HEADER SIGNALING PROTEIN 15-JAN-17 5UIW TITLE CRYSTAL STRUCTURE OF CC CHEMOKINE RECEPTOR 5 (CCR5) IN COMPLEX WITH TITLE 2 HIGH POTENCY HIV ENTRY INHIBITOR 5P7-CCL5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-C CHEMOKINE RECEPTOR TYPE 5,RUBREDOXIN CHIMERA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CCR5,CHEMR13,HIV-1 FUSION CORECEPTOR,RD,CCR5,CHEMR13,HIV-1 COMPND 5 FUSION CORECEPTOR; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: RUBREDOXIN FUSION SEQUENCE P00268; IN BETWEEN CCR5 COMPND 9 RESIDUE 223 AND 227 COMPND 10 MKKYTCTVCGYIYNPEDGDPDNGVNPGTDFKDIPDDWVCPLCGVGKDQFEEVEE; COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: C-C MOTIF CHEMOKINE 5; COMPND 13 CHAIN: B; COMPND 14 SYNONYM: EOCP,EOSINOPHIL CHEMOTACTIC CYTOKINE,SIS-DELTA,SMALL- COMPND 15 INDUCIBLE CYTOKINE A5,T CELL-SPECIFIC PROTEIN P228,TCP228,T-CELL- COMPND 16 SPECIFIC PROTEIN RANTES; COMPND 17 ENGINEERED: YES; COMPND 18 OTHER_DETAILS: SEQUENCE BEFORE CC MOTIF "QGPPLMALQS" (WHERE THE FIRST COMPND 19 RESIDUE Q IS PCA AS GLUTAMINE IS CYCLIZED INTO PYROGLUTAMIC ACID COMPND 20 RESIDUE) IS ARTIFICIAL TO REPLACE NATIVE SEQUENCE "SPYSSDTTP". AS THE COMPND 21 REGISTER 0 FOR PCA, ALL THE REST OF RESIDUE NUMBERS ARE CONSISTENT COMPND 22 FOR CHEMOKINE RESIDUES. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, CLOSTRIDIUM PASTEURIANUM; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 1501; SOURCE 5 GENE: CCR5, CMKBR5; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1711; SOURCE 10 EXPRESSION_SYSTEM_ORGAN: OVARY; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-1; SOURCE 13 MOL_ID: 2; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: CCL5, D17S136E, SCYA5; SOURCE 18 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 21 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1711; SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID; SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-1 KEYWDS G-PROTEIN COUPLED RECEPTOR, CHEMOKINE RECEPTOR, HIV ENTRY INHIBITOR, KEYWDS 2 HIV-1 R5 ISOLATES CO-RECEPTOR, RECEPTOR-LIGAND COMPLEX, SIGNALING KEYWDS 3 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.ZHENG,L.QIN,G.W.HAN,M.GUSTAVSSON,T.KAWAMURA,R.C.STEVENS,V.CHEREZOV, AUTHOR 2 I.KUFAREVA,T.M.HANDEL REVDAT 4 11-DEC-19 5UIW 1 SEQRES REVDAT 3 18-APR-18 5UIW 1 JRNL REVDAT 2 13-SEP-17 5UIW 1 REMARK REVDAT 1 28-JUN-17 5UIW 0 JRNL AUTH Y.ZHENG,G.W.HAN,R.ABAGYAN,B.WU,R.C.STEVENS,V.CHEREZOV, JRNL AUTH 2 I.KUFAREVA,T.M.HANDEL JRNL TITL STRUCTURE OF CC CHEMOKINE RECEPTOR 5 WITH A POTENT CHEMOKINE JRNL TITL 2 ANTAGONIST REVEALS MECHANISMS OF CHEMOKINE RECOGNITION AND JRNL TITL 3 MOLECULAR MIMICRY BY HIV. JRNL REF IMMUNITY V. 46 1005 2017 JRNL REFN ISSN 1097-4180 JRNL PMID 28636951 JRNL DOI 10.1016/J.IMMUNI.2017.05.002 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.47 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970 REMARK 3 COMPLETENESS FOR RANGE (%) : 73.4 REMARK 3 NUMBER OF REFLECTIONS : 23465 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.218 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1196 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 29.4746 - 4.5786 1.00 3602 217 0.1929 0.2022 REMARK 3 2 4.5786 - 3.6363 1.00 3435 177 0.1859 0.2473 REMARK 3 3 3.6363 - 3.1773 1.00 3362 168 0.2164 0.2487 REMARK 3 4 3.1773 - 2.8870 0.99 3349 175 0.2521 0.2838 REMARK 3 5 2.8870 - 2.6803 0.87 2945 133 0.2485 0.3031 REMARK 3 6 2.6803 - 2.5223 0.71 2315 127 0.2569 0.2937 REMARK 3 7 2.5223 - 2.3961 0.54 1772 108 0.2540 0.2765 REMARK 3 8 2.3961 - 2.2918 0.35 1165 65 0.2687 0.3529 REMARK 3 9 2.2918 - 2.2036 0.10 324 26 0.2707 0.3290 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.720 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.07 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.31 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 3491 REMARK 3 ANGLE : 0.969 4722 REMARK 3 CHIRALITY : 0.035 539 REMARK 3 PLANARITY : 0.005 582 REMARK 3 DIHEDRAL : 15.102 1218 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A):-132.3783 -94.8877 611.2836 REMARK 3 T TENSOR REMARK 3 T11: 0.1809 T22: 0.5747 REMARK 3 T33: 0.1637 T12: -0.0413 REMARK 3 T13: 0.0045 T23: 0.0814 REMARK 3 L TENSOR REMARK 3 L11: 1.8342 L22: 1.6547 REMARK 3 L33: 3.0254 L12: -0.0167 REMARK 3 L13: -1.2391 L23: 1.9151 REMARK 3 S TENSOR REMARK 3 S11: 0.0723 S12: 0.6294 S13: 0.3912 REMARK 3 S21: -0.4836 S22: 0.0168 S23: -0.0362 REMARK 3 S31: -0.5779 S32: -0.0707 S33: -0.2481 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A):-133.5119 -97.4485 642.3796 REMARK 3 T TENSOR REMARK 3 T11: 0.1291 T22: 0.2860 REMARK 3 T33: 0.1217 T12: 0.0486 REMARK 3 T13: 0.0267 T23: -0.0463 REMARK 3 L TENSOR REMARK 3 L11: 1.1851 L22: 1.0823 REMARK 3 L33: 1.5743 L12: -0.1183 REMARK 3 L13: -0.1359 L23: 0.5161 REMARK 3 S TENSOR REMARK 3 S11: -0.2134 S12: 0.0107 S13: 0.0044 REMARK 3 S21: 0.3315 S22: 0.0373 S23: 0.0766 REMARK 3 S31: 0.1471 S32: 0.0040 S33: -0.0889 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1054 ) REMARK 3 ORIGIN FOR THE GROUP (A):-140.0878-122.1137 683.0264 REMARK 3 T TENSOR REMARK 3 T11: 0.9807 T22: 0.3849 REMARK 3 T33: 0.3185 T12: -0.0308 REMARK 3 T13: 0.1317 T23: 0.0936 REMARK 3 L TENSOR REMARK 3 L11: 0.9235 L22: 2.6023 REMARK 3 L33: 3.2562 L12: 0.9010 REMARK 3 L13: -0.6138 L23: -2.7813 REMARK 3 S TENSOR REMARK 3 S11: -0.1827 S12: 0.2252 S13: -0.3645 REMARK 3 S21: -1.1064 S22: -0.1435 S23: -0.4323 REMARK 3 S31: 1.2492 S32: 0.1416 S33: 0.2980 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 227 THROUGH 316 ) REMARK 3 ORIGIN FOR THE GROUP (A):-141.3603-104.9308 644.9275 REMARK 3 T TENSOR REMARK 3 T11: 0.2582 T22: 0.2310 REMARK 3 T33: 0.1808 T12: -0.0512 REMARK 3 T13: 0.1137 T23: -0.0148 REMARK 3 L TENSOR REMARK 3 L11: 2.1561 L22: 1.4603 REMARK 3 L33: 1.6640 L12: 0.0454 REMARK 3 L13: 0.2461 L23: -0.5368 REMARK 3 S TENSOR REMARK 3 S11: -0.1376 S12: -0.1311 S13: -0.0179 REMARK 3 S21: 0.4265 S22: 0.0629 S23: 0.2439 REMARK 3 S31: 0.4221 S32: -0.3262 S33: 0.1196 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5UIW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-17. REMARK 100 THE DEPOSITION ID IS D_1000225727. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUL-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.3 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : OTHER REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.29 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32803 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180 REMARK 200 RESOLUTION RANGE LOW (A) : 29.472 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 13.70 REMARK 200 R MERGE (I) : 0.14500 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3 REMARK 200 DATA REDUNDANCY IN SHELL : 7.40 REMARK 200 R MERGE FOR SHELL (I) : 2.29200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.600 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: 4MBS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.65 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 29% (V/V) PEG 400, 120 MM LITHIUM REMARK 280 CITRATE, 1.2% (W/V) 1,5-DIAMINOPENTANE DIHYDROCHLORIDE, 100 MM 2- REMARK 280 (N-MORPHOLINO)ETHANESULFONIC ACID, PH 6.3, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 295.5K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 X,-Y,-Z REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,Z+1/2 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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.32000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 151.33500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.32000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 151.33500 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 ASP A 2 REMARK 465 TYR A 3 REMARK 465 GLN A 4 REMARK 465 VAL A 5 REMARK 465 SER A 6 REMARK 465 SER A 7 REMARK 465 PRO A 8 REMARK 465 ILE A 9 REMARK 465 TYR A 10 REMARK 465 ASP A 11 REMARK 465 ILE A 12 REMARK 465 ASN A 13 REMARK 465 TYR A 14 REMARK 465 TYR A 15 REMARK 465 PHE A 317 REMARK 465 CYS A 318 REMARK 465 LYS A 319 REMARK 465 CYS A 320 REMARK 465 CYS A 321 REMARK 465 SER A 322 REMARK 465 ILE A 323 REMARK 465 PHE A 324 REMARK 465 GLN A 325 REMARK 465 GLN A 326 REMARK 465 GLU A 327 REMARK 465 ALA A 328 REMARK 465 PRO A 329 REMARK 465 GLU A 330 REMARK 465 ARG A 331 REMARK 465 ALA A 332 REMARK 465 SER A 333 REMARK 465 SER A 334 REMARK 465 VAL A 335 REMARK 465 TYR A 336 REMARK 465 THR A 337 REMARK 465 ARG A 338 REMARK 465 SER A 339 REMARK 465 THR A 340 REMARK 465 GLY A 341 REMARK 465 GLU A 342 REMARK 465 GLN A 343 REMARK 465 GLU A 344 REMARK 465 ILE A 345 REMARK 465 SER A 346 REMARK 465 VAL A 347 REMARK 465 GLY A 348 REMARK 465 LEU A 349 REMARK 465 GLY A 350 REMARK 465 ARG A 351 REMARK 465 PRO A 352 REMARK 465 LEU A 353 REMARK 465 GLU A 354 REMARK 465 VAL A 355 REMARK 465 LEU A 356 REMARK 465 PHE A 357 REMARK 465 GLN A 358 REMARK 465 SER B 68 REMARK 465 LEU B 69 REMARK 465 GLU B 70 REMARK 465 VAL B 71 REMARK 465 LEU B 72 REMARK 465 PHE B 73 REMARK 465 GLN B 74 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 22 CE NZ REMARK 470 ILE A 23 CD1 REMARK 470 ASN A 57 CG OD1 ND2 REMARK 470 ARG A 60 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 62 CG CD CE NZ REMARK 470 VAL A 134 CG1 CG2 REMARK 470 LEU A 137 CG CD1 CD2 REMARK 470 LYS A 138 CD CE NZ REMARK 470 LEU A 174 CG CD1 CD2 REMARK 470 HIS A 175 CG ND1 CD2 CE1 NE2 REMARK 470 ARG A 223 CD NE CZ NH1 NH2 REMARK 470 MET A1001 CG SD CE REMARK 470 LYS A1002 CG CD CE NZ REMARK 470 GLU A1016 CG CD OE1 OE2 REMARK 470 THR A1028 OG1 CG2 REMARK 470 ASP A1029 CG OD1 OD2 REMARK 470 LYS A1031 CG CD CE NZ REMARK 470 ASP A1032 CG OD1 OD2 REMARK 470 LYS A1046 NZ REMARK 470 ASP A1047 CG OD1 OD2 REMARK 470 GLN A1048 CG CD OE1 NE2 REMARK 470 GLU A1050 CD OE1 OE2 REMARK 470 GLU A1053 CG CD OE1 OE2 REMARK 470 GLU A 227 CG CD OE1 OE2 REMARK 470 LYS A 229 CG CD CE NZ REMARK 470 HIS A 231 CG ND1 CD2 CE1 NE2 REMARK 470 ASP A 233 CG OD1 OD2 REMARK 470 GLU A 302 CG CD OE1 OE2 REMARK 470 VAL A 310 CG1 CG2 REMARK 470 LYS A 314 CG CD CE NZ REMARK 470 HIS A 315 CG ND1 CD2 CE1 NE2 REMARK 470 ILE A 316 CG1 CG2 CD1 REMARK 470 ARG B 17 CZ NH1 NH2 REMARK 470 HIS B 23 ND1 CD2 CE1 NE2 REMARK 470 ARG B 44 CZ NH1 NH2 REMARK 470 LYS B 45 CG CD CE NZ REMARK 470 GLU B 54 CG CD OE1 OE2 REMARK 470 LYS B 56 CG CD CE NZ REMARK 470 GLU B 60 CG CD OE1 OE2 REMARK 470 MET B 67 CG SD CE 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 LEU A 61 81.71 62.19 REMARK 500 ALA A 92 -95.49 -135.56 REMARK 500 HIS A 132 67.40 -114.25 REMARK 500 LEU A 203 -58.27 -136.71 REMARK 500 ASP A1019 92.03 -166.79 REMARK 500 CYS A 290 5.77 -69.44 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1102 REMARK 610 OLC A 1103 REMARK 610 OLC A 1104 REMARK 610 OLC A 1105 REMARK 610 OLC A 1106 REMARK 610 OLC A 1107 REMARK 610 OLA A 1108 REMARK 610 OLA A 1109 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1101 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A1006 SG REMARK 620 2 CYS A1009 SG 114.7 REMARK 620 3 CYS A1039 SG 108.4 97.2 REMARK 620 4 CYS A1042 SG 99.9 127.9 107.7 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1103 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1104 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1105 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1106 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1107 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1108 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1109 DBREF 5UIW A 2 223 UNP P51681 CCR5_HUMAN 2 223 DBREF 5UIW A 1001 1054 UNP P00268 RUBR_CLOPA 1 54 DBREF 5UIW A 227 349 UNP P51681 CCR5_HUMAN 227 352 DBREF 5UIW B 10 68 UNP P13501 CCL5_HUMAN 33 91 SEQADV 5UIW GLY A -1 UNP P51681 EXPRESSION TAG SEQADV 5UIW ALA A 0 UNP P51681 EXPRESSION TAG SEQADV 5UIW PRO A 1 UNP P51681 EXPRESSION TAG SEQADV 5UIW TYR A 58 UNP P51681 CYS 58 ENGINEERED MUTATION SEQADV 5UIW ASN A 163 UNP P51681 GLY 163 ENGINEERED MUTATION SEQADV 5UIW ASP A 233 UNP P51681 ALA 233 ENGINEERED MUTATION SEQADV 5UIW GLU A 303 UNP P51681 LYS 303 ENGINEERED MUTATION SEQADV 5UIW A UNP P51681 ALA 317 DELETION SEQADV 5UIW A UNP P51681 LYS 318 DELETION SEQADV 5UIW A UNP P51681 ARG 319 DELETION SEQADV 5UIW GLY A 350 UNP P51681 EXPRESSION TAG SEQADV 5UIW ARG A 351 UNP P51681 EXPRESSION TAG SEQADV 5UIW PRO A 352 UNP P51681 EXPRESSION TAG SEQADV 5UIW LEU A 353 UNP P51681 EXPRESSION TAG SEQADV 5UIW GLU A 354 UNP P51681 EXPRESSION TAG SEQADV 5UIW VAL A 355 UNP P51681 EXPRESSION TAG SEQADV 5UIW LEU A 356 UNP P51681 EXPRESSION TAG SEQADV 5UIW PHE A 357 UNP P51681 EXPRESSION TAG SEQADV 5UIW GLN A 358 UNP P51681 EXPRESSION TAG SEQADV 5UIW PCA B 0 UNP P13501 EXPRESSION TAG SEQADV 5UIW GLY B 1 UNP P13501 EXPRESSION TAG SEQADV 5UIW PRO B 2 UNP P13501 EXPRESSION TAG SEQADV 5UIW PRO B 3 UNP P13501 EXPRESSION TAG SEQADV 5UIW LEU B 4 UNP P13501 EXPRESSION TAG SEQADV 5UIW MET B 5 UNP P13501 EXPRESSION TAG SEQADV 5UIW ALA B 6 UNP P13501 EXPRESSION TAG SEQADV 5UIW LEU B 7 UNP P13501 EXPRESSION TAG SEQADV 5UIW GLN B 8 UNP P13501 EXPRESSION TAG SEQADV 5UIW SER B 9 UNP P13501 EXPRESSION TAG SEQADV 5UIW LEU B 69 UNP P13501 EXPRESSION TAG SEQADV 5UIW GLU B 70 UNP P13501 EXPRESSION TAG SEQADV 5UIW VAL B 71 UNP P13501 EXPRESSION TAG SEQADV 5UIW LEU B 72 UNP P13501 EXPRESSION TAG SEQADV 5UIW PHE B 73 UNP P13501 EXPRESSION TAG SEQADV 5UIW GLN B 74 UNP P13501 EXPRESSION TAG SEQRES 1 A 411 GLY ALA PRO ASP TYR GLN VAL SER SER PRO ILE TYR ASP SEQRES 2 A 411 ILE ASN TYR TYR THR SER GLU PRO CYS GLN LYS ILE ASN SEQRES 3 A 411 VAL LYS GLN ILE ALA ALA ARG LEU LEU PRO PRO LEU TYR SEQRES 4 A 411 SER LEU VAL PHE ILE PHE GLY PHE VAL GLY ASN MET LEU SEQRES 5 A 411 VAL ILE LEU ILE LEU ILE ASN TYR LYS ARG LEU LYS SER SEQRES 6 A 411 MET THR ASP ILE TYR LEU LEU ASN LEU ALA ILE SER ASP SEQRES 7 A 411 LEU PHE PHE LEU LEU THR VAL PRO PHE TRP ALA HIS TYR SEQRES 8 A 411 ALA ALA ALA GLN TRP ASP PHE GLY ASN THR MET CYS GLN SEQRES 9 A 411 LEU LEU THR GLY LEU TYR PHE ILE GLY PHE PHE SER GLY SEQRES 10 A 411 ILE PHE PHE ILE ILE LEU LEU THR ILE ASP ARG TYR LEU SEQRES 11 A 411 ALA VAL VAL HIS ALA VAL PHE ALA LEU LYS ALA ARG THR SEQRES 12 A 411 VAL THR PHE GLY VAL VAL THR SER VAL ILE THR TRP VAL SEQRES 13 A 411 VAL ALA VAL PHE ALA SER LEU PRO ASN ILE ILE PHE THR SEQRES 14 A 411 ARG SER GLN LYS GLU GLY LEU HIS TYR THR CYS SER SER SEQRES 15 A 411 HIS PHE PRO TYR SER GLN TYR GLN PHE TRP LYS ASN PHE SEQRES 16 A 411 GLN THR LEU LYS ILE VAL ILE LEU GLY LEU VAL LEU PRO SEQRES 17 A 411 LEU LEU VAL MET VAL ILE CYS TYR SER GLY ILE LEU LYS SEQRES 18 A 411 THR LEU LEU ARG MET LYS LYS TYR THR CYS THR VAL CYS SEQRES 19 A 411 GLY TYR ILE TYR ASN PRO GLU ASP GLY ASP PRO ASP ASN SEQRES 20 A 411 GLY VAL ASN PRO GLY THR ASP PHE LYS ASP ILE PRO ASP SEQRES 21 A 411 ASP TRP VAL CYS PRO LEU CYS GLY VAL GLY LYS ASP GLN SEQRES 22 A 411 PHE GLU GLU VAL GLU GLU GLU LYS LYS ARG HIS ARG ASP SEQRES 23 A 411 VAL ARG LEU ILE PHE THR ILE MET ILE VAL TYR PHE LEU SEQRES 24 A 411 PHE TRP ALA PRO TYR ASN ILE VAL LEU LEU LEU ASN THR SEQRES 25 A 411 PHE GLN GLU PHE PHE GLY LEU ASN ASN CYS SER SER SER SEQRES 26 A 411 ASN ARG LEU ASP GLN ALA MET GLN VAL THR GLU THR LEU SEQRES 27 A 411 GLY MET THR HIS CYS CYS ILE ASN PRO ILE ILE TYR ALA SEQRES 28 A 411 PHE VAL GLY GLU GLU PHE ARG ASN TYR LEU LEU VAL PHE SEQRES 29 A 411 PHE GLN LYS HIS ILE PHE CYS LYS CYS CYS SER ILE PHE SEQRES 30 A 411 GLN GLN GLU ALA PRO GLU ARG ALA SER SER VAL TYR THR SEQRES 31 A 411 ARG SER THR GLY GLU GLN GLU ILE SER VAL GLY LEU GLY SEQRES 32 A 411 ARG PRO LEU GLU VAL LEU PHE GLN SEQRES 1 B 75 PCA GLY PRO PRO LEU MET ALA LEU GLN SER CYS CYS PHE SEQRES 2 B 75 ALA TYR ILE ALA ARG PRO LEU PRO ARG ALA HIS ILE LYS SEQRES 3 B 75 GLU TYR PHE TYR THR SER GLY LYS CYS SER ASN PRO ALA SEQRES 4 B 75 VAL VAL PHE VAL THR ARG LYS ASN ARG GLN VAL CYS ALA SEQRES 5 B 75 ASN PRO GLU LYS LYS TRP VAL ARG GLU TYR ILE ASN SER SEQRES 6 B 75 LEU GLU MET SER LEU GLU VAL LEU PHE GLN HET PCA B 0 8 HET ZN A1101 1 HET OLC A1102 16 HET OLC A1103 13 HET OLC A1104 21 HET OLC A1105 16 HET OLC A1106 13 HET OLC A1107 24 HET OLA A1108 12 HET OLA A1109 8 HETNAM PCA PYROGLUTAMIC ACID HETNAM ZN ZINC ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 PCA C5 H7 N O3 FORMUL 3 ZN ZN 2+ FORMUL 4 OLC 6(C21 H40 O4) FORMUL 10 OLA 2(C18 H34 O2) FORMUL 12 HOH *44(H2 O) HELIX 1 AA1 LYS A 22 TYR A 58 1 37 HELIX 2 AA2 SER A 63 ALA A 92 1 30 HELIX 3 AA3 PHE A 96 HIS A 132 1 37 HELIX 4 AA4 PHE A 135 ARG A 140 1 6 HELIX 5 AA5 THR A 141 PHE A 166 1 26 HELIX 6 AA6 PRO A 183 SER A 185 5 3 HELIX 7 AA7 GLN A 186 LEU A 203 1 18 HELIX 8 AA8 LEU A 203 LEU A 222 1 20 HELIX 9 AA9 ASP A 1019 GLY A 1023 5 5 HELIX 10 AB1 ASP A 1029 ILE A 1033 5 5 HELIX 11 AB2 GLY A 1045 ASP A 1047 5 3 HELIX 12 AB3 VAL A 1052 PHE A 260 1 37 HELIX 13 AB4 ASN A 268 HIS A 289 1 22 HELIX 14 AB5 CYS A 291 VAL A 300 1 10 HELIX 15 AB6 GLY A 301 LYS A 314 1 14 HELIX 16 AB7 LEU B 4 GLN B 8 5 5 HELIX 17 AB8 PRO B 20 ALA B 22 5 3 HELIX 18 AB9 LYS B 55 MET B 67 1 13 SHEET 1 AA1 2 THR A 167 GLU A 172 0 SHEET 2 AA1 2 HIS A 175 SER A 180 -1 O HIS A 175 N GLU A 172 SHEET 1 AA2 3 ILE A1012 TYR A1013 0 SHEET 2 AA2 3 TYR A1004 CYS A1006 -1 N TYR A1004 O TYR A1013 SHEET 3 AA2 3 PHE A1049 GLU A1051 -1 O GLU A1050 N THR A1005 SHEET 1 AA3 3 ILE B 24 TYR B 29 0 SHEET 2 AA3 3 VAL B 39 THR B 43 -1 O VAL B 40 N PHE B 28 SHEET 3 AA3 3 GLN B 48 ALA B 51 -1 O ALA B 51 N VAL B 39 SSBOND 1 CYS A 20 CYS A 269 1555 1555 2.04 SSBOND 2 CYS A 101 CYS A 178 1555 1555 2.06 SSBOND 3 CYS B 10 CYS B 34 1555 1555 2.04 SSBOND 4 CYS B 11 CYS B 50 1555 1555 2.05 LINK SG CYS A1006 ZN ZN A1101 1555 1555 2.45 LINK SG CYS A1009 ZN ZN A1101 1555 1555 2.18 LINK SG CYS A1039 ZN ZN A1101 1555 1555 2.29 LINK SG CYS A1042 ZN ZN A1101 1555 1555 2.29 LINK C PCA B 0 N GLY B 1 1555 1555 1.33 SITE 1 AC1 4 CYS A1006 CYS A1009 CYS A1039 CYS A1042 SITE 1 AC2 6 PHE A 189 ASN A 192 PHE A 193 LEU A 196 SITE 2 AC2 6 OLC A1107 HOH A1230 SITE 1 AC3 1 PHE A 85 SITE 1 AC4 3 ALA A 249 LEU A 266 ARG A 274 SITE 1 AC5 2 GLN A 277 ALA A 278 SITE 1 AC6 2 SER A 38 HIS A 88 SITE 1 AC7 6 ASN A 24 ILE A 28 LEU A 32 PHE A 189 SITE 2 AC7 6 GLN A 277 OLC A1102 SITE 1 AC8 2 ARG A 235 OLA A1109 SITE 1 AC9 2 ILE A 242 OLA A1108 CRYST1 38.010 52.640 302.670 90.00 90.00 90.00 P 2 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.026309 0.000000 0.000000 0.00000 SCALE2 0.000000 0.018997 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003304 0.00000 ATOM 1 N THR A 16 -141.703-102.119 603.566 1.00 65.61 N ANISOU 1 N THR A 16 6303 12124 6500 -406 53 -1152 N ATOM 2 CA THR A 16 -140.504-102.951 603.634 1.00 62.92 C ANISOU 2 CA THR A 16 5998 11706 6203 -455 104 -1172 C ATOM 3 C THR A 16 -139.411-102.205 604.391 1.00 59.78 C ANISOU 3 C THR A 16 5687 11181 5845 -444 99 -1030 C ATOM 4 O THR A 16 -139.277-100.988 604.258 1.00 62.15 O ANISOU 4 O THR A 16 5971 11555 6087 -418 72 -906 O ATOM 5 CB THR A 16 -140.001-103.367 602.215 1.00 59.81 C ANISOU 5 CB THR A 16 5519 11477 5728 -491 110 -1207 C ATOM 6 OG1 THR A 16 -139.169-104.532 602.313 1.00 57.05 O ANISOU 6 OG1 THR A 16 5205 11017 5454 -536 142 -1277 O ATOM 7 CG2 THR A 16 -139.234-102.239 601.520 1.00 58.32 C ANISOU 7 CG2 THR A 16 5297 11416 5445 -483 85 -1062 C ATOM 8 N SER A 17 -138.654-102.938 605.203 1.00 53.47 N ANISOU 8 N SER A 17 4974 10200 5142 -464 123 -1051 N ATOM 9 CA SER A 17 -137.631-102.354 606.070 1.00 52.71 C ANISOU 9 CA SER A 17 4964 9973 5091 -452 119 -938 C ATOM 10 C SER A 17 -138.157-101.198 606.923 1.00 50.08 C ANISOU 10 C SER A 17 4662 9604 4763 -410 92 -849 C ATOM 11 O SER A 17 -137.495-100.169 607.057 1.00 51.16 O ANISOU 11 O SER A 17 4815 9744 4881 -400 77 -723 O ATOM 12 CB SER A 17 -136.443-101.858 605.248 1.00 53.24 C ANISOU 12 CB SER A 17 4998 10126 5105 -472 114 -848 C ATOM 13 OG SER A 17 -136.774-100.649 604.592 1.00 54.09 O ANISOU 13 OG SER A 17 5042 10391 5118 -459 85 -752 O ATOM 14 N GLU A 18 -139.347-101.359 607.489 1.00 45.88 N ANISOU 14 N GLU A 18 4129 9046 4258 -389 88 -918 N ATOM 15 CA GLU A 18 -139.882-100.354 608.395 1.00 45.14 C ANISOU 15 CA GLU A 18 4059 8914 4179 -346 65 -850 C ATOM 16 C GLU A 18 -139.643-100.796 609.832 1.00 35.01 C ANISOU 16 C GLU A 18 2874 7429 3000 -347 74 -869 C ATOM 17 O GLU A 18 -139.513-101.988 610.099 1.00 33.88 O ANISOU 17 O GLU A 18 2764 7198 2912 -378 95 -963 O ATOM 18 CB GLU A 18 -141.376-100.128 608.142 1.00 57.54 C ANISOU 18 CB GLU A 18 5573 10545 5744 -315 20 -899 C ATOM 19 CG GLU A 18 -142.240-101.359 608.392 1.00 68.68 C ANISOU 19 CG GLU A 18 6966 11948 7183 -340 61 -1069 C ATOM 20 CD GLU A 18 -143.704-101.143 608.037 1.00 75.22 C ANISOU 20 CD GLU A 18 7732 12824 8023 -313 -1 -1116 C ATOM 21 OE1 GLU A 18 -144.134 -99.973 607.936 1.00 77.67 O ANISOU 21 OE1 GLU A 18 8038 13133 8341 -260 -85 -1013 O ATOM 22 OE2 GLU A 18 -144.421-102.150 607.852 1.00 76.66 O ANISOU 22 OE2 GLU A 18 7872 13049 8209 -344 32 -1262 O ATOM 23 N PRO A 19 -139.567 -99.838 610.766 1.00 31.37 N ANISOU 23 N PRO A 19 2452 6905 2563 -315 57 -781 N ATOM 24 CA PRO A 19 -139.432-100.238 612.167 1.00 31.99 C ANISOU 24 CA PRO A 19 2610 6811 2734 -314 62 -804 C ATOM 25 C PRO A 19 -140.630-101.079 612.600 1.00 36.07 C ANISOU 25 C PRO A 19 3114 7297 3292 -323 73 -934 C ATOM 26 O PRO A 19 -141.705-100.950 612.018 1.00 38.41 O ANISOU 26 O PRO A 19 3343 7688 3562 -313 60 -979 O ATOM 27 CB PRO A 19 -139.386 -98.900 612.914 1.00 28.19 C ANISOU 27 CB PRO A 19 2153 6264 2292 -273 24 -679 C ATOM 28 CG PRO A 19 -138.935 -97.910 611.904 1.00 29.29 C ANISOU 28 CG PRO A 19 2252 6505 2370 -268 -4 -570 C ATOM 29 CD PRO A 19 -139.512 -98.376 610.600 1.00 32.56 C ANISOU 29 CD PRO A 19 2590 7073 2708 -281 1 -637 C ATOM 30 N CYS A 20 -140.432-101.942 613.589 1.00 36.09 N ANISOU 30 N CYS A 20 3176 7159 3377 -346 88 -987 N ATOM 31 CA CYS A 20 -141.483-102.820 614.089 1.00 41.10 C ANISOU 31 CA CYS A 20 3799 7753 4063 -372 105 -1110 C ATOM 32 C CYS A 20 -142.373-102.096 615.088 1.00 49.46 C ANISOU 32 C CYS A 20 4860 8755 5178 -338 86 -1084 C ATOM 33 O CYS A 20 -141.888-101.627 616.117 1.00 51.15 O ANISOU 33 O CYS A 20 5128 8854 5452 -316 74 -1005 O ATOM 34 CB CYS A 20 -140.870-104.056 614.743 1.00 39.51 C ANISOU 34 CB CYS A 20 3650 7422 3939 -416 128 -1167 C ATOM 35 SG CYS A 20 -142.042-104.999 615.726 1.00 45.14 S ANISOU 35 SG CYS A 20 4359 8056 4736 -460 159 -1297 S ATOM 36 N GLN A 21 -143.669-102.020 614.793 1.00 58.35 N ANISOU 36 N GLN A 21 5922 9936 6313 -332 74 -1140 N ATOM 37 CA GLN A 21 -144.598-101.217 615.589 1.00 65.69 C ANISOU 37 CA GLN A 21 6838 10803 7319 -292 39 -1101 C ATOM 38 C GLN A 21 -145.109-101.946 616.826 1.00 67.75 C ANISOU 38 C GLN A 21 7125 10947 7669 -325 72 -1174 C ATOM 39 O GLN A 21 -145.486-103.113 616.743 1.00 67.33 O ANISOU 39 O GLN A 21 7057 10902 7622 -384 114 -1298 O ATOM 40 CB GLN A 21 -145.802-100.805 614.731 1.00 68.83 C ANISOU 40 CB GLN A 21 7147 11316 7691 -268 0 -1133 C ATOM 41 CG GLN A 21 -145.493-100.335 613.313 1.00 68.83 C ANISOU 41 CG GLN A 21 7103 11454 7597 -249 -32 -1086 C ATOM 42 CD GLN A 21 -144.529 -99.156 613.217 1.00 70.76 C ANISOU 42 CD GLN A 21 7384 11680 7824 -208 -71 -928 C ATOM 43 OE1 GLN A 21 -144.105 -98.576 614.226 1.00 68.80 O ANISOU 43 OE1 GLN A 21 7191 11315 7637 -188 -79 -850 O ATOM 44 NE2 GLN A 21 -144.163 -98.809 611.983 1.00 73.12 N ANISOU 44 NE2 GLN A 21 7647 12097 8038 -203 -94 -883 N ATOM 45 N LYS A 22 -145.115-101.262 617.966 1.00 74.89 N ANISOU 45 N LYS A 22 8063 11745 8645 -291 58 -1100 N ATOM 46 CA LYS A 22 -145.873-101.738 619.121 1.00 75.57 C ANISOU 46 CA LYS A 22 8154 11740 8820 -315 87 -1160 C ATOM 47 C LYS A 22 -147.042-100.785 619.366 1.00 76.63 C ANISOU 47 C LYS A 22 8232 11894 8989 -268 50 -1144 C ATOM 48 O LYS A 22 -147.287-100.365 620.495 1.00 80.08 O ANISOU 48 O LYS A 22 8688 12245 9496 -247 52 -1111 O ATOM 49 CB LYS A 22 -144.999-101.855 620.380 1.00 71.54 C ANISOU 49 CB LYS A 22 7721 11092 8371 -317 109 -1103 C ATOM 50 CG LYS A 22 -143.627-101.212 620.289 1.00 68.29 C ANISOU 50 CG LYS A 22 7360 10661 7924 -282 85 -989 C ATOM 51 CD LYS A 22 -142.566-102.236 619.920 1.00 65.71 C ANISOU 51 CD LYS A 22 7069 10332 7566 -324 112 -1021 C ATOM 52 N ILE A 23 -147.760-100.459 618.295 1.00 66.89 N ANISOU 52 N ILE A 23 6926 10780 7707 -248 13 -1170 N ATOM 53 CA ILE A 23 -148.777 -99.409 618.312 1.00 61.18 C ANISOU 53 CA ILE A 23 6143 10092 7011 -188 -43 -1144 C ATOM 54 C ILE A 23 -149.866 -99.619 619.380 1.00 58.67 C ANISOU 54 C ILE A 23 5796 9720 6774 -200 -18 -1215 C ATOM 55 O ILE A 23 -150.296 -98.663 620.038 1.00 56.52 O ANISOU 55 O ILE A 23 5512 9413 6552 -145 -52 -1164 O ATOM 56 CB ILE A 23 -149.420 -99.283 616.917 1.00 57.78 C ANISOU 56 CB ILE A 23 5631 9809 6514 -172 -87 -1182 C ATOM 57 CG1 ILE A 23 -150.744 -98.518 616.980 1.00 55.85 C ANISOU 57 CG1 ILE A 23 5307 9606 6306 -118 -144 -1198 C ATOM 58 CG2 ILE A 23 -149.596-100.664 616.296 1.00 59.55 C ANISOU 58 CG2 ILE A 23 5829 10099 6698 -247 -32 -1315 C ATOM 59 N ASN A 24 -150.292-100.864 619.570 1.00 55.24 N ANISOU 59 N ASN A 24 5352 9280 6359 -276 44 -1335 N ATOM 60 CA ASN A 24 -151.296-101.162 620.584 1.00 53.16 C ANISOU 60 CA ASN A 24 5059 8967 6173 -303 80 -1406 C ATOM 61 C ASN A 24 -150.747-100.967 621.985 1.00 53.23 C ANISOU 61 C ASN A 24 5140 8839 6245 -296 109 -1336 C ATOM 62 O ASN A 24 -151.306-100.217 622.787 1.00 55.32 O ANISOU 62 O ASN A 24 5386 9073 6560 -255 96 -1309 