N  
ATOM   1310  N   SER A 217      34.491 -30.000 162.214  1.00145.52           N  
ANISOU 1310  N   SER A 217    16844  23631  14815   2339  -1621  -2456       N  
ATOM   1311  CA  SER A 217      33.671 -29.325 163.214  1.00144.71           C  
ANISOU 1311  CA  SER A 217    16722  23479  14783   2352  -1665  -2476       C  
ATOM   1312  C   SER A 217      33.648 -30.017 164.572  1.00145.44           C  
ANISOU 1312  C   SER A 217    16616  23442  15200   2054  -1527  -2492       C  
ATOM   1313  O   SER A 217      33.646 -29.326 165.589  1.00143.97           O  
ANISOU 1313  O   SER A 217    16522  23118  15060   1973  -1485  -2339       O  
ATOM   1314  CB  SER A 217      32.255 -29.099 162.703  1.00150.60           C  
ANISOU 1314  CB  SER A 217    17351  24428  15444   2641  -1871  -2788       C  
ATOM   1315  OG  SER A 217      31.544 -28.264 163.604  1.00159.39           O  
ANISOU 1315  OG  SER A 217    18485  25479  16597   2669  -1913  -2778       O  
ATOM   1316  N   PHE A 218      33.615 -31.362 164.597  1.00140.59           N  
ANISOU 1316  N   PHE A 218    15743  22868  14806   1903  -1448  -2677       N  
ATOM   1317  CA  PHE A 218      33.558 -32.137 165.842  1.00138.31           C  
ANISOU 1317  CA  PHE A 218    15277  22452  14822   1642  -1292  -2707       C  
ATOM   1318  C   PHE A 218      34.935 -32.454 166.442  1.00139.21           C  
ANISOU 1318  C   PHE A 218    15500  22385  15010   1394  -1117  -2419       C  
ATOM   1319  O   PHE A 218      35.028 -32.830 167.611  1.00137.23           O  
ANISOU 1319  O   PHE A 218    15187  21995  14957   1203   -990  -2367       O  
ATOM   1320  CB  PHE A 218      32.720 -33.414 165.655  1.00140.80           C  
ANISOU 1320  CB  PHE A 218    15253  22883  15359   1612  -1267  -3078       C  
ATOM   1321  CG  PHE A 218      31.259 -33.134 165.393  1.00143.99           C  
ANISOU 1321  CG  PHE A 218    15500  23443  15766   1823  -1424  -3406       C  
ATOM   1322  CD1 PHE A 218      30.373 -32.936 166.444  1.00146.72           C  
ANISOU 1322  CD1 PHE A 218    15745  23712  16288   1772  -1392  -3512       C  
ATOM   1323  CD2 PHE A 218      30.771 -33.055 164.095  1.00148.03           C  
ANISOU 1323  CD2 PHE A 218    15967  24177  16100   2086  -1609  -3621       C  
ATOM   1324  CE1 PHE A 218      29.025 -32.655 166.201  1.00149.42           C  
ANISOU 1324  CE1 PHE A 218    15929  24196  16649   1968  -1540  -3836       C  
ATOM   1325  CE2 PHE A 218      29.423 -32.780 163.853  1.00152.72           C  
ANISOU 1325  CE2 PHE A 218    16403  24926  16697   2302  -1775  -3950       C  
ATOM   1326  CZ  PHE A 218      28.558 -32.585 164.909  1.00150.58           C  
ANISOU 1326  CZ  PHE A 218    16017  24575  16624   2235  -1738  -4061       C  
ATOM   1327  N   GLY A 219      35.981 -32.285 165.649  1.00135.42           N  
ANISOU 1327  N   GLY A 219    15185  21903  14366   1413  -1112  -2242       N  
ATOM   1328  CA  GLY A 219      37.346 -32.534 166.085  1.00133.84           C  
ANISOU 1328  CA  GLY A 219    15084  21544  14225   1200   -965  -1989       C  
ATOM   1329  C   GLY A 219      38.186 -31.279 166.205  1.00138.58           C  
ANISOU 1329  C   GLY A 219    15977  22022  14656   1220   -964  -1693       C  
ATOM   1330  O   GLY A 219      39.358 -31.360 166.582  1.00137.36           O  
ANISOU 1330  O   GLY A 219    15906  21731  14554   1052   -852  -1493       O  
ATOM   1331  N   PHE A 220      37.608 -30.111 165.874  1.00136.71           N  
ANISOU 1331  N   PHE A 220    15894  21830  14221   1431  -1081  -1676       N  
ATOM   1332  CA  PHE A 220      38.319 -28.838 165.980  1.00136.48           C  
ANISOU 1332  CA  PHE A 220    16148  21672  14035   1460  -1057  -1410       C  
ATOM   1333  C   PHE A 220      37.477 -27.778 166.665  1.00139.85           C  
ANISOU 1333  C   PHE A 220    16648  22071  14416   1559  -1131  -1395       C  
ATOM   1334  O   PHE A 220      37.894 -27.271 167.702  1.00138.06           O  
ANISOU 1334  O   PHE A 220    16501  21694  14262   1426  -1060  -1230       O  
ATOM   1335  CB  PHE A 220      38.869 -28.352 164.619  1.00139.83           C  
ANISOU 1335  CB  PHE A 220    16782  22138  14210   1629  -1073  -1328       C  
ATOM   1336  CG  PHE A 220      39.491 -26.969 164.630  1.00141.83           C  
ANISOU 1336  CG  PHE A 220    17341  22251  14299   1686  -1021  -1078       C  
ATOM   1337  CD1 PHE A 220      40.748 -26.756 165.188  1.00143.85           C  
ANISOU 1337  CD1 PHE A 220    17693  22321  14641   1480   -872   -865       C  
ATOM   1338  CD2 PHE A 220      38.826 -25.885 164.068  1.00145.80           C  
ANISOU 1338  CD2 PHE A 220    18030  22802  14564   1954  -1114  -1071       C  
ATOM   1339  CE1 PHE A 220      41.322 -25.478 165.198  1.00145.12           C  
ANISOU 1339  CE1 PHE A 220    18121  22341  14678   1522   -798   -661       C  
ATOM   1340  CE2 PHE A 220      39.400 -24.608 164.079  1.00148.97           C  
ANISOU 1340  CE2 PHE A 220    18722  23055  14826   2004  -1031   -842       C  
ATOM   1341  CZ  PHE A 220      40.644 -24.414 164.643  1.00145.80           C  
ANISOU 1341  CZ  PHE A 220    18400  22462  14534   1778   -865   -644       C  
ATOM   1342  N   ILE A 221      36.294 -27.462 166.103  1.00137.44           N  
ANISOU 1342  N   ILE A 221    16311  21916  13994   1796  -1278  -1580       N  
ATOM   1343  CA  ILE A 221      35.394 -26.426 166.613  1.00137.39           C  
ANISOU 1343  CA  ILE A 221    16373  21903  13926   1926  -1366  -1589       C  
ATOM   1344  C   ILE A 221      34.702 -26.849 167.937  1.00139.46           C  
ANISOU 1344  C   ILE A 221    16434  22115  14441   1768  -1339  -1696       C  
ATOM   1345  O   ILE A 221      34.697 -26.049 168.872  1.00138.19           O  
ANISOU 1345  O   ILE A 221    16374  21832  14299   1714  -1312  -1559       O  
ATOM   1346  CB  ILE A 221      34.408 -25.957 165.506  1.00142.70           C  
ANISOU 1346  CB  ILE A 221    17081  22761  14378   2259  -1543  -1764       C  
ATOM   1347  CG1 ILE A 221      35.192 -25.298 164.346  1.00144.27           C  
ANISOU 1347  CG1 ILE A 221    17566  22958  14292   2430  -1535  -1594       C  
ATOM   1348  CG2 ILE A 221      33.354 -24.980 166.049  1.00144.10           C  
ANISOU 1348  CG2 ILE A 221    17289  22946  14514   2401  -1647  -1816       C  
ATOM   1349  CD1 ILE A 221      34.704 -25.643 162.935  1.00155.43           C  
ANISOU 1349  CD1 ILE A 221    18958  24580  15518   2705  -1674  -1797       C  
ATOM   1350  N   VAL A 222      34.163 -28.087 168.029  1.00135.38           N  
ANISOU 1350  N   VAL A 222    15643  21677  14119   1691  -1326  -1939       N  
ATOM   1351  CA  VAL A 222      33.485 -28.599 169.235  1.00134.25           C  
ANISOU 1351  CA  VAL A 222    15312  21469  14228   1543  -1261  -2061       C  
ATOM   1352  C   VAL A 222      34.421 -28.564 170.485  1.00136.06           C  
ANISOU 1352  C   VAL A 222    15635  21492  14572   1305  -1111  -1812       C  
ATOM   1353  O   VAL A 222      34.001 -27.959 171.476  1.00134.83           O  
ANISOU 1353  O   VAL A 222    15519  21245  14467   1275  -1103  -1766       O  
ATOM   1354  CB  VAL A 222      32.800 -29.980 169.014  1.00138.69           C  
ANISOU 1354  CB  VAL A 222    15569  22135  14990   1501  -1232  -2376       C  
ATOM   1355  CG1 VAL A 222      32.470 -30.677 170.335  1.00137.33           C  
ANISOU 1355  CG1 VAL A 222    15247  21835  15098   1298  -1084  -2443       C  
ATOM   1356  CG2 VAL A 222      31.540 -29.828 168.169  1.00140.73           C  
ANISOU 1356  CG2 VAL A 222    15701  22594  15177   1750  -1405  -2680       C  
ATOM   1357  N   PRO A 223      35.666 -29.130 170.485  1.00131.71           N  
ANISOU 1357  N   PRO A 223    15124  20866  14054   1150  -1003  -1657       N  
ATOM   1358  CA  PRO A 223      36.511 -29.019 171.692  1.00129.70           C  
ANISOU 1358  CA  PRO A 223    14956  20431  13893    960   -889  -1446       C  
ATOM   1359  C   PRO A 223      36.999 -27.592 171.945  1.00132.59           C  
ANISOU 1359  C   PRO A 223    15563  20708  14108   1001   -922  -1219       C  
ATOM   1360  O   PRO A 223      37.178 -27.219 173.104  1.00131.40           O  
ANISOU 1360  O   PRO A 223    15467  20430  14029    901   -874  -1108       O  
ATOM   1361  CB  PRO A 223      37.683 -29.970 171.417  1.00130.75           C  
ANISOU 1361  CB  PRO A 223    15058  20535  14086    822   -790  -1373       C  
ATOM   1362  CG  PRO A 223      37.341 -30.700 170.179  1.00136.47           C  
ANISOU 1362  CG  PRO A 223    15652  21419  14782    914   -833  -1564       C  
ATOM   1363  CD  PRO A 223      36.373 -29.869 169.420  1.00133.60           C  
ANISOU 1363  CD  PRO A 223    15334  21181  14248   1146   -984  -1671       C  
ATOM   1364  N   LEU A 224      37.199 -26.800 170.864  1.00129.25           N  
ANISOU 1364  N   LEU A 224    15291  20344  13475   1158   -991  -1157       N  
ATOM   1365  CA  LEU A 224      37.640 -25.399 170.907  1.00128.76           C  
ANISOU 1365  CA  LEU A 224    15471  20194  13258   1220   -997   -956       C  
ATOM   1366  C   LEU A 224      36.580 -24.529 171.599  1.00132.46           C  
ANISOU 1366  C   LEU A 224    15967  20652  13710   1310  -1068   -990       C  
ATOM   1367  O   LEU A 224      36.929 -23.705 172.451  1.00131.22           O  
ANISOU 1367  O   LEU A 224    15934  20367  13556   1244  -1026   -831       O  
ATOM   1368  CB  LEU A 224      37.918 -24.900 169.470  1.00129.99           C  
ANISOU 1368  CB  LEU A 224    15786  20416  13187   1398  -1031   -911       C  
ATOM   1369  CG  LEU A 224      38.707 -23.600 169.211  1.00134.81           C  
ANISOU 1369  CG  LEU A 224    16676  20910  13636   1451   -973   -686       C  
ATOM   1370  CD1 LEU A 224      37.789 -22.449 168.856  1.00136.29           C  
ANISOU 1370  CD1 LEU A 224    17005  21139  13639   1688  -1065   -694       C  
ATOM   1371  CD2 LEU A 224      39.726 -23.271 170.312  1.00135.48           C  
ANISOU 1371  CD2 LEU A 224    16813  20816  13850   1233   -855   -512       C  
ATOM   1372  N   LEU A 225      35.289 -24.748 171.247  1.00129.49           N  
ANISOU 1372  N   LEU A 225    15458  20411  13330   1456  -1175  -1216       N  
ATOM   1373  CA  LEU A 225      34.119 -24.060 171.801  1.00129.40           C  
ANISOU 1373  CA  LEU A 225    15434  20409  13322   1554  -1253  -1300       C  
ATOM   1374  C   LEU A 225      34.059 -24.283 173.314  1.00131.14           C  
ANISOU 1374  C   LEU A 225    15584  20495  13747   1354  -1164  -1267       C  
ATOM   1375  O   LEU A 225      33.977 -23.315 174.072  1.00130.32           O  
ANISOU 1375  O   LEU A 225    15598  20296  13620   1346  -1162  -1150       O  
ATOM   1376  CB  LEU A 225      32.839 -24.587 171.135  1.00130.84           C  
ANISOU 1376  CB  LEU A 225    15424  20771  13518   1719  -1373  -1606       C  
ATOM   1377  CG  LEU A 225      31.778 -23.554 170.807  1.00136.81           C  
ANISOU 1377  CG  LEU A 225    16245  21609  14128   1966  -1519  -1692       C  
ATOM   1378  CD1 LEU A 225      31.948 -23.031 169.389  1.00138.41           C  
ANISOU 1378  CD1 LEU A 225    16611  21924  14053   2217  -1615  -1661       C  
ATOM   1379  CD2 LEU A 225      30.395 -24.143 170.975  1.00140.03           C  
ANISOU 1379  CD2 LEU A 225    16390  22127  14689   2025  -1597  -2023       C  
ATOM   1380  N   ILE A 226      34.170 -25.561 173.740  1.00126.24           N  
ANISOU 1380  N   ILE A 226    14787  19859  13319   1197  -1077  -1362       N  
ATOM   1381  CA  ILE A 226      34.194 -26.003 175.136  1.00124.35           C  
ANISOU 1381  CA  ILE A 226    14491  19486  13271   1017   -967  -1337       C  
ATOM   1382  C   ILE A 226      35.390 -25.361 175.858  1.00127.86           C  
ANISOU 1382  C   ILE A 226    15119  19787  13674    904   -908  -1068       C  
ATOM   1383  O   ILE A 226      35.229 -24.884 176.980  1.00127.02           O  
ANISOU 1383  O   ILE A 226    15067  19574  13619    845   -880   -999       O  
ATOM   1384  CB  ILE A 226      34.191 -27.560 175.198  1.00126.68           C  
ANISOU 1384  CB  ILE A 226    14586  19796  13752    903   -866  -1489       C  
ATOM   1385  CG1 ILE A 226      32.805 -28.117 174.810  1.00127.95           C  
ANISOU 1385  CG1 ILE A 226    14533  20072  14009    997   -906  -1803       C  
ATOM   1386  CG2 ILE A 226      34.645 -28.099 176.565  1.00126.01           C  
ANISOU 1386  CG2 ILE A 226    14505  19549  13825    720   -723  -1398       C  
ATOM   1387  CD1 ILE A 226      32.809 -29.514 174.221  1.00134.35           C  
ANISOU 1387  CD1 ILE A 226    15143  20957  14947    947   -836  -1989       C  
ATOM   1388  N   MET A 227      36.561 -25.308 175.193  1.00124.95           N  
ANISOU 1388  N   MET A 227    14843  19417  13215    882   -890   -932       N  
ATOM   1389  CA  MET A 227      37.782 -24.708 175.731  1.00124.30           C  
ANISOU 1389  CA  MET A 227    14914  19208  13107    779   -834   -712       C  
ATOM   1390  C   MET A 227      37.641 -23.218 175.970  1.00130.35           C  
ANISOU 1390  C   MET A 227    15851  19919  13760    854   -873   -597       C  
ATOM   1391  O   MET A 227      38.052 -22.745 177.024  1.00129.15           O  
ANISOU 1391  O   MET A 227    15762  19651  13657    759   -833   -490       O  
ATOM   1392  CB  MET A 227      38.977 -24.978 174.820  1.00126.48           C  
ANISOU 1392  CB  MET A 227    15235  19495  13327    747   -796   -628       C  
ATOM   1393  CG  MET A 227      39.693 -26.251 175.150  1.00129.12           C  
ANISOU 1393  CG  MET A 227    15455  19797  13806    594   -716   -638       C  
ATOM   1394  SD  MET A 227      41.184 -26.429 174.158  1.00133.23           S  
ANISOU 1394  SD  MET A 227    16029  20316  14275    545   -666   -541       S  
ATOM   1395  CE  MET A 227      40.531 -27.260 172.788  1.00130.99           C  
ANISOU 1395  CE  MET A 227    15629  20197  13943    658   -710   -717       C  
ATOM   1396  N   LEU A 228      37.054 -22.480 175.008  1.00129.84           N  
ANISOU 1396  N   LEU A 228    15862  19934  13537   1036   -948   -627       N  
ATOM   1397  CA  LEU A 228      36.856 -21.034 175.128  1.00130.85           C  
ANISOU 1397  CA  LEU A 228    16165  20007  13544   1130   -972   -519       C  
ATOM   1398  C   LEU A 228      35.896 -20.677 176.260  1.00136.00           C  
ANISOU 1398  C   LEU A 228    16776  20620  14278   1116  -1003   -568       C  
ATOM   1399  O   LEU A 228      36.183 -19.739 177.005  1.00135.13           O  
ANISOU 1399  O   LEU A 228    16785  20402  14157   1073   -970   -438       O  
ATOM   1400  CB  LEU A 228      36.401 -20.394 173.799  1.00132.54           C  
ANISOU 1400  CB  LEU A 228    16488  20320  13550   1363  -1044   -544       C  
ATOM   1401  CG  LEU A 228      37.412 -20.335 172.639  1.00137.66           C  
ANISOU 1401  CG  LEU A 228    17264  20970  14071   1406   -989   -448       C  
ATOM   1402  CD1 LEU A 228      36.747 -19.823 171.387  1.00139.54           C  
ANISOU 1402  CD1 LEU A 228    17614  21318  14089   1675  -1071   -499       C  
ATOM   1403  CD2 LEU A 228      38.610 -19.445 172.966  1.00139.73           C  
ANISOU 1403  CD2 LEU A 228    17703  21065  14323   1299   -863   -238       C  
ATOM   1404  N   PHE A 229      34.780 -21.432 176.413  1.00134.43           N  
ANISOU 1404  N   PHE A 229    16401  20499  14176   1144  -1050   -767       N  
ATOM   1405  CA  PHE A 229      33.810 -21.187 177.487  1.00135.02           C  
ANISOU 1405  CA  PHE A 229    16426  20526  14351   1124  -1060   -837       C  
ATOM   1406  C   PHE A 229      34.437 -21.474 178.852  1.00138.72           C  
ANISOU 1406  C   PHE A 229    16901  20852  14954    929   -959   -736       C  
ATOM   1407  O   PHE A 229      34.474 -20.581 179.699  1.00138.02           O  
ANISOU 1407  O   PHE A 229    16914  20668  14859    899   -948   -634       O  
ATOM   1408  CB  PHE A 229      32.498 -21.987 177.300  1.00137.97           C  
ANISOU 1408  CB  PHE A 229    16593  21002  14827   1190  -1107  -1105       C  
ATOM   1409  CG  PHE A 229      31.609 -21.592 176.136  1.00141.74           C  
ANISOU 1409  CG  PHE A 229    17048  21633  15175   1421  -1242  -1253       C  
ATOM   1410  CD1 PHE A 229      31.169 -20.279 175.984  1.00145.91           C  
ANISOU 1410  CD1 PHE A 229    17720  22164  15556   1574  -1322  -1190       C  
ATOM   1411  CD2 PHE A 229      31.147 -22.549 175.237  1.00145.00           C  
ANISOU 1411  CD2 PHE A 229    17287  22189  15618   1498  -1291  -1475       C  
ATOM   1412  CE1 PHE A 229      30.339 -19.919 174.914  1.00148.46           C  
ANISOU 1412  CE1 PHE A 229    18034  22635  15739   1822  -1460  -1333       C  
ATOM   1413  CE2 PHE A 229      30.317 -22.188 174.169  1.00149.52           C  
ANISOU 1413  CE2 PHE A 229    17836  22919  16058   1740  -1437  -1634       C  
ATOM   1414  CZ  PHE A 229      29.915 -20.877 174.018  1.00148.40           C  
ANISOU 1414  CZ  PHE A 229    17854  22781  15750   1910  -1526  -1560       C  
ATOM   1415  N   CYS A 230      34.994 -22.691 179.032  1.00135.27           N  
ANISOU 1415  N   CYS A 230    16367  20402  14626    811   -886   -762       N  
ATOM   1416  CA  CYS A 230      35.619 -23.130 180.278  1.00134.18           C  
ANISOU 1416  CA  CYS A 230    16240  20141  14601    657   -794   -680       C  
ATOM   1417  C   CYS A 230      36.845 -22.317 180.671  1.00138.54           C  
ANISOU 1417  C   CYS A 230    16945  20606  15087    594   -781   -478       C  
ATOM   1418  O   CYS A 230      36.846 -21.780 181.772  1.00137.92           O  
ANISOU 1418  O   CYS A 230    16936  20434  15034    549   -766   -410       O  
ATOM   1419  CB  CYS A 230      35.923 -24.622 180.253  1.00134.06           C  
ANISOU 1419  CB  CYS A 230    16094  20136  14705    574   -715   -762       C  
ATOM   1420  SG  CYS A 230      34.453 -25.678 180.287  1.00138.58           S  
ANISOU 1420  SG  CYS A 230    16468  20755  15432    600   -671  -1030       S  
ATOM   1421  N   TYR A 231      37.867 -22.200 179.795  1.00136.00           N  
ANISOU 1421  N   TYR A 231    16673  20311  14689    593   -780   -396       N  
ATOM   1422  CA  TYR A 231      39.081 -21.434 180.118  1.00136.01           C  
ANISOU 1422  CA  TYR A 231    16797  20223  14656    526   -751   -237       C  
ATOM   1423  C   TYR A 231      38.836 -19.939 180.314  1.00140.96           C  
ANISOU 1423  C   TYR A 231    17560  20799  15198    583   -771   -157       C  
ATOM   1424  O   TYR A 231      39.493 -19.324 181.159  1.00139.68           O  
ANISOU 1424  O   TYR A 231    17468  20540  15063    507   -741    -67       O  
ATOM   1425  CB  TYR A 231      40.216 -21.665 179.111  1.00137.64           C  
ANISOU 1425  CB  TYR A 231    17025  20453  14821    506   -720   -186       C  
ATOM   1426  CG  TYR A 231      40.887 -23.017 179.226  1.00139.35           C  
ANISOU 1426  CG  TYR A 231    17128  20678  15140    408   -680   -221       C  
ATOM   1427  CD1 TYR A 231      41.491 -23.421 180.416  1.00140.75           C  
ANISOU 1427  CD1 TYR A 231    17289  20775  15415    304   -649   -185       C  
ATOM   1428  CD2 TYR A 231      40.985 -23.864 178.127  1.00140.56           C  
ANISOU 1428  CD2 TYR A 231    17201  20921  15285    431   -674   -291       C  
ATOM   1429  CE1 TYR A 231      42.123 -24.659 180.523  1.00141.46           C  
ANISOU 1429  CE1 TYR A 231    17289  20869  15589    233   -609   -211       C  
ATOM   1430  CE2 TYR A 231      41.633 -25.094 178.216  1.00141.09           C  
ANISOU 1430  CE2 TYR A 231    17166  20990  15450    340   -627   -318       C  
ATOM   1431  CZ  TYR A 231      42.196 -25.491 179.418  1.00148.43           C  
ANISOU 1431  CZ  TYR A 231    18087  21835  16475    244   -592   -275       C  
ATOM   1432  OH  TYR A 231      42.839 -26.701 179.508  1.00149.61           O  
ANISOU 1432  OH  TYR A 231    18151  21984  16712    173   -543   -297       O  
ATOM   1433  N   GLY A 232      37.894 -19.386 179.546  1.00139.36           N  
ANISOU 1433  N   GLY A 232    17391  20664  14896    726   -823   -202       N  
ATOM   1434  CA  GLY A 232      37.515 -17.979 179.606  1.00140.06           C  
ANISOU 1434  CA  GLY A 232    17615  20710  14891    808   -838   -132       C  
ATOM   1435  C   GLY A 232      36.909 -17.594 180.940  1.00144.09           C  
ANISOU 1435  C   GLY A 232    18120  21150  15477    759   -846   -136       C  
ATOM   1436  O   GLY A 232      37.407 -16.678 181.605  1.00143.64           O  
ANISOU 1436  O   GLY A 232    18162  20996  15417    706   -810    -31       O  
ATOM   1437  N   PHE A 233      35.856 -18.329 181.358  1.00140.41           N  
ANISOU 1437  N   PHE A 233    17532  20724  15093    767   -879   -270       N  
ATOM   1438  CA  PHE A 233      35.158 -18.094 182.620  1.00139.73           C  
ANISOU 1438  CA  PHE A 233    17439  20564  15088    724   -872   -290       C  
ATOM   1439  C   PHE A 233      35.970 -18.520 183.856  1.00142.64           C  
ANISOU 1439  C   PHE A 233    17815  20831  15550    577   -809   -224       C  
ATOM   1440  O   PHE A 233      35.681 -18.034 184.951  1.00142.24           O  
ANISOU 1440  O   PHE A 233    17813  20699  15534    541   -796   -195       O  
ATOM   1441  CB  PHE A 233      33.751 -18.711 182.607  1.00142.02           C  
ANISOU 1441  CB  PHE A 233    17600  20911  15449    785   -902   -475       C  
ATOM   1442  CG  PHE A 233      32.812 -18.056 181.613  1.00144.84           C  
ANISOU 1442  CG  PHE A 233    17959  21367  15706    959   -992   -556       C  
ATOM   1443  CD1 PHE A 233      32.693 -16.670 181.547  1.00147.24           C  
ANISOU 1443  CD1 PHE A 233    18406  21643  15896   1043  -1025   -457       C  
ATOM   1444  CD2 PHE A 233      32.052 -18.824 180.739  1.00148.89           C  
ANISOU 1444  CD2 PHE A 233    18331  22003  16237   1054  -1044   -744       C  
ATOM   1445  CE1 PHE A 233      31.837 -16.067 180.621  1.00151.22           C  
ANISOU 1445  CE1 PHE A 233    18930  22240  16286   1236  -1115   -530       C  
ATOM   1446  CE2 PHE A 233      31.196 -18.219 179.813  1.00150.97           C  
ANISOU 1446  CE2 PHE A 233    18599  22373  16391   1247  -1150   -836       C  
ATOM   1447  CZ  PHE A 233      31.092 -16.845 179.764  1.00150.25           C  
ANISOU 1447  CZ  PHE A 233    18668  22251  16168   1345  -1187   -722       C  
ATOM   1448  N   THR A 234      37.002 -19.378 183.690  1.00138.46           N  
ANISOU 1448  N   THR A 234    17248  20309  15053    506   -775   -201       N  
ATOM   1449  CA  THR A 234      37.884 -19.748 184.804  1.00137.33           C  
ANISOU 1449  CA  THR A 234    17123  20082  14976    400   -733   -142       C  
ATOM   1450  C   THR A 234      38.880 -18.617 185.009  1.00140.45           C  
ANISOU 1450  C   THR A 234    17624  20420  15322    366   -737    -24       C  
ATOM   1451  O   THR A 234      39.148 -18.251 186.151  1.00139.61           O  
ANISOU 1451  O   THR A 234    17564  20236  15244    317   -732     16       O  
ATOM   1452  CB  THR A 234      38.603 -21.086 184.593  1.00145.54           C  
ANISOU 1452  CB  THR A 234    18079  21148  16071    348   -697   -170       C  
ATOM   1453  OG1 THR A 234      39.266 -21.090 183.334  1.00145.93           O  
ANISOU 1453  OG1 THR A 234    18116  21267  16065    367   -710   -152       O  
ATOM   1454  CG2 THR A 234      37.683 -22.275 184.728  1.00144.22           C  
ANISOU 1454  CG2 THR A 234    17808  20999  15990    356   -653   -294       C  
ATOM   1455  N   LEU A 235      39.399 -18.041 183.895  1.00137.13           N  
ANISOU 1455  N   LEU A 235    17246  20031  14828    399   -735     21       N  
ATOM   1456  CA  LEU A 235      40.337 -16.915 183.903  1.00137.00           C  
ANISOU 1456  CA  LEU A 235    17325  19946  14781    366   -702    113       C  
ATOM   1457  C   LEU A 235      39.699 -15.698 184.561  1.00140.67           C  
ANISOU 1457  C   LEU A 235    17876  20353  15219    394   -707    149       C  
ATOM   1458  O   LEU A 235      40.362 -15.003 185.333  1.00140.20           O  
ANISOU 1458  O   LEU A 235    17862  20215  15192    328   -683    194       O  
ATOM   1459  CB  LEU A 235      40.776 -16.561 182.476  1.00137.74           C  
ANISOU 1459  CB  LEU A 235    17471  20070  14794    420   -665    147       C  
ATOM   1460  CG  LEU A 235      42.227 -16.859 182.122  1.00142.51           C  
ANISOU 1460  CG  LEU A 235    18063  20643  15440    336   -607    175       C  
ATOM   1461  CD1 LEU A 235      42.413 -16.899 180.621  1.00143.58           C  
ANISOU 1461  CD1 LEU A 235    18243  20819  15491    405   -566    191       C  
ATOM   1462  CD2 LEU A 235      43.180 -15.841 182.745  1.00144.87           C  
ANISOU 1462  CD2 LEU A 235    18423  20834  15786    259   -550    225       C  
ATOM   1463  N   ARG A 236      38.397 -15.472 184.270  1.00137.16           N  
ANISOU 1463  N   ARG A 236    17439  19951  14725    493   -744    110       N  
ATOM   1464  CA  ARG A 236      37.564 -14.397 184.805  1.00137.14           C  
ANISOU 1464  CA  ARG A 236    17508  19903  14695    536   -755    130       C  
ATOM   1465  C   ARG A 236      37.581 -14.420 186.339  1.00140.47           C  
ANISOU 1465  C   ARG A 236    17922  20249  15202    445   -753    132       C  
ATOM   1466  O   ARG A 236      37.913 -13.403 186.951  1.00140.10           O  
ANISOU 1466  O   ARG A 236    17952  20129  15153    411   -730    192       O  
ATOM   1467  CB  ARG A 236      36.133 -14.501 184.227  1.00138.15           C  
ANISOU 1467  CB  ARG A 236    17600  20109  14779    662   -812     43       C  
ATOM   1468  CG  ARG A 236      35.071 -13.667 184.942  1.00150.26           C  
ANISOU 1468  CG  ARG A 236    19171  21600  16319    698   -834     30       C  
ATOM   1469  CD  ARG A 236      33.878 -13.343 184.061  1.00162.80           C  
ANISOU 1469  CD  ARG A 236    20760  23268  17830    860   -895    -40       C  
ATOM   1470  NE  ARG A 236      33.986 -12.000 183.488  1.00174.14           N  
ANISOU 1470  NE  ARG A 236    22346  24676  19143    954   -877     62       N  
ATOM   1471  CZ  ARG A 236      32.951 -11.245 183.129  1.00190.47           C  
ANISOU 1471  CZ  ARG A 236    24465  26775  21132   1102   -925     35       C  
ATOM   1472  NH1 ARG A 236      31.709 -11.689 183.280  1.00178.75           N  
ANISOU 1472  NH1 ARG A 236    22869  25355  19692   1167  -1005   -112       N  
ATOM   1473  NH2 ARG A 236      33.151 -10.036 182.619  1.00178.01           N  
ANISOU 1473  NH2 ARG A 236    23048  25154  19436   1192   -882    145       N  
ATOM   1474  N   THR A 237      37.285 -15.588 186.949  1.00136.70           N  
ANISOU 1474  N   THR A 237    17362  19782  14796    410   -763     63       N  
ATOM   1475  CA  THR A 237      37.287 -15.743 188.409  1.00136.12           C  
ANISOU 1475  CA  THR A 237    17304  19632  14784    348   -752     64       C  
ATOM   1476  C   THR A 237      38.703 -15.879 188.974  1.00140.16           C  
ANISOU 1476  C   THR A 237    17830  20107  15316    274   -745    110       C  
ATOM   1477  O   THR A 237      38.885 -15.698 190.180  1.00139.51           O  
ANISOU 1477  O   THR A 237    17791  19962  15256    243   -749    122       O  
ATOM   1478  CB  THR A 237      36.352 -16.866 188.883  1.00142.84           C  
ANISOU 1478  CB  THR A 237    18089  20482  15701    358   -731    -29       C  
ATOM   1479  OG1 THR A 237      36.705 -18.093 188.250  1.00143.04           O  
ANISOU 1479  OG1 THR A 237    18030  20566  15753    352   -716    -75       O  
ATOM   1480  CG2 THR A 237      34.882 -16.542 188.658  1.00141.41           C  
ANISOU 1480  CG2 THR A 237    17884  20317  15527    425   -742   -106       C  
ATOM   1481  N   LEU A 238      39.655 -16.252 188.134  1.00137.46           N  
ANISOU 1481  N   LEU A 238    17455  19806  14968    255   -739    124       N  
ATOM   1482  CA  LEU A 238      41.026 -16.367 188.582  1.00137.86           C  
ANISOU 1482  CA  LEU A 238    17498  19829  15053    190   -741    140       C  
ATOM   1483  C   LEU A 238      41.543 -14.986 188.909  1.00144.03           C  
ANISOU 1483  C   LEU A 238    18338  20553  15832    157   -725    178       C  
ATOM   1484  O   LEU A 238      42.244 -14.779 189.889  1.00143.80           O  
ANISOU 1484  O   LEU A 238    18304  20489  15845    112   -743    161       O  
ATOM   1485  CB  LEU A 238      41.898 -17.028 187.526  1.00137.92           C  
ANISOU 1485  CB  LEU A 238    17437  19889  15077    170   -729    127       C  
ATOM   1486  CG  LEU A 238      41.805 -18.552 187.495  1.00142.26           C  
ANISOU 1486  CG  LEU A 238    17920  20468  15664    170   -735     83       C  
ATOM   1487  CD1 LEU A 238      43.018 -19.122 186.783  1.00142.59           C  
ANISOU 1487  CD1 LEU A 238    17896  20552  15729    139   -724     75       C  
ATOM   1488  CD2 LEU A 238      41.720 -19.115 188.903  1.00144.02           C  
ANISOU 1488  CD2 LEU A 238    18173  20637  15910    165   -756     76       C  
ATOM   1489  N   PHE A 239      41.177 -14.039 188.061  1.00142.45           N  
ANISOU 1489  N   PHE A 239    18195  20343  15585    189   -687    217       N  
ATOM   1490  CA  PHE A 239      41.582 -12.651 188.205  1.00143.58           C  
ANISOU 1490  CA  PHE A 239    18405  20414  15734    160   -635    252       C  
ATOM   1491  C   PHE A 239      41.054 -11.993 189.469  1.00148.33           C  
ANISOU 1491  C   PHE A 239    19043  20964  16352    145   -661    249       C  
ATOM   1492  O   PHE A 239      41.735 -11.183 190.092  1.00148.55           O  
ANISOU 1492  O   PHE A 239    19088  20932  16421     92   -634    244       O  
ATOM   1493  CB  PHE A 239      41.104 -11.843 187.002  1.00146.19           C  
ANISOU 1493  CB  PHE A 239    18817  20739  15989    228   -571    306       C  
ATOM   1494  CG  PHE A 239      42.031 -11.897 185.827  1.00148.57           C  
ANISOU 1494  CG  PHE A 239    19133  21034  16281    222   -492    324       C  
ATOM   1495  CD1 PHE A 239      43.060 -10.983 185.702  1.00152.42           C  
ANISOU 1495  CD1 PHE A 239    19644  21435  16833    146   -395    327       C  
ATOM   1496  CD2 PHE A 239      41.865 -12.851 184.843  1.00150.98           C  
ANISOU 1496  CD2 PHE A 239    19433  21414  16519    294   -501    327       C  
ATOM   1497  CE1 PHE A 239      43.913 -11.021 184.620  1.00154.11           C  
ANISOU 1497  CE1 PHE A 239    19883  21621  17050    136   -293    339       C  
ATOM   1498  CE2 PHE A 239      42.714 -12.896 183.757  1.00154.53           C  
ANISOU 1498  CE2 PHE A 239    19916  21846  16951    294   -415    350       C  
ATOM   1499  CZ  PHE A 239      43.740 -11.979 183.645  1.00153.29           C  
ANISOU 1499  CZ  PHE A 239    19792  21586  16863    212   -303    360       C  
ATOM   1500  N   LYS A 240      39.828 -12.340 189.830  1.00144.67           N  
ANISOU 1500  N   LYS A 240    18584  20517  15868    189   -705    239       N  
ATOM   1501  CA  LYS A 240      39.143 -11.745 190.971  1.00144.29           C  
ANISOU 1501  CA  LYS A 240    18580  20415  15828    184   -723    237       C  
ATOM   1502  C   LYS A 240      39.752 -11.890 192.365  1.00148.90           C  
ANISOU 1502  C   LYS A 240    19154  20971  16450    142   -759    204       C  
ATOM   1503  O   LYS A 240      39.707 -10.938 193.143  1.00148.88           O  
ANISOU 1503  O   LYS A 240    19195  20916  16457    119   -764    204       O  
ATOM   1504  CB  LYS A 240      37.688 -12.221 191.000  1.00145.84           C  
ANISOU 1504  CB  LYS A 240    18777  20627  16010    241   -738    214       C  
ATOM   1505  CG  LYS A 240      36.905 -11.860 189.750  1.00155.48           C  
ANISOU 1505  CG  LYS A 240    20021  21874  17181    312   -726    230       C  
ATOM   1506  CD  LYS A 240      35.508 -12.456 189.775  1.00162.66           C  
ANISOU 1506  CD  LYS A 240    20872  22835  18096    375   -751    159       C  
ATOM   1507  CE  LYS A 240      34.743 -12.133 188.502  1.00170.13           C  
ANISOU 1507  CE  LYS A 240    21828  23838  18974    478   -766    153       C  
ATOM   1508  NZ  LYS A 240      33.374 -12.719 188.510  1.00176.44           N  
ANISOU 1508  NZ  LYS A 240    22534  24711  19796    540   -800     44       N  
ATOM   1509  N   ALA A 241      40.309 -13.048 192.704  1.00145.33           N  
ANISOU 1509  N   ALA A 241    18651  20556  16011    144   -786    173       N  
ATOM   1510  CA  ALA A 241      40.848 -13.209 194.052  1.00170.94           C  
ANISOU 1510  CA  ALA A 241    21898  23784  19266    143   -832    138       C  
ATOM   1511  C   ALA A 241      42.306 -12.807 194.244  1.00187.07           C  
ANISOU 1511  C   ALA A 241    23911  25821  21345     99   -857    101       C  
ATOM   1512  O   ALA A 241      43.219 -13.487 193.787  1.00142.79           O  
ANISOU 1512  O   ALA A 241    18280  20205  15768     54   -811    106       O  
ATOM   1513  CB  ALA A 241      40.631 -14.637 194.535  1.00 30.00           C  
ATOM   1514  N   GLY A1001      42.500 -11.686 194.935  1.00158.38           N  
ANISOU 1514  N   GLY A1001    20310  22074  17791     -4   -800     55       N  
ATOM   1515  CA  GLY A1001      43.819 -11.175 195.263  1.00158.69           C  
ANISOU 1515  CA  GLY A1001    20297  22144  17856      7   -886    -39       C  
ATOM   1516  C   GLY A1001      43.959 -10.916 196.755  1.00162.88           C  
ANISOU 1516  C   GLY A1001    20882  22654  18349     49   -954    -72       C  
ATOM   1517  O   GLY A1001      45.040 -10.612 197.248  1.00163.41           O  
ANISOU 1517  O   GLY A1001    20907  22722  18458     37   -998   -171       O  
ATOM   1518  N   ILE A1002      42.844 -11.028 197.467  1.00158.78           N  
ANISOU 1518  N   ILE A1002    20456  22117  17758    100   -957     -3       N  
ATOM   1519  CA  ILE A1002      42.784 -10.781 198.905  1.00158.74           C  
ANISOU 1519  CA  ILE A1002    20535  22076  17702    149  -1003    -18       C  
ATOM   1520  C   ILE A1002      43.443 -11.828 199.782  1.00163.25           C  
ANISOU 1520  C   ILE A1002    21130  22679  18217    243  -1090    -68       C  
ATOM   1521  O   ILE A1002      43.439 -13.009 199.454  1.00162.66           O  
ANISOU 1521  O   ILE A1002    21074  22619  18111    289  -1079    -33       O  
ATOM   1522  CB  ILE A1002      41.328 -10.680 199.374  1.00161.04           C  
ANISOU 1522  CB  ILE A1002    20923  22309  17957    159   -944     62       C  
ATOM   1523  CG1 ILE A1002      41.277 -10.305 200.851  1.00161.56           C  
ANISOU 1523  CG1 ILE A1002    21096  22324  17965    216   -976     48       C  
ATOM   1524  CG2 ILE A1002      40.616 -12.001 199.149  1.00160.93           C  
ANISOU 1524  CG2 ILE A1002    20910  22306  17931    183   -899    113       C  
ATOM   1525  CD1 ILE A1002      39.874 -10.218 201.403  1.00167.49           C  
ANISOU 1525  CD1 ILE A1002    21918  23004  18716    191   -918     93       C  
ATOM   1526  N   ASP A1003      43.993 -11.390 200.912  1.00160.50           N  
ANISOU 1526  N   ASP A1003    20784  22344  17856    283  -1174   -160       N  
ATOM   1527  CA  ASP A1003      44.615 -12.314 201.856  1.00161.00           C  
ANISOU 1527  CA  ASP A1003    20893  22441  17841    410  -1274   -217       C  
ATOM   1528  C   ASP A1003      43.781 -12.367 203.135  1.00165.38           C  
ANISOU 1528  C   ASP A1003    21613  22935  18291    499  -1277   -182       C  
ATOM   1529  O   ASP A1003      43.592 -11.343 203.796  1.00165.06           O  
ANISOU 1529  O   ASP A1003    21597  22867  18251    478  -1289   -212       O  
ATOM   1530  CB  ASP A1003      46.089 -11.950 202.133  1.00163.81           C  
ANISOU 1530  CB  ASP A1003    21131  22865  18245    425  -1384   -374       C  
ATOM   1531  CG  ASP A1003      46.313 -10.548 202.663  1.00172.85           C  
ANISOU 1531  CG  ASP A1003    22232  23997  19444    372  -1401   -466       C  
ATOM   1532  OD1 ASP A1003      46.030  -9.582 201.923  1.00172.89           O  
ANISOU 1532  OD1 ASP A1003    22186  23963  19542    245  -1300   -437       O  
ATOM   1533  OD2 ASP A1003      46.770 -10.417 203.818  1.00178.70           O  
ANISOU 1533  OD2 ASP A1003    22996  24768  20134    468  -1511   -573       O  
ATOM   1534  N   CYS A1004      43.258 -13.562 203.465  1.00162.40           N  
ANISOU 1534  N   CYS A1004    21355  22523  17828    596  -1244   -119       N  
ATOM   1535  CA  CYS A1004      42.423 -13.790 204.649  1.00162.85           C  
ANISOU 1535  CA  CYS A1004    21599  22495  17782    691  -1209    -77       C  
ATOM   1536  C   CYS A1004      43.213 -13.700 205.971  1.00168.68           C  
ANISOU 1536  C   CYS A1004    22419  23260  18411    836  -1334   -162       C  
ATOM   1537  O   CYS A1004      42.645 -13.897 207.052  1.00168.74           O  
ANISOU 1537  O   CYS A1004    22609  23194  18310    942  -1308   -131       O  
ATOM   1538  CB  CYS A1004      41.651 -15.101 204.526  1.00162.86           C  
ANISOU 1538  CB  CYS A1004    21703  22430  17747    744  -1095      5       C  
ATOM   1539  SG  CYS A1004      40.471 -15.137 203.149  1.00165.42           S  
ANISOU 1539  SG  CYS A1004    21938  22723  18191    598   -957     73       S  
ATOM   1540  N   SER A1005      44.516 -13.363 205.873  1.00166.32           N  
ANISOU 1540  N   SER A1005    21984  23063  18146    846  -1466   -285       N  
ATOM   1541  CA  SER A1005      45.431 -13.162 206.995  1.00167.72           C  
ANISOU 1541  CA  SER A1005    22187  23298  18240    987  -1619   -415       C  
ATOM   1542  C   SER A1005      45.252 -11.737 207.554  1.00171.75           C  
ANISOU 1542  C   SER A1005    22670  23798  18788    919  -1640   -480       C  
ATOM   1543  O   SER A1005      45.634 -11.470 208.698  1.00172.73           O  
ANISOU 1543  O   SER A1005    22857  23949  18821   1045  -1750   -578       O  
ATOM   1544  CB  SER A1005      46.872 -13.378 206.540  1.00172.09           C  
ANISOU 1544  CB  SER A1005    22568  23966  18853   1009  -1741   -552       C  
ATOM   1545  OG  SER A1005      47.769 -13.397 207.638  1.00183.24           O  
ANISOU 1545  OG  SER A1005    24006  25449  20170   1186  -1909   -699       O  
ATOM   1546  N   PHE A1006      44.656 -10.834 206.741  1.00166.71           N  
ANISOU 1546  N   PHE A1006    21947  23119  18276    734  -1534   -428       N  
ATOM   1547  CA  PHE A1006      44.381  -9.434 207.078  1.00166.26           C  
ANISOU 1547  CA  PHE A1006    21857  23036  18279    641  -1515   -469       C  
ATOM   1548  C   PHE A1006      42.874  -9.223 207.310  1.00167.64           C  
ANISOU 1548  C   PHE A1006    22178  23099  18419    603  -1393   -327       C  
ATOM   1549  O   PHE A1006      42.478  -8.777 208.391  1.00167.48           O  
ANISOU 1549  O   PHE A1006    22267  23037  18331    653  -1408   -341       O  
ATOM   1550  CB  PHE A1006      44.872  -8.514 205.937  1.00167.90           C  
ANISOU 1550  CB  PHE A1006    21869  23267  18659    472  -1465   -516       C  
ATOM   1551  CG  PHE A1006      45.366  -7.132 206.311  1.00170.37           C  
ANISOU 1551  CG  PHE A1006    22079  23589  19063    400  -1483   -651       C  
ATOM   1552  CD1 PHE A1006      44.589  -6.282 207.093  1.00173.34           C  
ANISOU 1552  CD1 PHE A1006    22542  23907  19413    383  -1451   -629       C  
ATOM   1553  CD2 PHE A1006      46.569  -6.648 205.809  1.00173.45           C  
ANISOU 1553  CD2 PHE A1006    22280  24033  19589    334  -1504   -806       C  
ATOM   1554  CE1 PHE A1006      45.038  -5.000 207.420  1.00175.11           C  
ANISOU 1554  CE1 PHE A1006    22664  24135  19735    309  -1450   -761       C  
ATOM   1555  CE2 PHE A1006      47.011  -5.361 206.125  1.00177.17           C  
ANISOU 1555  CE2 PHE A1006    22646  24499  20172    256  -1489   -949       C  
ATOM   1556  CZ  PHE A1006      46.244  -4.546 206.929  1.00175.20           C  
ANISOU 1556  CZ  PHE A1006    22482  24198  19887    244  -1464   -925       C  
ATOM   1557  N   TRP A1007      42.046  -9.535 206.283  1.00161.85           N  
ANISOU 1557  N   TRP A1007    21437  22320  17738    517  -1275   -208       N  
ATOM   1558  CA  TRP A1007      40.586  -9.372 206.279  1.00160.04           C  
ANISOU 1558  CA  TRP A1007    21309  21990  17510    469  -1153    -97       C  
ATOM   1559  C   TRP A1007      39.880 -10.646 206.761  1.00162.53           C  
ANISOU 1559  C   TRP A1007    21785  22238  17732    575  -1096    -29       C  
ATOM   1560  O   TRP A1007      39.537 -11.516 205.953  1.00161.44           O  
ANISOU 1560  O   TRP A1007    21626  22092  17622    561  -1029     24       O  
ATOM   1561  CB  TRP A1007      40.073  -8.948 204.880  1.00157.57           C  
ANISOU 1561  CB  TRP A1007    20889  21674  17308    336  -1065    -35       C  
ATOM   1562  CG  TRP A1007      40.920  -7.923 204.176  1.00158.53           C  
ANISOU 1562  CG  TRP A1007    20862  21848  17524    242  -1083    -94       C  
ATOM   1563  CD1 TRP A1007      41.917  -8.163 203.276  1.00161.51           C  
ANISOU 1563  CD1 TRP A1007    21117  22294  17957    216  -1107   -138       C  
ATOM   1564  CD2 TRP A1007      40.835  -6.499 204.314  1.00158.50           C  
ANISOU 1564  CD2 TRP A1007    20825  21815  17583    160  -1050   -120       C  
ATOM   1565  NE1 TRP A1007      42.463  -6.976 202.847  1.00161.22           N  
ANISOU 1565  NE1 TRP A1007    20978  22260  18016    122  -1077   -193       N  
ATOM   1566  CE2 TRP A1007      41.818  -5.938 203.468  1.00162.68           C  
ANISOU 1566  CE2 TRP A1007    21216  22388  18209     87  -1039   -182       C  
ATOM   1567  CE3 TRP A1007      40.024  -5.638 205.073  1.00159.70           C  
ANISOU 1567  CE3 TRP A1007    21054  21898  17726    137  -1013   -100       C  
ATOM   1568  CZ2 TRP A1007      42.016  -4.556 203.364  1.00162.42           C  
ANISOU 1568  CZ2 TRP A1007    21124  22322  18264     -4   -977   -225       C  
ATOM   1569  CZ3 TRP A1007      40.219  -4.270 204.968  1.00161.49           C  
ANISOU 1569  CZ3 TRP A1007    21215  22107  18036     47   -971   -137       C  
ATOM   1570  CH2 TRP A1007      41.200  -3.741 204.117  1.00162.56           C  
ANISOU 1570  CH2 TRP A1007    21218  22278  18268    -22   -945   -199       C  
ATOM   1571  N   ASN A1008      39.677 -10.754 208.086  1.00158.98           N  
ANISOU 1571  N   ASN A1008    21502  21730  17172    685  -1108    -37       N  
ATOM   1572  CA  ASN A1008      39.020 -11.902 208.714  1.00158.81           C  
ANISOU 1572  CA  ASN A1008    21673  21611  17056    800  -1018     24       C  
ATOM   1573  C   ASN A1008      38.102 -11.465 209.857  1.00162.52           C  
ANISOU 1573  C   ASN A1008    22321  21962  17467    833   -947     50       C  
ATOM   1574  O   ASN A1008      38.312 -10.400 210.439  1.00162.33           O  
ANISOU 1574  O   ASN A1008    22288  21960  17432    815  -1019      1       O  
ATOM   1575  CB  ASN A1008      40.063 -12.908 209.211  1.00160.93           C  
ANISOU 1575  CB  ASN A1008    22012  21932  17201    975  -1107    -15       C  
ATOM   1576  CG  ASN A1008      39.619 -14.348 209.120  1.00186.00           C  
ANISOU 1576  CG  ASN A1008    25309  25029  20333   1055   -983     57       C  
ATOM   1577  OD1 ASN A1008      38.675 -14.784 209.792  1.00181.00           O  
ANISOU 1577  OD1 ASN A1008    24866  24258  19648   1111   -843    114       O  
ATOM   1578  ND2 ASN A1008      40.302 -15.124 208.291  1.00177.84           N  
ANISOU 1578  ND2 ASN A1008    24170  24071  19330   1059  -1013     49       N  
ATOM   1579  N   GLU A1009      37.085 -12.289 210.174  1.00159.00           N  
ANISOU 1579  N   GLU A1009    22034  21382  16997    874   -790    117       N  
ATOM   1580  CA  GLU A1009      36.119 -12.028 211.249  1.00159.24           C  
ANISOU 1580  CA  GLU A1009    22256  21269  16980    906   -683    145       C  
ATOM   1581  C   GLU A1009      36.750 -12.178 212.652  1.00164.13           C  
ANISOU 1581  C   GLU A1009    23078  21875  17409   1099   -756    119       C  
ATOM   1582  O   GLU A1009      36.396 -11.421 213.561  1.00164.05           O  
ANISOU 1582  O   GLU A1009    23170  21810  17352   1112   -755    109       O  
ATOM   1583  CB  GLU A1009      34.892 -12.949 211.095  1.00160.46           C  
ANISOU 1583  CB  GLU A1009    22508  21270  17190    890   -465    200       C  
ATOM   1584  CG  GLU A1009      33.666 -12.526 211.895  1.00172.20           C  
ANISOU 1584  CG  GLU A1009    24139  22591  18697    861   -319    220       C  
ATOM   1585  CD  GLU A1009      33.584 -13.066 213.311  1.00195.40           C  
ANISOU 1585  CD  GLU A1009    27373  25396  21476   1032   -233    243       C  
ATOM   1586  OE1 GLU A1009      33.466 -14.302 213.473  1.00191.17           O  
ANISOU 1586  OE1 GLU A1009    26978  24766  20892   1136    -99    271       O  
ATOM   1587  OE2 GLU A1009      33.618 -12.249 214.261  1.00189.05           O  
ANISOU 1587  OE2 GLU A1009    26668  24572  20591   1068   -287    233       O  
ATOM   1588  N   SER A1010      37.669 -13.162 212.815  1.00161.02           N  
ANISOU 1588  N   SER A1010    22745  21534  16900   1260   -822    105       N  
ATOM   1589  CA  SER A1010      38.372 -13.511 214.060  1.00162.05           C  
ANISOU 1589  CA  SER A1010    23080  21670  16821   1496   -909     72       C  
ATOM   1590  C   SER A1010      39.095 -12.351 214.751  1.00165.73           C  
ANISOU 1590  C   SER A1010    23494  22244  17231   1530  -1103    -33       C  
ATOM   1591  O   SER A1010      39.143 -12.313 215.982  1.00166.67           O  
ANISOU 1591  O   SER A1010    23822  22322  17182   1702  -1135    -53       O  
ATOM   1592  CB  SER A1010      39.353 -14.654 213.814  1.00165.98           C  
ANISOU 1592  CB  SER A1010    23587  22242  17236   1645   -976     60       C  
ATOM   1593  OG  SER A1010      40.421 -14.252 212.972  1.00173.44           O  
ANISOU 1593  OG  SER A1010    24267  23366  18266   1570  -1155    -27       O  
ATOM   1594  N   TYR A1011      39.661 -11.421 213.962  1.00160.77           N  
ANISOU 1594  N   TYR A1011    22596  21746  16743   1374  -1220   -109       N  
ATOM   1595  CA  TYR A1011      40.409 -10.256 214.442  1.00160.92           C  
ANISOU 1595  CA  TYR A1011    22511  21873  16760   1371  -1387   -240       C  
ATOM   1596  C   TYR A1011      39.541  -9.200 215.163  1.00163.50           C  
ANISOU 1596  C   TYR A1011    22916  22112  17096   1301  -1325   -227       C  
ATOM   1597  O   TYR A1011      40.080  -8.386 215.920  1.00163.94           O  
ANISOU 1597  O   TYR A1011    22952  22234  17104   1351  -1451   -340       O  
ATOM   1598  CB  TYR A1011      41.212  -9.630 213.288  1.00161.49           C  
ANISOU 1598  CB  TYR A1011    22279  22075  17004   1210  -1474   -321       C  
ATOM   1599  CG  TYR A1011      42.372 -10.486 212.826  1.00164.12           C  
ANISOU 1599  CG  TYR A1011    22520  22521  17315   1304  -1587   -386       C  
ATOM   1600  CD1 TYR A1011      42.189 -11.498 211.886  1.00165.42           C  
ANISOU 1600  CD1 TYR A1011    22667  22664  17522   1272  -1498   -292       C  
ATOM   1601  CD2 TYR A1011      43.658 -10.277 213.316  1.00166.40           C  
ANISOU 1601  CD2 TYR A1011    22726  22943  17555   1424  -1784   -560       C  
ATOM   1602  CE1 TYR A1011      43.254 -12.293 211.461  1.00166.97           C  
ANISOU 1602  CE1 TYR A1011    22779  22960  17703   1355  -1597   -350       C  
ATOM   1603  CE2 TYR A1011      44.731 -11.063 212.895  1.00167.91           C  
ANISOU 1603  CE2 TYR A1011    22824  23237  17736   1513  -1891   -633       C  
ATOM   1604  CZ  TYR A1011      44.524 -12.070 211.966  1.00174.28           C  
ANISOU 1604  CZ  TYR A1011    23627  24012  18579   1474  -1793   -518       C  
ATOM   1605  OH  TYR A1011      45.578 -12.846 211.546  1.00175.26           O  
ANISOU 1605  OH  TYR A1011    23659  24233  18699   1557  -1894   -587       O  
ATOM   1606  N   LEU A1012      38.210  -9.229 214.948  1.00158.01           N  
ANISOU 1606  N   LEU A1012    22300  21269  16468   1191  -1133   -106       N  
ATOM   1607  CA  LEU A1012      37.259  -8.290 215.550  1.00157.10           C  
ANISOU 1607  CA  LEU A1012    22259  21051  16379   1110  -1050    -82       C  
ATOM   1608  C   LEU A1012      36.908  -8.654 216.989  1.00161.21           C  
ANISOU 1608  C   LEU A1012    23080  21462  16712   1296  -1006    -63       C  
ATOM   1609  O   LEU A1012      36.671  -9.826 217.291  1.00161.19           O  
ANISOU 1609  O   LEU A1012    23275  21369  16602   1436   -911      2       O  
ATOM   1610  CB  LEU A1012      35.969  -8.206 214.718  1.00155.67           C  
ANISOU 1610  CB  LEU A1012    22031  20760  16357    929   -868     17       C  
ATOM   1611  CG  LEU A1012      36.090  -7.761 213.262  1.00159.16           C  
ANISOU 1611  CG  LEU A1012    22211  21289  16973    755   -886     16       C  
ATOM   1612  CD1 LEU A1012      34.916  -8.270 212.453  1.00158.33           C  
ANISOU 1612  CD1 LEU A1012    22098  21087  16972    663   -722    101       C  
ATOM   1613  CD2 LEU A1012      36.207  -6.244 213.148  1.00161.25           C  
ANISOU 1613  CD2 LEU A1012    22333  21604  17332    624   -939    -34       C  
ATOM   1614  N   THR A1013      36.837  -7.636 217.865  1.00157.91           N  
ANISOU 1614  N   THR A1013    22705  21038  16255   1297  -1054   -118       N  
ATOM   1615  CA  THR A1013      36.493  -7.781 219.286  1.00158.91           C  
ANISOU 1615  CA  THR A1013    23126  21058  16194   1473  -1015   -107       C  