O ATOM 63 CB ASN A 24 -151.817-102.585 620.423 1.00 55.71 C ANISOU 63 CB ASN A 24 5356 9307 6504 -398 147 -1551 C ATOM 64 CG ASN A 24 -152.792-102.717 619.275 1.00 61.90 C ANISOU 64 CG ASN A 24 6040 10235 7243 -403 122 -1647 C ATOM 65 OD1 ASN A 24 -153.330-101.724 618.781 1.00 64.14 O ANISOU 65 OD1 ASN A 24 6263 10599 7506 -331 53 -1610 O ATOM 66 ND2 ASN A 24 -153.027-103.948 618.841 1.00 65.09 N ANISOU 66 ND2 ASN A 24 6423 10672 7636 -487 176 -1775 N ATOM 67 N VAL A 25 -149.641-101.649 622.261 1.00 49.37 N ANISOU 67 N VAL A 25 4730 8275 5753 -334 147 -1312 N ATOM 68 CA VAL A 25 -148.952-101.568 623.542 1.00 44.00 C ANISOU 68 CA VAL A 25 4121 7469 5127 -328 175 -1243 C ATOM 69 C VAL A 25 -148.734-100.132 623.999 1.00 39.65 C ANISOU 69 C VAL A 25 3581 6899 4586 -243 122 -1133 C ATOM 70 O VAL A 25 -148.931 -99.799 625.166 1.00 38.95 O ANISOU 70 O VAL A 25 3506 6739 4555 -227 141 -1111 O ATOM 71 CB VAL A 25 -147.596-102.269 623.464 1.00 45.03 C ANISOU 71 CB VAL A 25 4326 7546 5236 -357 196 -1212 C ATOM 72 CG1 VAL A 25 -146.924-102.298 624.828 1.00 41.86 C ANISOU 72 CG1 VAL A 25 3991 7018 4894 -350 230 -1148 C ATOM 73 CG2 VAL A 25 -147.776-103.667 622.895 1.00 52.17 C ANISOU 73 CG2 VAL A 25 5218 8473 6133 -440 245 -1328 C ATOM 74 N LYS A 26 -148.329 -99.281 623.069 1.00 37.73 N ANISOU 74 N LYS A 26 3329 6720 4288 -192 60 -1067 N ATOM 75 CA LYS A 26 -148.080 -97.886 623.383 1.00 34.59 C ANISOU 75 CA LYS A 26 2938 6300 3903 -116 7 -964 C ATOM 76 C LYS A 26 -149.380 -97.230 623.805 1.00 31.56 C ANISOU 76 C LYS A 26 2488 5937 3567 -77 -14 -996 C ATOM 77 O LYS A 26 -149.468 -96.679 624.898 1.00 32.98 O ANISOU 77 O LYS A 26 2682 6049 3799 -46 -8 -967 O ATOM 78 CB LYS A 26 -147.470 -97.164 622.179 1.00 37.47 C ANISOU 78 CB LYS A 26 3300 6734 4203 -81 -52 -889 C ATOM 79 CG LYS A 26 -147.116 -95.708 622.424 1.00 42.57 C ANISOU 79 CG LYS A 26 3958 7348 4869 -10 -111 -777 C ATOM 80 CD LYS A 26 -145.820 -95.336 621.711 1.00 49.15 C ANISOU 80 CD LYS A 26 4835 8190 5648 -9 -135 -685 C ATOM 81 CE LYS A 26 -145.844 -93.878 621.282 1.00 55.77 C ANISOU 81 CE LYS A 26 5655 9046 6490 55 -218 -590 C ATOM 82 NZ LYS A 26 -146.425 -93.004 622.343 1.00 58.47 N ANISOU 82 NZ LYS A 26 5987 9321 6906 109 -245 -574 N ATOM 83 N GLN A 27 -150.393 -97.326 622.944 1.00 33.55 N ANISOU 83 N GLN A 27 2662 6288 3798 -76 -38 -1064 N ATOM 84 CA GLN A 27 -151.673 -96.642 623.151 1.00 36.90 C ANISOU 84 CA GLN A 27 3007 6753 4262 -28 -71 -1099 C ATOM 85 C GLN A 27 -152.397 -97.113 624.408 1.00 32.45 C ANISOU 85 C GLN A 27 2430 6133 3766 -61 -6 -1170 C ATOM 86 O GLN A 27 -153.041 -96.319 625.100 1.00 33.25 O ANISOU 86 O GLN A 27 2497 6223 3915 -9 -23 -1164 O ATOM 87 CB GLN A 27 -152.574 -96.815 621.923 1.00 42.57 C ANISOU 87 CB GLN A 27 3638 7599 4939 -26 -107 -1169 C ATOM 88 CG GLN A 27 -152.395 -95.705 620.891 1.00 49.44 C ANISOU 88 CG GLN A 27 4487 8532 5765 50 -201 -1083 C ATOM 89 CD GLN A 27 -152.989 -96.042 619.536 1.00 60.64 C ANISOU 89 CD GLN A 27 5834 10083 7123 44 -234 -1144 C ATOM 90 OE1 GLN A 27 -153.292 -97.201 619.243 1.00 67.06 O ANISOU 90 OE1 GLN A 27 6623 10940 7915 -27 -181 -1249 O ATOM 91 NE2 GLN A 27 -153.166 -95.023 618.699 1.00 62.77 N ANISOU 91 NE2 GLN A 27 6070 10418 7364 120 -327 -1079 N ATOM 92 N ILE A 28 -152.279 -98.397 624.713 1.00 27.29 N ANISOU 92 N ILE A 28 1805 5444 3120 -148 69 -1236 N ATOM 93 CA ILE A 28 -152.825 -98.916 625.953 1.00 29.07 C ANISOU 93 CA ILE A 28 2031 5604 3411 -191 141 -1290 C ATOM 94 C ILE A 28 -152.079 -98.327 627.146 1.00 28.50 C ANISOU 94 C ILE A 28 2028 5429 3372 -154 153 -1200 C ATOM 95 O ILE A 28 -152.694 -97.845 628.109 1.00 23.70 O ANISOU 95 O ILE A 28 1397 4795 2813 -127 170 -1208 O ATOM 96 CB ILE A 28 -152.761-100.447 625.986 1.00 29.13 C ANISOU 96 CB ILE A 28 2062 5581 3425 -297 220 -1371 C ATOM 97 CG1 ILE A 28 -153.871-101.009 625.098 1.00 32.77 C ANISOU 97 CG1 ILE A 28 2433 6148 3872 -340 222 -1493 C ATOM 98 CG2 ILE A 28 -152.899-100.958 627.416 1.00 24.15 C ANISOU 98 CG2 ILE A 28 1466 4848 2861 -340 304 -1383 C ATOM 99 CD1 ILE A 28 -153.759-102.488 624.815 1.00 35.90 C ANISOU 99 CD1 ILE A 28 2847 6529 4265 -444 290 -1583 C ATOM 100 N ALA A 29 -150.751 -98.353 627.067 1.00 28.24 N ANISOU 100 N ALA A 29 2075 5346 3310 -150 144 -1121 N ATOM 101 CA ALA A 29 -149.900 -97.808 628.119 1.00 29.81 C ANISOU 101 CA ALA A 29 2339 5456 3533 -115 151 -1038 C ATOM 102 C ALA A 29 -150.199 -96.340 628.390 1.00 21.09 C ANISOU 102 C ALA A 29 1204 4365 2445 -26 92 -989 C ATOM 103 O ALA A 29 -150.133 -95.893 629.529 1.00 25.59 O ANISOU 103 O ALA A 29 1795 4876 3053 2 112 -967 O ATOM 104 CB ALA A 29 -148.431 -97.980 627.753 1.00 27.40 C ANISOU 104 CB ALA A 29 2106 5118 3185 -120 137 -966 C ATOM 105 N ALA A 30 -150.522 -95.592 627.340 1.00 21.67 N ANISOU 105 N ALA A 30 1227 4515 2490 21 19 -973 N ATOM 106 CA ALA A 30 -150.767 -94.158 627.476 1.00 28.28 C ANISOU 106 CA ALA A 30 2038 5359 3350 112 -48 -920 C ATOM 107 C ALA A 30 -152.025 -93.869 628.290 1.00 28.98 C ANISOU 107 C ALA A 30 2062 5457 3493 140 -30 -988 C ATOM 108 O ALA A 30 -152.149 -92.805 628.894 1.00 33.56 O ANISOU 108 O ALA A 30 2634 6011 4106 213 -62 -955 O ATOM 109 CB ALA A 30 -150.869 -93.508 626.106 1.00 26.90 C ANISOU 109 CB ALA A 30 1825 5262 3135 154 -131 -884 C ATOM 110 N ARG A 31 -152.957 -94.819 628.309 1.00 25.72 N ANISOU 110 N ARG A 31 1601 5081 3091 81 24 -1087 N ATOM 111 CA ARG A 31 -154.176 -94.654 629.087 1.00 29.90 C ANISOU 111 CA ARG A 31 2062 5625 3672 95 53 -1159 C ATOM 112 C ARG A 31 -154.009 -95.196 630.501 1.00 29.21 C ANISOU 112 C ARG A 31 2024 5451 3622 50 145 -1173 C ATOM 113 O ARG A 31 -154.361 -94.521 631.464 1.00 28.47 O ANISOU 113 O ARG A 31 1918 5332 3567 98 157 -1172 O ATOM 114 CB ARG A 31 -155.361 -95.334 628.389 1.00 32.87 C ANISOU 114 CB ARG A 31 2349 6094 4045 52 63 -1266 C ATOM 115 CG ARG A 31 -155.715 -94.670 627.070 1.00 39.77 C ANISOU 115 CG ARG A 31 3161 7066 4884 113 -32 -1257 C ATOM 116 CD ARG A 31 -156.933 -95.286 626.414 1.00 50.27 C ANISOU 116 CD ARG A 31 4390 8500 6209 78 -26 -1373 C ATOM 117 NE ARG A 31 -157.325 -94.543 625.217 1.00 55.54 N ANISOU 117 NE ARG A 31 4995 9266 6844 152 -125 -1358 N ATOM 118 CZ ARG A 31 -158.238 -93.578 625.206 1.00 57.37 C ANISOU 118 CZ ARG A 31 5146 9550 7103 241 -186 -1372 C ATOM 119 NH1 ARG A 31 -158.860 -93.240 626.326 1.00 58.44 N ANISOU 119 NH1 ARG A 31 5251 9654 7298 265 -153 -1407 N ATOM 120 NH2 ARG A 31 -158.531 -92.953 624.076 1.00 59.94 N ANISOU 120 NH2 ARG A 31 5421 9960 7395 310 -281 -1350 N ATOM 121 N LEU A 32 -153.464 -96.406 630.622 1.00 25.05 N ANISOU 121 N LEU A 32 1555 4879 3085 -37 210 -1182 N ATOM 122 CA LEU A 32 -153.328 -97.053 631.922 1.00 25.19 C ANISOU 122 CA LEU A 32 1622 4811 3136 -84 305 -1189 C ATOM 123 C LEU A 32 -152.319 -96.394 632.868 1.00 30.85 C ANISOU 123 C LEU A 32 2415 5451 3856 -32 304 -1103 C ATOM 124 O LEU A 32 -152.636 -96.122 634.023 1.00 29.58 O ANISOU 124 O LEU A 32 2260 5253 3727 -12 351 -1109 O ATOM 125 CB LEU A 32 -152.934 -98.511 631.730 1.00 25.70 C ANISOU 125 CB LEU A 32 1734 4840 3193 -182 369 -1214 C ATOM 126 CG LEU A 32 -154.024 -99.415 631.177 1.00 27.28 C ANISOU 126 CG LEU A 32 1863 5099 3403 -257 404 -1324 C ATOM 127 CD1 LEU A 32 -153.543-100.850 631.173 1.00 23.99 C ANISOU 127 CD1 LEU A 32 1505 4624 2988 -352 478 -1347 C ATOM 128 CD2 LEU A 32 -155.285 -99.258 632.000 1.00 27.75 C ANISOU 128 CD2 LEU A 32 1857 5176 3512 -262 454 -1390 C ATOM 129 N LEU A 33 -151.104 -96.151 632.379 1.00 28.44 N ANISOU 129 N LEU A 33 2166 5127 3514 -11 253 -1028 N ATOM 130 CA LEU A 33 -149.993 -95.766 633.251 1.00 25.47 C ANISOU 130 CA LEU A 33 1866 4677 3135 22 260 -955 C ATOM 131 C LEU A 33 -150.147 -94.416 633.971 1.00 28.51 C ANISOU 131 C LEU A 33 2235 5057 3541 110 224 -933 C ATOM 132 O LEU A 33 -149.846 -94.337 635.166 1.00 32.67 O ANISOU 132 O LEU A 33 2807 5527 4082 124 272 -921 O ATOM 133 CB LEU A 33 -148.678 -95.776 632.458 1.00 19.16 C ANISOU 133 CB LEU A 33 1118 3873 2291 22 209 -887 C ATOM 134 CG LEU A 33 -148.216 -97.141 631.935 1.00 25.15 C ANISOU 134 CG LEU A 33 1910 4617 3028 -56 250 -902 C ATOM 135 CD1 LEU A 33 -146.768 -97.078 631.488 1.00 24.23 C ANISOU 135 CD1 LEU A 33 1852 4484 2871 -47 212 -830 C ATOM 136 CD2 LEU A 33 -148.386 -98.230 632.983 1.00 24.74 C ANISOU 136 CD2 LEU A 33 1895 4495 3008 -110 352 -933 C ATOM 137 N PRO A 34 -150.595 -93.350 633.269 1.00 25.36 N ANISOU 137 N PRO A 34 1778 4714 3144 175 141 -928 N ATOM 138 CA PRO A 34 -150.654 -92.063 633.983 1.00 25.41 C ANISOU 138 CA PRO A 34 1777 4702 3176 265 105 -909 C ATOM 139 C PRO A 34 -151.499 -92.042 635.268 1.00 34.31 C ANISOU 139 C PRO A 34 2885 5809 4343 278 175 -969 C ATOM 140 O PRO A 34 -151.034 -91.448 636.242 1.00 39.82 O ANISOU 140 O PRO A 34 3623 6458 5049 325 183 -948 O ATOM 141 CB PRO A 34 -151.244 -91.108 632.936 1.00 24.72 C ANISOU 141 CB PRO A 34 1622 4676 3093 330 11 -901 C ATOM 142 CG PRO A 34 -150.797 -91.670 631.648 1.00 26.62 C ANISOU 142 CG PRO A 34 1872 4953 3290 281 -17 -871 C ATOM 143 CD PRO A 34 -150.829 -93.174 631.823 1.00 26.55 C ANISOU 143 CD PRO A 34 1884 4936 3269 182 72 -922 C ATOM 144 N PRO A 35 -152.703 -92.656 635.285 1.00 32.59 N ANISOU 144 N PRO A 35 2606 5630 4146 237 227 -1045 N ATOM 145 CA PRO A 35 -153.414 -92.621 636.568 1.00 30.77 C ANISOU 145 CA PRO A 35 2365 5376 3949 245 304 -1094 C ATOM 146 C PRO A 35 -152.738 -93.499 637.607 1.00 22.33 C ANISOU 146 C PRO A 35 1387 4230 2868 188 402 -1070 C ATOM 147 O PRO A 35 -152.666 -93.127 638.776 1.00 22.36 O ANISOU 147 O PRO A 35 1427 4191 2878 224 446 -1067 O ATOM 148 CB PRO A 35 -154.803 -93.161 636.222 1.00 24.25 C ANISOU 148 CB PRO A 35 1449 4618 3147 202 337 -1180 C ATOM 149 CG PRO A 35 -154.926 -93.001 634.758 1.00 26.67 C ANISOU 149 CG PRO A 35 1705 4993 3434 212 248 -1178 C ATOM 150 CD PRO A 35 -153.557 -93.197 634.213 1.00 29.75 C ANISOU 150 CD PRO A 35 2176 5345 3783 195 213 -1097 C ATOM 151 N LEU A 36 -152.240 -94.650 637.173 1.00 25.33 N ANISOU 151 N LEU A 36 1807 4589 3227 107 434 -1053 N ATOM 152 CA LEU A 36 -151.555 -95.574 638.067 1.00 28.38 C ANISOU 152 CA LEU A 36 2287 4896 3600 60 524 -1022 C ATOM 153 C LEU A 36 -150.356 -94.919 638.741 1.00 31.37 C ANISOU 153 C LEU A 36 2741 5224 3954 121 501 -957 C ATOM 154 O LEU A 36 -150.244 -94.925 639.969 1.00 34.03 O ANISOU 154 O LEU A 36 3135 5511 4285 138 570 -949 O ATOM 155 CB LEU A 36 -151.098 -96.821 637.310 1.00 28.85 C ANISOU 155 CB LEU A 36 2376 4942 3644 -22 543 -1013 C ATOM 156 CG LEU A 36 -150.294 -97.787 638.181 1.00 28.77 C ANISOU 156 CG LEU A 36 2470 4844 3618 -57 632 -971 C ATOM 157 CD1 LEU A 36 -151.100 -98.190 639.420 1.00 28.58 C ANISOU 157 CD1 LEU A 36 2465 4784 3609 -78 746 -999 C ATOM 158 CD2 LEU A 36 -149.895 -99.012 637.385 1.00 25.88 C ANISOU 158 CD2 LEU A 36 2127 4462 3243 -130 648 -971 C ATOM 159 N TYR A 37 -149.467 -94.355 637.932 1.00 29.63 N ANISOU 159 N TYR A 37 2524 5021 3713 153 407 -912 N ATOM 160 CA TYR A 37 -148.278 -93.688 638.451 1.00 27.44 C ANISOU 160 CA TYR A 37 2306 4708 3411 208 372 -858 C ATOM 161 C TYR A 37 -148.688 -92.538 639.367 1.00 29.92 C ANISOU 161 C TYR A 37 2607 5018 3743 290 363 -882 C ATOM 162 O TYR A 37 -148.060 -92.310 640.404 1.00 31.50 O ANISOU 162 O TYR A 37 2872 5173 3925 324 390 -867 O ATOM 163 CB TYR A 37 -147.382 -93.196 637.305 1.00 24.64 C ANISOU 163 CB TYR A 37 1942 4383 3035 225 270 -808 C ATOM 164 CG TYR A 37 -146.645 -94.317 636.590 1.00 24.12 C ANISOU 164 CG TYR A 37 1912 4309 2942 155 284 -780 C ATOM 165 CD1 TYR A 37 -146.877 -95.649 636.921 1.00 26.02 C ANISOU 165 CD1 TYR A 37 2185 4513 3187 87 376 -803 C ATOM 166 CD2 TYR A 37 -145.704 -94.046 635.601 1.00 25.65 C ANISOU 166 CD2 TYR A 37 2111 4527 3107 158 209 -729 C ATOM 167 CE1 TYR A 37 -146.203 -96.687 636.275 1.00 28.25 C ANISOU 167 CE1 TYR A 37 2501 4783 3451 32 388 -784 C ATOM 168 CE2 TYR A 37 -145.019 -95.081 634.949 1.00 25.68 C ANISOU 168 CE2 TYR A 37 2148 4525 3086 100 224 -711 C ATOM 169 CZ TYR A 37 -145.275 -96.401 635.297 1.00 25.79 C ANISOU 169 CZ TYR A 37 2190 4501 3109 41 311 -743 C ATOM 170 OH TYR A 37 -144.613 -97.441 634.668 1.00 23.38 O ANISOU 170 OH TYR A 37 1915 4184 2785 -9 326 -732 O ATOM 171 N SER A 38 -149.762 -91.842 639.004 1.00 31.33 N ANISOU 171 N SER A 38 2704 5244 3955 326 326 -925 N ATOM 172 CA SER A 38 -150.300 -90.775 639.848 1.00 33.85 C ANISOU 172 CA SER A 38 3004 5558 4298 410 320 -960 C ATOM 173 C SER A 38 -150.716 -91.306 641.213 1.00 31.75 C ANISOU 173 C SER A 38 2782 5252 4028 389 438 -993 C ATOM 174 O SER A 38 -150.466 -90.672 642.232 1.00 31.98 O ANISOU 174 O SER A 38 2856 5246 4048 449 452 -999 O ATOM 175 CB SER A 38 -151.497 -90.101 639.178 1.00 37.32 C ANISOU 175 CB SER A 38 3344 6059 4776 452 267 -1005 C ATOM 176 OG SER A 38 -151.119 -89.489 637.961 1.00 39.56 O ANISOU 176 OG SER A 38 3601 6372 5057 484 158 -962 O ATOM 177 N LEU A 39 -151.363 -92.469 641.224 1.00 31.71 N ANISOU 177 N LEU A 39 2770 5251 4028 305 525 -1014 N ATOM 178 CA LEU A 39 -151.803 -93.090 642.469 1.00 29.59 C ANISOU 178 CA LEU A 39 2550 4943 3750 277 649 -1032 C ATOM 179 C LEU A 39 -150.589 -93.476 643.297 1.00 32.33 C ANISOU 179 C LEU A 39 3022 5216 4046 278 691 -974 C ATOM 180 O LEU A 39 -150.547 -93.239 644.508 1.00 27.35 O ANISOU 180 O LEU A 39 2455 4547 3389 316 749 -977 O ATOM 181 CB LEU A 39 -152.664 -94.317 642.187 1.00 29.67 C ANISOU 181 CB LEU A 39 2528 4970 3777 181 727 -1063 C ATOM 182 CG LEU A 39 -153.331 -94.989 643.388 1.00 34.36 C ANISOU 182 CG LEU A 39 3160 5533 4362 146 862 -1085 C ATOM 183 CD1 LEU A 39 -154.269 -94.025 644.089 1.00 34.97 C ANISOU 183 CD1 LEU A 39 3183 5643 4460 209 876 -1140 C ATOM 184 CD2 LEU A 39 -154.078 -96.241 642.955 1.00 34.85 C ANISOU 184 CD2 LEU A 39 3186 5611 4444 42 928 -1119 C ATOM 185 N VAL A 40 -149.601 -94.066 642.622 1.00 31.50 N ANISOU 185 N VAL A 40 2953 5095 3922 242 659 -924 N ATOM 186 CA VAL A 40 -148.319 -94.406 643.237 1.00 27.22 C ANISOU 186 CA VAL A 40 2521 4492 3328 253 679 -869 C ATOM 187 C VAL A 40 -147.643 -93.178 643.847 1.00 21.17 C ANISOU 187 C VAL A 40 1783 3720 2539 343 618 -867 C ATOM 188 O VAL A 40 -147.186 -93.212 644.983 1.00 21.38 O ANISOU 188 O VAL A 40 1903 3699 2521 372 668 -856 O ATOM 189 CB VAL A 40 -147.361 -95.041 642.212 1.00 25.20 C ANISOU 189 CB VAL A 40 2274 4238 3062 211 632 -824 C ATOM 190 CG1 VAL A 40 -145.966 -95.158 642.792 1.00 20.98 C ANISOU 190 CG1 VAL A 40 1839 3657 2476 242 630 -774 C ATOM 191 CG2 VAL A 40 -147.885 -96.403 641.769 1.00 24.21 C ANISOU 191 CG2 VAL A 40 2145 4102 2951 124 702 -831 C ATOM 192 N PHE A 41 -147.586 -92.092 643.085 1.00 22.56 N ANISOU 192 N PHE A 41 1885 3943 2744 391 508 -878 N ATOM 193 CA PHE A 41 -146.985 -90.858 643.578 1.00 26.14 C ANISOU 193 CA PHE A 41 2358 4388 3185 483 438 -884 C ATOM 194 C PHE A 41 -147.766 -90.295 644.761 1.00 33.16 C ANISOU 194 C PHE A 41 3268 5256 4077 535 490 -937 C ATOM 195 O PHE A 41 -147.183 -89.752 645.692 1.00 33.80 O ANISOU 195 O PHE A 41 3420 5302 4122 593 483 -945 O ATOM 196 CB PHE A 41 -146.903 -89.812 642.473 1.00 26.31 C ANISOU 196 CB PHE A 41 2299 4454 3244 530 313 -879 C ATOM 197 CG PHE A 41 -146.345 -88.505 642.935 1.00 29.50 C ANISOU 197 CG PHE A 41 2722 4837 3650 630 236 -889 C ATOM 198 CD1 PHE A 41 -144.981 -88.310 643.004 1.00 33.24 C ANISOU 198 CD1 PHE A 41 3245 5295 4091 652 184 -852 C ATOM 199 CD2 PHE A 41 -147.183 -87.477 643.326 1.00 31.05 C ANISOU 199 CD2 PHE A 41 2888 5025 3884 707 214 -941 C ATOM 200 CE1 PHE A 41 -144.458 -87.101 643.444 1.00 33.89 C ANISOU 200 CE1 PHE A 41 3348 5347 4182 746 105 -869 C ATOM 201 CE2 PHE A 41 -146.669 -86.281 643.765 1.00 32.24 C ANISOU 201 CE2 PHE A 41 3068 5138 4044 804 138 -956 C ATOM 202 CZ PHE A 41 -145.303 -86.094 643.826 1.00 30.59 C ANISOU 202 CZ PHE A 41 2912 4905 3807 822 82 -921 C ATOM 203 N ILE A 42 -149.089 -90.413 644.719 1.00 35.40 N ANISOU 203 N ILE A 42 3487 5565 4399 515 539 -979 N ATOM 204 CA ILE A 42 -149.914 -89.973 645.835 1.00 30.69 C ANISOU 204 CA ILE A 42 2903 4954 3803 558 602 -1030 C ATOM 205 C ILE A 42 -149.606 -90.782 647.087 1.00 26.95 C ANISOU 205 C ILE A 42 2548 4424 3266 529 717 -1010 C ATOM 206 O ILE A 42 -149.134 -90.243 648.084 1.00 25.90 O ANISOU 206 O ILE A 42 2496 4255 3091 587 721 -1019 O ATOM 207 CB ILE A 42 -151.411 -90.091 645.512 1.00 32.96 C ANISOU 207 CB ILE A 42 3088 5292 4142 534 639 -1081 C ATOM 208 CG1 ILE A 42 -151.819 -89.007 644.512 1.00 37.26 C ANISOU 208 CG1 ILE A 42 3530 5887 4741 597 520 -1107 C ATOM 209 CG2 ILE A 42 -152.233 -89.967 646.775 1.00 28.36 C ANISOU 209 CG2 ILE A 42 2530 4696 3549 556 737 -1127 C ATOM 210 CD1 ILE A 42 -153.253 -89.114 644.043 1.00 36.65 C ANISOU 210 CD1 ILE A 42 3342 5872 4710 579 538 -1161 C ATOM 211 N PHE A 43 -149.864 -92.081 647.026 1.00 28.26 N ANISOU 211 N PHE A 43 2735 4582 3422 445 807 -983 N ATOM 212 CA PHE A 43 -149.674 -92.944 648.180 1.00 32.63 C ANISOU 212 CA PHE A 43 3409 5079 3908 424 924 -954 C ATOM 213 C PHE A 43 -148.219 -92.964 648.634 1.00 29.51 C ANISOU 213 C PHE A 43 3131 4635 3446 456 895 -907 C ATOM 214 O PHE A 43 -147.941 -92.970 649.828 1.00 31.24 O ANISOU 214 O PHE A 43 3459 4812 3598 489 951 -902 O ATOM 215 CB PHE A 43 -150.147 -94.368 647.869 1.00 40.22 C ANISOU 215 CB PHE A 43 4369 6039 4875 334 1011 -931 C ATOM 216 CG PHE A 43 -151.645 -94.520 647.837 1.00 48.72 C ANISOU 216 CG PHE A 43 5352 7162 5997 297 1071 -987 C ATOM 217 CD1 PHE A 43 -152.468 -93.536 648.358 1.00 54.18 C ANISOU 217 CD1 PHE A 43 5993 7885 6708 352 1073 -1046 C ATOM 218 CD2 PHE A 43 -152.230 -95.651 647.293 1.00 52.44 C ANISOU 218 CD2 PHE A 43 5785 7648 6493 207 1123 -991 C ATOM 219 CE1 PHE A 43 -153.850 -93.675 648.334 1.00 56.52 C ANISOU 219 CE1 PHE A 43 6195 8234 7047 319 1128 -1105 C ATOM 220 CE2 PHE A 43 -153.615 -95.795 647.267 1.00 55.75 C ANISOU 220 CE2 PHE A 43 6109 8118 6955 166 1176 -1055 C ATOM 221 CZ PHE A 43 -154.422 -94.805 647.788 1.00 55.49 C ANISOU 221 CZ PHE A 43 6020 8124 6940 223 1179 -1111 C ATOM 222 N GLY A 44 -147.293 -92.963 647.683 1.00 26.54 N ANISOU 222 N GLY A 44 2731 4270 3082 447 804 -877 N ATOM 223 CA GLY A 44 -145.883 -93.086 648.008 1.00 28.02 C ANISOU 223 CA GLY A 44 3014 4424 3206 471 769 -836 C ATOM 224 C GLY A 44 -145.321 -91.865 648.699 1.00 29.92 C ANISOU 224 C GLY A 44 3290 4664 3416 558 695 -866 C ATOM 225 O GLY A 44 -144.500 -91.968 649.618 1.00 31.00 O ANISOU 225 O GLY A 44 3538 4765 3476 588 704 -851 O ATOM 226 N PHE A 45 -145.767 -90.699 648.253 1.00 28.61 N ANISOU 226 N PHE A 45 3032 4535 3305 604 616 -911 N ATOM 227 CA PHE A 45 -145.258 -89.458 648.796 1.00 31.53 C ANISOU 227 CA PHE A 45 3430 4895 3656 695 533 -947 C ATOM 228 C PHE A 45 -145.686 -89.301 650.246 1.00 32.15 C ANISOU 228 C PHE A 45 3597 4935 3685 724 610 -983 C ATOM 229 O PHE A 45 -144.850 -89.095 651.127 1.00 33.09 O ANISOU 229 O PHE A 45 3818 5023 3732 764 589 -983 O ATOM 230 CB PHE A 45 -145.738 -88.269 647.972 1.00 35.28 C ANISOU 230 CB PHE A 45 3794 5401 4209 747 437 -986 C ATOM 231 CG PHE A 45 -144.971 -87.015 648.236 1.00 39.99 C ANISOU 231 CG PHE A 45 4421 5973 4800 841 328 -1015 C ATOM 232 CD1 PHE A 45 -143.798 -86.754 647.554 1.00 42.12 C ANISOU 232 CD1 PHE A 45 4685 6250 5067 860 229 -985 C ATOM 233 CD2 PHE A 45 -145.411 -86.108 649.182 1.00 41.56 C ANISOU 233 CD2 PHE A 45 4657 6135 4997 911 327 -1077 C ATOM 234 CE1 PHE A 45 -143.086 -85.605 647.802 1.00 43.99 C ANISOU 234 CE1 PHE A 45 4974 6425 5314 916 116 -987 C ATOM 235 CE2 PHE A 45 -144.703 -84.956 649.435 1.00 41.87 C ANISOU 235 CE2 PHE A 45 4739 6132 5039 996 222 -1111 C ATOM 236 CZ PHE A 45 -143.542 -84.702 648.743 1.00 43.59 C ANISOU 236 CZ PHE A 45 4965 6332 5265 992 114 -1062 C ATOM 237 N VAL A 46 -146.987 -89.412 650.498 1.00 30.67 N ANISOU 237 N VAL A 46 3369 4755 3530 705 698 -1014 N ATOM 238 CA VAL A 46 -147.485 -89.261 651.861 1.00 33.94 C ANISOU 238 CA VAL A 46 3862 5139 3896 732 784 -1049 C ATOM 239 C VAL A 46 -147.012 -90.408 652.758 1.00 35.27 C ANISOU 239 C VAL A 46 4166 5265 3971 690 887 -1000 C ATOM 240 O VAL A 46 -146.814 -90.214 653.952 1.00 40.00 O ANISOU 240 O VAL A 46 4869 5833 4496 723 923 -1018 O ATOM 241 CB VAL A 46 -149.039 -89.169 651.916 1.00 44.19 C ANISOU 241 CB VAL A 46 5077 6466 5248 722 862 -1094 C ATOM 242 CG1 VAL A 46 -149.559 -88.201 650.863 1.00 41.32 C ANISOU 242 CG1 VAL A 46 4575 6147 4978 761 759 -1134 C ATOM 243 CG2 VAL A 46 -149.688 -90.535 651.762 1.00 45.13 C ANISOU 243 CG2 VAL A 46 5188 6593 5365 636 980 -1055 C ATOM 244 N GLY A 47 -146.816 -91.593 652.183 1.00 29.02 N ANISOU 244 N GLY A 47 3379 4468 3179 623 931 -941 N ATOM 245 CA GLY A 47 -146.365 -92.738 652.951 1.00 26.58 C ANISOU 245 CA GLY A 47 3207 4109 2784 594 1028 -889 C ATOM 246 C GLY A 47 -144.942 -92.568 653.456 1.00 30.37 C ANISOU 246 C GLY A 47 3785 4567 3186 628 954 -874 C ATOM 247 O GLY A 47 -144.664 -92.754 654.646 1.00 29.47 O ANISOU 247 O GLY A 47 3791 4422 2984 639 1005 -878 O ATOM 248 N ASN A 48 -144.036 -92.207 652.550 1.00 30.67 N ANISOU 248 N ASN A 48 3767 4634 3251 646 825 -860 N ATOM 249 CA ASN A 48 -142.637 -92.030 652.906 1.00 27.23 C ANISOU 249 CA ASN A 48 3407 4196 2743 694 730 -839 C ATOM 250 C ASN A 48 -142.391 -90.738 653.683 1.00 30.01 C ANISOU 250 C ASN A 48 3788 4550 3063 775 647 -893 C ATOM 251 O ASN A 48 -141.511 -90.690 654.536 1.00 35.81 O ANISOU 251 O ASN A 48 4624 5271 3710 815 606 -885 O ATOM 252 CB ASN A 48 -141.757 -92.073 651.655 1.00 23.00 C ANISOU 252 CB ASN A 48 2801 3694 2244 691 627 -805 C ATOM 253 CG ASN A 48 -141.614 -93.478 651.096 1.00 25.94 C ANISOU 253 CG ASN A 48 3185 4052 2621 621 698 -748 C ATOM 254 OD1 ASN A 48 -140.936 -94.326 651.683 1.00 24.46 O ANISOU 254 OD1 ASN A 48 3103 3833 2359 621 732 -709 O ATOM 255 ND2 ASN A 48 -142.256 -93.734 649.958 1.00 26.69 N ANISOU 255 ND2 ASN A 48 3173 4167 2800 566 714 -745 N ATOM 256 N MET A 49 -143.153 -89.690 653.397 1.00 28.08 N ANISOU 256 N MET A 49 3458 4321 2890 803 616 -951 N ATOM 257 CA MET A 49 -143.053 -88.482 654.206 1.00 35.15 C ANISOU 257 CA MET A 49 4392 5203 3762 878 552 -1013 C ATOM 258 C MET A 49 -143.434 -88.802 655.644 1.00 33.09 C ANISOU 258 C MET A 49 4239 4915 3418 875 656 -1027 C ATOM 259 O MET A 49 -142.778 -88.362 656.587 1.00 33.79 O ANISOU 259 O MET A 49 4420 4990 3430 922 606 -1047 O ATOM 260 CB MET A 49 -143.939 -87.364 653.653 1.00 40.69 C ANISOU 260 CB MET A 49 4984 5916 4562 913 512 -1074 C ATOM 261 CG MET A 49 -143.346 -86.665 652.437 1.00 39.92 C ANISOU 261 CG MET A 49 4803 5833 4530 943 379 -1075 C ATOM 262 SD MET A 49 -141.706 -86.006 652.777 1.00 52.76 S ANISOU 262 SD MET A 49 6519 7433 6095 1002 239 -1084 S ATOM 263 CE MET A 49 -141.184 -85.501 651.143 1.00 72.68 C ANISOU 263 CE MET A 49 8937 9958 8721 983 115 -1041 C ATOM 264 N LEU A 50 -144.491 -89.590 655.801 1.00 32.06 N ANISOU 264 N LEU A 50 4101 4780 3300 815 801 -1019 N ATOM 265 CA LEU A 50 -144.928 -90.035 657.117 1.00 33.68 C ANISOU 265 CA LEU A 50 4410 4962 3423 797 924 -1033 C ATOM 266 C LEU A 50 -143.824 -90.820 657.820 1.00 38.20 C ANISOU 266 C LEU A 50 5108 5524 3884 788 916 -985 C ATOM 267 O LEU A 50 -143.499 -90.549 658.975 1.00 43.32 O ANISOU 267 O LEU A 50 5848 6170 4441 823 907 -1007 O ATOM 268 CB LEU A 50 -146.185 -90.898 657.003 1.00 36.66 C ANISOU 268 CB LEU A 50 4762 5331 3837 730 1087 -1021 C ATOM 269 CG LEU A 50 -147.478 -90.350 657.603 1.00 41.05 C ANISOU 269 CG LEU A 50 5293 5894 4411 754 1173 -1078 C ATOM 270 CD1 LEU A 50 -147.836 -89.028 656.950 1.00 44.51 C ANISOU 270 CD1 LEU A 50 5603 6365 4942 814 1060 -1137 C ATOM 271 CD2 LEU A 50 -148.592 -91.358 657.426 1.00 38.71 C ANISOU 271 CD2 LEU A 50 4976 5602 4131 714 1316 -1038 C ATOM 272 N VAL A 51 -143.261 -91.800 657.117 1.00 34.39 N ANISOU 272 N VAL A 51 4623 5038 3406 747 914 -920 N ATOM 273 CA VAL A 51 -142.176 -92.611 657.653 1.00 31.64 C ANISOU 273 CA VAL A 51 4381 4684 2956 753 890 -864 C ATOM 274 C VAL A 51 -141.026 -91.732 658.119 1.00 32.83 C ANISOU 274 C VAL A 51 4583 4844 3046 846 740 -868 C ATOM 275 O VAL A 51 -140.503 -91.912 659.219 1.00 33.77 O ANISOU 275 O VAL A 51 4811 4960 3058 879 730 -856 O ATOM 276 CB VAL A 51 -141.645 -93.620 656.612 1.00 28.54 C ANISOU 276 CB VAL A 51 3961 4287 2595 713 883 -798 C ATOM 277 CG1 VAL A 51 -140.285 -94.142 657.030 1.00 22.92 C ANISOU 277 CG1 VAL A 51 3350 3572 1789 762 807 -736 C ATOM 278 CG2 VAL A 51 -142.630 -94.764 656.422 1.00 26.13 C ANISOU 278 CG2 VAL A 51 3638 3969 2322 609 1041 -798 C ATOM 279 N ILE A 52 -140.644 -90.768 657.286 1.00 31.75 N ANISOU 279 N ILE A 52 4364 4721 2976 885 619 -891 N ATOM 280 CA ILE A 52 -139.550 -89.870 657.632 1.00 35.06 C ANISOU 280 CA ILE A 52 4821 5147 3352 959 471 -913 C ATOM 281 C ILE A 52 -139.906 -89.021 658.850 1.00 39.68 C ANISOU 281 C ILE A 52 5466 5722 3888 999 474 -980 C ATOM 282 O ILE A 52 -139.072 -88.823 659.730 1.00 44.59 O ANISOU 282 O ILE A 52 6176 6345 4422 1045 406 -984 O ATOM 283 CB ILE A 52 -139.168 -88.964 656.443 1.00 31.34 C ANISOU 283 CB ILE A 52 4245 4693 2972 980 350 -939 C ATOM 284 CG1 ILE A 52 -138.536 -89.805 655.330 1.00 31.54 C ANISOU 284 CG1 ILE A 52 4223 4740 3023 947 331 -872 C ATOM 285 CG2 ILE A 52 -138.201 -87.888 656.877 1.00 27.60 C ANISOU 285 CG2 ILE A 52 3808 4213 2464 1043 206 -986 C ATOM 286 CD1 ILE A 52 -138.043 -89.001 654.153 1.00 29.82 C ANISOU 286 CD1 ILE A 52 3905 4547 2879 961 214 -895 C ATOM 287 N LEU A 53 -141.150 -88.550 658.918 1.00 38.81 N ANISOU 