ATOM   1616  C   THR A1013      35.004  -7.517 219.530  1.00161.09           C  
ANISOU 1616  C   THR A1013    23529  21136  16544   1355   -794     -8       C  
ATOM   1617  O   THR A1013      34.437  -6.597 218.940  1.00159.44           O  
ANISOU 1617  O   THR A1013    23148  20920  16514   1143   -753     -2       O  
ATOM   1618  CB  THR A1013      37.375  -6.876 220.168  1.00169.21           C  
ANISOU 1618  CB  THR A1013    24403  22488  17400   1568  -1217   -253       C  
ATOM   1619  OG1 THR A1013      37.401  -5.549 219.630  1.00168.69           O  
ANISOU 1619  OG1 THR A1013    24080  22491  17523   1347  -1258   -316       O  
ATOM   1620  CG2 THR A1013      38.794  -7.410 220.327  1.00169.06           C  
ANISOU 1620  CG2 THR A1013    24345  22637  17251   1772  -1431   -372       C  
ATOM   1621  N   GLY A1014      34.397  -8.322 220.401  1.00157.82           N  
ANISOU 1621  N   GLY A1014    23419  20553  15993   1502   -643     61       N  
ATOM   1622  CA  GLY A1014      32.987  -8.210 220.760  1.00157.00           C  
ANISOU 1622  CA  GLY A1014    23463  20232  15956   1411   -407    138       C  
ATOM   1623  C   GLY A1014      32.039  -8.691 219.681  1.00159.01           C  
ANISOU 1623  C   GLY A1014    23611  20394  16413   1242   -225    202       C  
ATOM   1624  O   GLY A1014      32.452  -9.416 218.771  1.00158.09           O  
ANISOU 1624  O   GLY A1014    23372  20354  16342   1236   -254    208       O  
ATOM   1625  N   SER A1015      30.752  -8.298 219.785  1.00154.89           N  
ANISOU 1625  N   SER A1015    23129  19705  16017   1108    -39    234       N  
ATOM   1626  CA  SER A1015      29.709  -8.671 218.823  1.00153.66           C  
ANISOU 1626  CA  SER A1015    22862  19454  16068    950    136    260       C  
ATOM   1627  C   SER A1015      29.403  -7.531 217.853  1.00155.95           C  
ANISOU 1627  C   SER A1015    22861  19842  16551    736     56    234       C  
ATOM   1628  O   SER A1015      29.486  -6.365 218.236  1.00155.22           O  
ANISOU 1628  O   SER A1015    22728  19792  16457    682    -31    212       O  
ATOM   1629  CB  SER A1015      28.440  -9.121 219.541  1.00158.00           C  
ANISOU 1629  CB  SER A1015    23645  19738  16648    957    415    290       C  
ATOM   1630  OG  SER A1015      27.461  -9.596 218.630  1.00166.68           O  
ANISOU 1630  OG  SER A1015    24625  20749  17958    823    585    279       O  
ATOM   1631  N   ARG A1016      29.019  -7.882 216.605  1.00151.70           N  
ANISOU 1631  N   ARG A1016    22134  19334  16171    628     97    233       N  
ATOM   1632  CA  ARG A1016      28.709  -6.962 215.497  1.00150.26           C  
ANISOU 1632  CA  ARG A1016    21690  19244  16158    457     33    216       C  
ATOM   1633  C   ARG A1016      27.634  -5.913 215.823  1.00152.09           C  
ANISOU 1633  C   ARG A1016    21921  19373  16495    341    113    210       C  
ATOM   1634  O   ARG A1016      27.683  -4.822 215.254  1.00151.06           O  
ANISOU 1634  O   ARG A1016    21617  19337  16442    237     19    203       O  
ATOM   1635  CB  ARG A1016      28.363  -7.720 214.196  1.00151.64           C  
ANISOU 1635  CB  ARG A1016    21706  19448  16461    400     84    207       C  
ATOM   1636  CG  ARG A1016      27.292  -8.807 214.332  1.00167.75           C  
ANISOU 1636  CG  ARG A1016    23859  21302  18575    415    315    192       C  
ATOM   1637  CD  ARG A1016      27.458  -9.911 213.297  1.00182.52           C  
ANISOU 1637  CD  ARG A1016    25620  23228  20500    427    338    175       C  
ATOM   1638  NE  ARG A1016      28.512 -10.865 213.657  1.00194.19           N  
ANISOU 1638  NE  ARG A1016    27223  24743  21819    573    302    208       N  
ATOM   1639  CZ  ARG A1016      29.725 -10.898 213.110  1.00207.98           C  
ANISOU 1639  CZ  ARG A1016    28858  26674  23492    611    114    220       C  
ATOM   1640  NH1 ARG A1016      30.060 -10.029 212.163  1.00194.00           N  
ANISOU 1640  NH1 ARG A1016    26862  25058  21792    509    -36    207       N  
ATOM   1641  NH2 ARG A1016      30.611 -11.802 213.504  1.00195.13           N  
ANISOU 1641  NH2 ARG A1016    27353  25067  21720    758     88    241       N  
ATOM   1642  N   ASP A1017      26.688  -6.223 216.730  1.00147.78           N  
ANISOU 1642  N   ASP A1017    21573  18624  15952    362    299    212       N  
ATOM   1643  CA  ASP A1017      25.670  -5.251 217.133  1.00146.87           C  
ANISOU 1643  CA  ASP A1017    21470  18398  15938    256    382    200       C  
ATOM   1644  C   ASP A1017      26.251  -4.264 218.160  1.00148.64           C  
ANISOU 1644  C   ASP A1017    21787  18654  16034    288    279    211       C  
ATOM   1645  O   ASP A1017      25.876  -3.093 218.153  1.00147.57           O  
ANISOU 1645  O   ASP A1017    21562  18527  15979    179    252    203       O  
ATOM   1646  CB  ASP A1017      24.396  -5.940 217.654  1.00149.77           C  
ANISOU 1646  CB  ASP A1017    21995  18521  16389    249    642    179       C  
ATOM   1647  CG  ASP A1017      24.554  -6.610 219.002  1.00166.02           C  
ANISOU 1647  CG  ASP A1017    24373  20427  18280    395    764    209       C  
ATOM   1648  OD1 ASP A1017      25.111  -7.730 219.046  1.00168.31           O  
ANISOU 1648  OD1 ASP A1017    24770  20715  18466    523    794    228       O  
ATOM   1649  OD2 ASP A1017      24.132  -6.009 220.017  1.00173.27           O  
ANISOU 1649  OD2 ASP A1017    25447  21225  19163    393    834    216       O  
ATOM   1650  N   GLU A1018      27.176  -4.742 219.027  1.00144.45           N  
ANISOU 1650  N   GLU A1018    21433  18148  15302    450    217    219       N  
ATOM   1651  CA  GLU A1018      27.857  -3.945 220.055  1.00144.02           C  
ANISOU 1651  CA  GLU A1018    21470  18146  15105    517     98    200       C  
ATOM   1652  C   GLU A1018      28.916  -3.062 219.415  1.00144.17           C  
ANISOU 1652  C   GLU A1018    21248  18388  15142    463   -121    157       C  
ATOM   1653  O   GLU A1018      29.120  -1.932 219.858  1.00143.85           O  
ANISOU 1653  O   GLU A1018    21165  18390  15102    414   -194    121       O  
ATOM   1654  CB  GLU A1018      28.489  -4.844 221.128  1.00147.10           C  
ANISOU 1654  CB  GLU A1018    22132  18497  15261    744     96    206       C  
ATOM   1655  CG  GLU A1018      27.484  -5.429 222.106  1.00159.45           C  
ANISOU 1655  CG  GLU A1018    23996  19807  16779    810    339    245       C  
ATOM   1656  CD  GLU A1018      27.447  -6.944 222.135  1.00180.84           C  
ANISOU 1656  CD  GLU A1018    26887  22410  19414    951    484    282       C  
ATOM   1657  OE1 GLU A1018      28.463  -7.558 222.536  1.00176.90           O  
ANISOU 1657  OE1 GLU A1018    26513  21990  18711   1150    379    287       O  
ATOM   1658  OE2 GLU A1018      26.401  -7.519 221.757  1.00172.31           O  
ANISOU 1658  OE2 GLU A1018    25819  21164  18487    867    708    294       O  
ATOM   1659  N   ARG A1019      29.577  -3.580 218.361  1.00137.94           N  
ANISOU 1659  N   ARG A1019    20301  17729  14382    466   -206    154       N  
ATOM   1660  CA  ARG A1019      30.585  -2.880 217.561  1.00136.17           C  
ANISOU 1660  CA  ARG A1019    19839  17697  14202    407   -378    110       C  
ATOM   1661  C   ARG A1019      29.916  -1.712 216.820  1.00136.38           C  
ANISOU 1661  C   ARG A1019    19692  17721  14405    223   -341    123       C  
ATOM   1662  O   ARG A1019      30.535  -0.661 216.651  1.00135.48           O  
ANISOU 1662  O   ARG A1019    19444  17706  14326    160   -434     81       O  
ATOM   1663  CB  ARG A1019      31.224  -3.838 216.537  1.00135.69           C  
ANISOU 1663  CB  ARG A1019    19672  17737  14146    444   -432    117       C  
ATOM   1664  CG  ARG A1019      32.172  -4.881 217.117  1.00145.11           C  
ANISOU 1664  CG  ARG A1019    20997  18976  15162    637   -509     94       C  
ATOM   1665  CD  ARG A1019      32.784  -5.725 216.014  1.00152.90           C  
ANISOU 1665  CD  ARG A1019    21852  20064  16178    649   -559     99       C  
ATOM   1666  NE  ARG A1019      32.605  -7.161 216.243  1.00161.22           N  
ANISOU 1666  NE  ARG A1019    23080  21033  17144    780   -463    142       N  
ATOM   1667  CZ  ARG A1019      32.192  -8.027 215.319  1.00172.96           C  
ANISOU 1667  CZ  ARG A1019    24509  22491  18718    740   -368    179       C  
ATOM   1668  NH1 ARG A1019      31.893  -7.612 214.094  1.00156.87           N  
ANISOU 1668  NH1 ARG A1019    22251  20512  16841    588   -372    181       N  
ATOM   1669  NH2 ARG A1019      32.067  -9.314 215.618  1.00159.91           N  
ANISOU 1669  NH2 ARG A1019    23026  20746  16988    863   -259    210       N  
ATOM   1670  N   LYS A1020      28.646  -1.913 216.389  1.00130.74           N  
ANISOU 1670  N   LYS A1020    18984  16887  13806    147   -195    169       N  
ATOM   1671  CA  LYS A1020      27.804  -0.947 215.672  1.00128.81           C  
ANISOU 1671  CA  LYS A1020    18600  16620  13721      4   -146    184       C  
ATOM   1672  C   LYS A1020      27.389   0.216 216.580  1.00130.78           C  
ANISOU 1672  C   LYS A1020    18910  16795  13984    -56   -114    176       C  
ATOM   1673  O   LYS A1020      27.545   1.374 216.184  1.00130.45           O  
ANISOU 1673  O   LYS A1020    18736  16815  14014   -146   -157    171       O  
ATOM   1674  CB  LYS A1020      26.564  -1.649 215.084  1.00130.55           C  
ANISOU 1674  CB  LYS A1020    18816  16733  14053    -28    -10    199       C  
ATOM   1675  CG  LYS A1020      25.801  -0.827 214.043  1.00140.54           C  
ANISOU 1675  CG  LYS A1020    19910  18016  15472   -138      5    203       C  
ATOM   1676  CD  LYS A1020      24.655  -1.616 213.420  1.00148.35           C  
ANISOU 1676  CD  LYS A1020    20866  18923  16576   -150    116    176       C  
ATOM   1677  CE  LYS A1020      23.355  -1.501 214.184  1.00156.82           C  
ANISOU 1677  CE  LYS A1020    22041  19807  17736   -191    272    145       C  
ATOM   1678  NZ  LYS A1020      22.286  -2.346 213.589  1.00163.69           N  
ANISOU 1678  NZ  LYS A1020    22855  20598  18741   -201    386     79       N  
ATOM   1679  N   LYS A1021      26.858  -0.094 217.788  1.00125.53           N  
ANISOU 1679  N   LYS A1021    18457  15987  13252     -3    -21    176       N  
ATOM   1680  CA  LYS A1021      26.411   0.888 218.785  1.00124.50           C  
ANISOU 1680  CA  LYS A1021    18414  15768  13123    -50     24    166       C  
ATOM   1681  C   LYS A1021      27.566   1.790 219.219  1.00126.20           C  
ANISOU 1681  C   LYS A1021    18575  16115  13260    -36   -124    116       C  
ATOM   1682  O   LYS A1021      27.374   2.998 219.370  1.00125.70           O  
ANISOU 1682  O   LYS A1021    18446  16047  13269   -136   -119    102       O  
ATOM   1683  CB  LYS A1021      25.776   0.189 220.002  1.00127.84           C  
ANISOU 1683  CB  LYS A1021    19105  16008  13460     34    160    175       C  
ATOM   1684  CG  LYS A1021      24.427  -0.460 219.711  1.00140.37           C  
ANISOU 1684  CG  LYS A1021    20735  17423  15178    -15    353    191       C  
ATOM   1685  CD  LYS A1021      24.027  -1.464 220.788  1.00150.20           C  
ANISOU 1685  CD  LYS A1021    22264  18482  16324     97    514    199       C  
ATOM   1686  CE  LYS A1021      23.198  -2.609 220.245  1.00160.12           C  
ANISOU 1686  CE  LYS A1021    23532  19614  17692     90    687    189       C  
ATOM   1687  NZ  LYS A1021      21.828  -2.187 219.844  1.00167.54           N  
ANISOU 1687  NZ  LYS A1021    24367  20436  18855    -56    819    151       N  
ATOM   1688  N   SER A1022      28.768   1.201 219.384  1.00121.24           N  
ANISOU 1688  N   SER A1022    17960  15606  12499     87   -252     74       N  
ATOM   1689  CA  SER A1022      29.986   1.909 219.769  1.00120.95           C  
ANISOU 1689  CA  SER A1022    17846  15711  12398    118   -406    -17       C  
ATOM   1690  C   SER A1022      30.539   2.746 218.618  1.00121.75           C  
ANISOU 1690  C   SER A1022    17687  15935  12637     -5   -462    -42       C  
ATOM   1691  O   SER A1022      31.132   3.790 218.882  1.00121.66           O  
ANISOU 1691  O   SER A1022    17581  15988  12657    -55   -517   -120       O  
ATOM   1692  CB  SER A1022      31.043   0.930 220.261  1.00126.22           C  
ANISOU 1692  CB  SER A1022    18606  16465  12887    307   -527    -70       C  
ATOM   1693  OG  SER A1022      31.358  -0.011 219.247  1.00137.09           O  
ANISOU 1693  OG  SER A1022    19903  17902  14284    331   -547    -36       O  
ATOM   1694  N   LEU A1023      30.372   2.282 217.352  1.00115.68           N  
ANISOU 1694  N   LEU A1023    16809  15193  11951    -47   -436     16       N  
ATOM   1695  CA  LEU A1023      30.822   3.001 216.150  1.00113.95           C  
ANISOU 1695  CA  LEU A1023    16375  15068  11852   -148   -460     11       C  
ATOM   1696  C   LEU A1023      29.982   4.271 215.996  1.00115.88           C  
ANISOU 1696  C   LEU A1023    16571  15238  12220   -280   -362     46       C  
ATOM   1697  O   LEU A1023      30.534   5.332 215.696  1.00115.92           O  
ANISOU 1697  O   LEU A1023    16450  15299  12298   -355   -371      6       O  
ATOM   1698  CB  LEU A1023      30.700   2.121 214.886  1.00113.06           C  
ANISOU 1698  CB  LEU A1023    16193  14989  11775   -138   -449     70       C  
ATOM   1699  CG  LEU A1023      31.197   2.741 213.566  1.00117.34           C  
ANISOU 1699  CG  LEU A1023    16545  15621  12418   -216   -462     76       C  
ATOM   1700  CD1 LEU A1023      32.512   2.134 213.128  1.00118.11           C  
ANISOU 1700  CD1 LEU A1023    16557  15846  12472   -157   -567     20       C  
ATOM   1701  CD2 LEU A1023      30.182   2.567 212.464  1.00118.46           C  
ANISOU 1701  CD2 LEU A1023    16650  15721  12640   -255   -383    160       C  
ATOM   1702  N   LEU A1024      28.652   4.153 216.218  1.00110.06           N  
ANISOU 1702  N   LEU A1024    15935  14367  11517   -305   -255    110       N  
ATOM   1703  CA  LEU A1024      27.695   5.253 216.119  1.00108.55           C  
ANISOU 1703  CA  LEU A1024    15715  14090  11439   -414   -159    145       C  
ATOM   1704  C   LEU A1024      27.973   6.300 217.184  1.00111.74           C  
ANISOU 1704  C   LEU A1024    16152  14474  11830   -455   -161     91       C  
ATOM   1705  O   LEU A1024      28.000   7.492 216.880  1.00110.69           O  
ANISOU 1705  O   LEU A1024    15920  14346  11790   -550   -124     89       O  
ATOM   1706  CB  LEU A1024      26.250   4.730 216.197  1.00108.06           C  
ANISOU 1706  CB  LEU A1024    15750  13887  11422   -419    -50    192       C  
ATOM   1707  CG  LEU A1024      25.737   4.006 214.943  1.00112.10           C  
ANISOU 1707  CG  LEU A1024    16183  14415  11996   -405    -32    225       C  
ATOM   1708  CD1 LEU A1024      24.573   3.092 215.268  1.00112.45           C  
ANISOU 1708  CD1 LEU A1024    16335  14321  12069   -381     72    222       C  
ATOM   1709  CD2 LEU A1024      25.337   4.985 213.866  1.00113.56           C  
ANISOU 1709  CD2 LEU A1024    16230  14629  12290   -472    -14    258       C  
ATOM   1710  N   SER A1025      28.255   5.838 218.415  1.00109.09           N  
ANISOU 1710  N   SER A1025    15960  14119  11369   -369   -202     41       N  
ATOM   1711  CA  SER A1025      28.613   6.660 219.571  1.00109.71           C  
ANISOU 1711  CA  SER A1025    16086  14194  11406   -377   -227    -35       C  
ATOM   1712  C   SER A1025      29.929   7.395 219.296  1.00114.78           C  
ANISOU 1712  C   SER A1025    16551  14982  12077   -403   -322   -137       C  
ATOM   1713  O   SER A1025      30.103   8.530 219.745  1.00115.15           O  
ANISOU 1713  O   SER A1025    16542  15028  12180   -479   -303   -201       O  
ATOM   1714  CB  SER A1025      28.729   5.787 220.821  1.00113.53           C  
ANISOU 1714  CB  SER A1025    16782  14639  11716   -232   -265    -67       C  
ATOM   1715  OG  SER A1025      29.233   6.491 221.944  1.00122.35           O  
ANISOU 1715  OG  SER A1025    17943  15780  12765   -208   -320   -162       O  
ATOM   1716  N   LYS A1026      30.842   6.746 218.542  1.00111.31           N  
ANISOU 1716  N   LYS A1026    16018  14659  11617   -348   -409   -164       N  
ATOM   1717  CA  LYS A1026      32.137   7.300 218.155  1.00111.69           C  
ANISOU 1717  CA  LYS A1026    15884  14838  11716   -374   -483   -279       C  
ATOM   1718  C   LYS A1026      31.927   8.335 217.055  1.00114.81           C  
ANISOU 1718  C   LYS A1026    16132  15212  12278   -518   -371   -231       C  
ATOM   1719  O   LYS A1026      32.658   9.329 216.999  1.00115.30           O  
ANISOU 1719  O   LYS A1026    16062  15319  12430   -589   -355   -329       O  
ATOM   1720  CB  LYS A1026      33.077   6.181 217.673  1.00114.52           C  
ANISOU 1720  CB  LYS A1026    16203  15307  12001   -267   -596   -313       C  
ATOM   1721  CG  LYS A1026      34.564   6.530 217.731  1.00131.91           C  
ANISOU 1721  CG  LYS A1026    18247  17647  14225   -250   -704   -488       C  
ATOM   1722  CD  LYS A1026      35.447   5.402 217.176  1.00142.61           C  
ANISOU 1722  CD  LYS A1026    19559  19106  15519   -146   -812   -517       C  
ATOM   1723  CE  LYS A1026      35.658   5.463 215.677  1.00151.08           C  
ANISOU 1723  CE  LYS A1026    20486  20202  16715   -236   -749   -461       C  
ATOM   1724  NZ  LYS A1026      36.540   6.596 215.283  1.00161.33           N  
ANISOU 1724  NZ  LYS A1026    21591  21547  18161   -341   -714   -586       N  
ATOM   1725  N   PHE A1027      30.912   8.104 216.195  1.00109.78           N  
ANISOU 1725  N   PHE A1027    15524  14503  11685   -548   -286    -92       N  
ATOM   1726  CA  PHE A1027      30.578   8.979 215.070  1.00108.66           C  
ANISOU 1726  CA  PHE A1027    15281  14335  11669   -644   -179    -24       C  
ATOM   1727  C   PHE A1027      29.506  10.026 215.404  1.00111.86           C  
ANISOU 1727  C   PHE A1027    15730  14623  12148   -728    -64     29       C  
ATOM   1728  O   PHE A1027      29.112  10.790 214.517  1.00111.89           O  
ANISOU 1728  O   PHE A1027    15676  14593  12244   -787     32     95       O  
ATOM   1729  CB  PHE A1027      30.201   8.154 213.821  1.00109.37           C  
ANISOU 1729  CB  PHE A1027    15357  14443  11758   -602   -177     72       C  
ATOM   1730  CG  PHE A1027      31.348   7.477 213.100  1.00110.99           C  
ANISOU 1730  CG  PHE A1027    15474  14763  11936   -553   -254     32       C  
ATOM   1731  CD1 PHE A1027      32.663   7.645 213.526  1.00114.79           C  
ANISOU 1731  CD1 PHE A1027    15876  15327  12411   -550   -321    -98       C  
ATOM   1732  CD2 PHE A1027      31.117   6.690 211.980  1.00112.73           C  
ANISOU 1732  CD2 PHE A1027    15677  15009  12145   -511   -260    107       C  
ATOM   1733  CE1 PHE A1027      33.719   7.023 212.858  1.00115.93           C  
ANISOU 1733  CE1 PHE A1027    15931  15571  12546   -509   -388   -146       C  
ATOM   1734  CE2 PHE A1027      32.176   6.068 211.311  1.00115.69           C  
ANISOU 1734  CE2 PHE A1027    15972  15484  12499   -472   -324     71       C  
ATOM   1735  CZ  PHE A1027      33.470   6.242 211.754  1.00114.45           C  
ANISOU 1735  CZ  PHE A1027    15741  15400  12343   -474   -385    -52       C  
ATOM   1736  N   GLY A1028      29.087  10.072 216.672  1.00107.36           N  
ANISOU 1736  N   GLY A1028    15269  13992  11531   -724    -71     -3       N  
ATOM   1737  CA  GLY A1028      28.097  11.016 217.186  1.00106.79           C  
ANISOU 1737  CA  GLY A1028    15248  13803  11526   -805     33     33       C  
ATOM   1738  C   GLY A1028      26.714  10.882 216.584  1.00109.67           C  
ANISOU 1738  C   GLY A1028    15658  14070  11942   -818    113    148       C  
ATOM   1739  O   GLY A1028      25.986  11.874 216.491  1.00108.32           O  
ANISOU 1739  O   GLY A1028    15475  13820  11861   -892    210    188       O  
ATOM   1740  N   MET A1029      26.349   9.654 216.172  1.00106.93           N  
ANISOU 1740  N   MET A1029    15356  13728  11546   -740     75    185       N  
ATOM   1741  CA  MET A1029      25.065   9.325 215.552  1.00106.75           C  
ANISOU 1741  CA  MET A1029    15353  13628  11579   -734    133    254       C  
ATOM   1742  C   MET A1029      24.217   8.429 216.464  1.00113.38           C  
ANISOU 1742  C   MET A1029    16337  14359  12385   -700    163    243       C  
ATOM   1743  O   MET A1029      24.770   7.641 217.229  1.00113.19           O  
ANISOU 1743  O   MET A1029    16404  14348  12254   -636    116    207       O  
ATOM   1744  CB  MET A1029      25.284   8.623 214.203  1.00108.54           C  
ANISOU 1744  CB  MET A1029    15495  13942  11801   -675     88    286       C  
ATOM   1745  CG  MET A1029      25.881   9.507 213.128  1.00112.28           C  
ANISOU 1745  CG  MET A1029    15852  14489  12319   -699    100    315       C  
ATOM   1746  SD  MET A1029      25.668   8.835 211.453  1.00116.30           S  
ANISOU 1746  SD  MET A1029    16290  15070  12829   -619     71    368       S  
ATOM   1747  CE  MET A1029      26.889   7.543 211.448  1.00113.06           C  
ANISOU 1747  CE  MET A1029    15864  14769  12325   -562    -35    322       C  
ATOM   1748  N   ASP A1030      22.874   8.530 216.351  1.00111.86           N  
ANISOU 1748  N   ASP A1030    16167  14052  12284   -732    251    267       N  
ATOM   1749  CA  ASP A1030      21.909   7.732 217.119  1.00112.67           C  
ANISOU 1749  CA  ASP A1030    16399  14016  12394   -716    326    245       C  
ATOM   1750  C   ASP A1030      21.897   6.258 216.686  1.00118.46           C  
ANISOU 1750  C   ASP A1030    17151  14768  13092   -631    309    231       C  
ATOM   1751  O   ASP A1030      22.441   5.925 215.631  1.00117.92           O  
ANISOU 1751  O   ASP A1030    16973  14821  13011   -593    234    244       O  
ATOM   1752  CB  ASP A1030      20.500   8.337 217.002  1.00114.52           C  
ANISOU 1752  CB  ASP A1030    16615  14128  12770   -781    427    247       C  
ATOM   1753  CG  ASP A1030      20.217   9.455 217.987  1.00128.14           C  
ANISOU 1753  CG  ASP A1030    18401  15762  14526   -864    491    249       C  
ATOM   1754  OD1 ASP A1030      20.095   9.163 219.201  1.00129.75           O  
ANISOU 1754  OD1 ASP A1030    18755  15867  14678   -866    542    225       O  
ATOM   1755  OD2 ASP A1030      20.096  10.617 217.544  1.00134.83           O  
ANISOU 1755  OD2 ASP A1030    19157  16628  15443   -920    502    277       O  
ATOM   1756  N   GLU A1031      21.282   5.376 217.502  1.00117.12           N  
ANISOU 1756  N   GLU A1031    17127  14464  12908   -603    399    203       N  
ATOM   1757  CA  GLU A1031      21.183   3.939 217.218  1.00117.95           C  
ANISOU 1757  CA  GLU A1031    17269  14553  12995   -528    425    181       C  
ATOM   1758  C   GLU A1031      20.269   3.692 216.016  1.00122.51           C  
ANISOU 1758  C   GLU A1031    17702  15131  13715   -545    453    151       C  
ATOM   1759  O   GLU A1031      19.190   4.283 215.933  1.00122.42           O  
ANISOU 1759  O   GLU A1031    17649  15031  13832   -604    522    122       O  
ATOM   1760  CB  GLU A1031      20.669   3.176 218.452  1.00120.28           C  
ANISOU 1760  CB  GLU A1031    17781  14667  13251   -495    561    157       C  
ATOM   1761  CG  GLU A1031      20.947   1.682 218.403  1.00133.85           C  
ANISOU 1761  CG  GLU A1031    19582  16371  14904   -396    596    144       C  
ATOM   1762  CD  GLU A1031      20.301   0.874 219.512  1.00161.85           C  
ANISOU 1762  CD  GLU A1031    23361  19703  18431   -357    781    123       C  
ATOM   1763  OE1 GLU A1031      20.803   0.926 220.658  1.00158.11           O  
ANISOU 1763  OE1 GLU A1031    23081  19187  17808   -294    786    149       O  
ATOM   1764  OE2 GLU A1031      19.297   0.180 219.231  1.00159.82           O  
ANISOU 1764  OE2 GLU A1031    23098  19317  18310   -380    931     68       O  
ATOM   1765  N   GLY A1032      20.714   2.837 215.101  1.00119.36           N  
ANISOU 1765  N   GLY A1032    17223  14838  13293   -484    390    145       N  
ATOM   1766  CA  GLY A1032      19.957   2.496 213.899  1.00119.28           C  
ANISOU 1766  CA  GLY A1032    17066  14856  13399   -475    392     97       C  
ATOM   1767  C   GLY A1032      20.736   1.689 212.880  1.00123.17           C  
ANISOU 1767  C   GLY A1032    17469  15496  13832   -407    297    105       C  
ATOM   1768  O   GLY A1032      21.902   1.352 213.117  1.00122.83           O  
ANISOU 1768  O   GLY A1032    17477  15530  13663   -370    232    149       O  
ATOM   1769  N   VAL A1033      20.087   1.370 211.732  1.00119.44           N  
ANISOU 1769  N   VAL A1033    16859  15070  13454   -383    284     50       N  
ATOM   1770  CA  VAL A1033      20.710   0.603 210.640  1.00118.90           C  
ANISOU 1770  CA  VAL A1033    16693  15141  13342   -319    198     49       C  
ATOM   1771  C   VAL A1033      21.772   1.445 209.944  1.00121.49           C  
ANISOU 1771  C   VAL A1033    16958  15623  13580   -308     74    136       C  
ATOM   1772  O   VAL A1033      21.537   2.625 209.683  1.00121.52           O  
ANISOU 1772  O   VAL A1033    16925  15638  13610   -334     57    168       O  
ATOM   1773  CB  VAL A1033      19.719  -0.065 209.642  1.00123.02           C  
ANISOU 1773  CB  VAL A1033    17084  15672  13986   -284    218    -59       C  
ATOM   1774  CG1 VAL A1033      18.916  -1.162 210.324  1.00123.43           C  
ANISOU 1774  CG1 VAL A1033    17198  15562  14136   -299    374   -163       C  
ATOM   1775  CG2 VAL A1033      18.790   0.947 208.982  1.00122.88           C  
ANISOU 1775  CG2 VAL A1033    16958  15672  14059   -282    185    -94       C  
ATOM   1776  N   THR A1034      22.949   0.861 209.687  1.00116.44           N  
ANISOU 1776  N   THR A1034    16315  15086  12842   -271      4    170       N  
ATOM   1777  CA  THR A1034      24.046   1.609 209.080  1.00115.53           C  
ANISOU 1777  CA  THR A1034    16142  15096  12657   -270    -86    235       C  
ATOM   1778  C   THR A1034      24.382   1.162 207.663  1.00117.67           C  
ANISOU 1778  C   THR A1034    16302  15492  12915   -212   -152    238       C  
ATOM   1779  O   THR A1034      24.365  -0.033 207.357  1.00116.95           O  
ANISOU 1779  O   THR A1034    16190  15424  12821   -170   -158    198       O  
ATOM   1780  CB  THR A1034      25.284   1.604 209.982  1.00124.96           C  
ANISOU 1780  CB  THR A1034    17414  16313  13754   -280   -122    258       C  
ATOM   1781  OG1 THR A1034      25.544   0.275 210.430  1.00127.79           O  
ANISOU 1781  OG1 THR A1034    17840  16655  14058   -228   -116    231       O  
ATOM   1782  CG2 THR A1034      25.135   2.520 211.173  1.00123.28           C  
ANISOU 1782  CG2 THR A1034    17290  16011  13540   -335    -80    263       C  
ATOM   1783  N   PHE A1035      24.702   2.155 206.808  1.00113.12           N  
ANISOU 1783  N   PHE A1035    15666  14988  12327   -206   -187    289       N  
ATOM   1784  CA  PHE A1035      25.103   2.012 205.409  1.00112.24           C  
ANISOU 1784  CA  PHE A1035    15470  14991  12184   -143   -242    309       C  
ATOM   1785  C   PHE A1035      26.449   2.720 205.222  1.00116.83           C  
ANISOU 1785  C   PHE A1035    16050  15631  12708   -170   -258    369       C  
ATOM   1786  O   PHE A1035      26.626   3.840 205.702  1.00116.39           O  
ANISOU 1786  O   PHE A1035    16026  15531  12665   -223   -216    399       O  
ATOM   1787  CB  PHE A1035      24.030   2.595 204.481  1.00113.78           C  
ANISOU 1787  CB  PHE A1035    15616  15193  12422    -84   -240    300       C  
ATOM   1788  CG  PHE A1035      22.694   1.894 204.570  1.00114.96           C  
ANISOU 1788  CG  PHE A1035    15731  15290  12658    -57   -224    199       C  
ATOM   1789  CD1 PHE A1035      22.431   0.764 203.805  1.00117.68           C  
ANISOU 1789  CD1 PHE A1035    15996  15697  13018      8   -260    124       C  
ATOM   1790  CD2 PHE A1035      21.691   2.372 205.407  1.00116.73           C  
ANISOU 1790  CD2 PHE A1035    15991  15396  12964   -103   -161    163       C  
ATOM   1791  CE1 PHE A1035      21.195   0.114 203.889  1.00118.58           C  
ANISOU 1791  CE1 PHE A1035    16058  15754  13242     25   -226     -4       C  
ATOM   1792  CE2 PHE A1035      20.455   1.722 205.486  1.00119.44           C  
ANISOU 1792  CE2 PHE A1035    16289  15676  13416    -87   -127     42       C  
ATOM   1793  CZ  PHE A1035      20.215   0.600 204.725  1.00117.59           C  
ANISOU 1793  CZ  PHE A1035    15966  15504  13210    -24   -156    -49       C  
ATOM   1794  N   MET A1036      27.405   2.052 204.566  1.00114.56           N  
ANISOU 1794  N   MET A1036    15720  15436  12372   -140   -305    373       N  
ATOM   1795  CA  MET A1036      28.758   2.570 204.378  1.00115.41           C  
ANISOU 1795  CA  MET A1036    15810  15593  12448   -170   -309    400       C  
ATOM   1796  C   MET A1036      29.181   2.688 202.915  1.00119.98           C  
ANISOU 1796  C   MET A1036    16338  16246  13002   -117   -309    439       C  
ATOM   1797  O   MET A1036      28.779   1.885 202.072  1.00119.54           O  
ANISOU 1797  O   MET A1036    16250  16244  12926    -47   -347    431       O  
ATOM   1798  CB  MET A1036      29.753   1.678 205.143  1.00118.15           C  
ANISOU 1798  CB  MET A1036    16162  15970  12758   -185   -362    355       C  
ATOM   1799  CG  MET A1036      31.137   2.274 205.325  1.00122.98           C  
ANISOU 1799  CG  MET A1036    16744  16618  13364   -230   -369    336       C  
ATOM   1800  SD  MET A1036      32.252   1.088 206.116  1.00128.01           S  
ANISOU 1800  SD  MET A1036    17382  17311  13943   -205   -462    265       S  
ATOM   1801  CE  MET A1036      33.755   1.431 205.270  1.00125.15           C  
ANISOU 1801  CE  MET A1036    16915  17031  13603   -229   -471    235       C  
ATOM   1802  N   PHE A1037      30.021   3.693 202.640  1.00117.27           N  
ANISOU 1802  N   PHE A1037    15994  15899  12665   -152   -252    470       N  
ATOM   1803  CA  PHE A1037      30.654   3.959 201.360  1.00117.72           C  
ANISOU 1803  CA  PHE A1037    16032  16000  12697   -111   -214    511       C  
ATOM   1804  C   PHE A1037      32.142   4.177 201.643  1.00122.17           C  
ANISOU 1804  C   PHE A1037    16558  16574  13289   -187   -185    473       C  
ATOM   1805  O   PHE A1037      32.479   4.929 202.557  1.00121.62           O  
ANISOU 1805  O   PHE A1037    16490  16454  13267   -264   -146    438       O  
ATOM   1806  CB  PHE A1037      30.032   5.181 200.678  1.00120.31           C  
ANISOU 1806  CB  PHE A1037    16414  16276  13022    -66   -121    582       C  
ATOM   1807  CG  PHE A1037      30.592   5.435 199.298  1.00123.02           C  
ANISOU 1807  CG  PHE A1037    16775  16647  13319      5    -60    636       C  
ATOM   1808  CD1 PHE A1037      30.189   4.664 198.212  1.00126.34           C  
ANISOU 1808  CD1 PHE A1037    17190  17143  13670    121   -124    650       C  
ATOM   1809  CD2 PHE A1037      31.550   6.422 199.088  1.00126.27           C  
ANISOU 1809  CD2 PHE A1037    17211  17003  13762    -45     74    660       C  
ATOM   1810  CE1 PHE A1037      30.728   4.882 196.940  1.00128.03           C  
ANISOU 1810  CE1 PHE A1037    17443  17378  13825    199    -61    703       C  
ATOM   1811  CE2 PHE A1037      32.088   6.640 197.817  1.00129.91           C  
ANISOU 1811  CE2 PHE A1037    17713  17467  14179     24    161    713       C  
ATOM   1812  CZ  PHE A1037      31.673   5.868 196.752  1.00127.97           C  
ANISOU 1812  CZ  PHE A1037    17482  17299  13844    151     89    742       C  
ATOM   1813  N   ILE A1038      33.027   3.496 200.888  1.00119.51           N  
ANISOU 1813  N   ILE A1038    16175  16304  12931   -166   -208    461       N  
ATOM   1814  CA  ILE A1038      34.486   3.576 201.075  1.00119.85           C  
ANISOU 1814  CA  ILE A1038    16158  16363  13017   -232   -189    395       C  
ATOM   1815  C   ILE A1038      35.239   3.822 199.729  1.00123.75           C  
ANISOU 1815  C   ILE A1038    16639  16863  13515   -213    -97    425       C  
ATOM   1816  O   ILE A1038      36.465   3.688 199.655  1.00123.89           O  
ANISOU 1816  O   ILE A1038    16592  16900  13580   -261    -79    357       O  
ATOM   1817  CB  ILE A1038      34.991   2.324 201.872  1.00122.59           C  
ANISOU 1817  CB  ILE A1038    16460  16776  13342   -233   -319    318       C  
ATOM   1818  CG1 ILE A1038      36.430   2.503 202.425  1.00123.58           C  
ANISOU 1818  CG1 ILE A1038    16512  16922  13522   -295   -329    209       C  
ATOM   1819  CG2 ILE A1038      34.853   1.017 201.078  1.00123.06           C  
ANISOU 1819  CG2 ILE A1038    16504  16908  13347   -163   -387    342       C  
ATOM   1820  CD1 ILE A1038      36.562   3.328 203.653  1.00130.26           C  
ANISOU 1820  CD1 ILE A1038    17358  17724  14412   -354   -320    139       C  
ATOM   1821  N   GLY A1039      34.499   4.231 198.705  1.00119.83           N  
ANISOU 1821  N   GLY A1039    16213  16345  12971   -135    -33    518       N  
ATOM   1822  CA  GLY A1039      35.062   4.515 197.392  1.00120.29           C  
ANISOU 1822  CA  GLY A1039    16302  16392  13009    -90     74    565       C  
ATOM   1823  C   GLY A1039      35.605   5.921 197.227  1.00124.44           C  
ANISOU 1823  C   GLY A1039    16875  16807  13600   -138    271    582       C  
ATOM   1824  O   GLY A1039      35.434   6.771 198.105  1.00123.58           O  
ANISOU 1824  O   GLY A1039    16771  16633  13551   -204    321    561       O  
ATOM   1825  N   ARG A1040      36.269   6.164 196.083  1.00122.00           N  
ANISOU 1825  N   ARG A1040    16607  16465  13284   -106    402    615       N  
ATOM   1826  CA  ARG A1040      36.842   7.458 195.718  1.00123.20           C  
ANISOU 1826  CA  ARG A1040    16823  16486  13503   -143    641    633       C  
ATOM   1827  C   ARG A1040      35.740   8.371 195.172  1.00127.30           C  
ANISOU 1827  C   ARG A1040    17497  16937  13935    -24    735    762       C  
ATOM   1828  O   ARG A1040      34.871   7.913 194.425  1.00126.57           O  
ANISOU 1828  O   ARG A1040    17473  16906  13712    122    646    840       O  
ATOM   1829  CB  ARG A1040      37.979   7.275 194.686  1.00124.69           C  
ANISOU 1829  CB  ARG A1040    17013  16648  13715   -146    764    617       C  
ATOM   1830  CG  ARG A1040      38.674   8.573 194.269  1.00137.64           C  
ANISOU 1830  CG  ARG A1040    18724  18125  15447   -191   1059    619       C  
ATOM   1831  CD  ARG A1040      40.171   8.414 194.096  1.00150.03           C  
ANISOU 1831  CD  ARG A1040    20194  19659  17153   -302   1168    493       C  
ATOM   1832  NE  ARG A1040      40.909   9.508 194.738  1.00160.63           N  
ANISOU 1832  NE  ARG A1040    21477  20877  18677   -439   1364    378       N  
ATOM   1833  CZ  ARG A1040      41.236  10.655 194.146  1.00176.10           C  
ANISOU 1833  CZ  ARG A1040    23542  22664  20705   -450   1673    406       C  
ATOM   1834  NH1 ARG A1040      40.896  10.880 192.881  1.00165.04           N  
ANISOU 1834  NH1 ARG A1040    22334  21192  19181   -313   1818    561       N  
ATOM   1835  NH2 ARG A1040      41.905  11.585 194.813  1.00162.05           N  
ANISOU 1835  NH2 ARG A1040    21680  20777  19114   -589   1849    271       N  
ATOM   1836  N   PHE A1041      35.781   9.660 195.547  1.00124.40           N  
ANISOU 1836  N   PHE A1041    17178  16446  13643    -79    913    771       N  
ATOM   1837  CA  PHE A1041      34.816  10.655 195.088  1.00124.70           C  
ANISOU 1837  CA  PHE A1041    17372  16402  13605     37   1026    893       C  
ATOM   1838  C   PHE A1041      35.135  11.043 193.639  1.00130.12           C  
ANISOU 1838  C   PHE A1041    18216  17015  14210    165   1216    990       C  
ATOM   1839  O   PHE A1041      36.080  11.797 193.385  1.00130.47           O  
ANISOU 1839  O   PHE A1041    18300  16929  14345     99   1464    975       O  
ATOM   1840  CB  PHE A1041      34.797  11.880 196.026  1.00126.75           C  
ANISOU 1840  CB  PHE A1041    17630  16548  13982    -73   1167    865       C  
ATOM   1841  CG  PHE A1041      34.021  11.756 197.321  1.00126.97           C  
ANISOU 1841  CG  PHE A1041    17578  16626  14040   -138   1000    819       C  
ATOM   1842  CD1 PHE A1041      34.004  10.560 198.036  1.00128.56           C  
ANISOU 1842  CD1 PHE A1041    17659  16950  14239   -183    769    738       C  
ATOM   1843  CD2 PHE A1041      33.369  12.855 197.864  1.00129.28           C  
ANISOU 1843  CD2 PHE A1041    17924  16827  14368   -157   1096    854       C  
ATOM   1844  CE1 PHE A1041      33.302  10.453 199.240  1.00128.25           C  
ANISOU 1844  CE1 PHE A1041    17571  16935  14223   -237    644    698       C  
ATOM   1845  CE2 PHE A1041      32.683  12.751 199.077  1.00130.93           C  
ANISOU 1845  CE2 PHE A1041    18068  17070  14609   -223    957    808       C  
ATOM   1846  CZ  PHE A1041      32.654  11.551 199.756  1.00127.64           C  
ANISOU 1846  CZ  PHE A1041    17546  16768  14181   -260    736    731       C  
ATOM   1847  N   ASP A1042      34.378  10.453 192.689  1.00127.23           N  
ANISOU 1847  N   ASP A1042    17933  16732  13676    352   1102   1071       N  
ATOM   1848  CA  ASP A1042      34.531  10.672 191.246  1.00128.50           C  
ANISOU 1848  CA  ASP A1042    18269  16844  13711    521   1246   1172       C  
ATOM   1849  C   ASP A1042      33.227  10.491 190.454  1.00131.35           C  
ANISOU 1849  C   ASP A1042    18746  17286  13874    768   1113   1262       C  
ATOM   1850  O   ASP A1042      32.282   9.844 190.923  1.00129.49           O  
ANISOU 1850  O   ASP A1042    18415  17171  13615    792    879   1219       O  
ATOM   1851  CB  ASP A1042      35.667   9.797 190.653  1.00130.67           C  
ANISOU 1851  CB  ASP A1042    18485  17155  14009    472   1254   1121       C  
ATOM   1852  CG  ASP A1042      35.467   8.287 190.724  1.00141.29           C  
ANISOU 1852  CG  ASP A1042    19690  18683  15312    477    971   1060       C  
ATOM   1853  OD1 ASP A1042      34.394   7.805 190.295  1.00141.70           O  
ANISOU 1853  OD1 ASP A1042    19778  18835  15227    636    809   1101       O  
ATOM   1854  OD2 ASP A1042      36.403   7.584 191.174  1.00146.77           O  
ANISOU 1854  OD2 ASP A1042    20236  19416  16114    329    920    959       O  
ATOM   1855  N   ARG A1043      33.213  11.031 189.229  1.00128.87           N  
ANISOU 1855  N   ARG A1043    18643  16903  13420    961   1271   1371       N  
ATOM   1856  CA  ARG A1043      32.087  10.950 188.307  1.00129.10           C  
ANISOU 1856  CA  ARG A1043    18804  17009  13239   1239   1158   1445       C  
ATOM   1857  C   ARG A1043      32.370   9.909 187.219  1.00131.79           C  
ANISOU 1857  C   ARG A1043    19160  17457  13458   1358   1064   1440       C  
ATOM   1858  O   ARG A1043      33.375  10.010 186.506  1.00131.98           O  
ANISOU 1858  O   ARG A1043    19283  17395  13468   1358   1254   1480       O  
ATOM   1859  CB  ARG A1043      31.806  12.328 187.674  1.00132.39           C  
ANISOU 1859  CB  ARG A1043    19481  17271  13548   1418   1401   1580       C  
ATOM   1860  CG  ARG A1043      31.235  13.365 188.639  1.00146.30           C  
ANISOU 1860  CG  ARG A1043    21245  18944  15400   1349   1469   1595       C  
ATOM   1861  CD  ARG A1043      31.419  14.792 188.141  1.00164.55           C  
ANISOU 1861  CD  ARG A1043    23807  21052  17663   1455   1802   1723       C  
ATOM   1862  NE  ARG A1043      32.812  15.242 188.231  1.00180.82           N  
ANISOU 1862  NE  ARG A1043    25878  22948  19880   1264   2101   1707       N  
ATOM   1863  CZ  ARG A1043      33.261  16.409 187.775  1.00201.97           C  
ANISOU 1863  CZ  ARG A1043    28767  25413  22559   1312   2459   1799       C  
ATOM   1864  NH1 ARG A1043      32.438  17.258 187.171  1.00193.70           N  
ANISOU 1864  NH1 ARG A1043    27965  24293  21340   1565   2561   1935       N  
ATOM   1865  NH2 ARG A1043      34.544  16.725 187.896  1.00190.64           N  
ANISOU 1865  NH2 ARG A1043    27303  23831  21302   1117   2728   1744       N  
ATOM   1866  N   GLY A1044      31.491   8.912 187.128  1.00126.71           N  
ANISOU 1866  N   GLY A1044    18411  16991  12744   1450    785   1376       N  
ATOM   1867  CA  GLY A1044      31.545   7.861 186.114  1.00126.12           C  
ANISOU 1867  CA  GLY A1044    18330  17041  12547   1579    661   1352       C  
ATOM   1868  C   GLY A1044      32.358   6.613 186.396  1.00126.94           C  
ANISOU 1868  C   GLY A1044    18242  17227  12762   1393    563   1257       C  
ATOM   1869  O   GLY A1044      32.552   5.801 185.485  1.00126.40           O  
ANISOU 1869  O   GLY A1044    18179  17246  12601   1488    496   1244       O  
ATOM   1870  N   GLN A1045      32.838   6.436 187.642  1.00121.24           N  
ANISOU 1870  N   GLN A1045    17355  16481  12229   1142    551   1187       N  
ATOM   1871  CA  GLN A1045      33.622   5.255 188.009  1.00119.33           C  
ANISOU 1871  CA  GLN A1045    16936  16315  12089    977    454   1095       C  
ATOM   1872  C   GLN A1045      33.104   4.576 189.284  1.00120.63           C  
ANISOU 1872  C   GLN A1045    16914  16557  12362    845    266    997       C  
ATOM   1873  O   GLN A1045      32.625   3.444 189.199  1.00119.00           O  
ANISOU 1873  O   GLN A1045    16605  16477  12133    877     86    931       O  
ATOM   1874  CB  GLN A1045      35.126   5.573 188.090  1.00121.09           C  
ANISOU 1874  CB  GLN A1045    17160  16421  12427    815    657   1093       C  
ATOM   1875  CG  GLN A1045      35.796   5.748 186.735  1.00143.51           C  
ANISOU 1875  CG  GLN A1045    20155  19202  15172    926    826   1164       C  
ATOM   1876  CD  GLN A1045      37.012   6.633 186.824  1.00169.54           C  
ANISOU 1876  CD  GLN A1045    23506  22319  18594    793   1112   1171       C  
ATOM   1877  OE1 GLN A1045      38.088   6.209 187.261  1.00166.39           O  
ANISOU 1877  OE1 GLN A1045    22968  21906  18345    610   1139   1079       O  
ATOM   1878  NE2 GLN A1045      36.867   7.887 186.406  1.00163.25           N  
ANISOU 1878  NE2 GLN A1045    22910  21374  17744    891   1340   1268       N  
ATOM   1879  N   LYS A1046      33.179   5.267 190.453  1.00116.33           N  
ANISOU 1879  N   LYS A1046    16335  15930  11935    703    322    982       N  
ATOM   1880  CA  LYS A1046      32.747   4.744 191.763  1.00114.01           C  
ANISOU 1880  CA  LYS A1046    15898  15681  11739    579    177    898       C  
ATOM   1881  C   LYS A1046      31.285   5.070 192.109  1.00115.99           C  
ANISOU 1881  C   LYS A1046    16167  15948  11958    667     89    899       C  
ATOM   1882  O   LYS A1046      30.739   4.479 193.047  1.00114.49           O  
ANISOU 1882  O   LYS A1046    15871  15797  11831    595    -35    826       O  
ATOM   1883  CB  LYS A1046      33.697   5.186 192.893  1.00116.03           C  
ANISOU 1883  CB  LYS A1046    16092  15856  12140    379    264    855       C  
ATOM   1884  CG  LYS A1046      35.134   4.671 192.759  1.00130.31           C  
ANISOU 1884  CG  LYS A1046    17831  17668  14014    275    310    804       C  
ATOM   1885  CD  LYS A1046      35.290   3.195 193.114  1.00139.06           C  
ANISOU 1885  CD  LYS A1046    18808  18895  15134    235    126    726       C  
ATOM   1886  CE  LYS A1046      36.678   2.699 192.801  1.00151.37           C  
ANISOU 1886  CE  LYS A1046    20305  20462  16746    159    169    678       C  
ATOM   1887  NZ  LYS A1046      36.841   1.264 193.144  1.00161.13           N  
ANISOU 1887  NZ  LYS A1046    21425  21808  17990    130     -1    609       N  
ATOM   1888  N   GLY A1047      30.677   5.980 191.338  1.00112.27           N  
ANISOU 1888  N   GLY A1047    15837  15436  11385    831    162    978       N  
ATOM   1889  CA  GLY A1047      29.277   6.378 191.449  1.00111.49           C  
ANISOU 1889  CA  GLY A1047    15765  15353  11243    952     83    976       C  
ATOM   1890  C   GLY A1047      28.785   6.886 192.790  1.00112.70           C  
ANISOU 1890  C   GLY A1047    15869  15440  11510    823     83    949       C  
ATOM   1891  O   GLY A1047      27.689   6.515 193.219  1.00111.62           O  
ANISOU 1891  O   GLY A1047    15664  15352  11394    852    -49    882       O  
ATOM   1892  N   VAL A1048      29.576   7.762 193.446  1.00107.62           N  
ANISOU 1892  N   VAL A1048    15259  14683  10951    681    242    987       N  
ATOM   1893  CA  VAL A1048      29.233   8.408 194.719  1.00105.76           C  
ANISOU 1893  CA  VAL A1048    14991  14372  10820    555    267    967       C  
ATOM   1894  C   VAL A1048      28.086   9.413 194.481  1.00109.61           C  
ANISOU 1894  C   VAL A1048    15584  14810  11252    693    303   1027       C  
ATOM   1895  O   VAL A1048      27.262   9.611 195.369  1.00108.48           O  
ANISOU 1895  O   VAL A1048    15398  14647  11171    645    247    990       O  
ATOM   1896  CB  VAL A1048      30.479   9.030 195.420  1.00109.21           C  
ANISOU 1896  CB  VAL A1048    15413  14713  11369    371    422    961       C  
ATOM   1897  CG1 VAL A1048      31.178  10.061 194.541  1.00110.43           C  
ANISOU 1897  CG1 VAL A1048    15700  14763  11497    420    652   1046       C  
ATOM   1898  CG2 VAL A1048      30.141   9.609 196.794  1.00108.42           C  
ANISOU 1898  CG2 VAL A1048    15269  14553  11374    239    428    923       C  
ATOM   1899  N   ASP A1049      28.014   9.995 193.258  1.00107.27           N  
ANISOU 1899  N   ASP A1049    15435  14494  10829    882    392   1116       N  
ATOM   1900  CA  ASP A1049      26.976  10.941 192.831  1.00108.02           C  
ANISOU 1900  CA  ASP A1049    15657  14550  10837   1066    423   1180       C  
ATOM   1901  C   ASP A1049      25.594  10.290 192.859  1.00110.35           C  
ANISOU 1901  C   ASP A1049    15866  14957  11106   1180    199   1090       C  
ATOM   1902  O   ASP A1049      24.614  10.939 193.233  1.00109.75           O  
ANISOU 1902  O   ASP A1049    15809  14845  11044   1232    183   1087       O  
ATOM   1903  CB  ASP A1049      27.296  11.533 191.439  1.00111.85           C  
ANISOU 1903  CB  ASP A1049    16339  14996  11162   1276    563   1293       C  
ATOM   1904  CG  ASP A1049      27.506  10.530 190.314  1.00124.83           C  
ANISOU 1904  CG  ASP A1049    17985  16759  12684   1415    458   1273       C  
ATOM   1905  OD1 ASP A1049      28.351   9.615 190.478  1.00125.34           O  
ANISOU 1905  OD1 ASP A1049    17937  16871  12817   1269    421   1218       O  
ATOM   1906  OD2 ASP A1049      26.853  10.681 189.253  1.00131.21           O  
ANISOU 1906  OD2 ASP A1049    18916  17615  13322   1681    416   1311       O  
ATOM   1907  N   VAL A1050      25.537   8.994 192.494  1.00105.98           N  
ANISOU 1907  N   VAL A1050    15204  14532  10531   1208     38   1001       N  
ATOM   1908  CA  VAL A1050      24.335   8.157 192.502  1.00105.28           C  
ANISOU 1908  CA  VAL A1050    14997  14553  10450   1294   -166    873       C  
ATOM   1909  C   VAL A1050      23.913   8.001 193.972  1.00106.70           C  
ANISOU 1909  C   VAL A1050    15059  14685  10795   1095   -196    798       C  
ATOM   1910  O   VAL A1050      22.735   8.183 194.293  1.00106.82           O  
ANISOU 1910  O   VAL A1050    15037  14700  10849   1151   -268    730       O  
ATOM   1911  CB  VAL A1050      24.587   6.779 191.814  1.00109.08           C  
ANISOU 1911  CB  VAL A1050    15386  15168  10892   1337   -291    793       C  
ATOM   1912  CG1 VAL A1050      23.319   5.931 191.756  1.00108.81           C  
ANISOU 1912  CG1 VAL A1050    15215  15240  10887   1429   -479    630       C  
ATOM   1913  CG2 VAL A1050      25.163   6.955 190.416  1.00110.28           C  
ANISOU 1913  CG2 VAL A1050    15673  15354  10876   1519   -239    877       C  
ATOM   1914  N   LEU A1051      24.891   7.711 194.862  1.00100.28           N  
ANISOU 1914  N   LEU A1051    14199  13825  10077    875   -136    805       N  
ATOM   1915  CA  LEU A1051      24.644   7.556 196.292  1.00 98.00           C  
ANISOU 1915  CA  LEU A1051    13829  13482   9923    695   -150    745       C  
ATOM   1916  C   LEU A1051      24.180   8.859 196.928  1.00101.79           C  
ANISOU 1916  C   LEU A1051    14379  13851  10446    663    -53    797       C  
ATOM   1917  O   LEU A1051      23.200   8.831 197.663  1.00102.13           O  
ANISOU 1917  O   LEU A1051    14373  13869  10564    633   -106    730       O  
ATOM   1918  CB  LEU A1051      25.857   6.969 197.032  1.00 96.59           C  
ANISOU 1918  CB  LEU A1051    13600  13294   9807    509   -122    736       C  
ATOM   1919  CG  LEU A1051      25.653   6.634 198.513  1.00 99.25           C  
ANISOU 1919  CG  LEU A1051    13873  13584  10255    348   -148    669       C  
ATOM   1920  CD1 LEU A1051      24.619   5.540 198.709  1.00 98.56           C  
ANISOU 1920  CD1 LEU A1051    13701  13543  10204    379   -265    560       C  
ATOM   1921  CD2 LEU A1051      26.941   6.223 199.140  1.00100.76           C  
ANISOU 1921  CD2 LEU A1051    14036  13772  10477    208   -122    663       C  
ATOM   1922  N   LEU A1052      24.830   9.996 196.611  1.00 97.36           N  
ANISOU 1922  N   LEU A1052    13934  13214   9846    674    103    908       N  
ATOM   1923  CA  LEU A1052      24.439  11.298 197.149  1.00 96.91           C  
ANISOU 1923  CA  LEU A1052    13951  13043   9829    648    220    964       C  
ATOM   1924  C   LEU A1052      23.069  11.727 196.636  1.00101.20           C  
ANISOU 1924  C   LEU A1052    14540  13599  10314    843    159    963       C  
ATOM   1925  O   LEU A1052      22.342  12.415 197.354  1.00100.32           O  
ANISOU 1925  O   LEU A1052    14433  13414  10268    806    186    959       O  
ATOM   1926  CB  LEU A1052      25.496  12.377 196.885  1.00 97.70           C  
ANISOU 1926  CB  LEU A1052    14161  13043   9916    613    433   1070       C  
ATOM   1927  CG  LEU A1052      26.873  12.184 197.535  1.00101.70           C  
ANISOU 1927  CG  LEU A1052    14606  13523  10512    409    510   1042       C  
ATOM   1928  CD1 LEU A1052      27.845  13.233 197.049  1.00103.23           C  
ANISOU 1928  CD1 LEU A1052    14904  13612  10706    398    743   1121       C  
ATOM   1929  CD2 LEU A1052      26.800  12.198 199.057  1.00101.97           C  
ANISOU 1929  CD2 LEU A1052    14551  13521  10672    219    481    970       C  
ATOM   1930  N   LYS A1053      22.693  11.279 195.422  1.00 99.31           N  
ANISOU 1930  N   LYS A1053    14324  13458   9951   1058     64    951       N  
ATOM   1931  CA  LYS A1053      21.373  11.576 194.864  1.00100.26           C  
ANISOU 1931  CA  LYS A1053    14469  13618  10007   1278    -30    914       C  
ATOM   1932  C   LYS A1053      20.308  10.667 195.482  1.00104.70           C  
ANISOU 1932  C   LYS A1053    14862  14240  10679   1237   -199    744       C  
ATOM   1933  O   LYS A1053      19.191  11.130 195.715  1.00104.67           O  
ANISOU 1933  O   LYS A1053    14842  14214  10713   1310   -243    690       O  
ATOM   1934  CB  LYS A1053      21.360  11.530 193.324  1.00103.06           C  
ANISOU 1934  CB  LYS A1053    14926  14059  10174   1554    -69    951       C  
ATOM   1935  CG  LYS A1053      20.155  12.235 192.696  1.00109.12           C  
ANISOU 1935  CG  LYS A1053    15771  14848  10842   1823   -132    941       C  
ATOM   1936  CD  LYS A1053      20.104  13.739 193.001  1.00115.42           C  
ANISOU 1936  CD  LYS A1053    16724  15499  11633   1833     51   1074       C  
ATOM   1937  CE  LYS A1053      18.705  14.289 192.896  1.00121.52           C  
ANISOU 1937  CE  LYS A1053    17507  16286  12378   2030    -45   1018       C  
ATOM   1938  NZ  LYS A1053      18.638  15.711 193.310  1.00127.43           N  
ANISOU 1938  NZ  LYS A1053    18392  16882  13142   2012    140   1144       N  
ATOM   1939  N   ALA A1054      20.657   9.386 195.765  1.00101.05           N  
ANISOU 1939  N   ALA A1054    14276  13839  10279   1120   -277    655       N  
ATOM   1940  CA  ALA A1054      19.751   8.426 196.400  1.00100.73           C  
ANISOU 1940  CA  ALA A1054    14082  13828  10362   1060   -392    488       C  
ATOM   1941  C   ALA A1054      19.402   8.926 197.804  1.00105.96           C  
ANISOU 1941  C   ALA A1054    14735  14365  11162    878   -319    483       C  
ATOM   1942  O   ALA A1054      18.218   8.996 198.127  1.00106.68           O  
ANISOU 1942  O   ALA A1054    14765  14433  11335    910   -369    379       O  
ATOM   1943  CB  ALA A1054      20.388   7.048 196.462  1.00100.53           C  
ANISOU 1943  CB  ALA A1054    13961  13870  10365    967   -445    422       C  
ATOM   1944  N   ILE A1055      20.425   9.363 198.595  1.00102.24           N  
ANISOU 1944  N   ILE A1055    14322  13809  10714    702   -197    587       N  
ATOM   1945  CA  ILE A1055      20.299   9.957 199.940  1.00101.42           C  
ANISOU 1945  CA  ILE A1055    14230  13586  10719    529   -115    598       C  
ATOM   1946  C   ILE A1055      19.342  11.158 199.842  1.00107.91           C  
ANISOU 1946  C   ILE A1055    15109  14347  11547    624    -78    626       C  
ATOM   1947  O   ILE A1055      18.436  11.288 200.670  1.00107.50           O  
ANISOU 1947  O   ILE A1055    15015  14229  11601    562    -86    555       O  
ATOM   1948  CB  ILE A1055      21.699  10.381 200.500  1.00103.57           C  
ANISOU 1948  CB  ILE A1055    14557  13804  10990    371      3    694       C  
ATOM   1949  CG1 ILE A1055      22.596   9.162 200.798  1.00102.84           C  
ANISOU 1949  CG1 ILE A1055    14401  13768  10905    274    -47    648       C  
ATOM   1950  CG2 ILE A1055      21.575  11.275 201.741  1.00103.74           C  
ANISOU 1950  CG2 ILE A1055    14608  13706  11104    225     98    712       C  
ATOM   1951  CD1 ILE A1055      24.116   9.459 200.790  1.00106.81           C  
ANISOU 1951  CD1 ILE A1055    14939  14265  11378    189     40    720       C  
ATOM   1952  N   GLU A1056      19.535  12.006 198.799  1.00106.46           N  
ANISOU 1952  N   GLU A1056    15030  14176  11242    787    -29    728       N  
ATOM   1953  CA  GLU A1056      18.727  13.192 198.512  1.00107.73           C  
ANISOU 1953  CA  GLU A1056    15275  14286  11373    925     14    776       C  
ATOM   1954  C   GLU A1056      17.252  12.866 198.276  1.00111.92           C  
ANISOU 1954  C   GLU A1056    15722  14870  11934   1074   -135    635       C  
ATOM   1955  O   GLU A1056      16.386  13.591 198.765  1.00111.64           O  
ANISOU 1955  O   GLU A1056    15692  14761  11963   1081   -114    617       O  
ATOM   1956  CB  GLU A1056      19.288  13.949 197.306  1.00110.59           C  
ANISOU 1956  CB  GLU A1056    15789  14656  11573   1105    101    911       C  
ATOM   1957  CG  GLU A1056      20.222  15.079 197.687  1.00123.39           C  
ANISOU 1957  CG  GLU A1056    17525  16148  13209    986    321   1049       C  
ATOM   1958  CD  GLU A1056      20.128  16.319 196.819  1.00148.45           C  
ANISOU 1958  CD  GLU A1056    20880  19260  16264   1183    456   1179       C  
ATOM   1959  OE1 GLU A1056      19.215  16.398 195.964  1.00143.36           O  
ANISOU 1959  OE1 GLU A1056    20283  18676  15512   1437    357   1164       O  
ATOM   1960  OE2 GLU A1056      20.969  17.225 197.010  1.00144.24           O  
ANISOU 1960  OE2 GLU A1056    20444  18612  15748   1092    668   1285       O  
ATOM   1961  N   ILE A1057      16.965  11.783 197.532  1.00108.57           N  
ANISOU 1961  N   ILE A1057    15207  14572  11474   1192   -283    518       N  
ATOM   1962  CA  ILE A1057      15.579  11.408 197.262  1.00108.86           C  
ANISOU 1962  CA  ILE A1057    15132  14670  11561   1337   -430    340       C  
ATOM   1963  C   ILE A1057      14.988  10.664 198.470  1.00111.52           C  
ANISOU 1963  C   ILE A1057    15326  14946  12100   1135   -443    191       C  
ATOM   1964  O   ILE A1057      13.772  10.699 198.651  1.00112.20           O  
ANISOU 1964  O   ILE A1057    15325  15018  12289   1189   -505     45       O  
ATOM   1965  CB  ILE A1057      15.348  10.690 195.898  1.00112.82           C  
ANISOU 1965  CB  ILE A1057    15589  15334  11945   1584   -584    246       C  
ATOM   1966  CG1 ILE A1057      15.725   9.203 195.929  1.00112.18           C  
ANISOU 1966  CG1 ILE A1057    15375  15328  11919   1482   -650    136       C  
ATOM   1967  CG2 ILE A1057      16.043  11.423 194.737  1.00114.44           C  
ANISOU 1967  CG2 ILE A1057    15976  15577  11930   1786   -539    414       C  
ATOM   1968  CD1 ILE A1057      14.733   8.346 195.159  1.00121.48           C  
ANISOU 1968  CD1 ILE A1057    16404  16639  13113   1668   -826    -89       C  
ATOM   1969  N   LEU A1058      15.845  10.041 199.312  1.00106.13           N  
ANISOU 1969  N   LEU A1058    14632  14218  11475    912   -375    225       N  
ATOM   1970  CA  LEU A1058      15.422   9.344 200.530  1.00105.00           C  
ANISOU 1970  CA  LEU A1058    14401  13993  11501    723   -350    112       C  
ATOM   1971  C   LEU A1058      15.045  10.356 201.601  1.00110.55           C  
ANISOU 1971  C   LEU A1058    15160  14554  12290    604   -248    160       C  
ATOM   1972  O   LEU A1058      14.140  10.099 202.389  1.00109.61           O  
ANISOU 1972  O   LEU A1058    14972  14357  12316    527   -239     36       O  
ATOM   1973  CB  LEU A1058      16.532   8.430 201.073  1.00103.61           C  
ANISOU 1973  CB  LEU A1058    14229  13816  11324    559   -310    151       C  
ATOM   1974  CG  LEU A1058      16.771   7.106 200.355  1.00107.97           C  
ANISOU 1974  CG  LEU A1058    14693  14481  11848    619   -398     62       C  
ATOM   1975  CD1 LEU A1058      18.104   6.520 200.744  1.00106.96           C  
ANISOU 1975  CD1 LEU A1058    14606  14358  11677    487   -352    149       C  
ATOM   1976  CD2 LEU A1058      15.662   6.115 200.619  1.00110.56           C  
ANISOU 1976  CD2 LEU A1058    14886  14797  12326    612   -440   -151       C  
ATOM   1977  N   SER A1059      15.741  11.513 201.610  1.00109.42           N  
ANISOU 1977  N   SER A1059    15140  14369  12065    587   -155    332       N  
ATOM   1978  CA  SER A1059      15.582  12.639 202.536  1.00110.17           C  
ANISOU 1978  CA  SER A1059    15303  14335  12224    475    -41    403       C  
ATOM   1979  C   SER A1059      14.121  13.007 202.830  1.00116.80           C  
ANISOU 1979  C   SER A1059    16089  15114  13176    522    -68    291       C  
ATOM   1980  O   SER A1059      13.789  13.284 203.984  1.00115.68           O  
ANISOU 1980  O   SER A1059    15950  14854  13151    365      9    273       O  
ATOM   1981  CB  SER A1059      16.358  13.849 202.020  1.00114.99           C  
ANISOU 1981  CB  SER A1059    16041  14929  12720    528     59    577       C  
ATOM   1982  OG  SER A1059      16.171  15.012 202.809  1.00126.41           O  
ANISOU 1982  OG  SER A1059    17548  16254  14230    436    178    640       O  
ATOM   1983  N   SER A1060      13.258  12.981 201.790  1.00116.73           N  
ANISOU 1983  N   SER A1060    16029  15190  13132    746   -181    203       N  
ATOM   1984  CA  SER A1060      11.823  13.296 201.851  1.00118.24           C  
ANISOU 1984  CA  SER A1060    16147  15349  13429    835   -234     64       C  
ATOM   1985  C   SER A1060      10.965  12.235 202.572  1.00123.44           C  
ANISOU 1985  C   SER A1060    16656  15963  14281    725   -265   -153       C  
ATOM   1986  O   SER A1060       9.866  12.560 203.031  1.00123.84           O  
ANISOU 1986  O   SER A1060    16648  15935  14470    715   -257   -268       O  
ATOM   1987  CB  SER A1060      11.274  13.550 200.448  1.00123.21           C  
ANISOU 1987  CB  SER A1060    16769  16103  13941   1141   -364     19       C  
ATOM   1988  OG  SER A1060      11.248  12.369 199.662  1.00131.09           O  
ANISOU 1988  OG  SER A1060    17663  17236  14910   1244   -494   -113       O  
ATOM   1989  N   LYS A1061      11.459  10.980 202.663  1.00119.96           N  
ANISOU 1989  N   LYS A1061    16159  15563  13858    644   -281   -212       N  
ATOM   1990  CA  LYS A1061      10.757   9.852 203.287  1.00119.93           C  
ANISOU 1990  CA  LYS A1061    16030  15504  14034    543   -274   -416       C  
ATOM   1991  C   LYS A1061      10.946   9.746 204.810  1.00124.20           C  
ANISOU 1991  C   LYS A1061    16633  15877  14681    295   -124   -379       C  
ATOM   1992  O   LYS A1061      11.934  10.246 205.352  1.00123.16           O  
ANISOU 1992  O   LYS A1061    16626  15708  14461    189    -51   -198       O  
ATOM   1993  CB  LYS A1061      11.143   8.531 202.596  1.00122.22           C  
ANISOU 1993  CB  LYS A1061    16238  15911  14289    595   -349   -502       C  
ATOM   1994  CG  LYS A1061      10.272   8.169 201.392  1.00138.11           C  
ANISOU 1994  CG  LYS A1061    18105  18055  16314    821   -501   -699       C  
ATOM   1995  CD  LYS A1061      10.594   8.962 200.122  1.00148.58           C  
ANISOU 1995  CD  LYS A1061    19500  19522  17432   1059   -610   -586       C  
ATOM   1996  CE  LYS A1061      11.502   8.220 199.178  1.00159.44           C  
ANISOU 1996  CE  LYS A1061    20884  21036  18661   1140   -676   -538       C  
ATOM   1997  NZ  LYS A1061      11.681   8.967 197.905  1.00170.32           N  
ANISOU 1997  NZ  LYS A1061    22345  22535  19834   1397   -768   -445       N  
ATOM   1998  N   LYS A1062       9.984   9.090 205.491  1.00121.86           N  
ANISOU 1998  N   LYS A1062    16250  15476  14576    213    -73   -568       N  
ATOM   1999  CA  LYS A1062       9.988   8.863 206.942  1.00121.28           C  
ANISOU 1999  CA  LYS A1062    16247  15227  14608      3     79   -562       C  
ATOM   2000  C   LYS A1062      11.022   7.792 207.314  1.00124.46           C  
ANISOU 2000  C   LYS A1062    16708  15636  14943    -87    122   -506       C  
ATOM   2001  O   LYS A1062      11.618   7.852 208.391  1.00123.57           O  
ANISOU 2001  O   LYS A1062    16719  15427  14805   -227    222   -403       O  
ATOM   2002  CB  LYS A1062       8.584   8.437 207.416  1.00124.86           C  
ANISOU 2002  CB  LYS A1062    16591  15554  15298    -36    142   -802       C  
ATOM   2003  CG  LYS A1062       8.367   8.524 208.928  1.00141.48           C  
ANISOU 2003  CG  LYS A1062    18796  17448  17514   -233    318   -789       C  
ATOM   2004  CD  LYS A1062       8.356   7.150 209.593  1.00151.75           C  
ANISOU 2004  CD  LYS A1062    20106  18642  18908   -335    439   -897       C  
ATOM   2005  CE  LYS A1062       8.104   7.255 211.077  1.00162.76           C  
ANISOU 2005  CE  LYS A1062    21630  19817  20393   -505    624   -882       C  
ATOM   2006  NZ  LYS A1062       7.889   5.922 211.699  1.00172.86           N  
ANISOU 2006  NZ  LYS A1062    22933  20964  21781   -580    774  -1007       N  
ATOM   2007  N   GLU A1063      11.225   6.819 206.411  1.00120.97           N  
ANISOU 2007  N   GLU A1063    16179  15315  14470      7     41   -583       N  
ATOM   2008  CA  GLU A1063      12.151   5.693 206.556  1.00119.99           C  
ANISOU 2008  CA  GLU A1063    16090  15218  14283    -46     65   -549       C  
ATOM   2009  C   GLU A1063      13.627   6.130 206.600  1.00123.12           C  
ANISOU 2009  C   GLU A1063    16611  15682  14487    -74     44   -323       C  
ATOM   2010  O   GLU A1063      14.482   5.353 207.038  1.00122.22           O  
ANISOU 2010  O   GLU A1063    16555  15565  14318   -140     78   -275       O  
ATOM   2011  CB  GLU A1063      11.916   4.672 205.435  1.00121.85           C  
ANISOU 2011  CB  GLU A1063    16181  15577  14539     76    -26   -698       C  
ATOM   2012  CG  GLU A1063      10.548   4.008 205.479  1.00132.26           C  
ANISOU 2012  CG  GLU A1063    17351  16820  16080     83     17   -967       C  
ATOM   2013  CD  GLU A1063       9.449   4.636 204.639  1.00150.52           C  
ANISOU 2013  CD  GLU A1063    19524  19200  18467    232    -93  -1119       C  
ATOM   2014  OE1 GLU A1063       9.361   5.884 204.581  1.00132.77           O  
ANISOU 2014  OE1 GLU A1063    17334  16962  16152    279   -137  -1009       O  
ATOM   2015  OE2 GLU A1063       8.660   3.866 204.047  1.00150.33           O  
ANISOU 2015  OE2 GLU A1063    19327  19217  18573    309   -133  -1362       O  
ATOM   2016  N   PHE A1064      13.912   7.379 206.159  1.00119.28           N  
ANISOU 2016  N   PHE A1064    16165  15249  13909    -19      0   -197       N  
ATOM   2017  CA  PHE A1064      15.241   7.995 206.140  1.00118.13           C  
ANISOU 2017  CA  PHE A1064    16119  15153  13611    -47      2     -8       C  
ATOM   2018  C   PHE A1064      15.779   8.233 207.546  1.00120.69           C  
ANISOU 2018  C   PHE A1064    16551  15362  13942   -212    104     64       C  
ATOM   2019  O   PHE A1064      16.990   8.135 207.752  1.00120.10           O  
ANISOU 2019  O   PHE A1064    16535  15330  13769   -257    105    158       O  
ATOM   2020  CB  PHE A1064      15.213   9.305 205.338  1.00120.36           C  
ANISOU 2020  CB  PHE A1064    16422  15486  13821     59    -28     85       C  
ATOM   2021  CG  PHE A1064      16.526  10.045 205.226  1.00121.49           C  
ANISOU 2021  CG  PHE A1064    16659  15664  13839     30      7    259       C  
ATOM   2022  CD1 PHE A1064      17.584   9.514 204.497  1.00124.31           C  
ANISOU 2022  CD1 PHE A1064    17016  16130  14087     75    -37    311       C  
ATOM   2023  CD2 PHE A1064      16.692  11.290 205.819  1.00123.37           C  
ANISOU 2023  CD2 PHE A1064    16974  15819  14082    -45     97    354       C  
ATOM   2024  CE1 PHE A1064      18.793  10.207 204.384  1.00124.96           C  
ANISOU 2024  CE1 PHE A1064    17170  16229  14080     42     15    444       C  
ATOM   2025  CE2 PHE A1064      17.898  11.984 205.699  1.00125.87           C  
ANISOU 2025  CE2 PHE A1064    17358  16156  14311    -77    153    483       C  
ATOM   2026  CZ  PHE A1064      18.939  11.440 204.982  1.00123.81           C  
ANISOU 2026  CZ  PHE A1064    17092  15997  13954    -35    115    522       C  
ATOM   2027  N   GLN A1065      14.882   8.530 208.510  1.00116.39           N  
ANISOU 2027  N   GLN A1065    16031  14677  13517   -294    185      5       N  
ATOM   2028  CA  GLN A1065      15.245   8.774 209.911  1.00115.23           C  
ANISOU 2028  CA  GLN A1065    15996  14411  13373   -436    282     58       C  
ATOM   2029  C   GLN A1065      15.637   7.481 210.629  1.00116.44           C  
ANISOU 2029  C   GLN A1065    16202  14524  13515   -486    320     15       C  
ATOM   2030  O   GLN A1065      16.326   7.532 211.647  1.00115.31           O  
ANISOU 2030  O   GLN A1065    16169  14330  13314   -565    367     75       O  
ATOM   2031  CB  GLN A1065      14.124   9.522 210.669  1.00117.08           C  
ANISOU 2031  CB  GLN A1065    16249  14499  13736   -501    368     10       C  
ATOM   2032  CG  GLN A1065      13.641  10.843 210.023  1.00140.05           C  
ANISOU 2032  CG  GLN A1065    19118  17433  16661   -437    341     49       C  
ATOM   2033  CD  GLN A1065      14.732  11.804 209.571  1.00163.64           C  
ANISOU 2033  CD  GLN A1065    22150  20508  19518   -414    322    206       C  
ATOM   2034  OE1 GLN A1065      14.805  12.186 208.396  1.00159.03           O  
ANISOU 2034  OE1 GLN A1065    21528  20023  18872   -285    260    244       O  
ATOM   2035  NE2 GLN A1065      15.599  12.224 210.487  1.00157.48           N  
ANISOU 2035  NE2 GLN A1065    21455  19686  18695   -530    386    288       N  
ATOM   2036  N   GLU A1066      15.224   6.331 210.076  1.00112.28           N  
ANISOU 2036  N   GLU A1066    15600  14022  13038   -428    301    -95       N  
ATOM   2037  CA  GLU A1066      15.511   4.994 210.602  1.00111.72           C  
ANISOU 2037  CA  GLU A1066    15580  13906  12963   -454    356   -142       C  
ATOM   2038  C   GLU A1066      16.932   4.509 210.262  1.00113.18           C  
ANISOU 2038  C   GLU A1066    15789  14222  12991   -420    277    -48       C  
ATOM   2039  O   GLU A1066      17.433   3.581 210.909  1.00112.68           O  
ANISOU 2039  O   GLU A1066    15808  14120  12884   -439    321    -49       O  
ATOM   2040  CB  GLU A1066      14.470   3.984 210.081  1.00113.85           C  
ANISOU 2040  CB  GLU A1066    15737  14146  13374   -409    385   -318       C  
ATOM   2041  CG  GLU A1066      13.077   4.172 210.661  1.00126.07           C  
ANISOU 2041  CG  GLU A1066    17265  15528  15110   -461    498   -453       C  
ATOM   2042  CD  GLU A1066      11.981   3.333 210.034  1.00147.00           C  
ANISOU 2042  CD  GLU A1066    19760  18160  17932   -412    521   -669       C  
ATOM   2043  OE1 GLU A1066      12.143   2.092 209.956  1.00139.42           O  
ANISOU 2043  OE1 GLU A1066    18789  17191  16994   -405    572   -740       O  
ATOM   2044  OE2 GLU A1066      10.946   3.918 209.639  1.00140.46           O  
ANISOU 2044  OE2 GLU A1066    18817  17326  17226   -376    492   -780       O  
ATOM   2045  N   MET A1067      17.575   5.135 209.257  1.00107.84           N  
ANISOU 2045  N   MET A1067    15053  13690  12230   -361    173     31       N  
ATOM   2046  CA  MET A1067      18.905   4.744 208.784  1.00106.53           C  
ANISOU 2046  CA  MET A1067    14891  13651  11936   -329    101    105       C  
ATOM   2047  C   MET A1067      20.009   5.798 208.951  1.00105.77           C  
ANISOU 2047  C   MET A1067    14841  13600  11745   -365     80    224       C  
ATOM   2048  O   MET A1067      19.752   7.000 208.965  1.00104.63           O  
ANISOU 2048  O   MET A1067    14703  13429  11623   -385    104    267       O  
ATOM   2049  CB  MET A1067      18.851   4.262 207.323  1.00109.63           C  
ANISOU 2049  CB  MET A1067    15167  14173  12314   -220     14     70       C  
ATOM   2050  CG  MET A1067      17.959   5.080 206.402  1.00114.41           C  
ANISOU 2050  CG  MET A1067    15694  14815  12960   -138    -27     45       C  
ATOM   2051  SD  MET A1067      17.483   4.068 204.981  1.00119.61           S  
ANISOU 2051  SD  MET A1067    16214  15596  13637      1   -118    -75       S  
ATOM   2052  CE  MET A1067      16.379   5.160 204.157  1.00117.14           C  
ANISOU 2052  CE  MET A1067    15840  15312  13358    121   -172   -116       C  
ATOM   2053  N   ARG A1068      21.251   5.307 209.065  1.00100.02           N  
ANISOU 2053  N   ARG A1068    14140  12940  10922   -370     43    262       N  
ATOM   2054  CA  ARG A1068      22.480   6.081 209.222  1.00 98.98           C  
ANISOU 2054  CA  ARG A1068    14031  12862  10717   -406     25    335       C  
ATOM   2055  C   ARG A1068      23.394   5.808 208.029  1.00102.17           C  
ANISOU 2055  C   ARG A1068    14366  13399  11056   -345    -42    367       C  
ATOM   2056  O   ARG A1068      23.464   4.671 207.551  1.00101.30           O  
ANISOU 2056  O   ARG A1068    14223  13342  10924   -292    -87    334       O  
ATOM   2057  CB  ARG A1068      23.203   5.715 210.534  1.00 97.96           C  
ANISOU 2057  CB  ARG A1068    13991  12694  10535   -456     32    321       C  
ATOM   2058  CG  ARG A1068      22.291   5.521 211.753  1.00105.26           C  
ANISOU 2058  CG  ARG A1068    15015  13474  11504   -496    108    280       C  
ATOM   2059  CD  ARG A1068      21.843   6.823 212.390  1.00112.31           C  
ANISOU 2059  CD  ARG A1068    15940  14284  12448   -570    168    299       C  
ATOM   2060  NE  ARG A1068      20.746   6.602 213.333  1.00121.48           N  
ANISOU 2060  NE  ARG A1068    17188  15295  13675   -604    256    254       N  
ATOM   2061  CZ  ARG A1068      19.457   6.727 213.030  1.00136.23           C  
ANISOU 2061  CZ  ARG A1068    19017  17085  15658   -609    311    215       C  
ATOM   2062  NH1 ARG A1068      19.086   7.089 211.808  1.00124.87           N  
ANISOU 2062  NH1 ARG A1068    17463  15719  14263   -563    267    220       N  
ATOM   2063  NH2 ARG A1068      18.529   6.498 213.949  1.00121.39           N  
ANISOU 2063  NH2 ARG A1068    17219  15053  13852   -650    411    162       N  
ATOM   2064  N   PHE A1069      24.084   6.859 207.547  1.00 98.65           N  
ANISOU 2064  N   PHE A1069    13902  12992  10588   -354    -28    427       N  
ATOM   2065  CA  PHE A1069      24.979   6.812 206.391  1.00 98.14           C  
ANISOU 2065  CA  PHE A1069    13788  13030  10469   -302    -58    464       C  
ATOM   2066  C   PHE A1069      26.384   7.294 206.731  1.00101.47           C  
ANISOU 2066  C   PHE A1069    14209  13478  10868   -366    -39    475       C  
ATOM   2067  O   PHE A1069      26.544   8.319 207.396  1.00100.92           O  
ANISOU 2067  O   PHE A1069    14162  13351  10833   -437     25    481       O  
ATOM   2068  CB  PHE A1069      24.396   7.629 205.216  1.00100.30           C  
ANISOU 2068  CB  PHE A1069    14048  13316  10745   -223    -30    516       C  
ATOM   2069  CG  PHE A1069      23.063   7.126 204.704  1.00101.90           C  
ANISOU 2069  CG  PHE A1069    14221  13521  10974   -134    -73    471       C  
ATOM   2070  CD1 PHE A1069      23.002   6.147 203.718  1.00104.91           C  
ANISOU 2070  CD1 PHE A1069    14547  13994  11320    -38   -146    438       C  
ATOM   2071  CD2 PHE A1069      21.868   7.629 205.213  1.00103.89           C  
ANISOU 2071  CD2 PHE A1069    14489  13686  11300   -145    -41    442       C  
ATOM   2072  CE1 PHE A1069      21.767   5.668 203.261  1.00105.92           C  
ANISOU 2072  CE1 PHE A1069    14623  14133  11490     47   -190    358       C  
ATOM   2073  CE2 PHE A1069      20.635   7.144 204.761  1.00106.73           C  
ANISOU 2073  CE2 PHE A1069    14795  14049  11707    -62    -84    363       C  
ATOM   2074  CZ  PHE A1069      20.593   6.169 203.788  1.00105.00           C  
ANISOU 2074  CZ  PHE A1069    14510  13928  11457     36   -160    312       C  
ATOM   2075  N   ILE A1070      27.401   6.527 206.290  1.00 98.22           N  
ANISOU 2075  N   ILE A1070    13758  13153  10409   -342    -92    460       N  
ATOM   2076  CA  ILE A1070      28.829   6.829 206.455  1.00 98.30           C  
ANISOU 2076  CA  ILE A1070    13736  13202  10411   -392    -85    437       C  
ATOM   2077  C   ILE A1070      29.442   6.849 205.056  1.00102.89           C  
ANISOU 2077  C   ILE A1070    14274  13847  10974   -344    -65    475       C  
ATOM   2078  O   ILE A1070      29.563   5.799 204.426  1.00102.17           O  
ANISOU 2078  O   ILE A1070    14156  13824  10839   -283   -132    472       O  
ATOM   2079  CB  ILE A1070      29.572   5.847 207.408  1.00101.01           C  
ANISOU 2079  CB  ILE A1070    14081  13583  10715   -403   -170    363       C  
ATOM   2080  CG1 ILE A1070      28.852   5.697 208.763  1.00101.05           C  
ANISOU 2080  CG1 ILE A1070    14168  13511  10716   -423   -176    336       C  
ATOM   2081  CG2 ILE A1070      31.015   6.296 207.615  1.00102.05           C  
ANISOU 2081  CG2 ILE A1070    14157  13758  10860   -451   -170    302       C  
ATOM   2082  CD1 ILE A1070      28.855   4.286 209.318  1.00107.41           C  
ANISOU 2082  CD1 ILE A1070    15023  14329  11460   -370   -243    302       C  
ATOM   2083  N   ILE A1071      29.782   8.046 204.555  1.00100.72           N  
ANISOU 2083  N   ILE A1071    14001  13535  10732   -366     45    512       N  
ATOM   2084  CA  ILE A1071      30.343   8.223 203.211  1.00101.19           C  
ANISOU 2084  CA  ILE A1071    14052  13626  10770   -313    103    559       C  
ATOM   2085  C   ILE A1071      31.833   8.616 203.294  1.00106.76           C  
ANISOU 2085  C   ILE A1071    14704  14334  11528   -392    172    501       C  
ATOM   2086  O   ILE A1071      32.169   9.799 203.391  1.00106.35           O  
ANISOU 2086  O   ILE A1071    14659  14208  11541   -451    309    499       O  
ATOM   2087  CB  ILE A1071      29.474   9.184 202.338  1.00104.44           C  
ANISOU 2087  CB  ILE A1071    14535  13983  11167   -235    199    653       C  
ATOM   2088  CG1 ILE A1071      27.982   8.825 202.402  1.00103.99           C  
ANISOU 2088  CG1 ILE A1071    14501  13926  11085   -161    118    667       C  
ATOM   2089  CG2 ILE A1071      29.940   9.218 200.886  1.00106.22           C  
ANISOU 2089  CG2 ILE A1071    14785  14238  11337   -144    257    711       C  
ATOM   2090  CD1 ILE A1071      27.169   9.826 203.074  1.00109.74           C  
ANISOU 2090  CD1 ILE A1071    15272  14562  11863   -198    180    684       C  
ATOM   2091  N   ILE A1072      32.713   7.598 203.270  1.00105.05           N  
ANISOU 2091  N   ILE A1072    14424  14197  11293   -394     83    438       N  
ATOM   2092  CA  ILE A1072      34.172   7.745 203.343  1.00106.51           C  
ANISOU 2092  CA  ILE A1072    14531  14400  11538   -461    121    346       C  
ATOM   2093  C   ILE A1072      34.775   7.773 201.941  1.00111.54           C  
ANISOU 2093  C   ILE A1072    15164  15042  12173   -424    211    388       C  
ATOM   2094  O   ILE A1072      34.436   6.943 201.096  1.00110.40           O  
ANISOU 2094  O   ILE A1072    15044  14951  11952   -337    151    449       O  
ATOM   2095  CB  ILE A1072      34.842   6.652 204.229  1.00109.78           C  
ANISOU 2095  CB  ILE A1072    14883  14896  11933   -471    -32    240       C  
ATOM   2096  CG1 ILE A1072      34.083   6.448 205.561  1.00109.93           C  
ANISOU 2096  CG1 ILE A1072    14950  14901  11919   -472   -119    222       C  
ATOM   2097  CG2 ILE A1072      36.328   6.977 204.473  1.00111.97           C  
ANISOU 2097  CG2 ILE A1072    15057  15191  12296   -541     -1    104       C  
ATOM   2098  CD1 ILE A1072      34.319   5.100 206.276  1.00117.78           C  
ANISOU 2098  CD1 ILE A1072    15945  15965  12843   -424   -269    165       C  
ATOM   2099  N   GLY A1073      35.672   8.729 201.727  1.00109.85           N  
ANISOU 2099  N   GLY A1073    14921  14764  12052   -492    369    342       N  
ATOM   2100  CA  GLY A1073      36.363   8.915 200.461  1.00110.69           C  
ANISOU 2100  CA  GLY A1073    15040  14842  12173   -469    504    372       C  
ATOM   2101  C   GLY A1073      36.775  10.345 200.198  1.00115.81           C  
ANISOU 2101  C   GLY A1073    15719  15360  12923   -528    752    368       C  
ATOM   2102  O   GLY A1073      36.125  11.289 200.659  1.00115.00           O  
ANISOU 2102  O   GLY A1073    15668  15183  12845   -549    831    403       O  
ATOM   2103  N   LYS A1074      37.869  10.496 199.444  1.00113.87           N  
ANISOU 2103  N   LYS A1074    15445  15075  12747   -557    894    321       N  
ATOM   2104  CA  LYS A1074      38.440  11.778 199.046  1.00115.46           C  
ANISOU 2104  CA  LYS A1074    15676  15127  13064   -616   1182    302       C  
ATOM   2105  C   LYS A1074      38.393  11.847 197.526  1.00120.24           C  
ANISOU 2105  C   LYS A1074    16421  15674  13590   -506   1330    437       C  
ATOM   2106  O   LYS A1074      38.439  10.805 196.866  1.00119.17           O  
ANISOU 2106  O   LYS A1074    16291  15629  13359   -429   1205    475       O  
ATOM   2107  CB  LYS A1074      39.894  11.879 199.547  1.00119.00           C  
ANISOU 2107  CB  LYS A1074    15957  15566  13693   -754   1243     86       C  
ATOM   2108  CG  LYS A1074      40.409  13.304 199.729  1.00133.36           C  
ANISOU 2108  CG  LYS A1074    17757  17227  15685   -861   1528      0       C  
ATOM   2109  CD  LYS A1074      41.742  13.335 200.477  1.00144.98           C  
ANISOU 2109  CD  LYS A1074    19019  18718  17351   -998   1536   -267       C  
ATOM   2110  CE  LYS A1074      42.948  13.345 199.562  1.00159.75           C  
ANISOU 2110  CE  LYS A1074    20836  20519  19345  -1041   1723   -363       C  
ATOM   2111  NZ  LYS A1074      44.221  13.222 200.323  1.00170.64           N  
ANISOU 2111  NZ  LYS A1074    21980  21944  20912  -1158   1679   -656       N  
ATOM   2112  N   GLY A1075      38.284  13.057 196.986  1.00118.48           N  
ANISOU 2112  N   GLY A1075    16323  15298  13398   -488   1600    509       N  
ATOM   2113  CA  GLY A1075      38.255  13.253 195.543  1.00119.52           C  
ANISOU 2113  CA  GLY A1075    16626  15351  13436   -359   1774    644       C  
ATOM   2114  C   GLY A1075      37.679  14.573 195.090  1.00125.11           C  
ANISOU 2114  C   GLY A1075    17521  15899  14115   -283   2027    770       C  
ATOM   2115  O   GLY A1075      38.057  15.632 195.600  1.00125.65           O  
ANISOU 2115  O   GLY A1075    17569  15838  14334   -395   2240    704       O  
ATOM   2116  N   ASP A1076      36.766  14.495 194.106  1.00122.26           N  
ANISOU 2116  N   ASP A1076    17344  15550  13559    -79   2004    943       N  
ATOM   2117  CA  ASP A1076      36.066  15.601 193.447  1.00123.74           C  
ANISOU 2117  CA  ASP A1076    17756  15604  13655     68   2214   1096       C  
ATOM   2118  C   ASP A1076      35.565  16.690 194.411  1.00128.58           C  
ANISOU 2118  C   ASP A1076    18362  16132  14360    -11   2302   1088       C  
ATOM   2119  O   ASP A1076      34.815  16.362 195.333  1.00127.30           O  
ANISOU 2119  O   ASP A1076    18101  16078  14191    -46   2067   1059       O  
ATOM   2120  CB  ASP A1076      34.898  15.047 192.617  1.00125.20           C  
ANISOU 2120  CB  ASP A1076    18073  15896  13601    310   2027   1237       C  
ATOM   2121  CG  ASP A1076      34.767  15.648 191.235  1.00137.92           C  
ANISOU 2121  CG  ASP A1076    19947  17396  15061    527   2247   1388       C  
ATOM   2122  OD1 ASP A1076      34.709  16.893 191.131  1.00139.79           O  
ANISOU 2122  OD1 ASP A1076    20333  17458  15320    558   2523   1457       O  
ATOM   2123  OD2 ASP A1076      34.714  14.873 190.257  1.00144.55           O  
ANISOU 2123  OD2 ASP A1076    20853  18319  15752    677   2149   1436       O  
ATOM   2124  N   PRO A1077      35.959  17.979 194.228  1.00126.74           N  
ANISOU 2124  N   PRO A1077    18239  15697  14220    -41   2654   1111       N  
ATOM   2125  CA  PRO A1077      35.497  19.031 195.155  1.00126.59           C  
ANISOU 2125  CA  PRO A1077    18208  15593  14299   -124   2751   1098       C  
ATOM   2126  C   PRO A1077      33.993  19.307 195.105  1.00129.45           C  
ANISOU 2126  C   PRO A1077    18701  15989  14495     48   2630   1248       C  
ATOM   2127  O   PRO A1077      33.430  19.709 196.124  1.00128.23           O  
ANISOU 2127  O   PRO A1077    18473  15842  14408    -37   2564   1214       O  
ATOM   2128  CB  PRO A1077      36.330  20.257 194.759  1.00130.62           C  
ANISOU 2128  CB  PRO A1077    18822  15865  14943   -177   3193   1090       C  
ATOM   2129  CG  PRO A1077      37.440  19.725 193.904  1.00135.97           C  
ANISOU 2129  CG  PRO A1077    19501  16514  15647   -185   3303   1042       C  
ATOM   2130  CD  PRO A1077      36.855  18.544 193.204  1.00130.34           C  
ANISOU 2130  CD  PRO A1077    18837  15976  14710    -10   3005   1141       C  
ATOM   2131  N   GLU A1078      33.341  19.080 193.940  1.00126.19           N  
ANISOU 2131  N   GLU A1078    18476  15602  13868    296   2593   1399       N  
ATOM   2132  CA  GLU A1078      31.890  19.257 193.798  1.00125.58           C  
ANISOU 2132  CA  GLU A1078    18510  15575  13627    490   2450   1516       C  
ATOM   2133  C   GLU A1078      31.146  18.146 194.538  1.00126.24           C  
ANISOU 2133  C   GLU A1078    18414  15861  13690    454   2065   1442       C  
ATOM   2134  O   GLU A1078      30.092  18.403 195.120  1.00125.28           O  
ANISOU 2134  O   GLU A1078    18282  15766  13554    481   1950   1458       O  
ATOM   2135  CB  GLU A1078      31.440  19.383 192.323  1.00128.57           C  
ANISOU 2135  CB  GLU A1078    19146  15927  13777    793   2521   1675       C  
ATOM   2136  CG  GLU A1078      31.766  18.202 191.421  1.00140.40           C  
ANISOU 2136  CG  GLU A1078    20640  17552  15156    893   2368   1669       C  
ATOM   2137  CD  GLU A1078      31.159  18.256 190.032  1.00164.44           C  
ANISOU 2137  CD  GLU A1078    23931  20602  17945   1222   2381   1811       C  
ATOM   2138  OE1 GLU A1078      31.654  19.045 189.194  1.00158.63           O  
ANISOU 2138  OE1 GLU A1078    23423  19696  17152   1331   2697   1912       O  
ATOM   2139  OE2 GLU A1078      30.194  17.499 189.777  1.00159.42           O  
ANISOU 2139  OE2 GLU A1078    23266  20138  17167   1380   2084   1811       O  
ATOM   2140  N   LEU A1079      31.724  16.927 194.546  1.00121.02           N  
ANISOU 2140  N   LEU A1079    17614  15327  13040    387   1887   1353       N  
ATOM   2141  CA  LEU A1079      31.180  15.763 195.245  1.00118.71           C  
ANISOU 2141  CA  LEU A1079    17157  15209  12741    341   1558   1272       C  
ATOM   2142  C   LEU A1079      31.456  15.860 196.746  1.00121.83           C  
ANISOU 2142  C   LEU A1079    17384  15599  13307    111   1517   1153       C  
ATOM   2143  O   LEU A1079      30.615  15.443 197.545  1.00120.10           O  
ANISOU 2143  O   LEU A1079    17091  15456  13087     89   1320   1120       O  
ATOM   2144  CB  LEU A1079      31.743  14.446 194.669  1.00117.98           C  
ANISOU 2144  CB  LEU A1079    16994  15239  12595    362   1412   1228       C  
ATOM   2145  CG  LEU A1079      31.032  13.802 193.456  1.00122.61           C  
ANISOU 2145  CG  LEU A1079    17678  15922  12985    604   1282   1305       C  
ATOM   2146  CD1 LEU A1079      29.533  13.688 193.657  1.00122.25           C  
ANISOU 2146  CD1 LEU A1079    17634  15954  12862    727   1089   1320       C  
ATOM   2147  CD2 LEU A1079      31.348  14.510 192.165  1.00126.49           C  
ANISOU 2147  CD2 LEU A1079    18386  16307  13365    774   1514   1423       C  
ATOM   2148  N   GLU A1080      32.631  16.427 197.123  1.00119.12           N  
ANISOU 2148  N   GLU A1080    16985  15159  13115    -54   1714   1074       N  
ATOM   2149  CA  GLU A1080      33.040  16.652 198.514  1.00118.24           C  
ANISOU 2149  CA  GLU A1080    16719  15039  13167   -261   1699    939       C  
ATOM   2150  C   GLU A1080      32.086  17.647 199.169  1.00120.73           C  
ANISOU 2150  C   GLU A1080    17088  15278  13508   -270   1756    986       C  
ATOM   2151  O   GLU A1080      31.692  17.441 200.316  1.00119.28           O  
ANISOU 2151  O   GLU A1080    16802  15145  13373   -366   1608    914       O  
ATOM   2152  CB  GLU A1080      34.489  17.173 198.597  1.00120.94           C  
ANISOU 2152  CB  GLU A1080    16991  15285  13676   -409   1927    823       C  
ATOM   2153  CG  GLU A1080      35.547  16.078 198.572  1.00132.14           C  
ANISOU 2153  CG  GLU A1080    18270  16805  15132   -476   1805    700       C  
ATOM   2154  CD  GLU A1080      36.984  16.502 198.824  1.00151.33           C  
ANISOU 2154  CD  GLU A1080    20582  19159  17759   -636   1995    531       C  
ATOM   2155  OE1 GLU A1080      37.339  17.665 198.520  1.00144.69           O  
ANISOU 2155  OE1 GLU A1080    19808  18150  17019   -674   2306    534       O  
ATOM   2156  OE2 GLU A1080      37.763  15.656 199.320  1.00141.93           O  
ANISOU 2156  OE2 GLU A1080    19228  18072  16625   -718   1839    384       O  
ATOM   2157  N   GLY A1081      31.710  18.684 198.414  1.00117.51           N  
ANISOU 2157  N   GLY A1081    16851  14743  13053   -156   1975   1110       N  
ATOM   2158  CA  GLY A1081      30.778  19.725 198.829  1.00117.29           C  
ANISOU 2158  CA  GLY A1081    16901  14627  13038   -136   2060   1176       C  
ATOM   2159  C   GLY A1081      29.388  19.182 199.092  1.00119.59           C  
ANISOU 2159  C   GLY A1081    17191  15024  13222    -34   1797   1219       C  
ATOM   2160  O   GLY A1081      28.829  19.423 200.169  1.00118.69           O  
ANISOU 2160  O   GLY A1081    17012  14906  13179   -129   1731   1176       O  
ATOM   2161  N   TRP A1082      28.839  18.407 198.118  1.00115.21           N  
ANISOU 2161  N   TRP A1082    16702  14566  12508    159   1648   1285       N  
ATOM   2162  CA  TRP A1082      27.517  17.757 198.186  1.00113.69           C  
ANISOU 2162  CA  TRP A1082    16493  14481  12223    276   1396   1295       C  
ATOM   2163  C   TRP A1082      27.430  16.799 199.387  1.00114.61           C  
ANISOU 2163  C   TRP A1082    16431  14693  12421    117   1180   1171       C  
ATOM   2164  O   TRP A1082      26.396  16.748 200.059  1.00113.67           O  
ANISOU 2164  O   TRP A1082    16281  14590  12318    112   1064   1151       O  
ATOM   2165  CB  TRP A1082      27.219  17.010 196.871  1.00112.80           C  
ANISOU 2165  CB  TRP A1082    16456  14463  11940    500   1288   1349       C  
ATOM   2166  CG  TRP A1082      25.799  16.538 196.667  1.00113.37           C  
ANISOU 2166  CG  TRP A1082    16525  14633  11917    666   1068   1346       C  
ATOM   2167  CD1 TRP A1082      24.707  16.831 197.433  1.00115.74           C  
ANISOU 2167  CD1 TRP A1082    16787  14922  12266    650    987   1319       C  
ATOM   2168  CD2 TRP A1082      25.317  15.742 195.572  1.00113.54           C  
ANISOU 2168  CD2 TRP A1082    16578  14772  11790    880    914   1353       C  
ATOM   2169  NE1 TRP A1082      23.584  16.235 196.908  1.00115.15           N  
ANISOU 2169  NE1 TRP A1082    16702  14951  12099    833    791   1292       N  
ATOM   2170  CE2 TRP A1082      23.926  15.571 195.758  1.00117.11           C  
ANISOU 2170  CE2 TRP A1082    16990  15285  12222    982    737   1308       C  
ATOM   2171  CE3 TRP A1082      25.928  15.148 194.451  1.00115.25           C  
ANISOU 2171  CE3 TRP A1082    16846  15049  11895    996    908   1379       C  
ATOM   2172  CZ2 TRP A1082      23.136  14.831 194.867  1.00116.67           C  
ANISOU 2172  CZ2 TRP A1082    16928  15356  12045   1198    550   1269       C  
ATOM   2173  CZ3 TRP A1082      25.146  14.411 193.573  1.00116.86           C  
ANISOU 2173  CZ3 TRP A1082    17057  15381  11964   1211    720   1357       C  
ATOM   2174  CH2 TRP A1082      23.769  14.258 193.784  1.00117.26           C  
ANISOU 2174  CH2 TRP A1082    17053  15499  12004   1312    540   1294       C  
ATOM   2175  N   ALA A1083      28.528  16.073 199.667  1.00109.20           N  
ANISOU 2175  N   ALA A1083    15642  14060  11790     -7   1143   1085       N  
ATOM   2176  CA  ALA A1083      28.636  15.141 200.786  1.00106.98           C  
ANISOU 2176  CA  ALA A1083    15219  13861  11569   -139    962    972       C  
ATOM   2177  C   ALA A1083      28.677  15.871 202.126  1.00108.51           C  
ANISOU 2177  C   ALA A1083    15363  13982  11883   -303   1022    911       C  
ATOM   2178  O   ALA A1083      28.067  15.399 203.087  1.00106.25           O  
ANISOU 2178  O   ALA A1083    15025  13731  11615   -353    880    860       O  
ATOM   2179  CB  ALA A1083      29.877  14.289 200.624  1.00107.68           C  
ANISOU 2179  CB  ALA A1083    15225  14018  11670   -199    923    900       C  
ATOM   2180  N   ARG A1084      29.397  17.018 202.190  1.00105.81           N  
ANISOU 2180  N   ARG A1084    15041  13530  11630   -383   1248    907       N  
ATOM   2181  CA  ARG A1084      29.514  17.836 203.402  1.00105.55           C  
ANISOU 2181  CA  ARG A1084    14956  13425  11722   -538   1329    836       C  
ATOM   2182  C   ARG A1084      28.205  18.539 203.708  1.00108.75           C  
ANISOU 2182  C   ARG A1084    15437  13767  12117   -498   1344    912       C  
ATOM   2183  O   ARG A1084      27.787  18.555 204.868  1.00107.55           O  
ANISOU 2183  O   ARG A1084    15232  13614  12020   -594   1269    852       O  
ATOM   2184  CB  ARG A1084      30.683  18.835 203.323  1.00106.93           C  
ANISOU 2184  CB  ARG A1084    15112  13497  12019   -640   1586    784       C  
ATOM   2185  CG  ARG A1084      32.064  18.213 203.560  1.00117.83           C  
ANISOU 2185  CG  ARG A1084    16359  14941  13470   -742   1551    635       C  
ATOM   2186  CD  ARG A1084      32.390  17.984 205.029  1.00130.38           C  
ANISOU 2186  CD  ARG A1084    17813  16586  15138   -879   1422    478       C  
ATOM   2187  NE  ARG A1084      33.613  17.195 205.193  1.00143.99           N  
ANISOU 2187  NE  ARG A1084    19412  18398  16900   -932   1336    332       N  
ATOM   2188  CZ  ARG A1084      33.878  16.415 206.239  1.00161.83           C  
ANISOU 2188  CZ  ARG A1084    21577  20760  19153   -977   1133    212       C  
ATOM   2189  NH1 ARG A1084      33.001  16.299 207.229  1.00147.08           N  
ANISOU 2189  NH1 ARG A1084    19734  18908  17243   -983   1010    224       N  
ATOM   2190  NH2 ARG A1084      35.016  15.738 206.298  1.00153.73           N  
ANISOU 2190  NH2 ARG A1084    20440  19814  18158  -1004   1059     77       N  
ATOM   2191  N   SER A1085      27.534  19.067 202.662  1.00105.50           N  
ANISOU 2191  N   SER A1085    15156  13305  11626   -338   1433   1040       N  
ATOM   2192  CA  SER A1085      26.232  19.729 202.770  1.00105.37           C  
ANISOU 2192  CA  SER A1085    15216  13231  11587   -262   1441   1115       C  
ATOM   2193  C   SER A1085      25.183  18.785 203.364  1.00106.98           C  
ANISOU 2193  C   SER A1085    15359  13524  11764   -246   1192   1070       C  
ATOM   2194  O   SER A1085      24.446  19.186 204.266  1.00105.72           O  
ANISOU 2194  O   SER A1085    15186  13316  11666   -312   1180   1051       O  
ATOM   2195  CB  SER A1085      25.774  20.229 201.408  1.00110.89           C  
ANISOU 2195  CB  SER A1085    16073  13890  12171    -44   1541   1248       C  
ATOM   2196  OG  SER A1085      26.750  21.108 200.874  1.00125.00           O  
ANISOU 2196  OG  SER A1085    17939  15567  13987    -57   1812   1293       O  
ATOM   2197  N   LEU A1086      25.162  17.518 202.890  1.00102.38           N  
ANISOU 2197  N   LEU A1086    14737  13061  11103   -169   1014   1042       N  
ATOM   2198  CA  LEU A1086      24.255  16.475 203.368  1.00100.63           C  
ANISOU 2198  CA  LEU A1086    14451  12913  10869   -156    803    980       C  
ATOM   2199  C   LEU A1086      24.582  16.075 204.808  1.00104.88           C  
ANISOU 2199  C   LEU A1086    14907  13450  11493   -338    748    883       C  
ATOM   2200  O   LEU A1086      23.670  15.755 205.576  1.00103.53           O  
ANISOU 2200  O   LEU A1086    14717  13267  11352   -365    660    842       O  
ATOM   2201  CB  LEU A1086      24.284  15.252 202.438  1.00 99.94           C  
ANISOU 2201  CB  LEU A1086    14340  12946  10687    -33    659    967       C  
ATOM   2202  CG  LEU A1086      23.463  15.345 201.152  1.00104.78           C  
ANISOU 2202  CG  LEU A1086    15026  13591  11194    191    628   1030       C  
ATOM   2203  CD1 LEU A1086      23.939  14.347 200.148  1.00104.90           C  
ANISOU 2203  CD1 LEU A1086    15027  13714  11115    294    542   1024       C  
ATOM   2204  CD2 LEU A1086      21.983  15.109 201.408  1.00106.51           C  
ANISOU 2204  CD2 LEU A1086    15214  13823  11431    259    501    978       C  
ATOM   2205  N   GLU A1087      25.877  16.110 205.176  1.00103.14           N  
ANISOU 2205  N   GLU A1087    14641  13235  11311   -451    805    835       N  
ATOM   2206  CA  GLU A1087      26.338  15.792 206.527  1.00103.40           C  
ANISOU 2206  CA  GLU A1087    14607  13277  11404   -596    749    732       C  
ATOM   2207  C   GLU A1087      25.845  16.871 207.502  1.00109.43           C  
ANISOU 2207  C   GLU A1087    15391  13937  12251   -692    845    725       C  
ATOM   2208  O   GLU A1087      25.310  16.547 208.563  1.00107.91           O  
ANISOU 2208  O   GLU A1087    15188  13734  12078   -752    765    673       O  
ATOM   2209  CB  GLU A1087      27.873  15.687 206.556  1.00105.25           C  
ANISOU 2209  CB  GLU A1087    14775  13552  11664   -668    784    660       C  
ATOM   2210  CG  GLU A1087      28.449  15.331 207.920  1.00116.65           C  
ANISOU 2210  CG  GLU A1087    16151  15022  13147   -784    707    536       C  
ATOM   2211  CD  GLU A1087      29.879  15.768 208.179  1.00138.45           C  
ANISOU 2211  CD  GLU A1087    18830  17791  15984   -877    787    429       C  
ATOM   2212  OE1 GLU A1087      30.279  16.842 207.673  1.00134.63           O  
ANISOU 2212  OE1 GLU A1087    18346  17233  15573   -910    978    446       O  
ATOM   2213  OE2 GLU A1087      30.596  15.039 208.903  1.00129.58           O  
ANISOU 2213  OE2 GLU A1087    17642  16743  14851   -911    668    316       O  
ATOM   2214  N   GLU A1088      26.021  18.150 207.117  1.00108.69           N  
ANISOU 2214  N   GLU A1088    15335  13757  12205   -703   1035    779       N  
ATOM   2215  CA  GLU A1088      25.635  19.331 207.888  1.00109.43           C  
ANISOU 2215  CA  GLU A1088    15448  13744  12388   -794   1162    780       C  
ATOM   2216  C   GLU A1088      24.120  19.478 208.011  1.00113.92           C  
ANISOU 2216  C   GLU A1088    16073  14267  12943   -732   1115    839       C  
ATOM   2217  O   GLU A1088      23.651  20.049 208.996  1.00113.86           O  
ANISOU 2217  O   GLU A1088    16065  14190  13005   -826   1151    813       O  
ATOM   2218  CB  GLU A1088      26.255  20.596 207.273  1.00112.30           C  
ANISOU 2218  CB  GLU A1088    15846  14015  12808   -807   1408    825       C  
ATOM   2219  CG  GLU A1088      27.755  20.714 207.506  1.00126.07           C  
ANISOU 2219  CG  GLU A1088    17501  15771  14630   -922   1494    713       C  
ATOM   2220  CD  GLU A1088      28.575  21.280 206.359  1.00152.40           C  
ANISOU 2220  CD  GLU A1088    20873  19050  17982   -880   1701    756       C  
ATOM   2221  OE1 GLU A1088      28.204  22.346 205.816  1.00143.61           O  
ANISOU 2221  OE1 GLU A1088    19861  17821  16883   -830   1902    856       O  
ATOM   2222  OE2 GLU A1088      29.604  20.656 206.011  1.00150.36           O  
ANISOU 2222  OE2 GLU A1088    20552  18854  17724   -893   1675    687       O  
ATOM   2223  N   LYS A1089      23.357  18.976 207.021  1.00110.72           N  
ANISOU 2223  N   LYS A1089    15709  13903  12455   -571   1035    903       N  
ATOM   2224  CA  LYS A1089      21.893  19.052 207.028  1.00110.36           C  
ANISOU 2224  CA  LYS A1089    15697  13826  12409   -491    976    928       C  
ATOM   2225  C   LYS A1089      21.258  17.897 207.800  1.00112.05           C  
ANISOU 2225  C   LYS A1089    15859  14080  12635   -527    807    841       C  
ATOM   2226  O   LYS A1089      20.268  18.115 208.497  1.00111.20           O  
ANISOU 2226  O   LYS A1089    15758  13906  12588   -563    800    817       O  