287 N LEU A 53 5305 5605 3834 984 555 -1035 N ATOM 288 CA LEU A 53 -141.598 -87.741 660.049 1.00 40.12 C ANISOU 288 CA LEU A 53 5521 5763 3959 1021 571 -1107 C ATOM 289 C LEU A 53 -141.600 -88.532 661.353 1.00 38.14 C ANISOU 289 C LEU A 53 5389 5517 3583 1005 662 -1087 C ATOM 290 O LEU A 53 -141.239 -88.015 662.409 1.00 39.68 O ANISOU 290 O LEU A 53 5664 5715 3698 1051 621 -1124 O ATOM 291 CB LEU A 53 -142.991 -87.174 659.783 1.00 44.95 C ANISOU 291 CB LEU A 53 6045 6371 4663 1011 648 -1167 C ATOM 292 CG LEU A 53 -143.047 -85.708 659.341 1.00 50.04 C ANISOU 292 CG LEU A 53 6622 7002 5390 1074 533 -1238 C ATOM 293 CD1 LEU A 53 -142.008 -85.406 658.262 1.00 48.64 C ANISOU 293 CD1 LEU A 53 6399 6823 5260 1091 389 -1212 C ATOM 294 CD2 LEU A 53 -144.448 -85.355 658.854 1.00 52.70 C ANISOU 294 CD2 LEU A 53 6852 7344 5829 1068 607 -1278 C ATOM 295 N ILE A 54 -142.007 -89.790 661.275 1.00 37.36 N ANISOU 295 N ILE A 54 5304 5422 3470 938 783 -1033 N ATOM 296 CA ILE A 54 -142.019 -90.652 662.448 1.00 38.97 C ANISOU 296 CA ILE A 54 5617 5635 3553 919 870 -1008 C ATOM 297 C ILE A 54 -140.603 -91.038 662.897 1.00 41.63 C ANISOU 297 C ILE A 54 6056 5975 3786 975 764 -944 C ATOM 298 O ILE A 54 -140.312 -91.050 664.091 1.00 41.66 O ANISOU 298 O ILE A 54 6162 5991 3676 1011 761 -947 O ATOM 299 CB ILE A 54 -142.849 -91.923 662.185 1.00 38.29 C ANISOU 299 CB ILE A 54 5509 5555 3486 825 1024 -976 C ATOM 300 CG1 ILE A 54 -144.325 -91.552 662.045 1.00 40.75 C ANISOU 300 CG1 ILE A 54 5731 5871 3881 771 1144 -1054 C ATOM 301 CG2 ILE A 54 -142.676 -92.928 663.312 1.00 37.93 C ANISOU 301 CG2 ILE A 54 5579 5527 3305 817 1090 -932 C ATOM 302 CD1 ILE A 54 -145.243 -92.737 661.945 1.00 42.45 C ANISOU 302 CD1 ILE A 54 5904 6116 4108 665 1295 -1055 C ATOM 303 N LEU A 55 -139.719 -91.339 661.950 1.00 40.90 N ANISOU 303 N LEU A 55 5933 5874 3732 985 677 -888 N ATOM 304 CA LEU A 55 -138.356 -91.729 662.307 1.00 39.72 C ANISOU 304 CA LEU A 55 5868 5730 3494 1044 573 -830 C ATOM 305 C LEU A 55 -137.592 -90.578 662.951 1.00 42.66 C ANISOU 305 C LEU A 55 6270 6117 3822 1116 436 -886 C ATOM 306 O LEU A 55 -136.827 -90.792 663.886 1.00 44.19 O ANISOU 306 O LEU A 55 6559 6323 3907 1166 386 -865 O ATOM 307 CB LEU A 55 -137.590 -92.244 661.086 1.00 33.20 C ANISOU 307 CB LEU A 55 4987 4900 2727 1038 510 -772 C ATOM 308 CG LEU A 55 -138.002 -93.631 660.574 1.00 32.80 C ANISOU 308 CG LEU A 55 4938 4829 2696 975 628 -704 C ATOM 309 CD1 LEU A 55 -137.168 -94.031 659.383 1.00 33.13 C ANISOU 309 CD1 LEU A 55 4925 4872 2792 978 557 -656 C ATOM 310 CD2 LEU A 55 -137.901 -94.685 661.665 1.00 35.19 C ANISOU 310 CD2 LEU A 55 5374 5118 2880 989 699 -647 C ATOM 311 N ILE A 56 -137.802 -89.360 662.463 1.00 43.34 N ANISOU 311 N ILE A 56 6274 6201 3994 1123 373 -960 N ATOM 312 CA ILE A 56 -137.099 -88.197 663.004 1.00 43.25 C ANISOU 312 CA ILE A 56 6283 6195 3955 1180 240 -1028 C ATOM 313 C ILE A 56 -137.700 -87.679 664.308 1.00 46.75 C ANISOU 313 C ILE A 56 6795 6640 4327 1199 291 -1093 C ATOM 314 O ILE A 56 -136.977 -87.410 665.268 1.00 50.56 O ANISOU 314 O ILE A 56 7355 7139 4717 1245 217 -1113 O ATOM 315 CB ILE A 56 -137.073 -87.032 662.000 1.00 37.92 C ANISOU 315 CB ILE A 56 5503 5505 3399 1182 147 -1089 C ATOM 316 CG1 ILE A 56 -136.264 -87.408 660.768 1.00 32.66 C ANISOU 316 CG1 ILE A 56 4772 4850 2789 1168 73 -1035 C ATOM 317 CG2 ILE A 56 -136.485 -85.788 662.641 1.00 39.79 C ANISOU 317 CG2 ILE A 56 5767 5733 3617 1227 23 -1173 C ATOM 318 CD1 ILE A 56 -136.274 -86.333 659.713 1.00 32.01 C ANISOU 318 CD1 ILE A 56 4590 4753 2821 1164 -13 -1091 C ATOM 319 N ASN A 57 -139.019 -87.543 664.347 1.00 45.57 N ANISOU 319 N ASN A 57 6613 6482 4221 1164 416 -1130 N ATOM 320 CA ASN A 57 -139.657 -86.852 665.461 1.00 48.72 C ANISOU 320 CA ASN A 57 7056 6884 4570 1183 462 -1210 C ATOM 321 C ASN A 57 -140.255 -87.755 666.554 1.00 49.05 C ANISOU 321 C ASN A 57 7185 6950 4500 1157 605 -1187 C ATOM 322 O ASN A 57 -140.458 -87.301 667.674 1.00 52.04 O ANISOU 322 O ASN A 57 7628 7346 4799 1182 624 -1245 O ATOM 323 CB ASN A 57 -140.745 -85.917 664.919 1.00 48.73 C ANISOU 323 CB ASN A 57 6961 6862 4691 1174 500 -1287 C ATOM 324 N TYR A 58 -140.531 -89.021 666.244 1.00 49.57 N ANISOU 324 N TYR A 58 7256 7020 4559 1104 705 -1108 N ATOM 325 CA TYR A 58 -141.209 -89.906 667.204 1.00 53.93 C ANISOU 325 CA TYR A 58 7881 7596 5014 1067 852 -1090 C ATOM 326 C TYR A 58 -140.346 -91.089 667.678 1.00 56.36 C ANISOU 326 C TYR A 58 8299 7910 5205 1087 838 -987 C ATOM 327 O TYR A 58 -140.436 -91.489 668.835 1.00 61.49 O ANISOU 327 O TYR A 58 9050 8584 5728 1101 894 -975 O ATOM 328 CB TYR A 58 -142.519 -90.449 666.610 1.00 58.34 C ANISOU 328 CB TYR A 58 8352 8155 5658 977 1009 -1099 C ATOM 329 CG TYR A 58 -143.651 -89.438 666.441 1.00 61.33 C ANISOU 329 CG TYR A 58 8640 8532 6133 961 1065 -1203 C ATOM 330 CD1 TYR A 58 -143.455 -88.240 665.767 1.00 61.81 C ANISOU 330 CD1 TYR A 58 8633 8562 6289 1011 952 -1248 C ATOM 331 CD2 TYR A 58 -144.930 -89.709 666.917 1.00 64.50 C ANISOU 331 CD2 TYR A 58 9015 8962 6530 899 1229 -1255 C ATOM 332 CE1 TYR A 58 -144.487 -87.330 665.597 1.00 63.86 C ANISOU 332 CE1 TYR A 58 8817 8810 6638 1017 997 -1331 C ATOM 333 CE2 TYR A 58 -145.970 -88.802 666.749 1.00 64.79 C ANISOU 333 CE2 TYR A 58 8974 8985 6659 896 1285 -1345 C ATOM 334 CZ TYR A 58 -145.741 -87.614 666.087 1.00 63.55 C ANISOU 334 CZ TYR A 58 8763 8787 6595 965 1165 -1375 C ATOM 335 OH TYR A 58 -146.760 -86.703 665.911 1.00 63.65 O ANISOU 335 OH TYR A 58 8703 8782 6698 989 1207 -1451 O ATOM 336 N LYS A 59 -139.538 -91.661 666.788 1.00 53.69 N ANISOU 336 N LYS A 59 7943 7549 4906 1094 768 -911 N ATOM 337 CA LYS A 59 -138.574 -92.701 667.163 1.00 52.15 C ANISOU 337 CA LYS A 59 7853 7349 4611 1136 733 -813 C ATOM 338 C LYS A 59 -137.209 -92.074 667.422 1.00 52.05 C ANISOU 338 C LYS A 59 7873 7351 4554 1225 553 -820 C ATOM 339 O LYS A 59 -136.406 -92.605 668.180 1.00 59.97 O ANISOU 339 O LYS A 59 8979 8364 5444 1285 506 -769 O ATOM 340 CB LYS A 59 -138.464 -93.770 666.071 1.00 53.57 C ANISOU 340 CB LYS A 59 7996 7498 4859 1096 766 -732 C ATOM 341 CG LYS A 59 -139.492 -94.881 666.171 1.00 56.22 C ANISOU 341 CG LYS A 59 8353 7823 5186 1021 940 -694 C ATOM 342 CD LYS A 59 -139.294 -95.945 665.099 1.00 58.80 C ANISOU 342 CD LYS A 59 8652 8112 5579 986 963 -618 C ATOM 343 CE LYS A 59 -137.897 -96.529 665.143 1.00 61.65 C ANISOU 343 CE LYS A 59 9102 8448 5875 1070 856 -533 C ATOM 344 NZ LYS A 59 -137.511 -96.974 666.516 1.00 66.11 N ANISOU 344 NZ LYS A 59 9822 9011 6284 1138 861 -487 N ATOM 345 N ARG A 60 -136.960 -90.960 666.739 1.00 49.14 N ANISOU 345 N ARG A 60 7410 6982 4279 1231 451 -886 N ATOM 346 CA ARG A 60 -135.858 -90.027 667.012 1.00 49.73 C ANISOU 346 CA ARG A 60 7488 7076 4332 1296 281 -933 C ATOM 347 C ARG A 60 -134.458 -90.460 666.538 1.00 52.42 C ANISOU 347 C ARG A 60 7824 7425 4667 1339 151 -873 C ATOM 348 O ARG A 60 -133.488 -89.745 666.792 1.00 60.49 O ANISOU 348 O ARG A 60 8839 8471 5672 1384 9 -917 O ATOM 349 CB ARG A 60 -135.808 -89.703 668.516 1.00 51.18 C ANISOU 349 CB ARG A 60 7774 7288 4384 1340 276 -975 C ATOM 350 N LEU A 61 -134.352 -91.591 665.841 1.00 45.14 N ANISOU 350 N LEU A 61 6898 6487 3768 1322 199 -785 N ATOM 351 CA LEU A 61 -133.074 -92.050 665.267 1.00 43.36 C ANISOU 351 CA LEU A 61 6653 6272 3551 1363 86 -732 C ATOM 352 C LEU A 61 -132.014 -92.327 666.329 1.00 47.49 C ANISOU 352 C LEU A 61 7270 6823 3952 1448 -4 -710 C ATOM 353 O LEU A 61 -131.134 -91.502 666.580 1.00 51.77 O ANISOU 353 O LEU A 61 7783 7399 4488 1484 -143 -767 O ATOM 354 CB LEU A 61 -132.508 -91.034 664.266 1.00 37.33 C ANISOU 354 CB LEU A 61 5766 5521 2895 1349 -39 -789 C ATOM 355 CG LEU A 61 -133.274 -90.601 663.016 1.00 35.34 C ANISOU 355 CG LEU A 61 5404 5250 2774 1282 4 -815 C ATOM 356 CD1 LEU A 61 -132.353 -89.766 662.147 1.00 26.12 C ANISOU 356 CD1 LEU A 61 4138 4101 1684 1283 -144 -855 C ATOM 357 CD2 LEU A 61 -133.812 -91.799 662.239 1.00 33.65 C ANISOU 357 CD2 LEU A 61 5176 5013 2596 1238 123 -737 C ATOM 358 N LYS A 62 -132.079 -93.501 666.938 1.00 46.40 N ANISOU 358 N LYS A 62 7240 6669 3720 1479 73 -630 N ATOM 359 CA LYS A 62 -131.199 -93.798 668.053 1.00 46.31 C ANISOU 359 CA LYS A 62 7329 6685 3582 1569 -2 -608 C ATOM 360 C LYS A 62 -130.307 -94.993 667.752 1.00 43.28 C ANISOU 360 C LYS A 62 6981 6288 3176 1630 -34 -514 C ATOM 361 O LYS A 62 -129.477 -95.383 668.577 1.00 40.96 O ANISOU 361 O LYS A 62 6766 6015 2781 1718 -102 -487 O ATOM 362 CB LYS A 62 -132.024 -94.051 669.316 1.00 47.87 C ANISOU 362 CB LYS A 62 7650 6878 3660 1573 109 -600 C ATOM 363 N SER A 63 -130.477 -95.567 666.565 1.00 39.86 N ANISOU 363 N SER A 63 6488 5821 2836 1587 15 -471 N ATOM 364 CA SER A 63 -129.768 -96.787 666.212 1.00 40.40 C ANISOU 364 CA SER A 63 6596 5865 2889 1643 7 -384 C ATOM 365 C SER A 63 -129.378 -96.806 664.745 1.00 40.59 C ANISOU 365 C SER A 63 6492 5893 3038 1608 -34 -384 C ATOM 366 O SER A 63 -129.829 -95.976 663.955 1.00 39.53 O ANISOU 366 O SER A 63 6248 5770 3002 1531 -34 -441 O ATOM 367 CB SER A 63 -130.623 -98.011 666.532 1.00 43.16 C ANISOU 367 CB SER A 63 7068 6147 3184 1628 171 -299 C ATOM 368 OG SER A 63 -131.792 -98.024 665.729 1.00 46.71 O ANISOU 368 OG SER A 63 7457 6564 3727 1515 298 -309 O ATOM 369 N MET A 64 -128.541 -97.770 664.385 1.00 41.79 N ANISOU 369 N MET A 64 6662 6034 3181 1671 -68 -322 N ATOM 370 CA MET A 64 -128.101 -97.917 663.009 1.00 40.78 C ANISOU 370 CA MET A 64 6419 5916 3160 1645 -102 -319 C ATOM 371 C MET A 64 -129.271 -98.301 662.110 1.00 41.59 C ANISOU 371 C MET A 64 6497 5967 3337 1546 43 -298 C ATOM 372 O MET A 64 -129.268 -98.011 660.919 1.00 43.95 O ANISOU 372 O MET A 64 6677 6284 3737 1490 27 -322 O ATOM 373 CB MET A 64 -126.988 -98.958 662.919 1.00 41.54 C ANISOU 373 CB MET A 64 6551 6011 3222 1745 -158 -261 C ATOM 374 CG MET A 64 -126.000 -98.705 661.800 1.00 43.19 C ANISOU 374 CG MET A 64 6613 6275 3524 1744 -266 -291 C ATOM 375 SD MET A 64 -124.489 -99.680 661.946 1.00 66.71 S ANISOU 375 SD MET A 64 9613 9275 6457 1881 -362 -252 S ATOM 376 CE MET A 64 -125.002-101.259 661.279 1.00 28.87 C ANISOU 376 CE MET A 64 4915 4393 1662 1898 -222 -155 C ATOM 377 N THR A 65 -130.282 -98.937 662.690 1.00 40.86 N ANISOU 377 N THR A 65 6512 5816 3196 1517 186 -258 N ATOM 378 CA THR A 65 -131.435 -99.398 661.924 1.00 36.49 C ANISOU 378 CA THR A 65 5933 5215 2719 1412 334 -243 C ATOM 379 C THR A 65 -132.320 -98.234 661.498 1.00 34.82 C ANISOU 379 C THR A 65 5604 5032 2592 1318 354 -325 C ATOM 380 O THR A 65 -132.756 -98.154 660.347 1.00 33.69 O ANISOU 380 O THR A 65 5356 4888 2555 1244 389 -343 O ATOM 381 CB THR A 65 -132.267-100.397 662.736 1.00 35.01 C ANISOU 381 CB THR A 65 5887 4959 2458 1398 485 -184 C ATOM 382 OG1 THR A 65 -131.430-101.485 663.135 1.00 37.29 O ANISOU 382 OG1 THR A 65 6298 5206 2663 1501 464 -103 O ATOM 383 CG2 THR A 65 -133.431-100.929 661.917 1.00 34.34 C ANISOU 383 CG2 THR A 65 5757 4827 2463 1279 637 -180 C ATOM 384 N ASP A 66 -132.587 -97.335 662.436 1.00 32.20 N ANISOU 384 N ASP A 66 5295 4727 2214 1327 330 -377 N ATOM 385 CA ASP A 66 -133.369 -96.146 662.143 1.00 36.97 C ANISOU 385 CA ASP A 66 5801 5355 2892 1259 338 -461 C ATOM 386 C ASP A 66 -132.701 -95.320 661.049 1.00 34.66 C ANISOU 386 C ASP A 66 5377 5099 2692 1256 215 -503 C ATOM 387 O ASP A 66 -133.370 -94.687 660.239 1.00 34.39 O ANISOU 387 O ASP A 66 5243 5069 2754 1192 239 -548 O ATOM 388 CB ASP A 66 -133.554 -95.294 663.404 1.00 46.17 C ANISOU 388 CB ASP A 66 7020 6542 3979 1289 314 -515 C ATOM 389 CG ASP A 66 -134.281 -96.038 664.514 1.00 55.42 C ANISOU 389 CG ASP A 66 8318 7687 5051 1286 442 -478 C ATOM 390 OD1 ASP A 66 -135.006 -97.007 664.202 1.00 57.39 O ANISOU 390 OD1 ASP A 66 8587 7896 5323 1229 574 -430 O ATOM 391 OD2 ASP A 66 -134.127 -95.653 665.697 1.00 60.14 O ANISOU 391 OD2 ASP A 66 8993 8307 5549 1335 411 -500 O ATOM 392 N ILE A 67 -131.374 -95.326 661.036 1.00 33.80 N ANISOU 392 N ILE A 67 5266 5023 2555 1327 82 -490 N ATOM 393 CA ILE A 67 -130.626 -94.561 660.052 1.00 29.30 C ANISOU 393 CA ILE A 67 4570 4495 2066 1318 -40 -531 C ATOM 394 C ILE A 67 -130.836 -95.134 658.658 1.00 31.75 C ANISOU 394 C ILE A 67 4800 4799 2465 1265 12 -500 C ATOM 395 O ILE A 67 -131.059 -94.395 657.692 1.00 33.37 O ANISOU 395 O ILE A 67 4894 5025 2760 1213 -13 -543 O ATOM 396 CB ILE A 67 -129.133 -94.543 660.378 1.00 26.61 C ANISOU 396 CB ILE A 67 4231 4198 1682 1396 -186 -529 C ATOM 397 CG1 ILE A 67 -128.902 -93.783 661.682 1.00 32.35 C ANISOU 397 CG1 ILE A 67 5016 4942 2334 1438 -252 -579 C ATOM 398 CG2 ILE A 67 -128.350 -93.893 659.258 1.00 24.04 C ANISOU 398 CG2 ILE A 67 3766 3919 1451 1367 -297 -565 C ATOM 399 CD1 ILE A 67 -129.408 -92.371 661.638 1.00 34.11 C ANISOU 399 CD1 ILE A 67 5179 5171 2610 1388 -282 -668 C ATOM 400 N TYR A 68 -130.772 -96.456 658.556 1.00 26.93 N ANISOU 400 N TYR A 68 4251 4156 1827 1281 86 -427 N ATOM 401 CA TYR A 68 -130.942 -97.105 657.272 1.00 28.36 C ANISOU 401 CA TYR A 68 4362 4327 2087 1231 140 -400 C ATOM 402 C TYR A 68 -132.387 -97.023 656.801 1.00 33.39 C ANISOU 402 C TYR A 68 4956 4932 2797 1131 272 -420 C ATOM 403 O TYR A 68 -132.649 -96.918 655.599 1.00 31.73 O ANISOU 403 O TYR A 68 4638 4738 2680 1072 285 -435 O ATOM 404 CB TYR A 68 -130.487 -98.554 657.351 1.00 30.16 C ANISOU 404 CB TYR A 68 4678 4516 2264 1280 185 -323 C ATOM 405 CG TYR A 68 -129.000 -98.692 657.566 1.00 28.86 C ANISOU 405 CG TYR A 68 4523 4393 2047 1385 48 -307 C ATOM 406 CD1 TYR A 68 -128.119 -97.734 657.084 1.00 28.23 C ANISOU 406 CD1 TYR A 68 4325 4389 2012 1390 -93 -360 C ATOM 407 CD2 TYR A 68 -128.477 -99.777 658.255 1.00 28.29 C ANISOU 407 CD2 TYR A 68 4574 4285 1889 1475 59 -244 C ATOM 408 CE1 TYR A 68 -126.763 -97.856 657.277 1.00 23.39 C ANISOU 408 CE1 TYR A 68 3698 3821 1369 1472 -216 -356 C ATOM 409 CE2 TYR A 68 -127.122 -99.906 658.455 1.00 29.08 C ANISOU 409 CE2 TYR A 68 4668 4429 1950 1576 -69 -238 C ATOM 410 CZ TYR A 68 -126.269 -98.944 657.962 1.00 31.15 C ANISOU 410 CZ TYR A 68 4793 4774 2269 1569 -205 -298 C ATOM 411 OH TYR A 68 -124.913 -99.080 658.156 1.00 36.81 O ANISOU 411 OH TYR A 68 5481 5539 2966 1655 -326 -302 O ATOM 412 N LEU A 69 -133.325 -97.064 657.741 1.00 22.84 N ANISOU 412 N LEU A 69 3696 3562 1421 1109 366 -426 N ATOM 413 CA LEU A 69 -134.735 -96.954 657.391 1.00 27.60 C ANISOU 413 CA LEU A 69 4245 4144 2096 1013 490 -458 C ATOM 414 C LEU A 69 -135.021 -95.557 656.875 1.00 29.16 C ANISOU 414 C LEU A 69 4329 4382 2368 994 424 -531 C ATOM 415 O LEU A 69 -135.786 -95.379 655.928 1.00 21.23 O ANISOU 415 O LEU A 69 3225 3382 1461 928 472 -556 O ATOM 416 CB LEU A 69 -135.625 -97.285 658.587 1.00 26.20 C ANISOU 416 CB LEU A 69 4167 3935 1852 995 603 -455 C ATOM 417 CG LEU A 69 -135.799 -98.785 658.816 1.00 27.85 C ANISOU 417 CG LEU A 69 4472 4090 2019 979 714 -384 C ATOM 418 CD1 LEU A 69 -136.339 -99.066 660.195 1.00 25.91 C ANISOU 418 CD1 LEU A 69 4348 3824 1675 988 796 -370 C ATOM 419 CD2 LEU A 69 -136.723 -99.362 657.761 1.00 23.87 C ANISOU 419 CD2 LEU A 69 3883 3569 1620 872 823 -394 C ATOM 420 N LEU A 70 -134.379 -94.573 657.494 1.00 22.22 N ANISOU 420 N LEU A 70 3466 3531 1446 1055 309 -569 N ATOM 421 CA LEU A 70 -134.466 -93.203 657.035 1.00 21.72 C ANISOU 421 CA LEU A 70 3309 3498 1447 1051 226 -640 C ATOM 422 C LEU A 70 -133.964 -93.088 655.603 1.00 27.09 C ANISOU 422 C LEU A 70 3873 4210 2207 1030 162 -636 C ATOM 423 O LEU A 70 -134.684 -92.622 654.719 1.00 23.13 O ANISOU 423 O LEU A 70 3277 3718 1795 984 186 -666 O ATOM 424 CB LEU A 70 -133.666 -92.279 657.948 1.00 28.61 C ANISOU 424 CB LEU A 70 4225 4389 2256 1116 103 -684 C ATOM 425 CG LEU A 70 -133.720 -90.792 657.578 1.00 26.57 C ANISOU 425 CG LEU A 70 3887 4146 2062 1112 11 -767 C ATOM 426 CD1 LEU A 70 -135.148 -90.287 657.587 1.00 22.20 C ANISOU 426 CD1 LEU A 70 3304 3567 1563 1078 109 -813 C ATOM 427 CD2 LEU A 70 -132.870 -89.982 658.530 1.00 28.06 C ANISOU 427 CD2 LEU A 70 4125 4346 2191 1164 -110 -814 C ATOM 428 N ASN A 71 -132.731 -93.521 655.373 1.00 20.42 N ANISOU 428 N ASN A 71 3035 3392 1331 1066 78 -601 N ATOM 429 CA ASN A 71 -132.147 -93.442 654.042 1.00 19.47 C ANISOU 429 CA ASN A 71 2805 3317 1277 1043 15 -599 C ATOM 430 C ASN A 71 -132.950 -94.220 653.005 1.00 18.82 C ANISOU 430 C ASN A 71 2663 3222 1265 977 128 -568 C ATOM 431 O ASN A 71 -133.004 -93.838 651.839 1.00 18.36 O ANISOU 431 O ASN A 71 2488 3192 1296 928 99 -577 O ATOM 432 CB ASN A 71 -130.703 -93.936 654.066 1.00 19.60 C ANISOU 432 CB ASN A 71 2836 3366 1244 1092 -81 -564 C ATOM 433 CG ASN A 71 -129.747 -92.885 654.571 1.00 26.28 C ANISOU 433 CG ASN A 71 3669 4245 2069 1124 -232 -611 C ATOM 434 OD1 ASN A 71 -129.395 -91.954 653.848 1.00 28.19 O ANISOU 434 OD1 ASN A 71 3810 4512 2390 1077 -322 -642 O ATOM 435 ND2 ASN A 71 -129.323 -93.021 655.820 1.00 25.63 N ANISOU 435 ND2 ASN A 71 3682 4149 1906 1185 -260 -606 N ATOM 436 N LEU A 72 -133.590 -95.299 653.437 1.00 20.08 N ANISOU 436 N LEU A 72 2899 3329 1403 957 253 -526 N ATOM 437 CA LEU A 72 -134.372 -96.121 652.531 1.00 20.69 C ANISOU 437 CA LEU A 72 2925 3386 1552 881 363 -505 C ATOM 438 C LEU A 72 -135.625 -95.370 652.084 1.00 18.54 C ANISOU 438 C LEU A 72 2563 3119 1362 820 410 -556 C ATOM 439 O LEU A 72 -136.065 -95.491 650.947 1.00 27.50 O ANISOU 439 O LEU A 72 3597 4272 2580 762 435 -560 O ATOM 440 CB LEU A 72 -134.741 -97.446 653.194 1.00 19.53 C ANISOU 440 CB LEU A 72 2891 3172 1356 867 485 -459 C ATOM 441 CG LEU A 72 -135.624 -98.369 652.362 1.00 24.28 C ANISOU 441 CG LEU A 72 3450 3744 2032 773 608 -451 C ATOM 442 CD1 LEU A 72 -134.966 -98.664 651.011 1.00 23.89 C ANISOU 442 CD1 LEU A 72 3309 3728 2041 761 558 -437 C ATOM 443 CD2 LEU A 72 -135.916 -99.644 653.122 1.00 20.22 C ANISOU 443 CD2 LEU A 72 3058 3164 1461 761 721 -412 C ATOM 444 N ALA A 73 -136.187 -94.577 652.984 1.00 21.68 N ANISOU 444 N ALA A 73 2995 3505 1737 839 415 -597 N ATOM 445 CA ALA A 73 -137.356 -93.762 652.659 1.00 22.35 C ANISOU 445 CA ALA A 73 2996 3598 1900 802 449 -652 C ATOM 446 C ALA A 73 -136.952 -92.614 651.751 1.00 22.09 C ANISOU 446 C ALA A 73 2855 3616 1923 824 327 -689 C ATOM 447 O ALA A 73 -137.716 -92.176 650.894 1.00 23.88 O ANISOU 447 O ALA A 73 2976 3862 2234 790 337 -715 O ATOM 448 CB ALA A 73 -138.003 -93.229 653.923 1.00 23.67 C ANISOU 448 CB ALA A 73 3233 3739 2022 825 488 -692 C ATOM 449 N ILE A 74 -135.742 -92.118 651.960 1.00 22.57 N ANISOU 449 N ILE A 74 2943 3697 1934 880 207 -694 N ATOM 450 CA ILE A 74 -135.213 -91.056 651.132 1.00 25.68 C ANISOU 450 CA ILE A 74 3243 4097 2416 854 77 -695 C ATOM 451 C ILE A 74 -134.992 -91.603 649.735 1.00 24.76 C ANISOU 451 C ILE A 74 3029 4008 2370 792 75 -644 C ATOM 452 O ILE A 74 -135.286 -90.948 648.736 1.00 27.96 O ANISOU 452 O ILE A 74 3335 4422 2865 749 35 -644 O ATOM 453 CB ILE A 74 -133.919 -90.496 651.722 1.00 28.47 C ANISOU 453 CB ILE A 74 3643 4450 2724 892 -52 -699 C ATOM 454 CG1 ILE A 74 -134.258 -89.625 652.938 1.00 31.62 C ANISOU 454 CG1 ILE A 74 4118 4824 3073 945 -68 -768 C ATOM 455 CG2 ILE A 74 -133.156 -89.701 650.681 1.00 30.24 C ANISOU 455 CG2 ILE A 74 3768 4683 3040 843 -173 -681 C ATOM 456 CD1 ILE A 74 -133.065 -89.251 653.789 1.00 32.93 C ANISOU 456 CD1 ILE A 74 4350 4995 3166 990 -180 -787 C ATOM 457 N SER A 75 -134.509 -92.833 649.674 1.00 21.24 N ANISOU 457 N SER A 75 2620 3572 1877 793 122 -602 N ATOM 458 CA SER A 75 -134.335 -93.499 648.402 1.00 17.99 C ANISOU 458 CA SER A 75 2126 3188 1522 737 136 -564 C ATOM 459 C SER A 75 -135.636 -93.579 647.607 1.00 18.14 C ANISOU 459 C SER A 75 2064 3217 1611 681 219 -584 C ATOM 460 O SER A 75 -135.646 -93.319 646.402 1.00 18.98 O ANISOU 460 O SER A 75 2067 3354 1790 632 179 -570 O ATOM 461 CB SER A 75 -133.779 -94.896 648.610 1.00 21.74 C ANISOU 461 CB SER A 75 2672 3657 1933 758 194 -526 C ATOM 462 OG SER A 75 -133.829 -95.595 647.384 1.00 28.81 O ANISOU 462 OG SER A 75 3488 4574 2884 701 229 -504 O ATOM 463 N ASP A 76 -136.732 -93.932 648.273 1.00 21.16 N ANISOU 463 N ASP A 76 2490 3582 1968 688 336 -618 N ATOM 464 CA ASP A 76 -138.027 -94.003 647.597 1.00 24.84 C ANISOU 464 CA ASP A 76 2875 4046 2519 619 404 -634 C ATOM 465 C ASP A 76 -138.480 -92.624 647.116 1.00 24.23 C ANISOU 465 C ASP A 76 2699 4009 2499 639 331 -681 C ATOM 466 O ASP A 76 -139.112 -92.507 646.068 1.00 29.79 O ANISOU 466 O ASP A 76 3299 4745 3276 595 331 -685 O ATOM 467 CB ASP A 76 -139.089 -94.613 648.510 1.00 32.34 C ANISOU 467 CB ASP A 76 3899 4933 3458 591 531 -641 C ATOM 468 CG ASP A 76 -138.826 -96.082 648.822 1.00 43.70 C ANISOU 468 CG ASP A 76 5432 6317 4853 560 623 -597 C ATOM 469 OD1 ASP A 76 -138.182 -96.766 647.999 1.00 48.16 O ANISOU 469 OD1 ASP A 76 5974 6893 5431 540 605 -565 O ATOM 470 OD2 ASP A 76 -139.271 -96.557 649.892 1.00 49.09 O ANISOU 470 OD2 ASP A 76 6216 6948 5489 557 717 -598 O ATOM 471 N LEU A 77 -138.145 -91.576 647.860 1.00 20.66 N ANISOU 471 N LEU A 77 2292 3528 2030 691 253 -698 N ATOM 472 CA LEU A 77 -138.525 -90.224 647.448 1.00 25.04 C ANISOU 472 CA LEU A 77 2777 4077 2658 702 169 -722 C ATOM 473 C LEU A 77 -137.791 -89.730 646.188 1.00 25.49 C ANISOU 473 C LEU A 77 2759 4149 2777 664 57 -670 C ATOM 474 O LEU A 77 -138.387 -89.026 645.372 1.00 26.79 O ANISOU 474 O LEU A 77 2843 4324 3013 653 21 -673 O ATOM 475 CB LEU A 77 -138.303 -89.245 648.597 1.00 26.04 C ANISOU 475 CB LEU A 77 2982 4159 2751 764 116 -761 C ATOM 476 CG LEU A 77 -139.392 -89.338 649.663 1.00 29.14 C ANISOU 476 CG LEU A 77 3422 4546 3103 805 226 -828 C ATOM 477 CD1 LEU A 77 -139.096 -88.396 650.804 1.00 33.21 C ANISOU 477 CD1 LEU A 77 4021 5021 3576 868 170 -874 C ATOM 478 CD2 LEU A 77 -140.763 -89.044 649.062 1.00 25.86 C ANISOU 478 CD2 LEU A 77 2901 4158 2767 796 278 -870 C ATOM 479 N PHE A 78 -136.515 -90.086 646.026 1.00 20.01 N ANISOU 479 N PHE A 78 2090 3460 2054 646 3 -623 N ATOM 480 CA PHE A 78 -135.793 -89.761 644.785 1.00 22.71 C ANISOU 480 CA PHE A 78 2357 3827 2446 598 -83 -571 C ATOM 481 C PHE A 78 -136.528 -90.373 643.610 1.00 23.90 C ANISOU 481 C PHE A 78 2419 4029 2635 551 -27 -559 C ATOM 482 O PHE A 78 -136.760 -89.736 642.578 1.00 24.21 O ANISOU 482 O PHE A 78 2382 4088 2730 525 -80 -539 O ATOM 483 CB PHE A 78 -134.359 -90.287 644.798 1.00 24.89 C ANISOU 483 CB PHE A 78 2659 4118 2679 586 -126 -532 C ATOM 484 CG PHE A 78 -133.431 -89.534 645.708 1.00 31.11 C ANISOU 484 CG PHE A 78 3509 4873 3438 619 -214 -544 C ATOM 485 CD1 PHE A 78 -133.911 -88.792 646.762 1.00 33.95 C ANISOU 485 CD1 PHE A 78 3931 5186 3784 667 -222 -595 C ATOM 486 CD2 PHE A 78 -132.068 -89.564 645.493 1.00 35.00 C ANISOU 486 CD2 PHE A 78 3989 5389 3920 600 -291 -514 C ATOM 487 CE1 PHE A 78 -133.052 -88.108 647.588 1.00 34.35 C ANISOU 487 CE1 PHE A 78 4036 5210 3805 692 -307 -617 C ATOM 488 CE2 PHE A 78 -131.209 -88.881 646.319 1.00 30.51 C ANISOU 488 CE2 PHE A 78 3466 4799 3327 623 -376 -536 C ATOM 489 CZ PHE A 78 -131.700 -88.155 647.363 1.00 31.03 C ANISOU 489 CZ PHE A 78 3599 4815 3376 668 -387 -588 C ATOM 490 N PHE A 79 -136.884 -91.636 643.789 1.00 19.99 N ANISOU 490 N PHE A 79 1940 3550 2103 541 82 -572 N ATOM 491 CA PHE A 79 -137.687 -92.370 642.833 1.00 24.31 C ANISOU 491 CA PHE A 79 2409 4145 2681 493 152 -581 C ATOM 492 C PHE A 79 -139.042 -91.714 642.565 1.00 27.62 C ANISOU 492 C PHE A 79 2758 4583 3155 499 167 -625 C ATOM 493 O PHE A 79 -139.488 -91.621 641.426 1.00 29.75 O ANISOU 493 O PHE A 79 2933 4903 3469 466 147 -620 O ATOM 494 CB PHE A 79 -137.900 -93.782 643.356 1.00 28.85 C ANISOU 494 CB PHE A 79 3043 4709 3211 482 277 -596 C ATOM 495 CG PHE A 79 -138.028 -94.802 642.293 1.00 30.90 C ANISOU 495 CG PHE A 79 3269 4969 3502 403 308 -569 C ATOM 496 CD1 PHE A 79 -139.229 -94.990 641.645 1.00 33.47 C ANISOU 496 CD1 PHE A 79 3544 5290 3884 345 342 -585 C ATOM 497 CD2 PHE A 79 -136.945 -95.590 641.952 1.00 31.85 C ANISOU 497 CD2 PHE A 79 3412 5096 3595 394 300 -534 C ATOM 498 CE1 PHE A 79 -139.342 -95.945 640.662 1.00 38.09 C ANISOU 498 CE1 PHE A 79 4108 5871 4492 277 365 -570 C ATOM 499 CE2 PHE A 79 -137.049 -96.538 640.980 1.00 31.70 C ANISOU 499 CE2 PHE A 79 3370 5069 3605 327 329 -519 C ATOM 500 CZ PHE A 79 -138.245 -96.727 640.335 1.00 37.56 C ANISOU 500 CZ PHE A 79 4070 5801 4399 268 361 -538 C ATOM 501 N LEU A 80 -139.700 -91.267 643.627 1.00 27.88 N ANISOU 501 N LEU A 80 2833 4581 3180 546 200 -671 N ATOM 502 CA LEU A 80 -141.046 -90.717 643.517 1.00 24.90 C ANISOU 502 CA LEU A 80 2388 4220 2853 562 223 -723 C ATOM 503 C LEU A 80 -141.057 -89.390 642.797 1.00 25.05 C ANISOU 503 C LEU A 80 2348 4240 2931 591 102 -706 C ATOM 504 O LEU A 80 -141.995 -89.082 642.072 1.00 29.54 O ANISOU 504 O LEU A 80 2824 4851 3549 595 95 -728 O ATOM 505 CB LEU A 80 -141.676 -90.545 644.895 1.00 19.76 C ANISOU 505 CB LEU A 80 1811 3520 2177 602 287 -771 C ATOM 506 CG LEU A 80 -142.268 -91.820 645.466 1.00 20.27 C ANISOU 506 CG LEU A 80 1939 3544 2220 538 412 -760 C ATOM 507 CD1 LEU A 80 -142.178 -91.787 646.969 1.00 17.61 C ANISOU 507 CD1 LEU A 80 1715 3157 1819 582 463 -778 C ATOM 508 CD2 LEU A 80 -143.715 -91.957 645.021 1.00 26.41 C ANISOU 508 CD2 LEU A 80 2642 4332 3061 494 462 -786 C ATOM 509 N LEU A 81 -140.020 -88.596 643.010 1.00 22.17 N ANISOU 509 N LEU A 81 2041 3822 2558 608 4 -666 N ATOM 510 CA LEU A 81 -139.952 -87.286 642.377 1.00 29.21 C ANISOU 510 CA LEU A 81 2903 4689 3506 628 -111 -638 C ATOM 511 C LEU A 81 -139.954 -87.372 