ATOM   2227  CB  LYS A1089      21.325  19.120 205.595  1.00114.16           C  
ANISOU 2227  CB  LYS A1089    16240  14338  12797   -279    962   1008       C  
ATOM   2228  CG  LYS A1089      21.485  20.481 204.910  1.00137.37           C  
ANISOU 2228  CG  LYS A1089    19282  17190  15721   -207   1163   1117       C  
ATOM   2229  CD  LYS A1089      20.278  21.402 205.119  1.00151.52           C  
ANISOU 2229  CD  LYS A1089    21126  18894  17550   -159   1213   1156       C  
ATOM   2230  CE  LYS A1089      20.423  22.719 204.390  1.00163.35           C  
ANISOU 2230  CE  LYS A1089    22751  20297  19019    -63   1429   1275       C  
ATOM   2231  NZ  LYS A1089      19.246  23.604 204.602  1.00170.12           N  
ANISOU 2231  NZ  LYS A1089    23660  21070  19907     -4   1472   1314       N  
ATOM   2232  N   HIS A1090      21.821  16.675 207.675  1.00107.56           N  
ANISOU 2232  N   HIS A1090    15247  13607  12016   -516    691    792       N  
ATOM   2233  CA  HIS A1090      21.294  15.471 208.324  1.00106.35           C  
ANISOU 2233  CA  HIS A1090    15060  13479  11869   -536    559    711       C  
ATOM   2234  C   HIS A1090      22.216  14.926 209.411  1.00109.90           C  
ANISOU 2234  C   HIS A1090    15493  13944  12320   -657    531    647       C  
ATOM   2235  O   HIS A1090      23.401  14.687 209.160  1.00110.17           O  
ANISOU 2235  O   HIS A1090    15500  14046  12313   -667    522    639       O  
ATOM   2236  CB  HIS A1090      20.996  14.379 207.287  1.00106.85           C  
ANISOU 2236  CB  HIS A1090    15093  13637  11868   -399    442    697       C  
ATOM   2237  CG  HIS A1090      20.188  14.852 206.122  1.00110.80           C  
ANISOU 2237  CG  HIS A1090    15611  14148  12338   -240    443    744       C  
ATOM   2238  ND1 HIS A1090      18.839  15.115 206.241  1.00112.64           N  
ANISOU 2238  ND1 HIS A1090    15841  14329  12627   -192    425    712       N  
ATOM   2239  CD2 HIS A1090      20.573  15.099 204.849  1.00113.04           C  
ANISOU 2239  CD2 HIS A1090    15924  14490  12536   -107    459    812       C  
ATOM   2240  CE1 HIS A1090      18.446  15.513 205.042  1.00112.79           C  
ANISOU 2240  CE1 HIS A1090    15885  14388  12584    -17    413    757       C  
ATOM   2241  NE2 HIS A1090      19.456  15.520 204.173  1.00113.44           N  
ANISOU 2241  NE2 HIS A1090    15999  14533  12570     43    438    825       N  
ATOM   2242  N   GLY A1091      21.645  14.700 210.596  1.00104.86           N  
ANISOU 2242  N   GLY A1091    14878  13240  11724   -733    517    594       N  
ATOM   2243  CA  GLY A1091      22.351  14.169 211.758  1.00103.65           C  
ANISOU 2243  CA  GLY A1091    14739  13093  11552   -816    482    528       C  
ATOM   2244  C   GLY A1091      22.646  12.683 211.686  1.00105.60           C  
ANISOU 2244  C   GLY A1091    14980  13413  11730   -761    371    486       C  
ATOM   2245  O   GLY A1091      23.296  12.136 212.581  1.00104.96           O  
ANISOU 2245  O   GLY A1091    14926  13348  11608   -795    330    434       O  
ATOM   2246  N   ASN A1092      22.162  12.016 210.625  1.00101.01           N  
ANISOU 2246  N   ASN A1092    14368  12878  11133   -662    321    502       N  
ATOM   2247  CA  ASN A1092      22.382  10.593 210.382  1.00100.12           C  
ANISOU 2247  CA  ASN A1092    14240  12834  10967   -605    231    464       C  
ATOM   2248  C   ASN A1092      23.305  10.377 209.178  1.00104.00           C  
ANISOU 2248  C   ASN A1092    14676  13442  11399   -538    189    497       C  
ATOM   2249  O   ASN A1092      23.369   9.276 208.637  1.00103.32           O  
ANISOU 2249  O   ASN A1092    14563  13422  11274   -473    117    476       O  
ATOM   2250  CB  ASN A1092      21.053   9.845 210.226  1.00 99.30           C  
ANISOU 2250  CB  ASN A1092    14132  12685  10912   -554    213    420       C  
ATOM   2251  CG  ASN A1092      20.105  10.409 209.197  1.00110.35           C  
ANISOU 2251  CG  ASN A1092    15485  14088  12356   -476    218    437       C  
ATOM   2252  OD1 ASN A1092      20.319  11.484 208.622  1.00101.49           O  
ANISOU 2252  OD1 ASN A1092    14361  12980  11220   -453    254    505       O  
ATOM   2253  ND2 ASN A1092      19.017   9.693 208.959  1.00 99.26           N  
ANISOU 2253  ND2 ASN A1092    14044  12663  11006   -421    190    362       N  
ATOM   2254  N   VAL A1093      24.030  11.434 208.770  1.00101.08           N  
ANISOU 2254  N   VAL A1093    14292  13085  11029   -559    253    544       N  
ATOM   2255  CA  VAL A1093      24.995  11.394 207.667  1.00101.29           C  
ANISOU 2255  CA  VAL A1093    14280  13196  11009   -508    251    576       C  
ATOM   2256  C   VAL A1093      26.366  11.837 208.211  1.00106.48           C  
ANISOU 2256  C   VAL A1093    14913  13866  11678   -598    292    540       C  
ATOM   2257  O   VAL A1093      26.457  12.877 208.872  1.00105.94           O  
ANISOU 2257  O   VAL A1093    14854  13731  11666   -679    380    530       O  
ATOM   2258  CB  VAL A1093      24.535  12.204 206.410  1.00105.13           C  
ANISOU 2258  CB  VAL A1093    14783  13673  11487   -416    317    657       C  
ATOM   2259  CG1 VAL A1093      25.620  12.246 205.338  1.00105.11           C  
ANISOU 2259  CG1 VAL A1093    14768  13733  11437   -370    351    694       C  
ATOM   2260  CG2 VAL A1093      23.244  11.638 205.824  1.00104.65           C  
ANISOU 2260  CG2 VAL A1093    14720  13629  11413   -302    242    652       C  
ATOM   2261  N   LYS A1094      27.411  11.014 207.959  1.00104.38           N  
ANISOU 2261  N   LYS A1094    14603  13688  11369   -583    226    501       N  
ATOM   2262  CA  LYS A1094      28.803  11.241 208.362  1.00105.33           C  
ANISOU 2262  CA  LYS A1094    14671  13841  11508   -651    241    429       C  
ATOM   2263  C   LYS A1094      29.739  11.075 207.160  1.00110.81           C  
ANISOU 2263  C   LYS A1094    15316  14597  12189   -612    263    442       C  
ATOM   2264  O   LYS A1094      29.682  10.056 206.475  1.00109.56           O  
ANISOU 2264  O   LYS A1094    15153  14505  11970   -535    182    465       O  
ATOM   2265  CB  LYS A1094      29.215  10.273 209.491  1.00107.85           C  
ANISOU 2265  CB  LYS A1094    14990  14203  11783   -662    121    340       C  
ATOM   2266  CG  LYS A1094      29.441  10.936 210.859  1.00125.33           C  
ANISOU 2266  CG  LYS A1094    17216  16375  14029   -742    138    262       C  
ATOM   2267  CD  LYS A1094      30.822  11.596 211.018  1.00136.47           C  
ANISOU 2267  CD  LYS A1094    18533  17826  15494   -803    171    157       C  
ATOM   2268  CE  LYS A1094      31.919  10.624 211.387  1.00145.69           C  
ANISOU 2268  CE  LYS A1094    19655  19097  16605   -762     41     51       C  
ATOM   2269  NZ  LYS A1094      33.209  11.320 211.635  1.00154.71           N  
ANISOU 2269  NZ  LYS A1094    20682  20275  17825   -824     72    -92       N  
ATOM   2270  N   VAL A1095      30.585  12.076 206.897  1.00110.09           N  
ANISOU 2270  N   VAL A1095    15189  14475  12164   -669    392    421       N  
ATOM   2271  CA  VAL A1095      31.529  12.019 205.779  1.00111.72           C  
ANISOU 2271  CA  VAL A1095    15359  14714  12375   -643    451    426       C  
ATOM   2272  C   VAL A1095      32.958  12.166 206.267  1.00118.68           C  
ANISOU 2272  C   VAL A1095    16140  15621  13332   -732    474    286       C  
ATOM   2273  O   VAL A1095      33.261  13.093 207.025  1.00119.31           O  
ANISOU 2273  O   VAL A1095    16185  15647  13499   -822    558    210       O  
ATOM   2274  CB  VAL A1095      31.212  12.972 204.589  1.00116.68           C  
ANISOU 2274  CB  VAL A1095    16056  15269  13010   -592    621    537       C  
ATOM   2275  CG1 VAL A1095      29.982  12.510 203.822  1.00116.04           C  
ANISOU 2275  CG1 VAL A1095    16049  15208  12832   -459    550    645       C  
ATOM   2276  CG2 VAL A1095      31.058  14.423 205.034  1.00117.28           C  
ANISOU 2276  CG2 VAL A1095    16157  15230  13175   -667    794    542       C  
ATOM   2277  N   ILE A1096      33.833  11.236 205.853  1.00116.54           N  
ANISOU 2277  N   ILE A1096    15811  15434  13036   -704    395    236       N  
ATOM   2278  CA  ILE A1096      35.239  11.261 206.251  1.00117.74           C  
ANISOU 2278  CA  ILE A1096    15845  15624  13266   -772    395     74       C  
ATOM   2279  C   ILE A1096      36.139  11.479 205.032  1.00125.09           C  
ANISOU 2279  C   ILE A1096    16737  16537  14256   -777    530     69       C  
ATOM   2280  O   ILE A1096      36.265  10.594 204.180  1.00124.35           O  
ANISOU 2280  O   ILE A1096    16654  16498  14094   -707    470    122       O  
ATOM   2281  CB  ILE A1096      35.659  10.037 207.118  1.00120.05           C  
ANISOU 2281  CB  ILE A1096    16095  16027  13493   -738    182    -23       C  
ATOM   2282  CG1 ILE A1096      34.591   9.705 208.184  1.00119.50           C  
ANISOU 2282  CG1 ILE A1096    16111  15949  13344   -710     77     13       C  
ATOM   2283  CG2 ILE A1096      37.016  10.300 207.775  1.00121.77           C  
ANISOU 2283  CG2 ILE A1096    16181  16284  13801   -800    169   -227       C  
ATOM   2284  CD1 ILE A1096      34.591   8.297 208.684  1.00126.45           C  
ANISOU 2284  CD1 ILE A1096    17020  16909  14116   -630   -101     -5       C  
ATOM   2285  N   THR A1097      36.751  12.676 204.955  1.00124.92           N  
ANISOU 2285  N   THR A1097    16673  16424  14366   -864    732      2       N  
ATOM   2286  CA  THR A1097      37.672  13.085 203.884  1.00126.74           C  
ANISOU 2286  CA  THR A1097    16876  16596  14684   -888    923    -21       C  
ATOM   2287  C   THR A1097      39.050  12.417 204.042  1.00132.68           C  
ANISOU 2287  C   THR A1097    17476  17429  15508   -929    847   -209       C  
ATOM   2288  O   THR A1097      39.781  12.279 203.057  1.00132.42           O  
ANISOU 2288  O   THR A1097    17421  17373  15517   -927    950   -220       O  
ATOM   2289  CB  THR A1097      37.780  14.624 203.807  1.00137.43           C  
ANISOU 2289  CB  THR A1097    18245  17800  16172   -970   1201    -39       C  
ATOM   2290  OG1 THR A1097      38.049  15.165 205.105  1.00137.55           O  
ANISOU 2290  OG1 THR A1097    18156  17817  16289  -1072   1180   -200       O  
ATOM   2291  CG2 THR A1097      36.534  15.275 203.219  1.00136.14           C  
ANISOU 2291  CG2 THR A1097    18253  17546  15928   -895   1312    169       C  
ATOM   2292  N   GLU A1098      39.385  12.000 205.288  1.00130.81           N  
ANISOU 2292  N   GLU A1098    17141  17282  15278   -954    667   -359       N  
ATOM   2293  CA  GLU A1098      40.640  11.349 205.687  1.00132.00           C  
ANISOU 2293  CA  GLU A1098    17138  17529  15485   -970    549   -566       C  
ATOM   2294  C   GLU A1098      40.829   9.995 205.013  1.00136.81           C  
ANISOU 2294  C   GLU A1098    17763  18230  15990   -881    408   -503       C  
ATOM   2295  O   GLU A1098      39.864   9.250 204.820  1.00134.61           O  
ANISOU 2295  O   GLU A1098    17600  17985  15562   -795    301   -337       O  
ATOM   2296  CB  GLU A1098      40.704  11.161 207.217  1.00133.48           C  
ANISOU 2296  CB  GLU A1098    17268  17800  15649   -965    360   -709       C  
ATOM   2297  CG  GLU A1098      40.584  12.436 208.043  1.00145.37           C  
ANISOU 2297  CG  GLU A1098    18737  19234  17263  -1056    474   -804       C  
ATOM   2298  CD  GLU A1098      40.350  12.262 209.536  1.00165.92           C  
ANISOU 2298  CD  GLU A1098    21334  21912  19798  -1027    286   -901       C  
ATOM   2299  OE1 GLU A1098      39.920  11.164 209.963  1.00152.77           O  
ANISOU 2299  OE1 GLU A1098    19749  20328  17969   -923     81   -834       O  
ATOM   2300  OE2 GLU A1098      40.587  13.240 210.281  1.00164.19           O  
ANISOU 2300  OE2 GLU A1098    21037  21658  19689  -1105    358  -1048       O  
ATOM   2301  N   MET A1099      42.088   9.678 204.674  1.00136.28           N  
ANISOU 2301  N   MET A1099    17567  18198  16014   -907    415   -656       N  
ATOM   2302  CA  MET A1099      42.476   8.417 204.046  1.00136.39           C  
ANISOU 2302  CA  MET A1099    17570  18299  15953   -836    292   -628       C  
ATOM   2303  C   MET A1099      42.840   7.402 205.153  1.00140.74           C  
ANISOU 2303  C   MET A1099    18056  18987  16431   -772     28   -752       C  
ATOM   2304  O   MET A1099      43.988   7.337 205.600  1.00141.81           O  
ANISOU 2304  O   MET A1099    18040  19178  16662   -793    -28   -974       O  
ATOM   2305  CB  MET A1099      43.609   8.643 203.016  1.00140.12           C  
ANISOU 2305  CB  MET A1099    17952  18720  16567   -895    463   -718       C  
ATOM   2306  CG  MET A1099      43.120   9.262 201.697  1.00144.15           C  
ANISOU 2306  CG  MET A1099    18594  19103  17075   -897    703   -535       C  
ATOM   2307  SD  MET A1099      44.431   9.884 200.590  1.00150.39           S  
ANISOU 2307  SD  MET A1099    19306  19772  18063   -985    991   -653       S  
ATOM   2308  CE  MET A1099      43.647   9.673 198.995  1.00146.32           C  
ANISOU 2308  CE  MET A1099    19006  19191  17398   -883   1113   -369       C  
ATOM   2309  N   LEU A1100      41.815   6.660 205.629  1.00135.97           N  
ANISOU 2309  N   LEU A1100    17573  18428  15660   -684   -122   -617       N  
ATOM   2310  CA  LEU A1100      41.872   5.657 206.705  1.00135.42           C  
ANISOU 2310  CA  LEU A1100    17513  18464  15477   -592   -351   -679       C  
ATOM   2311  C   LEU A1100      42.750   4.450 206.400  1.00139.61           C  
ANISOU 2311  C   LEU A1100    17978  19092  15975   -524   -478   -745       C  
ATOM   2312  O   LEU A1100      42.827   4.013 205.249  1.00138.77           O  
ANISOU 2312  O   LEU A1100    17874  18978  15874   -527   -419   -657       O  
ATOM   2313  CB  LEU A1100      40.452   5.154 207.035  1.00134.01           C  
ANISOU 2313  CB  LEU A1100    17502  18268  15146   -524   -413   -493       C  
ATOM   2314  CG  LEU A1100      39.605   5.997 207.977  1.00138.26           C  
ANISOU 2314  CG  LEU A1100    18111  18744  15676   -553   -382   -473       C  
ATOM   2315  CD1 LEU A1100      38.833   7.049 207.220  1.00138.07           C  
ANISOU 2315  CD1 LEU A1100    18133  18612  15717   -627   -192   -348       C  
ATOM   2316  CD2 LEU A1100      38.615   5.135 208.702  1.00139.40           C  
ANISOU 2316  CD2 LEU A1100    18395  18899  15673   -464   -498   -376       C  
ATOM   2317  N   SER A1101      43.362   3.877 207.455  1.00137.20           N  
ANISOU 2317  N   SER A1101    17628  18882  15621   -446   -659   -895       N  
ATOM   2318  CA  SER A1101      44.197   2.679 207.360  1.00137.57           C  
ANISOU 2318  CA  SER A1101    17620  19029  15620   -358   -804   -970       C  
ATOM   2319  C   SER A1101      43.317   1.435 207.399  1.00140.03           C  
ANISOU 2319  C   SER A1101    18089  19362  15752   -249   -899   -790       C  
ATOM   2320  O   SER A1101      42.294   1.430 208.091  1.00138.86           O  
ANISOU 2320  O   SER A1101    18076  19178  15505   -211   -917   -692       O  
ATOM   2321  CB  SER A1101      45.221   2.635 208.491  1.00143.09           C  
ANISOU 2321  CB  SER A1101    18211  19823  16334   -292   -962  -1223       C  
ATOM   2322  OG  SER A1101      46.046   1.482 208.413  1.00152.74           O  
ANISOU 2322  OG  SER A1101    19386  21145  17505   -188  -1110  -1299       O  
ATOM   2323  N   ARG A1102      43.750   0.370 206.683  1.00136.14           N  
ANISOU 2323  N   ARG A1102    17575  18923  15231   -201   -948   -762       N  
ATOM   2324  CA  ARG A1102      43.084  -0.935 206.549  1.00134.74           C  
ANISOU 2324  CA  ARG A1102    17520  18766  14911   -105  -1015   -614       C  
ATOM   2325  C   ARG A1102      42.659  -1.582 207.877  1.00137.79           C  
ANISOU 2325  C   ARG A1102    18037  19172  15146     24  -1141   -614       C  
ATOM   2326  O   ARG A1102      41.768  -2.436 207.881  1.00136.13           O  
ANISOU 2326  O   ARG A1102    17959  18934  14832     84  -1140   -475       O  
ATOM   2327  CB  ARG A1102      43.960  -1.900 205.738  1.00135.55           C  
ANISOU 2327  CB  ARG A1102    17540  18935  15028    -75  -1060   -646       C  
ATOM   2328  N   GLU A1103      43.284  -1.160 208.994  1.00135.31           N  
ANISOU 2328  N   GLU A1103    17689  18899  14822     71  -1237   -779       N  
ATOM   2329  CA  GLU A1103      42.980  -1.640 210.346  1.00135.32           C  
ANISOU 2329  CA  GLU A1103    17835  18915  14666    214  -1353   -796       C  
ATOM   2330  C   GLU A1103      41.643  -1.042 210.800  1.00137.13           C  
ANISOU 2330  C   GLU A1103    18202  19039  14863    168  -1256   -669       C  
ATOM   2331  O   GLU A1103      40.828  -1.754 211.387  1.00136.02           O  
ANISOU 2331  O   GLU A1103    18237  18853  14591    259  -1267   -567       O  
ATOM   2332  CB  GLU A1103      44.109  -1.305 211.358  1.00138.56           C  
ANISOU 2332  CB  GLU A1103    18154  19417  15074    295  -1499  -1039       C  
ATOM   2333  CG  GLU A1103      45.528  -1.164 210.803  1.00151.26           C  
ANISOU 2333  CG  GLU A1103    19537  21112  16821    261  -1547  -1237       C  
ATOM   2334  CD  GLU A1103      46.123  -2.314 210.003  1.00175.29           C  
ANISOU 2334  CD  GLU A1103    22543  24211  19849    315  -1595  -1214       C  
ATOM   2335  OE1 GLU A1103      45.932  -3.487 210.397  1.00174.55           O  
ANISOU 2335  OE1 GLU A1103    22587  24145  19589    470  -1690  -1141       O  
ATOM   2336  OE2 GLU A1103      46.796  -2.034 208.984  1.00167.92           O  
ANISOU 2336  OE2 GLU A1103    21448  23281  19072    203  -1522  -1269       O  
ATOM   2337  N   PHE A1104      41.413   0.257 210.496  1.00133.07           N  
ANISOU 2337  N   PHE A1104    17612  18472  14477     26  -1144   -677       N  
ATOM   2338  CA  PHE A1104      40.179   0.979 210.831  1.00132.06           C  
ANISOU 2338  CA  PHE A1104    17590  18241  14344    -34  -1043   -567       C  
ATOM   2339  C   PHE A1104      39.013   0.528 209.943  1.00132.61           C  
ANISOU 2339  C   PHE A1104    17744  18240  14402    -64   -941   -368       C  
ATOM   2340  O   PHE A1104      37.897   0.368 210.441  1.00131.32           O  
ANISOU 2340  O   PHE A1104    17719  18003  14175    -42   -907   -272       O  
ATOM   2341  CB  PHE A1104      40.367   2.506 210.713  1.00134.63           C  
ANISOU 2341  CB  PHE A1104    17803  18531  14819   -169   -942   -642       C  
ATOM   2342  CG  PHE A1104      41.552   3.103 211.435  1.00138.12           C  
ANISOU 2342  CG  PHE A1104    18113  19043  15322   -165  -1019   -879       C  
ATOM   2343  CD1 PHE A1104      41.609   3.113 212.825  1.00142.39           C  
ANISOU 2343  CD1 PHE A1104    18718  19617  15767    -71  -1135   -981       C  
ATOM   2344  CD2 PHE A1104      42.583   3.707 210.727  1.00141.36           C  
ANISOU 2344  CD2 PHE A1104    18334  19479  15896   -255   -961  -1015       C  
ATOM   2345  CE1 PHE A1104      42.702   3.675 213.492  1.00145.09           C  
ANISOU 2345  CE1 PHE A1104    18919  20039  16171    -54  -1222  -1233       C  
ATOM   2346  CE2 PHE A1104      43.675   4.273 211.395  1.00146.06           C  
ANISOU 2346  CE2 PHE A1104    18778  20139  16578   -256  -1025  -1273       C  
ATOM   2347  CZ  PHE A1104      43.726   4.253 212.773  1.00145.07           C  
ANISOU 2347  CZ  PHE A1104    18701  20067  16353   -152  -1167  -1388       C  
ATOM   2348  N   VAL A1105      39.282   0.326 208.631  1.00127.40           N  
ANISOU 2348  N   VAL A1105    16996  17602  13809   -111   -892   -324       N  
ATOM   2349  CA  VAL A1105      38.312  -0.118 207.618  1.00125.40           C  
ANISOU 2349  CA  VAL A1105    16790  17306  13549   -126   -812   -167       C  
ATOM   2350  C   VAL A1105      37.769  -1.508 207.984  1.00128.19           C  
ANISOU 2350  C   VAL A1105    17260  17660  13788    -21   -868   -109       C  
ATOM   2351  O   VAL A1105      36.598  -1.794 207.729  1.00126.67           O  
ANISOU 2351  O   VAL A1105    17142  17404  13582    -23   -803     -5       O  
ATOM   2352  CB  VAL A1105      38.885  -0.068 206.171  1.00128.89           C  
ANISOU 2352  CB  VAL A1105    17122  17781  14070   -177   -756   -151       C  
ATOM   2353  CG1 VAL A1105      37.766  -0.091 205.135  1.00127.65           C  
ANISOU 2353  CG1 VAL A1105    17012  17577  13913   -193   -666     -6       C  
ATOM   2354  CG2 VAL A1105      39.760   1.165 205.959  1.00129.56           C  
ANISOU 2354  CG2 VAL A1105    17093  17858  14277   -268   -686   -249       C  
ATOM   2355  N   ARG A1106      38.621  -2.347 208.617  1.00125.62           N  
ANISOU 2355  N   ARG A1106    16947  17397  13385     79   -980   -189       N  
ATOM   2356  CA  ARG A1106      38.281  -3.688 209.105  1.00125.28           C  
ANISOU 2356  CA  ARG A1106    17034  17342  13225    198  -1017   -145       C  
ATOM   2357  C   ARG A1106      37.241  -3.584 210.227  1.00128.07           C  
ANISOU 2357  C   ARG A1106    17556  17595  13509    234   -974   -102       C  
ATOM   2358  O   ARG A1106      36.242  -4.308 210.206  1.00126.64           O  
ANISOU 2358  O   ARG A1106    17480  17336  13300    258   -897    -15       O  
ATOM   2359  CB  ARG A1106      39.540  -4.425 209.597  1.00126.93           C  
ANISOU 2359  CB  ARG A1106    17227  17644  13358    317  -1151   -253       C  
ATOM   2360  N   GLU A1107      37.456  -2.643 211.175  1.00124.94           N  
ANISOU 2360  N   GLU A1107    17177  17192  13103    228  -1008   -176       N  
ATOM   2361  CA  GLU A1107      36.537  -2.378 212.285  1.00124.88           C  
ANISOU 2361  CA  GLU A1107    17329  17084  13035    254   -963   -146       C  
ATOM   2362  C   GLU A1107      35.185  -1.894 211.746  1.00127.00           C  
ANISOU 2362  C   GLU A1107    17610  17251  13393    142   -824    -39       C  
ATOM   2363  O   GLU A1107      34.144  -2.239 212.306  1.00126.75           O  
ANISOU 2363  O   GLU A1107    17722  17113  13325    167   -749     19       O  
ATOM   2364  CB  GLU A1107      37.133  -1.345 213.262  1.00127.42           C  
ANISOU 2364  CB  GLU A1107    17630  17438  13347    256  -1033   -265       C  
ATOM   2365  CG  GLU A1107      38.184  -1.902 214.212  1.00141.47           C  
ANISOU 2365  CG  GLU A1107    19456  19302  14996    420  -1184   -388       C  
ATOM   2366  CD  GLU A1107      37.655  -2.627 215.437  1.00166.71           C  
ANISOU 2366  CD  GLU A1107    22898  22425  18017    576  -1188   -351       C  
ATOM   2367  OE1 GLU A1107      37.238  -3.800 215.302  1.00160.72           O  
ANISOU 2367  OE1 GLU A1107    22264  21616  17187    656  -1139   -258       O  
ATOM   2368  OE2 GLU A1107      37.665  -2.025 216.536  1.00164.89           O  
ANISOU 2368  OE2 GLU A1107    22746  22182  17724    623  -1227   -420       O  
ATOM   2369  N   LEU A1108      35.212  -1.130 210.636  1.00121.95           N  
ANISOU 2369  N   LEU A1108    16827  16638  12870     30   -784    -20       N  
ATOM   2370  CA  LEU A1108      34.036  -0.583 209.965  1.00120.31           C  
ANISOU 2370  CA  LEU A1108    16611  16357  12745    -55   -674     68       C  
ATOM   2371  C   LEU A1108      33.218  -1.650 209.248  1.00122.14           C  
ANISOU 2371  C   LEU A1108    16870  16563  12976    -24   -628    138       C  
ATOM   2372  O   LEU A1108      31.997  -1.658 209.389  1.00121.21           O  
ANISOU 2372  O   LEU A1108    16820  16351  12883    -39   -549    180       O  
ATOM   2373  CB  LEU A1108      34.446   0.519 208.982  1.00120.31           C  
ANISOU 2373  CB  LEU A1108    16473  16395  12845   -148   -640     65       C  
ATOM   2374  CG  LEU A1108      34.592   1.906 209.577  1.00125.62           C  
ANISOU 2374  CG  LEU A1108    17123  17035  13570   -220   -608     17       C  
ATOM   2375  CD1 LEU A1108      35.767   2.628 208.972  1.00126.20           C  
ANISOU 2375  CD1 LEU A1108    17058  17171  13723   -277   -601    -56       C  
ATOM   2376  CD2 LEU A1108      33.317   2.710 209.406  1.00128.28           C  
ANISOU 2376  CD2 LEU A1108    17502  17277  13960   -281   -502    101       C  
ATOM   2377  N   TYR A1109      33.878  -2.544 208.484  1.00117.82           N  
ANISOU 2377  N   TYR A1109    16259  16094  12412     15   -673    134       N  
ATOM   2378  CA  TYR A1109      33.212  -3.615 207.736  1.00116.75           C  
ANISOU 2378  CA  TYR A1109    16127  15948  12285     44   -631    178       C  
ATOM   2379  C   TYR A1109      32.403  -4.567 208.632  1.00120.72           C  
ANISOU 2379  C   TYR A1109    16777  16351  12741    108   -573    185       C  
ATOM   2380  O   TYR A1109      31.291  -4.950 208.266  1.00119.22           O  
ANISOU 2380  O   TYR A1109    16596  16095  12606     94   -486    206       O  
ATOM   2381  CB  TYR A1109      34.218  -4.402 206.879  1.00117.66           C  
ANISOU 2381  CB  TYR A1109    16153  16167  12385     76   -692    163       C  
ATOM   2382  CG  TYR A1109      34.749  -3.694 205.649  1.00119.02           C  
ANISOU 2382  CG  TYR A1109    16191  16410  12622     14   -699    170       C  
ATOM   2383  CD1 TYR A1109      33.913  -2.914 204.850  1.00120.62           C  
ANISOU 2383  CD1 TYR A1109    16361  16585  12883    -35   -632    219       C  
ATOM   2384  CD2 TYR A1109      36.054  -3.901 205.212  1.00120.13           C  
ANISOU 2384  CD2 TYR A1109    16245  16638  12759     21   -761    126       C  
ATOM   2385  CE1 TYR A1109      34.385  -2.297 203.691  1.00121.25           C  
ANISOU 2385  CE1 TYR A1109    16353  16713  13002    -68   -615    238       C  
ATOM   2386  CE2 TYR A1109      36.532  -3.305 204.045  1.00120.99           C  
ANISOU 2386  CE2 TYR A1109    16251  16790  12929    -33   -734    135       C  
ATOM   2387  CZ  TYR A1109      35.696  -2.499 203.290  1.00126.86           C  
ANISOU 2387  CZ  TYR A1109    16991  17495  13715    -73   -655    198       C  
ATOM   2388  OH  TYR A1109      36.166  -1.912 202.140  1.00126.15           O  
ANISOU 2388  OH  TYR A1109    16834  17431  13666   -104   -608    217       O  
ATOM   2389  N   GLY A1110      32.963  -4.910 209.794  1.00118.85           N  
ANISOU 2389  N   GLY A1110    16654  16099  12405    186   -612    156       N  
ATOM   2390  CA  GLY A1110      32.334  -5.792 210.773  1.00119.41           C  
ANISOU 2390  CA  GLY A1110    16907  16055  12410    267   -533    168       C  
ATOM   2391  C   GLY A1110      31.139  -5.174 211.475  1.00123.84           C  
ANISOU 2391  C   GLY A1110    17562  16481  13009    220   -430    183       C  
ATOM   2392  O   GLY A1110      30.085  -5.812 211.585  1.00123.83           O  
ANISOU 2392  O   GLY A1110    17640  16361  13048    223   -301    197       O  
ATOM   2393  N   SER A1111      31.300  -3.914 211.940  1.00120.07           N  
ANISOU 2393  N   SER A1111    17068  16016  12538    168   -474    168       N  
ATOM   2394  CA  SER A1111      30.291  -3.126 212.659  1.00119.79           C  
ANISOU 2394  CA  SER A1111    17113  15860  12540    115   -389    179       C  
ATOM   2395  C   SER A1111      29.099  -2.653 211.803  1.00122.85           C  
ANISOU 2395  C   SER A1111    17410  16198  13068     15   -303    204       C  
ATOM   2396  O   SER A1111      27.953  -2.779 212.248  1.00122.65           O  
ANISOU 2396  O   SER A1111    17472  16040  13091     -1   -188    206       O  
ATOM   2397  CB  SER A1111      30.944  -1.936 213.354  1.00123.76           C  
ANISOU 2397  CB  SER A1111    17607  16404  13012     90   -466    143       C  
ATOM   2398  OG  SER A1111      31.646  -1.127 212.426  1.00133.31           O  
ANISOU 2398  OG  SER A1111    18635  17727  14288     18   -533    126       O  
ATOM   2399  N   VAL A1112      29.364  -2.094 210.597  1.00118.26           N  
ANISOU 2399  N   VAL A1112    16665  15718  12552    -40   -354    215       N  
ATOM   2400  CA  VAL A1112      28.327  -1.587 209.679  1.00117.08           C  
ANISOU 2400  CA  VAL A1112    16427  15545  12513   -101   -299    233       C  
ATOM   2401  C   VAL A1112      27.514  -2.751 209.074  1.00119.72           C  
ANISOU 2401  C   VAL A1112    16743  15850  12897    -68   -240    213       C  
ATOM   2402  O   VAL A1112      28.097  -3.771 208.708  1.00119.77           O  
ANISOU 2402  O   VAL A1112    16730  15914  12863    -17   -269    206       O  
ATOM   2403  CB  VAL A1112      28.897  -0.615 208.600  1.00120.58           C  
ANISOU 2403  CB  VAL A1112    16736  16092  12987   -142   -355    257       C  
ATOM   2404  CG1 VAL A1112      27.800  -0.098 207.681  1.00120.04           C  
ANISOU 2404  CG1 VAL A1112    16604  16004  13004   -165   -308    275       C  
ATOM   2405  CG2 VAL A1112      29.623   0.564 209.243  1.00120.72           C  
ANISOU 2405  CG2 VAL A1112    16760  16118  12988   -189   -379    250       C  
ATOM   2406  N   ASP A1113      26.175  -2.591 208.990  1.00115.10           N  
ANISOU 2406  N   ASP A1113    16153  15171  12409    -98   -153    187       N  
ATOM   2407  CA  ASP A1113      25.237  -3.589 208.463  1.00114.71           C  
ANISOU 2407  CA  ASP A1113    16063  15079  12444    -78    -79    127       C  
ATOM   2408  C   ASP A1113      25.379  -3.848 206.962  1.00118.20           C  
ANISOU 2408  C   ASP A1113    16348  15652  12910    -52   -150    114       C  
ATOM   2409  O   ASP A1113      25.504  -5.008 206.550  1.00117.80           O  
ANISOU 2409  O   ASP A1113    16266  15628  12863    -15   -135     78       O  
ATOM   2410  CB  ASP A1113      23.783  -3.209 208.802  1.00116.60           C  
ANISOU 2410  CB  ASP A1113    16315  15186  12802   -119     25     72       C  
ATOM   2411  CG  ASP A1113      23.491  -3.068 210.283  1.00126.62           C  
ANISOU 2411  CG  ASP A1113    17754  16301  14055   -142    123     78       C  
ATOM   2412  OD1 ASP A1113      24.016  -3.885 211.076  1.00127.96           O  
ANISOU 2412  OD1 ASP A1113    18057  16421  14142    -97    164     91       O  
ATOM   2413  OD2 ASP A1113      22.728  -2.150 210.650  1.00130.92           O  
ANISOU 2413  OD2 ASP A1113    18309  16771  14665   -195    162     70       O  
ATOM   2414  N   PHE A1114      25.347  -2.769 206.151  1.00114.17           N  
ANISOU 2414  N   PHE A1114    15752  15216  12411    -65   -213    143       N  
ATOM   2415  CA  PHE A1114      25.427  -2.835 204.691  1.00113.28           C  
ANISOU 2415  CA  PHE A1114    15515  15224  12302    -21   -278    138       C  
ATOM   2416  C   PHE A1114      26.530  -1.960 204.121  1.00115.82           C  
ANISOU 2416  C   PHE A1114    15813  15643  12550    -24   -349    219       C  
ATOM   2417  O   PHE A1114      26.826  -0.907 204.675  1.00115.13           O  
ANISOU 2417  O   PHE A1114    15773  15523  12447    -68   -341    263       O  
ATOM   2418  CB  PHE A1114      24.086  -2.415 204.065  1.00115.26           C  
ANISOU 2418  CB  PHE A1114    15692  15458  12643      3   -262     75       C  
ATOM   2419  CG  PHE A1114      22.890  -3.250 204.453  1.00117.13           C  
ANISOU 2419  CG  PHE A1114    15916  15594  12995      0   -174    -44       C  
ATOM   2420  CD1 PHE A1114      22.549  -4.384 203.726  1.00120.46           C  
ANISOU 2420  CD1 PHE A1114    16243  16056  13469     44   -166   -142       C  
ATOM   2421  CD2 PHE A1114      22.086  -2.887 205.527  1.00119.54           C  
ANISOU 2421  CD2 PHE A1114    16296  15754  13368    -52    -83    -72       C  
ATOM   2422  CE1 PHE A1114      21.442  -5.159 204.087  1.00121.82           C  
ANISOU 2422  CE1 PHE A1114    16391  16119  13777     31    -55   -279       C  
ATOM   2423  CE2 PHE A1114      20.976  -3.658 205.883  1.00122.83           C  
ANISOU 2423  CE2 PHE A1114    16701  16055  13914    -63     30   -199       C  
ATOM   2424  CZ  PHE A1114      20.665  -4.792 205.164  1.00121.20           C  
ANISOU 2424  CZ  PHE A1114    16392  15883  13773    -24     50   -308       C  
ATOM   2425  N   VAL A1115      27.104  -2.373 202.987  1.00112.35           N  
ANISOU 2425  N   VAL A1115    15300  15312  12077     21   -402    228       N  
ATOM   2426  CA  VAL A1115      28.138  -1.611 202.282  1.00112.24           C  
ANISOU 2426  CA  VAL A1115    15263  15375  12008     21   -439    294       C  
ATOM   2427  C   VAL A1115      27.624  -1.340 200.865  1.00115.70           C  
ANISOU 2427  C   VAL A1115    15641  15879  12441     96   -458    299       C  
ATOM   2428  O   VAL A1115      27.336  -2.287 200.133  1.00115.46           O  
ANISOU 2428  O   VAL A1115    15549  15908  12413    152   -489    250       O  
ATOM   2429  CB  VAL A1115      29.533  -2.308 202.323  1.00116.25           C  
ANISOU 2429  CB  VAL A1115    15761  15945  12465     11   -478    302       C  
ATOM   2430  CG1 VAL A1115      30.505  -1.697 201.312  1.00116.25           C  
ANISOU 2430  CG1 VAL A1115    15717  16018  12434     14   -492    347       C  
ATOM   2431  CG2 VAL A1115      30.129  -2.260 203.730  1.00116.16           C  
ANISOU 2431  CG2 VAL A1115    15822  15881  12434    -34   -477    294       C  
ATOM   2432  N   ILE A1116      27.471  -0.054 200.498  1.00112.06           N  
ANISOU 2432  N   ILE A1116    15204  15404  11968    110   -435    353       N  
ATOM   2433  CA  ILE A1116      26.964   0.337 199.176  1.00112.11           C  
ANISOU 2433  CA  ILE A1116    15187  15468  11942    216   -453    366       C  
ATOM   2434  C   ILE A1116      28.113   0.624 198.198  1.00116.27           C  
ANISOU 2434  C   ILE A1116    15725  16057  12396    243   -443    436       C  
ATOM   2435  O   ILE A1116      28.970   1.468 198.481  1.00115.77           O  
ANISOU 2435  O   ILE A1116    15705  15953  12328    182   -383    493       O  
ATOM   2436  CB  ILE A1116      25.922   1.500 199.248  1.00115.23           C  
ANISOU 2436  CB  ILE A1116    15621  15803  12359    250   -423    380       C  
ATOM   2437  CG1 ILE A1116      24.764   1.161 200.220  1.00115.09           C  
ANISOU 2437  CG1 ILE A1116    15585  15710  12432    212   -418    294       C  
ATOM   2438  CG2 ILE A1116      25.378   1.842 197.851  1.00116.19           C  
ANISOU 2438  CG2 ILE A1116    15733  15994  12420    402   -457    386       C  
ATOM   2439  CD1 ILE A1116      23.980   2.347 200.735  1.00120.10           C  
ANISOU 2439  CD1 ILE A1116    16268  16258  13107    196   -373    314       C  
ATOM   2440  N   ILE A1117      28.119  -0.094 197.049  1.00113.35           N  
ANISOU 2440  N   ILE A1117    15310  15777  11980    334   -491    416       N  
ATOM   2441  CA  ILE A1117      29.105   0.054 195.961  1.00113.71           C  
ANISOU 2441  CA  ILE A1117    15374  15877  11954    377   -472    475       C  
ATOM   2442  C   ILE A1117      28.350   0.462 194.657  1.00119.25           C  
ANISOU 2442  C   ILE A1117    16104  16628  12577    542   -490    490       C  
ATOM   2443  O   ILE A1117      28.099  -0.392 193.804  1.00118.66           O  
ANISOU 2443  O   ILE A1117    15975  16643  12465    632   -559    437       O  
ATOM   2444  CB  ILE A1117      30.016  -1.209 195.780  1.00116.10           C  
ANISOU 2444  CB  ILE A1117    15613  16246  12255    341   -511    443       C  
ATOM   2445  CG1 ILE A1117      30.526  -1.781 197.125  1.00115.62           C  
ANISOU 2445  CG1 ILE A1117    15532  16145  12252    224   -518    410       C  
ATOM   2446  CG2 ILE A1117      31.187  -0.919 194.841  1.00117.18           C  
ANISOU 2446  CG2 ILE A1117    15775  16410  12337    355   -465    504       C  
ATOM   2447  CD1 ILE A1117      29.795  -3.015 197.626  1.00119.73           C  
ANISOU 2447  CD1 ILE A1117    16007  16673  12814    226   -561    329       C  
ATOM   2448  N   PRO A1118      27.944   1.747 194.489  1.00117.83           N  
ANISOU 2448  N   PRO A1118    16012  16393  12364    600   -432    554       N  
ATOM   2449  CA  PRO A1118      27.186   2.121 193.283  1.00119.31           C  
ANISOU 2449  CA  PRO A1118    16247  16633  12454    794   -461    564       C  
ATOM   2450  C   PRO A1118      28.073   2.463 192.083  1.00126.46           C  
ANISOU 2450  C   PRO A1118    17245  17558  13247    884   -395    653       C  
ATOM   2451  O   PRO A1118      27.743   3.346 191.280  1.00126.98           O  
ANISOU 2451  O   PRO A1118    17424  17610  13214   1036   -350    717       O  
ATOM   2452  CB  PRO A1118      26.322   3.298 193.758  1.00121.36           C  
ANISOU 2452  CB  PRO A1118    16569  16812  12731    821   -421    591       C  
ATOM   2453  CG  PRO A1118      26.955   3.786 195.036  1.00124.91           C  
ANISOU 2453  CG  PRO A1118    17030  17158  13273    631   -334    628       C  
ATOM   2454  CD  PRO A1118      28.122   2.911 195.378  1.00119.67           C  
ANISOU 2454  CD  PRO A1118    16310  16516  12642    507   -336    612       C  
ATOM   2455  N   SER A1119      29.185   1.713 191.948  1.00124.42           N  
ANISOU 2455  N   SER A1119    16946  17327  13001    800   -382    655       N  
ATOM   2456  CA  SER A1119      30.192   1.851 190.902  1.00125.55           C  
ANISOU 2456  CA  SER A1119    17164  17476  13064    849   -301    725       C  
ATOM   2457  C   SER A1119      29.638   1.647 189.500  1.00132.94           C  
ANISOU 2457  C   SER A1119    18149  18500  13860   1068   -358    725       C  
ATOM   2458  O   SER A1119      28.876   0.707 189.266  1.00132.53           O  
ANISOU 2458  O   SER A1119    17999  18554  13802   1137   -497    624       O  
ATOM   2459  CB  SER A1119      31.361   0.903 191.159  1.00127.50           C  
ANISOU 2459  CB  SER A1119    17325  17746  13375    709   -304    695       C  
ATOM   2460  OG  SER A1119      32.075   1.273 192.327  1.00134.37           O  
ANISOU 2460  OG  SER A1119    18170  18534  14350    538   -242    695       O  
ATOM   2461  N   TYR A1120      30.009   2.553 188.575  1.00132.51           N  
ANISOU 2461  N   TYR A1120    18257  18397  13695   1187   -238    829       N  
ATOM   2462  CA  TYR A1120      29.629   2.499 187.162  1.00134.42           C  
ANISOU 2462  CA  TYR A1120    18592  18713  13767   1427   -274    846       C  
ATOM   2463  C   TYR A1120      30.455   1.401 186.488  1.00140.26           C  
ANISOU 2463  C   TYR A1120    19275  19528  14488   1404   -302    818       C  
ATOM   2464  O   TYR A1120      29.918   0.616 185.707  1.00139.82           O  
ANISOU 2464  O   TYR A1120    19175  19599  14354   1545   -430    745       O  
ATOM   2465  CB  TYR A1120      29.896   3.850 186.485  1.00137.13           C  
ANISOU 2465  CB  TYR A1120    19162  18947  13995   1556    -93    984       C  
ATOM   2466  CG  TYR A1120      28.851   4.907 186.756  1.00139.52           C  
ANISOU 2466  CG  TYR A1120    19548  19202  14262   1668    -88   1014       C  
ATOM   2467  CD1 TYR A1120      28.980   5.784 187.829  1.00139.77           C  
ANISOU 2467  CD1 TYR A1120    19586  19109  14410   1511     24   1054       C  
ATOM   2468  CD2 TYR A1120      27.767   5.078 185.900  1.00142.99           C  
ANISOU 2468  CD2 TYR A1120    20063  19722  14543   1945   -191    996       C  
ATOM   2469  CE1 TYR A1120      28.038   6.785 188.063  1.00141.41           C  
ANISOU 2469  CE1 TYR A1120    19874  19266  14587   1612     40   1087       C  
ATOM   2470  CE2 TYR A1120      26.817   6.073 186.125  1.00145.07           C  
ANISOU 2470  CE2 TYR A1120    20407  19943  14773   2062   -187   1020       C  
ATOM   2471  CZ  TYR A1120      26.954   6.922 187.210  1.00150.84           C  
ANISOU 2471  CZ  TYR A1120    21144  20540  15629   1888    -66   1072       C  
ATOM   2472  OH  TYR A1120      26.023   7.908 187.424  1.00152.80           O  
ANISOU 2472  OH  TYR A1120    21471  20740  15846   2000    -55   1099       O  
ATOM   2473  N   PHE A1121      31.766   1.352 186.807  1.00138.78           N  
ANISOU 2473  N   PHE A1121    19079  19268  14385   1227   -183    858       N  
ATOM   2474  CA  PHE A1121      32.713   0.354 186.316  1.00139.36           C  
ANISOU 2474  CA  PHE A1121    19091  19392  14467   1170   -190    833       C  
ATOM   2475  C   PHE A1121      33.618  -0.147 187.445  1.00143.44           C  
ANISOU 2475  C   PHE A1121    19475  19876  15150    927   -180    789       C  
ATOM   2476  O   PHE A1121      34.258   0.641 188.149  1.00142.42           O  
ANISOU 2476  O   PHE A1121    19371  19636  15105    803    -62    821       O  
ATOM   2477  CB  PHE A1121      33.540   0.871 185.122  1.00142.76           C  
ANISOU 2477  CB  PHE A1121    19692  19761  14790   1266    -27    930       C  
ATOM   2478  CG  PHE A1121      34.268  -0.219 184.364  1.00144.55           C  
ANISOU 2478  CG  PHE A1121    19865  20061  14996   1257    -57    898       C  
ATOM   2479  CD1 PHE A1121      33.630  -0.933 183.354  1.00148.61           C  
ANISOU 2479  CD1 PHE A1121    20381  20706  15378   1441   -182    858       C  
ATOM   2480  CD2 PHE A1121      35.591  -0.530 184.658  1.00146.42           C  
ANISOU 2480  CD2 PHE A1121    20041  20241  15351   1069     35    891       C  
ATOM   2481  CE1 PHE A1121      34.302  -1.946 182.656  1.00149.49           C  
ANISOU 2481  CE1 PHE A1121    20440  20885  15475   1427   -205    827       C  
ATOM   2482  CE2 PHE A1121      36.261  -1.544 183.961  1.00149.32           C  
ANISOU 2482  CE2 PHE A1121    20356  20673  15706   1058      9    860       C  
ATOM   2483  CZ  PHE A1121      35.613  -2.244 182.964  1.00147.87           C  
ANISOU 2483  CZ  PHE A1121    20182  20613  15389   1232   -105    837       C  
ATOM   2484  N   GLU A1122      33.646  -1.474 187.604  1.00140.83           N  
ANISOU 2484  N   GLU A1122    19002  19643  14862    874   -306    704       N  
ATOM   2485  CA  GLU A1122      34.440  -2.206 188.583  1.00140.39           C  
ANISOU 2485  CA  GLU A1122    18823  19583  14936    688   -329    651       C  
ATOM   2486  C   GLU A1122      34.892  -3.501 187.875  1.00146.25           C  
ANISOU 2486  C   GLU A1122    19487  20421  15661    700   -391    606       C  
ATOM   2487  O   GLU A1122      34.041  -4.346 187.619  1.00145.77           O  
ANISOU 2487  O   GLU A1122    19358  20456  15572    775   -506    541       O  
ATOM   2488  CB  GLU A1122      33.574  -2.521 189.819  1.00140.84           C  
ANISOU 2488  CB  GLU A1122    18795  19650  15068    628   -427    586       C  
ATOM   2489  CG  GLU A1122      34.341  -3.033 191.028  1.00151.31           C  
ANISOU 2489  CG  GLU A1122    20036  20950  16505    462   -440    544       C  
ATOM   2490  CD  GLU A1122      35.055  -2.004 191.887  1.00177.54           C  
ANISOU 2490  CD  GLU A1122    23394  24170  19894    352   -348    570       C  
ATOM   2491  OE1 GLU A1122      34.808  -0.789 191.708  1.00180.12           O  
ANISOU 2491  OE1 GLU A1122    23814  24425  20197    387   -256    628       O  
ATOM   2492  OE2 GLU A1122      35.856  -2.418 192.756  1.00171.32           O  
ANISOU 2492  OE2 GLU A1122    22540  23374  19181    241   -367    522       O  
ATOM   2493  N   PRO A1123      36.170  -3.663 187.449  1.00144.30           N  
ANISOU 2493  N   PRO A1123    19245  20149  15435    634   -310    627       N  
ATOM   2494  CA  PRO A1123      36.545  -4.917 186.765  1.00144.11           C  
ANISOU 2494  CA  PRO A1123    19144  20216  15394    646   -370    584       C  
ATOM   2495  C   PRO A1123      36.681  -6.090 187.736  1.00147.98           C  
ANISOU 2495  C   PRO A1123    19487  20754  15984    533   -470    503       C  
ATOM   2496  O   PRO A1123      36.387  -7.231 187.380  1.00146.99           O  
ANISOU 2496  O   PRO A1123    19282  20720  15848    566   -552    448       O  
ATOM   2497  CB  PRO A1123      37.869  -4.579 186.065  1.00146.48           C  
ANISOU 2497  CB  PRO A1123    19505  20450  15700    605   -229    631       C  
ATOM   2498  CG  PRO A1123      38.256  -3.202 186.526  1.00151.53           C  
ANISOU 2498  CG  PRO A1123    20234  20955  16383    551    -85    680       C  
ATOM   2499  CD  PRO A1123      37.336  -2.772 187.621  1.00146.55           C  
ANISOU 2499  CD  PRO A1123    19585  20317  15782    535   -153    668       C  
ATOM   2500  N   PHE A1124      37.100  -5.787 188.973  1.00145.40           N  
ANISOU 2500  N   PHE A1124    19133  20362  15749    412   -456    491       N  
ATOM   2501  CA  PHE A1124      37.312  -6.723 190.074  1.00144.99           C  
ANISOU 2501  CA  PHE A1124    18983  20332  15776    322   -532    427       C  
ATOM   2502  C   PHE A1124      36.604  -6.199 191.327  1.00148.18           C  
ANISOU 2502  C   PHE A1124    19405  20683  16215    290   -553    418       C  
ATOM   2503  O   PHE A1124      36.789  -5.039 191.700  1.00148.48           O  
ANISOU 2503  O   PHE A1124    19501  20645  16270    257   -487    451       O  
ATOM   2504  CB  PHE A1124      38.825  -6.927 190.330  1.00147.29           C  
ANISOU 2504  CB  PHE A1124    19228  20601  16136    219   -499    405       C  
ATOM   2505  CG  PHE A1124      39.679  -5.673 190.351  1.00150.09           C  
ANISOU 2505  CG  PHE A1124    19632  20862  16532    162   -381    427       C  
ATOM   2506  CD1 PHE A1124      40.263  -5.188 189.184  1.00153.37           C  
ANISOU 2506  CD1 PHE A1124    20105  21244  16926    185   -264    466       C  
ATOM   2507  CD2 PHE A1124      39.936  -5.005 191.543  1.00153.48           C  
ANISOU 2507  CD2 PHE A1124    20054  21231  17030     86   -371    395       C  
ATOM   2508  CE1 PHE A1124      41.054  -4.034 189.205  1.00157.22           C  
ANISOU 2508  CE1 PHE A1124    20639  21622  17474    125   -117    471       C  
ATOM   2509  CE2 PHE A1124      40.725  -3.850 191.562  1.00155.40           C  
ANISOU 2509  CE2 PHE A1124    20325  21384  17336     25   -243    390       C  
ATOM   2510  CZ  PHE A1124      41.283  -3.376 190.393  1.00155.38           C  
ANISOU 2510  CZ  PHE A1124    20376  21334  17328     39   -106    425       C  
ATOM   2511  N   GLY A1125      35.798  -7.050 191.958  1.00143.16           N  
ANISOU 2511  N   GLY A1125    18723  20075  15598    299   -625    367       N  
ATOM   2512  CA  GLY A1125      35.049  -6.687 193.157  1.00142.23           C  
ANISOU 2512  CA  GLY A1125    18628  19899  15512    272   -637    353       C  
ATOM   2513  C   GLY A1125      35.856  -6.786 194.433  1.00144.64           C  
ANISOU 2513  C   GLY A1125    18930  20161  15866    183   -645    334       C  
ATOM   2514  O   GLY A1125      35.402  -7.406 195.396  1.00143.82           O  
ANISOU 2514  O   GLY A1125    18826  20038  15783    173   -675    299       O  
ATOM   2515  N   LEU A1126      37.048  -6.157 194.451  1.00140.96           N  
ANISOU 2515  N   LEU A1126    18465  19673  15420    128   -608    345       N  
ATOM   2516  CA  LEU A1126      37.995  -6.153 195.571  1.00140.65           C  
ANISOU 2516  CA  LEU A1126    18406  19610  15425     60   -631    300       C  
ATOM   2517  C   LEU A1126      37.433  -5.509 196.842  1.00143.31           C  
ANISOU 2517  C   LEU A1126    18794  19884  15773     39   -637    292       C  
ATOM   2518  O   LEU A1126      37.662  -6.031 197.933  1.00142.71           O  
ANISOU 2518  O   LEU A1126    18721  19804  15698     31   -690    249       O  
ATOM   2519  CB  LEU A1126      39.307  -5.466 195.158  1.00141.55           C  
ANISOU 2519  CB  LEU A1126    18490  19708  15584      5   -572    282       C  
ATOM   2520  CG  LEU A1126      40.587  -6.035 195.769  1.00146.66           C  
ANISOU 2520  CG  LEU A1126    19063  20382  16278    -37   -625    197       C  
ATOM   2521  CD1 LEU A1126      41.673  -6.167 194.718  1.00147.50           C  
ANISOU 2521  CD1 LEU A1126    19112  20507  16423    -63   -575    178       C  
ATOM   2522  CD2 LEU A1126      41.074  -5.185 196.933  1.00149.39           C  
ANISOU 2522  CD2 LEU A1126    19402  20685  16674    -86   -631    130       C  
ATOM   2523  N   VAL A1127      36.704  -4.384 196.699  1.00139.08           N  
ANISOU 2523  N   VAL A1127    18310  19298  15236     41   -579    335       N  
ATOM   2524  CA  VAL A1127      36.091  -3.658 197.819  1.00138.25           C  
ANISOU 2524  CA  VAL A1127    18256  19127  15147     16   -572    333       C  
ATOM   2525  C   VAL A1127      34.922  -4.439 198.426  1.00139.49           C  
ANISOU 2525  C   VAL A1127    18439  19274  15287     54   -614    323       C  
ATOM   2526  O   VAL A1127      34.679  -4.333 199.631  1.00138.82           O  
ANISOU 2526  O   VAL A1127    18397  19138  15210     32   -624    302       O  
ATOM   2527  CB  VAL A1127      35.711  -2.193 197.481  1.00142.88           C  
ANISOU 2527  CB  VAL A1127    18891  19653  15744      8   -484    383       C  
ATOM   2528  CG1 VAL A1127      36.922  -1.273 197.608  1.00143.47           C  
ANISOU 2528  CG1 VAL A1127    18948  19690  15874    -65   -413    357       C  
ATOM   2529  CG2 VAL A1127      35.063  -2.070 196.099  1.00142.86           C  
ANISOU 2529  CG2 VAL A1127    18913  19674  15692     91   -451    442       C  
ATOM   2530  N   ALA A1128      34.220  -5.238 197.590  1.00134.29           N  
ANISOU 2530  N   ALA A1128    17754  18658  14611    111   -627    324       N  
ATOM   2531  CA  ALA A1128      33.107  -6.097 197.999  1.00132.90           C  
ANISOU 2531  CA  ALA A1128    17582  18464  14449    143   -637    286       C  
ATOM   2532  C   ALA A1128      33.648  -7.340 198.702  1.00134.80           C  
ANISOU 2532  C   ALA A1128    17821  18710  14687    137   -659    250       C  
ATOM   2533  O   ALA A1128      33.063  -7.778 199.693  1.00134.00           O  
ANISOU 2533  O   ALA A1128    17771  18544  14597    141   -638    225       O  
ATOM   2534  CB  ALA A1128      32.281  -6.502 196.789  1.00133.57           C  
ANISOU 2534  CB  ALA A1128    17616  18604  14530    211   -643    267       C  
ATOM   2535  N   LEU A1129      34.773  -7.896 198.189  1.00130.49           N  
ANISOU 2535  N   LEU A1129    17228  18230  14124    136   -690    249       N  
ATOM   2536  CA  LEU A1129      35.469  -9.072 198.725  1.00129.86           C  
ANISOU 2536  CA  LEU A1129    17147  18165  14030    149   -717    220       C  
ATOM   2537  C   LEU A1129      35.920  -8.821 200.163  1.00132.03           C  
ANISOU 2537  C   LEU A1129    17496  18387  14281    143   -739    207       C  
ATOM   2538  O   LEU A1129      35.748  -9.693 201.014  1.00131.43           O  
ANISOU 2538  O   LEU A1129    17485  18273  14180    184   -731    190       O  
ATOM   2539  CB  LEU A1129      36.687  -9.430 197.848  1.00130.20           C  
ANISOU 2539  CB  LEU A1129    17115  18287  14066    142   -749    218       C  
ATOM   2540  CG  LEU A1129      36.460 -10.427 196.713  1.00134.82           C  
ANISOU 2540  CG  LEU A1129    17636  18933  14655    172   -741    211       C  
ATOM   2541  CD1 LEU A1129      37.361 -10.125 195.529  1.00135.21           C  
ANISOU 2541  CD1 LEU A1129    17627  19044  14703    156   -747    229       C  
ATOM   2542  CD2 LEU A1129      36.657 -11.864 197.187  1.00137.34           C  
ANISOU 2542  CD2 LEU A1129    17955  19255  14972    200   -744    180       C  
ATOM   2543  N   GLU A1130      36.470  -7.619 200.425  1.00127.56           N  
ANISOU 2543  N   GLU A1130    16930  17815  13723    101   -754    207       N  
ATOM   2544  CA  GLU A1130      36.928  -7.178 201.739  1.00127.30           C  
ANISOU 2544  CA  GLU A1130    16952  17746  13669    100   -788    174       C  
ATOM   2545  C   GLU A1130      35.740  -7.010 202.684  1.00130.80           C  
ANISOU 2545  C   GLU A1130    17498  18100  14100    111   -747    191       C  
ATOM   2546  O   GLU A1130      35.796  -7.482 203.819  1.00130.52           O  
ANISOU 2546  O   GLU A1130    17551  18026  14015    158   -763    170       O  
ATOM   2547  CB  GLU A1130      37.719  -5.870 201.620  1.00129.01           C  
ANISOU 2547  CB  GLU A1130    17118  17974  13927     38   -789    150       C  
ATOM   2548  CG  GLU A1130      39.054  -6.029 200.913  1.00139.63           C  
ANISOU 2548  CG  GLU A1130    18364  19386  15301     21   -816    105       C  
ATOM   2549  CD  GLU A1130      39.619  -4.772 200.281  1.00163.12           C  
ANISOU 2549  CD  GLU A1130    21282  22350  18348    -52   -751     92       C  
ATOM   2550  OE1 GLU A1130      38.831  -3.961 199.742  1.00156.57           O  
ANISOU 2550  OE1 GLU A1130    20485  21474  17529    -73   -672    158       O  
ATOM   2551  OE2 GLU A1130      40.860  -4.609 200.308  1.00161.17           O  
ANISOU 2551  OE2 GLU A1130    20957  22131  18150    -81   -769      7       O  
ATOM   2552  N   ALA A1131      34.652  -6.376 202.194  1.00127.05           N  
ANISOU 2552  N   ALA A1131    17021  17589  13665     82   -690    225       N  
ATOM   2553  CA  ALA A1131      33.418  -6.136 202.945  1.00126.77           C  
ANISOU 2553  CA  ALA A1131    17065  17460  13643     81   -637    231       C  
ATOM   2554  C   ALA A1131      32.731  -7.440 203.344  1.00131.14           C  
ANISOU 2554  C   ALA A1131    17674  17964  14192    128   -592    210       C  
ATOM   2555  O   ALA A1131      32.300  -7.574 204.489  1.00131.04           O  
ANISOU 2555  O   ALA A1131    17769  17860  14160    145   -552    202       O  
ATOM   2556  CB  ALA A1131      32.469  -5.268 202.130  1.00127.24           C  
ANISOU 2556  CB  ALA A1131    17087  17507  13750     57   -597    257       C  
ATOM   2557  N   MET A1132      32.657  -8.404 202.413  1.00128.09           N  
ANISOU 2557  N   MET A1132    17219  17626  13823    152   -584    197       N  
ATOM   2558  CA  MET A1132      32.026  -9.703 202.642  1.00128.24           C  
ANISOU 2558  CA  MET A1132    17272  17591  13861    190   -512    163       C  
ATOM   2559  C   MET A1132      32.835 -10.594 203.581  1.00134.34           C  
ANISOU 2559  C   MET A1132    18143  18339  14562    246   -514    166       C  
ATOM   2560  O   MET A1132      32.235 -11.335 204.355  1.00134.05           O  
ANISOU 2560  O   MET A1132    18210  18198  14523    283   -419    151       O  
ATOM   2561  CB  MET A1132      31.717 -10.410 201.316  1.00130.12           C  
ANISOU 2561  CB  MET A1132    17392  17898  14148    198   -503    131       C  
ATOM   2562  CG  MET A1132      30.540  -9.812 200.582  1.00133.26           C  
ANISOU 2562  CG  MET A1132    17721  18298  14613    186   -485     98       C  
ATOM   2563  SD  MET A1132      30.583 -10.137 198.810  1.00136.96           S  
ANISOU 2563  SD  MET A1132    18045  18899  15094    217   -534     71       S  
ATOM   2564  CE  MET A1132      29.750 -11.699 198.750  1.00133.84           C  
ANISOU 2564  CE  MET A1132    17603  18467  14784    239   -443    -39       C  
ATOM   2565  N   CYS A1133      34.186 -10.489 203.548  1.00132.89           N  
ANISOU 2565  N   CYS A1133    17933  18241  14319    262   -613    177       N  
ATOM   2566  CA  CYS A1133      35.105 -11.256 204.408  1.00134.23           C  
ANISOU 2566  CA  CYS A1133    18189  18411  14402    343   -648    170       C  
ATOM   2567  C   CYS A1133      34.914 -10.953 205.901  1.00138.75           C  
ANISOU 2567  C   CYS A1133    18922  18891  14904    393   -633    170       C  
ATOM   2568  O   CYS A1133      35.283 -11.778 206.743  1.00139.29           O  
ANISOU 2568  O   CYS A1133    19115  18924  14884    496   -626    167       O  
ATOM   2569  CB  CYS A1133      36.559 -11.056 203.981  1.00135.28           C  
ANISOU 2569  CB  CYS A1133    18227  18661  14510    343   -768    151       C  
ATOM   2570  SG  CYS A1133      37.116 -12.177 202.666  1.00139.16           S  
ANISOU 2570  SG  CYS A1133    18605  19240  15029    349   -775    148       S  
ATOM   2571  N   LEU A1134      34.341  -9.771 206.219  1.00134.54           N  
ANISOU 2571  N   LEU A1134    18400  18318  14403    333   -624    175       N  
ATOM   2572  CA  LEU A1134      34.059  -9.322 207.583  1.00134.33           C  
ANISOU 2572  CA  LEU A1134    18521  18202  14317    368   -606    173       C  
ATOM   2573  C   LEU A1134      32.559  -9.352 207.920  1.00137.47           C  
ANISOU 2573  C   LEU A1134    19003  18459  14772    339   -462    187       C  
ATOM   2574  O   LEU A1134      32.159  -8.950 209.016  1.00137.29           O  
ANISOU 2574  O   LEU A1134    19111  18341  14711    357   -423    190       O  
ATOM   2575  CB  LEU A1134      34.684  -7.950 207.844  1.00134.45           C  
ANISOU 2575  CB  LEU A1134    18484  18272  14329    322   -701    150       C  
ATOM   2576  CG  LEU A1134      36.203  -7.964 207.937  1.00139.72           C  
ANISOU 2576  CG  LEU A1134    19094  19052  14941    370   -833     96       C  
ATOM   2577  CD1 LEU A1134      36.830  -7.159 206.822  1.00141.88           C  
ANISOU 2577  CD1 LEU A1134    19190  19417  15303    274   -876     77       C  
ATOM   2578  CD2 LEU A1134      36.676  -7.492 209.290  1.00140.70           C  
ANISOU 2578  CD2 LEU A1134    19316  19165  14978    438   -901     43       C  
ATOM   2579  N   GLY A1135      31.761  -9.863 206.983  1.00133.81           N  
ANISOU 2579  N   GLY A1135    18458  17982  14403    300   -384    178       N  
ATOM   2580  CA  GLY A1135      30.322 -10.046 207.131  1.00133.88           C  
ANISOU 2580  CA  GLY A1135    18505  17861  14501    270   -240    153       C  
ATOM   2581  C   GLY A1135      29.443  -8.829 206.939  1.00137.78           C  
ANISOU 2581  C   GLY A1135    18942  18334  15076    190   -236    146       C  
ATOM   2582  O   GLY A1135      28.551  -8.582 207.755  1.00137.95           O  
ANISOU 2582  O   GLY A1135    19059  18226  15129    175   -141    132       O  
ATOM   2583  N   ALA A1136      29.659  -8.076 205.851  1.00133.54           N  
ANISOU 2583  N   ALA A1136    18258  17910  14570    145   -325    155       N  
ATOM   2584  CA  ALA A1136      28.836  -6.909 205.541  1.00133.07           C  
ANISOU 2584  CA  ALA A1136    18145  17836  14578     90   -323    154       C  
ATOM   2585  C   ALA A1136      28.056  -7.197 204.269  1.00137.40           C  
ANISOU 2585  C   ALA A1136    18563  18431  15211     91   -310    107       C  
ATOM   2586  O   ALA A1136      28.658  -7.566 203.255  1.00137.15           O  
ANISOU 2586  O   ALA A1136    18441  18509  15159    112   -370    113       O  
ATOM   2587  CB  ALA A1136      29.704  -5.672 205.369  1.00133.60           C  
ANISOU 2587  CB  ALA A1136    18176  17983  14603     58   -417    202       C  
ATOM   2588  N   ILE A1137      26.713  -7.078 204.334  1.00134.03           N  
ANISOU 2588  N   ILE A1137    18123  17920  14882     76   -233     45       N  
ATOM   2589  CA  ILE A1137      25.823  -7.338 203.196  1.00133.80           C  
ANISOU 2589  CA  ILE A1137    17959  17936  14942     96   -230    -38       C  
ATOM   2590  C   ILE A1137      26.013  -6.238 202.140  1.00137.55           C  
ANISOU 2590  C   ILE A1137    18355  18527  15382    114   -337      6       C  
ATOM   2591  O   ILE A1137      25.748  -5.073 202.432  1.00137.04           O  
ANISOU 2591  O   ILE A1137    18325  18430  15315     92   -346     44       O  
ATOM   2592  CB  ILE A1137      24.343  -7.519 203.632  1.00137.27           C  
ANISOU 2592  CB  ILE A1137    18396  18246  15513     79   -114   -149       C  
ATOM   2593  CG1 ILE A1137      24.201  -8.622 204.707  1.00137.93           C  
ANISOU 2593  CG1 ILE A1137    18595  18185  15628     68     35   -183       C  
ATOM   2594  CG2 ILE A1137      23.443  -7.801 202.419  1.00138.44           C  
ANISOU 2594  CG2 ILE A1137    18379  18462  15761    117   -133   -274       C  
ATOM   2595  CD1 ILE A1137      23.074  -8.397 205.711  1.00145.20           C  
ANISOU 2595  CD1 ILE A1137    19595  18928  16647     30    173   -244       C  
ATOM   2596  N   PRO A1138      26.502  -6.570 200.923  1.00134.27           N  
ANISOU 2596  N   PRO A1138    17850  18236  14932    158   -405      8       N  
ATOM   2597  CA  PRO A1138      26.753  -5.512 199.935  1.00134.01           C  
ANISOU 2597  CA  PRO A1138    17779  18292  14845    192   -480     64       C  
ATOM   2598  C   PRO A1138      25.578  -5.140 199.034  1.00137.47           C  
ANISOU 2598  C   PRO A1138    18141  18766  15326    264   -505     -8       C  
ATOM   2599  O   PRO A1138      24.913  -6.015 198.479  1.00137.29           O  
ANISOU 2599  O   PRO A1138    18025  18778  15361    310   -508   -121       O  
ATOM   2600  CB  PRO A1138      27.937  -6.055 199.132  1.00135.67           C  
ANISOU 2600  CB  PRO A1138    17954  18608  14987    211   -530    104       C  
ATOM   2601  CG  PRO A1138      27.851  -7.553 199.275  1.00140.13           C  
ANISOU 2601  CG  PRO A1138    18484  19166  15594    214   -496     30       C  
ATOM   2602  CD  PRO A1138      26.917  -7.893 200.409  1.00135.81           C  
ANISOU 2602  CD  PRO A1138    17989  18488  15126    183   -404    -33       C  
ATOM   2603  N   ILE A1139      25.339  -3.824 198.884  1.00133.78           N  
ANISOU 2603  N   ILE A1139    17709  18292  14831    284   -523     48       N  
ATOM   2604  CA  ILE A1139      24.319  -3.270 197.989  1.00134.06           C  
ANISOU 2604  CA  ILE A1139    17691  18371  14876    386   -566     -8       C  
ATOM   2605  C   ILE A1139      25.102  -2.658 196.822  1.00137.90           C  
ANISOU 2605  C   ILE A1139    18199  18955  15243    464   -615     87       C  
ATOM   2606  O   ILE A1139      25.369  -1.453 196.797  1.00137.28           O  
ANISOU 2606  O   ILE A1139    18199  18850  15113    471   -595    184       O  
ATOM   2607  CB  ILE A1139      23.342  -2.262 198.668  1.00137.35           C  
ANISOU 2607  CB  ILE A1139    18145  18694  15350    372   -533    -20       C  
ATOM   2608  CG1 ILE A1139      22.814  -2.788 200.019  1.00137.52           C  
ANISOU 2608  CG1 ILE A1139    18186  18586  15481    272   -450    -85       C  
ATOM   2609  CG2 ILE A1139      22.185  -1.904 197.714  1.00138.81           C  
ANISOU 2609  CG2 ILE A1139    18255  18935  15550    505   -594   -114       C  
ATOM   2610  CD1 ILE A1139      22.253  -1.716 200.922  1.00145.57           C  
ANISOU 2610  CD1 ILE A1139    19276  19496  16539    221   -402    -55       C  
ATOM   2611  N   ALA A1140      25.537  -3.524 195.896  1.00134.84           N  
ANISOU 2611  N   ALA A1140    17753  18665  14816    516   -657     60       N  
ATOM   2612  CA  ALA A1140      26.331  -3.136 194.736  1.00135.06           C  
ANISOU 2612  CA  ALA A1140    17812  18776  14729    593   -685    143       C  
ATOM   2613  C   ALA A1140      25.576  -3.291 193.425  1.00140.62           C  
ANISOU 2613  C   ALA A1140    18459  19585  15385    760   -761     64       C  
ATOM   2614  O   ALA A1140      24.803  -4.237 193.259  1.00140.19           O  
ANISOU 2614  O   ALA A1140    18294  19575  15399    794   -804    -81       O  
ATOM   2615  CB  ALA A1140      27.616  -3.938 194.694  1.00135.16           C  
ANISOU 2615  CB  ALA A1140    17816  18819  14720    524   -675    183       C  
ATOM   2616  N   SER A1141      25.818  -2.357 192.490  1.00138.75           N  
ANISOU 2616  N   SER A1141    18304  19384  15029    873   -769    152       N  
ATOM   2617  CA  SER A1141      25.209  -2.348 191.163  1.00139.94           C  
ANISOU 2617  CA  SER A1141    18438  19644  15090   1072   -850     94       C  
ATOM   2618  C   SER A1141      25.731  -3.507 190.314  1.00144.91           C  
ANISOU 2618  C   SER A1141    18996  20378  15687   1103   -893     44       C  
ATOM   2619  O   SER A1141      26.913  -3.852 190.398  1.00144.21           O  
ANISOU 2619  O   SER A1141    18932  20274  15588   1000   -842    126       O  
ATOM   2620  CB  SER A1141      25.448  -1.011 190.470  1.00143.92           C  
ANISOU 2620  CB  SER A1141    19095  20132  15457   1193   -813    227       C  
ATOM   2621  OG  SER A1141      26.826  -0.688 190.382  1.00151.41           O  
ANISOU 2621  OG  SER A1141    20137  21036  16357   1112   -715    367       O  
ATOM   2622  N   ALA A1142      24.836  -4.128 189.529  1.00142.43           N  
ANISOU 2622  N   ALA A1142    18579  20170  15367   1242   -991   -109       N  
ATOM   2623  CA  ALA A1142      25.147  -5.259 188.661  1.00142.42           C  
ANISOU 2623  CA  ALA A1142    18491  20280  15342   1287  -1041   -186       C  
ATOM   2624  C   ALA A1142      26.062  -4.849 187.506  1.00146.48           C  
ANISOU 2624  C   ALA A1142    19125  20848  15684   1393  -1035    -58       C  
ATOM   2625  O   ALA A1142      25.598  -4.442 186.437  1.00147.19           O  
ANISOU 2625  O   ALA A1142    19259  21021  15647   1602  -1104    -83       O  
ATOM   2626  CB  ALA A1142      23.865  -5.900 188.149  1.00144.16           C  
ANISOU 2626  CB  ALA A1142    18559  20602  15614   1418  -1147   -413       C  
ATOM   2627  N   VAL A1143      27.377  -4.900 187.770  1.00142.31           N  
ANISOU 2627  N   VAL A1143    18659  20260  15152   1254   -945     75       N  
ATOM   2628  CA  VAL A1143      28.458  -4.587 186.826  1.00142.74           C  
ANISOU 2628  CA  VAL A1143    18827  20328  15079   1304   -895    198       C  
ATOM   2629  C   VAL A1143      29.515  -5.717 186.878  1.00146.67           C  
ANISOU 2629  C   VAL A1143    19250  20845  15632   1169   -872    195       C  
ATOM   2630  O   VAL A1143      29.237  -6.772 187.458  1.00145.45           O  
ANISOU 2630  O   VAL A1143    18963  20713  15590   1082   -908     89       O  
ATOM   2631  CB  VAL A1143      29.061  -3.150 186.986  1.00146.75           C  
ANISOU 2631  CB  VAL A1143    19511  20721  15527   1291   -776    365       C  
ATOM   2632  CG1 VAL A1143      28.038  -2.064 186.659  1.00147.63           C  
ANISOU 2632  CG1 VAL A1143    19718  20827  15549   1473   -798    376       C  
ATOM   2633  CG2 VAL A1143      29.673  -2.927 188.366  1.00145.39           C  
ANISOU 2633  CG2 VAL A1143    19326  20434  15480   1074   -698    414       C  
ATOM   2634  N   GLY A1144      30.686  -5.496 186.268  1.00144.18           N  
ANISOU 2634  N   GLY A1144    19025  20513  15245   1158   -799    304       N  
ATOM   2635  CA  GLY A1144      31.785  -6.457 186.241  1.00143.74           C  
ANISOU 2635  CA  GLY A1144    18908  20472  15236   1039   -774    308       C  
ATOM   2636  C   GLY A1144      32.243  -6.867 187.628  1.00147.66           C  
ANISOU 2636  C   GLY A1144    19335  20899  15869    845   -749    301       C  
ATOM   2637  O   GLY A1144      32.316  -6.028 188.530  1.00147.02           O  
ANISOU 2637  O   GLY A1144    19309  20727  15827    773   -701    353       O  
ATOM   2638  N   GLY A1145      32.488  -8.164 187.809  1.00144.38           N  
ANISOU 2638  N   GLY A1145    18808  20530  15521    777   -782    230       N  
ATOM   2639  CA  GLY A1145      32.914  -8.735 189.084  1.00143.46           C  
ANISOU 2639  CA  GLY A1145    18641  20356  15511    628   -764    216       C  
ATOM   2640  C   GLY A1145      31.802  -8.830 190.112  1.00147.53           C  
ANISOU 2640  C   GLY A1145    19123  20830  16102    608   -782    147       C  
ATOM   2641  O   GLY A1145      31.616  -9.882 190.727  1.00146.52           O  
ANISOU 2641  O   GLY A1145    18922  20695  16052    553   -783     75       O  
ATOM   2642  N   LEU A1146      31.056  -7.724 190.295  1.00145.06           N  
ANISOU 2642  N   LEU A1146    18872  20475  15769    655   -780    168       N  
ATOM   2643  CA  LEU A1146      29.950  -7.573 191.238  1.00144.99           C  
ANISOU 2643  CA  LEU A1146    18846  20411  15834    639   -784    106       C  
ATOM   2644  C   LEU A1146      28.725  -8.432 190.896  1.00149.53           C  
ANISOU 2644  C   LEU A1146    19306  21043  16463    711   -831    -51       C  
ATOM   2645  O   LEU A1146      28.055  -8.902 191.816  1.00148.89           O  
ANISOU 2645  O   LEU A1146    19181  20902  16487    652   -802   -131       O  
ATOM   2646  CB  LEU A1146      29.567  -6.089 191.412  1.00145.48           C  
ANISOU 2646  CB  LEU A1146    19005  20414  15856    675   -764    174       C  
ATOM   2647  CG  LEU A1146      30.644  -5.171 192.034  1.00149.95           C  
ANISOU 2647  CG  LEU A1146    19666  20896  16412    579   -694    295       C  
ATOM   2648  CD1 LEU A1146      30.247  -3.716 191.939  1.00150.78           C  
ANISOU 2648  CD1 LEU A1146    19867  20949  16472    634   -656    361       C  
ATOM   2649  CD2 LEU A1146      30.912  -5.519 193.487  1.00151.48           C  
ANISOU 2649  CD2 LEU A1146    19848  21018  16691    447   -674    281       C  
ATOM   2650  N   ARG A1147      28.443  -8.661 189.595  1.00146.84           N  
ANISOU 2650  N   ARG A1147    18919  20815  16059    840   -892   -109       N  
ATOM   2651  CA  ARG A1147      27.327  -9.513 189.163  1.00147.24           C  
ANISOU 2651  CA  ARG A1147    18832  20939  16175    917   -943   -296       C  
ATOM   2652  C   ARG A1147      27.649 -10.983 189.496  1.00150.90           C  
ANISOU 2652  C   ARG A1147    19197  21399  16738    817   -898   -370       C  
ATOM   2653  O   ARG A1147      26.753 -11.744 189.874  1.00150.54           O  
ANISOU 2653  O   ARG A1147    19047  21334  16819    798   -871   -524       O  
ATOM   2654  CB  ARG A1147      27.071  -9.345 187.654  1.00148.43           C  
ANISOU 2654  CB  ARG A1147    18968  21223  16207   1102  -1033   -341       C  
ATOM   2655  CG  ARG A1147      25.795 -10.018 187.151  1.00160.75           C  
ANISOU 2655  CG  ARG A1147    20368  22875  17834   1211  -1108   -572       C  
ATOM   2656  CD  ARG A1147      25.953 -10.499 185.720  1.00174.49           C  
ANISOU 2656  CD  ARG A1147    22063  24764  19472   1355  -1188   -634       C  
ATOM   2657  NE  ARG A1147      24.794 -11.269 185.259  1.00186.72           N  
ANISOU 2657  NE  ARG A1147    23427  26412  21107   1452  -1263   -894       N  
ATOM   2658  CZ  ARG A1147      24.698 -12.596 185.308  1.00200.73           C  
ANISOU 2658  CZ  ARG A1147    25044  28211  23015   1373  -1228  -1043       C  
ATOM   2659  NH1 ARG A1147      25.691 -13.324 185.806  1.00187.43           N  
ANISOU 2659  NH1 ARG A1147    23378  26461  21377   1209  -1129   -943       N  
ATOM   2660  NH2 ARG A1147      23.607 -13.205 184.861  1.00186.97           N  
ANISOU 2660  NH2 ARG A1147    23117  26555  21367   1465  -1288  -1307       N  
ATOM   2661  N   ASP A1148      28.945 -11.350 189.379  1.00147.13           N  
ANISOU 2661  N   ASP A1148    18759  20929  16214    752   -872   -263       N  
ATOM   2662  CA  ASP A1148      29.501 -12.683 189.623  1.00146.54           C  
ANISOU 2662  CA  ASP A1148    18618  20853  16208    667   -826   -298       C  
ATOM   2663  C   ASP A1148      29.544 -13.054 191.114  1.00149.54           C  
ANISOU 2663  C   ASP A1148    19031  21106  16680    551   -743   -286       C  
ATOM   2664  O   ASP A1148      29.074 -14.132 191.479  1.00149.37           O  
ANISOU 2664  O   ASP A1148    18937  21054  16761    521   -682   -395       O  
ATOM   2665  CB  ASP A1148      30.919 -12.796 189.025  1.00148.33           C  
ANISOU 2665  CB  ASP A1148    18887  21122  16351    645   -832   -183       C  
ATOM   2666  CG  ASP A1148      31.088 -12.257 187.613  1.00162.27           C  
ANISOU 2666  CG  ASP A1148    20675  22984  17996    763   -889   -156       C  
ATOM   2667  OD1 ASP A1148      30.921 -11.033 187.420  1.00163.70           O  
ANISOU 2667  OD1 ASP A1148    20952  23148  18099    828   -902    -86       O  
ATOM   2668  OD2 ASP A1148      31.428 -13.052 186.711  1.00169.95           O  
ANISOU 2668  OD2 ASP A1148    21585  24042  18947    795   -907   -197       O  
ATOM   2669  N   ILE A1149      30.127 -12.176 191.964  1.00145.00           N  
ANISOU 2669  N   ILE A1149    18572  20454  16068    495   -729   -160       N  
ATOM   2670  CA  ILE A1149      30.291 -12.401 193.405  1.00143.99           C  
ANISOU 2670  CA  ILE A1149    18508  20210  15991    409   -662   -133       C  
ATOM   2671  C   ILE A1149      28.954 -12.339 194.183  1.00147.37           C  
ANISOU 2671  C   ILE A1149    18932  20550  16512    405   -609   -225       C  
ATOM   2672  O   ILE A1149      28.750 -13.144 195.092  1.00146.56           O  
ANISOU 2672  O   ILE A1149    18847  20357  16481    359   -521   -267       O  
ATOM   2673  CB  ILE A1149      31.385 -11.467 194.017  1.00146.81           C  
ANISOU 2673  CB  ILE A1149    18973  20528  16281    358   -676      3       C  
ATOM   2674  CG1 ILE A1149      31.754 -11.889 195.457  1.00147.03           C  
ANISOU 2674  CG1 ILE A1149    19071  20459  16335    296   -627     23       C  
ATOM   2675  CG2 ILE A1149      31.027  -9.970 193.927  1.00147.87           C  
ANISOU 2675  CG2 ILE A1149    19164  20644  16376    382   -698     55       C  
ATOM   2676  CD1 ILE A1149      33.046 -11.351 195.986  1.00154.29           C  
ANISOU 2676  CD1 ILE A1149    20057  21368  17198    256   -656    112       C  
ATOM   2677  N   ILE A1150      28.063 -11.399 193.833  1.00144.46           N  
ANISOU 2677  N   ILE A1150    18551  20196  16142    460   -649   -258       N  
ATOM   2678  CA  ILE A1150      26.793 -11.219 194.533  1.00144.78           C  
ANISOU 2678  CA  ILE A1150    18580  20149  16282    454   -600   -355       C  
ATOM   2679  C   ILE A1150      25.684 -12.086 193.928  1.00150.14           C  
ANISOU 2679  C   ILE A1150    19109  20865  17071    505   -584   -556       C  
ATOM   2680  O   ILE A1150      25.418 -12.029 192.724  1.00150.50           O  
ANISOU 2680  O   ILE A1150    19065  21034  17083    602   -672   -625       O  
ATOM   2681  CB  ILE A1150      26.407  -9.712 194.647  1.00148.08           C  
ANISOU 2681  CB  ILE A1150    19065  20546  16652    482   -644   -291       C  
ATOM   2682  CG1 ILE A1150      27.487  -8.931 195.427  1.00147.91           C  
ANISOU 2682  CG1 ILE A1150    19174  20469  16556    412   -633   -125       C  
ATOM   2683  CG2 ILE A1150      25.031  -9.514 195.305  1.00149.38           C  
ANISOU 2683  CG2 ILE A1150    19205  20621  16932    478   -597   -406       C  
ATOM   2684  CD1 ILE A1150      27.812  -7.586 194.877  1.00154.44           C  
ANISOU 2684  CD1 ILE A1150    20058  21331  17292    453   -681    -25       C  
ATOM   2685  N   THR A1151      25.051 -12.892 194.794  1.00147.22           N  
ANISOU 2685  N   THR A1151    18719  20381  16836    445   -461   -660       N  
ATOM   2686  CA  THR A1151      23.927 -13.783 194.497  1.00147.92           C  
ANISOU 2686  CA  THR A1151    18656  20462  17083    465   -397   -888       C  
ATOM   2687  C   THR A1151      22.715 -13.256 195.293  1.00151.97           C  
ANISOU 2687  C   THR A1151    19173  20855  17713    445   -331   -985       C  
ATOM   2688  O   THR A1151      22.879 -12.347 196.110  1.00151.08           O  
ANISOU 2688  O   THR A1151    19194  20666  17546    409   -329   -855       O  
ATOM   2689  CB  THR A1151      24.283 -15.236 194.902  1.00156.33           C  
ANISOU 2689  CB  THR A1151    19712  21459  18227    400   -255   -930       C  
ATOM   2690  OG1 THR A1151      25.699 -15.444 194.846  1.00153.35           O  
ANISOU 2690  OG1 THR A1151    19422  21126  17717    382   -293   -755       O  
ATOM   2691  CG2 THR A1151      23.571 -16.276 194.045  1.00156.94           C  
ANISOU 2691  CG2 THR A1151    19596  21597  18436    433   -219  -1158       C  
ATOM   2692  N   ASN A1152      21.512 -13.825 195.080  1.00149.48           N  
ANISOU 2692  N   ASN A1152    18704  20519  17571    463   -270  -1228       N  
ATOM   2693  CA  ASN A1152      20.298 -13.434 195.816  1.00149.96           C  
ANISOU 2693  CA  ASN A1152    18747  20453  17779    437   -187  -1357       C  
ATOM   2694  C   ASN A1152      20.367 -13.860 197.303  1.00152.42           C  
ANISOU 2694  C   ASN A1152    19204  20547  18159    321     18  -1298       C  
ATOM   2695  O   ASN A1152      19.532 -13.446 198.114  1.00151.99           O  
ANISOU 2695  O   ASN A1152    19185  20358  18206    282    107  -1357       O  
ATOM   2696  CB  ASN A1152      19.036 -13.979 195.127  1.00154.14           C  
ANISOU 2696  CB  ASN A1152    19047  21023  18496    491   -174  -1670       C  
ATOM   2697  CG  ASN A1152      18.994 -15.484 194.985  1.00183.55           C  
ANISOU 2697  CG  ASN A1152    22665  24716  22360    446    -29  -1826       C  
ATOM   2698  OD1 ASN A1152      18.448 -16.198 195.834  1.00180.56           O  
ANISOU 2698  OD1 ASN A1152    22288  24157  22158    358    189  -1939       O  
ATOM   2699  ND2 ASN A1152      19.563 -15.997 193.903  1.00175.55           N  
ANISOU 2699  ND2 ASN A1152    21564  23866  21273    507   -128  -1838       N  
ATOM   2700  N   GLU A1153      21.394 -14.665 197.643  1.00147.86           N  
ANISOU 2700  N   GLU A1153    18725  19940  17516    280     90  -1178       N  
ATOM   2701  CA  GLU A1153      21.691 -15.204 198.973  1.00147.17           C  
ANISOU 2701  CA  GLU A1153    18811  19664  17444    209    275  -1098       C  
ATOM   2702  C   GLU A1153      22.798 -14.395 199.674  1.00148.53           C  
ANISOU 2702  C   GLU A1153    19178  19836  17421    200    192   -845       C  
ATOM   2703  O   GLU A1153      22.914 -14.466 200.902  1.00147.78           O  
ANISOU 2703  O   GLU A1153    19250  19587  17311    164    311   -773       O  
ATOM   2704  CB  GLU A1153      22.145 -16.676 198.855  1.00148.85           C  
ANISOU 2704  CB  GLU A1153    19007  19849  17701    196    406  -1141       C  
ATOM   2705  CG  GLU A1153      21.156 -17.611 198.177  1.00160.61           C  
ANISOU 2705  CG  GLU A1153    20289  21336  19400    195    511  -1411       C  
ATOM   2706  CD  GLU A1153      21.780 -18.875 197.615  1.00181.22           C  
ANISOU 2706  CD  GLU A1153    22840  23997  22019    199    567  -1438       C  
ATOM   2707  OE1 GLU A1153      22.040 -19.813 198.402  1.00176.05           O  
ANISOU 2707  OE1 GLU A1153    22303  23188  21400    162    773  -1409       O  
ATOM   2708  OE2 GLU A1153      22.013 -18.926 196.385  1.00173.59           O  
ANISOU 2708  OE2 GLU A1153    21722  23220  21015    248    412  -1485       O  
ATOM   2709  N   THR A1154      23.632 -13.660 198.892  1.00143.49           N  
ANISOU 2709  N   THR A1154    18519  19364  16635    240     -1   -725       N  
ATOM   2710  CA  THR A1154      24.770 -12.881 199.406  1.00141.98           C  
ANISOU 2710  CA  THR A1154    18476  19191  16281    229    -85   -519       C  
ATOM   2711  C   THR A1154      24.812 -11.415 198.889  1.00143.51           C  
ANISOU 2711  C   THR A1154    18654  19477  16395    255   -235   -447       C  
ATOM   2712  O   THR A1154      25.758 -11.022 198.199  1.00142.26           O  
ANISOU 2712  O   THR A1154    18492  19438  16124    281   -347   -347       O  
ATOM   2713  CB  THR A1154      26.097 -13.629 199.141  1.00150.19           C  
ANISOU 2713  CB  THR A1154    19542  20304  17221    239   -119   -425       C  
ATOM   2714  OG1 THR A1154      26.164 -14.022 197.770  1.00150.43           O  
ANISOU 2714  OG1 THR A1154    19420  20477  17259    278   -196   -490       O  
ATOM   2715  CG2 THR A1154      26.274 -14.842 200.030  1.00148.94           C  
ANISOU 2715  CG2 THR A1154    19477  20020  17095    224     39   -436       C  
ATOM   2716  N   GLY A1155      23.809 -10.622 199.270  1.00139.13           N  
ANISOU 2716  N   GLY A1155    18103  18854  15906    248   -215   -498       N  
ATOM   2717  CA  GLY A1155      23.711  -9.212 198.901  1.00138.18           C  
ANISOU 2717  CA  GLY A1155    17989  18793  15720    279   -325   -432       C  
ATOM   2718  C   GLY A1155      22.552  -8.838 197.995  1.00140.92           C  
ANISOU 2718  C   GLY A1155    18204  19203  16136    356   -383   -570       C  
ATOM   2719  O   GLY A1155      21.691  -9.671 197.695  1.00141.25           O  
ANISOU 2719  O   GLY A1155    18124  19240  16306    375   -337   -753       O  
ATOM   2720  N   ILE A1156      22.518  -7.557 197.568  1.00135.84           N  
ANISOU 2720  N   ILE A1156    17586  18616  15412    408   -479   -495       N  
ATOM   2721  CA  ILE A1156      21.486  -6.993 196.687  1.00135.74           C  
ANISOU 2721  CA  ILE A1156    17475  18675  15425    518   -560   -607       C  
ATOM   2722  C   ILE A1156      22.142  -6.372 195.436  1.00138.27           C  
ANISOU 2722  C   ILE A1156    17808  19142  15585    629   -682   -508       C  
ATOM   2723  O   ILE A1156      23.075  -5.575 195.569  1.00137.44           O  
ANISOU 2723  O   ILE A1156    17821  19030  15370    602   -687   -331       O  
ATOM   2724  CB  ILE A1156      20.581  -5.954 197.433  1.00138.92           C  
ANISOU 2724  CB  ILE A1156    17920  18974  15888    499   -531   -620       C  
ATOM   2725  CG1 ILE A1156      20.054  -6.492 198.783  1.00139.14           C  
ANISOU 2725  CG1 ILE A1156    17977  18828  16061    381   -382   -690       C  
ATOM   2726  CG2 ILE A1156      19.423  -5.468 196.540  1.00140.69           C  
ANISOU 2726  CG2 ILE A1156    18031  19276  16150    636   -624   -767       C  
ATOM   2727  CD1 ILE A1156      19.791  -5.409 199.858  1.00146.81           C  
ANISOU 2727  CD1 ILE A1156    19065  19674  17041    316   -332   -607       C  
ATOM   2728  N   LEU A1157      21.643  -6.724 194.231  1.00134.15           N  
ANISOU 2728  N   LEU A1157    17169  18747  15056    760   -769   -637       N  
ATOM   2729  CA  LEU A1157      22.139  -6.173 192.967  1.00133.75           C  
ANISOU 2729  CA  LEU A1157    17148  18828  14842    896   -874   -557       C  
ATOM   2730  C   LEU A1157      21.172  -5.132 192.417  1.00137.23           C  
ANISOU 2730  C   LEU A1157    17587  19310  15243   1052   -956   -608       C  
ATOM   2731  O   LEU A1157      19.958  -5.314 192.530  1.00137.45           O  
ANISOU 2731  O   LEU A1157    17501  19331  15393   1093   -977   -800       O  
ATOM   2732  CB  LEU A1157      22.401  -7.273 191.928  1.00134.19           C  
ANISOU 2732  CB  LEU A1157    17099  19010  14877    961   -925   -649       C  
ATOM   2733  CG  LEU A1157      23.643  -8.142 192.150  1.00138.18           C  
ANISOU 2733  CG  LEU A1157    17632  19503  15366    846   -864   -554       C  
ATOM   2734  CD1 LEU A1157      23.556  -9.429 191.358  1.00138.84           C  
ANISOU 2734  CD1 LEU A1157    17577  19685  15492    886   -888   -701       C  
ATOM   2735  CD2 LEU A1157      24.932  -7.398 191.803  1.00140.29           C  
ANISOU 2735  CD2 LEU A1157    18035  19791  15477    845   -876   -343       C  
ATOM   2736  N   VAL A1158      21.706  -4.038 191.833  1.00133.08           N  
ANISOU 2736  N   VAL A1158    17191  18820  14555   1144   -991   -447       N  
ATOM   2737  CA  VAL A1158      20.895  -2.939 191.282  1.00133.76           C  
ANISOU 2737  CA  VAL A1158    17317  18939  14568   1319  -1061   -462       C  
ATOM   2738  C   VAL A1158      21.360  -2.455 189.899  1.00138.08           C  
ANISOU 2738  C   VAL A1158    17954  19599  14912   1515  -1129   -375       C  
ATOM   2739  O   VAL A1158      22.412  -2.872 189.423  1.00137.25           O  
ANISOU 2739  O   VAL A1158    17889  19531  14730   1488  -1106   -285       O  
ATOM   2740  CB  VAL A1158      20.751  -1.741 192.260  1.00137.27           C  
ANISOU 2740  CB  VAL A1158    17871  19251  15033   1242   -988   -346       C  
ATOM   2741  CG1 VAL A1158      19.590  -1.952 193.213  1.00137.14           C  
ANISOU 2741  CG1 VAL A1158    17753  19153  15200   1168   -968   -505       C  
ATOM   2742  CG2 VAL A1158      22.047  -1.444 193.014  1.00135.83           C  
ANISOU 2742  CG2 VAL A1158    17809  18975  14824   1069   -878   -147       C  
ATOM   2743  N   LYS A1159      20.564  -1.570 189.256  1.00135.39           N  
ANISOU 2743  N   LYS A1159    17657  19306  14480   1724  -1206   -405       N  
ATOM   2744  CA  LYS A1159      20.904  -0.981 187.958  1.00136.01           C  
ANISOU 2744  CA  LYS A1159    17865  19471  14340   1948  -1254   -313       C  
ATOM   2745  C   LYS A1159      21.944   0.124 188.185  1.00138.46           C  
ANISOU 2745  C   LYS A1159    18386  19667  14554   1882  -1116    -53       C  
ATOM   2746  O   LYS A1159      21.726   1.029 188.999  1.00137.83           O  
ANISOU 2746  O   LYS A1159    18370  19477  14521   1814  -1048     18       O  
ATOM   2747  CB  LYS A1159      19.653  -0.467 187.222  1.00140.39           C  
ANISOU 2747  CB  LYS A1159    18401  20118  14822   2224  -1390   -450       C  
ATOM   2748  CG  LYS A1159      18.679  -1.578 186.826  1.00155.65           C  
ANISOU 2748  CG  LYS A1159    20104  22183  16853   2312  -1531   -745       C  
ATOM   2749  CD  LYS A1159      17.500  -1.054 186.015  1.00165.98           C  
ANISOU 2749  CD  LYS A1159    21385  23603  18076   2616  -1690   -904       C  
ATOM   2750  CE  LYS A1159      16.246  -1.865 186.241  1.00172.32           C  
ANISOU 2750  CE  LYS A1159    21920  24468  19086   2622  -1790  -1238       C  
ATOM   2751  NZ  LYS A1159      15.049  -1.199 185.664  1.00179.52           N  
ANISOU 2751  NZ  LYS A1159    22795  25476  19939   2912  -1950  -1410       N  
ATOM   2752  N   ALA A1160      23.092  -0.002 187.489  1.00134.15           N  
ANISOU 2752  N   ALA A1160    17936  19140  13894   1889  -1062     71       N  
ATOM   2753  CA  ALA A1160      24.301   0.829 187.551  1.00133.29           C  
ANISOU 2753  CA  ALA A1160    18005  18925  13714   1811   -907    289       C  
ATOM   2754  C   ALA A1160      24.091   2.339 187.785  1.00136.94           C  
ANISOU 2754  C   ALA A1160    18631  19280  14121   1871   -814    414       C  
ATOM   2755  O   ALA A1160      24.501   2.837 188.838  1.00136.47           O  
ANISOU 2755  O   ALA A1160    18595  19099  14160   1679   -703    494       O  
ATOM   2756  CB  ALA A1160      25.155   0.610 186.311  1.00134.71           C  
ANISOU 2756  CB  ALA A1160    18278  19167  13740   1926   -887    359       C  
ATOM   2757  N   GLY A1161      23.484   3.042 186.827  1.00133.15           N  
ANISOU 2757  N   GLY A1161    18264  18845  13482   2142   -858    425       N  
ATOM   2758  CA  GLY A1161      23.316   4.488 186.909  1.00133.08           C  
ANISOU 2758  CA  GLY A1161    18435  18729  13401   2228   -752    556       C  
ATOM   2759  C   GLY A1161      21.974   5.040 187.341  1.00135.93           C  
ANISOU 2759  C   GLY A1161    18756  19088  13805   2318   -835    469       C  
ATOM   2760  O   GLY A1161      21.653   6.174 186.977  1.00136.98           O  
ANISOU 2760  O   GLY A1161    19054  19172  13819   2494   -782    561       O  
ATOM   2761  N   ASP A1162      21.187   4.287 188.134  1.00130.27           N  
ANISOU 2761  N   ASP A1162    17829  18406  13262   2201   -942    295       N  
ATOM   2762  CA  ASP A1162      19.892   4.809 188.572  1.00130.01           C  
ANISOU 2762  CA  ASP A1162    17744  18361  13294   2276  -1013    193       C  
ATOM   2763  C   ASP A1162      19.844   5.115 190.078  1.00131.14           C  
ANISOU 2763  C   ASP A1162    17840  18363  13625   2008   -916    219       C  
ATOM   2764  O   ASP A1162      19.867   4.188 190.898  1.00129.48           O  
ANISOU 2764  O   ASP A1162    17480  18141  13576   1808   -928    122       O  
ATOM   2765  CB  ASP A1162      18.711   3.921 188.133  1.00132.54           C  
ANISOU 2765  CB  ASP A1162    17871  18828  13659   2423  -1214    -70       C  
ATOM   2766  CG  ASP A1162      17.348   4.592 188.270  1.00144.20           C  
ANISOU 2766  CG  ASP A1162    19312  20313  15165   2580  -1304   -190       C  
ATOM   2767  OD1 ASP A1162      17.239   5.797 187.945  1.00145.98           O  
ANISOU 2767  OD1 ASP A1162    19719  20496  15252   2746  -1264    -61       O  
ATOM   2768  OD2 ASP A1162      16.392   3.912 188.693  1.00150.40           O  
ANISOU 2768  OD2 ASP A1162    19889  21137  16119   2541  -1402   -421       O  
ATOM   2769  N   PRO A1163      19.747   6.420 190.451  1.00126.56           N  
ANISOU 2769  N   PRO A1163    17397  17670  13022   2015   -812    346       N  
ATOM   2770  CA  PRO A1163      19.671   6.782 191.876  1.00124.61           C  
ANISOU 2770  CA  PRO A1163    17111  17292  12945   1774   -723    365       C  
ATOM   2771  C   PRO A1163      18.322   6.446 192.507  1.00127.25           C  
ANISOU 2771  C   PRO A1163    17285  17637  13428   1762   -828    170       C  
ATOM   2772  O   PRO A1163      18.246   6.271 193.724  1.00126.13           O  
ANISOU 2772  O   PRO A1163    17072  17405  13448   1541   -775    140       O  
ATOM   2773  CB  PRO A1163      19.926   8.296 191.875  1.00127.01           C  
ANISOU 2773  CB  PRO A1163    17607  17483  13167   1821   -579    545       C  
ATOM   2774  CG  PRO A1163      20.377   8.635 190.488  1.00132.91           C  
ANISOU 2774  CG  PRO A1163    18517  18283  13701   2062   -558    644       C  
ATOM   2775  CD  PRO A1163      19.721   7.631 189.611  1.00129.36           C  
ANISOU 2775  CD  PRO A1163    17959  18002  13191   2249   -755    480       C  
ATOM   2776  N   GLY A1164      17.282   6.372 191.677  1.00123.89           N  
ANISOU 2776  N   GLY A1164    16807  17317  12948   2009   -972     30       N  
ATOM   2777  CA  GLY A1164      15.927   6.036 192.096  1.00123.61           C  
ANISOU 2777  CA  GLY A1164    16599  17302  13067   2031  -1078   -198       C  
ATOM   2778  C   GLY A1164      15.800   4.593 192.540  1.00125.52           C  
ANISOU 2778  C   GLY A1164    16643  17572  13476   1872  -1114   -379       C  
ATOM   2779  O   GLY A1164      15.177   4.321 193.571  1.00124.72           O  
ANISOU 2779  O   GLY A1164    16436  17384  13567   1714  -1079   -490       O  
ATOM   2780  N   GLU A1165      16.408   3.658 191.770  1.00120.72           N  
ANISOU 2780  N   GLU A1165    15998  17072  12799   1912  -1163   -403       N  
ATOM   2781  CA  GLU A1165      16.398   2.220 192.059  1.00119.09           C  
ANISOU 2781  CA  GLU A1165    15617  16895  12736   1777  -1180   -564       C  
ATOM   2782  C   GLU A1165      17.246   1.871 193.274  1.00117.88           C  
ANISOU 2782  C   GLU A1165    15494  16612  12682   1486  -1035   -451       C  
ATOM   2783  O   GLU A1165      16.852   0.988 194.036  1.00116.65           O  
ANISOU 2783  O   GLU A1165    15216  16408  12699   1345  -1003   -588       O  
ATOM   2784  CB  GLU A1165      16.843   1.396 190.845  1.00121.38           C  
ANISOU 2784  CB  GLU A1165    15870  17339  12908   1915  -1271   -610       C  
ATOM   2785  CG  GLU A1165      15.759   0.472 190.315  1.00137.08           C  
ANISOU 2785  CG  GLU A1165    17644  19449  14989   2046  -1411   -915       C  
ATOM   2786  CD  GLU A1165      15.228   0.810 188.934  1.00172.48           C  
ANISOU 2786  CD  GLU A1165    22138  24099  19299   2382  -1578  -1001       C  
ATOM   2787  OE1 GLU A1165      16.046   1.043 188.015  1.00173.67           O  
ANISOU 2787  OE1 GLU A1165    22439  24311  19234   2505  -1586   -837       O  
ATOM   2788  OE2 GLU A1165      13.987   0.827 188.767  1.00174.67           O  
ANISOU 2788  OE2 GLU A1165    22269  24443  19653   2531  -1699  -1247       O  
ATOM   2789  N   LEU A1166      18.406   2.553 193.452  1.00111.61           N  
ANISOU 2789  N   LEU A1166    14865  15760  11782   1408   -939   -215       N  
ATOM   2790  CA  LEU A1166      19.312   2.355 194.592  1.00109.13           C  
ANISOU 2790  CA  LEU A1166    14591  15336  11537   1161   -818   -107       C  
ATOM   2791  C   LEU A1166      18.611   2.731 195.906  1.00112.69           C  
ANISOU 2791  C   LEU A1166    15029  15652  12135   1023   -752   -144       C  
ATOM   2792  O   LEU A1166      18.734   2.002 196.894  1.00111.40           O  
ANISOU 2792  O   LEU A1166    14826  15417  12085    852   -692   -183       O  
ATOM   2793  CB  LEU A1166      20.618   3.163 194.422  1.00108.44           C  
ANISOU 2793  CB  LEU A1166    14663  15219  11319   1130   -733    115       C  
ATOM   2794  CG  LEU A1166      21.671   3.029 195.541  1.00110.89           C  
ANISOU 2794  CG  LEU A1166    15009  15436  11687    899   -629    209       C  
ATOM   2795  CD1 LEU A1166      22.364   1.672 195.502  1.00110.01           C  
ANISOU 2795  CD1 LEU A1166    14823  15382  11594    826   -652    164       C  
ATOM   2796  CD2 LEU A1166      22.688   4.151 195.477  1.00112.56           C  
ANISOU 2796  CD2 LEU A1166    15361  15594  11812    873   -527    388       C  
ATOM   2797  N   ALA A1167      17.853   3.850 195.903  1.00109.47           N  
ANISOU 2797  N   ALA A1167    14664  15207  11721   1111   -758   -135       N  
ATOM   2798  CA  ALA A1167      17.097   4.297 197.065  1.00108.72           C  
ANISOU 2798  CA  ALA A1167    14558  14984  11765    996   -696   -176       C  
ATOM   2799  C   ALA A1167      16.105   3.206 197.472  1.00113.51           C  
ANISOU 2799  C   ALA A1167    15003  15576  12549    953   -722   -408       C  
ATOM   2800  O   ALA A1167      15.988   2.915 198.660  1.00112.43           O  
ANISOU 2800  O   ALA A1167    14861  15315  12540    778   -627   -433       O  
ATOM   2801  CB  ALA A1167      16.374   5.587 196.754  1.00110.24           C  
ANISOU 2801  CB  ALA A1167    14813  15162  11913   1136   -715   -144       C  
ATOM   2802  N   ASN A1168      15.472   2.542 196.477  1.00111.87           N  
ANISOU 2802  N   ASN A1168    14666  15491  12347   1114   -836   -584       N  
ATOM   2803  CA  ASN A1168      14.536   1.434 196.681  1.00112.58           C  
ANISOU 2803  CA  ASN A1168    14576  15575  12624   1085   -848   -842       C  
ATOM   2804  C   ASN A1168      15.245   0.186 197.226  1.00116.68           C  
ANISOU 2804  C   ASN A1168    15075  16053  13206    917   -759   -843       C  
ATOM   2805  O   ASN A1168      14.608  -0.623 197.903  1.00116.13           O  
ANISOU 2805  O   ASN A1168    14912  15895  13318    816   -682  -1007       O  
ATOM   2806  CB  ASN A1168      13.767   1.111 195.392  1.00115.60           C  
ANISOU 2806  CB  ASN A1168    14818  16119  12987   1319  -1005  -1045       C  
ATOM   2807  CG  ASN A1168      12.707   2.123 195.003  1.00142.02           C  
ANISOU 2807  CG  ASN A1168    18143  19493  16324   1503  -1098  -1129       C  
ATOM   2808  OD1 ASN A1168      12.723   2.683 193.900  1.00134.58           O  
ANISOU 2808  OD1 ASN A1168    17251  18676  15207   1734  -1218  -1090       O  
ATOM   2809  ND2 ASN A1168      11.745   2.368 195.885  1.00136.28           N  
ANISOU 2809  ND2 ASN A1168    17353  18646  15782   1417  -1043  -1250       N  
ATOM   2810  N   ALA A1169      16.556   0.034 196.937  1.00113.83           N  
ANISOU 2810  N   ALA A1169    14808  15744  12698    891   -756   -665       N  
ATOM   2811  CA  ALA A1169      17.367  -1.085 197.430  1.00113.51           C  
ANISOU 2811  CA  ALA A1169    14770  15672  12687    750   -680   -640       C  
ATOM   2812  C   ALA A1169      17.813  -0.802 198.861  1.00118.50           C  
ANISOU 2812  C   ALA A1169    15521  16148  13354    567   -555   -516       C  
ATOM   2813  O   ALA A1169      17.959  -1.739 199.651  1.00118.04           O  
ANISOU 2813  O   ALA A1169    15461  16011  13378    452   -466   -557       O  
ATOM   2814  CB  ALA A1169      18.577  -1.303 196.540  1.00113.92           C  
ANISOU 2814  CB  ALA A1169    14867  15842  12575    803   -734   -512       C  
ATOM   2815  N   ILE A1170      18.030   0.493 199.190  1.00115.58           N  
ANISOU 2815  N   ILE A1170    15265  15734  12918    553   -541   -371       N  
ATOM   2816  CA  ILE A1170      18.388   0.955 200.535  1.00114.82           C  
ANISOU 2816  CA  ILE A1170    15280  15499  12847    398   -437   -266       C  
ATOM   2817  C   ILE A1170      17.142   0.754 201.420  1.00118.75           C  
ANISOU 2817  C   ILE A1170    15732  15868  13521    336   -364   -416       C  
ATOM   2818  O   ILE A1170      17.259   0.268 202.547  1.00117.36           O  
ANISOU 2818  O   ILE A1170    15614  15571  13408    208   -258   -414       O  
ATOM   2819  CB  ILE A1170      18.916   2.423 200.499  1.00117.96           C  
ANISOU 2819  CB  ILE A1170    15789  15891  13138    408   -435    -93       C  
ATOM   2820  CG1 ILE A1170      20.278   2.493 199.777  1.00118.21           C  
ANISOU 2820  CG1 ILE A1170    15874  16016  13024    436   -461     44       C  
ATOM   2821  CG2 ILE A1170      19.039   3.018 201.902  1.00118.25           C  
ANISOU 2821  CG2 ILE A1170    15920  15788  13223    259   -336    -24       C  
ATOM   2822  CD1 ILE A1170      20.586   3.836 199.113  1.00127.89           C  
ANISOU 2822  CD1 ILE A1170    17183  17265  14144    521   -460    171       C  
ATOM   2823  N   LEU A1171      15.951   1.059 200.860  1.00116.80           N  
ANISOU 2823  N   LEU A1171    15381  15646  13351    442   -418   -561       N  
ATOM   2824  CA  LEU A1171      14.648   0.865 201.494  1.00117.42           C  
ANISOU 2824  CA  LEU A1171    15382  15608  13624    400   -352   -747       C  
ATOM   2825  C   LEU A1171      14.348  -0.626 201.664  1.00123.40           C  
ANISOU 2825  C   LEU A1171    16042  16328  14517    350   -280   -923       C  
ATOM   2826  O   LEU A1171      13.768  -1.008 202.682  1.00123.40           O  
ANISOU 2826  O   LEU A1171    16050  16166  14669    240   -141  -1016       O  
ATOM   2827  CB  LEU A1171      13.535   1.530 200.673  1.00118.42           C  
ANISOU 2827  CB  LEU A1171    15401  15801  13792    557   -456   -879       C  
ATOM   2828  CG  LEU A1171      13.435   3.043 200.768  1.00122.97           C  
ANISOU 2828  CG  LEU A1171    16074  16355  14293    596   -478   -745       C  
ATOM   2829  CD1 LEU A1171      12.698   3.615 199.576  1.00124.33           C  
ANISOU 2829  CD1 LEU A1171    16168  16653  14420    821   -621   -835       C  
ATOM   2830  CD2 LEU A1171      12.770   3.474 202.054  1.00125.48           C  
ANISOU 2830  CD2 LEU A1171    16428  16493  14754    458   -359   -772       C  
ATOM   2831  N   LYS A1172      14.744  -1.465 200.673  1.00121.19           N  
ANISOU 2831  N   LYS A1172    15679  16184  14185    431   -355   -972       N  
ATOM   2832  CA  LYS A1172      14.558  -2.920 200.727  1.00121.89           C  
ANISOU 2832  CA  LYS A1172    15672  16243  14397    388   -275  -1136       C  
ATOM   2833  C   LYS A1172      15.434  -3.512 201.835  1.00125.43           C  
ANISOU 2833  C   LYS A1172    16269  16571  14819    244   -135  -1002       C  
ATOM   2834  O   LYS A1172      14.963  -4.346 202.613  1.00124.94           O  
ANISOU 2834  O   LYS A1172    16205  16365  14903    158     22  -1116       O  
ATOM   2835  CB  LYS A1172      14.877  -3.586 199.371  1.00125.24           C  
ANISOU 2835  CB  LYS A1172    15979  16854  14752    514   -398  -1202       C  
ATOM   2836  CG  LYS A1172      13.782  -4.536 198.867  1.00145.39           C  
ANISOU 2836  CG  LYS A1172    18317  19429  17496    567   -390  -1514       C  
ATOM   2837  CD  LYS A1172      13.710  -5.869 199.635  1.00155.85           C  
ANISOU 2837  CD  LYS A1172    19622  20611  18983    430   -194  -1622       C  
ATOM   2838  CE  LYS A1172      12.313  -6.444 199.655  1.00166.22           C  