640.853 1.00 33.20 C ANISOU 511 C LEU A 81 3321 5253 4042 581 -152 -585 C ATOM 512 O LEU A 81 -140.332 -86.418 640.175 1.00 36.02 O ANISOU 512 O LEU A 81 3637 5603 4446 603 -226 -565 O ATOM 513 CB LEU A 81 -138.716 -86.527 642.856 1.00 29.36 C ANISOU 513 CB LEU A 81 3002 4640 3512 633 -201 -606 C ATOM 514 CG LEU A 81 -138.959 -85.594 644.048 1.00 33.47 C ANISOU 514 CG LEU A 81 3593 5088 4036 699 -222 -662 C ATOM 515 CD1 LEU A 81 -140.053 -86.105 644.997 1.00 32.50 C ANISOU 515 CD1 LEU A 81 3483 4982 3886 744 -108 -740 C ATOM 516 CD2 LEU A 81 -137.660 -85.358 644.809 1.00 32.84 C ANISOU 516 CD2 LEU A 81 3600 4962 3916 692 -278 -651 C ATOM 517 N THR A 82 -139.556 -88.523 640.320 1.00 29.75 N ANISOU 517 N THR A 82 2860 4871 3573 522 -104 -564 N ATOM 518 CA THR A 82 -139.437 -88.684 638.881 1.00 27.20 C ANISOU 518 CA THR A 82 2461 4611 3262 473 -140 -517 C ATOM 519 C THR A 82 -140.730 -89.236 638.299 1.00 28.23 C ANISOU 519 C THR A 82 2558 4762 3405 444 -77 -546 C ATOM 520 O THR A 82 -141.002 -89.094 637.108 1.00 26.41 O ANISOU 520 O THR A 82 2301 4547 3185 410 -113 -509 O ATOM 521 CB THR A 82 -138.272 -89.617 638.517 1.00 20.23 C ANISOU 521 CB THR A 82 1604 3746 2336 411 -123 -475 C ATOM 522 OG1 THR A 82 -138.628 -90.975 638.805 1.00 18.76 O ANISOU 522 OG1 THR A 82 1435 3574 2121 386 -13 -513 O ATOM 523 CG2 THR A 82 -137.033 -89.246 639.311 1.00 16.28 C ANISOU 523 CG2 THR A 82 1175 3197 1814 425 -172 -451 C ATOM 524 N VAL A 83 -141.537 -89.851 639.155 1.00 28.94 N ANISOU 524 N VAL A 83 2658 4846 3490 453 16 -611 N ATOM 525 CA VAL A 83 -142.739 -90.542 638.703 1.00 25.45 C ANISOU 525 CA VAL A 83 2189 4418 3063 407 75 -642 C ATOM 526 C VAL A 83 -143.733 -89.656 637.935 1.00 24.31 C ANISOU 526 C VAL A 83 1982 4296 2960 435 16 -648 C ATOM 527 O VAL A 83 -144.247 -90.091 636.903 1.00 27.24 O ANISOU 527 O VAL A 83 2321 4698 3332 389 15 -642 O ATOM 528 CB VAL A 83 -143.454 -91.216 639.886 1.00 24.61 C ANISOU 528 CB VAL A 83 2118 4280 2951 403 183 -698 C ATOM 529 CG1 VAL A 83 -144.669 -92.001 639.406 1.00 20.11 C ANISOU 529 CG1 VAL A 83 1514 3722 2406 343 240 -729 C ATOM 530 CG2 VAL A 83 -142.494 -92.148 640.579 1.00 26.81 C ANISOU 530 CG2 VAL A 83 2478 4526 3184 381 241 -679 C ATOM 531 N PRO A 84 -144.001 -88.422 638.404 1.00 24.54 N ANISOU 531 N PRO A 84 1997 4306 3022 519 -37 -663 N ATOM 532 CA PRO A 84 -144.946 -87.627 637.607 1.00 27.39 C ANISOU 532 CA PRO A 84 2302 4682 3421 554 -97 -661 C ATOM 533 C PRO A 84 -144.481 -87.404 636.166 1.00 30.06 C ANISOU 533 C PRO A 84 2632 5039 3752 522 -173 -581 C ATOM 534 O PRO A 84 -145.314 -87.364 635.257 1.00 32.77 O ANISOU 534 O PRO A 84 2931 5417 4104 518 -191 -581 O ATOM 535 CB PRO A 84 -145.016 -86.299 638.368 1.00 28.44 C ANISOU 535 CB PRO A 84 2443 4771 3593 658 -155 -680 C ATOM 536 CG PRO A 84 -144.674 -86.655 639.772 1.00 30.07 C ANISOU 536 CG PRO A 84 2696 4951 3777 672 -83 -731 C ATOM 537 CD PRO A 84 -143.626 -87.727 639.651 1.00 28.40 C ANISOU 537 CD PRO A 84 2521 4754 3516 594 -45 -692 C ATOM 538 N PHE A 85 -143.171 -87.293 635.963 1.00 27.18 N ANISOU 538 N PHE A 85 2309 4653 3364 496 -213 -515 N ATOM 539 CA PHE A 85 -142.610 -87.082 634.630 1.00 25.60 C ANISOU 539 CA PHE A 85 2113 4462 3150 455 -274 -432 C ATOM 540 C PHE A 85 -142.748 -88.312 633.736 1.00 26.00 C ANISOU 540 C PHE A 85 2154 4562 3163 379 -216 -437 C ATOM 541 O PHE A 85 -143.084 -88.198 632.561 1.00 28.19 O ANISOU 541 O PHE A 85 2407 4870 3433 365 -250 -408 O ATOM 542 CB PHE A 85 -141.139 -86.698 634.727 1.00 25.90 C ANISOU 542 CB PHE A 85 2200 4464 3176 434 -322 -365 C ATOM 543 CG PHE A 85 -140.889 -85.442 635.506 1.00 28.43 C ANISOU 543 CG PHE A 85 2541 4729 3533 504 -397 -359 C ATOM 544 CD1 PHE A 85 -140.899 -84.206 634.876 1.00 31.15 C ANISOU 544 CD1 PHE A 85 2888 5039 3908 538 -498 -297 C ATOM 545 CD2 PHE A 85 -140.629 -85.498 636.866 1.00 27.89 C ANISOU 545 CD2 PHE A 85 2495 4637 3466 542 -372 -417 C ATOM 546 CE1 PHE A 85 -140.658 -83.050 635.590 1.00 31.84 C ANISOU 546 CE1 PHE A 85 3006 5060 4033 607 -575 -298 C ATOM 547 CE2 PHE A 85 -140.386 -84.343 637.588 1.00 30.66 C ANISOU 547 CE2 PHE A 85 2878 4922 3849 609 -447 -423 C ATOM 548 CZ PHE A 85 -140.402 -83.119 636.951 1.00 32.57 C ANISOU 548 CZ PHE A 85 3132 5114 4128 637 -546 -365 C ATOM 549 N TRP A 86 -142.461 -89.488 634.279 1.00 24.89 N ANISOU 549 N TRP A 86 2037 4426 2996 334 -135 -476 N ATOM 550 CA TRP A 86 -142.694 -90.714 633.524 1.00 22.53 C ANISOU 550 CA TRP A 86 1734 4161 2667 268 -82 -497 C ATOM 551 C TRP A 86 -144.181 -90.842 633.225 1.00 26.13 C ANISOU 551 C TRP A 86 2135 4651 3143 275 -65 -555 C ATOM 552 O TRP A 86 -144.572 -91.388 632.193 1.00 28.27 O ANISOU 552 O TRP A 86 2383 4962 3394 237 -63 -564 O ATOM 553 CB TRP A 86 -142.184 -91.950 634.284 1.00 20.46 C ANISOU 553 CB TRP A 86 1513 3880 2382 227 -2 -527 C ATOM 554 CG TRP A 86 -140.767 -91.815 634.779 1.00 18.42 C ANISOU 554 CG TRP A 86 1299 3596 2103 234 -19 -483 C ATOM 555 CD1 TRP A 86 -140.330 -91.961 636.062 1.00 18.92 C ANISOU 555 CD1 TRP A 86 1393 3634 2164 261 14 -503 C ATOM 556 CD2 TRP A 86 -139.611 -91.469 633.996 1.00 15.50 C ANISOU 556 CD2 TRP A 86 946 3229 1713 215 -73 -412 C ATOM 557 NE1 TRP A 86 -138.969 -91.738 636.127 1.00 15.62 N ANISOU 557 NE1 TRP A 86 1001 3210 1723 263 -26 -454 N ATOM 558 CE2 TRP A 86 -138.508 -91.441 634.872 1.00 16.59 C ANISOU 558 CE2 TRP A 86 1118 3345 1840 228 -76 -397 C ATOM 559 CE3 TRP A 86 -139.401 -91.205 632.637 1.00 14.83 C ANISOU 559 CE3 TRP A 86 852 3167 1616 186 -114 -363 C ATOM 560 CZ2 TRP A 86 -137.210 -91.152 634.433 1.00 21.58 C ANISOU 560 CZ2 TRP A 86 1772 3972 2457 206 -120 -336 C ATOM 561 CZ3 TRP A 86 -138.116 -90.914 632.204 1.00 17.96 C ANISOU 561 CZ3 TRP A 86 1274 3555 1995 163 -149 -298 C ATOM 562 CH2 TRP A 86 -137.036 -90.891 633.100 1.00 19.77 C ANISOU 562 CH2 TRP A 86 1534 3756 2221 169 -151 -286 C ATOM 563 N ALA A 87 -145.013 -90.325 634.122 1.00 27.22 N ANISOU 563 N ALA A 87 2247 4777 3318 327 -55 -601 N ATOM 564 CA ALA A 87 -146.459 -90.424 633.942 1.00 26.75 C ANISOU 564 CA ALA A 87 2128 4755 3283 335 -37 -663 C ATOM 565 C ALA A 87 -146.909 -89.578 632.755 1.00 25.89 C ANISOU 565 C ALA A 87 1972 4685 3179 373 -123 -631 C ATOM 566 O ALA A 87 -147.757 -90.007 631.962 1.00 22.24 O ANISOU 566 O ALA A 87 1464 4277 2710 352 -119 -665 O ATOM 567 CB ALA A 87 -147.180 -90.005 635.201 1.00 23.95 C ANISOU 567 CB ALA A 87 1758 4377 2965 386 -4 -719 C ATOM 568 N HIS A 88 -146.326 -88.387 632.633 1.00 25.85 N ANISOU 568 N HIS A 88 1983 4651 3187 430 -204 -563 N ATOM 569 CA HIS A 88 -146.605 -87.503 631.504 1.00 31.68 C ANISOU 569 CA HIS A 88 2693 5413 3931 470 -295 -511 C ATOM 570 C HIS A 88 -146.024 -88.050 630.208 1.00 31.80 C ANISOU 570 C HIS A 88 2721 5465 3896 406 -306 -461 C ATOM 571 O HIS A 88 -146.671 -87.997 629.161 1.00 30.25 O ANISOU 571 O HIS A 88 2484 5325 3686 412 -341 -460 O ATOM 572 CB HIS A 88 -146.048 -86.097 631.744 1.00 34.63 C ANISOU 572 CB HIS A 88 3094 5728 4335 540 -383 -442 C ATOM 573 CG HIS A 88 -146.196 -85.188 630.556 1.00 40.18 C ANISOU 573 CG HIS A 88 3784 6443 5039 578 -483 -369 C ATOM 574 ND1 HIS A 88 -147.378 -84.554 630.251 1.00 39.08 N ANISOU 574 ND1 HIS A 88 3593 6329 4928 654 -532 -390 N ATOM 575 CD2 HIS A 88 -145.307 -84.825 629.600 1.00 41.54 C ANISOU 575 CD2 HIS A 88 3990 6610 5183 550 -544 -274 C ATOM 576 CE1 HIS A 88 -147.213 -83.829 629.152 1.00 39.99 C ANISOU 576 CE1 HIS A 88 3715 6449 5029 678 -624 -305 C ATOM 577 NE2 HIS A 88 -145.969 -83.972 628.744 1.00 40.48 N ANISOU 577 NE2 HIS A 88 3831 6494 5057 612 -632 -233 N ATOM 578 N TYR A 89 -144.791 -88.541 630.288 1.00 27.20 N ANISOU 578 N TYR A 89 2194 4856 3284 350 -279 -425 N ATOM 579 CA TYR A 89 -144.120 -89.156 629.154 1.00 23.50 C ANISOU 579 CA TYR A 89 1743 4423 2764 288 -275 -388 C ATOM 580 C TYR A 89 -145.030 -90.211 628.536 1.00 24.50 C ANISOU 580 C TYR A 89 1830 4614 2865 253 -228 -460 C ATOM 581 O TYR A 89 -145.269 -90.202 627.331 1.00 26.63 O ANISOU 581 O TYR A 89 2075 4941 3103 246 -262 -444 O ATOM 582 CB TYR A 89 -142.790 -89.759 629.607 1.00 23.40 C ANISOU 582 CB TYR A 89 1789 4373 2728 238 -231 -366 C ATOM 583 CG TYR A 89 -141.922 -90.372 628.524 1.00 18.10 C ANISOU 583 CG TYR A 89 1141 3734 2004 180 -221 -331 C ATOM 584 CD1 TYR A 89 -142.168 -90.156 627.175 1.00 18.02 C ANISOU 584 CD1 TYR A 89 1103 3781 1961 175 -262 -302 C ATOM 585 CD2 TYR A 89 -140.850 -91.166 628.868 1.00 19.14 C ANISOU 585 CD2 TYR A 89 1317 3845 2111 137 -173 -330 C ATOM 586 CE1 TYR A 89 -141.363 -90.728 626.200 1.00 19.61 C ANISOU 586 CE1 TYR A 89 1323 4023 2106 124 -245 -278 C ATOM 587 CE2 TYR A 89 -140.043 -91.741 627.910 1.00 20.48 C ANISOU 587 CE2 TYR A 89 1504 4048 2231 91 -160 -306 C ATOM 588 CZ TYR A 89 -140.297 -91.520 626.585 1.00 21.05 C ANISOU 588 CZ TYR A 89 1548 4180 2269 82 -192 -282 C ATOM 589 OH TYR A 89 -139.471 -92.108 625.661 1.00 23.85 O ANISOU 589 OH TYR A 89 1917 4577 2567 38 -172 -265 O ATOM 590 N ALA A 90 -145.567 -91.097 629.368 1.00 24.83 N ANISOU 590 N ALA A 90 1867 4648 2920 230 -155 -540 N ATOM 591 CA ALA A 90 -146.521 -92.100 628.896 1.00 25.38 C ANISOU 591 CA ALA A 90 1896 4771 2975 190 -113 -618 C ATOM 592 C ALA A 90 -147.780 -91.461 628.313 1.00 26.50 C ANISOU 592 C ALA A 90 1963 4973 3134 238 -163 -645 C ATOM 593 O ALA A 90 -148.370 -91.977 627.369 1.00 28.34 O ANISOU 593 O ALA A 90 2156 5274 3339 214 -166 -684 O ATOM 594 CB ALA A 90 -146.895 -93.051 630.030 1.00 20.43 C ANISOU 594 CB ALA A 90 1280 4110 2372 153 -28 -691 C ATOM 595 N ALA A 91 -148.196 -90.336 628.881 1.00 29.32 N ANISOU 595 N ALA A 91 2298 5307 3535 313 -207 -629 N ATOM 596 CA ALA A 91 -149.459 -89.723 628.483 1.00 30.25 C ANISOU 596 CA ALA A 91 2340 5478 3675 372 -256 -662 C ATOM 597 C ALA A 91 -149.331 -88.941 627.179 1.00 31.81 C ANISOU 597 C ALA A 91 2524 5714 3847 410 -351 -589 C ATOM 598 O ALA A 91 -150.294 -88.802 626.434 1.00 35.75 O ANISOU 598 O ALA A 91 2960 6284 4341 441 -391 -619 O ATOM 599 CB ALA A 91 -149.971 -88.823 629.585 1.00 29.37 C ANISOU 599 CB ALA A 91 2212 5326 3622 447 -267 -679 C ATOM 600 N ALA A 92 -148.141 -88.425 626.916 1.00 28.68 N ANISOU 600 N ALA A 92 2188 5276 3434 408 -390 -494 N ATOM 601 CA ALA A 92 -147.888 -87.659 625.705 1.00 29.11 C ANISOU 601 CA ALA A 92 2243 5358 3459 436 -482 -411 C ATOM 602 C ALA A 92 -146.570 -88.094 625.088 1.00 31.64 C ANISOU 602 C ALA A 92 2620 5675 3725 366 -465 -351 C ATOM 603 O ALA A 92 -146.515 -89.080 624.357 1.00 36.38 O ANISOU 603 O ALA A 92 3212 6336 4275 310 -423 -385 O ATOM 604 CB ALA A 92 -147.866 -86.169 626.010 1.00 29.21 C ANISOU 604 CB ALA A 92 2269 5314 3517 525 -573 -341 C ATOM 605 N GLN A 93 -145.506 -87.363 625.406 1.00 29.61 N ANISOU 605 N GLN A 93 2418 5351 3480 371 -498 -269 N ATOM 606 CA GLN A 93 -144.172 -87.671 624.907 1.00 32.41 C ANISOU 606 CA GLN A 93 2823 5704 3787 306 -481 -212 C ATOM 607 C GLN A 93 -143.133 -87.075 625.850 1.00 31.74 C ANISOU 607 C GLN A 93 2791 5532 3736 306 -490 -160 C ATOM 608 O GLN A 93 -143.464 -86.730 626.982 1.00 34.73 O ANISOU 608 O GLN A 93 3169 5857 4168 347 -487 -189 O ATOM 609 CB GLN A 93 -143.997 -87.127 623.498 1.00 35.73 C ANISOU 609 CB GLN A 93 3241 6180 4155 312 -554 -138 C ATOM 610 CG GLN A 93 -144.250 -85.643 623.398 1.00 38.21 C ANISOU 610 CG GLN A 93 3563 6459 4498 390 -666 -60 C ATOM 611 CD GLN A 93 -143.936 -85.112 622.025 1.00 43.14 C ANISOU 611 CD GLN A 93 4201 7136 5055 391 -739 27 C ATOM 612 OE1 GLN A 93 -143.679 -85.881 621.098 1.00 47.36 O ANISOU 612 OE1 GLN A 93 4725 7750 5521 337 -702 17 O ATOM 613 NE2 GLN A 93 -143.938 -83.793 621.884 1.00 42.23 N ANISOU 613 NE2 GLN A 93 4116 6977 4951 455 -844 116 N ATOM 614 N TRP A 94 -141.883 -86.938 625.413 1.00 26.17 N ANISOU 614 N TRP A 94 2128 4819 2998 260 -500 -90 N ATOM 615 CA TRP A 94 -140.911 -86.304 626.292 1.00 26.45 C ANISOU 615 CA TRP A 94 2207 4779 3066 258 -519 -45 C ATOM 616 C TRP A 94 -140.836 -84.809 626.013 1.00 32.72 C ANISOU 616 C TRP A 94 3016 5540 3876 307 -632 44 C ATOM 617 O TRP A 94 -140.109 -84.356 625.129 1.00 35.21 O ANISOU 617 O TRP A 94 3354 5878 4148 278 -675 126 O ATOM 618 CB TRP A 94 -139.520 -86.929 626.178 1.00 22.74 C ANISOU 618 CB TRP A 94 1771 4311 2557 183 -468 -23 C ATOM 619 CG TRP A 94 -138.643 -86.458 627.316 1.00 22.61 C ANISOU 619 CG TRP A 94 1791 4220 2581 181 -478 -3 C ATOM 620 CD1 TRP A 94 -137.660 -85.513 627.260 1.00 26.16 C ANISOU 620 CD1 TRP A 94 2267 4640 3032 164 -538 75 C ATOM 621 CD2 TRP A 94 -138.720 -86.871 628.688 1.00 21.97 C ANISOU 621 CD2 TRP A 94 1719 4092 2535 198 -432 -66 C ATOM 622 NE1 TRP A 94 -137.107 -85.325 628.507 1.00 26.91 N ANISOU 622 NE1 TRP A 94 2386 4673 3168 169 -536 58 N ATOM 623 CE2 TRP A 94 -137.743 -86.146 629.400 1.00 25.21 C ANISOU 623 CE2 TRP A 94 2161 4448 2970 195 -472 -27 C ATOM 624 CE3 TRP A 94 -139.518 -87.786 629.382 1.00 21.78 C ANISOU 624 CE3 TRP A 94 1680 4075 2519 214 -362 -153 C ATOM 625 CZ2 TRP A 94 -137.539 -86.315 630.768 1.00 24.41 C ANISOU 625 CZ2 TRP A 94 2077 4304 2895 214 -446 -73 C ATOM 626 CZ3 TRP A 94 -139.314 -87.949 630.744 1.00 22.67 C ANISOU 626 CZ3 TRP A 94 1812 4146 2656 231 -332 -193 C ATOM 627 CH2 TRP A 94 -138.332 -87.218 631.419 1.00 23.12 C ANISOU 627 CH2 TRP A 94 1899 4153 2731 236 -374 -154 C ATOM 628 N ASP A 95 -141.589 -84.055 626.805 1.00 34.80 N ANISOU 628 N ASP A 95 3271 5754 4199 384 -676 27 N ATOM 629 CA ASP A 95 -141.725 -82.618 626.639 1.00 37.53 C ANISOU 629 CA ASP A 95 3637 6056 4566 454 -791 105 C ATOM 630 C ASP A 95 -140.730 -81.807 627.459 1.00 35.92 C ANISOU 630 C ASP A 95 3484 5773 4392 454 -832 155 C ATOM 631 O ASP A 95 -140.808 -80.582 627.471 1.00 40.61 O ANISOU 631 O ASP A 95 4107 6314 5008 520 -930 221 O ATOM 632 CB ASP A 95 -143.144 -82.189 627.021 1.00 44.43 C ANISOU 632 CB ASP A 95 4472 6919 5490 555 -821 55 C ATOM 633 CG ASP A 95 -144.174 -82.585 625.985 1.00 51.18 C ANISOU 633 CG ASP A 95 5276 7856 6314 571 -823 30 C ATOM 634 OD1 ASP A 95 -143.824 -82.595 624.787 1.00 55.35 O ANISOU 634 OD1 ASP A 95 5817 8432 6782 538 -855 91 O ATOM 635 OD2 ASP A 95 -145.333 -82.871 626.363 1.00 52.24 O ANISOU 635 OD2 ASP A 95 5356 8015 6479 615 -794 -53 O ATOM 636 N PHE A 96 -139.801 -82.469 628.142 1.00 27.64 N ANISOU 636 N PHE A 96 2448 4713 3340 386 -764 124 N ATOM 637 CA PHE A 96 -138.996 -81.782 629.149 1.00 27.24 C ANISOU 637 CA PHE A 96 2434 4593 3323 391 -800 144 C ATOM 638 C PHE A 96 -137.574 -81.486 628.710 1.00 28.02 C ANISOU 638 C PHE A 96 2565 4695 3387 308 -825 230 C ATOM 639 O PHE A 96 -136.777 -80.944 629.471 1.00 34.28 O ANISOU 639 O PHE A 96 3383 5441 4202 292 -857 251 O ATOM 640 CB PHE A 96 -138.980 -82.603 630.440 1.00 27.81 C ANISOU 640 CB PHE A 96 2499 4650 3419 387 -716 45 C ATOM 641 CG PHE A 96 -140.350 -82.998 630.907 1.00 24.56 C ANISOU 641 CG PHE A 96 2048 4251 3032 452 -671 -42 C ATOM 642 CD1 PHE A 96 -141.155 -82.091 631.576 1.00 23.57 C ANISOU 642 CD1 PHE A 96 1918 4080 2956 554 -720 -69 C ATOM 643 CD2 PHE A 96 -140.850 -84.263 630.640 1.00 23.01 C ANISOU 643 CD2 PHE A 96 1821 4114 2807 415 -579 -101 C ATOM 644 CE1 PHE A 96 -142.436 -82.444 631.987 1.00 25.00 C ANISOU 644 CE1 PHE A 96 2055 4285 3159 609 -671 -156 C ATOM 645 CE2 PHE A 96 -142.129 -84.626 631.053 1.00 22.59 C ANISOU 645 CE2 PHE A 96 1727 4084 2774 462 -535 -183 C ATOM 646 CZ PHE A 96 -142.919 -83.714 631.730 1.00 24.32 C ANISOU 646 CZ PHE A 96 1932 4267 3043 556 -578 -211 C ATOM 647 N GLY A 97 -137.242 -81.838 627.482 1.00 25.66 N ANISOU 647 N GLY A 97 2261 4459 3028 248 -806 278 N ATOM 648 CA GLY A 97 -135.918 -81.541 626.982 1.00 22.34 C ANISOU 648 CA GLY A 97 1862 4056 2569 159 -819 366 C ATOM 649 C GLY A 97 -134.878 -82.496 627.509 1.00 23.08 C ANISOU 649 C GLY A 97 1950 4160 2660 86 -733 310 C ATOM 650 O GLY A 97 -135.118 -83.235 628.459 1.00 27.48 O ANISOU 650 O GLY A 97 2503 4692 3248 111 -677 218 O ATOM 651 N ASN A 98 -133.704 -82.455 626.896 1.00 25.37 N ANISOU 651 N ASN A 98 2242 4489 2910 -4 -723 374 N ATOM 652 CA ASN A 98 -132.665 -83.439 627.136 1.00 27.15 C ANISOU 652 CA ASN A 98 2457 4736 3123 -66 -639 325 C ATOM 653 C ASN A 98 -132.053 -83.398 628.527 1.00 37.02 C ANISOU 653 C ASN A 98 3722 5921 4425 -64 -640 276 C ATOM 654 O ASN A 98 -131.846 -84.441 629.148 1.00 41.74 O ANISOU 654 O ASN A 98 4322 6511 5025 -55 -569 198 O ATOM 655 CB ASN A 98 -131.558 -83.268 626.109 1.00 25.48 C ANISOU 655 CB ASN A 98 2233 4594 2856 -161 -633 408 C ATOM 656 CG ASN A 98 -130.404 -84.201 626.350 1.00 28.35 C ANISOU 656 CG ASN A 98 2582 4979 3209 -213 -552 357 C ATOM 657 OD1 ASN A 98 -130.449 -85.365 625.965 1.00 29.94 O ANISOU 657 OD1 ASN A 98 2775 5224 3376 -206 -474 304 O ATOM 658 ND2 ASN A 98 -129.364 -83.702 627.006 1.00 34.07 N ANISOU 658 ND2 ASN A 98 3307 5672 3965 -262 -577 372 N ATOM 659 N THR A 99 -131.734 -82.205 629.011 1.00 39.46 N ANISOU 659 N THR A 99 4044 6182 4767 -77 -727 328 N ATOM 660 CA THR A 99 -131.050 -82.109 630.290 1.00 40.41 C ANISOU 660 CA THR A 99 4175 6252 4928 -85 -738 279 C ATOM 661 C THR A 99 -131.971 -82.628 631.388 1.00 35.32 C ANISOU 661 C THR A 99 3540 5569 4309 10 -712 182 C ATOM 662 O THR A 99 -131.527 -83.331 632.297 1.00 33.86 O ANISOU 662 O THR A 99 3365 5372 4129 16 -667 114 O ATOM 663 CB THR A 99 -130.580 -80.668 630.592 1.00 45.03 C ANISOU 663 CB THR A 99 4811 6737 5560 -124 -822 341 C ATOM 664 OG1 THR A 99 -131.671 -79.759 630.419 1.00 51.40 O ANISOU 664 OG1 THR A 99 5674 7460 6397 -54 -872 377 O ATOM 665 CG2 THR A 99 -129.435 -80.272 629.654 1.00 44.03 C ANISOU 665 CG2 THR A 99 4678 6640 5410 -246 -824 430 C ATOM 666 N MET A 100 -133.258 -82.323 631.277 1.00 30.10 N ANISOU 666 N MET A 100 2878 4899 3661 86 -737 179 N ATOM 667 CA MET A 100 -134.232 -82.854 632.215 1.00 31.39 C ANISOU 667 CA MET A 100 3040 5042 3844 167 -698 88 C ATOM 668 C MET A 100 -134.365 -84.380 632.061 1.00 35.53 C ANISOU 668 C MET A 100 3556 5607 4338 149 -585 33 C ATOM 669 O MET A 100 -134.692 -85.085 633.018 1.00 37.55 O ANISOU 669 O MET A 100 3816 5856 4595 184 -532 -38 O ATOM 670 CB MET A 100 -135.578 -82.164 632.016 1.00 31.55 C ANISOU 670 CB MET A 100 3050 5049 3888 253 -746 93 C ATOM 671 CG MET A 100 -136.536 -82.286 633.183 1.00 34.08 C ANISOU 671 CG MET A 100 3367 5341 4241 344 -724 -2 C ATOM 672 SD MET A 100 -135.908 -81.532 634.701 1.00 51.69 S ANISOU 672 SD MET A 100 5682 7444 6514 361 -751 -44 S ATOM 673 CE MET A 100 -135.673 -79.842 634.161 1.00 69.29 C ANISOU 673 CE MET A 100 7984 9552 8792 354 -852 48 C ATOM 674 N CYS A 101 -134.098 -84.888 630.858 1.00 34.78 N ANISOU 674 N CYS A 101 3449 5561 4204 98 -550 68 N ATOM 675 CA CYS A 101 -134.111 -86.331 630.609 1.00 28.21 C ANISOU 675 CA CYS A 101 2613 4770 3337 79 -453 20 C ATOM 676 C CYS A 101 -132.946 -87.027 631.290 1.00 23.01 C ANISOU 676 C CYS A 101 1973 4102 2666 51 -411 -4 C ATOM 677 O CYS A 101 -133.100 -88.100 631.861 1.00 22.63 O ANISOU 677 O CYS A 101 1934 4062 2604 70 -347 -61 O ATOM 678 CB CYS A 101 -134.079 -86.623 629.107 1.00 28.64 C ANISOU 678 CB CYS A 101 2649 4887 3344 38 -435 59 C ATOM 679 SG CYS A 101 -133.678 -88.345 628.673 1.00 30.68 S ANISOU 679 SG CYS A 101 2909 5198 3549 5 -329 9 S ATOM 680 N GLN A 102 -131.773 -86.416 631.239 1.00 24.18 N ANISOU 680 N GLN A 102 2126 4241 2820 7 -451 39 N ATOM 681 CA GLN A 102 -130.604 -87.028 631.850 1.00 26.51 C ANISOU 681 CA GLN A 102 2433 4534 3106 -13 -420 14 C ATOM 682 C GLN A 102 -130.655 -86.920 633.365 1.00 28.39 C ANISOU 682 C GLN A 102 2692 4727 3368 35 -441 -34 C ATOM 683 O GLN A 102 -130.212 -87.819 634.081 1.00 30.01 O ANISOU 683 O GLN A 102 2910 4939 3553 54 -398 -77 O ATOM 684 CB GLN A 102 -129.329 -86.385 631.331 1.00 25.55 C ANISOU 684 CB GLN A 102 2297 4427 2983 -81 -455 66 C ATOM 685 CG GLN A 102 -129.105 -86.597 629.865 1.00 33.39 C ANISOU 685 CG GLN A 102 3267 5486 3933 -130 -424 111 C ATOM 686 CD GLN A 102 -127.687 -86.305 629.474 1.00 38.25 C ANISOU 686 CD GLN A 102 3861 6136 4538 -203 -430 147 C ATOM 687 OE1 GLN A 102 -127.347 -85.176 629.115 1.00 43.60 O ANISOU 687 OE1 GLN A 102 4522 6821 5225 -259 -488 212 O ATOM 688 NE2 GLN A 102 -126.839 -87.317 629.558 1.00 39.74 N ANISOU 688 NE2 GLN A 102 4045 6350 4705 -204 -373 108 N ATOM 689 N LEU A 103 -131.188 -85.806 633.848 1.00 25.18 N ANISOU 689 N LEU A 103 2289 4283 2995 62 -511 -28 N ATOM 690 CA LEU A 103 -131.292 -85.580 635.274 1.00 24.94 C ANISOU 690 CA LEU A 103 2280 4218 2977 115 -538 -81 C ATOM 691 C LEU A 103 -132.218 -86.612 635.898 1.00 26.73 C ANISOU 691 C LEU A 103 2512 4464 3181 176 -464 -145 C ATOM 692 O LEU A 103 -131.839 -87.313 636.839 1.00 26.71 O ANISOU 692 O LEU A 103 2528 4470 3152 202 -434 -190 O ATOM 693 CB LEU A 103 -131.806 -84.173 635.553 1.00 28.56 C ANISOU 693 CB LEU A 103 2741 4638 3474 144 -630 -71 C ATOM 694 CG LEU A 103 -131.751 -83.736 637.012 1.00 38.38 C ANISOU 694 CG LEU A 103 4027 5827 4730 197 -665 -136 C ATOM 695 CD1 LEU A 103 -130.498 -82.912 637.235 1.00 44.20 C ANISOU 695 CD1 LEU A 103 4791 6516 5489 135 -730 -116 C ATOM 696 CD2 LEU A 103 -132.994 -82.949 637.394 1.00 40.08 C ANISOU 696 CD2 LEU A 103 4281 5962 4984 270 -682 -161 C ATOM 697 N LEU A 104 -133.428 -86.709 635.356 1.00 23.86 N ANISOU 697 N LEU A 104 2127 4115 2823 198 -438 -149 N ATOM 698 CA LEU A 104 -134.445 -87.588 635.908 1.00 19.04 C ANISOU 698 CA LEU A 104 1508 3530 2198 247 -368 -215 C ATOM 699 C LEU A 104 -134.058 -89.061 635.795 1.00 17.71 C ANISOU 699 C LEU A 104 1343 3401 1985 221 -286 -236 C ATOM 700 O LEU A 104 -134.376 -89.861 636.673 1.00 21.98 O ANISOU 700 O LEU A 104 1886 3960 2503 259 -234 -293 O ATOM 701 CB LEU A 104 -135.778 -87.334 635.220 1.00 17.53 C ANISOU 701 CB LEU A 104 1284 3349 2027 266 -363 -218 C ATOM 702 CG LEU A 104 -136.362 -85.967 635.567 1.00 18.53 C ANISOU 702 CG LEU A 104 1406 3437 2198 323 -443 -216 C ATOM 703 CD1 LEU A 104 -137.504 -85.609 634.635 1.00 21.64 C ANISOU 703 CD1 LEU A 104 1765 3845 2613 343 -456 -200 C ATOM 704 CD2 LEU A 104 -136.833 -85.963 637.003 1.00 20.21 C ANISOU 704 CD2 LEU A 104 1625 3637 2416 398 -427 -298 C ATOM 705 N THR A 105 -133.368 -89.426 634.723 1.00 14.55 N ANISOU 705 N THR A 105 942 3017 1570 165 -274 -193 N ATOM 706 CA THR A 105 -132.881 -90.796 634.588 1.00 16.31 C ANISOU 706 CA THR A 105 1171 3274 1751 149 -207 -215 C ATOM 707 C THR A 105 -131.890 -91.068 635.710 1.00 18.62 C ANISOU 707 C THR A 105 1485 3562 2029 176 -214 -234 C ATOM 708 O THR A 105 -131.865 -92.157 636.299 1.00 19.81 O ANISOU 708 O THR A 105 1641 3739 2146 206 -164 -276 O ATOM 709 CB THR A 105 -132.224 -91.033 633.219 1.00 13.45 C ANISOU 709 CB THR A 105 803 2935 1372 92 -199 -173 C ATOM 710 OG1 THR A 105 -133.235 -90.968 632.209 1.00 17.83 O ANISOU 710 OG1 THR A 105 1339 3508 1926 78 -190 -167 O ATOM 711 CG2 THR A 105 -131.561 -92.401 633.159 1.00 13.17 C ANISOU 711 CG2 THR A 105 777 2932 1296 86 -142 -201 C ATOM 712 N GLY A 106 -131.091 -90.055 636.019 1.00 18.14 N ANISOU 712 N GLY A 106 1433 3468 1989 168 -283 -205 N ATOM 713 CA GLY A 106 -130.132 -90.143 637.106 1.00 21.02 C ANISOU 713 CA GLY A 106 1820 3828 2339 196 -308 -226 C ATOM 714 C GLY A 106 -130.786 -90.357 638.453 1.00 21.96 C ANISOU 714 C GLY A 106 1957 3952 2435 274 -302 -285 C ATOM 715 O GLY A 106 -130.398 -91.260 639.195 1.00 25.89 O ANISOU 715 O GLY A 106 2468 4479 2889 319 -277 -316 O ATOM 716 N LEU A 107 -131.779 -89.531 638.769 1.00 17.88 N ANISOU 716 N LEU A 107 1437 3413 1943 301 -328 -302 N ATOM 717 CA LEU A 107 -132.508 -89.656 640.025 1.00 19.83 C ANISOU 717 CA LEU A 107 1728 3636 2173 372 -300 -360 C ATOM 718 C LEU A 107 -133.138 -91.035 640.163 1.00 20.84 C ANISOU 718 C LEU A 107 1864 3787 2268 389 -191 -390 C ATOM 719 O LEU A 107 -133.156 -91.634 641.235 1.00 23.03 O ANISOU 719 O LEU A 107 2211 4034 2504 434 -143 -419 O ATOM 720 CB LEU A 107 -133.598 -88.589 640.117 1.00 23.23 C ANISOU 720 CB LEU A 107 2162 4018 2647 393 -322 -374 C ATOM 721 CG LEU A 107 -133.185 -87.163 640.455 1.00 25.66 C ANISOU 721 CG LEU A 107 2501 4260 2988 396 -418 -364 C ATOM 722 CD1 LEU A 107 -134.427 -86.289 640.589 1.00 21.97 C ANISOU 722 CD1 LEU A 107 2042 3743 2564 438 -425 -388 C ATOM 723 CD2 LEU A 107 -132.379 -87.172 641.748 1.00 29.09 C ANISOU 723 CD2 LEU A 107 3008 4660 3385 427 -439 -399 C ATOM 724 N TYR A 108 -133.664 -91.518 639.049 1.00 17.85 N ANISOU 724 N TYR A 108 1416 3461 1904 350 -153 -381 N ATOM 725 CA TYR A 108 -134.365 -92.783 638.990 1.00 17.98 C ANISOU 725 CA TYR A 108 1431 3498 1904 347 -47 -416 C ATOM 726 C TYR A 108 -133.428 -93.925 639.358 1.00 20.19 C ANISOU 726 C TYR A 108 1756 3777 2138 360 -7 -413 C ATOM 727 O TYR A 108 -133.760 -94.761 640.205 1.00 18.57 O ANISOU 727 O TYR A 108 1619 3535 1903 391 72 -441 O ATOM 728 CB TYR A 108 -134.948 -92.961 637.588 1.00 13.31 C ANISOU 728 CB TYR A 108 800 2923 1334 281 -36 -398 C ATOM 729 CG TYR A 108 -135.600 -94.284 637.292 1.00 13.28 C ANISOU 729 CG TYR A 108 812 2913 1322 249 53 -428 C ATOM 730 CD1 TYR A 108 -136.922 -94.530 637.642 1.00 14.27 C ANISOU 730 CD1 TYR A 108 942 3011 1468 247 112 -471 C ATOM 731 CD2 TYR A 108 -134.908 -95.269 636.607 1.00 20.85 C ANISOU 731 CD2 TYR A 108 1783 3877 2261 212 70 -414 C ATOM 732 CE1 TYR A 108 -137.524 -95.735 637.336 1.00 16.06 C ANISOU 732 CE1 TYR A 108 1190 3209 1704 201 183 -493 C ATOM 733 CE2 TYR A 108 -135.492 -96.473 636.301 1.00 22.53 C ANISOU 733 CE2 TYR A 108 2017 4064 2482 177 139 -441 C ATOM 734 CZ TYR A 108 -136.796 -96.708 636.665 1.00 22.22 C