ANISOU 2838  CE  LYS A1172    20743  21848  20564    428   -109  -1954       C  
ATOM   2839  NZ  LYS A1172      12.188  -7.554 200.637  1.00174.04           N  
ANISOU 2839  NZ  LYS A1172    21767  22638  21721    280    142  -2033       N  
ATOM   2840  N   ALA A1173      16.696  -3.036 201.922  1.00121.81           N  
ANISOU 2840  N   ALA A1173    15945  16164  14175    226   -183   -770       N  
ATOM   2841  CA  ALA A1173      17.681  -3.426 202.929  1.00121.11           C  
ANISOU 2841  CA  ALA A1173    16006  15992  14020    123    -93   -631       C  
ATOM   2842  C   ALA A1173      17.212  -3.019 204.330  1.00125.49           C  
ANISOU 2842  C   ALA A1173    16676  16358  14646     22     37   -616       C  
ATOM   2843  O   ALA A1173      17.520  -3.710 205.300  1.00124.52           O  
ANISOU 2843  O   ALA A1173    16662  16120  14530    -47    158   -592       O  
ATOM   2844  CB  ALA A1173      19.020  -2.780 202.618  1.00121.15           C  
ANISOU 2844  CB  ALA A1173    16093  16104  13834    140   -191   -427       C  
ATOM   2845  N   LEU A1174      16.457  -1.906 204.424  1.00123.48           N  
ANISOU 2845  N   LEU A1174    16409  16070  14438     27     16   -631       N  
ATOM   2846  CA  LEU A1174      15.894  -1.390 205.671  1.00124.22           C  
ANISOU 2846  CA  LEU A1174    16601  15988  14610    -66    134   -627       C  
ATOM   2847  C   LEU A1174      14.857  -2.378 206.214  1.00132.19           C  
ANISOU 2847  C   LEU A1174    17570  16839  15817   -114    298   -824       C  
ATOM   2848  O   LEU A1174      14.870  -2.677 207.410  1.00131.34           O  
ANISOU 2848  O   LEU A1174    17602  16564  15739   -199    452   -798       O  
ATOM   2849  CB  LEU A1174      15.264  -0.004 205.430  1.00124.25           C  
ANISOU 2849  CB  LEU A1174    16573  16011  14626    -33     64   -613       C  
ATOM   2850  CG  LEU A1174      14.631   0.691 206.628  1.00128.56           C  
ANISOU 2850  CG  LEU A1174    17207  16383  15256   -128    174   -610       C  
ATOM   2851  CD1 LEU A1174      15.538   1.756 207.177  1.00127.83           C  
ANISOU 2851  CD1 LEU A1174    17253  16294  15021   -174    151   -406       C  
ATOM   2852  CD2 LEU A1174      13.313   1.304 206.249  1.00131.69           C  
ANISOU 2852  CD2 LEU A1174    17483  16761  15791    -81    151   -755       C  
ATOM   2853  N   GLU A1175      13.990  -2.902 205.321  1.00132.68           N  
ANISOU 2853  N   GLU A1175    17444  16952  16015    -51    275  -1031       N  
ATOM   2854  CA  GLU A1175      12.941  -3.866 205.658  1.00134.86           C  
ANISOU 2854  CA  GLU A1175    17641  17081  16519    -95    445  -1265       C  
ATOM   2855  C   GLU A1175      13.473  -5.261 205.961  1.00141.57           C  
ANISOU 2855  C   GLU A1175    18550  17867  17375   -132    583  -1275       C  
ATOM   2856  O   GLU A1175      12.876  -5.973 206.770  1.00141.60           O  
ANISOU 2856  O   GLU A1175    18598  17671  17532   -205    801  -1391       O  
ATOM   2857  CB  GLU A1175      11.853  -3.911 204.577  1.00137.48           C  
ANISOU 2857  CB  GLU A1175    17727  17504  17004     -4    360  -1516       C  
ATOM   2858  CG  GLU A1175      10.865  -2.755 204.653  1.00151.16           C  
ANISOU 2858  CG  GLU A1175    19404  19206  18823     17    313  -1590       C  
ATOM   2859  CD  GLU A1175      10.111  -2.601 205.964  1.00179.49           C  
ANISOU 2859  CD  GLU A1175    23077  22548  22573   -111    517  -1646       C  
ATOM   2860  OE1 GLU A1175       9.454  -3.576 206.399  1.00177.03           O  
ANISOU 2860  OE1 GLU A1175    22724  22078  22460   -179    712  -1836       O  
ATOM   2861  OE2 GLU A1175      10.187  -1.503 206.561  1.00177.06           O  
ANISOU 2861  OE2 GLU A1175    22883  22194  22196   -145    498  -1502       O  
ATOM   2862  N   LEU A1176      14.591  -5.649 205.323  1.00140.16           N  
ANISOU 2862  N   LEU A1176    18379  17843  17032    -80    472  -1156       N  
ATOM   2863  CA  LEU A1176      15.223  -6.954 205.535  1.00141.31           C  
ANISOU 2863  CA  LEU A1176    18586  17948  17159    -99    584  -1145       C  
ATOM   2864  C   LEU A1176      15.957  -7.031 206.879  1.00148.03           C  
ANISOU 2864  C   LEU A1176    19690  18658  17896   -159    701   -968       C  
ATOM   2865  O   LEU A1176      16.116  -8.127 207.426  1.00148.24           O  
ANISOU 2865  O   LEU A1176    19809  18567  17949   -177    868   -989       O  
ATOM   2866  CB  LEU A1176      16.161  -7.317 204.370  1.00140.96           C  
ANISOU 2866  CB  LEU A1176    18457  18118  16981    -21    419  -1085       C  
ATOM   2867  CG  LEU A1176      15.475  -7.727 203.062  1.00146.72           C  
ANISOU 2867  CG  LEU A1176    18946  18977  17822     57    338  -1296       C  
ATOM   2868  CD1 LEU A1176      16.350  -7.422 201.872  1.00146.57           C  
ANISOU 2868  CD1 LEU A1176    18876  19190  17626    153    122  -1186       C  
ATOM   2869  CD2 LEU A1176      15.086  -9.202 203.067  1.00150.27           C  
ANISOU 2869  CD2 LEU A1176    19317  19343  18435     29    510  -1483       C  
ATOM   2870  N   SER A1177      16.376  -5.869 207.421  1.00145.99           N  
ANISOU 2870  N   SER A1177    19546  18408  17513   -177    620   -805       N  
ATOM   2871  CA  SER A1177      17.088  -5.772 208.696  1.00146.33           C  
ANISOU 2871  CA  SER A1177    19823  18343  17431   -212    695   -649       C  
ATOM   2872  C   SER A1177      16.229  -6.107 209.919  1.00152.80           C  
ANISOU 2872  C   SER A1177    20776  18907  18375   -272    936   -727       C  
ATOM   2873  O   SER A1177      16.792  -6.453 210.962  1.00152.67           O  
ANISOU 2873  O   SER A1177    20974  18781  18253   -273   1037   -627       O  
ATOM   2874  CB  SER A1177      17.729  -4.400 208.857  1.00149.44           C  
ANISOU 2874  CB  SER A1177    20270  18827  17682   -218    543   -488       C  
ATOM   2875  OG  SER A1177      18.560  -4.392 210.005  1.00159.06           O  
ANISOU 2875  OG  SER A1177    21695  19975  18764   -232    585   -358       O  
ATOM   2876  N   ARG A1178      14.880  -6.005 209.794  1.00151.15           N  
ANISOU 2876  N   ARG A1178    20447  18597  18385   -312   1033   -914       N  
ATOM   2877  CA  ARG A1178      13.904  -6.309 210.853  1.00152.25           C  
ANISOU 2877  CA  ARG A1178    20691  18471  18687   -380   1293  -1023       C  
ATOM   2878  C   ARG A1178      14.083  -7.735 211.396  1.00158.01           C  
ANISOU 2878  C   ARG A1178    21556  19044  19436   -373   1523  -1055       C  
ATOM   2879  O   ARG A1178      14.017  -7.940 212.611  1.00158.05           O  
ANISOU 2879  O   ARG A1178    21792  18839  19420   -397   1721  -1007       O  
ATOM   2880  CB  ARG A1178      12.464  -6.084 210.357  1.00152.61           C  
ANISOU 2880  CB  ARG A1178    20525  18467  18993   -413   1338  -1265       C  
ATOM   2881  CG  ARG A1178      11.958  -4.649 210.515  1.00159.72           C  
ANISOU 2881  CG  ARG A1178    21398  19380  19908   -440   1236  -1237       C  
ATOM   2882  CD  ARG A1178      12.291  -3.777 209.320  1.00164.45           C  
ANISOU 2882  CD  ARG A1178    21836  20239  20409   -364    955  -1183       C  
ATOM   2883  NE  ARG A1178      11.429  -2.596 209.228  1.00169.88           N  
ANISOU 2883  NE  ARG A1178    22440  20924  21183   -371    889  -1239       N  
ATOM   2884  CZ  ARG A1178      11.727  -1.400 209.728  1.00181.00           C  
ANISOU 2884  CZ  ARG A1178    23956  22336  22479   -396    823  -1073       C  
ATOM   2885  NH1 ARG A1178      12.869  -1.210 210.378  1.00167.73           N  
ANISOU 2885  NH1 ARG A1178    22460  20667  20601   -417    806   -859       N  
ATOM   2886  NH2 ARG A1178      10.883  -0.387 209.586  1.00165.40           N  
ANISOU 2886  NH2 ARG A1178    21896  20354  20594   -394    773  -1135       N  
ATOM   2887  N   SER A1179      14.346  -8.702 210.491  1.00155.59           N  
ANISOU 2887  N   SER A1179    21120  18840  19157   -331   1500  -1128       N  
ATOM   2888  CA  SER A1179      14.618 -10.104 210.811  1.00156.52           C  
ANISOU 2888  CA  SER A1179    21349  18835  19286   -312   1708  -1152       C  
ATOM   2889  C   SER A1179      16.131 -10.269 210.982  1.00160.52           C  
ANISOU 2889  C   SER A1179    22015  19463  19513   -238   1579   -920       C  
ATOM   2890  O   SER A1179      16.899  -9.651 210.237  1.00158.94           O  
ANISOU 2890  O   SER A1179    21716  19495  19177   -205   1316   -819       O  
ATOM   2891  CB  SER A1179      14.115 -11.016 209.695  1.00160.79           C  
ANISOU 2891  CB  SER A1179    21645  19435  20013   -308   1743  -1368       C  
ATOM   2892  OG  SER A1179      12.717 -10.884 209.501  1.00170.76           O  
ANISOU 2892  OG  SER A1179    22732  20598  21552   -366   1850  -1621       O  
ATOM   2893  N   ASP A1180      16.554 -11.092 211.967  1.00158.68           N  
ANISOU 2893  N   ASP A1180    22033  19064  19193   -201   1772   -845       N  
ATOM   2894  CA  ASP A1180      17.962 -11.355 212.294  1.00158.52           C  
ANISOU 2894  CA  ASP A1180    22185  19135  18911   -111   1668   -649       C  
ATOM   2895  C   ASP A1180      18.757 -11.924 211.111  1.00162.63           C  
ANISOU 2895  C   ASP A1180    22538  19874  19381    -68   1506   -639       C  
ATOM   2896  O   ASP A1180      18.633 -13.107 210.780  1.00162.77           O  
ANISOU 2896  O   ASP A1180    22523  19837  19486    -53   1653   -728       O  
ATOM   2897  CB  ASP A1180      18.084 -12.240 213.551  1.00161.54           C  
ANISOU 2897  CB  ASP A1180    22879  19276  19222    -51   1936   -598       C  
ATOM   2898  CG  ASP A1180      18.091 -11.467 214.859  1.00171.58           C  
ANISOU 2898  CG  ASP A1180    24399  20421  20374    -37   1976   -493       C  
ATOM   2899  OD1 ASP A1180      17.118 -10.718 215.116  1.00171.75           O  
ANISOU 2899  OD1 ASP A1180    24380  20342  20536   -124   2039   -570       O  
ATOM   2900  OD2 ASP A1180      19.061 -11.618 215.632  1.00178.03           O  
ANISOU 2900  OD2 ASP A1180    25448  21239  20956     70   1942   -345       O  
ATOM   2901  N   LEU A1181      19.566 -11.051 210.471  1.00158.74           N  
ANISOU 2901  N   LEU A1181    21939  19618  18756    -54   1218   -536       N  
ATOM   2902  CA  LEU A1181      20.393 -11.371 209.301  1.00158.21           C  
ANISOU 2902  CA  LEU A1181    21715  19772  18626    -17   1039   -511       C  
ATOM   2903  C   LEU A1181      21.781 -11.938 209.659  1.00162.37           C  
ANISOU 2903  C   LEU A1181    22395  20354  18945     65    986   -365       C  
ATOM   2904  O   LEU A1181      22.745 -11.745 208.907  1.00160.99           O  
ANISOU 2904  O   LEU A1181    22124  20379  18665     91    783   -294       O  
ATOM   2905  CB  LEU A1181      20.517 -10.148 208.367  1.00157.38           C  
ANISOU 2905  CB  LEU A1181    21428  19871  18496    -38    789   -484       C  
ATOM   2906  CG  LEU A1181      19.233  -9.598 207.742  1.00162.38           C  
ANISOU 2906  CG  LEU A1181    21876  20503  19316    -84    787   -636       C  
ATOM   2907  CD1 LEU A1181      19.481  -8.234 207.141  1.00161.80           C  
ANISOU 2907  CD1 LEU A1181    21716  20597  19166    -80    564   -557       C  
ATOM   2908  CD2 LEU A1181      18.667 -10.546 206.683  1.00165.54           C  
ANISOU 2908  CD2 LEU A1181    22078  20951  19871    -72    827   -814       C  
ATOM   2909  N   SER A1182      21.863 -12.667 210.794  1.00160.17           N  
ANISOU 2909  N   SER A1182    22359  19890  18607    117   1178   -329       N  
ATOM   2910  CA  SER A1182      23.077 -13.310 211.304  1.00160.26           C  
ANISOU 2910  CA  SER A1182    22548  19926  18415    227   1150   -207       C  
ATOM   2911  C   SER A1182      23.623 -14.317 210.288  1.00164.05           C  
ANISOU 2911  C   SER A1182    22898  20523  18910    255   1117   -232       C  
ATOM   2912  O   SER A1182      24.828 -14.336 210.035  1.00162.81           O  
ANISOU 2912  O   SER A1182    22736  20525  18599    314    939   -139       O  
ATOM   2913  CB  SER A1182      22.793 -14.000 212.636  1.00165.12           C  
ANISOU 2913  CB  SER A1182    23464  20289  18985    297   1408   -187       C  
ATOM   2914  OG  SER A1182      22.210 -13.110 213.575  1.00174.04           O  
ANISOU 2914  OG  SER A1182    24719  21296  20114    267   1460   -174       O  
ATOM   2915  N   LYS A1183      22.722 -15.119 209.678  1.00161.54           N  
ANISOU 2915  N   LYS A1183    22458  20129  18792    206   1287   -377       N  
ATOM   2916  CA  LYS A1183      23.059 -16.114 208.660  1.00161.42           C  
ANISOU 2916  CA  LYS A1183    22298  20212  18823    219   1281   -430       C  
ATOM   2917  C   LYS A1183      23.393 -15.445 207.325  1.00164.30           C  
ANISOU 2917  C   LYS A1183    22402  20833  19191    182   1014   -439       C  
ATOM   2918  O   LYS A1183      24.341 -15.870 206.665  1.00163.38           O  
ANISOU 2918  O   LYS A1183    22225  20862  18990    220    896   -387       O  
ATOM   2919  CB  LYS A1183      21.929 -17.157 208.509  1.00164.96           C  
ANISOU 2919  CB  LYS A1183    22692  20481  19503    176   1572   -611       C  
ATOM   2920  CG  LYS A1183      22.248 -18.372 207.610  1.00178.40           C  
ANISOU 2920  CG  LYS A1183    24271  22249  21265    193   1620   -678       C  
ATOM   2921  CD  LYS A1183      23.525 -19.171 207.977  1.00188.07           C  
ANISOU 2921  CD  LYS A1183    25675  23493  22290    301   1614   -526       C  
ATOM   2922  CE  LYS A1183      23.408 -20.034 209.215  1.00199.80           C  
ANISOU 2922  CE  LYS A1183    27462  24716  23738    378   1914   -489       C  
ATOM   2923  NZ  LYS A1183      23.800 -19.295 210.444  1.00208.42           N  
ANISOU 2923  NZ  LYS A1183    28813  25746  24633    452   1861   -343       N  
ATOM   2924  N   PHE A1184      22.634 -14.393 206.941  1.00160.64           N  
ANISOU 2924  N   PHE A1184    21803  20416  18816    119    925   -500       N  
ATOM   2925  CA  PHE A1184      22.851 -13.638 205.702  1.00159.71           C  
ANISOU 2925  CA  PHE A1184    21474  20521  18689    104    690   -503       C  
ATOM   2926  C   PHE A1184      24.243 -12.999 205.684  1.00162.29           C  
ANISOU 2926  C   PHE A1184    21855  20998  18810    140    482   -330       C  
ATOM   2927  O   PHE A1184      24.919 -13.037 204.653  1.00161.07           O  
ANISOU 2927  O   PHE A1184    21575  21014  18610    155    339   -308       O  
ATOM   2928  CB  PHE A1184      21.763 -12.568 205.509  1.00161.68           C  
ANISOU 2928  CB  PHE A1184    21619  20763  19050     55    653   -587       C  
ATOM   2929  CG  PHE A1184      21.442 -12.280 204.060  1.00163.28           C  
ANISOU 2929  CG  PHE A1184    21580  21141  19317     64    506   -681       C  
ATOM   2930  CD1 PHE A1184      22.218 -11.394 203.320  1.00165.69           C  
ANISOU 2930  CD1 PHE A1184    21832  21632  19490     92    286   -571       C  
ATOM   2931  CD2 PHE A1184      20.367 -12.898 203.433  1.00166.48           C  
ANISOU 2931  CD2 PHE A1184    21817  21520  19916     56    597   -894       C  
ATOM   2932  CE1 PHE A1184      21.927 -11.137 201.976  1.00166.66           C  
ANISOU 2932  CE1 PHE A1184    21766  21911  19646    129    158   -649       C  
ATOM   2933  CE2 PHE A1184      20.075 -12.639 202.089  1.00169.37           C  
ANISOU 2933  CE2 PHE A1184    21969  22063  20319     95    443   -992       C  
ATOM   2934  CZ  PHE A1184      20.857 -11.759 201.370  1.00166.63           C  
ANISOU 2934  CZ  PHE A1184    21602  21898  19812    139    224   -858       C  
ATOM   2935  N   ARG A1185      24.669 -12.436 206.838  1.00158.86           N  
ANISOU 2935  N   ARG A1185    21607  20494  18260    154    476   -224       N  
ATOM   2936  CA  ARG A1185      25.985 -11.820 207.032  1.00158.09           C  
ANISOU 2936  CA  ARG A1185    21565  20517  17986    188    299    -92       C  
ATOM   2937  C   ARG A1185      27.076 -12.895 206.989  1.00162.15           C  
ANISOU 2937  C   ARG A1185    22130  21081  18400    261    285    -48       C  
ATOM   2938  O   ARG A1185      28.153 -12.649 206.446  1.00161.22           O  
ANISOU 2938  O   ARG A1185    21943  21119  18195    276    120      9       O  
ATOM   2939  CB  ARG A1185      26.038 -11.048 208.363  1.00157.93           C  
ANISOU 2939  CB  ARG A1185    21728  20397  17881    196    314    -28       C  
ATOM   2940  CG  ARG A1185      25.450  -9.640 208.297  1.00165.64           C  
ANISOU 2940  CG  ARG A1185    22640  21387  18910    125    250    -31       C  
ATOM   2941  CD  ARG A1185      25.272  -9.056 209.683  1.00174.16           C  
ANISOU 2941  CD  ARG A1185    23905  22334  19932    127    309      9       C  
ATOM   2942  NE  ARG A1185      25.648  -7.642 209.764  1.00181.41           N  
ANISOU 2942  NE  ARG A1185    24791  23335  20801     88    169     63       N  
ATOM   2943  CZ  ARG A1185      26.851  -7.199 210.127  1.00195.64           C  
ANISOU 2943  CZ  ARG A1185    26635  25229  22468    121     41    128       C  
ATOM   2944  NH1 ARG A1185      27.823  -8.055 210.417  1.00184.75           N  
ANISOU 2944  NH1 ARG A1185    25334  23887  20977    207     10    152       N  
ATOM   2945  NH2 ARG A1185      27.092  -5.899 210.193  1.00180.47           N  
ANISOU 2945  NH2 ARG A1185    24673  23364  20534     73    -53    157       N  
ATOM   2946  N   GLU A1186      26.781 -14.089 207.542  1.00159.63           N  
ANISOU 2946  N   GLU A1186    21932  20617  18103    306    475    -80       N  
ATOM   2947  CA  GLU A1186      27.690 -15.235 207.566  1.00159.89           C  
ANISOU 2947  CA  GLU A1186    22034  20669  18049    389    498    -42       C  
ATOM   2948  C   GLU A1186      27.886 -15.846 206.178  1.00162.97           C  
ANISOU 2948  C   GLU A1186    22215  21192  18514    361    447    -94       C  
ATOM   2949  O   GLU A1186      28.994 -16.283 205.874  1.00162.32           O  
ANISOU 2949  O   GLU A1186    22122  21217  18336    410    350    -39       O  
ATOM   2950  CB  GLU A1186      27.208 -16.298 208.564  1.00162.55           C  
ANISOU 2950  CB  GLU A1186    22584  20783  18393    452    757    -59       C  
ATOM   2951  CG  GLU A1186      27.712 -16.087 209.985  1.00174.97           C  
ANISOU 2951  CG  GLU A1186    24428  22265  19789    556    768     35       C  
ATOM   2952  CD  GLU A1186      29.155 -16.461 210.277  1.00198.21           C  
ANISOU 2952  CD  GLU A1186    27466  25311  22532    685    630    123       C  
ATOM   2953  OE1 GLU A1186      29.757 -17.226 209.486  1.00196.62           O  
ANISOU 2953  OE1 GLU A1186    27164  25207  22335    703    590    119       O  
ATOM   2954  OE2 GLU A1186      29.684 -15.992 211.311  1.00191.12           O  
ANISOU 2954  OE2 GLU A1186    26742  24400  21476    775    558    183       O  
ATOM   2955  N   ASN A1187      26.820 -15.864 205.338  1.00159.26           N  
ANISOU 2955  N   ASN A1187    21576  20720  18214    290    506   -211       N  
ATOM   2956  CA  ASN A1187      26.836 -16.394 203.964  1.00158.66           C  
ANISOU 2956  CA  ASN A1187    21291  20775  18218    269    457   -286       C  
ATOM   2957  C   ASN A1187      27.842 -15.654 203.083  1.00161.07           C  
ANISOU 2957  C   ASN A1187    21488  21289  18422    269    217   -207       C  
ATOM   2958  O   ASN A1187      28.478 -16.275 202.228  1.00160.13           O  
ANISOU 2958  O   ASN A1187    21276  21279  18288    283    162   -207       O  
ATOM   2959  CB  ASN A1187      25.444 -16.312 203.328  1.00160.35           C  
ANISOU 2959  CB  ASN A1187    21343  20960  18624    212    533   -450       C  
ATOM   2960  CG  ASN A1187      24.399 -17.229 203.915  1.00187.77           C  
ANISOU 2960  CG  ASN A1187    24865  24225  22253    195    805   -578       C  
ATOM   2961  OD1 ASN A1187      24.682 -18.132 204.715  1.00184.21           O  
ANISOU 2961  OD1 ASN A1187    24583  23639  21771    234    974   -542       O  
ATOM   2962  ND2 ASN A1187      23.151 -17.007 203.528  1.00180.21           N  
ANISOU 2962  ND2 ASN A1187    23766  23229  21474    146    865   -743       N  
ATOM   2963  N   CYS A1188      27.962 -14.323 203.290  1.00157.09           N  
ANISOU 2963  N   CYS A1188    21001  20827  17860    248     94   -145       N  
ATOM   2964  CA  CYS A1188      28.884 -13.430 202.585  1.00156.06           C  
ANISOU 2964  CA  CYS A1188    20793  20858  17644    242    -97    -71       C  
ATOM   2965  C   CYS A1188      30.338 -13.809 202.895  1.00159.22           C  
ANISOU 2965  C   CYS A1188    21262  21314  17919    285   -169     11       C  
ATOM   2966  O   CYS A1188      31.164 -13.827 201.981  1.00158.36           O  
ANISOU 2966  O   CYS A1188    21054  21336  17781    284   -273     32       O  
ATOM   2967  CB  CYS A1188      28.595 -11.972 202.933  1.00156.13           C  
ANISOU 2967  CB  CYS A1188    20827  20859  17638    208   -160    -34       C  
ATOM   2968  SG  CYS A1188      26.961 -11.392 202.405  1.00160.14           S  
ANISOU 2968  SG  CYS A1188    21229  21330  18286    176   -114   -140       S  
ATOM   2969  N   LYS A1189      30.633 -14.145 204.177  1.00155.69           N  
ANISOU 2969  N   LYS A1189    20993  20764  17400    335   -109     47       N  
ATOM   2970  CA  LYS A1189      31.954 -14.578 204.652  1.00155.30           C  
ANISOU 2970  CA  LYS A1189    21026  20758  17225    408   -180    104       C  
ATOM   2971  C   LYS A1189      32.365 -15.882 203.971  1.00158.35           C  
ANISOU 2971  C   LYS A1189    21356  21186  17625    440   -143     86       C  
ATOM   2972  O   LYS A1189      33.536 -16.050 203.631  1.00157.79           O  
ANISOU 2972  O   LYS A1189    21244  21223  17488    469   -256    115       O  
ATOM   2973  CB  LYS A1189      31.967 -14.746 206.182  1.00158.41           C  
ANISOU 2973  CB  LYS A1189    21645  21020  17525    489   -108    133       C  
ATOM   2974  CG  LYS A1189      31.980 -13.436 206.959  1.00171.62           C  
ANISOU 2974  CG  LYS A1189    23379  22681  19148    472   -184    158       C  
ATOM   2975  CD  LYS A1189      32.256 -13.663 208.439  1.00183.23           C  
ANISOU 2975  CD  LYS A1189    25080  24049  20488    584   -146    186       C  
ATOM   2976  CE  LYS A1189      31.023 -13.533 209.301  1.00195.41           C  
ANISOU 2976  CE  LYS A1189    26768  25410  22070    573     23    178       C  
ATOM   2977  NZ  LYS A1189      30.856 -12.155 209.831  1.00204.93           N  
ANISOU 2977  NZ  LYS A1189    27982  26618  23263    523    -53    186       N  
ATOM   2978  N   LYS A1190      31.387 -16.789 203.754  1.00154.47           N  
ANISOU 2978  N   LYS A1190    20851  20603  17238    429     25     22       N  
ATOM   2979  CA  LYS A1190      31.573 -18.076 203.088  1.00154.12           C  
ANISOU 2979  CA  LYS A1190    20744  20579  17236    447     97    -14       C  
ATOM   2980  C   LYS A1190      31.857 -17.889 201.588  1.00156.29           C  
ANISOU 2980  C   LYS A1190    20803  21023  17558    392    -26    -41       C  
ATOM   2981  O   LYS A1190      32.810 -18.481 201.075  1.00155.38           O  
ANISOU 2981  O   LYS A1190    20641  20996  17402    415    -84    -17       O  
ATOM   2982  CB  LYS A1190      30.344 -18.982 203.301  1.00157.31           C  
ANISOU 2982  CB  LYS A1190    21180  20822  17769    438    336   -105       C  
ATOM   2983  CG  LYS A1190      30.469 -19.943 204.486  1.00173.01           C  
ANISOU 2983  CG  LYS A1190    23399  22642  19696    530    514    -69       C  
ATOM   2984  CD  LYS A1190      29.683 -19.496 205.727  1.00183.84           C  
ANISOU 2984  CD  LYS A1190    24955  23834  21060    546    639    -63       C  
ATOM   2985  CE  LYS A1190      28.215 -19.871 205.697  1.00192.75           C  
ANISOU 2985  CE  LYS A1190    26051  24804  22383    480    875   -189       C  
ATOM   2986  NZ  LYS A1190      27.479 -19.331 206.871  1.00199.24           N  
ANISOU 2986  NZ  LYS A1190    27049  25451  23203    485    993   -182       N  
ATOM   2987  N   ARG A1191      31.042 -17.055 200.900  1.00151.97           N  
ANISOU 2987  N   ARG A1191    20137  20517  17086    333    -66    -90       N  
ATOM   2988  CA  ARG A1191      31.160 -16.770 199.467  1.00151.06           C  
ANISOU 2988  CA  ARG A1191    19845  20553  16999    304   -174   -117       C  
ATOM   2989  C   ARG A1191      32.451 -16.049 199.076  1.00154.06           C  
ANISOU 2989  C   ARG A1191    20207  21054  17277    303   -335    -26       C  
ATOM   2990  O   ARG A1191      33.012 -16.358 198.025  1.00153.02           O  
ANISOU 2990  O   ARG A1191    19972  21029  17141    300   -391    -29       O  
ATOM   2991  CB  ARG A1191      29.931 -16.006 198.947  1.00151.26           C  
ANISOU 2991  CB  ARG A1191    19778  20584  17109    277   -177   -194       C  
ATOM   2992  CG  ARG A1191      28.831 -16.909 198.389  1.00162.58           C  
ANISOU 2992  CG  ARG A1191    21098  21990  18683    274    -63   -346       C  
ATOM   2993  CD  ARG A1191      29.146 -17.468 197.005  1.00172.95           C  
ANISOU 2993  CD  ARG A1191    22255  23447  20010    287   -126   -397       C  
ATOM   2994  NE  ARG A1191      28.976 -16.475 195.942  1.00178.54           N  
ANISOU 2994  NE  ARG A1191    22867  24283  20685    307   -268   -402       N  
ATOM   2995  CZ  ARG A1191      29.412 -16.629 194.694  1.00188.44           C  
ANISOU 2995  CZ  ARG A1191    24018  25677  21905    335   -355   -412       C  
ATOM   2996  NH1 ARG A1191      30.064 -17.729 194.341  1.00174.50           N  
ANISOU 2996  NH1 ARG A1191    22212  23946  20145    330   -323   -420       N  
ATOM   2997  NH2 ARG A1191      29.208 -15.679 193.794  1.00172.58           N  
ANISOU 2997  NH2 ARG A1191    21960  23766  19848    377   -467   -408       N  
ATOM   2998  N   ALA A1192      32.862 -15.074 199.876  1.00150.80           N  
ANISOU 2998  N   ALA A1192    19887  20617  16792    302   -396     39       N  
ATOM   2999  CA  ALA A1192      34.085 -14.341 199.607  1.00150.46           C  
ANISOU 2999  CA  ALA A1192    19822  20666  16678    291   -524     98       C  
ATOM   3000  C   ALA A1192      35.268 -15.272 199.756  1.00154.53           C  
ANISOU 3000  C   ALA A1192    20356  21220  17137    332   -560    115       C  
ATOM   3001  O   ALA A1192      36.201 -15.257 198.962  1.00153.65           O  
ANISOU 3001  O   ALA A1192    20169  21202  17008    315   -647    129       O  
ATOM   3002  CB  ALA A1192      34.215 -13.169 200.560  1.00151.31           C  
ANISOU 3002  CB  ALA A1192    20012  20730  16748    277   -563    132       C  
ATOM   3003  N   MET A1193      35.212 -16.088 200.798  1.00152.21           N  
ANISOU 3003  N   MET A1193    20173  20843  16818    392   -482    110       N  
ATOM   3004  CA  MET A1193      36.266 -17.044 201.096  1.00152.83           C  
ANISOU 3004  CA  MET A1193    20291  20945  16831    460   -508    124       C  
ATOM   3005  C   MET A1193      36.408 -18.106 200.017  1.00157.03           C  
ANISOU 3005  C   MET A1193    20734  21513  17418    457   -447     98       C  
ATOM   3006  O   MET A1193      37.515 -18.534 199.701  1.00156.51           O  
ANISOU 3006  O   MET A1193    20670  21488  17311    504   -477    109       O  
ATOM   3007  CB  MET A1193      36.094 -17.641 202.493  1.00156.03           C  
ANISOU 3007  CB  MET A1193    20892  21240  17153    559   -454    142       C  
ATOM   3008  CG  MET A1193      36.206 -16.583 203.582  1.00160.11           C  
ANISOU 3008  CG  MET A1193    21477  21768  17590    583   -567    156       C  
ATOM   3009  SD  MET A1193      37.027 -17.126 205.090  1.00165.42           S  
ANISOU 3009  SD  MET A1193    22407  22309  18137    722   -509    175       S  
ATOM   3010  CE  MET A1193      37.679 -15.573 205.694  1.00162.31           C  
ANISOU 3010  CE  MET A1193    22003  21994  17673    730   -694    154       C  
ATOM   3011  N   SER A1194      35.300 -18.483 199.394  1.00153.92           N  
ANISOU 3011  N   SER A1194    20250  21113  17122    405   -368     50       N  
ATOM   3012  CA  SER A1194      35.361 -19.483 198.342  1.00153.61           C  
ANISOU 3012  CA  SER A1194    20095  21117  17152    389   -310      0       C  
ATOM   3013  C   SER A1194      36.271 -18.935 197.253  1.00156.95           C  
ANISOU 3013  C   SER A1194    20380  21686  17569    349   -435     10       C  
ATOM   3014  O   SER A1194      37.088 -19.655 196.691  1.00156.39           O  
ANISOU 3014  O   SER A1194    20216  21677  17528    343   -422    -16       O  
ATOM   3015  CB  SER A1194      33.966 -19.735 197.784  1.00156.94           C  
ANISOU 3015  CB  SER A1194    20465  21477  17687    361   -186    -91       C  
ATOM   3016  OG  SER A1194      33.023 -19.821 198.836  1.00165.25           O  
ANISOU 3016  OG  SER A1194    21650  22371  18766    393    -25   -112       O  
ATOM   3017  N   PHE A1195      36.124 -17.651 196.964  1.00153.38           N  
ANISOU 3017  N   PHE A1195    19923  21275  17081    323   -536     48       N  
ATOM   3018  CA  PHE A1195      36.955 -16.971 195.981  1.00152.96           C  
ANISOU 3018  CA  PHE A1195    19778  21328  17012    290   -628     70       C  
ATOM   3019  C   PHE A1195      38.394 -16.868 196.472  1.00156.74           C  
ANISOU 3019  C   PHE A1195    20279  21835  17442    294   -704    103       C  
ATOM   3020  O   PHE A1195      39.330 -16.805 195.684  1.00156.73           O  
ANISOU 3020  O   PHE A1195    20198  21906  17445    274   -744    104       O  
ATOM   3021  CB  PHE A1195      36.399 -15.588 195.665  1.00154.67           C  
ANISOU 3021  CB  PHE A1195    19996  21547  17226    266   -660     86       C  
ATOM   3022  CG  PHE A1195      35.102 -15.620 194.917  1.00156.19           C  
ANISOU 3022  CG  PHE A1195    20117  21770  17458    276   -636     39       C  
ATOM   3023  CD1 PHE A1195      33.942 -16.039 195.540  1.00159.37           C  
ANISOU 3023  CD1 PHE A1195    20527  22108  17918    289   -566    -26       C  
ATOM   3024  CD2 PHE A1195      35.045 -15.237 193.592  1.00158.48           C  
ANISOU 3024  CD2 PHE A1195    20339  22149  17726    284   -681     47       C  
ATOM   3025  CE1 PHE A1195      32.744 -16.073 194.855  1.00160.49           C  
ANISOU 3025  CE1 PHE A1195    20583  22291  18104    314   -562   -103       C  
ATOM   3026  CE2 PHE A1195      33.852 -15.268 192.901  1.00161.57           C  
ANISOU 3026  CE2 PHE A1195    20670  22584  18134    326   -680    -12       C  
ATOM   3027  CZ  PHE A1195      32.700 -15.687 193.532  1.00159.76           C  
ANISOU 3027  CZ  PHE A1195    20425  22307  17971    342   -632    -96       C  
ATOM   3028  N   SER A1196      38.552 -16.833 197.790  1.00152.61           N  
ANISOU 3028  N   SER A1196    19859  21250  16874    326   -725    116       N  
ATOM   3029  CA  SER A1196      39.860 -16.698 198.422  1.00164.50           C  
ANISOU 3029  CA  SER A1196    21389  22780  18333    355   -812    112       C  
ATOM   3030  C   SER A1196      40.839 -17.825 198.111  1.00200.67           C  
ANISOU 3030  C   SER A1196    25876  27430  22940    293   -883    102       C  
ATOM   3031  O   SER A1196      42.030 -17.574 197.951  1.00165.50           O  
ANISOU 3031  O   SER A1196    21396  22975  18512    240   -865    119       O  
ATOM   3032  CB  SER A1196      39.708 -16.556 199.935  1.00167.05           C  
ANISOU 3032  CB  SER A1196    21727  23115  18628    422   -810    101       C  
ATOM   3033  OG  SER A1196      40.958 -16.284 200.543  1.00176.04           O  
ANISOU 3033  OG  SER A1196    22906  24271  19709    484   -905     77       O  
ATOM   3034  N   GLY A 244      40.355 -19.061 198.031  1.00164.46           N  
ANISOU 3034  N   GLY A 244    21405  22781  18300    467   -751    100       N  
ATOM   3035  CA  GLY A 244      41.241 -20.177 197.744  1.00163.48           C  
ANISOU 3035  CA  GLY A 244    21224  22696  18194    486   -726     91       C  
ATOM   3036  C   GLY A 244      41.887 -19.917 196.402  1.00164.72           C  
ANISOU 3036  C   GLY A 244    21236  22956  18394    416   -798     76       C  
ATOM   3037  O   GLY A 244      41.226 -19.463 195.472  1.00163.80           O  
ANISOU 3037  O   GLY A 244    21040  22872  18325    343   -778     78       O  
ATOM   3038  N   GLN A 245      43.184 -20.185 196.298  1.00159.75           N  
ANISOU 3038  N   GLN A 245    20578  22374  17748    448   -878     53       N  
ATOM   3039  CA  GLN A 245      43.901 -19.912 195.058  1.00158.45           C  
ANISOU 3039  CA  GLN A 245    20280  22288  17637    379   -931     27       C  
ATOM   3040  C   GLN A 245      44.650 -21.085 194.417  1.00159.23           C  
ANISOU 3040  C   GLN A 245    20308  22425  17767    375   -891     25       C  
ATOM   3041  O   GLN A 245      45.458 -21.747 195.059  1.00159.00           O  
ANISOU 3041  O   GLN A 245    20314  22389  17710    453   -894     18       O  
ATOM   3042  CB  GLN A 245      44.840 -18.719 195.308  1.00160.55           C  
ANISOU 3042  CB  GLN A 245    20520  22582  17899    396  -1045    -32       C  
ATOM   3043  CG  GLN A 245      46.124 -18.657 194.500  1.00175.99           C  
ANISOU 3043  CG  GLN A 245    22361  24576  19933    291  -1061    -65       C  
ATOM   3044  CD  GLN A 245      47.238 -17.992 195.278  1.00196.16           C  
ANISOU 3044  CD  GLN A 245    24941  27094  22495    231  -1021    -33       C  
ATOM   3045  OE1 GLN A 245      48.407 -18.351 195.143  1.00192.21           O  
ANISOU 3045  OE1 GLN A 245    24484  26565  21982    240  -1057    -57       O  
ATOM   3046  NE2 GLN A 245      46.878 -17.026 196.113  1.00187.75           N  
ANISOU 3046  NE2 GLN A 245    23854  26036  21447    181   -948     16       N  
ATOM   3047  N   LYS A 246      44.372 -21.314 193.136  1.00153.13           N  
ANISOU 3047  N   LYS A 246    19445  21693  17046    296   -850     32       N  
ATOM   3048  CA  LYS A 246      45.038 -22.345 192.358  1.00151.56           C  
ANISOU 3048  CA  LYS A 246    19160  21540  16885    273   -807     25       C  
ATOM   3049  C   LYS A 246      45.817 -21.596 191.295  1.00154.00           C  
ANISOU 3049  C   LYS A 246    19376  21904  17235    198   -840     12       C  
ATOM   3050  O   LYS A 246      46.799 -22.084 190.740  1.00153.19           O  
ANISOU 3050  O   LYS A 246    19198  21840  17166    177   -837     -5       O  
ATOM   3051  CB  LYS A 246      44.016 -23.259 191.694  1.00152.66           C  
ANISOU 3051  CB  LYS A 246    19285  21674  17044    262   -711     26       C  
ATOM   3052  CG  LYS A 246      42.780 -23.523 192.533  1.00156.52           C  
ANISOU 3052  CG  LYS A 246    19869  22082  17520    315   -636     26       C  
ATOM   3053  CD  LYS A 246      41.888 -22.298 192.581  1.00163.57           C  
ANISOU 3053  CD  LYS A 246    20792  22948  18408    297   -634     27       C  
ATOM   3054  CE  LYS A 246      40.711 -22.509 193.514  1.00175.20           C  
ANISOU 3054  CE  LYS A 246    22357  24325  19886    339   -543     15       C  
ATOM   3055  NZ  LYS A 246      39.934 -21.256 193.720  1.00182.64           N  
ANISOU 3055  NZ  LYS A 246    23322  25242  20830    320   -550     10       N  
ATOM   3056  N   HIS A 247      45.351 -20.381 191.040  1.00150.18           N  
ANISOU 3056  N   HIS A 247    18907  21408  16748    160   -854     22       N  
ATOM   3057  CA  HIS A 247      45.942 -19.466 190.053  1.00149.89           C  
ANISOU 3057  CA  HIS A 247    18823  21385  16742     94   -844     20       C  
ATOM   3058  C   HIS A 247      47.399 -19.756 189.663  1.00151.18           C  
ANISOU 3058  C   HIS A 247    18904  21569  16967     55   -862    -28       C  
ATOM   3059  O   HIS A 247      47.725 -19.650 188.476  1.00151.30           O  
ANISOU 3059  O   HIS A 247    18877  21601  17010      6   -812    -22       O  
ATOM   3060  CB  HIS A 247      45.795 -18.004 190.527  1.00151.41           C  
ANISOU 3060  CB  HIS A 247    19070  21531  16927     77   -853     26       C  
ATOM   3061  CG  HIS A 247      46.129 -16.967 189.493  1.00155.59           C  
ANISOU 3061  CG  HIS A 247    19588  22047  17482     21   -797     37       C  
ATOM   3062  ND1 HIS A 247      45.747 -17.110 188.164  1.00157.47           N  
ANISOU 3062  ND1 HIS A 247    19822  22313  17697     21   -738     75       N  
ATOM   3063  CD2 HIS A 247      46.766 -15.781 189.637  1.00158.29           C  
ANISOU 3063  CD2 HIS A 247    19935  22341  17868    -24   -775     10       C  
ATOM   3064  CE1 HIS A 247      46.187 -16.025 187.544  1.00157.59           C  
ANISOU 3064  CE1 HIS A 247    19862  22287  17728    -16   -675     85       C  
ATOM   3065  NE2 HIS A 247      46.801 -15.194 188.389  1.00158.41           N  
ANISOU 3065  NE2 HIS A 247    19967  22338  17885    -53   -683     45       N  
ATOM   3066  N   ARG A 248      48.267 -20.103 190.634  1.00144.88           N  
ANISOU 3066  N   ARG A 248    18089  20770  16187     87   -933    -83       N  
ATOM   3067  CA  ARG A 248      49.668 -20.397 190.338  1.00143.62           C  
ANISOU 3067  CA  ARG A 248    17834  20632  16101     57   -961   -156       C  
ATOM   3068  C   ARG A 248      49.842 -21.709 189.579  1.00142.87           C  
ANISOU 3068  C   ARG A 248    17687  20577  16018     57   -931   -140       C  
ATOM   3069  O   ARG A 248      50.636 -21.756 188.637  1.00143.03           O  
ANISOU 3069  O   ARG A 248    17629  20610  16105     -6   -901   -170       O  
ATOM   3070  CB  ARG A 248      50.549 -20.341 191.596  1.00145.44           C  
ANISOU 3070  CB  ARG A 248    18053  20865  16344    116  -1067   -245       C  
ATOM   3071  CG  ARG A 248      51.428 -19.090 191.665  1.00159.16           C  
ANISOU 3071  CG  ARG A 248    19727  22578  18168     54  -1082   -343       C  
ATOM   3072  CD  ARG A 248      52.640 -19.169 190.745  1.00171.83           C  
ANISOU 3072  CD  ARG A 248    21209  24186  19891    -24  -1048   -423       C  
ATOM   3073  NE  ARG A 248      52.945 -17.872 190.138  1.00182.27           N  
ANISOU 3073  NE  ARG A 248    22505  25449  21302   -126   -953   -460       N  
ATOM   3074  CZ  ARG A 248      53.712 -17.702 189.064  1.00196.50           C  
ANISOU 3074  CZ  ARG A 248    24238  27218  23205   -215   -857   -499       C  
ATOM   3075  NH1 ARG A 248      54.256 -18.750 188.455  1.00183.33           N  
ANISOU 3075  NH1 ARG A 248    22507  25583  21566   -223   -859   -509       N  
ATOM   3076  NH2 ARG A 248      53.931 -16.486 188.584  1.00183.49           N  
ANISOU 3076  NH2 ARG A 248    22595  25491  21632   -297   -739   -528       N  
ATOM   3077  N   GLU A 249      49.078 -22.756 189.960  1.00135.05           N  
ANISOU 3077  N   GLU A 249    16745  19596  14973    123   -920    -99       N  
ATOM   3078  CA  GLU A 249      49.109 -24.078 189.314  1.00132.53           C  
ANISOU 3078  CA  GLU A 249    16378  19308  14669    126   -874    -87       C  
ATOM   3079  C   GLU A 249      48.575 -24.000 187.878  1.00130.35           C  
ANISOU 3079  C   GLU A 249    16060  19060  14408     58   -797    -60       C  
ATOM   3080  O   GLU A 249      49.123 -24.640 186.983  1.00129.32           O  
ANISOU 3080  O   GLU A 249    15855  18962  14318     20   -768    -73       O  
ATOM   3081  CB  GLU A 249      48.312 -25.121 190.131  1.00133.80           C  
ANISOU 3081  CB  GLU A 249    16613  19446  14777    213   -842    -59       C  
ATOM   3082  CG  GLU A 249      48.920 -25.457 191.488  1.00145.13           C  
ANISOU 3082  CG  GLU A 249    18114  20858  16171    319   -912    -81       C  
ATOM   3083  CD  GLU A 249      49.254 -26.917 191.741  1.00165.87           C  
ANISOU 3083  CD  GLU A 249    20754  23482  18787    395   -881    -77       C  
ATOM   3084  OE1 GLU A 249      49.794 -27.578 190.824  1.00165.09           O  
ANISOU 3084  OE1 GLU A 249    20558  23422  18748    345   -855    -91       O  
ATOM   3085  OE2 GLU A 249      48.991 -27.397 192.868  1.00155.90           O  
ANISOU 3085  OE2 GLU A 249    19612  22172  17453    513   -872    -58       O  
ATOM   3086  N   MET A 250      47.523 -23.192 187.670  1.00123.39           N  
ANISOU 3086  N   MET A 250    15229  18168  13486     55   -772    -27       N  
ATOM   3087  CA  MET A 250      46.864 -22.982 186.384  1.00121.60           C  
ANISOU 3087  CA  MET A 250    14986  17975  13244     30   -719     -9       C  
ATOM   3088  C   MET A 250      47.708 -22.245 185.364  1.00123.87           C  
ANISOU 3088  C   MET A 250    15252  18262  13552    -26   -695     -7       C  
ATOM   3089  O   MET A 250      47.502 -22.440 184.163  1.00123.09           O  
ANISOU 3089  O   MET A 250    15133  18200  13436    -34   -649      3       O  
ATOM   3090  CB  MET A 250      45.518 -22.275 186.569  1.00123.52           C  
ANISOU 3090  CB  MET A 250    15294  18206  13432     68   -712     13       C  
ATOM   3091  CG  MET A 250      44.404 -23.217 186.925  1.00126.65           C  
ANISOU 3091  CG  MET A 250    15684  18609  13826    111   -681     -8       C  
ATOM   3092  SD  MET A 250      44.148 -24.493 185.669  1.00130.50           S  
ANISOU 3092  SD  MET A 250    16068  19171  14343    103   -625    -52       S  
ATOM   3093  CE  MET A 250      43.026 -23.658 184.585  1.00127.35           C  
ANISOU 3093  CE  MET A 250    15674  18823  13889    138   -629    -69       C  
ATOM   3094  N   ARG A 251      48.666 -21.416 185.830  1.00119.87           N  
ANISOU 3094  N   ARG A 251    14751  17707  13088    -61   -714    -29       N  
ATOM   3095  CA  ARG A 251      49.568 -20.641 184.974  1.00120.00           C  
ANISOU 3095  CA  ARG A 251    14754  17689  13151   -125   -655    -43       C  
ATOM   3096  C   ARG A 251      50.330 -21.524 183.967  1.00122.51           C  
ANISOU 3096  C   ARG A 251    14998  18035  13517   -166   -615    -63       C  
ATOM   3097  O   ARG A 251      50.668 -21.058 182.875  1.00122.64           O  
ANISOU 3097  O   ARG A 251    15032  18025  13542   -203   -531    -52       O  
ATOM   3098  CB  ARG A 251      50.521 -19.780 185.812  1.00121.93           C  
ANISOU 3098  CB  ARG A 251    14983  17875  13470   -162   -678   -106       C  
ATOM   3099  CG  ARG A 251      50.890 -18.476 185.118  1.00137.03           C  
ANISOU 3099  CG  ARG A 251    16933  19714  15417   -217   -574   -107       C  
ATOM   3100  CD  ARG A 251      51.909 -17.667 185.893  1.00150.69           C  
ANISOU 3100  CD  ARG A 251    18616  21383  17254   -267   -579   -207       C  
ATOM   3101  NE  ARG A 251      52.816 -16.957 184.988  1.00160.55           N  
ANISOU 3101  NE  ARG A 251    19851  22550  18600   -349   -442   -250       N  
ATOM   3102  CZ  ARG A 251      54.033 -17.380 184.658  1.00173.25           C  
ANISOU 3102  CZ  ARG A 251    21358  24142  20329   -411   -414   -345       C  
ATOM   3103  NH1 ARG A 251      54.518 -18.503 185.174  1.00158.96           N  
ANISOU 3103  NH1 ARG A 251    19449  22403  18547   -390   -532   -403       N  
ATOM   3104  NH2 ARG A 251      54.782 -16.674 183.821  1.00159.85           N  
ANISOU 3104  NH2 ARG A 251    19663  22347  18727   -489   -255   -387       N  
ATOM   3105  N   VAL A 252      50.541 -22.810 184.325  1.00117.16           N  
ANISOU 3105  N   VAL A 252    14253  17400  12860   -150   -660    -87       N  
ATOM   3106  CA  VAL A 252      51.183 -23.834 183.497  1.00116.02           C  
ANISOU 3106  CA  VAL A 252    14031  17288  12763   -185   -628   -107       C  
ATOM   3107  C   VAL A 252      50.218 -24.236 182.371  1.00117.60           C  
ANISOU 3107  C   VAL A 252    14247  17540  12897   -166   -575    -65       C  
ATOM   3108  O   VAL A 252      50.614 -24.222 181.209  1.00117.50           O  
ANISOU 3108  O   VAL A 252    14222  17532  12892   -202   -513    -62       O  
ATOM   3109  CB  VAL A 252      51.634 -25.066 184.340  1.00119.77           C  
ANISOU 3109  CB  VAL A 252    14445  17788  13275   -155   -688   -144       C  
ATOM   3110  CG1 VAL A 252      52.269 -26.148 183.465  1.00119.48           C  
ANISOU 3110  CG1 VAL A 252    14321  17781  13293   -196   -649   -164       C  
ATOM   3111  CG2 VAL A 252      52.587 -24.656 185.460  1.00120.27           C  
ANISOU 3111  CG2 VAL A 252    14493  17819  13387   -141   -768   -208       C  
ATOM   3112  N   ILE A 253      48.960 -24.577 182.718  1.00112.39           N  
ANISOU 3112  N   ILE A 253    13612  16915  12176   -105   -595    -47       N  
ATOM   3113  CA  ILE A 253      47.924 -25.005 181.774  1.00111.52           C  
ANISOU 3113  CA  ILE A 253    13492  16867  12012    -70   -563    -46       C  
ATOM   3114  C   ILE A 253      47.584 -23.901 180.770  1.00116.04           C  
ANISOU 3114  C   ILE A 253    14138  17441  12510    -46   -535    -16       C  
ATOM   3115  O   ILE A 253      47.409 -24.202 179.584  1.00116.02           O  
ANISOU 3115  O   ILE A 253    14122  17490  12470    -28   -502    -25       O  
ATOM   3116  CB  ILE A 253      46.687 -25.570 182.512  1.00113.97           C  
ANISOU 3116  CB  ILE A 253    13801  17196  12306    -14   -577    -66       C  
ATOM   3117  CG1 ILE A 253      47.056 -26.891 183.200  1.00114.16           C  
ANISOU 3117  CG1 ILE A 253    13771  17212  12393    -22   -563    -89       C  
ATOM   3118  CG2 ILE A 253      45.481 -25.763 181.570  1.00114.54           C  
ANISOU 3118  CG2 ILE A 253    13848  17338  12333     32   -556   -103       C  
ATOM   3119  CD1 ILE A 253      46.103 -27.327 184.180  1.00124.06           C  
ANISOU 3119  CD1 ILE A 253    15051  18441  13646     27   -544   -104       C  
ATOM   3120  N   PHE A 254      47.532 -22.630 181.221  1.00112.56           N  
ANISOU 3120  N   PHE A 254    13783  16942  12043    -36   -541     17       N  
ATOM   3121  CA  PHE A 254      47.255 -21.516 180.310  1.00112.69           C  
ANISOU 3121  CA  PHE A 254    13899  16941  11979      4   -495     58       C  
ATOM   3122  C   PHE A 254      48.372 -21.341 179.287  1.00116.25           C  
ANISOU 3122  C   PHE A 254    14367  17352  12452    -44   -408     68       C  
ATOM   3123  O   PHE A 254      48.083 -21.071 178.122  1.00116.42           O  
ANISOU 3123  O   PHE A 254    14459  17390  12385     13   -357     95       O  
ATOM   3124  CB  PHE A 254      46.923 -20.218 181.057  1.00114.74           C  
ANISOU 3124  CB  PHE A 254    14246  17134  12214     21   -502     92       C  
ATOM   3125  CG  PHE A 254      45.579 -20.260 181.752  1.00115.98           C  
ANISOU 3125  CG  PHE A 254    14411  17328  12326     86   -568     85       C  
ATOM   3126  CD1 PHE A 254      44.401 -20.387 181.020  1.00119.22           C  
ANISOU 3126  CD1 PHE A 254    14835  17810  12655    177   -584     72       C  
ATOM   3127  CD2 PHE A 254      45.490 -20.168 183.134  1.00117.66           C  
ANISOU 3127  CD2 PHE A 254    14619  17503  12582     65   -612     78       C  
ATOM   3128  CE1 PHE A 254      43.162 -20.444 181.664  1.00119.71           C  
ANISOU 3128  CE1 PHE A 254    14888  17896  12702    229   -633     41       C  
ATOM   3129  CE2 PHE A 254      44.250 -20.220 183.774  1.00120.14           C  
ANISOU 3129  CE2 PHE A 254    14948  17833  12868    118   -650     68       C  
ATOM   3130  CZ  PHE A 254      43.095 -20.351 183.034  1.00118.32           C  
ANISOU 3130  CZ  PHE A 254    14715  17664  12578    192   -655     45       C  
ATOM   3131  N   ALA A 255      49.632 -21.591 179.698  1.00111.88           N  
ANISOU 3131  N   ALA A 255    13748  16749  12014   -137   -391     36       N  
ATOM   3132  CA  ALA A 255      50.787 -21.547 178.808  1.00111.98           C  
ANISOU 3132  CA  ALA A 255    13755  16708  12084   -202   -294     23       C  
ATOM   3133  C   ALA A 255      50.708 -22.701 177.801  1.00115.93           C  
ANISOU 3133  C   ALA A 255    14203  17285  12559   -192   -284     16       C  
ATOM   3134  O   ALA A 255      51.033 -22.502 176.630  1.00116.52           O  
ANISOU 3134  O   ALA A 255    14335  17335  12601   -191   -192     34       O  
ATOM   3135  CB  ALA A 255      52.073 -21.635 179.611  1.00112.76           C  
ANISOU 3135  CB  ALA A 255    13765  16750  12330   -295   -301    -45       C  
ATOM   3136  N   VAL A 256      50.228 -23.886 178.247  1.00111.73           N  
ANISOU 3136  N   VAL A 256    13575  16838  12038   -179   -364    -13       N  
ATOM   3137  CA  VAL A 256      50.065 -25.096 177.426  1.00111.40           C  
ANISOU 3137  CA  VAL A 256    13460  16876  11990   -174   -356    -38       C  
ATOM   3138  C   VAL A 256      49.086 -24.843 176.277  1.00116.70           C  
ANISOU 3138  C   VAL A 256    14202  17610  12530    -80   -339    -24       C  
ATOM   3139  O   VAL A 256      49.455 -25.058 175.117  1.00116.75           O  
ANISOU 3139  O   VAL A 256    14223  17629  12507    -79   -280    -23       O  
ATOM   3140  CB  VAL A 256      49.690 -26.348 178.279  1.00114.26           C  
ANISOU 3140  CB  VAL A 256    13717  17293  12404   -174   -416    -77       C  
ATOM   3141  CG1 VAL A 256      49.145 -27.489 177.421  1.00113.65           C  
ANISOU 3141  CG1 VAL A 256    13566  17305  12313   -155   -396   -117       C  
ATOM   3142  CG2 VAL A 256      50.874 -26.824 179.114  1.00114.00           C  
ANISOU 3142  CG2 VAL A 256    13619  17213  12482   -241   -431    -98       C  
ATOM   3143  N   VAL A 257      47.862 -24.355 176.604  1.00113.93           N  
ANISOU 3143  N   VAL A 257    13897  17294  12098      9   -394    -20       N  