ANISOU 734 CZ TYR A 108 1984 3988 2469 167 194 -478 C ATOM 735 OH TYR A 108 -137.358 -97.924 636.347 1.00 24.66 O ANISOU 735 OH TYR A 108 2314 4259 2796 122 262 -502 O ATOM 736 N PHE A 109 -132.246 -93.956 638.750 1.00 18.37 N ANISOU 736 N PHE A 109 1492 3586 1900 339 -60 -380 N ATOM 737 CA PHE A 109 -131.326 -95.049 639.045 1.00 20.63 C ANISOU 737 CA PHE A 109 1816 3877 2147 366 -29 -381 C ATOM 738 C PHE A 109 -130.641 -94.870 640.396 1.00 24.43 C ANISOU 738 C PHE A 109 2380 4311 2591 431 -66 -382 C ATOM 739 O PHE A 109 -130.301 -95.858 641.050 1.00 25.71 O ANISOU 739 O PHE A 109 2609 4451 2709 480 -21 -390 O ATOM 740 CB PHE A 109 -130.302 -95.215 637.922 1.00 13.06 C ANISOU 740 CB PHE A 109 814 2959 1190 317 -64 -349 C ATOM 741 CG PHE A 109 -130.837 -96.003 636.760 1.00 20.52 C ANISOU 741 CG PHE A 109 1755 3899 2141 259 -8 -352 C ATOM 742 CD1 PHE A 109 -130.929 -97.384 636.829 1.00 12.99 C ANISOU 742 CD1 PHE A 109 829 2931 1175 273 63 -378 C ATOM 743 CD2 PHE A 109 -131.301 -95.362 635.617 1.00 16.68 C ANISOU 743 CD2 PHE A 109 1254 3406 1678 196 -28 -327 C ATOM 744 CE1 PHE A 109 -131.443 -98.107 635.773 1.00 12.95 C ANISOU 744 CE1 PHE A 109 825 2910 1187 214 98 -387 C ATOM 745 CE2 PHE A 109 -131.815 -96.089 634.557 1.00 15.69 C ANISOU 745 CE2 PHE A 109 1127 3285 1551 151 9 -337 C ATOM 746 CZ PHE A 109 -131.889 -97.460 634.638 1.00 12.86 C ANISOU 746 CZ PHE A 109 785 2914 1186 156 66 -372 C ATOM 747 N ILE A 110 -130.456 -93.627 640.831 1.00 23.42 N ANISOU 747 N ILE A 110 2257 4164 2477 434 -148 -377 N ATOM 748 CA ILE A 110 -129.928 -93.391 642.176 1.00 13.97 C ANISOU 748 CA ILE A 110 1141 2927 1239 496 -186 -391 C ATOM 749 C ILE A 110 -130.931 -93.898 643.199 1.00 14.16 C ANISOU 749 C ILE A 110 1257 2897 1227 544 -101 -420 C ATOM 750 O ILE A 110 -130.567 -94.562 644.174 1.00 15.65 O ANISOU 750 O ILE A 110 1531 3061 1353 605 -78 -425 O ATOM 751 CB ILE A 110 -129.610 -91.898 642.418 1.00 19.87 C ANISOU 751 CB ILE A 110 1875 3656 2016 481 -289 -392 C ATOM 752 CG1 ILE A 110 -128.385 -91.487 641.593 1.00 21.26 C ANISOU 752 CG1 ILE A 110 1972 3886 2217 429 -367 -362 C ATOM 753 CG2 ILE A 110 -129.329 -91.627 643.887 1.00 17.35 C ANISOU 753 CG2 ILE A 110 1647 3295 1649 546 -322 -423 C ATOM 754 CD1 ILE A 110 -128.176 -90.003 641.504 1.00 14.50 C ANISOU 754 CD1 ILE A 110 1113 2982 1415 378 -442 -350 C ATOM 755 N GLY A 111 -132.202 -93.595 642.966 1.00 17.82 N ANISOU 755 N GLY A 111 1702 3345 1726 519 -52 -438 N ATOM 756 CA GLY A 111 -133.260 -94.107 643.811 1.00 17.11 C ANISOU 756 CA GLY A 111 1681 3213 1607 548 48 -469 C ATOM 757 C GLY A 111 -133.212 -95.622 643.823 1.00 17.69 C ANISOU 757 C GLY A 111 1797 3282 1643 554 145 -463 C ATOM 758 O GLY A 111 -133.288 -96.259 644.871 1.00 21.00 O ANISOU 758 O GLY A 111 2319 3657 2001 601 205 -468 O ATOM 759 N PHE A 112 -133.064 -96.194 642.638 1.00 21.21 N ANISOU 759 N PHE A 112 2170 3768 2121 506 160 -452 N ATOM 760 CA PHE A 112 -133.108 -97.631 642.466 1.00 14.15 C ANISOU 760 CA PHE A 112 1311 2861 1206 501 257 -454 C ATOM 761 C PHE A 112 -131.986 -98.332 643.216 1.00 28.07 C ANISOU 761 C PHE A 112 3163 4595 2906 572 244 -429 C ATOM 762 O PHE A 112 -132.244 -99.166 644.081 1.00 32.19 O ANISOU 762 O PHE A 112 3794 5059 3380 610 325 -428 O ATOM 763 CB PHE A 112 -133.037 -97.982 640.990 1.00 13.79 C ANISOU 763 CB PHE A 112 1173 2855 1213 430 250 -445 C ATOM 764 CG PHE A 112 -133.001 -99.453 640.729 1.00 29.09 C ANISOU 764 CG PHE A 112 3162 4734 3157 407 325 -438 C ATOM 765 CD1 PHE A 112 -134.127-100.236 640.954 1.00 28.90 C ANISOU 765 CD1 PHE A 112 3195 4628 3159 365 427 -452 C ATOM 766 CD2 PHE A 112 -131.850-100.060 640.263 1.00 26.02 C ANISOU 766 CD2 PHE A 112 2763 4373 2752 430 300 -424 C ATOM 767 CE1 PHE A 112 -134.103-101.594 640.719 1.00 26.83 C ANISOU 767 CE1 PHE A 112 2984 4306 2903 345 506 -452 C ATOM 768 CE2 PHE A 112 -131.821-101.423 640.018 1.00 27.75 C ANISOU 768 CE2 PHE A 112 3032 4532 2978 419 374 -426 C ATOM 769 CZ PHE A 112 -132.949-102.188 640.245 1.00 29.13 C ANISOU 769 CZ PHE A 112 3271 4620 3178 375 479 -441 C ATOM 770 N PHE A 113 -130.742 -97.998 642.885 1.00 21.62 N ANISOU 770 N PHE A 113 2302 3822 2089 590 144 -408 N ATOM 771 CA PHE A 113 -129.607 -98.708 643.466 1.00 23.52 C ANISOU 771 CA PHE A 113 2609 4054 2275 666 121 -390 C ATOM 772 C PHE A 113 -129.516 -98.466 644.964 1.00 25.56 C ANISOU 772 C PHE A 113 2980 4267 2464 742 101 -388 C ATOM 773 O PHE A 113 -129.298 -99.410 645.724 1.00 20.59 O ANISOU 773 O PHE A 113 2459 3594 1771 811 146 -373 O ATOM 774 CB PHE A 113 -128.297 -98.303 642.799 1.00 14.61 C ANISOU 774 CB PHE A 113 1389 2999 1165 664 15 -379 C ATOM 775 CG PHE A 113 -128.156 -98.796 641.394 1.00 14.29 C ANISOU 775 CG PHE A 113 1254 3008 1167 608 42 -380 C ATOM 776 CD1 PHE A 113 -128.041-100.151 641.128 1.00 19.75 C ANISOU 776 CD1 PHE A 113 1978 3680 1845 633 119 -385 C ATOM 777 CD2 PHE A 113 -128.111 -97.905 640.331 1.00 15.67 C ANISOU 777 CD2 PHE A 113 1315 3247 1392 531 -9 -375 C ATOM 778 CE1 PHE A 113 -127.892-100.609 639.830 1.00 14.30 C ANISOU 778 CE1 PHE A 113 1202 3040 1189 583 143 -397 C ATOM 779 CE2 PHE A 113 -127.967 -98.364 639.025 1.00 16.78 C ANISOU 779 CE2 PHE A 113 1373 3445 1560 480 16 -378 C ATOM 780 CZ PHE A 113 -127.862 -99.717 638.780 1.00 13.88 C ANISOU 780 CZ PHE A 113 1034 3062 1177 505 92 -394 C ATOM 781 N SER A 114 -129.691 -97.214 645.387 1.00 15.23 N ANISOU 781 N SER A 114 1655 2966 1164 733 34 -402 N ATOM 782 CA SER A 114 -129.614 -96.906 646.809 1.00 19.44 C ANISOU 782 CA SER A 114 2294 3467 1626 803 10 -410 C ATOM 783 C SER A 114 -130.700 -97.673 647.537 1.00 16.18 C ANISOU 783 C SER A 114 1991 2991 1167 820 140 -412 C ATOM 784 O SER A 114 -130.505 -98.103 648.667 1.00 21.46 O ANISOU 784 O SER A 114 2780 3625 1748 894 158 -401 O ATOM 785 CB SER A 114 -129.748 -95.407 647.078 1.00 15.76 C ANISOU 785 CB SER A 114 1792 3010 1187 782 -74 -438 C ATOM 786 OG SER A 114 -131.063 -94.977 646.807 1.00 21.94 O ANISOU 786 OG SER A 114 2550 3769 2015 732 -11 -458 O ATOM 787 N GLY A 115 -131.834 -97.862 646.870 1.00 15.85 N ANISOU 787 N GLY A 115 1905 2938 1181 750 233 -426 N ATOM 788 CA GLY A 115 -132.929 -98.628 647.433 1.00 16.29 C ANISOU 788 CA GLY A 115 2046 2929 1215 735 368 -429 C ATOM 789 C GLY A 115 -132.513-100.022 647.853 1.00 29.91 C ANISOU 789 C GLY A 115 3883 4591 2891 770 431 -388 C ATOM 790 O GLY A 115 -132.671-100.419 649.005 1.00 29.72 O ANISOU 790 O GLY A 115 3986 4507 2800 809 477 -368 O ATOM 791 N ILE A 116 -131.958-100.772 646.919 1.00 16.60 N ANISOU 791 N ILE A 116 2154 2919 1233 760 433 -376 N ATOM 792 CA ILE A 116 -131.593-102.130 647.216 1.00 19.15 C ANISOU 792 CA ILE A 116 2584 3175 1516 801 496 -342 C ATOM 793 C ILE A 116 -130.365-102.154 648.132 1.00 24.62 C ANISOU 793 C ILE A 116 3363 3882 2110 933 411 -313 C ATOM 794 O ILE A 116 -130.236-103.067 648.952 1.00 24.43 O ANISOU 794 O ILE A 116 3477 3785 2021 993 461 -274 O ATOM 795 CB ILE A 116 -131.351-102.960 645.913 1.00 23.90 C ANISOU 795 CB ILE A 116 3115 3786 2180 757 524 -348 C ATOM 796 CG1 ILE A 116 -131.168-104.433 646.263 1.00 23.91 C ANISOU 796 CG1 ILE A 116 3245 3696 2144 799 611 -319 C ATOM 797 CG2 ILE A 116 -130.176-102.429 645.116 1.00 23.32 C ANISOU 797 CG2 ILE A 116 2928 3815 2117 793 406 -356 C ATOM 798 CD1 ILE A 116 -132.275-104.970 647.190 1.00 21.35 C ANISOU 798 CD1 ILE A 116 3042 3274 1797 759 734 -308 C ATOM 799 N PHE A 117 -129.492-101.146 648.040 1.00 17.44 N ANISOU 799 N PHE A 117 2373 3056 1196 967 276 -329 N ATOM 800 CA PHE A 117 -128.294-101.127 648.889 1.00 21.95 C ANISOU 800 CA PHE A 117 3006 3647 1689 1078 174 -309 C ATOM 801 C PHE A 117 -128.653-100.981 650.368 1.00 25.73 C ANISOU 801 C PHE A 117 3628 4085 2064 1141 193 -300 C ATOM 802 O PHE A 117 -128.021-101.577 651.226 1.00 30.17 O ANISOU 802 O PHE A 117 4302 4622 2541 1240 171 -265 O ATOM 803 CB PHE A 117 -127.336-100.001 648.496 1.00 17.67 C ANISOU 803 CB PHE A 117 2334 3195 1186 1069 24 -333 C ATOM 804 CG PHE A 117 -126.660-100.202 647.170 1.00 19.26 C ANISOU 804 CG PHE A 117 2405 3452 1463 1030 -8 -336 C ATOM 805 CD1 PHE A 117 -126.704-101.425 646.521 1.00 24.84 C ANISOU 805 CD1 PHE A 117 3125 4128 2186 1032 76 -321 C ATOM 806 CD2 PHE A 117 -125.996 -99.153 646.559 1.00 19.09 C ANISOU 806 CD2 PHE A 117 2251 3509 1495 984 -116 -356 C ATOM 807 CE1 PHE A 117 -126.091-101.596 645.288 1.00 23.86 C ANISOU 807 CE1 PHE A 117 2879 4062 2124 997 51 -331 C ATOM 808 CE2 PHE A 117 -125.380 -99.318 645.324 1.00 19.53 C ANISOU 808 CE2 PHE A 117 2186 3624 1612 941 -136 -358 C ATOM 809 CZ PHE A 117 -125.427-100.538 644.693 1.00 16.43 C ANISOU 809 CZ PHE A 117 1803 3211 1228 951 -54 -348 C ATOM 810 N PHE A 118 -129.668-100.189 650.673 1.00 18.64 N ANISOU 810 N PHE A 118 2721 3172 1191 1076 228 -325 N ATOM 811 CA PHE A 118 -130.028 -99.986 652.070 1.00 27.04 C ANISOU 811 CA PHE A 118 3903 4189 2181 1112 242 -315 C ATOM 812 C PHE A 118 -130.852-101.141 652.627 1.00 28.21 C ANISOU 812 C PHE A 118 4178 4238 2304 1093 386 -271 C ATOM 813 O PHE A 118 -130.825-101.400 653.824 1.00 24.09 O ANISOU 813 O PHE A 118 3783 3675 1694 1150 400 -242 O ATOM 814 CB PHE A 118 -130.773 -98.666 652.244 1.00 25.19 C ANISOU 814 CB PHE A 118 3612 3979 1980 1058 222 -368 C ATOM 815 CG PHE A 118 -129.879 -97.462 652.181 1.00 25.63 C ANISOU 815 CG PHE A 118 3592 4114 2030 1092 69 -410 C ATOM 816 CD1 PHE A 118 -128.958 -97.220 653.183 1.00 24.84 C ANISOU 816 CD1 PHE A 118 3555 4030 1852 1173 -31 -410 C ATOM 817 CD2 PHE A 118 -129.961 -96.571 651.125 1.00 18.04 C ANISOU 817 CD2 PHE A 118 2490 3194 1170 1018 19 -442 C ATOM 818 CE1 PHE A 118 -128.128 -96.110 653.131 1.00 27.14 C ANISOU 818 CE1 PHE A 118 3769 4387 2155 1181 -175 -456 C ATOM 819 CE2 PHE A 118 -129.137 -95.460 651.063 1.00 23.91 C ANISOU 819 CE2 PHE A 118 3161 3983 1941 1015 -121 -469 C ATOM 820 CZ PHE A 118 -128.217 -95.229 652.063 1.00 25.13 C ANISOU 820 CZ PHE A 118 3377 4160 2011 1094 -217 -483 C ATOM 821 N ILE A 119 -131.580-101.830 651.755 1.00 33.76 N ANISOU 821 N ILE A 119 4842 4904 3081 1007 493 -271 N ATOM 822 CA ILE A 119 -132.268-103.055 652.129 1.00 20.57 C ANISOU 822 CA ILE A 119 3285 3138 1394 978 632 -234 C ATOM 823 C ILE A 119 -131.222-104.092 652.499 1.00 29.90 C ANISOU 823 C ILE A 119 4586 4279 2495 1093 612 -174 C ATOM 824 O ILE A 119 -131.353-104.795 653.498 1.00 34.65 O ANISOU 824 O ILE A 119 5340 4808 3019 1138 671 -126 O ATOM 825 CB ILE A 119 -133.162-103.569 650.993 1.00 20.06 C ANISOU 825 CB ILE A 119 3136 3053 1434 856 733 -262 C ATOM 826 CG1 ILE A 119 -134.401-102.691 650.868 1.00 19.67 C ANISOU 826 CG1 ILE A 119 2994 3031 1449 754 772 -318 C ATOM 827 CG2 ILE A 119 -133.594-105.003 651.241 1.00 21.87 C ANISOU 827 CG2 ILE A 119 3481 3182 1646 834 865 -225 C ATOM 828 CD1 ILE A 119 -135.264-103.060 649.695 1.00 19.20 C ANISOU 828 CD1 ILE A 119 2829 2974 1493 637 849 -358 C ATOM 829 N ILE A 120 -130.167-104.175 651.700 1.00 25.82 N ANISOU 829 N ILE A 120 4002 3815 1995 1148 526 -179 N ATOM 830 CA ILE A 120 -129.055-105.061 652.017 1.00 26.78 C ANISOU 830 CA ILE A 120 4223 3914 2037 1282 486 -132 C ATOM 831 C ILE A 120 -128.377-104.659 653.334 1.00 31.72 C ANISOU 831 C ILE A 120 4941 4562 2550 1399 388 -108 C ATOM 832 O ILE A 120 -128.097-105.510 654.183 1.00 35.34 O ANISOU 832 O ILE A 120 5556 4953 2919 1493 412 -50 O ATOM 833 CB ILE A 120 -128.033-105.077 650.882 1.00 21.07 C ANISOU 833 CB ILE A 120 3378 3270 1356 1318 403 -159 C ATOM 834 CG1 ILE A 120 -128.652-105.722 649.641 1.00 20.50 C ANISOU 834 CG1 ILE A 120 3238 3164 1388 1212 507 -178 C ATOM 835 CG2 ILE A 120 -126.784-105.841 651.297 1.00 24.19 C ANISOU 835 CG2 ILE A 120 3864 3665 1662 1480 337 -122 C ATOM 836 CD1 ILE A 120 -127.770-105.672 648.412 1.00 23.88 C ANISOU 836 CD1 ILE A 120 3521 3673 1878 1218 432 -209 C ATOM 837 N LEU A 121 -128.138-103.364 653.523 1.00 31.47 N ANISOU 837 N LEU A 121 4818 4617 2523 1391 279 -153 N ATOM 838 CA LEU A 121 -127.549-102.883 654.775 1.00 30.17 C ANISOU 838 CA LEU A 121 4722 4475 2265 1483 180 -146 C ATOM 839 C LEU A 121 -128.446-103.132 655.987 1.00 32.04 C ANISOU 839 C LEU A 121 5106 4631 2438 1474 276 -112 C ATOM 840 O LEU A 121 -127.948-103.440 657.067 1.00 35.08 O ANISOU 840 O LEU A 121 5608 4996 2724 1576 239 -75 O ATOM 841 CB LEU A 121 -127.222-101.396 654.677 1.00 29.74 C ANISOU 841 CB LEU A 121 4536 4518 2247 1453 56 -213 C ATOM 842 CG LEU A 121 -125.964-101.116 653.857 1.00 28.79 C ANISOU 842 CG LEU A 121 4286 4492 2160 1488 -76 -242 C ATOM 843 CD1 LEU A 121 -125.760 -99.623 653.662 1.00 26.31 C ANISOU 843 CD1 LEU A 121 3843 4256 1899 1429 -183 -307 C ATOM 844 CD2 LEU A 121 -124.755-101.749 654.534 1.00 28.06 C ANISOU 844 CD2 LEU A 121 4257 4410 1993 1626 -163 -212 C ATOM 845 N LEU A 122 -129.757-102.985 655.816 1.00 30.26 N ANISOU 845 N LEU A 122 4864 4366 2269 1352 397 -128 N ATOM 846 CA LEU A 122 -130.710-103.395 656.847 1.00 29.02 C ANISOU 846 CA LEU A 122 4836 4132 2057 1326 514 -97 C ATOM 847 C LEU A 122 -130.530-104.875 657.186 1.00 30.09 C ANISOU 847 C LEU A 122 5133 4172 2130 1389 595 -16 C ATOM 848 O LEU A 122 -130.412-105.257 658.349 1.00 27.81 O ANISOU 848 O LEU A 122 4991 3840 1737 1464 606 32 O ATOM 849 CB LEU A 122 -132.145-103.152 656.387 1.00 26.50 C ANISOU 849 CB LEU A 122 4445 3795 1827 1177 637 -137 C ATOM 850 CG LEU A 122 -132.704-101.749 656.567 1.00 29.40 C ANISOU 850 CG LEU A 122 4718 4224 2227 1124 598 -206 C ATOM 851 CD1 LEU A 122 -133.990-101.606 655.770 1.00 30.94 C ANISOU 851 CD1 LEU A 122 4810 4416 2530 989 703 -251 C ATOM 852 CD2 LEU A 122 -132.939-101.451 658.043 1.00 26.49 C ANISOU 852 CD2 LEU A 122 4460 3846 1759 1164 606 -200 C ATOM 853 N THR A 123 -130.519-105.708 656.154 1.00 27.13 N ANISOU 853 N THR A 123 4734 3758 1816 1361 653 -4 N ATOM 854 CA THR A 123 -130.352-107.133 656.355 1.00 29.84 C ANISOU 854 CA THR A 123 5236 3994 2107 1422 737 69 C ATOM 855 C THR A 123 -129.059-107.447 657.113 1.00 36.82 C ANISOU 855 C THR A 123 6231 4884 2876 1605 624 120 C ATOM 856 O THR A 123 -129.082-108.199 658.087 1.00 40.77 O ANISOU 856 O THR A 123 6908 5300 3283 1676 674 187 O ATOM 857 CB THR A 123 -130.385-107.875 655.025 1.00 25.65 C ANISOU 857 CB THR A 123 4645 3432 1668 1371 798 58 C ATOM 858 OG1 THR A 123 -131.697-107.748 654.474 1.00 41.27 O ANISOU 858 OG1 THR A 123 6538 5394 3747 1201 913 13 O ATOM 859 CG2 THR A 123 -130.092-109.333 655.230 1.00 31.22 C ANISOU 859 CG2 THR A 123 5531 4016 2315 1453 878 132 C ATOM 860 N ILE A 124 -127.943-106.852 656.709 1.00 37.58 N ANISOU 860 N ILE A 124 6216 5084 2978 1681 468 84 N ATOM 861 CA ILE A 124 -126.678-107.146 657.381 1.00 39.26 C ANISOU 861 CA ILE A 124 6504 5318 3095 1855 346 117 C ATOM 862 C ILE A 124 -126.645-106.586 658.806 1.00 41.56 C ANISOU 862 C ILE A 124 6867 5625 3300 1902 292 123 C ATOM 863 O ILE A 124 -126.140-107.241 659.719 1.00 45.95 O ANISOU 863 O ILE A 124 7564 6136 3759 2025 271 177 O ATOM 864 CB ILE A 124 -125.485-106.603 656.589 1.00 37.29 C ANISOU 864 CB ILE A 124 6091 5192 2888 1909 189 64 C ATOM 865 CG1 ILE A 124 -125.495-107.196 655.180 1.00 34.45 C ANISOU 865 CG1 ILE A 124 5661 4824 2604 1868 248 52 C ATOM 866 CG2 ILE A 124 -124.178-106.940 657.299 1.00 28.35 C ANISOU 866 CG2 ILE A 124 5011 4086 1674 2084 60 85 C ATOM 867 CD1 ILE A 124 -124.409-106.663 654.278 1.00 33.60 C ANISOU 867 CD1 ILE A 124 5376 4846 2543 1900 109 -6 C ATOM 868 N ASP A 125 -127.195-105.388 658.994 1.00 39.63 N ANISOU 868 N ASP A 125 6529 5440 3089 1806 271 65 N ATOM 869 CA ASP A 125 -127.242-104.755 660.310 1.00 39.67 C ANISOU 869 CA ASP A 125 6592 5467 3015 1837 227 56 C ATOM 870 C ASP A 125 -127.982-105.616 661.320 1.00 39.69 C ANISOU 870 C ASP A 125 6787 5363 2929 1849 357 127 C ATOM 871 O ASP A 125 -127.593-105.686 662.483 1.00 41.77 O ANISOU 871 O ASP A 125 7157 5626 3090 1942 313 152 O ATOM 872 CB ASP A 125 -127.904-103.376 660.226 1.00 43.04 C ANISOU 872 CB ASP A 125 6895 5958 3501 1722 211 -22 C ATOM 873 CG ASP A 125 -128.432-102.890 661.573 1.00 48.15 C ANISOU 873 CG ASP A 125 7629 6601 4067 1721 231 -28 C ATOM 874 OD1 ASP A 125 -127.644-102.323 662.359 1.00 48.07 O ANISOU 874 OD1 ASP A 125 7621 6646 3996 1800 109 -54 O ATOM 875 OD2 ASP A 125 -129.643-103.062 661.840 1.00 49.74 O ANISOU 875 OD2 ASP A 125 7886 6747 4267 1635 372 -15 O ATOM 876 N ARG A 126 -129.053-106.267 660.876 1.00 39.77 N ANISOU 876 N ARG A 126 6839 5289 2984 1747 521 155 N ATOM 877 CA ARG A 126 -129.832-107.123 661.762 1.00 43.47 C ANISOU 877 CA ARG A 126 7487 5650 3381 1736 663 222 C ATOM 878 C ARG A 126 -129.138-108.469 661.924 1.00 46.51 C ANISOU 878 C ARG A 126 8035 5940 3698 1863 679 308 C ATOM 879 O ARG A 126 -129.197-109.086 662.985 1.00 50.20 O ANISOU 879 O ARG A 126 8675 6337 4062 1928 725 371 O ATOM 880 CB ARG A 126 -131.254-107.303 661.229 1.00 44.95 C ANISOU 880 CB ARG A 126 7640 5785 3653 1565 833 207 C ATOM 881 CG ARG A 126 -132.177-108.096 662.142 1.00 50.10 C ANISOU 881 CG ARG A 126 8459 6335 4242 1526 991 265 C ATOM 882 CD ARG A 126 -132.088-107.611 663.581 1.00 57.34 C ANISOU 882 CD ARG A 126 9464 7286 5038 1591 948 275 C ATOM 883 NE ARG A 126 -132.341-106.179 663.713 1.00 61.65 N ANISOU 883 NE ARG A 126 9866 7947 5611 1539 874 187 N ATOM 884 CZ ARG A 126 -132.253-105.516 664.862 1.00 66.49 C ANISOU 884 CZ ARG A 126 10521 8612 6132 1585 821 171 C ATOM 885 NH1 ARG A 126 -131.918-106.158 665.973 1.00 68.99 N ANISOU 885 NH1 ARG A 126 11012 8883 6319 1683 829 239 N ATOM 886 NH2 ARG A 126 -132.500-104.213 664.906 1.00 66.69 N ANISOU 886 NH2 ARG A 126 10420 8730 6190 1536 761 85 N ATOM 887 N TYR A 127 -128.469-108.910 660.865 1.00 44.82 N ANISOU 887 N TYR A 127 7766 5725 3539 1904 640 308 N ATOM 888 CA TYR A 127 -127.682-110.136 660.904 1.00 44.70 C ANISOU 888 CA TYR A 127 7893 5627 3466 2045 638 379 C ATOM 889 C TYR A 127 -126.620-110.036 661.993 1.00 43.78 C ANISOU 889 C TYR A 127 7840 5553 3240 2212 499 395 C ATOM 890 O TYR A 127 -126.509-110.916 662.849 1.00 43.93 O ANISOU 890 O TYR A 127 8046 5481 3165 2304 542 467 O ATOM 891 CB TYR A 127 -127.031-110.402 659.537 1.00 41.15 C ANISOU 891 CB TYR A 127 7337 5205 3095 2068 594 354 C ATOM 892 CG TYR A 127 -126.108-111.604 659.520 1.00 43.32 C ANISOU 892 CG TYR A 127 7744 5405 3311 2234 574 417 C ATOM 893 CD1 TYR A 127 -126.622-112.897 659.461 1.00 45.95 C ANISOU 893 CD1 TYR A 127 8259 5573 3628 2231 734 490 C ATOM 894 CD2 TYR A 127 -124.725-111.450 659.550 1.00 41.40 C ANISOU 894 CD2 TYR A 127 7437 5254 3040 2388 399 395 C ATOM 895 CE1 TYR A 127 -125.792-114.000 659.441 1.00 47.09 C ANISOU 895 CE1 TYR A 127 8534 5636 3721 2389 717 547 C ATOM 896 CE2 TYR A 127 -123.882-112.556 659.535 1.00 44.17 C ANISOU 896 CE2 TYR A 127 7896 5540 3345 2545 377 443 C ATOM 897 CZ TYR A 127 -124.425-113.827 659.482 1.00 49.19 C ANISOU 897 CZ TYR A 127 8729 6003 3959 2552 535 523 C ATOM 898 OH TYR A 127 -123.604-114.934 659.468 1.00 57.05 O ANISOU 898 OH TYR A 127 9839 6924 4915 2710 515 568 O ATOM 899 N LEU A 128 -125.856-108.948 661.957 1.00 41.75 N ANISOU 899 N LEU A 128 7423 5436 3002 2240 335 322 N ATOM 900 CA LEU A 128 -124.801-108.708 662.930 1.00 45.32 C ANISOU 900 CA LEU A 128 7895 5953 3370 2378 191 312 C ATOM 901 C LEU A 128 -125.356-108.697 664.343 1.00 50.73 C ANISOU 901 C LEU A 128 8729 6599 3947 2385 243 348 C ATOM 902 O LEU A 128 -124.731-109.210 665.267 1.00 54.88 O ANISOU 902 O LEU A 128 9374 7106 4370 2515 197 387 O ATOM 903 CB LEU A 128 -124.092-107.383 662.651 1.00 46.81 C ANISOU 903 CB LEU A 128 7873 6295 3616 2359 29 213 C ATOM 904 CG LEU A 128 -123.249-107.263 661.383 1.00 47.40 C ANISOU 904 CG LEU A 128 7779 6443 3788 2369 -59 165 C ATOM 905 CD1 LEU A 128 -122.635-105.864 661.289 1.00 44.35 C ANISOU 905 CD1 LEU A 128 7198 6196 3458 2327 -204 67 C ATOM 906 CD2 LEU A 128 -122.180-108.352 661.336 1.00 48.83 C ANISOU 906 CD2 LEU A 128 8021 6600 3932 2526 -107 199 C ATOM 907 N ALA A 129 -126.536-108.110 664.508 1.00 48.80 N ANISOU 907 N ALA A 129 8471 6347 3722 2244 340 332 N ATOM 908 CA ALA A 129 -127.145-108.001 665.829 1.00 46.46 C ANISOU 908 CA ALA A 129 8301 6029 3324 2236 396 357 C ATOM 909 C ALA A 129 -127.524-109.370 666.389 1.00 48.66 C ANISOU 909 C ALA A 129 8803 6165 3521 2280 532 461 C ATOM 910 O ALA A 129 -127.440-109.600 667.594 1.00 54.84 O ANISOU 910 O ALA A 129 9724 6929 4183 2353 531 501 O ATOM 911 CB ALA A 129 -128.366-107.093 665.775 1.00 43.11 C ANISOU 911 CB ALA A 129 7795 5634 2951 2071 479 306 C ATOM 912 N VAL A 130 -127.930-110.280 665.513 1.00 46.32 N ANISOU 912 N VAL A 130 8547 5764 3288 2234 649 503 N ATOM 913 CA VAL A 130 -128.431-111.574 665.953 1.00 49.35 C ANISOU 913 CA VAL A 130 9146 5991 3612 2247 802 598 C ATOM 914 C VAL A 130 -127.318-112.617 666.050 1.00 55.64 C ANISOU 914 C VAL A 130 10067 6727 4349 2428 741 657 C ATOM 915 O VAL A 130 -127.273-113.392 667.000 1.00 62.54 O ANISOU 915 O VAL A 130 11133 7516 5115 2508 786 730 O ATOM 916 CB VAL A 130 -129.542-112.081 665.014 1.00 45.32 C ANISOU 916 CB VAL A 130 8628 5386 3207 2087 980 606 C ATOM 917 CG1 VAL A 130 -129.944-113.501 665.367 1.00 48.36 C ANISOU 917 CG1 VAL A 130 9240 5593 3542 2100 1138 701 C ATOM 918 CG2 VAL A 130 -130.744-111.164 665.092 1.00 42.52 C ANISOU 918 CG2 VAL A 130 8166 5089 2903 1912 1055 547 C ATOM 919 N VAL A 131 -126.405-112.617 665.085 1.00 55.56 N ANISOU 919 N VAL A 131 9942 6765 4404 2494 635 623 N ATOM 920 CA VAL A 131 -125.394-113.672 664.989 1.00 53.80 C ANISOU 920 CA VAL A 131 9818 6482 4141 2659 588 668 C ATOM 921 C VAL A 131 -124.068-113.322 665.669 1.00 57.10 C ANISOU 921 C VAL A 131 10193 7016 4488 2823 393 637 C ATOM 922 O VAL A 131 -123.490-114.152 666.366 1.00 66.73 O ANISOU 922 O VAL A 131 11560 8181 5613 2961 373 691 O ATOM 923 CB VAL A 131 -125.122-114.027 663.514 1.00 49.25 C ANISOU 923 CB VAL A 131 9148 5891 3675 2646 594 647 C ATOM 924 CG1 VAL A 131 -123.991-115.025 663.401 1.00 47.88 C ANISOU 924 CG1 VAL A 131 9051 5676 3463 2825 527 679 C ATOM 925 CG2 VAL A 131 -126.383-114.568 662.867 1.00 45.13 C ANISOU 925 CG2 VAL A 131 8689 5239 3220 2490 797 680 C ATOM 926 N HIS A 132 -123.578-112.105 665.465 1.00 55.51 N ANISOU 926 N HIS A 132 9785 6973 4333 2801 252 546 N ATOM 927 CA HIS A 132 -122.361-111.663 666.143 1.00 63.33 C ANISOU 927 CA HIS A 132 10714 8083 5265 2929 71 500 C ATOM 928 C HIS A 132 -122.657-110.524 667.118 1.00 66.92 C ANISOU 928 C HIS A 132 11130 8627 5670 2876 23 458 C ATOM 929 O HIS A 132 -122.218-109.391 666.908 1.00 67.94 O ANISOU 929 O HIS A 132 11075 8887 5854 2839 -96 368 O ATOM 930 CB HIS A 132 -121.304-111.207 665.137 1.00 66.41 C ANISOU 930 CB HIS A 132 10888 8592 5752 2956 -69 417 C ATOM 931 CG HIS A 132 -121.024-112.199 664.053 1.00 70.20 C ANISOU 931 CG HIS A 132 11379 9004 6289 2997 -26 443 C ATOM 932 ND1 HIS A 132 -121.876-112.400 662.988 1.00 70.23 N ANISOU 932 ND1 HIS A 132 11367 8938 6379 2884 96 459 N ATOM 933 CD2 HIS A 132 -119.974-113.030 663.857 1.00 73.38 C ANISOU 933 CD2 HIS A 132 11800 9403 6677 3139 -91 451 C ATOM 934 CE1 HIS A 132 -121.366-113.317 662.186 1.00 70.57 C ANISOU 934 CE1 HIS A 132 11427 8932 6453 2957 106 478 C ATOM 935 NE2 HIS A 132 -120.214-113.717 662.692 1.00 73.63 N ANISOU 935 NE2 HIS A 132 11833 9359 6783 3112 -7 472 N ATOM 936 N ALA A 133 -123.394-110.828 668.182 1.00 67.14 N ANISOU 936 N ALA A 133 11335 8582 5594 2869 119 521 N ATOM 937 CA ALA A 133 -123.863-109.802 669.108 1.00 66.17 C ANISOU 937 CA ALA A 133 11193 8531 5417 2807 101 484 C ATOM 938 C ALA A 133 -122.725-108.988 669.732 1.00 66.04 C ANISOU 938 C ALA A 133 11077 8658 5356 2899 -92 411 C ATOM 939 O ALA A 133 -122.844-107.768 669.884 1.00 63.82 O ANISOU 939 O ALA A 133 10672 8475 5102 2823 -153 333 O ATOM 940 CB ALA A 133 -124.708-110.435 670.197 1.00 66.37 C ANISOU 940 CB ALA A 133 11439 8456 5323 2804 236 570 C ATOM 941 N VAL A 134 -121.629-109.657 670.088 1.00 67.38 N ANISOU 941 N VAL A 134 11301 8838 5462 3058 -184 432 N ATOM 942 CA VAL A 134 -120.519-108.992 670.768 1.00 68.51 C ANISOU 942 CA VAL A 134 11360 9116 5555 3148 -362 363 C ATOM 943 C VAL A 134 -119.783-108.019 669.847 1.00 69.88 C ANISOU 943 C VAL A 134 11281 9412 5859 3098 -488 252 C ATOM 944 O VAL A 134 -119.499-106.887 670.242 1.00 71.74 O ANISOU 944 O VAL A 134 11405 9757 6097 3062 -587 171 O ATOM 945 CB VAL A 134 -119.507-110.006 671.334 1.00 70.90 C ANISOU 945 CB VAL A 134 11776 9403 5759 3334 -430 411 C ATOM 946 N PHE A 135 -119.478-108.455 668.626 1.00 68.18 N ANISOU 946 N PHE A 135 10981 9177 5749 3091 -479 248 N ATOM 947 CA PHE A 135 -118.816-107.589 667.646 1.00 63.75 C ANISOU 947 CA PHE A 135 10180 8726 5317 3030 -582 149 C ATOM 948 C PHE A 135 -119.665-106.368 667.286 1.00 61.74 C ANISOU 948 C PHE A 135 9813 8504 5141 2862 -552 94 C ATOM 949 O PHE A 135 -119.144-105.272 667.044 1.00 59.82 O ANISOU 949 O PHE A 135 9394 8369 4965 2806 -658 1 O ATOM 950 CB PHE A 135 -118.487-108.374 666.377 1.00 58.41 C ANISOU 950 CB PHE A 135 9451 8013 4731 3047 -555 164 C ATOM 951 CG PHE A 135 -117.993-107.518 665.247 1.00 55.43 C ANISOU 951 CG PHE A 135 8833 7737 4491 2958 -631 71 C ATOM 952 CD1 PHE A 135 -116.650-107.193 665.143 1.00 57.18 C ANISOU 952 CD1 PHE A 135 8905 8077 4743 3012 -777 -4 C ATOM 953 CD2 PHE A 135 -118.872-107.035 664.286 1.00 54.56 C ANISOU 953 CD2 PHE A 135 8644 7606 4479 2815 -553 60 C ATOM 954 CE1 PHE A 135 -116.189-106.402 664.101 1.00 57.68 C ANISOU 954 CE1 PHE A 135 8750 8230 4935 2916 -836 -86 C ATOM 955 CE2 PHE A 135 -118.420-106.245 663.242 1.00 54.15 C ANISOU 955 CE2 PHE A 135 8378 7647 4550 2730 -620 -19 C ATOM 956 CZ PHE A 135 -117.077-105.927 663.148 1.00 55.34 C ANISOU 956 CZ PHE A 135 8385 7909 4733 2776 -758 -91 C ATOM 957 N ALA A 136 -120.977-106.572 667.250 1.00 62.72 N ANISOU 957 N ALA A 136 10043 8531 5258 2778 -402 152 N ATOM 958 CA ALA A 136 -121.920-105.532 666.858 1.00 62.56 C ANISOU 958 CA ALA A 136 9929 8529 5311 2620 -353 106 C ATOM 959 C ALA A 136 -122.032-104.403 667.883 1.00 67.18 C ANISOU 959 C ALA A 136 10497 9188 5840 2590 -415 48 C ATOM 960 O ALA A 136 -122.764-103.436 667.663 1.00 67.67 O ANISOU 960 O ALA A 136 10482 9273 5957 2467 -387 -1 O ATOM 961 CB ALA A 136 -123.289-106.149 666.612 1.00 63.35 C ANISOU 961 CB ALA A 136 10148 8507 5412 2537 -167 181 C ATOM 962 N LEU A 137 -121.319-104.524 669.001 1.00 67.84 N ANISOU 962 N LEU A 137 10654 9310 5813 2704 -498 49 N ATOM 963 CA LEU A 137 -121.350-103.492 670.029 1.00 67.57 C ANISOU 963 CA LEU A 137 10611 9350 5713 2686 -562 -10 C ATOM 964 C LEU A 137 -120.782-102.163 669.511 1.00 65.53 C ANISOU 964 C LEU A 137 10141 9197 5559 2612 -684 -127 C ATOM 965 O LEU A 137 -121.488-101.154 669.464 1.00 63.50 O ANISOU 965 O LEU A 137 9829 8957 5342 2501 -660 -178 O ATOM 966 CB LEU A 137 -120.581-103.955 671.270 1.00 67.31 C ANISOU 966 CB LEU A 137 10694 9345 5536 2834 -638 13 C ATOM 967 N LYS A 138 -119.511-102.171 669.113 1.00 65.18 N ANISOU 967 N LYS A 138 9979 9223 5562 2669 -807 -170 N ATOM 968 CA LYS A 138 -118.839-100.954 668.654 1.00 62.29 C ANISOU 968 CA LYS A 138 9416 8956 5296 2595 -923 -279 C ATOM 969 C LYS A 138 -119.079-100.714 667.165 1.00 61.33 C ANISOU 969 C LYS A 138 9157 8821 5327 2485 -885 -296 C ATOM 970 O LYS A 138 -118.865 -99.613 666.655 1.00 61.36 O ANISOU 970 O LYS A 138 9008 8881 5425 2387 -945 -376 O ATOM 971 CB LYS A 138 -117.334-101.040 668.937 1.00 62.74 C ANISOU 971 CB LYS A 138 9399 9104 5336 2693 -1068 -324 C ATOM 972 CG LYS A 138 -116.775 -99.884 669.755 1.00 63.71 C ANISOU 972 CG LYS A 138 9454 9324 5429 2677 -1189 -419 C ATOM 973 N ALA A 139 -119.531-101.754 666.474 1.00 59.69 N ANISOU 973 N ALA A 139 9009 8532 5138 2499 -783 -218 N ATOM 974 CA ALA A 139 -119.699-101.694 665.030 1.00 55.20 C ANISOU 974 CA ALA A 139 8317 7955 4701 2411 -747 -227 C ATOM 975 C ALA A 139 -121.036-101.085 664.634 1.00 51.30 C ANISOU 975 C ALA A 139 7821 7417 4254 2279 -646 -227 C ATOM 976 O ALA A 139 -121.175-100.550 663.534 1.00 49.86 O ANISOU 976 O ALA A 139 7506 7254 4184 2182 -645 -263 O ATOM 977 CB ALA A 139 -119.555-103.089 664.425 1.00 55.75 C ANISOU 977 CB ALA A 139 8451 7962 4770 2487 -685 -152 C ATOM 978 N ARG A 140 -122.022-101.167 665.521 1.00 48.11 N ANISOU 978 N ARG A 140 7561 6957 3762 2274 -559 -189 N ATOM 979 CA ARG A 140 -123.353-100.669 665.188 1.00 43.92 C ANISOU 979 CA ARG A 140 7031 6385 3273 2151 -449 -192 C ATOM 980 C ARG A 140 -123.599 -99.277 665.774 1.00 45.08 C ANISOU 980 C ARG A 140 7126 6585 3416 2088 -501 -275 C ATOM 981 O ARG A 140 -124.741 -98.870 665.994 1.00 47.63 O ANISOU 981 O ARG A 140 7490 6876 3731 2012 -409 -281 O ATOM 982 CB ARG A 140 -124.425-101.667 665.641 1.00 42.38 C ANISOU 982 CB ARG A 140 7015 6088 3000 2157 -290 -101 C ATOM 983 CG ARG A 140 -124.378-102.966 664.825 1.00 42.68 C ANISOU 983 CG ARG A 140 7099 6054 3065 2191 -217 -25 C ATOM 984 CD ARG A 140 -125.529-103.931 665.097 1.00 43.92 C ANISOU 984 CD ARG A 140 7421 6095 3171 2164 -39 60 C ATOM 985 NE ARG A 140 -126.842-103.386 664.764 1.00 46.86 N ANISOU 985 NE ARG A 140 7757 6448 3601 2016 74 37 N ATOM 986 CZ ARG A 140 -127.814-103.196 665.651 1.00 50.76 C ANISOU 986 CZ ARG A 140 8338 6915 4033 1966 167 44 C ATOM 987 NH1 ARG A 140 -127.624-103.515 666.926 1.00 52.42 N ANISOU 987 NH1 ARG A 140 8689 7114 4116 2051 161 80 N ATOM 988 NH2 ARG A 140 -128.980-102.697 665.265 1.00 52.37 N ANISOU 988 NH2 ARG A 140 8484 7111 4303 1831 269 11 N ATOM 989 N THR A 141 -122.510 -98.547 665.994 1.00 43.92 N ANISOU 989 N THR A 141 6884 6521 3284 2114 -646 -347 N ATOM 990 CA THR A 141 -122.565 -97.148 666.401 1.00 46.20 C ANISOU 990 CA THR A 141 7106 6860 3588 2051 -713 -439 C ATOM 991 C THR A 141 -123.321 -96.317 665.351 1.00 48.65 C ANISOU 991 C THR A 141 7311 7156 4017 1923 -671 -478 C ATOM 992 O THR A 141 -123.143 -96.519 664.147 1.00 51.31 O ANISOU 992 O THR A 141 7553 7491 4453 1883 -666 -466 O ATOM 993 CB THR A 141 -121.134 -96.580 666.606 1.00 57.20 C ANISOU 993 CB THR A 141 8394 8341 4998 2087 -874 -510 C ATOM 994 OG1 THR A 141 -120.420 -97.382 667.556 1.00 55.61 O ANISOU 994 OG1 THR A 141 8287 8158 4684 2216 -918 -476 O ATOM 995 CG2 THR A 141 -121.185 -95.167 667.121 1.00 60.56 C ANISOU 995 CG2 THR A 141 8771 8807 5431 2024 -941 -607 C ATOM 996 N VAL A 142 -124.174 -95.400 665.799 1.00 48.04 N ANISOU 996 N VAL A 142 7253 7070 3928 1862 -639 -525 N ATOM 997 CA VAL A 142 -124.912 -94.529 664.881 1.00 46.39 C ANISOU 997 CA VAL A 142 6950 6847 3827 1751 -606 -570 C ATOM 998 C VAL A 142 -123.952 -93.730 663.997 1.00 47.00 C ANISOU 998 C VAL A 142 6866 6975 4018 1705 -725 -631 C ATOM 999 O VAL A 142 -124.211 -93.517 662.809 1.00 48.80 O ANISOU 999 O VAL A 142 7001 7192 4349 1631 -703 -634 O ATOM 1000 CB VAL A 142 -125.850 -93.571 665.649 1.00 44.51 C ANISOU 1000 CB VAL A 142 6759 6599 3555 1710 -569 -628 C ATOM 1001 CG1 VAL A 142 -126.293 -92.409 664.772 1.00 29.86 C ANISOU 1001 CG1 VAL A 142 4789 4740 1816 1613 -581 -699 C ATOM 1002 CG2 VAL A 142 -127.057 -94.335 666.167 1.00 39.07 C ANISOU 1002 CG2 VAL A 142 6200 5854 2789 1712 -412 -566 C ATOM 1003 N THR A 143 -122.840 -93.307 664.591 1.00 46.23 N ANISOU 1003 N THR A 143 6735 6933 3898 1742 -848 -681 N ATOM 1004 CA THR A 143 -121.733 -92.699 663.861 1.00 43.25 C ANISOU 1004 CA THR A 143 6205 6605 3621 1695 -958 -733 C ATOM 1005 C THR A 143 -121.375 -93.496 662.611 1.00 42.55 C ANISOU 1005 C THR A 143 6039 6516 3610 1683 -934 -679 C ATOM 1006 O THR A 143 -121.354 -92.956 661.508 1.00 43.50 O ANISOU 1006 O THR A 143 6044 6640 3842 1593 -943 -700 O ATOM 1007 CB THR A 143 -120.489 -92.591 664.754 1.00 46.40 C ANISOU 1007 CB THR A 143 6595 7069 3966 1758 -1075 -774 C ATOM 1008 OG1 THR A 143 -120.721 -91.605 665.763 1.00 52.70 O ANISOU 1008 OG1 THR A 143 7436 7876 4711 1747 -1115 -846 O ATOM 1009 CG2 THR A 143 -119.262 -92.202 663.948 1.00 43.86 C ANISOU 1009 CG2 THR A 143 6114 6801 3750 1706 -1171 -815 C ATOM 1010 N PHE A 144 -121.102 -94.784 662.787 1.00 42.73 N ANISOU 1010 N PHE A 144 6131 6533 3571 1777 -902 -609 N ATOM 1011 CA PHE A 144 -120.746 -95.638 661.660 1.00 43.62 C ANISOU 1011 CA PHE A 144 6181 6645 3747 1780 -876 -562 C ATOM 1012 C PHE A 144 -121.926 -95.860 660.720 1.00 39.93 C ANISOU 1012 C PHE A 144 5721 6123 3327 1714 -761 -521 C ATOM 1013 O PHE A 144 -121.736 -96.040 659.524 1.00 40.67 O ANISOU 1013 O PHE A 144 5717 6229 3507 1668 -752 -511 O ATOM 1014 CB PHE A 144 -120.196 -96.976 662.153 1.00 47.18 C ANISOU 1014 CB PHE A 144 6722 7091 4112 1909 -869 -501 C ATOM 1015 CG PHE A 144 -118.775 -96.897 662.641 1.00 53.39 C ANISOU 1015 CG PHE A 144 7451 7951 4882 1970 -992 -544 C ATOM 1016 CD1 PHE A 144 -117.897 -95.969 662.101 1.00 55.27 C ANISOU 1016 CD1 PHE A 144 7527 8254 5218 1890 -1083 -616 C ATOM 1017 CD2 PHE A 144 -118.318 -97.740 663.643 1.00 57.15 C ANISOU 1017 CD2 PHE A 144 8037 8431 5246 2102 -1013 -511 C ATOM 1018 CE1 PHE A 144 -116.583 -95.887 662.548 1.00 58.73 C ANISOU 1018 CE1 PHE A 144 7905 8766 5643 1937 -1191 -661 C ATOM 1019 CE2 PHE A 144 -117.007 -97.664 664.093 1.00 58.96 C ANISOU 1019 CE2 PHE A 144 8206 8737 5458 2161 -1130 -556 C ATOM 1020 CZ PHE A 144 -116.139 -96.737 663.544 1.00 58.88 C ANISOU 1020 CZ PHE A 144 8025 8798 5548 2076 -1218 -634 C ATOM 1021 N GLY A 145 -123.142 -95.838 661.252 1.00 37.60 N ANISOU 1021 N GLY A 145 5536 5776 2976 1705 -669 -502 N ATOM 1022 CA GLY A 145 -124.318 -95.912 660.407 1.00 34.95 C ANISOU 1022 CA GLY A 145 5195 5395 2689 1630 -558 -478 C ATOM 1023 C GLY A 145 -124.327 -94.767 659.413 1.00 34.74 C ANISOU 1023 C GLY A 145 5024 5398 2778 1528 -607 -540 C ATOM 1024 O GLY A 145 -124.619 -94.944 658.230 1.00 35.51 O ANISOU 1024 O GLY A 145 5050 5493 2948 1473 -565 -523 O ATOM 1025 N VAL A 146 -123.978 -93.583 659.895 1.00 33.90 N ANISOU 1025 N VAL A 146 4877 5318 2686 1502 -696 -612 N ATOM 1026 CA VAL A 146 -123.994 -92.396 659.062 1.00 32.69 C ANISOU 1026 CA VAL A 146 4604 5178 2640 1403 -745 -671 C ATOM 1027 C VAL A 146 -122.921 -92.433 657.980 1.00 34.23 C ANISOU 1027 C VAL A 146 4662 5416 2928 1360 -809 -667 C ATOM 1028 O VAL A 146 -123.216 -92.190 656.813 1.00 36.75 O ANISOU 1028 O VAL A 146 4897 5733 3334 1284 -787 -661 O ATOM 1029 CB VAL A 146 -123.827 -91.133 659.914 1.00 34.99 C ANISOU 1029 CB VAL A 146 4898 5475 2921 1385 -824 -752 C ATOM 1030 CG1 VAL A 146 -123.722 -89.900 659.029 1.00 32.78 C ANISOU 1030 CG1 VAL A 146 4501 5196 2759 1281 -882 -809 C ATOM 1031 CG2 VAL A 146 -124.999 -91.005 660.867 1.00 26.30 C ANISOU 1031 CG2 VAL A 146 3921 4333 1739 1413 -747 -762 C ATOM 1032 N VAL A 147 -121.680 -92.744 658.348 1.00 34.66 N ANISOU 1032 N VAL A 147 4691 5513 2967 1406 -883 -671 N ATOM 1033 CA VAL A 147 -120.611 -92.772 657.352 1.00 32.30 C ANISOU 1033 CA VAL A 147 4256 5259 2760 1358 -933 -671 C ATOM 1034 C VAL A 147 -120.890 -93.866 656.316 1.00 32.60 C ANISOU 1034 C VAL A 147 4277 5289 2819 1368 -853 -606 C ATOM 1035 O VAL A 147 -120.613 -93.689 655.126 1.00 33.67 O ANISOU 1035 O VAL A 147 4298 5445 3049 1289 -854 -603 O ATOM 1036 CB VAL A 147 -119.204 -92.972 657.995 1.00 43.71 C ANISOU 1036 CB VAL A 147 5673 6758 4176 1414 -1022 -695 C ATOM 1037 CG1 VAL A 147 -118.998 -91.987 659.141 1.00 44.44 C ANISOU 1037 CG1 VAL A 147 5797 6860 4227 1414 -1097 -762 C ATOM 1038 CG2 VAL A 147 -119.000 -94.392 658.487 1.00 45.50 C ANISOU 1038 CG2 VAL A 147 5990 6986 4311 1545 -990 -640 C ATOM 1039 N THR A 148 -121.476 -94.975 656.756 1.00 29.05 N ANISOU 1039 N THR A 148 3949 4807 2282 1458 -778 -553 N ATOM 1040 CA THR A 148 -121.811 -96.062 655.848 1.00 28.23 C ANISOU 1040 CA THR A 148 3847 4690 2188 1473 -697 -495 C ATOM 1041 C THR A 148 -122.854 -95.591 654.843 1.00 30.83 C ANISOU 1041 C THR A 148 4128 5004 2583 1374 -636 -496 C ATOM 1042 O THR A 148 -122.745 -95.874 653.647 1.00 32.79 O ANISOU 1042 O THR A 148 4287 5275 2896 1329 -617 -480 O ATOM 1043 CB THR A 148 -122.330 -97.294 656.608 1.00 31.16 C ANISOU 1043 CB THR A 148 4383 5009 2448 1580 -617 -433 C ATOM 1044 OG1 THR A 148 -121.273 -97.837 657.405 1.00 34.34 O ANISOU 1044 OG1 THR A 148 4824 5431 2792 1684 -680 -427 O ATOM 1045 CG2 THR A 148 -122.815 -98.360 655.643 1.00 32.50 C ANISOU 1045 CG2 THR A 148 4566 5152 2629 1582 -521 -378 C ATOM 1046 N SER A 149 -123.850 -94.853 655.331 1.00 30.59 N ANISOU 1046 N SER A 149 4151 4939 2531 1343 -606 -521 N ATOM 1047 CA SER A 149 -124.896 -94.297 654.475 1.00 21.13 C ANISOU 1047 CA SER A 149 2908 3729 1391 1256 -552 -533 C ATOM 1048 C SER A 149 -124.320 -93.348 653.438 1.00 27.42 C ANISOU 1048 C SER A 149 3552 4563 2302 1162 -630 -564 C ATOM 1049 O SER A 149 -124.722 -93.373 652.267 1.00 26.14 O ANISOU 1049 O SER A 149 3317 4414 2202 1100 -595 -548 O ATOM 1050 CB SER A 149 -125.946 -93.573 655.309 1.00 21.37 C ANISOU 1050 CB SER A 149 3019 3717 1383 1249 -515 -569 C ATOM 1051 OG SER A 149 -126.502 -94.454 656.267 1.00 22.16 O ANISOU 1051 OG SER A 149 3259 3773 1388 1315 -425 -530 O ATOM 1052 N VAL A 150 -123.378 -92.517 653.874 1.00 26.82 N ANISOU 1052 N VAL A 150 3433 4503 2255 1144 -729 -605 N ATOM 1053 CA VAL A 150 -122.741 -91.541 652.990 1.00 27.77 C ANISOU 1053 CA VAL A 150 3422 4640 2488 1037 -793 -627 C ATOM 1054 C VAL A 150 -121.993 -92.235 651.863 1.00 25.16 C ANISOU 1054 C VAL A 150 2995 4349 2216 1006 -779 -587 C ATOM 1055 O VAL A 150 -122.194 -91.932 650.692 1.00 25.04 O ANISOU 1055 O VAL A 150 2895 4337 2281 920 -758 -570 O ATOM 1056 CB VAL A 150 -121.770 -90.625 653.767 1.00 29.47 C ANISOU 1056 CB VAL A 150 3620 4865 2712 1021 -892 -681 C ATOM 1057 CG1 VAL A 150 -120.833 -89.902 652.812 1.00 21.85 C ANISOU 1057 CG1 VAL A 150 2524 3920 1857 909 -944 -687 C ATOM 1058 CG2 VAL A 150 -122.555 -89.628 654.599 1.00 26.36 C ANISOU 1058 CG2 VAL A 150 3297 4429 2288 1021 -911 -735 C ATOM 1059 N ILE A 151 -121.131 -93.171 652.229 1.00 25.95 N ANISOU 1059 N ILE A 151 3111 4478 2272 1083 -789 -572 N ATOM 1060 CA ILE A 151 -120.442 -93.995 651.248 1.00 29.55 C ANISOU 1060 CA ILE A 151 3488 4971 2768 1076 -768 -541 C ATOM 1061 C ILE A 151 -121.435 -94.666 650.296 1.00 30.58 C ANISOU 1061 C ILE A 151 3619 5093 2906 1066 -679 -501 C ATOM 1062 O ILE A 151 -121.247 -94.660 649.073 1.00 31.06 O ANISOU 1062 O ILE A 151 3580 5178 3042 990 -659 -487 O ATOM 1063 CB ILE A 151 -119.577 -95.060 651.942 1.00 26.25 C ANISOU 1063 CB ILE A 151 3117 4578 2280 1195 -787 -534 C ATOM 1064 CG1 ILE A 151 -118.461 -94.379 652.734 1.00 28.20 C ANISOU 1064 CG1 ILE A 151 3334 4853 2527 1195 -883 -581 C ATOM 1065 CG2 ILE A 151 -118.983 -96.018 650.925 1.00 24.46 C ANISOU 1065 CG2 ILE A 151 2820 4388 2086 1205 -757 -508 C ATOM 1066 CD1 ILE A 151 -117.712 -95.318 653.645 1.00 32.15 C ANISOU 1066 CD1 ILE A 151 3895 5377 2944 1327 -912 -579 C ATOM 1067 N THR A 152 -122.508 -95.217 650.854 1.00 30.63 N ANISOU 1067 N THR A 152 3742 5067 2829 1134 -619 -484 N ATOM 1068 CA THR A 152 -123.513 -95.906 650.044 1.00 28.66 C ANISOU 1068 CA THR A 152 3505 4815 2570 1124 -527 -452 C ATOM 1069 C THR A 152 -124.171 -94.978 649.009 1.00 26.64 C ANISOU 1069 C THR A 152 3153 4569 2402 1007 -520 -464 C ATOM 1070 O THR A 152 -124.443 -95.387 647.881 1.00 27.35 O ANISOU 1070 O THR A 152 3177 4668 2548 954 -462 -439 O ATOM 1071 CB THR A 152 -124.596 -96.540 650.941 1.00 24.61 C ANISOU 1071 CB THR A 152 3154 4247 1949 1194 -437 -436 C ATOM 1072 OG1 THR A 152 -123.970 -97.431 651.868 1.00 23.66 O ANISOU 1072 OG1 THR A 152 3131 4106 1752 1304 -444 -409 O ATOM 1073 CG2 THR A 152 -125.584 -97.330 650.116 1.00 18.42 C ANISOU 1073 CG2 THR A 152 2375 3410 1213 1142 -297 -401 C ATOM 1074 N TRP A 153 -124.427 -93.729 649.381 1.00 25.85 N ANISOU 1074 N TRP A 153 3047 4445 2332 959 -565 -497 N ATOM 1075 CA TRP A 153 -125.009 -92.792 648.423 1.00 25.38 C ANISOU 1075 CA TRP A 153 2903 4383 2359 857 -567 -502 C ATOM 1076 C TRP A 153 -124.018 -92.482 647.300 1.00 27.04 C ANISOU 1076 C TRP A 153 2990 4612 2672 764 -595 -481 C ATOM 1077 O TRP A 153 -124.385 -92.427 646.127 1.00 29.94 O ANISOU 1077 O TRP A 153 3288 4990 3100 693 -557 -455 O ATOM 1078 CB TRP A 153 -125.444 -91.507 649.122 1.00 22.69 C ANISOU 1078 CB TRP A 153 2596 4001 2024 839 -616 -547 C ATOM 1079 CG TRP A 153 -126.791 -91.594 649.765 1.00 17.62 C ANISOU 1079 CG TRP A 153 2053 3296 1347 869 -524 -556 C ATOM 1080 CD1 TRP A 153 -127.059 -91.638 651.098 1.00 19.12 C ANISOU 1080 CD1 TRP A 153 2359 3462 1444 945 -515 -586 C ATOM 1081 CD2 TRP A 153 -128.055 -91.654 649.098 1.00 17.00 C ANISOU 1081 CD2 TRP A 153 1958 3179 1322 823 -424 -539 C ATOM 1082 NE1 TRP A 153 -128.413 -91.714 651.307 1.00 20.17 N ANISOU 1082 NE1 TRP A 153 2548 3543 1574 943 -407 -590 N ATOM 1083 CE2 TRP A 153 -129.047 -91.728 650.092 1.00 22.56 C ANISOU 1083 CE2 TRP A 153 2765 3837 1969 869 -353 -563 C ATOM 1084 CE3 TRP A 153 -128.445 -91.650 647.757 1.00 16.29 C ANISOU 1084 CE3 TRP A 153 1774 3097 1317 747 -389 -508 C ATOM 1085 CZ2 TRP A 153 -130.404 -91.795 649.789 1.00 17.01 C ANISOU 1085 CZ2 TRP A 153 2061 3100 1302 841 -248 -565 C ATOM 1086 CZ3 TRP A 153 -129.797 -91.717 647.458 1.00 15.95 C ANISOU 1086 CZ3 TRP A 153 1735 3021 1306 725 -295 -508 C ATOM 1087 CH2 TRP A 153 -130.757 -91.785 648.470 1.00 16.32 C ANISOU 1087 CH2 TRP A 153 1873 3025 1304 770 -226 -539 C ATOM 1088 N VAL A 154 -122.759 -92.282 647.670 1.00 25.87 N ANISOU 1088 N VAL A 154 2822 4471 2535 762 -654 -493 N ATOM 1089 CA VAL A 154 -121.699 -92.052 646.698 1.00 23.72 C ANISOU 1089 CA VAL A 154 2450 4223 2341 676 -671 -476 C ATOM 1090 C VAL A 154 -121.668 -93.170 645.667 1.00 20.95 C ANISOU 1090 C VAL A 154 2055 3908 1996 680 -602 -442 C ATOM 1091 O VAL A 154 -121.734 -92.925 644.465 1.00 25.47 O ANISOU 1091 O VAL A 154 2560 4486 2632 591 -572 -416 O ATOM 1092 CB VAL A 154 -120.327 -91.956 647.386 1.00 24.30 C ANISOU 1092 CB VAL A 154 2510 4317 2404 698 -740 -502 C ATOM 1093 CG1 VAL A 154 -119.210 -91.867 646.357 1.00 26.15 C ANISOU 1093 CG1 VAL A 154 2641 4588 2707 617 -747 -487 C ATOM 1094 CG2 VAL A 154 -120.298 -90.774 648.304 1.00 23.06 C ANISOU 1094 CG2 VAL A 154 2385 4129 2246 679 -812 -543 C ATOM 1095 N VAL A 155 -121.581 -94.400 646.159 1.00 19.19 N ANISOU 1095 N VAL A 155 1883 3708 1702 789 -578 -443 N ATOM 1096 CA VAL A 155 -121.580 -95.587 645.310 1.00 21.27 C ANISOU 1096 CA VAL A 155 2116 4008 1958 815 -516 -421 C ATOM 1097 C VAL A 155 -122.820 -95.679 644.416 1.00 22.21 C ANISOU 1097 C VAL A 155 2215 4128 2096 765 -449 -403 C ATOM 1098 O VAL A 155 -122.706 -95.935 643.223 1.00 25.36 O ANISOU 1098 O VAL A 155 2541 4552 2542 703 -409 -388 O ATOM 1099 CB VAL A 155 -121.475 -96.860 646.170 1.00 17.81 C ANISOU 1099 CB VAL A 155 1768 3577 1423 962 -506 -420 C ATOM 1100 CG1 VAL A 155 -121.863 -98.087 645.367 1.00 26.80 C ANISOU 1100 CG1 VAL A 155 2897 4744 2541 1001 -437 -399 C ATOM 1101 CG2 VAL A 155 -120.059 -96.991 646.731 1.00 21.17 C ANISOU 1101 CG2 VAL A 155 2182 4021 1840 1011 -568 -439 C ATOM 1102 N ALA A 156 -124.001 -95.462 644.989 1.00 19.57 N ANISOU 1102 N ALA A 156 1945 3770 1721 792 -435 -408 N ATOM 1103 CA ALA A 156 -125.241 -95.480 644.210 1.00 22.50 C ANISOU 1103 CA ALA A 156 2308 4105 2138 723 -345 -393 C ATOM 1104 C ALA A 156 -125.154 -94.506 643.048 1.00 15.11 C ANISOU 1104 C ALA A 156 1258 3203 1280 615 -380 -383 C ATOM 1105 O ALA A 156 -125.688 -94.749 641.967 1.00 14.64 O ANISOU 1105 O ALA A 156 1146 3161 1256 560 -326 -367 O ATOM 1106 CB ALA A 156 -126.431 -95.143 645.084 1.00 15.49 C ANISOU 1106 CB ALA A 156 1516 3142 1227 737 -301 -404 C ATOM 1107 N VAL A 157 -124.465 -93.399 643.271 1.00 18.04 N ANISOU 1107 N VAL A 157 1623 3540 1692 567 -443 -385 N ATOM 1108 CA VAL A 157 -124.342 -92.395 642.230 1.00 17.57 C ANISOU 1108 CA VAL A 157 1506 3457 1712 452 -454 -357 C ATOM 1109 C VAL A 157 -123.408 -92.876 641.131 1.00 19.97 C ANISOU 1109 C VAL A 157 1751 3794 2044 402 -427 -332 C ATOM 1110 O VAL A 157 -123.733 -92.778 639.953 1.00 17.72 O ANISOU 1110 O VAL A 157 1430 3510 1792 333 -388 -302 O ATOM 1111 CB VAL A 157 -123.835 -91.064 642.788 1.00 18.83 C ANISOU 1111 CB VAL A 157 1674 3576 1904 415 -536 -368 C ATOM 1112 CG1 VAL A 157 -123.353 -90.184 641.653 1.00 20.29 C ANISOU 1112 CG1 VAL A 157 1800 3748 2163 304 -552 -329 C ATOM 1113 CG2 VAL A 157 -124.934 -90.377 643.585 1.00 15.75 C ANISOU 1113 CG2 VAL A 157 1337 3149 1498 449 -558 -396 C ATOM 1114 N PHE A 158 -122.250 -93.411 641.506 1.00 23.09 N ANISOU 1114 N PHE A 158 2139 4218 2417 443 -449 -348 N ATOM 1115 CA PHE A 158 -121.324 -93.897 640.498 1.00 23.69 C ANISOU 1115 CA PHE A 158 2156 4334 2512 407 -423 -335 C ATOM 1116 C PHE A 158 -121.956 -95.027 639.712 1.00 19.87 C ANISOU 1116 C PHE A 158 1665 3880 2005 425 -345 -331 C ATOM 1117 O PHE A 158 -121.759 -95.125 638.512 1.00 23.59 O ANISOU 1117 O PHE A 158 2095 4370 2499 361 -310 -312 O ATOM 1118 CB PHE A 158 -119.999 -94.327 641.126 1.00 31.60 C ANISOU 1118 CB PHE A 158 3146 5370 3493 464 -464 -363 C ATOM 1119 CG PHE A 158 -119.004 -93.205 641.229 1.00 41.84 C ANISOU 1119 CG PHE A 158 4403 6659 4836 397 -530 -365 C ATOM 1120 CD1 PHE A 158 -119.001 -92.360 642.330 1.00 45.75 C ANISOU 1120 CD1 PHE A 158 4933 7121 5329 408 -598 -385 C ATOM 1121 CD2 PHE A 158 -118.092 -92.969 640.208 1.00 45.81 C ANISOU 1121 CD2 PHE A 158 4833 7194 5380 322 -524 -352 C ATOM 1122 CE1 PHE A 158 -118.090 -91.314 642.423 1.00 49.93 C ANISOU 1122 CE1 PHE A 158 5420 7649 5902 340 -663 -394 C ATOM 1123 CE2 PHE A 158 -117.180 -91.922 640.294 1.00 48.37 C ANISOU 1123 CE2 PHE A 158 5113 7519 5747 256 -585 -357 C ATOM 1124 CZ PHE A 158 -117.179 -91.097 641.402 1.00 50.18 C ANISOU 1124 CZ PHE A 158 5372 7714 5979 262 -656 -379 C ATOM 1125 N ALA A 159 -122.755 -95.852 640.376 1.00 20.59 N ANISOU 1125 N ALA A 159 1800 3979 2046 512 -320 -348 N ATOM 1126 CA ALA A 159 -123.447 -96.933 639.691 1.00 19.22 C ANISOU 1126 CA ALA A 159 1614 3836 1854 528 -247 -351 C ATOM 1127 C ALA A 159 -124.460 -96.391 638.691 1.00 20.10 C ANISOU 1127 C ALA A 159 1704 3928 2004 430 -208 -331 C ATOM 1128 O ALA A 159 -124.827 -97.062 637.735 1.00 22.42 O ANISOU 1128 O ALA A 159 1978 4240 2299 399 -152 -331 O ATOM 1129 CB ALA A 159 -124.132 -97.844 640.700 1.00 20.22 C ANISOU 1129 CB ALA A 159 1793 3967 1922 648 -225 -369 C ATOM 1130 N SER A 160 -124.912 -95.167 638.897 1.00 19.42 N ANISOU 1130 N SER A 160 1630 3799 1949 385 -244 -315 N ATOM 1131 CA SER A 160 -125.953 -94.632 638.042 1.00 22.87 C ANISOU 1131 CA SER A 160 2056 4215 2419 314 -216 -294 C ATOM 1132 C SER A 160 -125.402 -93.768 636.905 1.00 28.69 C ANISOU 1132 C SER A 160 2767 4936 3199 223 -235 -252 C ATOM 1133 O SER A 160 -126.128 -93.421 635.975 1.00 31.97 O ANISOU 1133 O SER A 160 3174 5340 3632 171 -215 -228 O ATOM 1134 CB SER A 160 -126.936 -93.829 638.886 1.00 23.71 C ANISOU 1134 CB SER A 160 2189 4288 2533 336 -243 -304 C ATOM 1135 OG SER A 160 -127.494 -94.644 639.908 1.00 29.39 O ANISOU 1135 OG SER A 160 2930 5033 3203 429 -220 -342 O ATOM 1136 N LEU A 161 -124.124 -93.418 636.983 1.00 32.65 N ANISOU 1136 N LEU A 161 3251 5441 3712 208 -275 -245 N ATOM 1137 CA LEU A 161 -123.499 -92.559 635.975 1.00 31.10 C ANISOU 1137 CA LEU A 161 3022 5241 3553 124 -294 -206 C ATOM 1138 C LEU A 161 -123.589 -93.082 634.543 1.00 28.63 C ANISOU 1138 C LEU A 161 2689 4965 3226 82 -238 -188 C ATOM 1139 O LEU A 161 -123.925 -92.309 633.642 1.00 30.44 O ANISOU 1139 O LEU A 161 2908 5184 3472 22 -242 -150 O ATOM 1140 CB LEU A 161 -122.030 -92.320 636.315 1.00 35.96 C ANISOU 1140 CB LEU A 161 3609 5875 4181 118 -337 -216 C ATOM 1141 CG LEU A 161 -121.742 -91.311 637.416 1.00 40.91 C ANISOU 1141 CG LEU A 161 4249 6463 4834 121 -414 -226 C ATOM 1142 CD1 LEU A 161 -120.243 -91.062 637.478 1.00 46.24 C ANISOU 1142 CD1 LEU A 161 4877 7166 5525 96 -453 -236 C ATOM 1143 CD2 LEU A 161 -122.500 -90.019 637.157 1.00 42.10 C ANISOU 1143 CD2 LEU A 161 4408 6563 5024 64 -448 -194 C ATOM 1144 N PRO A 162 -123.275 -94.377 634.313 1.00 25.67 N ANISOU 1144 N PRO A 162 2306 4635 2812 118 -193 -218 N ATOM 1145 CA PRO A 162 -123.332 -94.812 632.912 1.00 27.30 C ANISOU 1145 CA PRO A 162 2496 4877 2998 75 -148 -208 C ATOM 1146 C PRO A 162 -124.733 -94.683 632.338 1.00 26.66 C ANISOU 1146 C PRO A 162 2439 4777 2915 52 -125 -194 C ATOM 1147 O PRO A 162 -124.912 -94.321 631.182 1.00 27.05 O ANISOU 1147 O PRO A 162 2477 4844 2957 -1 -116 -166 O ATOM 1148 CB PRO A 162 -122.903 -96.284 632.976 1.00 25.01 C ANISOU 1148 CB PRO A 162 2202 4631 2671 131 -114 -254 C ATOM 1149 CG PRO A 162 -122.147 -96.415 634.245 1.00 23.84 C ANISOU 1149 CG PRO A 162 2051 4482 2525 197 -148 -276 C ATOM 1150 CD PRO A 162 -122.799 -95.459 635.197 1.00 25.24 C ANISOU 1150 CD PRO A 162 2256 4607 2727 201 -187 -261 C ATOM 1151 N ASN A 163 -125.729 -94.962 633.163 1.00 26.51 N ANISOU 1151 N ASN A 163 2446 4731 2896 93 -117 -217 N ATOM 1152 CA ASN A 163 -127.100 -94.900 632.700 1.00 25.64 C ANISOU 1152 CA ASN A 163 2348 4606 2787 76 -96 -216 C ATOM 1153 C ASN A 163 -127.463 -93.479 632.289 1.00 20.23 C ANISOU 1153 C ASN A 163 1657 3893 2135 34 -136 -167 C ATOM 1154 O ASN A 163 -128.135 -93.268 631.281 1.00 17.93 O ANISOU 1154 O ASN A 163 1360 3614 1837 2 -127 -148 O ATOM 1155 CB ASN A 163 -128.037 -95.425 633.779 1.00 29.30 C ANISOU 1155 CB ASN A 163 2830 5054 3248 129 -77 -255 C ATOM 1156 CG ASN A 163 -127.682 -96.833 634.208 1.00 31.16 C ANISOU 1156 CG ASN A 163 3070 5314 3454 177 -42 -298 C ATOM 1157 OD1 ASN A 163 -126.789 -97.034 635.028 1.00 31.41 O ANISOU 1157 OD1 ASN A 163 3100 5358 3475 228 -60 -306 O ATOM 1158 ND2 ASN A 163 -128.375 -97.818 633.648 1.00 33.74 N ANISOU 1158 ND2 ASN A 163 3403 5640 3776 163 5 -326 N ATOM 1159 N ILE A 164 -126.989 -92.508 633.059 1.00 16.65 N ANISOU 1159 N ILE A 164 1204 3407 1715 36 -188 -149 N ATOM 1160 CA ILE A 164 -127.191 -91.102 632.721 1.00 23.64 C ANISOU 1160 CA ILE A 164 2082 4264 2638 -4 -240 -102 C ATOM 1161 C ILE A 164 -126.568 -90.744 631.369 1.00 28.71 C ANISOU 1161 C ILE A 164 2696 4945 3268 -67 -239 -58 C ATOM 1162 O ILE A 164 -127.237 -90.143 630.520 1.00 28.14 O ANISOU 1162 O ILE A 164 2617 4881 3195 -95 -250 -21 O ATOM 1163 CB ILE A 164 -126.604 -90.180 633.816 1.00 23.89 C ANISOU 1163 CB ILE A 164 2118 4255 2705 3 -306 -101 C ATOM 1164 CG1 ILE A 164 -127.255 -90.501 635.158 1.00 20.49 C ANISOU 1164 CG1 ILE A 164 1716 3801 2268 72 -307 -147 C ATOM 1165 CG2 ILE A 164 -126.824 -88.717 633.467 1.00 22.74 C ANISOU 1165 CG2 ILE A 164 1963 4079 2597 -40 -369 -56 C ATOM 1166 CD1 ILE A 164 -126.586 -89.857 636.326 1.00 25.89 C ANISOU 1166 CD1 ILE A 164 2412 4457 2968 91 -370 -163 C ATOM 1167 N ILE A 165 -125.305 -91.128 631.163 1.00 27.41 N ANISOU 1167 N ILE A 165 2512 4817 3088 -85 -227 -62 N ATOM 1168 CA ILE A 165 -124.556 -90.698 629.977 1.00 27.41 C ANISOU 1168 CA ILE A 165 2477 4868 3070 -150 -226 -22 C ATOM 1169 C ILE A 165 -125.077 -91.340 628.697 1.00 27.63 C ANISOU 1169 C ILE A 165 2503 4951 3045 -163 -178 -16 C ATOM 1170 O ILE A 165 -124.989 -90.747 627.621 1.00 30.10 O ANISOU 1170 O ILE A 165 2792 5311 