ATOM   3144  CA  VAL A 257      46.785 -24.058 175.643  1.00114.54           C  
ANISOU 3144  CA  VAL A 257    14036  17445  12040    133   -409    -29       C  
ATOM   3145  C   VAL A 257      47.189 -22.929 174.689  1.00119.83           C  
ANISOU 3145  C   VAL A 257    14866  18054  12610    183   -331     38       C  
ATOM   3146  O   VAL A 257      47.004 -23.081 173.479  1.00119.98           O  
ANISOU 3146  O   VAL A 257    14931  18127  12530    265   -309     30       O  
ATOM   3147  CB  VAL A 257      45.409 -23.807 176.326  1.00118.16           C  
ANISOU 3147  CB  VAL A 257    14491  17945  12458    213   -487    -59       C  
ATOM   3148  CG1 VAL A 257      44.294 -23.632 175.294  1.00118.52           C  
ANISOU 3148  CG1 VAL A 257    14573  18089  12372    361   -526   -104       C  
ATOM   3149  CG2 VAL A 257      45.064 -24.938 177.291  1.00117.20           C  
ANISOU 3149  CG2 VAL A 257    14235  17852  12444    162   -520   -124       C  
ATOM   3150  N   LEU A 258      47.775 -21.829 175.229  1.00116.96           N  
ANISOU 3150  N   LEU A 258    14591  17572  12277    139   -277     96       N  
ATOM   3151  CA  LEU A 258      48.252 -20.671 174.461  1.00118.02           C  
ANISOU 3151  CA  LEU A 258    14894  17607  12341    174   -156    163       C  
ATOM   3152  C   LEU A 258      49.227 -21.100 173.362  1.00122.12           C  
ANISOU 3152  C   LEU A 258    15430  18095  12876    133    -50    163       C  
ATOM   3153  O   LEU A 258      49.035 -20.737 172.202  1.00122.44           O  
ANISOU 3153  O   LEU A 258    15610  18131  12781    239     19    201       O  
ATOM   3154  CB  LEU A 258      48.906 -19.626 175.392  1.00118.33           C  
ANISOU 3154  CB  LEU A 258    14976  17514  12470     93    -97    191       C  
ATOM   3155  CG  LEU A 258      49.529 -18.386 174.733  1.00124.77           C  
ANISOU 3155  CG  LEU A 258    15964  18187  13256    104     76    248       C  
ATOM   3156  CD1 LEU A 258      48.478 -17.333 174.422  1.00125.88           C  
ANISOU 3156  CD1 LEU A 258    16277  18323  13229    259     88    316       C  
ATOM   3157  CD2 LEU A 258      50.599 -17.783 175.619  1.00127.82           C  
ANISOU 3157  CD2 LEU A 258    16309  18445  13810    -34    149    218       C  
ATOM   3158  N   ILE A 259      50.234 -21.908 173.725  1.00118.29           N  
ANISOU 3158  N   ILE A 259    14809  17590  12545     -5    -41    119       N  
ATOM   3159  CA  ILE A 259      51.241 -22.407 172.794  1.00118.83           C  
ANISOU 3159  CA  ILE A 259    14868  17620  12660    -68     61    107       C  
ATOM   3160  C   ILE A 259      50.626 -23.446 171.819  1.00123.17           C  
ANISOU 3160  C   ILE A 259    15381  18303  13115      7     13     83       C  
ATOM   3161  O   ILE A 259      50.976 -23.436 170.636  1.00123.33           O  
ANISOU 3161  O   ILE A 259    15489  18301  13069     39    108    101       O  
ATOM   3162  CB  ILE A 259      52.501 -22.888 173.572  1.00121.41           C  
ANISOU 3162  CB  ILE A 259    15053  17887  13191   -230     72     52       C  
ATOM   3163  CG1 ILE A 259      53.292 -21.658 174.079  1.00122.37           C  
ANISOU 3163  CG1 ILE A 259    15237  17857  13402   -294    170     51       C  
ATOM   3164  CG2 ILE A 259      53.407 -23.803 172.731  1.00122.36           C  
ANISOU 3164  CG2 ILE A 259    15107  18004  13382   -303    139     18       C  
ATOM   3165  CD1 ILE A 259      54.062 -21.840 175.345  1.00128.56           C  
ANISOU 3165  CD1 ILE A 259    15877  18614  14354   -397    107    -23       C  
ATOM   3166  N   PHE A 260      49.676 -24.284 172.294  1.00119.54           N  
ANISOU 3166  N   PHE A 260    14801  17973  12648     43   -119     32       N  
ATOM   3167  CA  PHE A 260      48.999 -25.278 171.451  1.00119.78           C  
ANISOU 3167  CA  PHE A 260    14765  18137  12608    114   -168    -26       C  
ATOM   3168  C   PHE A 260      48.268 -24.605 170.285  1.00125.31           C  
ANISOU 3168  C   PHE A 260    15622  18881  13107    289   -159     -7       C  
ATOM   3169  O   PHE A 260      48.378 -25.063 169.146  1.00125.06           O  
ANISOU 3169  O   PHE A 260    15612  18900  13003    339   -128    -29       O  
ATOM   3170  CB  PHE A 260      48.016 -26.140 172.273  1.00120.78           C  
ANISOU 3170  CB  PHE A 260    14739  18367  12785    120   -281   -102       C  
ATOM   3171  CG  PHE A 260      47.238 -27.163 171.469  1.00122.60           C  
ANISOU 3171  CG  PHE A 260    14874  18738  12971    189   -323   -198       C  
ATOM   3172  CD1 PHE A 260      47.764 -28.426 171.221  1.00125.29           C  
ANISOU 3172  CD1 PHE A 260    15082  19114  13409    101   -293   -249       C  
ATOM   3173  CD2 PHE A 260      45.973 -26.867 170.973  1.00125.40           C  
ANISOU 3173  CD2 PHE A 260    15261  19192  13194    346   -395   -254       C  
ATOM   3174  CE1 PHE A 260      47.045 -29.370 170.482  1.00126.32           C  
ANISOU 3174  CE1 PHE A 260    15109  19373  13513    159   -322   -357       C  
ATOM   3175  CE2 PHE A 260      45.258 -27.810 170.231  1.00128.52           C  
ANISOU 3175  CE2 PHE A 260    15545  19725  13563    414   -439   -379       C  
ATOM   3176  CZ  PHE A 260      45.795 -29.057 169.997  1.00126.16           C  
ANISOU 3176  CZ  PHE A 260    15109  19456  13369    314   -397   -431       C  
ATOM   3177  N   LEU A 261      47.511 -23.534 170.586  1.00123.04           N  
ANISOU 3177  N   LEU A 261    15449  18578  12722    394   -191     30       N  
ATOM   3178  CA  LEU A 261      46.742 -22.778 169.602  1.00124.40           C  
ANISOU 3178  CA  LEU A 261    15793  18789  12683    596   -196     52       C  
ATOM   3179  C   LEU A 261      47.659 -21.969 168.694  1.00130.51           C  
ANISOU 3179  C   LEU A 261    16777  19431  13379    621    -29    147       C  
ATOM   3180  O   LEU A 261      47.442 -21.967 167.488  1.00131.54           O  
ANISOU 3180  O   LEU A 261    17024  19608  13347    766     -6    149       O  
ATOM   3181  CB  LEU A 261      45.685 -21.880 170.272  1.00124.50           C  
ANISOU 3181  CB  LEU A 261    15861  18814  12628    699   -275     63       C  
ATOM   3182  CG  LEU A 261      44.586 -22.583 171.087  1.00128.14           C  
ANISOU 3182  CG  LEU A 261    16139  19394  13153    701   -420    -44       C  
ATOM   3183  CD1 LEU A 261      43.890 -21.610 172.005  1.00128.11           C  
ANISOU 3183  CD1 LEU A 261    16192  19352  13134    743   -464    -13       C  
ATOM   3184  CD2 LEU A 261      43.567 -23.261 170.193  1.00131.26           C  
ANISOU 3184  CD2 LEU A 261    16465  19959  13450    849   -518   -168       C  
ATOM   3185  N   LEU A 262      48.721 -21.343 169.249  1.00127.33           N  
ANISOU 3185  N   LEU A 262    16419  18861  13100    482     98    210       N  
ATOM   3186  CA  LEU A 262      49.692 -20.578 168.458  1.00128.73           C  
ANISOU 3186  CA  LEU A 262    16789  18877  13248    477    303    285       C  
ATOM   3187  C   LEU A 262      50.420 -21.438 167.412  1.00134.95           C  
ANISOU 3187  C   LEU A 262    17560  19670  14044    438    378    262       C  
ATOM   3188  O   LEU A 262      50.891 -20.906 166.407  1.00136.15           O  
ANISOU 3188  O   LEU A 262    17911  19715  14103    500    545    320       O  
ATOM   3189  CB  LEU A 262      50.705 -19.862 169.362  1.00128.51           C  
ANISOU 3189  CB  LEU A 262    16753  18675  13401    310    421    308       C  
ATOM   3190  CG  LEU A 262      50.232 -18.555 169.999  1.00133.76           C  
ANISOU 3190  CG  LEU A 262    17536  19263  14023    368    444    362       C  
ATOM   3191  CD1 LEU A 262      51.070 -18.203 171.206  1.00133.16           C  
ANISOU 3191  CD1 LEU A 262    17352  19078  14164    185    482    331       C  
ATOM   3192  CD2 LEU A 262      50.250 -17.405 169.001  1.00138.91           C  
ANISOU 3192  CD2 LEU A 262    18476  19788  14514    509    631    454       C  
ATOM   3193  N   CYS A 263      50.473 -22.767 167.635  1.00131.91           N  
ANISOU 3193  N   CYS A 263    16952  19401  13765    344    270    179       N  
ATOM   3194  CA  CYS A 263      51.125 -23.745 166.762  1.00132.49           C  
ANISOU 3194  CA  CYS A 263    16971  19498  13870    290    322    145       C  
ATOM   3195  C   CYS A 263      50.167 -24.461 165.802  1.00138.57           C  
ANISOU 3195  C   CYS A 263    17731  20445  14473    450    219     89       C  
ATOM   3196  O   CYS A 263      50.561 -24.765 164.675  1.00139.08           O  
ANISOU 3196  O   CYS A 263    17874  20506  14463    489    301     92       O  
ATOM   3197  CB  CYS A 263      51.930 -24.748 167.587  1.00131.30           C  
ANISOU 3197  CB  CYS A 263    16588  19345  13955     82    294     86       C  
ATOM   3198  SG  CYS A 263      53.420 -24.064 168.362  1.00135.03           S  
ANISOU 3198  SG  CYS A 263    17058  19607  14639   -105    437    105       S  
ATOM   3199  N   TRP A 264      48.937 -24.764 166.250  1.00136.33           N  
ANISOU 3199  N   TRP A 264    17341  20314  14143    538     47     22       N  
ATOM   3200  CA  TRP A 264      47.965 -25.504 165.446  1.00137.76           C  
ANISOU 3200  CA  TRP A 264    17465  20680  14198    686    -67    -78       C  
ATOM   3201  C   TRP A 264      46.906 -24.660 164.742  1.00145.31           C  
ANISOU 3201  C   TRP A 264    18602  21706  14903    951   -129    -77       C  
ATOM   3202  O   TRP A 264      46.433 -25.076 163.684  1.00145.90           O  
ANISOU 3202  O   TRP A 264    18700  21904  14831   1105   -180   -148       O  
ATOM   3203  CB  TRP A 264      47.291 -26.593 166.277  1.00135.52           C  
ANISOU 3203  CB  TRP A 264    16916  20524  14050    612   -201   -198       C  
ATOM   3204  CG  TRP A 264      48.105 -27.843 166.407  1.00135.69           C  
ANISOU 3204  CG  TRP A 264    16758  20545  14252    430   -160   -239       C  
ATOM   3205  CD1 TRP A 264      48.682 -28.331 167.543  1.00137.34           C  
ANISOU 3205  CD1 TRP A 264    16831  20692  14661    250   -146   -230       C  
ATOM   3206  CD2 TRP A 264      48.427 -28.772 165.361  1.00135.96           C  
ANISOU 3206  CD2 TRP A 264    16739  20647  14273    424   -127   -296       C  
ATOM   3207  NE1 TRP A 264      49.328 -29.515 167.276  1.00136.47           N  
ANISOU 3207  NE1 TRP A 264    16585  20603  14664    136   -107   -275       N  
ATOM   3208  CE2 TRP A 264      49.185 -29.812 165.943  1.00138.93           C  
ANISOU 3208  CE2 TRP A 264    16938  20993  14858    228    -90   -317       C  
ATOM   3209  CE3 TRP A 264      48.128 -28.839 163.988  1.00138.44           C  
ANISOU 3209  CE3 TRP A 264    17143  21048  14410    580   -130   -337       C  
ATOM   3210  CZ2 TRP A 264      49.665 -30.899 165.196  1.00138.24           C  
ANISOU 3210  CZ2 TRP A 264    16752  20952  14820    166    -46   -372       C  
ATOM   3211  CZ3 TRP A 264      48.603 -29.914 163.250  1.00139.85           C  
ANISOU 3211  CZ3 TRP A 264    17224  21277  14635    517    -91   -397       C  
ATOM   3212  CH2 TRP A 264      49.361 -30.928 163.852  1.00139.23           C  
ANISOU 3212  CH2 TRP A 264    16959  21160  14780    303    -44   -412       C  
ATOM   3213  N   LEU A 265      46.507 -23.512 165.324  1.00144.03           N  
ANISOU 3213  N   LEU A 265    18560  21476  14687   1018   -133     -8       N  
ATOM   3214  CA  LEU A 265      45.514 -22.618 164.718  1.00146.31           C  
ANISOU 3214  CA  LEU A 265    19038  21821  14732   1287   -191      2       C  
ATOM   3215  C   LEU A 265      45.993 -22.048 163.361  1.00154.24           C  
ANISOU 3215  C   LEU A 265    20325  22754  15526   1447    -55     88       C  
ATOM   3216  O   LEU A 265      45.216 -22.148 162.411  1.00155.38           O  
ANISOU 3216  O   LEU A 265    20542  23036  15460   1685   -149     23       O  
ATOM   3217  CB  LEU A 265      45.080 -21.497 165.681  1.00146.21           C  
ANISOU 3217  CB  LEU A 265    19099  21731  14724   1305   -203     68       C  
ATOM   3218  CG  LEU A 265      43.606 -21.121 165.687  1.00151.76           C  
ANISOU 3218  CG  LEU A 265    19812  22571  15280   1527   -369     -6       C  
ATOM   3219  CD1 LEU A 265      42.806 -22.049 166.591  1.00150.63           C  
ANISOU 3219  CD1 LEU A 265    19377  22558  15298   1437   -526   -154       C  
ATOM   3220  CD2 LEU A 265      43.427 -19.695 166.159  1.00154.86           C  
ANISOU 3220  CD2 LEU A 265    20396  22841  15603   1597   -313    111       C  
ATOM   3221  N   PRO A 266      47.254 -21.539 163.191  1.00152.52           N  
ANISOU 3221  N   PRO A 266    20262  22329  15362   1332    167    211       N  
ATOM   3222  CA  PRO A 266      47.670 -21.042 161.864  1.00154.98           C  
ANISOU 3222  CA  PRO A 266    20865  22555  15467   1496    325    291       C  
ATOM   3223  C   PRO A 266      47.640 -22.080 160.739  1.00161.94           C  
ANISOU 3223  C   PRO A 266    21708  23571  16252   1577    275    207       C  
ATOM   3224  O   PRO A 266      47.397 -21.700 159.599  1.00163.53           O  
ANISOU 3224  O   PRO A 266    22153  23786  16196   1822    314    237       O  
ATOM   3225  CB  PRO A 266      49.085 -20.511 162.109  1.00156.50           C  
ANISOU 3225  CB  PRO A 266    21151  22491  15822   1291    583    397       C  
ATOM   3226  CG  PRO A 266      49.137 -20.231 163.562  1.00159.18           C  
ANISOU 3226  CG  PRO A 266    21325  22784  16371   1109    539    393       C  
ATOM   3227  CD  PRO A 266      48.337 -21.331 164.175  1.00153.07           C  
ANISOU 3227  CD  PRO A 266    20261  22224  15676   1068    294    269       C  
ATOM   3228  N   TYR A 267      47.853 -23.375 161.050  1.00158.94           N  
ANISOU 3228  N   TYR A 267    21037  23291  16063   1390    192    100       N  
ATOM   3229  CA  TYR A 267      47.804 -24.443 160.046  1.00160.23           C  
ANISOU 3229  CA  TYR A 267    21128  23592  16160   1447    141      2       C  
ATOM   3230  C   TYR A 267      46.368 -24.733 159.606  1.00166.54           C  
ANISOU 3230  C   TYR A 267    21868  24632  16776   1699    -83   -141       C  
ATOM   3231  O   TYR A 267      46.128 -24.883 158.410  1.00167.57           O  
ANISOU 3231  O   TYR A 267    22123  24852  16693   1908   -105   -183       O  
ATOM   3232  CB  TYR A 267      48.499 -25.725 160.542  1.00160.11           C  
ANISOU 3232  CB  TYR A 267    20823  23594  16417   1167    142    -66       C  
ATOM   3233  CG  TYR A 267      48.578 -26.818 159.495  1.00163.13           C  
ANISOU 3233  CG  TYR A 267    21131  24098  16753   1199    119   -163       C  
ATOM   3234  CD1 TYR A 267      49.603 -26.836 158.552  1.00166.17           C  
ANISOU 3234  CD1 TYR A 267    21674  24367  17096   1172    298    -93       C  
ATOM   3235  CD2 TYR A 267      47.632 -27.839 159.449  1.00163.86           C  
ANISOU 3235  CD2 TYR A 267    20988  24414  16856   1250    -65   -337       C  
ATOM   3236  CE1 TYR A 267      49.676 -27.835 157.580  1.00167.96           C  
ANISOU 3236  CE1 TYR A 267    21835  24706  17276   1202    278   -182       C  
ATOM   3237  CE2 TYR A 267      47.693 -28.841 158.481  1.00165.49           C  
ANISOU 3237  CE2 TYR A 267    21115  24738  17027   1278    -83   -441       C  
ATOM   3238  CZ  TYR A 267      48.719 -28.837 157.549  1.00174.51           C  
ANISOU 3238  CZ  TYR A 267    22423  25770  18112   1256     82   -357       C  
ATOM   3239  OH  TYR A 267      48.789 -29.826 156.594  1.00176.03           O  
ANISOU 3239  OH  TYR A 267    22539  26078  18267   1282     66   -461       O  
ATOM   3240  N   ASN A 268      45.430 -24.832 160.572  1.00163.75           N  
ANISOU 3240  N   ASN A 268    21321  24383  16512   1684   -246   -230       N  
ATOM   3241  CA  ASN A 268      44.006 -25.106 160.335  1.00165.00           C  
ANISOU 3241  CA  ASN A 268    21374  24768  16550   1901   -464   -405       C  
ATOM   3242  C   ASN A 268      43.295 -23.942 159.633  1.00172.22           C  
ANISOU 3242  C   ASN A 268    22575  25707  17155   2238   -509   -365       C  
ATOM   3243  O   ASN A 268      42.375 -24.182 158.847  1.00173.28           O  
ANISOU 3243  O   ASN A 268    22698  26032  17109   2489   -665   -514       O  
ATOM   3244  CB  ASN A 268      43.287 -25.471 161.645  1.00164.56           C  
ANISOU 3244  CB  ASN A 268    21049  24773  16702   1770   -583   -504       C  
ATOM   3245  CG  ASN A 268      43.772 -26.742 162.311  1.00184.12           C  
ANISOU 3245  CG  ASN A 268    23244  27257  19456   1492   -559   -571       C  
ATOM   3246  OD1 ASN A 268      43.841 -27.820 161.703  1.00178.04           O  
ANISOU 3246  OD1 ASN A 268    22333  26594  18720   1470   -579   -689       O  
ATOM   3247  ND2 ASN A 268      44.101 -26.645 163.591  1.00173.62           N  
ANISOU 3247  ND2 ASN A 268    21831  25813  18324   1286   -513   -501       N  
ATOM   3248  N   LEU A 269      43.716 -22.688 159.919  1.00169.94           N  
ANISOU 3248  N   LEU A 269    22538  25226  16808   2253   -369   -178       N  
ATOM   3249  CA  LEU A 269      43.153 -21.482 159.301  1.00172.35           C  
ANISOU 3249  CA  LEU A 269    23157  25513  16815   2573   -370   -105       C  
ATOM   3250  C   LEU A 269      43.598 -21.368 157.833  1.00179.90           C  
ANISOU 3250  C   LEU A 269    24394  26445  17516   2782   -264    -50       C  
ATOM   3251  O   LEU A 269      42.792 -20.981 156.983  1.00181.63           O  
ANISOU 3251  O   LEU A 269    24789  26779  17442   3128   -368    -96       O  
ATOM   3252  CB  LEU A 269      43.510 -20.213 160.101  1.00172.05           C  
ANISOU 3252  CB  LEU A 269    23295  25258  16820   2502   -221     76       C  
ATOM   3253  CG  LEU A 269      42.824 -20.038 161.469  1.00175.13           C  
ANISOU 3253  CG  LEU A 269    23482  25678  17379   2389   -343     30       C  
ATOM   3254  CD1 LEU A 269      43.628 -19.122 162.366  1.00174.41           C  
ANISOU 3254  CD1 LEU A 269    23490  25351  17426   2199   -156    197       C  
ATOM   3255  CD2 LEU A 269      41.401 -19.510 161.330  1.00178.86           C  
ANISOU 3255  CD2 LEU A 269    24003  26303  17654   2690   -534    -58       C  
ATOM   3256  N   VAL A 270      44.865 -21.742 157.537  1.00177.13           N  
ANISOU 3256  N   VAL A 270    24081  25947  17272   2582    -63     36       N  
ATOM   3257  CA  VAL A 270      45.435 -21.772 156.181  1.00179.28           C  
ANISOU 3257  CA  VAL A 270    24608  26172  17339   2733     71     89       C  
ATOM   3258  C   VAL A 270      44.800 -22.955 155.411  1.00185.19           C  
ANISOU 3258  C   VAL A 270    25174  27187  18005   2857   -135   -116       C  
ATOM   3259  O   VAL A 270      44.542 -22.832 154.210  1.00187.07           O  
ANISOU 3259  O   VAL A 270    25634  27496  17949   3155   -154   -135       O  
ATOM   3260  CB  VAL A 270      46.998 -21.786 156.203  1.00182.37           C  
ANISOU 3260  CB  VAL A 270    25072  26306  17912   2454    364    226       C  
ATOM   3261  CG1 VAL A 270      47.602 -22.254 154.879  1.00183.49           C  
ANISOU 3261  CG1 VAL A 270    25377  26430  17913   2540    481    235       C  
ATOM   3262  CG2 VAL A 270      47.549 -20.413 156.574  1.00182.78           C  
ANISOU 3262  CG2 VAL A 270    25393  26090  17963   2432    599    411       C  
ATOM   3263  N   LEU A 271      44.497 -24.069 156.128  1.00180.98           N  
ANISOU 3263  N   LEU A 271    24244  26799  17723   2647   -286   -278       N  
ATOM   3264  CA  LEU A 271      43.853 -25.276 155.590  1.00181.51           C  
ANISOU 3264  CA  LEU A 271    24069  27117  17779   2717   -475   -508       C  
ATOM   3265  C   LEU A 271      42.476 -24.940 155.004  1.00188.30           C  
ANISOU 3265  C   LEU A 271    24987  28193  18366   3103   -701   -659       C  
ATOM   3266  O   LEU A 271      42.163 -25.392 153.902  1.00189.68           O  
ANISOU 3266  O   LEU A 271    25194  28525  18348   3323   -791   -786       O  
ATOM   3267  CB  LEU A 271      43.725 -26.360 156.676  1.00179.18           C  
ANISOU 3267  CB  LEU A 271    23359  26895  17826   2415   -556   -638       C  
ATOM   3268  CG  LEU A 271      43.464 -27.783 156.185  1.00183.81           C  
ANISOU 3268  CG  LEU A 271    23670  27678  18491   2380   -660   -855       C  
ATOM   3269  CD1 LEU A 271      44.739 -28.614 156.210  1.00182.56           C  
ANISOU 3269  CD1 LEU A 271    23423  27403  18540   2081   -490   -785       C  
ATOM   3270  CD2 LEU A 271      42.384 -28.451 157.013  1.00185.31           C  
ANISOU 3270  CD2 LEU A 271    23516  28033  18859   2327   -839  -1070       C  
ATOM   3271  N   LEU A 272      41.677 -24.124 155.729  1.00185.27           N  
ANISOU 3271  N   LEU A 272    24619  27815  17959   3196   -794   -653       N  
ATOM   3272  CA  LEU A 272      40.351 -23.669 155.299  1.00187.29           C  
ANISOU 3272  CA  LEU A 272    24931  28264  17968   3570  -1015   -797       C  
ATOM   3273  C   LEU A 272      40.460 -22.737 154.080  1.00194.80           C  
ANISOU 3273  C   LEU A 272    26324  29168  18524   3937   -950   -674       C  
ATOM   3274  O   LEU A 272      39.642 -22.830 153.164  1.00196.29           O  
ANISOU 3274  O   LEU A 272    26564  29560  18455   4285  -1133   -835       O  
ATOM   3275  CB  LEU A 272      39.621 -22.959 156.455  1.00186.38           C  
ANISOU 3275  CB  LEU A 272    24742  28124  17949   3544  -1092   -790       C  
ATOM   3276  CG  LEU A 272      38.984 -23.860 157.512  1.00188.92           C  
ANISOU 3276  CG  LEU A 272    24638  28562  18583   3320  -1226   -988       C  
ATOM   3277  CD1 LEU A 272      39.092 -23.243 158.888  1.00187.27           C  
ANISOU 3277  CD1 LEU A 272    24399  28188  18567   3103  -1150   -853       C  
ATOM   3278  CD2 LEU A 272      37.531 -24.145 157.187  1.00192.50           C  
ANISOU 3278  CD2 LEU A 272    24917  29281  18943   3588  -1494  -1282       C  
ATOM   3279  N   ALA A 273      41.494 -21.868 154.068  1.00192.31           N  
ANISOU 3279  N   ALA A 273    26325  28577  18167   3864   -679   -401       N  
ATOM   3280  CA  ALA A 273      41.777 -20.897 153.008  1.00195.17           C  
ANISOU 3280  CA  ALA A 273    27158  28823  18177   4179   -535   -238       C  
ATOM   3281  C   ALA A 273      42.164 -21.532 151.667  1.00201.65           C  
ANISOU 3281  C   ALA A 273    28106  29708  18804   4330   -503   -282       C  
ATOM   3282  O   ALA A 273      41.870 -20.947 150.623  1.00204.18           O  
ANISOU 3282  O   ALA A 273    28771  30052  18755   4722   -505   -247       O  
ATOM   3283  CB  ALA A 273      42.858 -19.929 153.463  1.00195.36           C  
ANISOU 3283  CB  ALA A 273    27432  28511  18284   3994   -213     37       C  
ATOM   3284  N   ASP A 274      42.827 -22.709 151.689  1.00197.20           N  
ANISOU 3284  N   ASP A 274    27281  29168  18478   4035   -468   -355       N  
ATOM   3285  CA  ASP A 274      43.255 -23.425 150.478  1.00198.60           C  
ANISOU 3285  CA  ASP A 274    27539  29406  18514   4130   -431   -407       C  
ATOM   3286  C   ASP A 274      42.227 -24.443 149.969  1.00203.75           C  
ANISOU 3286  C   ASP A 274    27918  30401  19097   4308   -739   -715       C  
ATOM   3287  O   ASP A 274      42.200 -24.728 148.767  1.00205.36           O  
ANISOU 3287  O   ASP A 274    28274  30707  19046   4560   -773   -783       O  
ATOM   3288  CB  ASP A 274      44.633 -24.077 150.671  1.00198.51           C  
ANISOU 3288  CB  ASP A 274    27432  29209  18784   3728   -194   -307       C  
ATOM   3289  CG  ASP A 274      45.793 -23.119 150.481  1.00208.20           C  
ANISOU 3289  CG  ASP A 274    29038  30101  19967   3669    153    -36       C  
ATOM   3290  OD1 ASP A 274      45.918 -22.174 151.286  1.00213.71           O  
ANISOU 3290  OD1 ASP A 274    29833  30628  20738   3596    259    101       O  
ATOM   3291  OD2 ASP A 274      46.576 -23.318 149.528  1.00209.35           O  
ANISOU 3291  OD2 ASP A 274    29377  30147  20017   3689    331     27       O  
ATOM   3292  N   THR A 275      41.387 -24.989 150.877  1.00198.83           N  
ANISOU 3292  N   THR A 275    26894  29948  18705   4181   -949   -914       N  
ATOM   3293  CA  THR A 275      40.325 -25.942 150.530  1.00199.33           C  
ANISOU 3293  CA  THR A 275    26646  30331  18758   4325  -1232  -1248       C  
ATOM   3294  C   THR A 275      39.113 -25.213 149.928  1.00205.79           C  
ANISOU 3294  C   THR A 275    27631  31334  19226   4812  -1459  -1376       C  
ATOM   3295  O   THR A 275      38.535 -25.700 148.951  1.00207.26           O  
ANISOU 3295  O   THR A 275    27780  31753  19216   5093  -1641  -1600       O  
ATOM   3296  CB  THR A 275      39.957 -26.845 151.717  1.00205.04           C  
ANISOU 3296  CB  THR A 275    26891  31133  19883   3991  -1322  -1417       C  
ATOM   3297  OG1 THR A 275      39.717 -26.041 152.874  1.00203.61           O  
ANISOU 3297  OG1 THR A 275    26711  30831  19821   3888  -1301  -1303       O  
ATOM   3298  CG2 THR A 275      41.021 -27.905 152.003  1.00200.90           C  
ANISOU 3298  CG2 THR A 275    26161  30511  19659   3589  -1157  -1376       C  
ATOM   3299  N   LEU A 276      38.752 -24.034 150.497  1.00202.44           N  
ANISOU 3299  N   LEU A 276    27392  30806  18720   4923  -1451  -1240       N  
ATOM   3300  CA  LEU A 276      37.649 -23.190 150.018  1.00204.84           C  
ANISOU 3300  CA  LEU A 276    27888  31255  18687   5394  -1652  -1328       C  
ATOM   3301  C   LEU A 276      38.031 -22.354 148.776  1.00210.11           C  
ANISOU 3301  C   LEU A 276    29084  31835  18913   5778  -1539  -1149       C  
ATOM   3302  O   LEU A 276      37.147 -21.770 148.143  1.00212.10           O  
ANISOU 3302  O   LEU A 276    29518  32190  18882   6152  -1708  -1225       O  
ATOM   3303  CB  LEU A 276      37.084 -22.301 151.142  1.00204.10           C  
ANISOU 3303  CB  LEU A 276    27769  31086  18695   5351  -1683  -1261       C  
ATOM   3304  CG  LEU A 276      36.115 -22.979 152.111  1.00207.16           C  
ANISOU 3304  CG  LEU A 276    27674  31649  19391   5181  -1895  -1533       C  
ATOM   3305  CD1 LEU A 276      36.230 -22.387 153.497  1.00205.36           C  
ANISOU 3305  CD1 LEU A 276    27392  31230  19404   4904  -1788  -1370       C  
ATOM   3306  CD2 LEU A 276      34.679 -22.887 151.615  1.00209.98           C  
ANISOU 3306  CD2 LEU A 276    27942  32297  19545   5597  -2217  -1841       C  
ATOM   3307  N   MET A 277      39.341 -22.312 148.426  1.00205.42           N  
ANISOU 3307  N   MET A 277    28731  30997  18323   5604  -1234   -903       N  
ATOM   3308  CA  MET A 277      39.873 -21.627 147.240  1.00207.76           C  
ANISOU 3308  CA  MET A 277    29545  31162  18231   5922  -1058   -717       C  
ATOM   3309  C   MET A 277      39.440 -22.428 145.995  1.00212.78           C  
ANISOU 3309  C   MET A 277    30129  31981  18736   6053  -1239   -930       C  
ATOM   3310  O   MET A 277      39.078 -21.837 144.973  1.00213.47           O  
ANISOU 3310  O   MET A 277    30471  31900  18738   6008  -1236   -857       O  
ATOM   3311  CB  MET A 277      41.411 -21.523 147.316  1.00208.50           C  
ANISOU 3311  CB  MET A 277    29821  30918  18480   5584   -666   -437       C  
ATOM   3312  CG  MET A 277      41.991 -20.366 146.514  1.00214.29           C  
ANISOU 3312  CG  MET A 277    31147  31399  18874   5857   -388   -168       C  
ATOM   3313  SD  MET A 277      43.787 -20.481 146.283  1.00217.28           S  
ANISOU 3313  SD  MET A 277    31715  31413  19430   5493     67     80       S  
ATOM   3314  CE  MET A 277      44.120 -18.896 145.558  1.00216.44           C  
ANISOU 3314  CE  MET A 277    32238  30974  19024   5717    380    365       C  
ATOM   3315  N   ARG A 278      39.451 -23.778 146.109  1.00207.88           N  
ANISOU 3315  N   ARG A 278    29105  31614  18265   5973  -1372  -1177       N  
ATOM   3316  CA  ARG A 278      39.023 -24.716 145.068  1.00209.22           C  
ANISOU 3316  CA  ARG A 278    29154  32062  18279   6198  -1576  -1452       C  
ATOM   3317  C   ARG A 278      37.490 -24.733 144.995  1.00211.61           C  
ANISOU 3317  C   ARG A 278    29211  32365  18827   5983  -1863  -1660       C  
ATOM   3318  O   ARG A 278      36.931 -24.680 143.899  1.00211.60           O  
ANISOU 3318  O   ARG A 278    29326  32293  18778   5950  -1952  -1702       O  
ATOM   3319  CB  ARG A 278      39.538 -26.135 145.366  1.00206.15           C  
ANISOU 3319  CB  ARG A 278    28334  31721  18274   5762  -1544  -1583       C  
ATOM   3320  CG  ARG A 278      41.042 -26.321 145.200  1.00213.66           C  
ANISOU 3320  CG  ARG A 278    29454  32393  19335   5455  -1202  -1321       C  
ATOM   3321  CD  ARG A 278      41.371 -27.651 144.544  1.00219.07           C  
ANISOU 3321  CD  ARG A 278    29908  33142  20185   5225  -1213  -1476       C  
ATOM   3322  NE  ARG A 278      40.965 -28.800 145.359  1.00224.16           N  
ANISOU 3322  NE  ARG A 278    30005  33936  21229   4903  -1353  -1715       N  
ATOM   3323  CZ  ARG A 278      40.880 -30.049 144.910  1.00232.87           C  
ANISOU 3323  CZ  ARG A 278    30876  34755  22849   4245  -1342  -1794       C  
ATOM   3324  NH1 ARG A 278      41.165 -30.328 143.644  1.00225.40           N  
ANISOU 3324  NH1 ARG A 278    30072  34247  21324   4917  -1413  -1960       N  
ATOM   3325  NH2 ARG A 278      40.502 -31.027 145.722  1.00219.07           N  
ANISOU 3325  NH2 ARG A 278    28572  33685  20981   4656  -1559  -2198       N  
ATOM   3326  N   THR A 279      36.823 -24.809 146.173  1.00208.67           N  
ANISOU 3326  N   THR A 279    28520  32306  18460   6225  -2059  -1874       N  
ATOM   3327  CA  THR A 279      35.363 -24.841 146.329  1.00226.18           C  
ANISOU 3327  CA  THR A 279    30463  33808  21667   4938  -2083  -1771       C  
ATOM   3328  C   THR A 279      34.829 -23.460 146.717  1.00241.90           C  
ANISOU 3328  C   THR A 279    32582  34762  24566   3509  -1794  -1222       C  
ATOM   3329  O   THR A 279      33.640 -23.182 146.565  1.00213.00           O  
ANISOU 3329  O   THR A 279    28966  32526  19438   5841  -2445  -1946       O  
ATOM   3330  CB  THR A 279      34.948 -25.911 147.356  1.00229.82           C  
ANISOU 3330  CB  THR A 279    30454  34272  22595   4569  -2150  -1951       C  
ATOM   3331  OG1 THR A 279      35.600 -25.655 148.601  1.00228.53           O  
ANISOU 3331  OG1 THR A 279    30217  34263  22350   4741  -2073  -1909       O  
ATOM   3332  CG2 THR A 279      35.244 -27.334 146.885  1.00228.70           C  
ANISOU 3332  CG2 THR A 279    30062  34347  22487   4603  -2196  -2189       C  
ATOM   3333  N   ARG A 289      48.373 -20.295 144.659  1.00212.67           N  
ANISOU 3333  N   ARG A 289    31958  29804  19042   4894   1370    676       N  
ATOM   3334  CA  ARG A 289      49.276 -19.151 144.759  1.00213.43           C  
ANISOU 3334  CA  ARG A 289    32425  29499  19171   4822   1797    918       C  
ATOM   3335  C   ARG A 289      50.531 -19.489 145.571  1.00214.28           C  
ANISOU 3335  C   ARG A 289    32273  29381  19761   4278   2030    955       C  
ATOM   3336  O   ARG A 289      50.446 -20.249 146.535  1.00210.94           O  
ANISOU 3336  O   ARG A 289    31371  29112  19666   3963   1820    829       O  
ATOM   3337  CB  ARG A 289      48.554 -17.957 145.386  1.00 30.00           C  
ATOM   3338  N   ASN A 290      51.689 -18.914 145.178  1.00212.15           N  
ANISOU 3338  N   ASN A 290    32330  28743  19535   4181   2474   1120       N  
ATOM   3339  CA  ASN A 290      52.992 -19.103 145.831  1.00209.64           C  
ANISOU 3339  CA  ASN A 290    31817  28172  19663   3696   2740   1148       C  
ATOM   3340  C   ASN A 290      53.014 -18.514 147.246  1.00210.30           C  
ANISOU 3340  C   ASN A 290    31675  28179  20050   3441   2733   1165       C  
ATOM   3341  O   ASN A 290      53.662 -19.081 148.129  1.00207.16           O  
ANISOU 3341  O   ASN A 290    30899  27760  20054   3034   2721   1094       O  
ATOM   3342  CB  ASN A 290      54.118 -18.499 144.975  1.00213.23           C  
ANISOU 3342  CB  ASN A 290    32719  28237  20063   3709   3239   1301       C  
ATOM   3343  CG  ASN A 290      55.515 -18.679 145.530  1.00235.16           C  
ANISOU 3343  CG  ASN A 290    35235  30766  23347   3164   3496   1283       C  
ATOM   3344  OD1 ASN A 290      55.950 -19.788 145.864  1.00226.29           O  
ANISOU 3344  OD1 ASN A 290    33784  29735  22462   2921   3399   1178       O  
ATOM   3345  ND2 ASN A 290      56.254 -17.584 145.631  1.00229.07           N  
ANISOU 3345  ND2 ASN A 290    34822  29596  22619   3164   3950   1429       N  
ATOM   3346  N   HIS A 291      52.306 -17.382 147.451  1.00208.34           N  
ANISOU 3346  N   HIS A 291    31668  27893  19600   3695   2737   1256       N  
ATOM   3347  CA  HIS A 291      52.186 -16.677 148.734  1.00206.80           C  
ANISOU 3347  CA  HIS A 291    31311  27629  19635   3514   2727   1281       C  
ATOM   3348  C   HIS A 291      51.440 -17.528 149.767  1.00206.36           C  
ANISOU 3348  C   HIS A 291    30733  27901  19772   3349   2295   1115       C  
ATOM   3349  O   HIS A 291      51.783 -17.493 150.949  1.00203.31           O  
ANISOU 3349  O   HIS A 291    30062  27461  19727   3025   2290   1090       O  
ATOM   3350  CB  HIS A 291      51.467 -15.328 148.550  1.00210.41           C  
ANISOU 3350  CB  HIS A 291    32176  27996  19774   3883   2813   1414       C  
ATOM   3351  CG  HIS A 291      52.121 -14.420 147.556  1.00217.34           C  
ANISOU 3351  CG  HIS A 291    33609  28530  20441   4079   3267   1588       C  
ATOM   3352  ND1 HIS A 291      53.074 -13.497 147.941  1.00219.57           N  
ANISOU 3352  ND1 HIS A 291    34051  28430  20944   3870   3695   1699       N  
ATOM   3353  CD2 HIS A 291      51.935 -14.327 146.219  1.00221.96           C  
ANISOU 3353  CD2 HIS A 291    34561  29113  20660   4408   3334   1642       C  
ATOM   3354  CE1 HIS A 291      53.437 -12.873 146.832  1.00221.45           C  
ANISOU 3354  CE1 HIS A 291    34671  28466  21005   4005   3985   1802       C  
ATOM   3355  NE2 HIS A 291      52.779 -13.339 145.770  1.00222.01           N  
ANISOU 3355  NE2 HIS A 291    34689  28817  20847   4145   3684   1731       N  
ATOM   3356  N   ILE A 292      50.422 -18.289 149.308  1.00202.34           N  
ANISOU 3356  N   ILE A 292    30107  27726  19047   3580   1945    990       N  
ATOM   3357  CA  ILE A 292      49.600 -19.174 150.132  1.00199.35           C  
ANISOU 3357  CA  ILE A 292    29255  27665  18824   3465   1548    812       C  
ATOM   3358  C   ILE A 292      50.204 -20.595 150.208  1.00200.21           C  
ANISOU 3358  C   ILE A 292    28994  27872  19204   3150   1476    685       C  
ATOM   3359  O   ILE A 292      49.876 -21.345 151.129  1.00197.39           O  
ANISOU 3359  O   ILE A 292    28221  27689  19089   2936   1245    559       O  
ATOM   3360  CB  ILE A 292      48.113 -19.140 149.669  1.00203.93           C  
ANISOU 3360  CB  ILE A 292    29889  28544  19052   3889   1220    714       C  
ATOM   3361  CG1 ILE A 292      47.155 -19.162 150.876  1.00202.38           C  
ANISOU 3361  CG1 ILE A 292    29357  28533  19005   3815    930    611       C  
ATOM   3362  CG2 ILE A 292      47.773 -20.222 148.623  1.00205.54           C  
ANISOU 3362  CG2 ILE A 292    30022  28994  19078   4060   1029    562       C  
ATOM   3363  CD1 ILE A 292      45.826 -18.416 150.674  1.00210.21           C  
ANISOU 3363  CD1 ILE A 292    30524  29680  19667   4239    726    586       C  
ATOM   3364  N   ASP A 293      51.087 -20.949 149.247  1.00196.83           N  
ANISOU 3364  N   ASP A 293    28734  27318  18735   3127   1692    723       N  
ATOM   3365  CA  ASP A 293      51.770 -22.244 149.188  1.00194.47           C  
ANISOU 3365  CA  ASP A 293    28131  27079  18680   2841   1668    619       C  
ATOM   3366  C   ASP A 293      52.884 -22.294 150.237  1.00194.99           C  
ANISOU 3366  C   ASP A 293    27978  26937  19174   2401   1844    652       C  
ATOM   3367  O   ASP A 293      52.987 -23.283 150.966  1.00192.07           O  
ANISOU 3367  O   ASP A 293    27200  26699  19079   2135   1678    537       O  
ATOM   3368  CB  ASP A 293      52.335 -22.504 147.777  1.00198.34           C  
ANISOU 3368  CB  ASP A 293    28906  27488  18966   2982   1856    655       C  
ATOM   3369  CG  ASP A 293      52.606 -23.958 147.430  1.00205.94           C  
ANISOU 3369  CG  ASP A 293    29571  28618  20061   2816   1735    512       C  
ATOM   3370  OD1 ASP A 293      52.231 -24.846 148.231  1.00204.11           O  
ANISOU 3370  OD1 ASP A 293    28904  28596  20054   2624   1480    372       O  
ATOM   3371  OD2 ASP A 293      53.184 -24.210 146.352  1.00212.22           O  
ANISOU 3371  OD2 ASP A 293    30577  29326  20732   2883   1909    542       O  
ATOM   3372  N   ARG A 294      53.703 -21.214 150.325  1.00191.65           N  
ANISOU 3372  N   ARG A 294    27825  26186  18808   2339   2185    795       N  
ATOM   3373  CA  ARG A 294      54.793 -21.084 151.300  1.00189.31           C  
ANISOU 3373  CA  ARG A 294    27346  25674  18911   1952   2370    807       C  
ATOM   3374  C   ARG A 294      54.233 -20.806 152.701  1.00189.74           C  
ANISOU 3374  C   ARG A 294    27137  25823  19131   1841   2166    772       C  
ATOM   3375  O   ARG A 294      54.917 -21.064 153.695  1.00187.33           O  
ANISOU 3375  O   ARG A 294    26554  25453  19170   1517   2184    725       O  
ATOM   3376  CB  ARG A 294      55.805 -20.007 150.872  1.00191.77           C  
ANISOU 3376  CB  ARG A 294    28030  25600  19236   1934   2819    940       C  
ATOM   3377  CG  ARG A 294      57.197 -20.224 151.459  1.00201.17           C  
ANISOU 3377  CG  ARG A 294    29016  26568  20850   1526   3040    898       C  
ATOM   3378  CD  ARG A 294      58.232 -19.291 150.866  1.00213.44           C  
ANISOU 3378  CD  ARG A 294    30930  27731  22436   1504   3517    995       C  
ATOM   3379  NE  ARG A 294      59.556 -19.514 151.450  1.00221.40           N  
ANISOU 3379  NE  ARG A 294    31706  28540  23875   1112   3712    915       N  
ATOM   3380  CZ  ARG A 294      60.463 -20.359 150.967  1.00235.42           C  
ANISOU 3380  CZ  ARG A 294    33380  30256  25813    931   3817    850       C  
ATOM   3381  NH1 ARG A 294      60.202 -21.075 149.879  1.00223.11           N  
ANISOU 3381  NH1 ARG A 294    31935  28819  24018   1095   3756    863       N  
ATOM   3382  NH2 ARG A 294      61.637 -20.495 151.567  1.00221.20           N  
ANISOU 3382  NH2 ARG A 294    31355  28279  24412    590   3978    759       N  
ATOM   3383  N   ALA A 295      52.982 -20.293 152.773  1.00185.79           N  
ANISOU 3383  N   ALA A 295    26729  25484  18380   2123   1966    784       N  
ATOM   3384  CA  ALA A 295      52.261 -20.032 154.019  1.00183.33           C  
ANISOU 3384  CA  ALA A 295    26191  25286  18181   2063   1751    747       C  
ATOM   3385  C   ALA A 295      51.952 -21.372 154.692  1.00183.07           C  
ANISOU 3385  C   ALA A 295    25703  25508  18349   1873   1453    590       C  
ATOM   3386  O   ALA A 295      52.157 -21.501 155.898  1.00180.78           O  
ANISOU 3386  O   ALA A 295    25146  25210  18333   1625   1390    555       O  
ATOM   3387  CB  ALA A 295      50.972 -19.274 153.736  1.00185.59           C  
ANISOU 3387  CB  ALA A 295    26695  25693  18128   2438   1608    782       C  
ATOM   3388  N   LEU A 296      51.522 -22.384 153.897  1.00178.32           N  
ANISOU 3388  N   LEU A 296    25021  25117  17617   1988   1291    492       N  
ATOM   3389  CA  LEU A 296      51.238 -23.745 154.368  1.00175.26           C  
ANISOU 3389  CA  LEU A 296    24221  24959  17410   1823   1047    335       C  
ATOM   3390  C   LEU A 296      52.546 -24.483 154.703  1.00175.18           C  
ANISOU 3390  C   LEU A 296    24015  24820  17724   1467   1191    325       C  
ATOM   3391  O   LEU A 296      52.532 -25.401 155.522  1.00172.94           O  
ANISOU 3391  O   LEU A 296    23384  24652  17672   1260   1041    229       O  
ATOM   3392  CB  LEU A 296      50.418 -24.533 153.330  1.00176.45           C  
ANISOU 3392  CB  LEU A 296    24361  25358  17322   2066    861    218       C  
ATOM   3393  CG  LEU A 296      49.426 -25.559 153.896  1.00179.81           C  
ANISOU 3393  CG  LEU A 296    24405  26074  17841   2036    548     31       C  
ATOM   3394  CD1 LEU A 296      48.134 -25.567 153.100  1.00181.77           C  
ANISOU 3394  CD1 LEU A 296    24730  26561  17775   2405    334    -82       C  
ATOM   3395  CD2 LEU A 296      50.025 -26.961 153.930  1.00180.96           C  
ANISOU 3395  CD2 LEU A 296    24253  26282  18221   1780    536    -68       C  
ATOM   3396  N   ASP A 297      53.669 -24.068 154.080  1.00170.68           N  
ANISOU 3396  N   ASP A 297    23676  24001  17173   1406   1492    420       N  
ATOM   3397  CA  ASP A 297      55.005 -24.624 154.308  1.00168.44           C  
ANISOU 3397  CA  ASP A 297    23239  23563  17196   1084   1661    405       C  
ATOM   3398  C   ASP A 297      55.584 -24.099 155.631  1.00167.06           C  
ANISOU 3398  C   ASP A 297    22925  23241  17309    843   1723    422       C  
ATOM   3399  O   ASP A 297      56.357 -24.805 156.282  1.00164.44           O  
ANISOU 3399  O   ASP A 297    22325  22887  17270    572   1719    358       O  
ATOM   3400  CB  ASP A 297      55.932 -24.280 153.122  1.00172.80           C  
ANISOU 3400  CB  ASP A 297    24110  23886  17661   1124   1981    485       C  
ATOM   3401  CG  ASP A 297      57.330 -24.882 153.166  1.00185.27           C  
ANISOU 3401  CG  ASP A 297    25545  25301  19548    811   2170    452       C  
ATOM   3402  OD1 ASP A 297      57.472 -26.030 153.653  1.00184.68           O  
ANISOU 3402  OD1 ASP A 297    25125  25371  19673    621   2003    350       O  
ATOM   3403  OD2 ASP A 297      58.277 -24.215 152.693  1.00192.72           O  
ANISOU 3403  OD2 ASP A 297    26728  25964  20535    762   2496    521       O  
ATOM   3404  N   ALA A 298      55.198 -22.863 156.021  1.00162.25           N  
ANISOU 3404  N   ALA A 298    22501  22538  16609    959   1776    502       N  
ATOM   3405  CA  ALA A 298      55.625 -22.190 157.252  1.00160.20           C  
ANISOU 3405  CA  ALA A 298    22140  22143  16586    772   1834    514       C  
ATOM   3406  C   ALA A 298      54.740 -22.544 158.459  1.00159.66           C  
ANISOU 3406  C   ALA A 298    21786  22286  16591    735   1528    448       C  
ATOM   3407  O   ALA A 298      55.243 -22.586 159.583  1.00157.67           O  
ANISOU 3407  O   ALA A 298    21324  21984  16599    515   1510    410       O  
ATOM   3408  CB  ALA A 298      55.655 -20.685 157.044  1.00162.87           C  
ANISOU 3408  CB  ALA A 298    22826  22261  16795    911   2069    630       C  
ATOM   3409  N   THR A 299      53.429 -22.790 158.233  1.00154.34           N  
ANISOU 3409  N   THR A 299    21106  21843  15691    958   1294    421       N  
ATOM   3410  CA  THR A 299      52.497 -23.177 159.301  1.00151.48           C  
ANISOU 3410  CA  THR A 299    20484  21679  15395    936   1020    346       C  
ATOM   3411  C   THR A 299      52.711 -24.642 159.703  1.00151.69           C  
ANISOU 3411  C   THR A 299    20167  21843  15625    742    882    231       C  
ATOM   3412  O   THR A 299      52.395 -25.015 160.837  1.00150.12           O  
ANISOU 3412  O   THR A 299    19731  21729  15578    630    731    176       O  
ATOM   3413  CB  THR A 299      51.035 -22.869 158.943  1.00158.36           C  
ANISOU 3413  CB  THR A 299    21458  22732  15981   1240    836    331       C  
ATOM   3414  OG1 THR A 299      50.676 -23.539 157.738  1.00157.33           O  
ANISOU 3414  OG1 THR A 299    21385  22737  15655   1413    781    277       O  
ATOM   3415  CG2 THR A 299      50.746 -21.377 158.849  1.00158.34           C  
ANISOU 3415  CG2 THR A 299    21766  22594  15801   1424    950    448       C  
ATOM   3416  N   GLU A 300      53.261 -25.460 158.774  1.00146.47           N  
ANISOU 3416  N   GLU A 300    19497  21191  14962    707    952    201       N  
ATOM   3417  CA  GLU A 300      53.591 -26.875 158.960  1.00143.91           C  
ANISOU 3417  CA  GLU A 300    18880  20975  14825    528    866    101       C  
ATOM   3418  C   GLU A 300      54.659 -27.019 160.050  1.00143.47           C  
ANISOU 3418  C   GLU A 300    18647  20787  15080    248    934    100       C  
ATOM   3419  O   GLU A 300      54.419 -27.713 161.039  1.00141.66           O  
ANISOU 3419  O   GLU A 300    18164  20662  15000    140    781     35       O  
ATOM   3420  CB  GLU A 300      54.109 -27.475 157.642  1.00146.51           C  
ANISOU 3420  CB  GLU A 300    19294  21296  15077    554    976     89       C  
ATOM   3421  CG  GLU A 300      53.287 -28.633 157.101  1.00158.78           C  
ANISOU 3421  CG  GLU A 300    20696  23099  16534    654    792    -29       C  
ATOM   3422  CD  GLU A 300      53.659 -29.065 155.693  1.00180.41           C  
ANISOU 3422  CD  GLU A 300    23564  25840  19142    730    894    -38       C  
ATOM   3423  OE1 GLU A 300      54.788 -29.575 155.499  1.00169.74           O  
ANISOU 3423  OE1 GLU A 300    22158  24374  17963    533   1041    -30       O  
ATOM   3424  OE2 GLU A 300      52.817 -28.897 154.782  1.00174.90           O  
ANISOU 3424  OE2 GLU A 300    23024  25265  18167    998    822    -64       O  
ATOM   3425  N   ILE A 301      55.806 -26.313 159.893  1.00138.19           N  
ANISOU 3425  N   ILE A 301    18120  19882  14504    147   1168    160       N  
ATOM   3426  CA  ILE A 301      56.936 -26.329 160.828  1.00135.94           C  
ANISOU 3426  CA  ILE A 301    17681  19455  14515   -101   1248    134       C  
ATOM   3427  C   ILE A 301      56.561 -25.746 162.222  1.00135.02           C  
ANISOU 3427  C   ILE A 301    17468  19349  14483   -134   1132    132       C  
ATOM   3428  O   ILE A 301      57.210 -26.096 163.210  1.00133.39           O  
ANISOU 3428  O   ILE A 301    17057  19119  14508   -311   1092     76       O  
ATOM   3429  CB  ILE A 301      58.199 -25.669 160.198  1.00140.75           C  
ANISOU 3429  CB  ILE A 301    18472  19801  15206   -185   1551    169       C  
ATOM   3430  CG1 ILE A 301      59.499 -26.234 160.809  1.00140.48           C  
ANISOU 3430  CG1 ILE A 301    18211  19665  15498   -451   1614     84       C  
ATOM   3431  CG2 ILE A 301      58.161 -24.130 160.233  1.00143.24           C  
ANISOU 3431  CG2 ILE A 301    19049  19938  15438    -93   1717    250       C  
ATOM   3432  CD1 ILE A 301      60.658 -26.362 159.819  1.00149.95           C  
ANISOU 3432  CD1 ILE A 301    19507  20681  16787   -548   1873     72       C  
ATOM   3433  N   LEU A 302      55.513 -24.892 162.299  1.00129.06           N  
ANISOU 3433  N   LEU A 302    16863  18637  13535     49   1070    188       N  
ATOM   3434  CA  LEU A 302      55.032 -24.322 163.560  1.00126.66           C  
ANISOU 3434  CA  LEU A 302    16487  18352  13286     36    957    190       C  
ATOM   3435  C   LEU A 302      54.347 -25.408 164.384  1.00126.40           C  
ANISOU 3435  C   LEU A 302    16189  18521  13316      1    716    115       C  
ATOM   3436  O   LEU A 302      54.596 -25.506 165.585  1.00124.68           O  
ANISOU 3436  O   LEU A 302    15813  18291  13268   -123    649     84       O  
ATOM   3437  CB  LEU A 302      54.054 -23.162 163.314  1.00127.70           C  
ANISOU 3437  CB  LEU A 302    16856  18480  13184    255    959    268       C  
ATOM   3438  CG  LEU A 302      54.503 -21.767 163.751  1.00133.13           C  
ANISOU 3438  CG  LEU A 302    17707  18957  13918    229   1135    332       C  
ATOM   3439  CD1 LEU A 302      53.485 -20.731 163.341  1.00134.54           C  
ANISOU 3439  CD1 LEU A 302    18142  19142  13835    475   1142    417       C  
ATOM   3440  CD2 LEU A 302      54.712 -21.683 165.256  1.00134.20           C  
ANISOU 3440  CD2 LEU A 302    17638  19081  14269     68   1046    284       C  
ATOM   3441  N   ALA A 303      53.504 -26.238 163.723  1.00121.36           N  
ANISOU 3441  N   ALA A 303    15508  18060  12543    115    601     74       N  
ATOM   3442  CA  ALA A 303      52.775 -27.362 164.321  1.00119.03           C  
ANISOU 3442  CA  ALA A 303    14971  17947  12306     93    411    -13       C  
ATOM   3443  C   ALA A 303      53.729 -28.500 164.712  1.00119.81           C  
ANISOU 3443  C   ALA A 303    14858  18033  12630   -111    427    -65       C  
ATOM   3444  O   ALA A 303      53.438 -29.263 165.638  1.00118.08           O  
ANISOU 3444  O   ALA A 303    14447  17897  12523   -176    312   -118       O  
ATOM   3445  CB  ALA A 303      51.721 -27.869 163.351  1.00120.33           C  
ANISOU 3445  CB  ALA A 303    15151  18288  12280    271    317    -71       C  
ATOM   3446  N   ILE A 304      54.868 -28.602 164.004  1.00115.30           N  
ANISOU 3446  N   ILE A 304    14337  17348  12126   -202    582    -49       N  
ATOM   3447  CA  ILE A 304      55.919 -29.582 164.259  1.00113.57           C  
ANISOU 3447  CA  ILE A 304    13936  17094  12121   -389    617    -98       C  
ATOM   3448  C   ILE A 304      56.676 -29.210 165.542  1.00115.53           C  
ANISOU 3448  C   ILE A 304    14099  17233  12563   -521    618   -103       C  
ATOM   3449  O   ILE A 304      56.932 -30.089 166.361  1.00113.80           O  
ANISOU 3449  O   ILE A 304    13686  17062  12492   -616    535   -154       O  
ATOM   3450  CB  ILE A 304      56.818 -29.731 163.002  1.00117.60           C  
ANISOU 3450  CB  ILE A 304    14541  17512  12629   -429    790    -89       C  
ATOM   3451  CG1 ILE A 304      56.149 -30.675 161.991  1.00118.11           C  
ANISOU 3451  CG1 ILE A 304    14578  17737  12560   -336    735   -128       C  
ATOM   3452  CG2 ILE A 304      58.245 -30.203 163.334  1.00118.09           C  
ANISOU 3452  CG2 ILE A 304    14469  17454  12945   -638    882   -129       C  
ATOM   3453  CD1 ILE A 304      56.320 -30.281 160.576  1.00128.50           C  
ANISOU 3453  CD1 ILE A 304    16118  18996  13710   -235    875    -89       C  
ATOM   3454  N   LEU A 305      56.985 -27.906 165.727  1.00112.44           N  
ANISOU 3454  N   LEU A 305    13858  16700  12164   -510    713    -58       N  
ATOM   3455  CA  LEU A 305      57.684 -27.360 166.897  1.00111.88           C  
ANISOU 3455  CA  LEU A 305    13718  16522  12267   -617    718    -84       C  
ATOM   3456  C   LEU A 305      56.963 -27.610 168.216  1.00115.18           C  
ANISOU 3456  C   LEU A 305    14008  17051  12705   -597    527   -101       C  
ATOM   3457  O   LEU A 305      57.629 -27.759 169.243  1.00114.47           O  
ANISOU 3457  O   LEU A 305    13789  16924  12779   -694    484   -152       O  
ATOM   3458  CB  LEU A 305      57.949 -25.863 166.727  1.00113.16           C  
ANISOU 3458  CB  LEU A 305    14082  16515  12398   -591    877    -39       C  
ATOM   3459  CG  LEU A 305      59.325 -25.517 166.193  1.00119.40           C  
ANISOU 3459  CG  LEU A 305    14918  17107  13343   -716   1103    -75       C  
ATOM   3460  CD1 LEU A 305      59.279 -24.277 165.319  1.00121.41           C  
ANISOU 3460  CD1 LEU A 305    15453  17206  13471   -628   1317     -1       C  
ATOM   3461  CD2 LEU A 305      60.336 -25.362 167.322  1.00122.12           C  
ANISOU 3461  CD2 LEU A 305    15095  17364  13943   -868   1099   -176       C  
ATOM   3462  N   HIS A 306      55.611 -27.668 168.189  1.00111.42           N  
ANISOU 3462  N   HIS A 306    13566  16707  12061   -462    414    -72       N  
ATOM   3463  CA  HIS A 306      54.783 -27.924 169.370  1.00110.12           C  
ANISOU 3463  CA  HIS A 306    13299  16640  11903   -431    255    -88       C  
ATOM   3464  C   HIS A 306      55.149 -29.251 170.041  1.00112.07           C  
ANISOU 3464  C   HIS A 306    13342  16947  12292   -521    182   -147       C  
ATOM   3465  O   HIS A 306      55.205 -29.312 171.276  1.00111.24           O  
ANISOU 3465  O   HIS A 306    13159  16840  12265   -547    101   -163       O  
ATOM   3466  CB  HIS A 306      53.282 -27.886 169.023  1.00111.08           C  
ANISOU 3466  CB  HIS A 306    13479  16890  11837   -273    168    -76       C  
ATOM   3467  CG  HIS A 306      52.397 -28.086 170.216  1.00113.76           C  
ANISOU 3467  CG  HIS A 306    13728  17304  12192   -245     34    -98       C  
ATOM   3468  ND1 HIS A 306      51.821 -29.315 170.488  1.00114.82           N  
ANISOU 3468  ND1 HIS A 306    13709  17552  12364   -249    -43   -161       N  
ATOM   3469  CD2 HIS A 306      52.075 -27.224 171.209  1.00115.43           C  
ANISOU 3469  CD2 HIS A 306    13985  17474  12400   -223    -11    -70       C  
ATOM   3470  CE1 HIS A 306      51.152 -29.155 171.618  1.00113.68           C  
ANISOU 3470  CE1 HIS A 306    13536  17425  12234   -224   -124   -165       C  
ATOM   3471  NE2 HIS A 306      51.272 -27.912 172.088  1.00114.31           N  
ANISOU 3471  NE2 HIS A 306    13730  17419  12284   -207   -118   -110       N  
ATOM   3472  N   SER A 307      55.447 -30.289 169.217  1.00107.24           N  
ANISOU 3472  N   SER A 307    12659  16381  11708   -561    221   -178       N  
ATOM   3473  CA  SER A 307      55.804 -31.657 169.611  1.00105.61           C  
ANISOU 3473  CA  SER A 307    12272  16227  11625   -637    183   -229       C  
ATOM   3474  C   SER A 307      56.853 -31.771 170.743  1.00107.62           C  
ANISOU 3474  C   SER A 307    12434  16406  12050   -729    159   -255       C  
ATOM   3475  O   SER A 307      56.868 -32.790 171.439  1.00106.47           O  
ANISOU 3475  O   SER A 307    12167  16312  11976   -746     97   -284       O  
ATOM   3476  CB  SER A 307      56.252 -32.458 168.396  1.00109.45           C  
ANISOU 3476  CB  SER A 307    12726  16733  12125   -682    267   -253       C  
ATOM   3477  OG  SER A 307      56.036 -33.844 168.599  1.00119.21           O  
ANISOU 3477  OG  SER A 307    13803  18062  13428   -711    226   -300       O  
ATOM   3478  N   CYS A 308      57.690 -30.728 170.950  1.00103.37           N  
ANISOU 3478  N   CYS A 308    11956  15744  11574   -775    211   -257       N  
ATOM   3479  CA  CYS A 308      58.714 -30.707 172.003  1.00102.57           C  
ANISOU 3479  CA  CYS A 308    11760  15576  11634   -846    175   -315       C  
ATOM   3480  C   CYS A 308      58.565 -29.538 173.004  1.00106.24           C  
ANISOU 3480  C   CYS A 308    12286  15991  12091   -811    126   -313       C  
ATOM   3481  O   CYS A 308      59.349 -29.445 173.960  1.00105.82           O  
ANISOU 3481  O   CYS A 308    12151  15896  12160   -847     74   -380       O  
ATOM   3482  CB  CYS A 308      60.109 -30.737 171.385  1.00103.19           C  
ANISOU 3482  CB  CYS A 308    11797  15549  11861   -960    291   -375       C  
ATOM   3483  SG  CYS A 308      60.656 -29.158 170.694  1.00108.21           S  
ANISOU 3483  SG  CYS A 308    12590  16017  12509   -997    467   -373       S  
ATOM   3484  N   LEU A 309      57.565 -28.657 172.781  1.00102.24           N  
ANISOU 3484  N   LEU A 309    11916  15491  11438   -731    136   -247       N  
ATOM   3485  CA  LEU A 309      57.333 -27.459 173.590  1.00101.72           C  
ANISOU 3485  CA  LEU A 309    11923  15371  11354   -699    110   -237       C  
ATOM   3486  C   LEU A 309      56.722 -27.718 174.965  1.00103.87           C  
ANISOU 3486  C   LEU A 309    12141  15715  11611   -644    -41   -239       C  
ATOM   3487  O   LEU A 309      57.166 -27.092 175.928  1.00103.57           O  
ANISOU 3487  O   LEU A 309    12088  15624  11640   -657    -80   -279       O  
ATOM   3488  CB  LEU A 309      56.512 -26.417 172.820  1.00102.16           C  
ANISOU 3488  CB  LEU A 309    12158  15401  11256   -623    185   -161       C  
ATOM   3489  CG  LEU A 309      57.320 -25.568 171.838  1.00107.78           C  
ANISOU 3489  CG  LEU A 309    12982  15972  11998   -670    373   -158       C  
ATOM   3490  CD1 LEU A 309      56.429 -24.924 170.814  1.00108.32           C  
ANISOU 3490  CD1 LEU A 309    13243  16043  11869   -554    445    -70       C  
ATOM   3491  CD2 LEU A 309      58.147 -24.512 172.559  1.00111.29           C  
ANISOU 3491  CD2 LEU A 309    13430  16280  12577   -739    437   -213       C  
ATOM   3492  N   ASN A 310      55.714 -28.611 175.072  1.00 99.23           N  
ANISOU 3492  N   ASN A 310    11525  15236  10941   -580   -111   -210       N  
ATOM   3493  CA  ASN A 310      55.089 -28.937 176.362  1.00 98.07           C  
ANISOU 3493  CA  ASN A 310    11347  15137  10778   -523   -222   -209       C  
ATOM   3494  C   ASN A 310      56.120 -29.367 177.422  1.00101.53           C  
ANISOU 3494  C   ASN A 310    11693  15546  11337   -553   -284   -268       C  
ATOM   3495  O   ASN A 310      56.142 -28.720 178.469  1.00101.12           O  
ANISOU 3495  O   ASN A 310    11665  15467  11288   -520   -350   -281       O  
ATOM   3496  CB  ASN A 310      53.950 -29.955 176.223  1.00 98.43           C  
ANISOU 3496  CB  ASN A 310    11364  15283  10752   -465   -246   -194       C  
ATOM   3497  CG  ASN A 310      52.628 -29.353 175.819  1.00125.82           C  
ANISOU 3497  CG  ASN A 310    14919  18796  14089   -385   -252   -163       C  
ATOM   3498  OD1 ASN A 310      52.161 -28.368 176.393  1.00118.53           O  
ANISOU 3498  OD1 ASN A 310    14075  17844  13116   -343   -287   -136       O  
ATOM   3499  ND2 ASN A 310      51.982 -29.945 174.827  1.00121.44           N  
ANISOU 3499  ND2 ASN A 310    14345  18318  13478   -356   -224   -178       N  
ATOM   3500  N   PRO A 311      57.045 -30.347 177.165  1.00 98.24           N  
ANISOU 3500  N   PRO A 311    11174  15133  11021   -606   -266   -314       N  
ATOM   3501  CA  PRO A 311      58.050 -30.702 178.190  1.00 98.24           C  
ANISOU 3501  CA  PRO A 311    11090  15113  11125   -604   -342   -385       C  
ATOM   3502  C   PRO A 311      58.903 -29.532 178.660  1.00102.61           C  
ANISOU 3502  C   PRO A 311    11639  15588  11760   -635   -361   -459       C  
ATOM   3503  O   PRO A 311      59.215 -29.457 179.849  1.00102.51           O  
ANISOU 3503  O   PRO A 311    11597  15579  11774   -581   -466   -513       O  
ATOM   3504  CB  PRO A 311      58.912 -31.747 177.489  1.00100.17           C  
ANISOU 3504  CB  PRO A 311    11231  15363  11464   -667   -295   -422       C  
ATOM   3505  CG  PRO A 311      58.025 -32.339 176.476  1.00104.30           C  
ANISOU 3505  CG  PRO A 311    11780  15942  11908   -671   -222   -358       C  
ATOM   3506  CD  PRO A 311      57.200 -31.207 175.972  1.00 99.96           C  
ANISOU 3506  CD  PRO A 311    11346  15379  11257   -656   -186   -311       C  
ATOM   3507  N   LEU A 312      59.248 -28.612 177.730  1.00 99.27           N  
ANISOU 3507  N   LEU A 312    11254  15091  11373   -713   -249   -470       N  
ATOM   3508  CA  LEU A 312      60.021 -27.401 178.009  1.00 99.70           C  
ANISOU 3508  CA  LEU A 312    11305  15049  11527   -761   -217   -556       C  
ATOM   3509  C   LEU A 312      59.255 -26.440 178.917  1.00102.31           C  
ANISOU 3509  C   LEU A 312    11719  15381  11774   -694   -280   -525       C  
ATOM   3510  O   LEU A 312      59.865 -25.809 179.777  1.00102.08           O  
ANISOU 3510  O   LEU A 312    11644  15312  11830   -698   -328   -623       O  
ATOM   3511  CB  LEU A 312      60.419 -26.709 176.711  1.00100.45           C  
ANISOU 3511  CB  LEU A 312    11457  15043  11667   -851    -35   -555       C  
ATOM   3512  CG  LEU A 312      61.875 -26.861 176.359  1.00106.33           C  
ANISOU 3512  CG  LEU A 312    12086  15706  12611   -957     41   -686       C  
ATOM   3513  CD1 LEU A 312      62.053 -27.679 175.086  1.00106.43           C  
ANISOU 3513  CD1 LEU A 312    12099  15719  12622  -1008    143   -644       C  
ATOM   3514  CD2 LEU A 312      62.539 -25.511 176.261  1.00110.40           C  
ANISOU 3514  CD2 LEU A 312    12628  16077  13242  -1029    174   -773       C  
ATOM   3515  N   ILE A 313      57.922 -26.357 178.744  1.00 97.85           N  
ANISOU 3515  N   ILE A 313    11264  14865  11050   -629   -283   -407       N  
ATOM   3516  CA  ILE A 313      57.050 -25.530 179.574  1.00 97.69           C  
ANISOU 3516  CA  ILE A 313    11328  14849  10941   -563   -340   -367       C  
ATOM   3517  C   ILE A 313      57.036 -26.052 181.014  1.00100.49           C  
ANISOU 3517  C   ILE A 313    11632  15254  11295   -492   -487   -402       C  
ATOM   3518  O   ILE A 313      57.117 -25.257 181.954  1.00100.50           O  
ANISOU 3518  O   ILE A 313    11650  15230  11306   -467   -544   -442       O  
ATOM   3519  CB  ILE A 313      55.637 -25.367 178.932  1.00100.67           C  
ANISOU 3519  CB  ILE A 313    11822  15268  11160   -507   -305   -252       C  
ATOM   3520  CG1 ILE A 313      55.651 -24.286 177.826  1.00102.50           C  
ANISOU 3520  CG1 ILE A 313    12159  15422  11364   -535   -165   -219       C  
ATOM   3521  CG2 ILE A 313      54.515 -25.105 179.960  1.00100.68           C  
ANISOU 3521  CG2 ILE A 313    11880  15308  11064   -421   -396   -208       C  
ATOM   3522  CD1 ILE A 313      56.246 -22.823 178.236  1.00114.73           C  
ANISOU 3522  CD1 ILE A 313    13751  16850  12991   -579    -97   -266       C  
ATOM   3523  N   TYR A 314      56.989 -27.385 181.182  1.00 95.54           N  
ANISOU 3523  N   TYR A 314    10953  14692  10657   -455   -536   -391       N  
ATOM   3524  CA  TYR A 314      57.004 -27.993 182.509  1.00 94.82           C  
ANISOU 3524  CA  TYR A 314    10845  14636  10547   -362   -654   -415       C  
ATOM   3525  C   TYR A 314      58.378 -27.830 183.143  1.00 99.77           C  
ANISOU 3525  C   TYR A 314    11376  15239  11293   -367   -728   -548       C  
ATOM   3526  O   TYR A 314      58.470 -27.626 184.349  1.00 99.56           O  
ANISOU 3526  O   TYR A 314    11360  15223  11245   -281   -837   -594       O  
ATOM   3527  CB  TYR A 314      56.593 -29.472 182.470  1.00 94.94           C  
ANISOU 3527  CB  TYR A 314    10844  14706  10522   -316   -650   -367       C  
ATOM   3528  CG  TYR A 314      55.407 -29.807 181.593  1.00 95.09           C  
ANISOU 3528  CG  TYR A 314    10907  14758  10466   -329   -566   -284       C  
ATOM   3529  CD1 TYR A 314      54.221 -29.080 181.677  1.00 96.47           C  
ANISOU 3529  CD1 TYR A 314    11172  14936  10547   -297   -559   -230       C  
ATOM   3530  CD2 TYR A 314      55.429 -30.918 180.760  1.00 95.61           C  
ANISOU 3530  CD2 TYR A 314    10912  14858  10555   -360   -502   -275       C  
ATOM   3531  CE1 TYR A 314      53.116 -29.406 180.891  1.00 96.81           C  
ANISOU 3531  CE1 TYR A 314    11235  15022  10527   -291   -499   -187       C  
ATOM   3532  CE2 TYR A 314      54.329 -31.261 179.978  1.00 96.18           C  
ANISOU 3532  CE2 TYR A 314    11004  14974  10565   -361   -436   -231       C  
ATOM   3533  CZ  TYR A 314      53.175 -30.501 180.043  1.00103.87           C  
ANISOU 3533  CZ  TYR A 314    12060  15958  11450   -321   -440   -196       C  
ATOM   3534  OH  TYR A 314      52.105 -30.846 179.251  1.00104.90           O  
ANISOU 3534  OH  TYR A 314    12190  16142  11527   -308   -390   -186       O  
ATOM   3535  N   ALA A 315      59.445 -27.891 182.318  1.00 97.42           N  
ANISOU 3535  N   ALA A 315    10982  14906  11125   -461   -666   -626       N  
ATOM   3536  CA  ALA A 315      60.837 -27.705 182.746  1.00 98.30           C  
ANISOU 3536  CA  ALA A 315    10971  14992  11388   -480   -724   -792       C  
ATOM   3537  C   ALA A 315      61.099 -26.246 183.151  1.00102.95           C  
ANISOU 3537  C   ALA A 315    11560  15518  12038   -513   -719   -883       C  
ATOM   3538  O   ALA A 315      62.023 -25.984 183.918  1.00103.41           O  
ANISOU 3538  O   ALA A 315    11517  15572  12201   -490   -808  -1046       O  
ATOM   3539  CB  ALA A 315      61.788 -28.115 181.631  1.00 99.27           C  
ANISOU 3539  CB  ALA A 315    10995  15078  11645   -588   -628   -851       C  
ATOM   3540  N   PHE A 316      60.282 -25.306 182.638  1.00 99.44           N  
ANISOU 3540  N   PHE A 316    11225  15027  11529   -556   -615   -791       N  
ATOM   3541  CA  PHE A 316      60.403 -23.882 182.930  1.00 99.99           C  
ANISOU 3541  CA  PHE A 316    11315  15024  11653   -594   -574   -857       C  
ATOM   3542  C   PHE A 316      59.508 -23.427 184.081  1.00102.12           C  
ANISOU 3542  C   PHE A 316    11666  15334  11802   -495   -681   -811       C  
ATOM   3543  O   PHE A 316      60.018 -22.888 185.067  1.00102.62           O  
ANISOU 3543  O   PHE A 316    11672  15392  11927   -466   -766   -938       O  
ATOM   3544  CB  PHE A 316      60.159 -23.029 181.668  1.00102.18           C  
ANISOU 3544  CB  PHE A 316    11681  15207  11936   -689   -374   -789       C  
ATOM   3545  CG  PHE A 316      61.418 -22.563 180.973  1.00105.45           C  
ANISOU 3545  CG  PHE A 316    12010  15508  12546   -810   -231   -926       C  
ATOM   3546  CD1 PHE A 316      62.101 -21.435 181.416  1.00110.40           C  
ANISOU 3546  CD1 PHE A 316    12584  16045  13318   -863   -178  -1077       C  
ATOM   3547  CD2 PHE A 316      61.912 -23.242 179.866  1.00107.88           C  
ANISOU 3547  CD2 PHE A 316    12289  15791  12909   -876   -131   -918       C  
ATOM   3548  CE1 PHE A 316      63.269 -21.006 180.773  1.00112.87           C  
ANISOU 3548  CE1 PHE A 316    12812  16233  13841   -984    -14  -1227       C  
ATOM   3549  CE2 PHE A 316      63.078 -22.811 179.222  1.00112.11           C  
ANISOU 3549  CE2 PHE A 316    12753  16203  13641   -994     26  -1053       C  
ATOM   3550  CZ  PHE A 316      63.747 -21.696 179.678  1.00111.75           C  
ANISOU 3550  CZ  PHE A 316    12652  16057  13751  -1049     91  -1211       C  
ATOM   3551  N   ILE A 317      58.183 -23.634 183.963  1.00 96.23           N  
ANISOU 3551  N   ILE A 317    11045  14625  10893   -443   -676   -647       N  
ATOM   3552  CA  ILE A 317      57.234 -23.169 184.976  1.00 94.95           C  
ANISOU 3552  CA  ILE A 317    10974  14486  10618   -360   -753   -594       C  
ATOM   3553  C   ILE A 317      56.438 -24.296 185.665  1.00 96.21           C  
ANISOU 3553  C   ILE A 317    11182  14720  10654   -248   -846   -512       C  
ATOM   3554  O   ILE A 317      55.735 -24.011 186.632  1.00 96.21           O  
ANISOU 3554  O   ILE A 317    11258  14730  10568   -172   -909   -479       O  
ATOM   3555  CB  ILE A 317      56.294 -22.056 184.422  1.00 97.80           C  
ANISOU 3555  CB  ILE A 317    11450  14796  10914   -394   -646   -499       C  
ATOM   3556  CG1 ILE A 317      55.549 -22.494 183.133  1.00 97.72           C  
ANISOU 3556  CG1 ILE A 317    11504  14802  10823   -409   -551   -378       C  
ATOM   3557  CG2 ILE A 317      57.068 -20.744 184.220  1.00 99.34           C  
ANISOU 3557  CG2 ILE A 317    11620  14893  11233   -481   -549   -595       C  
ATOM   3558  CD1 ILE A 317      54.291 -21.657 182.757  1.00104.90           C  
ANISOU 3558  CD1 ILE A 317    12546  15697  11614   -380   -492   -270       C  
ATOM   3559  N   GLY A 318      56.577 -25.540 185.210  1.00 90.89           N  
ANISOU 3559  N   GLY A 318    10469  14085   9981   -240   -837   -487       N  
ATOM   3560  CA  GLY A 318      55.885 -26.678 185.811  1.00 89.66           C  
ANISOU 3560  CA  GLY A 318    10361  13978   9728   -139   -883   -419       C  
ATOM   3561  C   GLY A 318      56.505 -27.139 187.118  1.00 93.21           C  
ANISOU 3561  C   GLY A 318    10799  14447  10170    -23  -1010   -491       C  
ATOM   3562  O   GLY A 318      57.324 -28.058 187.122  1.00 92.38           O  
ANISOU 3562  O   GLY A 318    10622  14365  10113      7  -1046   -546       O  
ATOM   3563  N   GLN A 319      56.071 -26.521 188.239  1.00 90.71           N  
ANISOU 3563  N   GLN A 319    10564  14123   9780     58  -1081   -491       N  
ATOM   3564  CA  GLN A 319      56.539 -26.716 189.625  1.00 91.71           C  
ANISOU 3564  CA  GLN A 319    10715  14269   9862    202  -1216   -562       C  
ATOM   3565  C   GLN A 319      56.481 -28.159 190.149  1.00 95.42           C  
ANISOU 3565  C   GLN A 319    11239  14760  10254    335  -1238   -519       C  
ATOM   3566  O   GLN A 319      57.316 -28.524 190.983  1.00 95.25           O  
ANISOU 3566  O   GLN A 319    11202  14766  10222    458  -1354   -607       O  
ATOM   3567  CB  GLN A 319      55.808 -25.776 190.608  1.00 93.31           C  
ANISOU 3567  CB  GLN A 319    11023  14452   9980    257  -1259   -543       C  
ATOM   3568  CG  GLN A 319      55.809 -24.285 190.224  1.00114.93           C  
ANISOU 3568  CG  GLN A 319    13725  17156  12788    140  -1224   -583       C  
ATOM   3569  CD  GLN A 319      57.171 -23.622 190.231  1.00144.96           C  
ANISOU 3569  CD  GLN A 319    17389  20956  16731     93  -1277   -760       C  
ATOM   3570  OE1 GLN A 319      58.028 -23.880 191.092  1.00143.92           O  
ANISOU 3570  OE1 GLN A 319    17202  20864  16618    193  -1408   -887       O  
ATOM   3571  NE2 GLN A 319      57.394 -22.736 189.268  1.00139.63           N  
ANISOU 3571  NE2 GLN A 319    16659  20231  16163    -50  -1169   -784       N  
ATOM   3572  N   LYS A 320      55.503 -28.966 189.695  1.00 91.83           N  
ANISOU 3572  N   LYS A 320    10850  14293   9749    323  -1123   -398       N  
ATOM   3573  CA  LYS A 320      55.409 -30.370 190.112  1.00 92.15           C  
ANISOU 3573  CA  LYS A 320    10950  14331   9730    438  -1096   -352       C  
ATOM   3574  C   LYS A 320      56.478 -31.195 189.379  1.00 97.87           C  
ANISOU 3574  C   LYS A 320    11551  15087  10549    403  -1095   -404       C  
ATOM   3575  O   LYS A 320      57.165 -32.001 190.013  1.00 98.30           O  
ANISOU 3575  O   LYS A 320    11619  15154  10577    534  -1159   -439       O  
ATOM   3576  CB  LYS A 320      54.010 -30.946 189.854  1.00 93.17           C  
ANISOU 3576  CB  LYS A 320    11166  14426   9807    422   -949   -237       C  
ATOM   3577  CG  LYS A 320      52.971 -30.599 190.899  1.00101.97           C  
ANISOU 3577  CG  LYS A 320    12433  15493  10817    508   -937   -186       C  
ATOM   3578  CD  LYS A 320      51.670 -31.298 190.575  1.00111.67           C  
ANISOU 3578  CD  LYS A 320    13716  16680  12032    485   -775   -109       C  
ATOM   3579  CE  LYS A 320      50.677 -31.217 191.700  1.00128.73           C  
ANISOU 3579  CE  LYS A 320    16041  18771  14100    585   -733    -65       C  
ATOM   3580  NZ  LYS A 320      49.451 -32.000 191.396  1.00141.75           N  
ANISOU 3580  NZ  LYS A 320    17726  20367  15767    563   -552    -23       N  
ATOM   3581  N   PHE A 321      56.629 -30.967 188.050  1.00 94.72           N  
ANISOU 3581  N   PHE A 321    11042  14697  10252    238  -1023   -410       N  
ATOM   3582  CA  PHE A 321      57.606 -31.640 187.196  1.00 95.22           C  
ANISOU 3582  CA  PHE A 321    10980  14780  10419    175  -1004   -460       C  
ATOM   3583  C   PHE A 321      59.024 -31.265 187.589  1.00101.84           C  
ANISOU 3583  C   PHE A 321    11719  15635  11343    203  -1133   -608       C  
ATOM   3584  O   PHE A 321      59.868 -32.154 187.695  1.00102.53           O  
ANISOU 3584  O   PHE A 321    11748  15744  11467    265  -1176   -661       O  
ATOM   3585  CB  PHE A 321      57.351 -31.331 185.709  1.00 96.42           C  
ANISOU 3585  CB  PHE A 321    11067  14929  10641      4   -888   -429       C  
ATOM   3586  CG  PHE A 321      58.403 -31.844 184.745  1.00 98.53           C  
ANISOU 3586  CG  PHE A 321    11204  15204  11027    -83   -857   -489       C  
ATOM   3587  CD1 PHE A 321      58.475 -33.194 184.422  1.00101.73           C  
ANISOU 3587  CD1 PHE A 321    11581  15628  11443    -68   -803   -456       C  
ATOM   3588  CD2 PHE A 321      59.312 -30.974 184.153  1.00101.56           C  
ANISOU 3588  CD2 PHE A 321    11497  15564  11526   -187   -861   -582       C  
ATOM   3589  CE1 PHE A 321      59.441 -33.663 183.527  1.00103.18           C  
ANISOU 3589  CE1 PHE A 321    11645  15816  11743   -154   -770   -512       C  
ATOM   3590  CE2 PHE A 321      60.269 -31.442 183.249  1.00104.88           C  
ANISOU 3590  CE2 PHE A 321    11804  15978  12068   -275   -814   -642       C  
ATOM   3591  CZ  PHE A 321      60.328 -32.784 182.942  1.00102.82           C  
ANISOU 3591  CZ  PHE A 321    11513  15745  11808   -258   -778   -604       C  
ATOM   3592  N   ARG A 322      59.287 -29.955 187.796  1.00 99.54           N  
ANISOU 3592  N   ARG A 322    11398  15330  11092    161  -1189   -689       N  
ATOM   3593  CA  ARG A 322      60.589 -29.423 188.198  1.00101.05           C  
ANISOU 3593  CA  ARG A 322    11471  15534  11391    177  -1305   -872       C  
ATOM   3594  C   ARG A 322      61.092 -30.123 189.462  1.00108.21           C  
ANISOU 3594  C   ARG A 322    12405  16487  12224    388  -1461   -939       C  
ATOM   3595  O   ARG A 322      62.050 -30.894 189.380  1.00107.95           O  
ANISOU 3595  O   ARG A 322    12279  16482  12256    434  -1516  -1027       O  
ATOM   3596  CB  ARG A 322      60.519 -27.901 188.398  1.00100.94           C  
ANISOU 3596  CB  ARG A 322    11448  15489  11416    113  -1317   -939       C  
ATOM   3597  CG  ARG A 322      60.559 -27.114 187.100  1.00109.66           C  
ANISOU 3597  CG  ARG A 322    12498  16535  12632    -81  -1170   -933       C  
ATOM   3598  CD  ARG A 322      61.511 -25.939 187.197  1.00120.62           C  
ANISOU 3598  CD  ARG A 322    13776  17883  14172   -151  -1185  -1116       C  
ATOM   3599  NE  ARG A 322      60.911 -24.790 187.874  1.00127.05           N  
ANISOU 3599  NE  ARG A 322    14664  18678  14933   -133  -1206  -1112       N  
ATOM   3600  CZ  ARG A 322      61.510 -23.614 188.026  1.00141.43           C  
ANISOU 3600  CZ  ARG A 322    16406  20454  16879   -197  -1194  -1263       C  
ATOM   3601  NH1 ARG A 322      62.735 -23.419 187.553  1.00123.20           N  
ANISOU 3601  NH1 ARG A 322    13939  18106  14767   -287  -1153  -1442       N  
ATOM   3602  NH2 ARG A 322      60.889 -22.624 188.651  1.00134.64           N  
ANISOU 3602  NH2 ARG A 322    15619  19577  15961   -178  -1207  -1248       N  
ATOM   3603  N   HIS A 323      60.393 -29.924 190.602  1.00107.73           N  
ANISOU 3603  N   HIS A 323    12487  16431  12014    530  -1525   -889       N  
ATOM   3604  CA  HIS A 323      60.730 -30.535 191.892  1.00110.27           C  
ANISOU 3604  CA  HIS A 323    12887  16790  12220    769  -1668   -934       C  
ATOM   3605  C   HIS A 323      60.760 -32.055 191.838  1.00111.42           C  
ANISOU 3605  C   HIS A 323    13092  16938  12304    874  -1624   -850       C  
ATOM   3606  O   HIS A 323      61.708 -32.656 192.341  1.00112.13           O  
ANISOU 3606  O   HIS A 323    13152  17070  12383   1029  -1744   -949       O  
ATOM   3607  CB  HIS A 323      59.798 -30.039 193.008  1.00112.75           C  
ANISOU 3607  CB  HIS A 323    13376  17088  12375    886  -1701   -868       C  
ATOM   3608  CG  HIS A 323      60.021 -28.602 193.359  1.00118.10           C  
ANISOU 3608  CG  HIS A 323    13991  17775  13105    837  -1785   -990       C  
ATOM   3609  ND1 HIS A 323      59.212 -27.598 192.847  1.00119.55           N  
ANISOU 3609  ND1 HIS A 323    14192  17914  13318    677  -1680   -919       N  
ATOM   3610  CD2 HIS A 323      60.985 -28.040 194.127  1.00122.31           C  
ANISOU 3610  CD2 HIS A 323    14438  18359  13676    933  -1957  -1190       C  
ATOM   3611  CE1 HIS A 323      59.693 -26.466 193.337  1.00120.28           C  
ANISOU 3611  CE1 HIS A 323    14217  18019  13466    670  -1773  -1064       C  
ATOM   3612  NE2 HIS A 323      60.762 -26.682 194.111  1.00122.24           N  
ANISOU 3612  NE2 HIS A 323    14391  18327  13728    817  -1942  -1241       N  
ATOM   3613  N   GLY A 324      59.753 -32.643 191.190  1.00104.71           N  
ANISOU 3613  N   GLY A 324    12316  16046  11425    790  -1450   -686       N  
ATOM   3614  CA  GLY A 324      59.616 -34.084 191.009  1.00103.29           C  
ANISOU 3614  CA  GLY A 324    12190  15849  11205    856  -1356   -595       C  
ATOM   3615  C   GLY A 324      60.775 -34.728 190.274  1.00104.52           C  
ANISOU 3615  C   GLY A 324    12188  16037  11488    809  -1375   -678       C  
ATOM   3616  O   GLY A 324      61.168 -35.844 190.618  1.00104.25           O  
ANISOU 3616  O   GLY A 324    12195  16008  11408    951  -1383   -665       O  
ATOM   3617  N   LEU A 325      61.337 -34.026 189.261  1.00 98.88           N  
ANISOU 3617  N   LEU A 325    11302  15335  10933    615  -1370   -764       N  
ATOM   3618  CA  LEU A 325      62.470 -34.516 188.475  1.00 98.30           C  
ANISOU 3618  CA  LEU A 325    11063  15279  11006    542  -1376   -859       C  
ATOM   3619  C   LEU A 325      63.729 -34.570 189.335  1.00102.05           C  
ANISOU 3619  C   LEU A 325    11465  15802  11506    706  -1569  -1037       C  
ATOM   3620  O   LEU A 325      64.369 -35.625 189.400  1.00102.61           O  
ANISOU 3620  O   LEU A 325    11510  15893  11583    806  -1599  -1062       O  
ATOM   3621  CB  LEU A 325      62.688 -33.664 187.200  1.00 97.70           C  
ANISOU 3621  CB  LEU A 325    10852  15181  11089    299  -1292   -904       C  
ATOM   3622  CG  LEU A 325      63.873 -34.022 186.270  1.00102.43           C  
ANISOU 3622  CG  LEU A 325    11275  15778  11864    192  -1272  -1014       C  
ATOM   3623  CD1 LEU A 325      63.668 -35.366 185.580  1.00101.70           C  
ANISOU 3623  CD1 LEU A 325    11191  15686  11763    168  -1158   -905       C  
ATOM   3624  CD2 LEU A 325      64.078 -32.946 185.229  1.00103.84           C  
ANISOU 3624  CD2 LEU A 325    11362  15912  12182    -18  -1183  -1070       C  
ATOM   3625  N   LEU A 326      64.058 -33.457 190.026  1.00 97.09           N  
ANISOU 3625  N   LEU A 326    10805  15195  10889    747  -1703  -1171       N  
ATOM   3626  CA  LEU A 326      65.233 -33.409 190.892  1.00 97.55           C  
ANISOU 3626  CA  LEU A 326    10778  15314  10973    920  -1911  -1381       C  
ATOM   3627  C   LEU A 326      65.055 -34.272 192.153  1.00100.44           C  
ANISOU 3627  C   LEU A 326    11324  15714  11126   1224  -2016  -1327       C  
ATOM   3628  O   LEU A 326      66.053 -34.676 192.740  1.00101.64           O  
ANISOU 3628  O   LEU A 326    11420  15924  11273   1409  -2182  -1478       O  
ATOM   3629  CB  LEU A 326      65.693 -31.976 191.211  1.00 98.24           C  
ANISOU 3629  CB  LEU A 326    10751  15414  11160    867  -2011  -1573       C  
ATOM   3630  CG  LEU A 326      64.677 -30.996 191.756  1.00102.04           C  
ANISOU 3630  CG  LEU A 326    11362  15873  11534    859  -1995  -1493       C  
ATOM   3631  CD1 LEU A 326      64.908 -30.757 193.235  1.00103.69           C  
ANISOU 3631  CD1 LEU A 326    11638  16144  11615   1111  -2199  -1604       C  
ATOM   3632  CD2 LEU A 326      64.752 -29.679 191.002  1.00103.78           C  
ANISOU 3632  CD2 LEU A 326    11460  16046  11924    625  -1909  -1572       C  
ATOM   3633  N   LYS A 327      63.796 -34.614 192.516  1.00 94.94           N  
ANISOU 3633  N   LYS A 327    10847  14972  10256   1281  -1905  -1117       N  
ATOM   3634  CA  LYS A 327      63.450 -35.512 193.628  1.00 94.75           C  
ANISOU 3634  CA  LYS A 327    11043  14941  10017   1561  -1935  -1025       C  
ATOM   3635  C   LYS A 327      63.985 -36.915 193.282  1.00 98.44           C  
ANISOU 3635  C   LYS A 327    11500  15406  10496   1637  -1887   -992       C  
ATOM   3636  O   LYS A 327      64.576 -37.568 194.142  1.00 99.33           O  
ANISOU 3636  O   LYS A 327    11695  15551  10496   1905  -2007  -1041       O  
ATOM   3637  CB  LYS A 327      61.922 -35.575 193.810  1.00 94.97           C  
ANISOU 3637  CB  LYS A 327    11280  14890   9915   1538  -1760   -812       C  
ATOM   3638  CG  LYS A 327      61.418 -35.250 195.209  1.00 97.82           C  
ANISOU 3638  CG  LYS A 327    11852  15239  10076   1765  -1839   -787       C  
ATOM   3639  CD  LYS A 327      59.884 -35.395 195.319  1.00101.69           C  
ANISOU 3639  CD  LYS A 327    12537  15633  10468   1724  -1635   -587       C  
ATOM   3640  CE  LYS A 327      59.398 -36.749 195.820  1.00111.21           C  
ANISOU 3640  CE  LYS A 327    13962  16760  11532   1909  -1492   -446       C  
ATOM   3641  NZ  LYS A 327      59.439 -37.815 194.773  1.00118.07           N  
ANISOU 3641  NZ  LYS A 327    14749  17605  12508   1791  -1332   -385       N  
ATOM   3642  N   ILE A 328      63.808 -37.344 192.001  1.00 93.45           N  
ANISOU 3642  N   ILE A 328    10767  14740   9998   1409  -1716   -917       N  
ATOM   3643  CA  ILE A 328      64.269 -38.623 191.446  1.00 93.24           C  
ANISOU 3643  CA  ILE A 328    10702  14706  10019   1422  -1638   -883       C  
ATOM   3644  C   ILE A 328      65.795 -38.592 191.286  1.00100.84           C  
ANISOU 3644  C   ILE A 328    11459  15737  11119   1449  -1811  -1097       C  
ATOM   3645  O   ILE A 328      66.464 -39.577 191.613  1.00102.04           O  
ANISOU 3645  O   ILE A 328    11631  15910  11230   1634  -1870  -1126       O  
ATOM   3646  CB  ILE A 328      63.556 -38.969 190.105  1.00 93.94           C  
ANISOU 3646  CB  ILE A 328    10737  14745  10211   1162  -1408   -756       C  
ATOM   3647  CG1 ILE A 328      62.016 -38.949 190.249  1.00 92.77           C  
ANISOU 3647  CG1 ILE A 328    10763  14534   9952   1131  -1242   -582       C  
ATOM   3648  CG2 ILE A 328      64.030 -40.325 189.568  1.00 94.72           C  
ANISOU 3648  CG2 ILE A 328    10797  14834  10359   1180  -1320   -723       C  
ATOM   3649  CD1 ILE A 328      61.225 -38.697 188.955  1.00 93.50           C  
ANISOU 3649  CD1 ILE A 328    10772  14605  10149    861  -1075   -513       C  
ATOM   3650  N   LEU A 329      66.344 -37.459 190.789  1.00 98.40           N  
ANISOU 3650  N   LEU A 329    10954  15453  10979   1270  -1881  -1256       N  
ATOM   3651  CA  LEU A 329      67.791 -37.284 190.598  1.00 99.70           C  
ANISOU 3651  CA  LEU A 329    10895  15670  11318   1266  -2029  -1500       C  
ATOM   3652  C   LEU A 329      68.538 -37.401 191.921  1.00108.00           C  
ANISOU 3652  C   LEU A 329    11976  16798  12262   1585  -2275  -1659       C  
ATOM   3653  O   LEU A 329      69.575 -38.056 191.958  1.00109.18           O  
ANISOU 3653  O   LEU A 329    12020  16991  12472   1699  -2382  -1794       O  
ATOM   3654  CB  LEU A 329      68.120 -35.959 189.894  1.00 99.08           C  
ANISOU 3654  CB  LEU A 329    10629  15576  11442   1016  -2015  -1641       C  
ATOM   3655  CG  LEU A 329      67.606 -35.812 188.462  1.00101.58           C  
ANISOU 3655  CG  LEU A 329    10901  15822  11872    719  -1788  -1518       C  
ATOM   3656  CD1 LEU A 329      67.552 -34.361 188.051  1.00101.60           C  
ANISOU 3656  CD1 LEU A 329    10821  15789  11992    528  -1750  -1601       C  
ATOM   3657  CD2 LEU A 329      68.422 -36.630 187.481  1.00103.03           C  
ANISOU 3657  CD2 LEU A 329    10939  15994  12213    616  -1722  -1565       C  
ATOM   3658  N   ALA A 330      67.978 -36.819 193.013  1.00106.82           N  
ANISOU 3658  N   ALA A 330    11981  16665  11939   1745  -2364  -1639       N  
ATOM   3659  CA  ALA A 330      68.529 -36.876 194.373  1.00109.58           C  
ANISOU 3659  CA  ALA A 330    12402  17093  12139   2085  -2605  -1778       C  
ATOM   3660  C   ALA A 330      68.524 -38.313 194.905  1.00116.87           C  
ANISOU 3660  C   ALA A 330    13521  18013  12873   2366  -2600  -1655       C  
ATOM   3661  O   ALA A 330      69.483 -38.710 195.574  1.00119.12           O  
ANISOU 3661  O   ALA A 330    13782  18375  13104   2633  -2804  -1817       O  
ATOM   3662  CB  ALA A 330      67.741 -35.970 195.306  1.00110.22           C  
ANISOU 3662  CB  ALA A 330    12634  17176  12070   2167  -2656  -1747       C  
ATOM   3663  N   ILE A 331      67.461 -39.094 194.580  1.00113.09           N  
ANISOU 3663  N   ILE A 331    13228  17441  12300   2310  -2360  -1383       N  
ATOM   3664  CA  ILE A 331      67.309 -40.503 194.971  1.00114.19           C  
ANISOU 3664  CA  ILE A 331    13574  17540  12273   2542  -2279  -1234       C  
ATOM   3665  C   ILE A 331      68.462 -41.357 194.418  1.00121.24           C  
ANISOU 3665  C   ILE A 331    14303  18472  13291   2567  -2330  -1340       C  
ATOM   3666  O   ILE A 331      69.034 -42.159 195.159  1.00122.83           O  
ANISOU 3666  O   ILE A 331    14611  18703  13357   2881  -2438  -1372       O  
ATOM   3667  CB  ILE A 331      65.890 -41.054 194.598  1.00115.16           C  
ANISOU 3667  CB  ILE A 331    13885  17542  12328   2418  -1975   -956       C  
ATOM   3668  CG1 ILE A 331      64.822 -40.570 195.613  1.00115.15           C  
ANISOU 3668  CG1 ILE A 331    14127  17495  12130   2537  -1947   -851       C  
ATOM   3669  CG2 ILE A 331      65.866 -42.595 194.457  1.00115.97           C  
ANISOU 3669  CG2 ILE A 331    14114  17582  12366   2541  -1813   -818       C  
ATOM   3670  CD1 ILE A 331      63.362 -40.585 195.110  1.00117.40           C  
ANISOU 3670  CD1 ILE A 331    14518  17672  12417   2334  -1670   -644       C  
ATOM   3671  N   HIS A 332      68.833 -41.139 193.145  1.00118.35           N  
ANISOU 3671  N   HIS A 332    13687  18104  13178   2254  -2259  -1404       N  
ATOM   3672  CA  HIS A 332      69.887 -41.902 192.481  1.00119.63           C  
ANISOU 3672  CA  HIS A 332    13674  18291  13491   2228  -2282  -1504       C  
ATOM   3673  C   HIS A 332      71.272 -41.182 192.432  1.00126.85           C  
ANISOU 3673  C   HIS A 332    14308  19294  14593   2220  -2520  -1828       C  
ATOM   3674  O   HIS A 332      72.136 -41.483 193.260  1.00128.02           O  
ANISOU 3674  O   HIS A 332    14449  19520  14674   2511  -2736  -1989       O  
ATOM   3675  CB  HIS A 332      69.421 -42.339 191.079  1.00118.37           C  
ANISOU 3675  CB  HIS A 332    13434  18057  13483   1906  -2023  -1361       C  
ATOM   3676  CG  HIS A 332      68.088 -43.029 191.061  1.00120.62           C  
ANISOU 3676  CG  HIS A 332    13948  18256  13625   1897  -1781  -1089       C  
ATOM   3677  ND1 HIS A 332      67.988 -44.410 191.049  1.00122.72           N  
ANISOU 3677  ND1 HIS A 332    14334  18476  13820   2019  -1649   -962       N  
ATOM   3678  CD2 HIS A 332      66.840 -42.504 191.013  1.00120.95           C  
ANISOU 3678  CD2 HIS A 332    14104  18246  13606   1774  -1643   -947       C  
ATOM   3679  CE1 HIS A 332      66.691 -44.677 191.012  1.00120.86           C  
ANISOU 3679  CE1 HIS A 332    14271  18157  13494   1960  -1426   -760       C  
ATOM   3680  NE2 HIS A 332      65.961 -43.562 190.997  1.00120.10           N  
ANISOU 3680  NE2 HIS A 332    14175  18059  13400   1817  -1424   -748       N  
ATOM   3681  N   GLY A 333      71.456 -40.259 191.475  1.00124.24           N  
ANISOU 3681  N   GLY A 333    13760  18948  14496   1900  -2468  -1928       N  
ATOM   3682  CA  GLY A 333      72.709 -39.546 191.222  1.00125.75           C  
ANISOU 3682  CA  GLY A 333    13664  19191  14925   1822  -2623  -2244       C  
ATOM   3683  C   GLY A 333      73.025 -38.289 192.014  1.00131.54           C  
ANISOU 3683  C   GLY A 333    14314  19983  15681   1890  -2816  -2474       C  
ATOM   3684  O   GLY A 333      73.931 -38.311 192.854  1.00133.98           O  
ANISOU 3684  O   GLY A 333    14541  20384  15980   2138  -3062  -2716       O  
ATOM   3685  N   LEU A 334      72.331 -37.167 191.690  1.00126.13           N  
ANISOU 3685  N   LEU A 334    13633  19247  15043   1666  -2705  -2420       N  
ATOM   3686  CA  LEU A 334      72.487 -35.805 192.244  1.00126.55           C  
ANISOU 3686  CA  LEU A 334    13596  19332  15155   1651  -2826  -2621       C  
ATOM   3687  C   LEU A 334      72.651 -35.690 193.765  1.00131.93           C  
ANISOU 3687  C   LEU A 334    14370  20116  15642   2008  -3088  -2747       C  
ATOM   3688  O   LEU A 334      72.027 -36.438 194.520  1.00131.59           O  
ANISOU 3688  O   LEU A 334    14581  20087  15329   2256  -3115  -2562       O  
ATOM   3689  CB  LEU A 334      71.322 -34.905 191.799  1.00124.62           C  
ANISOU 3689  CB  LEU A 334    13448  19006  14894   1413  -2634  -2434       C  
ATOM   3690  CG  LEU A 334      71.516 -34.019 190.553  1.00128.45           C  
ANISOU 3690  CG  LEU A 334    13749  19410  15646   1060  -2461  -2502       C  
ATOM   3691  CD1 LEU A 334      72.587 -32.956 190.763  1.00130.39           C  
ANISOU 3691  CD1 LEU A 334    13748  19677  16115   1020  -2583  -2858       C  
ATOM   3692  CD2 LEU A 334      71.736 -34.839 189.283  1.00130.11           C  
ANISOU 3692  CD2 LEU A 334    13892  19564  15980    885  -2292  -2412       C  
ATOM   3693  N   ILE A 335      73.477 -34.705 194.195  1.00129.98           N  
ANISOU 3693  N   ILE A 335    13917  19931  15540   2029  -3265  -3075       N  
ATOM   3694  CA  ILE A 335      73.854 -34.400 195.590  1.00132.18           C  
ANISOU 3694  CA  ILE A 335    14217  20327  15680   2359  -3550  -3285       C  
ATOM   3695  C   ILE A 335      74.071 -32.874 195.795  1.00136.58           C  
ANISOU 3695  C   ILE A 335    14594  20896  16403   2227  -3606  -3535       C  
ATOM   3696  O   ILE A 335      74.265 -32.148 194.818  1.00135.08           O  
ANISOU 3696  O   ILE A 335    14216  20626  16482   1900  -3444  -3611       O  
ATOM   3697  CB  ILE A 335      75.082 -35.289 196.029  1.00137.86           C  
ANISOU 3697  CB  ILE A 335    14821  21151  16406   2649  -3786  -3520       C  
ATOM   3698  CG1 ILE A 335      75.801 -34.772 197.320  1.00141.16           C  
ANISOU 3698  CG1 ILE A 335    15161  21714  16761   2971  -4120  -3860       C  
ATOM   3699  CG2 ILE A 335      76.079 -35.482 194.876  1.00138.71           C  
ANISOU 3699  CG2 ILE A 335    14634  21224  16844   2414  -3713  -3693       C  
ATOM   3700  CD1 ILE A 335      76.677 -35.799 198.094  1.00150.04           C  
ANISOU 3700  CD1 ILE A 335    16304  22959  17743   3388  -4385  -4011       C  
ATOM   3701  N   SER A 336      74.012 -32.407 197.075  1.00134.91           N  
ANISOU 3701  N   SER A 336    14460  20778  16023   2489  -3820  -3656       N  
ATOM   3702  CA  SER A 336      74.188 -31.024 197.548  1.00163.40           C  
ANISOU 3702  CA  SER A 336    17921  24416  19746   2432  -3908  -3910       C  
ATOM   3703  C   SER A 336      73.197 -30.040 196.937  1.00193.23           C  
ANISOU 3703  C   SER A 336    21759  28074  23585   2108  -3655  -3717       C  
ATOM   3704  O   SER A 336      72.899 -29.013 197.544  1.00156.01           O  
ANISOU 3704  O   SER A 336    17051  23377  18850   2113  -3704  -3803       O  
ATOM   3705  CB  SER A 336      75.626 -30.541 197.364  1.00168.94           C  
ANISOU 3705  CB  SER A 336    18242  25171  20777   2377  -4036  -4365       C  
ATOM   3706  OG  SER A 336      76.508 -31.159 198.286  1.00180.04           O  
ANISOU 3706  OG  SER A 336    19586  26728  22092   2753  -4353  -4625       O  
TER    3707      SER A 336                                                      
HETATM 3708  C1  EBX A1201      46.467 -29.356 188.491  1.00104.04           C  
ANISOU 3708  C1  EBX A1201    12735  15694  11102    218   -492    -62       C  
HETATM 3709  C2  EBX A1201      47.633 -30.039 188.072  1.00105.04           C  
ANISOU 3709  C2  EBX A1201    12794  15855  11262    203   -510    -69       C  
HETATM 3710  C3  EBX A1201      48.625 -29.352 187.343  1.00104.65           C  
ANISOU 3710  C3  EBX A1201    12672  15858  11233    139   -594    -80       C  
HETATM 3711  C4  EBX A1201      48.386 -28.038 186.919  1.00104.10           C  
ANISOU 3711  C4  EBX A1201    12604  15802  11147     92   -640    -75       C  
HETATM 3712  C5  EBX A1201      47.224 -27.384 187.348  1.00103.13           C  
ANISOU 3712  C5  EBX A1201    12553  15652  10980    117   -630    -59       C  
HETATM 3713  C6  EBX A1201      45.469 -30.006 189.244  1.00102.99           C  
ANISOU 3713  C6  EBX A1201    12677  15487  10966    273   -382    -66       C  
HETATM 3714  C7  EBX A1201      46.782 -29.527 191.298  1.00103.98           C  
ANISOU 3714  C7  EBX A1201    12988  15547  10972    423   -524    -11       C  
HETATM 3715  C8  EBX A1201      44.571 -30.798 191.363  1.00103.99           C  
ANISOU 3715  C8  EBX A1201    13040  15434  11039    428   -228    -35       C  
HETATM 3716  C11 EBX A1201      52.904 -29.439 186.886  1.00103.16           C  
ANISOU 3716  C11 EBX A1201    12280  15724  11190     80   -792   -197       C  
HETATM 3717  C10 EBX A1201      52.093 -30.550 186.665  1.00100.47           C  
ANISOU 3717  C10 EBX A1201    11956  15386  10832    101   -697   -155       C  
HETATM 3718  C12 EBX A1201      51.784 -28.681 187.231  1.00103.20           C  
ANISOU 3718  C12 EBX A1201    12370  15709  11133     93   -779   -157       C  
HETATM 3719  C13 EBX A1201      53.624 -32.367 186.238  1.00 90.59           C  
ANISOU 3719  C13 EBX A1201    10588  14162   9671    110   -678   -196       C  
HETATM 3720  C14 EBX A1201      53.886 -33.433 187.323  1.00 90.50           C  
ANISOU 3720  C14 EBX A1201    10646  14123   9618    251   -683   -186       C  
HETATM 3721  C15 EBX A1201      53.981 -32.984 184.871  1.00 85.99           C  
ANISOU 3721  C15 EBX A1201     9889  13614   9168      4   -606   -209       C  
HETATM 3722  C16 EBX A1201      53.605 -32.081 183.701  1.00 83.45           C  
ANISOU 3722  C16 EBX A1201     9534  13315   8860   -104   -576   -206       C  
HETATM 3723  C17 EBX A1201      54.948 -34.911 188.457  1.00 91.80           C  
ANISOU 3723  C17 EBX A1201    10871  14265   9744    450   -720   -198       C  
HETATM 3724  C18 EBX A1201      53.710 -34.818 188.933  1.00 91.93           C  
ANISOU 3724  C18 EBX A1201    11001  14234   9694    481   -636   -139       C  
HETATM 3725  C19 EBX A1201      53.027 -33.902 188.232  1.00 90.73           C  
ANISOU 3725  C19 EBX A1201    10802  14102   9571    355   -621   -137       C  
HETATM 3726  C20 EBX A1201      53.231 -35.673 190.143  1.00 92.79           C  
ANISOU 3726  C20 EBX A1201    11286  14265   9704    655   -557    -85       C  
HETATM 3727  C21 EBX A1201      52.875 -37.110 189.737  1.00 93.20           C  
ANISOU 3727  C21 EBX A1201    11337  14276   9799    652   -369    -51       C  
HETATM 3728  C22 EBX A1201      52.107 -35.030 190.971  1.00 91.60           C  
ANISOU 3728  C22 EBX A1201    11273  14056   9474    700   -525    -47       C  
HETATM 3729  C9  EBX A1201      50.967 -29.793 186.984  1.00102.78           C  
ANISOU 3729  C9  EBX A1201    12326  15658  11068    111   -683   -123       C  
HETATM 3730  N1  EBX A1201      46.257 -28.078 188.103  1.00102.98           N  
ANISOU 3730  N1  EBX A1201    12593  15586  10948    175   -560    -58       N  
HETATM 3731  N2  EBX A1201      45.619 -30.105 190.596  1.00103.09           N  
ANISOU 3731  N2  EBX A1201    12826  15423  10921    369   -382    -32       N  
HETATM 3732  N3  EBX A1201      49.660 -30.118 186.929  1.00104.03           N  
ANISOU 3732  N3  EBX A1201    12521  15805  11201    121   -596    -97       N  
HETATM 3733  N4  EBX A1201      52.244 -31.827 186.280  1.00 95.43           N  
ANISOU 3733  N4  EBX A1201    11273  14760  10228    104   -627   -153       N  
HETATM 3734  O1  EBX A1201      47.831 -31.206 188.424  1.00105.29           O  
ANISOU 3734  O1  EBX A1201    12840  15858  11306    251   -441    -68       O  
HETATM 3735  O2  EBX A1201      44.497 -30.476 188.654  1.00101.94           O  
ANISOU 3735  O2  EBX A1201    12486  15359  10887    240   -280   -111       O  
HETATM 3736  O3  EBX A1201      51.620 -27.521 187.619  1.00102.69           O  
ANISOU 3736  O3  EBX A1201    12348  15625  11044     89   -824   -160       O  
HETATM 3737  O4  EBX A1201      54.119 -29.248 186.888  1.00104.68           O  
ANISOU 3737  O4  EBX A1201    12406  15925  11444     64   -859   -264       O  
HETATM 3738  O5  EBX A1201      55.066 -34.066 187.457  1.00 91.06           O  
ANISOU 3738  O5  EBX A1201    10667  14208   9724    298   -739   -229       O  
CONECT  577 1187                                                                
CONECT 1187  577                                                                
CONECT 3708 3709 3713 3730                                                      
CONECT 3709 3708 3710 3734                                                      
CONECT 3710 3709 3711 3732                                                      
CONECT 3711 3710 3712                                                           
CONECT 3712 3711 3730                                                           
CONECT 3713 3708 3731 3735                                                      
CONECT 3714 3731                                                                
CONECT 3715 3731                                                                
CONECT 3716 3717 3718 3737                                                      
CONECT 3717 3716 3729 3733                                                      
CONECT 3718 3716 3729 3736                                                      
CONECT 3719 3720 3721 3733                                                      
CONECT 3720 3719 3725 3738                                                      
CONECT 3721 3719 3722                                                           
CONECT 3722 3721                                                                
CONECT 3723 3724 3738                                                           
CONECT 3724 3723 3725 3726                                                      
CONECT 3725 3720 3724                                                           
CONECT 3726 3724 3727 3728                                                      
CONECT 3727 3726                                                                
CONECT 3728 3726                                                                
CONECT 3729 3717 3718 3732                                                      
CONECT 3730 3708 3712                                                           
CONECT 3731 3713 3714 3715                                                      
CONECT 3732 3710 3729                                                           
CONECT 3733 3717 3719                                                           
CONECT 3734 3709                                                                
CONECT 3735 3713                                                                
CONECT 3736 3718                                                                
CONECT 3737 3716                                                                
CONECT 3738 3720 3723                                                           
MASTER      305    0    1   20    8    0    4    6 3737    1   33   39          
END