3332 -217 -183 31 O ATOM 1171 CB ILE A 165 -123.032 -91.006 630.088 1.00 44.27 C ANISOU 1171 CB ILE A 165 4580 7039 5201 -163 -221 -39 C ATOM 1172 CG1 ILE A 165 -122.755 -92.503 629.937 1.00 52.80 C ANISOU 1172 CG1 ILE A 165 5663 8159 6239 -119 -168 -88 C ATOM 1173 CG2 ILE A 165 -122.463 -90.482 631.393 1.00 39.36 C ANISOU 1173 CG2 ILE A 165 3958 6372 4626 -146 -274 -57 C ATOM 1174 CD1 ILE A 165 -121.295 -92.856 629.740 1.00 57.93 C ANISOU 1174 CD1 ILE A 165 6270 8864 6876 -129 -160 -106 C ATOM 1175 N PHE A 166 -125.618 -92.549 628.820 1.00 25.01 N ANISOU 1175 N PHE A 166 2193 4622 2689 -119 -136 -66 N ATOM 1176 CA PHE A 166 -126.129 -93.295 627.679 1.00 22.26 C ANISOU 1176 CA PHE A 166 1844 4326 2288 -129 -96 -79 C ATOM 1177 C PHE A 166 -127.527 -92.836 627.288 1.00 19.78 C ANISOU 1177 C PHE A 166 1538 4001 1976 -132 -106 -61 C ATOM 1178 O PHE A 166 -128.054 -93.260 626.264 1.00 23.34 O ANISOU 1178 O PHE A 166 1983 4502 2381 -145 -84 -68 O ATOM 1179 CB PHE A 166 -126.164 -94.791 627.998 1.00 27.43 C ANISOU 1179 CB PHE A 166 2514 4985 2922 -86 -57 -146 C ATOM 1180 CG PHE A 166 -124.842 -95.495 627.821 1.00 27.30 C ANISOU 1180 CG PHE A 166 2478 5012 2884 -82 -43 -169 C ATOM 1181 CD1 PHE A 166 -124.002 -95.172 626.772 1.00 26.52 C ANISOU 1181 CD1 PHE A 166 2347 4976 2754 -128 -41 -144 C ATOM 1182 CD2 PHE A 166 -124.458 -96.499 628.700 1.00 27.38 C ANISOU 1182 CD2 PHE A 166 2496 5009 2900 -28 -32 -218 C ATOM 1183 CE1 PHE A 166 -122.794 -95.831 626.603 1.00 27.81 C ANISOU 1183 CE1 PHE A 166 2483 5185 2899 -120 -28 -173 C ATOM 1184 CE2 PHE A 166 -123.256 -97.162 628.539 1.00 28.81 C ANISOU 1184 CE2 PHE A 166 2649 5232 3064 -14 -23 -243 C ATOM 1185 CZ PHE A 166 -122.422 -96.829 627.482 1.00 27.87 C ANISOU 1185 CZ PHE A 166 2496 5174 2921 -60 -20 -225 C ATOM 1186 N THR A 167 -128.125 -91.975 628.104 1.00 18.57 N ANISOU 1186 N THR A 167 1394 3788 1873 -115 -144 -44 N ATOM 1187 CA THR A 167 -129.530 -91.597 627.936 1.00 20.09 C ANISOU 1187 CA THR A 167 1590 3967 2077 -101 -157 -39 C ATOM 1188 C THR A 167 -129.684 -90.185 627.395 1.00 23.00 C ANISOU 1188 C THR A 167 1940 4340 2461 -130 -215 31 C ATOM 1189 O THR A 167 -129.016 -89.256 627.855 1.00 27.34 O ANISOU 1189 O THR A 167 2486 4860 3043 -148 -260 67 O ATOM 1190 CB THR A 167 -130.298 -91.708 629.271 1.00 16.01 C ANISOU 1190 CB THR A 167 1093 3387 1601 -50 -161 -79 C ATOM 1191 OG1 THR A 167 -130.170 -93.044 629.771 1.00 15.73 O ANISOU 1191 OG1 THR A 167 1074 3357 1545 -26 -111 -138 O ATOM 1192 CG2 THR A 167 -131.782 -91.379 629.084 1.00 14.03 C ANISOU 1192 CG2 THR A 167 836 3130 1364 -31 -172 -86 C ATOM 1193 N ARG A 168 -130.569 -90.034 626.414 1.00 22.47 N ANISOU 1193 N ARG A 168 1857 4315 2365 -135 -219 49 N ATOM 1194 CA ARG A 168 -130.762 -88.766 625.723 1.00 26.07 C ANISOU 1194 CA ARG A 168 2293 4794 2819 -160 -279 125 C ATOM 1195 C ARG A 168 -132.209 -88.648 625.290 1.00 24.48 C ANISOU 1195 C ARG A 168 2083 4604 2615 -123 -298 118 C ATOM 1196 O ARG A 168 -132.875 -89.663 625.055 1.00 29.21 O ANISOU 1196 O ARG A 168 2680 5227 3190 -105 -250 58 O ATOM 1197 CB ARG A 168 -129.851 -88.661 624.489 1.00 37.54 C ANISOU 1197 CB ARG A 168 3719 6339 4206 -225 -268 181 C ATOM 1198 CG ARG A 168 -128.350 -88.873 624.725 1.00 48.17 C ANISOU 1198 CG ARG A 168 5061 7696 5547 -266 -243 181 C ATOM 1199 CD ARG A 168 -127.699 -87.687 625.435 1.00 56.00 C ANISOU 1199 CD ARG A 168 6049 8637 6592 -295 -302 228 C ATOM 1200 NE ARG A 168 -127.968 -86.430 624.738 1.00 63.16 N ANISOU 1200 NE ARG A 168 6937 9575 7486 -340 -365 323 N ATOM 1201 CZ ARG A 168 -127.255 -85.961 623.717 1.00 66.02 C ANISOU 1201 CZ ARG A 168 7267 10025 7792 -422 -369 402 C ATOM 1202 NH1 ARG A 168 -126.205 -86.635 623.262 1.00 67.23 N ANISOU 1202 NH1 ARG A 168 7398 10246 7901 -464 -309 384 N ATOM 1203 NH2 ARG A 168 -127.592 -84.811 623.150 1.00 66.51 N ANISOU 1203 NH2 ARG A 168 7321 10110 7839 -463 -438 506 N ATOM 1204 N SER A 169 -132.702 -87.419 625.176 1.00 20.18 N ANISOU 1204 N SER A 169 1532 4043 2092 -111 -373 176 N ATOM 1205 CA SER A 169 -133.970 -87.197 624.498 1.00 26.15 C ANISOU 1205 CA SER A 169 2272 4829 2835 -74 -403 180 C ATOM 1206 C SER A 169 -133.715 -87.021 623.007 1.00 27.65 C ANISOU 1206 C SER A 169 2439 5120 2946 -117 -412 246 C ATOM 1207 O SER A 169 -132.723 -86.418 622.610 1.00 28.80 O ANISOU 1207 O SER A 169 2583 5297 3064 -172 -432 323 O ATOM 1208 CB SER A 169 -134.691 -85.976 625.061 1.00 34.87 C ANISOU 1208 CB SER A 169 3385 5871 3995 -21 -490 211 C ATOM 1209 OG SER A 169 -134.058 -84.784 624.635 1.00 41.32 O ANISOU 1209 OG SER A 169 4210 6694 4798 -52 -563 315 O ATOM 1210 N GLN A 170 -134.589 -87.567 622.173 1.00 30.24 N ANISOU 1210 N GLN A 170 2746 5511 3232 -98 -396 215 N ATOM 1211 CA GLN A 170 -134.451 -87.344 620.744 1.00 32.29 C ANISOU 1211 CA GLN A 170 2983 5878 3408 -132 -412 278 C ATOM 1212 C GLN A 170 -135.806 -87.322 620.075 1.00 32.98 C ANISOU 1212 C GLN A 170 3050 6005 3476 -80 -447 259 C ATOM 1213 O GLN A 170 -136.769 -87.898 620.580 1.00 31.13 O ANISOU 1213 O GLN A 170 2808 5738 3281 -36 -428 173 O ATOM 1214 CB GLN A 170 -133.555 -88.405 620.102 1.00 31.78 C ANISOU 1214 CB GLN A 170 2902 5897 3275 -190 -329 251 C ATOM 1215 CG GLN A 170 -134.086 -89.819 620.158 1.00 31.55 C ANISOU 1215 CG GLN A 170 2870 5880 3236 -171 -260 139 C ATOM 1216 CD GLN A 170 -133.297 -90.773 619.268 1.00 33.82 C ANISOU 1216 CD GLN A 170 3143 6269 3440 -219 -196 116 C ATOM 1217 OE1 GLN A 170 -132.358 -90.372 618.582 1.00 34.60 O ANISOU 1217 OE1 GLN A 170 3224 6439 3483 -270 -196 185 O ATOM 1218 NE2 GLN A 170 -133.682 -92.041 619.276 1.00 36.76 N ANISOU 1218 NE2 GLN A 170 3520 6652 3797 -207 -145 18 N ATOM 1219 N LYS A 171 -135.882 -86.630 618.944 1.00 34.21 N ANISOU 1219 N LYS A 171 3199 6235 3566 -86 -502 342 N ATOM 1220 CA LYS A 171 -137.093 -86.629 618.149 1.00 34.41 C ANISOU 1220 CA LYS A 171 3203 6313 3560 -35 -542 324 C ATOM 1221 C LYS A 171 -137.107 -87.884 617.286 1.00 36.33 C ANISOU 1221 C LYS A 171 3407 6664 3733 -70 -467 255 C ATOM 1222 O LYS A 171 -136.212 -88.100 616.476 1.00 40.78 O ANISOU 1222 O LYS A 171 3961 7314 4221 -131 -433 295 O ATOM 1223 CB LYS A 171 -137.175 -85.364 617.298 1.00 34.47 C ANISOU 1223 CB LYS A 171 3233 6348 3515 -15 -641 449 C ATOM 1224 CG LYS A 171 -138.402 -85.270 616.417 1.00 33.65 C ANISOU 1224 CG LYS A 171 3112 6302 3371 50 -698 436 C ATOM 1225 CD LYS A 171 -138.442 -83.926 615.712 1.00 37.80 C ANISOU 1225 CD LYS A 171 3689 6827 3844 84 -805 574 C ATOM 1226 CE LYS A 171 -139.731 -83.730 614.938 1.00 42.03 C ANISOU 1226 CE LYS A 171 4214 7407 4347 168 -878 560 C ATOM 1227 NZ LYS A 171 -139.754 -84.550 613.700 1.00 47.47 N ANISOU 1227 NZ LYS A 171 4863 8235 4936 131 -840 532 N ATOM 1228 N GLU A 172 -138.108 -88.730 617.485 1.00 34.79 N ANISOU 1228 N GLU A 172 3188 6468 3561 -38 -437 149 N ATOM 1229 CA GLU A 172 -138.217 -89.949 616.706 1.00 37.28 C ANISOU 1229 CA GLU A 172 3470 6882 3812 -69 -372 73 C ATOM 1230 C GLU A 172 -139.416 -89.843 615.775 1.00 44.58 C ANISOU 1230 C GLU A 172 4356 7886 4698 -28 -424 53 C ATOM 1231 O GLU A 172 -140.498 -90.355 616.073 1.00 46.66 O ANISOU 1231 O GLU A 172 4593 8139 4995 5 -418 -37 O ATOM 1232 CB GLU A 172 -138.327 -91.170 617.627 1.00 34.19 C ANISOU 1232 CB GLU A 172 3088 6437 3465 -77 -292 -39 C ATOM 1233 CG GLU A 172 -137.165 -91.277 618.602 1.00 32.46 C ANISOU 1233 CG GLU A 172 2913 6135 3284 -105 -251 -22 C ATOM 1234 CD GLU A 172 -137.072 -92.627 619.308 1.00 37.98 C ANISOU 1234 CD GLU A 172 3635 6797 4001 -116 -177 -123 C ATOM 1235 OE1 GLU A 172 -137.770 -93.579 618.902 1.00 39.69 O ANISOU 1235 OE1 GLU A 172 3831 7062 4188 -120 -147 -207 O ATOM 1236 OE2 GLU A 172 -136.289 -92.730 620.280 1.00 41.66 O ANISOU 1236 OE2 GLU A 172 4139 7182 4508 -122 -155 -118 O ATOM 1237 N GLY A 173 -139.217 -89.172 614.643 1.00 47.55 N ANISOU 1237 N GLY A 173 4726 8345 4995 -31 -478 139 N ATOM 1238 CA GLY A 173 -140.315 -88.894 613.739 1.00 48.28 C ANISOU 1238 CA GLY A 173 4790 8508 5044 21 -549 135 C ATOM 1239 C GLY A 173 -141.268 -87.895 614.366 1.00 49.93 C ANISOU 1239 C GLY A 173 5016 8629 5327 104 -641 159 C ATOM 1240 O GLY A 173 -140.903 -86.742 614.602 1.00 50.09 O ANISOU 1240 O GLY A 173 5084 8584 5363 127 -707 263 O ATOM 1241 N LEU A 174 -142.487 -88.334 614.658 1.00 51.62 N ANISOU 1241 N LEU A 174 5187 8841 5585 147 -644 61 N ATOM 1242 CA LEU A 174 -143.488 -87.435 615.217 1.00 56.01 C ANISOU 1242 CA LEU A 174 5743 9329 6211 232 -729 71 C ATOM 1243 C LEU A 174 -143.322 -87.244 616.730 1.00 59.04 C ANISOU 1243 C LEU A 174 6151 9582 6700 238 -701 56 C ATOM 1244 O LEU A 174 -143.535 -86.146 617.243 1.00 61.76 O ANISOU 1244 O LEU A 174 6522 9849 7095 298 -776 114 O ATOM 1245 CB LEU A 174 -144.894 -87.950 614.903 1.00 59.97 C ANISOU 1245 CB LEU A 174 6175 9898 6715 272 -743 -29 C ATOM 1246 N HIS A 175 -142.927 -88.304 617.434 1.00 54.82 N ANISOU 1246 N HIS A 175 5614 9023 6193 181 -597 -20 N ATOM 1247 CA HIS A 175 -142.839 -88.273 618.894 1.00 46.26 C ANISOU 1247 CA HIS A 175 4552 7825 5200 187 -564 -47 C ATOM 1248 C HIS A 175 -141.433 -87.967 619.426 1.00 38.88 C ANISOU 1248 C HIS A 175 3673 6824 4275 145 -543 21 C ATOM 1249 O HIS A 175 -140.433 -88.249 618.773 1.00 36.43 O ANISOU 1249 O HIS A 175 3377 6562 3902 89 -511 59 O ATOM 1250 CB HIS A 175 -143.319 -89.609 619.469 1.00 43.74 C ANISOU 1250 CB HIS A 175 4208 7509 4903 157 -471 -170 C ATOM 1251 N TYR A 176 -141.374 -87.381 620.619 1.00 35.03 N ANISOU 1251 N TYR A 176 3210 6233 3866 174 -559 32 N ATOM 1252 CA TYR A 176 -140.114 -87.176 621.336 1.00 33.18 C ANISOU 1252 CA TYR A 176 3023 5932 3653 135 -536 76 C ATOM 1253 C TYR A 176 -139.951 -88.232 622.406 1.00 26.57 C ANISOU 1253 C TYR A 176 2193 5049 2854 109 -445 -9 C ATOM 1254 O TYR A 176 -140.905 -88.531 623.116 1.00 26.63 O ANISOU 1254 O TYR A 176 2181 5029 2906 143 -428 -80 O ATOM 1255 CB TYR A 176 -140.064 -85.797 621.984 1.00 36.28 C ANISOU 1255 CB TYR A 176 3443 6240 4100 185 -621 146 C ATOM 1256 CG TYR A 176 -139.623 -84.711 621.048 1.00 42.51 C ANISOU 1256 CG TYR A 176 4259 7054 4838 188 -707 265 C ATOM 1257 CD1 TYR A 176 -140.526 -84.105 620.185 1.00 44.18 C ANISOU 1257 CD1 TYR A 176 4462 7306 5019 250 -787 301 C ATOM 1258 CD2 TYR A 176 -138.306 -84.289 621.023 1.00 44.13 C ANISOU 1258 CD2 TYR A 176 4501 7248 5020 129 -707 347 C ATOM 1259 CE1 TYR A 176 -140.125 -83.112 619.324 1.00 45.24 C ANISOU 1259 CE1 TYR A 176 4638 7458 5094 257 -867 424 C ATOM 1260 CE2 TYR A 176 -137.899 -83.295 620.165 1.00 46.47 C ANISOU 1260 CE2 TYR A 176 4829 7570 5259 122 -780 472 C ATOM 1261 CZ TYR A 176 -138.813 -82.712 619.320 1.00 47.23 C ANISOU 1261 CZ TYR A 176 4931 7696 5318 188 -859 514 C ATOM 1262 OH TYR A 176 -138.408 -81.722 618.461 1.00 55.26 O ANISOU 1262 OH TYR A 176 6000 8730 6267 183 -931 652 O ATOM 1263 N THR A 177 -138.749 -88.788 622.532 1.00 22.80 N ANISOU 1263 N THR A 177 1743 4565 2353 53 -388 -1 N ATOM 1264 CA THR A 177 -138.526 -89.850 623.500 1.00 25.77 C ANISOU 1264 CA THR A 177 2139 4899 2754 35 -310 -75 C ATOM 1265 C THR A 177 -137.421 -89.518 624.492 1.00 28.75 C ANISOU 1265 C THR A 177 2555 5201 3166 23 -306 -42 C ATOM 1266 O THR A 177 -136.697 -88.543 624.329 1.00 30.18 O ANISOU 1266 O THR A 177 2747 5371 3350 13 -357 36 O ATOM 1267 CB THR A 177 -138.165 -91.165 622.813 1.00 24.01 C ANISOU 1267 CB THR A 177 1915 4741 2466 -12 -240 -123 C ATOM 1268 OG1 THR A 177 -136.840 -91.076 622.282 1.00 23.22 O ANISOU 1268 OG1 THR A 177 1830 4669 2321 -54 -232 -66 O ATOM 1269 CG2 THR A 177 -139.132 -91.455 621.697 1.00 23.96 C ANISOU 1269 CG2 THR A 177 1865 4825 2414 -7 -250 -156 C ATOM 1270 N CYS A 178 -137.315 -90.339 625.530 1.00 27.72 N ANISOU 1270 N CYS A 178 2446 5025 3061 24 -250 -103 N ATOM 1271 CA CYS A 178 -136.230 -90.250 626.496 1.00 27.61 C ANISOU 1271 CA CYS A 178 2467 4952 3072 14 -241 -86 C ATOM 1272 C CYS A 178 -135.782 -91.668 626.752 1.00 23.92 C ANISOU 1272 C CYS A 178 2019 4492 2576 -8 -167 -145 C ATOM 1273 O CYS A 178 -136.495 -92.451 627.385 1.00 22.43 O ANISOU 1273 O CYS A 178 1834 4288 2400 7 -129 -212 O ATOM 1274 CB CYS A 178 -136.663 -89.567 627.798 1.00 28.62 C ANISOU 1274 CB CYS A 178 2601 5010 3265 60 -271 -96 C ATOM 1275 SG CYS A 178 -135.347 -89.483 629.051 1.00 30.31 S ANISOU 1275 SG CYS A 178 2852 5162 3502 53 -266 -87 S ATOM 1276 N SER A 179 -134.592 -91.986 626.264 1.00 19.83 N ANISOU 1276 N SER A 179 1514 4000 2021 -44 -150 -120 N ATOM 1277 CA SER A 179 -134.202 -93.365 626.085 1.00 21.62 C ANISOU 1277 CA SER A 179 1755 4252 2208 -62 -93 -175 C ATOM 1278 C SER A 179 -132.687 -93.514 626.143 1.00 23.50 C ANISOU 1278 C SER A 179 2009 4491 2429 -82 -84 -148 C ATOM 1279 O SER A 179 -131.955 -92.548 625.909 1.00 22.97 O ANISOU 1279 O SER A 179 1932 4429 2365 -100 -117 -84 O ATOM 1280 CB SER A 179 -134.749 -93.859 624.739 1.00 26.59 C ANISOU 1280 CB SER A 179 2360 4963 2781 -84 -81 -197 C ATOM 1281 OG SER A 179 -134.355 -95.186 624.446 1.00 36.24 O ANISOU 1281 OG SER A 179 3594 6211 3962 -103 -37 -255 O ATOM 1282 N ASER A 180 -132.212 -94.718 626.446 0.45 21.80 N ANISOU 1282 N ASER A 180 1812 4273 2198 -81 -45 -200 N ATOM 1283 N BSER A 180 -132.228 -94.718 626.477 0.55 21.73 N ANISOU 1283 N BSER A 180 1803 4262 2190 -80 -45 -201 N ATOM 1284 CA ASER A 180 -130.780 -94.977 626.412 0.45 20.71 C ANISOU 1284 CA ASER A 180 1680 4147 2042 -93 -37 -186 C ATOM 1285 CA BSER A 180 -130.812 -95.054 626.394 0.55 20.15 C ANISOU 1285 CA BSER A 180 1609 4077 1969 -92 -35 -190 C ATOM 1286 C ASER A 180 -130.383 -95.569 625.064 0.45 21.01 C ANISOU 1286 C ASER A 180 1703 4266 2015 -125 -20 -198 C ATOM 1287 C BSER A 180 -130.453 -95.465 624.972 0.55 20.88 C ANISOU 1287 C BSER A 180 1684 4254 1997 -127 -22 -193 C ATOM 1288 O ASER A 180 -131.102 -96.400 624.502 0.45 20.53 O ANISOU 1288 O ASER A 180 1639 4235 1927 -130 -1 -250 O ATOM 1289 O BSER A 180 -131.267 -96.071 624.269 0.55 20.94 O ANISOU 1289 O BSER A 180 1684 4299 1973 -135 -8 -234 O ATOM 1290 CB ASER A 180 -130.365 -95.919 627.541 0.45 18.44 C ANISOU 1290 CB ASER A 180 1414 3817 1775 -62 -16 -233 C ATOM 1291 CB BSER A 180 -130.453 -96.188 627.362 0.55 17.72 C ANISOU 1291 CB BSER A 180 1322 3734 1675 -65 -9 -245 C ATOM 1292 OG ASER A 180 -130.455 -97.267 627.125 0.45 18.65 O ANISOU 1292 OG ASER A 180 1444 3866 1777 -66 15 -293 O ATOM 1293 OG BSER A 180 -130.434 -95.752 628.709 0.55 16.03 O ANISOU 1293 OG BSER A 180 1121 3464 1505 -33 -21 -237 O ATOM 1294 N HIS A 181 -129.235 -95.130 624.553 1.00 20.59 N ANISOU 1294 N HIS A 181 1634 4253 1936 -151 -27 -154 N ATOM 1295 CA HIS A 181 -128.685 -95.635 623.301 1.00 20.69 C ANISOU 1295 CA HIS A 181 1626 4356 1878 -182 -10 -165 C ATOM 1296 C HIS A 181 -127.252 -96.072 623.537 1.00 21.54 C ANISOU 1296 C HIS A 181 1730 4469 1985 -181 -1 -176 C ATOM 1297 O HIS A 181 -126.520 -95.424 624.280 1.00 22.09 O ANISOU 1297 O HIS A 181 1798 4501 2093 -178 -15 -141 O ATOM 1298 CB HIS A 181 -128.741 -94.576 622.203 1.00 21.78 C ANISOU 1298 CB HIS A 181 1733 4571 1970 -223 -28 -95 C ATOM 1299 CG HIS A 181 -130.107 -94.023 621.981 1.00 24.54 C ANISOU 1299 CG HIS A 181 2076 4920 2328 -215 -47 -78 C ATOM 1300 ND1 HIS A 181 -130.614 -92.977 622.725 1.00 23.51 N ANISOU 1300 ND1 HIS A 181 1950 4722 2263 -198 -84 -34 N ATOM 1301 CD2 HIS A 181 -131.082 -94.364 621.108 1.00 25.56 C ANISOU 1301 CD2 HIS A 181 2188 5112 2411 -217 -40 -105 C ATOM 1302 CE1 HIS A 181 -131.838 -92.704 622.323 1.00 20.42 C ANISOU 1302 CE1 HIS A 181 1543 4347 1868 -184 -102 -33 C ATOM 1303 NE2 HIS A 181 -132.149 -93.532 621.340 1.00 23.05 N ANISOU 1303 NE2 HIS A 181 1862 4762 2135 -196 -74 -76 N ATOM 1304 N PHE A 182 -126.856 -97.171 622.908 1.00 22.43 N ANISOU 1304 N PHE A 182 1834 4629 2057 -183 19 -232 N ATOM 1305 CA PHE A 182 -125.501 -97.683 623.054 1.00 23.14 C ANISOU 1305 CA PHE A 182 1910 4734 2150 -174 27 -251 C ATOM 1306 C PHE A 182 -124.762 -97.574 621.728 1.00 26.50 C ANISOU 1306 C PHE A 182 2297 5264 2506 -218 32 -240 C ATOM 1307 O PHE A 182 -125.351 -97.797 620.677 1.00 16.76 O ANISOU 1307 O PHE A 182 1055 4097 1216 -242 35 -256 O ATOM 1308 CB PHE A 182 -125.550 -99.121 623.551 1.00 21.64 C ANISOU 1308 CB PHE A 182 1730 4505 1986 -134 44 -329 C ATOM 1309 CG PHE A 182 -126.461 -99.309 624.732 1.00 21.56 C ANISOU 1309 CG PHE A 182 1753 4409 2030 -100 44 -342 C ATOM 1310 CD1 PHE A 182 -126.267 -98.578 625.895 1.00 14.59 C ANISOU 1310 CD1 PHE A 182 883 3474 1187 -76 30 -304 C ATOM 1311 CD2 PHE A 182 -127.499-100.220 624.690 1.00 23.03 C ANISOU 1311 CD2 PHE A 182 1950 4569 2230 -97 59 -396 C ATOM 1312 CE1 PHE A 182 -127.105 -98.743 626.985 1.00 14.16 C ANISOU 1312 CE1 PHE A 182 853 3353 1172 -46 32 -318 C ATOM 1313 CE2 PHE A 182 -128.337-100.387 625.780 1.00 20.94 C ANISOU 1313 CE2 PHE A 182 1709 4232 2015 -73 66 -408 C ATOM 1314 CZ PHE A 182 -128.139 -99.645 626.924 1.00 18.03 C ANISOU 1314 CZ PHE A 182 1354 3822 1674 -45 52 -368 C ATOM 1315 N PRO A 183 -123.474 -97.197 621.767 1.00 26.99 N ANISOU 1315 N PRO A 183 2332 5353 2570 -231 31 -216 N ATOM 1316 CA PRO A 183 -122.719 -97.035 620.516 1.00 23.80 C ANISOU 1316 CA PRO A 183 1885 5061 2098 -280 38 -204 C ATOM 1317 C PRO A 183 -122.757 -98.314 619.704 1.00 21.37 C ANISOU 1317 C PRO A 183 1564 4805 1750 -270 53 -282 C ATOM 1318 O PRO A 183 -122.488 -99.380 620.260 1.00 27.30 O ANISOU 1318 O PRO A 183 2321 5510 2544 -224 64 -345 O ATOM 1319 CB PRO A 183 -121.299 -96.716 620.992 1.00 21.62 C ANISOU 1319 CB PRO A 183 1577 4786 1852 -284 40 -191 C ATOM 1320 CG PRO A 183 -121.255 -97.149 622.407 1.00 19.69 C ANISOU 1320 CG PRO A 183 1358 4443 1681 -222 35 -220 C ATOM 1321 CD PRO A 183 -122.630 -97.001 622.953 1.00 23.19 C ANISOU 1321 CD PRO A 183 1849 4814 2150 -203 25 -209 C ATOM 1322 N TYR A 184 -123.105 -98.214 618.425 1.00 21.51 N ANISOU 1322 N TYR A 184 1562 4922 1690 -312 51 -278 N ATOM 1323 CA TYR A 184 -123.399 -99.400 617.621 1.00 25.58 C ANISOU 1323 CA TYR A 184 2063 5485 2173 -308 58 -361 C ATOM 1324 C TYR A 184 -122.188-100.285 617.399 1.00 28.55 C ANISOU 1324 C TYR A 184 2401 5888 2559 -294 78 -419 C ATOM 1325 O TYR A 184 -122.329-101.470 617.101 1.00 30.04 O ANISOU 1325 O TYR A 184 2579 6077 2759 -275 91 -499 O ATOM 1326 CB TYR A 184 -123.993 -98.993 616.274 1.00 32.96 C ANISOU 1326 CB TYR A 184 2973 6542 3009 -359 45 -343 C ATOM 1327 CG TYR A 184 -123.048 -98.231 615.374 1.00 39.96 C ANISOU 1327 CG TYR A 184 3812 7543 3827 -414 43 -287 C ATOM 1328 CD1 TYR A 184 -122.242 -98.898 614.455 1.00 41.14 C ANISOU 1328 CD1 TYR A 184 3911 7781 3938 -433 55 -340 C ATOM 1329 CD2 TYR A 184 -122.967 -96.840 615.434 1.00 44.39 C ANISOU 1329 CD2 TYR A 184 4372 8125 4370 -453 32 -181 C ATOM 1330 CE1 TYR A 184 -121.372 -98.200 613.624 1.00 46.05 C ANISOU 1330 CE1 TYR A 184 4484 8513 4500 -491 58 -290 C ATOM 1331 CE2 TYR A 184 -122.101 -96.133 614.608 1.00 47.51 C ANISOU 1331 CE2 TYR A 184 4718 8627 4706 -517 30 -125 C ATOM 1332 CZ TYR A 184 -121.309 -96.819 613.704 1.00 49.28 C ANISOU 1332 CZ TYR A 184 4894 8942 4889 -536 45 -181 C ATOM 1333 OH TYR A 184 -120.451 -96.124 612.882 1.00 53.77 O ANISOU 1333 OH TYR A 184 5410 9618 5403 -606 50 -127 O ATOM 1334 N SER A 185 -120.998 -99.708 617.541 1.00 31.43 N ANISOU 1334 N SER A 185 2738 6277 2927 -306 84 -381 N ATOM 1335 CA SER A 185 -119.761-100.449 617.337 1.00 36.73 C ANISOU 1335 CA SER A 185 3363 6986 3607 -289 107 -434 C ATOM 1336 C SER A 185 -119.506-101.452 618.459 1.00 41.94 C ANISOU 1336 C SER A 185 4037 7552 4346 -215 118 -488 C ATOM 1337 O SER A 185 -118.934-102.515 618.224 1.00 46.04 O ANISOU 1337 O SER A 185 4526 8091 4878 -183 139 -556 O ATOM 1338 CB SER A 185 -118.584 -99.488 617.211 1.00 39.65 C ANISOU 1338 CB SER A 185 3691 7414 3961 -328 113 -381 C ATOM 1339 OG SER A 185 -118.687 -98.730 616.019 1.00 44.78 O ANISOU 1339 OG SER A 185 4315 8170 4529 -401 109 -335 O ATOM 1340 N GLN A 186 -119.929-101.119 619.675 1.00 39.94 N ANISOU 1340 N GLN A 186 3827 7204 4146 -185 104 -456 N ATOM 1341 CA GLN A 186 -119.845-102.060 620.791 1.00 37.07 C ANISOU 1341 CA GLN A 186 3479 6758 3849 -113 110 -499 C ATOM 1342 C GLN A 186 -121.236-102.272 621.388 1.00 39.03 C ANISOU 1342 C GLN A 186 3782 6920 4128 -100 104 -500 C ATOM 1343 O GLN A 186 -121.416-102.236 622.608 1.00 38.73 O ANISOU 1343 O GLN A 186 3772 6806 4138 -60 97 -486 O ATOM 1344 CB GLN A 186 -118.868-101.555 621.859 1.00 34.05 C ANISOU 1344 CB GLN A 186 3083 6353 3503 -82 101 -471 C ATOM 1345 CG GLN A 186 -117.517-101.083 621.315 1.00 34.80 C ANISOU 1345 CG GLN A 186 3114 6535 3571 -111 107 -463 C ATOM 1346 CD GLN A 186 -117.511 -99.599 620.940 1.00 41.27 C ANISOU 1346 CD GLN A 186 3930 7387 4363 -186 95 -385 C ATOM 1347 OE1 GLN A 186 -118.125 -98.769 621.612 1.00 48.12 O ANISOU 1347 OE1 GLN A 186 4835 8193 5255 -197 76 -332 O ATOM 1348 NE2 GLN A 186 -116.815 -99.266 619.863 1.00 43.23 N ANISOU 1348 NE2 GLN A 186 4129 7735 4563 -240 110 -377 N ATOM 1349 N TYR A 187 -122.210-102.499 620.511 1.00 35.31 N ANISOU 1349 N TYR A 187 3319 6471 3626 -135 105 -521 N ATOM 1350 CA TYR A 187 -123.624-102.542 620.887 1.00 29.64 C ANISOU 1350 CA TYR A 187 2643 5689 2929 -138 99 -522 C ATOM 1351 C TYR A 187 -123.965-103.607 621.923 1.00 24.12 C ANISOU 1351 C TYR A 187 1966 4895 2304 -88 121 -565 C ATOM 1352 O TYR A 187 -124.484-103.291 622.992 1.00 19.96 O ANISOU 1352 O TYR A 187 1471 4297 1814 -67 114 -538 O ATOM 1353 CB TYR A 187 -124.491-102.767 619.650 1.00 25.01 C ANISOU 1353 CB TYR A 187 2045 5165 2291 -183 98 -556 C ATOM 1354 CG TYR A 187 -125.951-102.448 619.874 1.00 22.84 C ANISOU 1354 CG TYR A 187 1803 4852 2021 -197 86 -547 C ATOM 1355 CD1 TYR A 187 -126.363-101.141 620.099 1.00 21.79 C ANISOU 1355 CD1 TYR A 187 1690 4721 1868 -208 66 -471 C ATOM 1356 CD2 TYR A 187 -126.910-103.440 619.856 1.00 17.26 C ANISOU 1356 CD2 TYR A 187 1102 4110 1348 -199 103 -616 C ATOM 1357 CE1 TYR A 187 -127.691-100.832 620.296 1.00 16.58 C ANISOU 1357 CE1 TYR A 187 1052 4032 1215 -213 59 -466 C ATOM 1358 CE2 TYR A 187 -128.250-103.140 620.045 1.00 21.68 C ANISOU 1358 CE2 TYR A 187 1682 4645 1912 -213 94 -615 C ATOM 1359 CZ TYR A 187 -128.631-101.834 620.270 1.00 21.48 C ANISOU 1359 CZ TYR A 187 1674 4626 1861 -215 71 -541 C ATOM 1360 OH TYR A 187 -129.955-101.519 620.461 1.00 20.74 O ANISOU 1360 OH TYR A 187 1594 4512 1775 -221 67 -543 O ATOM 1361 N GLN A 188 -123.685-104.866 621.603 1.00 22.44 N ANISOU 1361 N GLN A 188 1734 4681 2113 -67 154 -632 N ATOM 1362 CA GLN A 188 -124.046-105.959 622.496 1.00 23.12 C ANISOU 1362 CA GLN A 188 1843 4672 2267 -20 192 -670 C ATOM 1363 C GLN A 188 -123.172-105.969 623.743 1.00 28.47 C ANISOU 1363 C GLN A 188 2528 5311 2980 50 193 -645 C ATOM 1364 O GLN A 188 -123.583-106.501 624.781 1.00 30.86 O ANISOU 1364 O GLN A 188 2864 5531 3330 94 220 -649 O ATOM 1365 CB GLN A 188 -123.947-107.306 621.787 1.00 24.14 C ANISOU 1365 CB GLN A 188 1955 4805 2412 -13 241 -748 C ATOM 1366 CG GLN A 188 -124.485-108.465 622.612 1.00 28.20 C ANISOU 1366 CG GLN A 188 2510 5211 2994 29 302 -785 C ATOM 1367 CD GLN A 188 -126.002-108.489 622.688 1.00 33.00 C ANISOU 1367 CD GLN A 188 3149 5770 3621 -20 314 -796 C ATOM 1368 OE1 GLN A 188 -126.689-108.189 621.707 1.00 38.99 O ANISOU 1368 OE1 GLN A 188 3886 6587 4342 -85 289 -817 O ATOM 1369 NE2 GLN A 188 -126.536-108.855 623.858 1.00 28.99 N ANISOU 1369 NE2 GLN A 188 2689 5162 3164 11 354 -787 N ATOM 1370 N PHE A 189 -121.972-105.395 623.651 1.00 25.72 N ANISOU 1370 N PHE A 189 2145 5026 2601 61 168 -621 N ATOM 1371 CA PHE A 189 -121.140-105.260 624.843 1.00 24.38 C ANISOU 1371 CA PHE A 189 1972 4836 2454 126 156 -600 C ATOM 1372 C PHE A 189 -121.848-104.395 625.868 1.00 22.02 C ANISOU 1372 C PHE A 189 1712 4486 2167 122 130 -549 C ATOM 1373 O PHE A 189 -121.998-104.784 627.021 1.00 23.43 O ANISOU 1373 O PHE A 189 1916 4608 2380 182 140 -550 O ATOM 1374 CB PHE A 189 -119.765-104.641 624.554 1.00 20.65 C ANISOU 1374 CB PHE A 189 1451 4446 1949 125 133 -585 C ATOM 1375 CG PHE A 189 -119.045-104.221 625.809 1.00 20.61 C ANISOU 1375 CG PHE A 189 1441 4430 1962 180 107 -560 C ATOM 1376 CD1 PHE A 189 -118.328-105.151 626.555 1.00 21.61 C ANISOU 1376 CD1 PHE A 189 1551 4545 2113 275 115 -597 C ATOM 1377 CD2 PHE A 189 -119.129-102.910 626.278 1.00 19.30 C ANISOU 1377 CD2 PHE A 189 1287 4258 1787 143 75 -502 C ATOM 1378 CE1 PHE A 189 -117.692-104.780 627.731 1.00 24.32 C ANISOU 1378 CE1 PHE A 189 1888 4888 2464 334 82 -580 C ATOM 1379 CE2 PHE A 189 -118.502-102.534 627.465 1.00 20.91 C ANISOU 1379 CE2 PHE A 189 1484 4451 2010 192 49 -487 C ATOM 1380 CZ PHE A 189 -117.782-103.467 628.188 1.00 24.41 C ANISOU 1380 CZ PHE A 189 1908 4897 2468 288 48 -527 C ATOM 1381 N TRP A 190 -122.264-103.206 625.448 1.00 18.80 N ANISOU 1381 N TRP A 190 1313 4102 1729 59 103 -503 N ATOM 1382 CA TRP A 190 -122.861-102.275 626.387 1.00 18.21 C ANISOU 1382 CA TRP A 190 1269 3981 1667 57 81 -456 C ATOM 1383 C TRP A 190 -124.197-102.778 626.898 1.00 19.57 C ANISOU 1383 C TRP A 190 1480 4082 1872 64 100 -472 C ATOM 1384 O TRP A 190 -124.504-102.600 628.077 1.00 17.84 O ANISOU 1384 O TRP A 190 1284 3814 1679 99 96 -457 O ATOM 1385 CB TRP A 190 -123.008-100.894 625.756 1.00 23.36 C ANISOU 1385 CB TRP A 190 1922 4666 2287 -6 60 -400 C ATOM 1386 CG TRP A 190 -121.681-100.217 625.650 1.00 33.67 C ANISOU 1386 CG TRP A 190 3191 6021 3579 -15 47 -372 C ATOM 1387 CD1 TRP A 190 -121.032 -99.844 624.503 1.00 35.45 C ANISOU 1387 CD1 TRP A 190 3382 6323 3766 -63 52 -360 C ATOM 1388 CD2 TRP A 190 -120.810 -99.867 626.736 1.00 37.74 C ANISOU 1388 CD2 TRP A 190 3693 6523 4124 21 30 -360 C ATOM 1389 NE1 TRP A 190 -119.820 -99.272 624.814 1.00 36.74 N ANISOU 1389 NE1 TRP A 190 3508 6512 3938 -65 42 -340 N ATOM 1390 CE2 TRP A 190 -119.660 -99.275 626.176 1.00 36.40 C ANISOU 1390 CE2 TRP A 190 3477 6415 3940 -13 25 -342 C ATOM 1391 CE3 TRP A 190 -120.896 -99.989 628.128 1.00 36.80 C ANISOU 1391 CE3 TRP A 190 3593 6353 4038 80 16 -364 C ATOM 1392 CZ2 TRP A 190 -118.611 -98.806 626.957 1.00 36.08 C ANISOU 1392 CZ2 TRP A 190 3405 6379 3927 5 4 -334 C ATOM 1393 CZ3 TRP A 190 -119.854 -99.527 628.896 1.00 34.91 C ANISOU 1393 CZ3 TRP A 190 3326 6123 3815 105 -10 -355 C ATOM 1394 CH2 TRP A 190 -118.724 -98.943 628.310 1.00 35.93 C ANISOU 1394 CH2 TRP A 190 3405 6307 3939 65 -17 -342 C ATOM 1395 N LYS A 191 -124.986-103.415 626.034 1.00 18.59 N ANISOU 1395 N LYS A 191 1359 3955 1748 30 124 -509 N ATOM 1396 CA LYS A 191 -126.275-103.953 626.473 1.00 20.51 C ANISOU 1396 CA LYS A 191 1633 4128 2031 27 154 -532 C ATOM 1397 C LYS A 191 -126.088-104.958 627.603 1.00 19.67 C ANISOU 1397 C LYS A 191 1550 3951 1971 94 200 -552 C ATOM 1398 O LYS A 191 -126.788-104.907 628.617 1.00 25.02 O ANISOU 1398 O LYS A 191 2262 4568 2676 113 218 -540 O ATOM 1399 CB LYS A 191 -127.024-104.608 625.310 1.00 22.65 C ANISOU 1399 CB LYS A 191 1896 4416 2295 -21 176 -581 C ATOM 1400 CG LYS A 191 -127.763-103.620 624.424 1.00 25.44 C ANISOU 1400 CG LYS A 191 2242 4825 2600 -77 138 -561 C ATOM 1401 CD LYS A 191 -128.299-104.293 623.169 1.00 29.84 C ANISOU 1401 CD LYS A 191 2778 5428 3132 -121 151 -620 C ATOM 1402 CE LYS A 191 -129.384-105.307 623.478 1.00 31.35 C ANISOU 1402 CE LYS A 191 2983 5553 3377 -131 197 -678 C ATOM 1403 NZ LYS A 191 -130.607-104.655 624.017 1.00 34.47 N ANISOU 1403 NZ LYS A 191 3396 5916 3786 -146 185 -660 N ATOM 1404 N ASN A 192 -125.146-105.874 627.418 1.00 17.94 N ANISOU 1404 N ASN A 192 1318 3743 1757 137 226 -584 N ATOM 1405 CA ASN A 192 -124.803-106.846 628.449 1.00 23.28 C ANISOU 1405 CA ASN A 192 2027 4354 2463 222 277 -600 C ATOM 1406 C ASN A 192 -124.251-106.196 629.705 1.00 23.90 C ANISOU 1406 C ASN A 192 2112 4438 2532 284 240 -560 C ATOM 1407 O ASN A 192 -124.614-106.571 630.813 1.00 24.00 O ANISOU 1407 O ASN A 192 2177 4383 2559 340 277 -556 O ATOM 1408 CB ASN A 192 -123.790-107.855 627.910 1.00 23.87 C ANISOU 1408 CB ASN A 192 2082 4450 2537 268 306 -644 C ATOM 1409 CG ASN A 192 -124.345-108.668 626.760 1.00 25.55 C ANISOU 1409 CG ASN A 192 2295 4654 2760 217 351 -697 C ATOM 1410 OD1 ASN A 192 -125.545-108.633 626.481 1.00 23.84 O ANISOU 1410 OD1 ASN A 192 2098 4408 2554 153 367 -705 O ATOM 1411 ND2 ASN A 192 -123.482-109.418 626.099 1.00 28.00 N ANISOU 1411 ND2 ASN A 192 2579 4994 3064 247 372 -739 N ATOM 1412 N PHE A 193 -123.366-105.223 629.528 1.00 22.33 N ANISOU 1412 N PHE A 193 1866 4318 2301 275 174 -533 N ATOM 1413 CA PHE A 193 -122.774-104.532 630.659 1.00 21.40 C ANISOU 1413 CA PHE A 193 1745 4218 2170 329 131 -502 C ATOM 1414 C PHE A 193 -123.875-103.903 631.510 1.00 20.79 C ANISOU 1414 C PHE A 193 1707 4092 2102 315 129 -474 C ATOM 1415 O PHE A 193 -123.947-104.120 632.730 1.00 22.44 O ANISOU 1415 O PHE A 193 1951 4264 2313 390 140 -470 O ATOM 1416 CB PHE A 193 -121.767-103.472 630.174 1.00 21.83 C ANISOU 1416 CB PHE A 193 1751 4351 2193 291 76 -478 C ATOM 1417 CG PHE A 193 -120.985-102.826 631.281 1.00 27.07 C ANISOU 1417 CG PHE A 193 2404 5033 2848 343 33 -458 C ATOM 1418 CD1 PHE A 193 -119.797-103.386 631.722 1.00 35.36 C ANISOU 1418 CD1 PHE A 193 3427 6117 3893 428 19 -483 C ATOM 1419 CD2 PHE A 193 -121.435-101.659 631.879 1.00 28.78 C ANISOU 1419 CD2 PHE A 193 2638 5232 3067 313 4 -419 C ATOM 1420 CE1 PHE A 193 -119.072-102.794 632.752 1.00 37.41 C ANISOU 1420 CE1 PHE A 193 3676 6394 4144 478 -30 -471 C ATOM 1421 CE2 PHE A 193 -120.715-101.059 632.904 1.00 30.86 C ANISOU 1421 CE2 PHE A 193 2893 5505 3329 357 -39 -407 C ATOM 1422 CZ PHE A 193 -119.536-101.628 633.342 1.00 34.05 C ANISOU 1422 CZ PHE A 193 3269 5945 3724 437 -58 -434 C ATOM 1423 N GLN A 194 -124.754-103.150 630.859 1.00 19.19 N ANISOU 1423 N GLN A 194 1505 3889 1899 231 118 -457 N ATOM 1424 CA GLN A 194 -125.812-102.444 631.564 1.00 21.62 C ANISOU 1424 CA GLN A 194 1839 4157 2217 216 113 -434 C ATOM 1425 C GLN A 194 -126.828-103.394 632.179 1.00 21.18 C ANISOU 1425 C GLN A 194 1834 4021 2194 238 182 -459 C ATOM 1426 O GLN A 194 -127.288-103.190 633.305 1.00 20.82 O ANISOU 1426 O GLN A 194 1823 3936 2152 274 196 -448 O ATOM 1427 CB GLN A 194 -126.506-101.472 630.619 1.00 23.67 C ANISOU 1427 CB GLN A 194 2091 4435 2467 134 88 -412 C ATOM 1428 CG GLN A 194 -125.661-100.265 630.301 1.00 29.40 C ANISOU 1428 CG GLN A 194 2795 5208 3166 111 43 -370 C ATOM 1429 CD GLN A 194 -125.353 -99.453 631.529 1.00 39.07 C ANISOU 1429 CD GLN A 194 4025 6419 4401 147 13 -344 C ATOM 1430 OE1 GLN A 194 -126.234 -99.191 632.343 1.00 45.11 O ANISOU 1430 OE1 GLN A 194 4811 7147 5180 163 14 -342 O ATOM 1431 NE2 GLN A 194 -124.093 -99.074 631.691 1.00 44.50 N ANISOU 1431 NE2 GLN A 194 4689 7136 5083 161 -13 -330 N ATOM 1432 N THR A 195 -127.181-104.439 631.449 1.00 18.84 N ANISOU 1432 N THR A 195 1549 3692 1918 214 236 -494 N ATOM 1433 CA THR A 195 -128.141-105.391 631.981 1.00 20.39 C ANISOU 1433 CA THR A 195 1809 3794 2145 221 322 -518 C ATOM 1434 C THR A 195 -127.547-106.139 633.177 1.00 21.91 C ANISOU 1434 C THR A 195 2063 3934 2326 322 370 -519 C ATOM 1435 O THR A 195 -128.196-106.276 634.208 1.00 22.81 O ANISOU 1435 O THR A 195 2247 3979 2440 347 419 -511 O ATOM 1436 CB THR A 195 -128.601-106.373 630.900 1.00 18.82 C ANISOU 1436 CB THR A 195 1610 3574 1967 172 373 -564 C ATOM 1437 OG1 THR A 195 -129.337-105.651 629.907 1.00 23.49 O ANISOU 1437 OG1 THR A 195 2156 4214 2554 91 326 -566 O ATOM 1438 CG2 THR A 195 -129.499-107.445 631.480 1.00 19.07 C ANISOU 1438 CG2 THR A 195 1717 3500 2027 176 477 -592 C ATOM 1439 N LEU A 196 -126.309-106.601 633.047 1.00 22.62 N ANISOU 1439 N LEU A 196 2136 4059 2400 386 354 -528 N ATOM 1440 CA LEU A 196 -125.668-107.339 634.132 1.00 26.09 C ANISOU 1440 CA LEU A 196 2642 4453 2816 505 386 -530 C ATOM 1441 C LEU A 196 -125.474-106.448 635.355 1.00 28.90 C ANISOU 1441 C LEU A 196 3012 4832 3136 564 333 -493 C ATOM 1442 O LEU A 196 -125.605-106.904 636.486 1.00 31.71 O ANISOU 1442 O LEU A 196 3463 5120 3463 647 374 -485 O ATOM 1443 CB LEU A 196 -124.321-107.914 633.686 1.00 25.52 C ANISOU 1443 CB LEU A 196 2532 4430 2735 572 363 -551 C ATOM 1444 CG LEU A 196 -124.343-109.118 632.736 1.00 28.78 C ANISOU 1444 CG LEU A 196 2959 4802 3175 556 433 -599 C ATOM 1445 CD1 LEU A 196 -122.943-109.673 632.588 1.00 30.73 C ANISOU 1445 CD1 LEU A 196 3175 5091 3409 652 408 -621 C ATOM 1446 CD2 LEU A 196 -125.301-110.199 633.223 1.00 27.83 C ANISOU 1446 CD2 LEU A 196 2955 4549 3071 566 548 -622 C ATOM 1447 N LYS A 197 -125.164-105.177 635.128 1.00 25.86 N ANISOU 1447 N LYS A 197 2544 4538 2744 525 245 -471 N ATOM 1448 CA LYS A 197 -124.994-104.259 636.238 1.00 25.16 C ANISOU 1448 CA LYS A 197 2460 4477 2622 577 192 -445 C ATOM 1449 C LYS A 197 -126.289-104.146 637.037 1.00 26.46 C ANISOU 1449 C LYS A 197 2705 4562 2788 562 247 -436 C ATOM 1450 O LYS A 197 -126.257-104.150 638.264 1.00 27.49 O ANISOU 1450 O LYS A 197 2908 4661 2875 646 253 -425 O ATOM 1451 CB LYS A 197 -124.542-102.885 635.753 1.00 29.42 C ANISOU 1451 CB LYS A 197 2907 5110 3161 515 102 -426 C ATOM 1452 CG LYS A 197 -124.242-101.929 636.893 1.00 38.14 C ANISOU 1452 CG LYS A 197 4009 6246 4239 570 41 -410 C ATOM 1453 CD LYS A 197 -123.595-100.640 636.414 1.00 42.72 C ANISOU 1453 CD LYS A 197 4525 6881 4826 497 -37 -389 C ATOM 1454 CE LYS A 197 -124.638 -99.586 636.100 1.00 42.23 C ANISOU 1454 CE LYS A 197 4465 6793 4786 407 -39 -367 C ATOM 1455 NZ LYS A 197 -125.561 -99.980 635.010 1.00 43.88 N ANISOU 1455 NZ LYS A 197 4679 6980 5014 334 11 -371 N ATOM 1456 N ILE A 198 -127.429-104.072 636.353 1.00 26.58 N ANISOU 1456 N ILE A 198 2712 4543 2844 459 285 -443 N ATOM 1457 CA ILE A 198 -128.716-104.005 637.056 1.00 28.35 C ANISOU 1457 CA ILE A 198 3003 4692 3077 434 344 -442 C ATOM 1458 C ILE A 198 -129.054-105.332 637.730 1.00 26.34 C ANISOU 1458 C ILE A 198 2867 4329 2812 476 452 -455 C ATOM 1459 O ILE A 198 -129.519-105.356 638.868 1.00 25.86 O ANISOU 1459 O ILE A 198 2895 4211 2720 514 494 -443 O ATOM 1460 CB ILE A 198 -129.887-103.612 636.113 1.00 27.17 C ANISOU 1460 CB ILE A 198 2808 4541 2976 322 350 -452 C ATOM 1461 CG1 ILE A 198 -130.020-102.091 636.020 1.00 31.38 C ANISOU 1461 CG1 ILE A 198 3274 5143 3506 295 264 -431 C ATOM 1462 CG2 ILE A 198 -131.220-104.155 636.633 1.00 24.83 C ANISOU 1462 CG2 ILE A 198 2584 4150 2702 292 446 -467 C ATOM 1463 CD1 ILE A 198 -128.996-101.417 635.153 1.00 35.31 C ANISOU 1463 CD1 ILE A 198 3696 5729 3989 278 179 -415 C ATOM 1464 N VAL A 199 -128.812-106.435 637.031 1.00 23.20 N ANISOU 1464 N VAL A 199 2480 3901 2433 471 503 -480 N ATOM 1465 CA VAL A 199 -129.229-107.737 637.532 1.00 24.71 C ANISOU 1465 CA VAL A 199 2790 3980 2618 497 622 -499 C ATOM 1466 C VAL A 199 -128.328-108.246 638.657 1.00 28.10 C ANISOU 1466 C VAL A 199 3318 4377 2981 638 623 -478 C ATOM 1467 O VAL A 199 -128.806-108.812 639.635 1.00 30.28 O ANISOU 1467 O VAL A 199 3722 4559 3223 675 701 -466 O ATOM 1468 CB VAL A 199 -129.268-108.767 636.403 1.00 23.99 C ANISOU 1468 CB VAL A 199 2685 3864 2567 453 679 -541 C ATOM 1469 CG1 VAL A 199 -129.610-110.140 636.952 1.00 24.85 C ANISOU 1469 CG1 VAL A 199 2926 3851 2665 487 812 -567 C ATOM 1470 CG2 VAL A 199 -130.284-108.345 635.364 1.00 24.48 C ANISOU 1470 CG2 VAL A 199 2669 3953 2679 332 668 -554 C ATOM 1471 N ILE A 200 -127.024-108.041 638.531 1.00 27.93 N ANISOU 1471 N ILE A 200 3243 4432 2937 722 533 -468 N ATOM 1472 CA ILE A 200 -126.120-108.452 639.590 1.00 24.62 C ANISOU 1472 CA ILE A 200 2916 3989 2450 878 510 -442 C ATOM 1473 C ILE A 200 -126.416-107.633 640.852 1.00 26.10 C ANISOU 1473 C ILE A 200 3165 4171 2581 917 479 -403 C ATOM 1474 O ILE A 200 -126.726-108.196 641.904 1.00 27.77 O ANISOU 1474 O ILE A 200 3526 4284 2740 983 537 -375 O ATOM 1475 CB ILE A 200 -124.645-108.308 639.156 1.00 23.05 C ANISOU 1475 CB ILE A 200 2621 3892 2245 957 411 -450 C ATOM 1476 CG1 ILE A 200 -124.348-109.256 637.998 1.00 18.27 C ANISOU 1476 CG1 ILE A 200 1978 3277 1688 929 453 -491 C ATOM 1477 CG2 ILE A 200 -123.721-108.666 640.288 1.00 27.25 C ANISOU 1477 CG2 ILE A 200 3242 4406 2705 1133 370 -424 C ATOM 1478 CD1 ILE A 200 -122.991-109.054 637.381 1.00 18.59 C ANISOU 1478 CD1 ILE A 200 1901 3429 1733 974 363 -505 C ATOM 1479 N LEU A 201 -126.374-106.309 640.739 1.00 24.99 N ANISOU 1479 N LEU A 201 2919 4128 2448 872 394 -401 N ATOM 1480 CA LEU A 201 -126.624-105.436 641.892 1.00 22.03 C ANISOU 1480 CA LEU A 201 2595 3753 2023 904 355 -375 C ATOM 1481 C LEU A 201 -128.070-105.486 642.393 1.00 22.74 C ANISOU 1481 C LEU A 201 2768 3752 2118 833 451 -370 C ATOM 1482 O LEU A 201 -128.323-105.384 643.598 1.00 27.47 O ANISOU 1482 O LEU A 201 3479 4301 2657 887 465 -344 O ATOM 1483 CB LEU A 201 -126.250-103.988 641.557 1.00 18.12 C ANISOU 1483 CB LEU A 201 1966 3367 1551 858 241 -379 C ATOM 1484 CG LEU A 201 -124.765-103.726 641.293 1.00 22.48 C ANISOU 1484 CG LEU A 201 2431 4011 2100 914 132 -381 C ATOM 1485 CD1 LEU A 201 -124.535-102.265 640.999 1.00 26.19 C ANISOU 1485 CD1 LEU A 201 2784 4570 2597 846 37 -382 C ATOM 1486 CD2 LEU A 201 -123.907-104.165 642.469 1.00 21.16 C ANISOU 1486 CD2 LEU A 201 2361 3813 1867 1053 84 -359 C ATOM 1487 N GLY A 202 -129.026-105.654 641.490 1.00 22.66 N ANISOU 1487 N GLY A 202 2707 3722 2182 709 515 -396 N ATOM 1488 CA GLY A 202 -130.422-105.624 641.897 1.00 20.44 C ANISOU 1488 CA GLY A 202 2476 3370 1918 630 603 -402 C ATOM 1489 C GLY A 202 -131.052-106.958 642.265 1.00 24.40 C ANISOU 1489 C GLY A 202 3104 3755 2413 619 740 -409 C ATOM 1490 O GLY A 202 -132.141-106.988 642.841 1.00 26.40 O ANISOU 1490 O GLY A 202 3410 3953 2667 562 821 -416 O ATOM 1491 N LEU A 203 -130.388-108.063 641.935 1.00 26.22 N ANISOU 1491 N LEU A 203 3377 3948 2636 669 771 -412 N ATOM 1492 CA LEU A 203 -130.995-109.381 642.121 1.00 29.49 C ANISOU 1492 CA LEU A 203 3907 4244 3053 647 906 -424 C ATOM 1493 C LEU A 203 -130.037-110.401 642.711 1.00 32.53 C ANISOU 1493 C LEU A 203 4435 4546 3379 787 919 -382 C ATOM 1494 O LEU A 203 -130.314-110.979 643.754 1.00 36.18 O ANISOU 1494 O LEU A 203 5057 4899 3790 829 988 -338 O ATOM 1495 CB LEU A 203 -131.536-109.916 640.792 1.00 29.00 C ANISOU 1495 CB LEU A 203 3755 4195 3070 532 964 -496 C ATOM 1496 CG LEU A 203 -132.400-111.169 640.929 1.00 28.42 C ANISOU 1496 CG LEU A 203 3774 4018 3008 484 1088 -516 C ATOM 1497 CD1 LEU A 203 -133.642-110.825 641.702 1.00 29.82 C ANISOU 1497 CD1 LEU A 203 3978 4171 3182 416 1133 -501 C ATOM 1498 CD2 LEU A 203 -132.771-111.724 639.571 1.00 30.46 C ANISOU 1498 CD2 LEU A 203 3939 4310 3324 411 1106 -574 C ATOM 1499 N VAL A 204 -128.921-110.633 642.029 1.00 31.64 N ANISOU 1499 N VAL A 204 4265 4482 3273 859 855 -394 N ATOM 1500 CA VAL A 204 -127.935-111.607 642.483 1.00 29.60 C ANISOU 1500 CA VAL A 204 4130 4151 2964 1011 856 -362 C ATOM 1501 C VAL A 204 -127.336-111.235 643.840 1.00 30.45 C ANISOU 1501 C VAL A 204 4342 4254 2974 1150 789 -295 C ATOM 1502 O VAL A 204 -127.340-112.037 644.773 1.00 31.66 O ANISOU 1502 O VAL A 204 4676 4285 3068 1231 844 -244 O ATOM 1503 CB VAL A 204 -126.800-111.753 641.467 1.00 30.08 C ANISOU 1503 CB VAL A 204 4075 4297 3058 1062 780 -399 C ATOM 1504 CG1 VAL A 204 -125.851-112.862 641.890 1.00 30.76 C ANISOU 1504 CG1 VAL A 204 4289 4298 3102 1228 786 -374 C ATOM 1505 CG2 VAL A 204 -127.369-112.028 640.083 1.00 31.58 C ANISOU 1505 CG2 VAL A 204 4156 4508 3333 921 835 -469 C ATOM 1506 N LEU A 205 -126.815-110.017 643.942 1.00 31.39 N ANISOU 1506 N LEU A 205 4348 4499 3079 1165 661 -294 N ATOM 1507 CA LEU A 205 -126.205-109.558 645.181 1.00 32.36 C ANISOU 1507 CA LEU A 205 4545 4633 3117 1278 571 -243 C ATOM 1508 C LEU A 205 -127.161-109.652 646.384 1.00 33.25 C ANISOU 1508 C LEU A 205 4822 4647 3164 1271 656 -199 C ATOM 1509 O LEU A 205 -126.808-110.275 647.387 1.00 31.17 O ANISOU 1509 O LEU A 205 4722 4304 2818 1387 664 -144 O ATOM 1510 CB LEU A 205 -125.684-108.125 645.017 1.00 33.74 C ANISOU 1510 CB LEU A 205 4562 4956 3303 1258 433 -263 C ATOM 1511 CG LEU A 205 -125.200-107.444 646.294 1.00 32.69 C ANISOU 1511 CG LEU A 205 4487 4848 3085 1349 336 -228 C ATOM 1512 CD1 LEU A 205 -123.981-108.172 646.826 1.00 35.00 C ANISOU 1512 CD1 LEU A 205 4852 5128 3316 1517 269 -199 C ATOM 1513 CD2 LEU A 205 -124.907-105.969 646.055 1.00 28.09 C ANISOU 1513 CD2 LEU A 205 3750 4393 2532 1293 219 -258 C ATOM 1514 N PRO A 206 -128.377-109.063 646.295 1.00 30.49 N ANISOU 1514 N PRO A 206 4432 4302 2850 1135 721 -222 N ATOM 1515 CA PRO A 206 -129.224-109.180 647.492 1.00 31.36 C ANISOU 1515 CA PRO A 206 4689 4321 2905 1120 797 -179 C ATOM 1516 C PRO A 206 -129.736-110.605 647.761 1.00 37.98 C ANISOU 1516 C PRO A 206 5694 5004 3732 1114 944 -147 C ATOM 1517 O PRO A 206 -130.058-110.915 648.908 1.00 41.12 O ANISOU 1517 O PRO A 206 6252 5317 4053 1151 999 -92 O ATOM 1518 CB PRO A 206 -130.385-108.233 647.189 1.00 27.30 C ANISOU 1518 CB PRO A 206 4057 3855 2460 966 819 -222 C ATOM 1519 CG PRO A 206 -130.456-108.188 645.710 1.00 19.52 C ANISOU 1519 CG PRO A 206 2914 2930 1574 877 813 -279 C ATOM 1520 CD PRO A 206 -129.039-108.279 645.234 1.00 25.70 C ANISOU 1520 CD PRO A 206 3649 3775 2339 987 714 -277 C ATOM 1521 N LEU A 207 -129.810-111.450 646.732 1.00 40.08 N ANISOU 1521 N LEU A 207 5928 5229 4072 1065 1008 -182 N ATOM 1522 CA LEU A 207 -130.138-112.864 646.936 1.00 41.24 C ANISOU 1522 CA LEU A 207 6245 5215 4211 1071 1145 -155 C ATOM 1523 C LEU A 207 -129.024-113.539 647.707 1.00 45.43 C ANISOU 1523 C LEU A 207 6946 5676 4637 1271 1114 -88 C ATOM 1524 O LEU A 207 -129.270-114.323 648.623 1.00 49.42 O ANISOU 1524 O LEU A 207 7659 6047 5071 1320 1206 -23 O ATOM 1525 CB LEU A 207 -130.346-113.595 645.610 1.00 36.54 C ANISOU 1525 CB LEU A 207 5570 4596 3718 982 1206 -221 C ATOM 1526 CG LEU A 207 -131.778-113.703 645.097 1.00 34.47 C ANISOU 1526 CG LEU A 207 5242 4313 3541 787 1311 -275 C ATOM 1527 CD1 LEU A 207 -131.796-114.379 643.736 1.00 33.02 C ANISOU 1527 CD1 LEU A 207 4971 4128 3447 718 1343 -349 C ATOM 1528 CD2 LEU A 207 -132.629-114.457 646.080 1.00 33.47 C ANISOU 1528 CD2 LEU A 207 5297 4037 3381 750 1450 -228 C ATOM 1529 N LEU A 208 -127.792-113.233 647.314 1.00 41.83 N ANISOU 1529 N LEU A 208 6393 5318 4182 1378 971 -101 N ATOM 1530 CA LEU A 208 -126.620-113.809 647.954 1.00 43.50 C ANISOU 1530 CA LEU A 208 6719 5490 4319 1569 895 -43 C ATOM 1531 C LEU A 208 -126.560-113.387 649.419 1.00 43.93 C ANISOU 1531 C LEU A 208 6903 5539 4248 1657 853 28 C ATOM 1532 O LEU A 208 -126.278-114.204 650.295 1.00 44.94 O ANISOU 1532 O LEU A 208 7229 5557 4288 1779 878 101 O ATOM 1533 CB LEU A 208 -125.350-113.388 647.209 1.00 43.52 C ANISOU 1533 CB LEU A 208 6547 5631 4359 1645 741 -86 C ATOM 1534 CG LEU A 208 -124.018-113.995 647.650 1.00 47.01 C ANISOU 1534 CG LEU A 208 7061 6059 4741 1850 646 -48 C ATOM 1535 CD1 LEU A 208 -124.161-115.481 647.869 1.00 50.23 C ANISOU 1535 CD1 LEU A 208 7676 6277 5134 1920 761 -3 C ATOM 1536 CD2 LEU A 208 -122.952-113.727 646.601 1.00 47.33 C ANISOU 1536 CD2 LEU A 208 6900 6234 4849 1883 537 -113 C ATOM 1537 N VAL A 209 -126.838-112.109 649.675 1.00 38.77 N ANISOU 1537 N VAL A 209 6145 5002 3582 1596 788 5 N ATOM 1538 CA VAL A 209 -126.861-111.591 651.030 1.00 35.37 C ANISOU 1538 CA VAL A 209 5824 4582 3032 1665 749 56 C ATOM 1539 C VAL A 209 -127.957-112.286 651.802 1.00 38.34 C ANISOU 1539 C VAL A 209 6401 4813 3352 1619 920 108 C ATOM 1540 O VAL A 209 -127.737-112.742 652.921 1.00 42.84 O ANISOU 1540 O VAL A 209 7163 5312 3802 1733 929 185 O ATOM 1541 CB VAL A 209 -127.090-110.063 651.070 1.00 33.95 C ANISOU 1541 CB VAL A 209 5491 4543 2867 1589 663 7 C ATOM 1542 CG1 VAL A 209 -127.552-109.617 652.459 1.00 33.18 C ANISOU 1542 CG1 VAL A 209 5512 4424 2670 1606 668 50 C ATOM 1543 CG2 VAL A 209 -125.823-109.323 650.668 1.00 32.86 C ANISOU 1543 CG2 VAL A 209 5191 4543 2750 1658 481 -28 C ATOM 1544 N MET A 210 -129.133-112.379 651.190 1.00 36.86 N ANISOU 1544 N MET A 210 6151 4585 3270 1436 1040 71 N ATOM 1545 CA MET A 210 -130.282-112.978 651.851 1.00 36.43 C ANISOU 1545 CA MET A 210 6239 4401 3203 1345 1197 111 C ATOM 1546 C MET A 210 -129.992-114.408 652.255 1.00 42.35 C ANISOU 1546 C MET A 210 7227 4984 3881 1448 1296 185 C ATOM 1547 O MET A 210 -130.209-114.790 653.404 1.00 47.00 O ANISOU 1547 O MET A 210 8008 5482 4370 1496 1352 264 O ATOM 1548 CB MET A 210 -131.513-112.941 650.953 1.00 35.98 C ANISOU 1548 CB MET A 210 6049 4340 3281 1136 1298 41 C ATOM 1549 CG MET A 210 -132.750-113.492 651.639 1.00 40.27 C ANISOU 1549 CG MET A 210 6713 4768 3820 1028 1457 70 C ATOM 1550 SD MET A 210 -134.231-113.406 650.628 1.00 76.78 S ANISOU 1550 SD MET A 210 11159 9414 8598 791 1554 -26 S ATOM 1551 CE MET A 210 -133.914-114.755 649.495 1.00 48.54 C ANISOU 1551 CE MET A 210 7622 5732 5089 780 1634 -49 C ATOM 1552 N VAL A 211 -129.495-115.190 651.301 1.00 44.23 N ANISOU 1552 N VAL A 211 7455 5178 4173 1484 1317 157 N ATOM 1553 CA VAL A 211 -129.138-116.583 651.538 1.00 42.99 C ANISOU 1553 CA VAL A 211 7505 4847 3983 1580 1388 223 C ATOM 1554 C VAL A 211 -128.156-116.711 652.703 1.00 45.37 C ANISOU 1554 C VAL A 211 7967 5133 4140 1791 1285 319 C ATOM 1555 O VAL A 211 -128.459-117.352 653.709 1.00 45.83 O ANISOU 1555 O VAL A 211 8259 5061 4096 1838 1378 409 O ATOM 1556 CB VAL A 211 -128.531-117.219 650.273 1.00 37.56 C ANISOU 1556 CB VAL A 211 6721 4144 3405 1595 1362 166 C ATOM 1557 CG1 VAL A 211 -127.818-118.507 650.612 1.00 36.91 C ANISOU 1557 CG1 VAL A 211 6845 3901 3278 1752 1382 237 C ATOM 1558 CG2 VAL A 211 -129.614-117.458 649.234 1.00 34.22 C ANISOU 1558 CG2 VAL A 211 6204 3690 3107 1390 1498 83 C ATOM 1559 N ILE A 212 -126.991-116.083 652.565 1.00 45.47 N ANISOU 1559 N ILE A 212 7852 5285 4141 1916 1095 297 N ATOM 1560 CA ILE A 212 -125.967-116.100 653.607 1.00 46.39 C ANISOU 1560 CA ILE A 212 8083 5419 4121 2124 968 371 C ATOM 1561 C ILE A 212 -126.505-115.662 654.968 1.00 51.04 C ANISOU 1561 C ILE A 212 8818 6004 4570 2133 997 435 C ATOM 1562 O ILE A 212 -126.377-116.383 655.963 1.00 54.68 O ANISOU 1562 O ILE A 212 9515 6353 4906 2250 1032 534 O ATOM 1563 CB ILE A 212 -124.789-115.189 653.231 1.00 45.96 C ANISOU 1563 CB ILE A 212 7817 5556 4088 2211 758 312 C ATOM 1564 CG1 ILE A 212 -124.015-115.785 652.055 1.00 47.91 C ANISOU 1564 CG1 ILE A 212 7954 5806 4443 2253 720 263 C ATOM 1565 CG2 ILE A 212 -123.875-114.974 654.424 1.00 47.63 C ANISOU 1565 CG2 ILE A 212 8126 5819 4151 2405 617 373 C ATOM 1566 CD1 ILE A 212 -123.059-114.805 651.399 1.00 48.88 C ANISOU 1566 CD1 ILE A 212 7823 6129 4620 2274 548 185 C ATOM 1567 N CYS A 213 -127.121-114.489 655.011 1.00 44.89 N ANISOU 1567 N CYS A 213 7906 5343 3807 2011 985 379 N ATOM 1568 CA CYS A 213 -127.538-113.934 656.283 1.00 44.83 C ANISOU 1568 CA CYS A 213 7964 5343 3725 2000 969 418 C ATOM 1569 C CYS A 213 -128.653-114.736 656.950 1.00 50.68 C ANISOU 1569 C CYS A 213 8892 5916 4449 1912 1156 481 C ATOM 1570 O CYS A 213 -128.668-114.883 658.175 1.00 51.08 O ANISOU 1570 O CYS A 213 9090 5916 4402 1979 1155 544 O ATOM 1571 CB CYS A 213 -127.971-112.480 656.105 1.00 37.49 C ANISOU 1571 CB CYS A 213 6815 4562 2870 1870 900 334 C ATOM 1572 SG CYS A 213 -126.585-111.368 655.793 1.00 57.01 S ANISOU 1572 SG CYS A 213 9096 7231 5334 1981 661 273 S ATOM 1573 N TYR A 214 -129.577-115.266 656.157 1.00 53.58 N ANISOU 1573 N TYR A 214 9244 6198 4916 1757 1315 454 N ATOM 1574 CA TYR A 214 -130.748-115.911 656.738 1.00 58.68 C ANISOU 1574 CA TYR A 214 10032 6700 5565 1638 1497 495 C ATOM 1575 C TYR A 214 -130.497-117.353 657.127 1.00 64.31 C ANISOU 1575 C TYR A 214 11015 7218 6202 1739 1600 593 C ATOM 1576 O TYR A 214 -131.322-117.974 657.800 1.00 66.33 O ANISOU 1576 O TYR A 214 11423 7339 6440 1665 1745 641 O ATOM 1577 CB TYR A 214 -131.937-115.819 655.787 1.00 59.41 C ANISOU 1577 CB TYR A 214 9974 6792 5806 1412 1617 413 C ATOM 1578 CG TYR A 214 -132.704-114.554 656.033 1.00 60.20 C ANISOU 1578 CG TYR A 214 9898 7025 5950 1291 1575 351 C ATOM 1579 CD1 TYR A 214 -133.286-114.325 657.272 1.00 63.35 C ANISOU 1579 CD1 TYR A 214 10386 7406 6277 1274 1613 388 C ATOM 1580 CD2 TYR A 214 -132.814-113.572 655.055 1.00 57.28 C ANISOU 1580 CD2 TYR A 214 9279 6799 5686 1206 1493 255 C ATOM 1581 CE1 TYR A 214 -133.974-113.166 657.534 1.00 64.58 C ANISOU 1581 CE1 TYR A 214 10391 7681 6464 1179 1578 328 C ATOM 1582 CE2 TYR A 214 -133.506-112.402 655.304 1.00 59.28 C ANISOU 1582 CE2 TYR A 214 9388 7165 5972 1112 1455 201 C ATOM 1583 CZ TYR A 214 -134.083-112.209 656.552 1.00 63.47 C ANISOU 1583 CZ TYR A 214 10015 7673 6428 1102 1499 236 C ATOM 1584 OH TYR A 214 -134.769-111.063 656.843 1.00 62.12 O ANISOU 1584 OH TYR A 214 9711 7609 6281 1023 1467 178 O ATOM 1585 N SER A 215 -129.358-117.889 656.717 1.00 66.47 N ANISOU 1585 N SER A 215 11349 7474 6433 1910 1526 621 N ATOM 1586 CA SER A 215 -128.974-119.191 657.217 1.00 70.35 C ANISOU 1586 CA SER A 215 12109 7780 6843 2042 1591 725 C ATOM 1587 C SER A 215 -128.276-119.000 658.559 1.00 70.51 C ANISOU 1587 C SER A 215 12221 7830 6738 2211 1459 784 C ATOM 1588 O SER A 215 -128.391-119.831 659.453 1.00 74.60 O ANISOU 1588 O SER A 215 12948 8209 7189 2262 1531 857 O ATOM 1589 CB SER A 215 -128.089-119.928 656.218 1.00 74.75 C ANISOU 1589 CB SER A 215 12660 8290 7451 2147 1549 716 C ATOM 1590 OG SER A 215 -128.884-120.502 655.194 1.00 77.18 O ANISOU 1590 OG SER A 215 12915 8502 7908 1968 1701 652 O ATOM 1591 N GLY A 216 -127.577-117.882 658.710 1.00 66.52 N ANISOU 1591 N GLY A 216 11547 7517 6210 2283 1269 737 N ATOM 1592 CA GLY A 216 -126.956-117.554 659.979 1.00 66.69 C ANISOU 1592 CA GLY A 216 11618 7596 6125 2417 1142 763 C ATOM 1593 C GLY A 216 -127.985-117.197 661.040 1.00 65.11 C ANISOU 1593 C GLY A 216 11475 7374 5888 2302 1231 778 C ATOM 1594 O GLY A 216 -127.778-117.461 662.226 1.00 66.69 O ANISOU 1594 O GLY A 216 11817 7539 5984 2394 1212 830 O ATOM 1595 N ILE A 217 -129.100-116.607 660.607 1.00 60.96 N ANISOU 1595 N ILE A 217 10831 6879 5450 2099 1326 727 N ATOM 1596 CA ILE A 217 -130.133-116.102 661.514 1.00 58.06 C ANISOU 1596 CA ILE A 217 10473 6523 5063 1977 1400 723 C ATOM 1597 C ILE A 217 -131.144-117.175 661.934 1.00 64.11 C ANISOU 1597 C ILE A 217 11432 7105 5821 1881 1613 782 C ATOM 1598 O ILE A 217 -131.486-117.277 663.116 1.00 66.56 O ANISOU 1598 O ILE A 217 11868 7380 6043 1891 1655 827 O ATOM 1599 CB ILE A 217 -130.880-114.911 660.875 1.00 49.90 C ANISOU 1599 CB ILE A 217 9199 5623 4137 1804 1392 625 C ATOM 1600 CG1 ILE A 217 -129.999-113.661 660.922 1.00 48.69 C ANISOU 1600 CG1 ILE A 217 8880 5654 3967 1889 1183 569 C ATOM 1601 CG2 ILE A 217 -132.195-114.635 661.589 1.00 46.93 C ANISOU 1601 CG2 ILE A 217 8835 5232 3765 1650 1517 616 C ATOM 1602 CD1 ILE A 217 -130.563-112.476 660.173 1.00 43.58 C ANISOU 1602 CD1 ILE A 217 7993 5136 3430 1740 1156 471 C ATOM 1603 N LEU A 218 -131.618-117.975 660.981 1.00 65.91 N ANISOU 1603 N LEU A 218 11683 7217 6141 1784 1749 778 N ATOM 1604 CA LEU A 218 -132.551-119.054 661.304 1.00 70.64 C ANISOU 1604 CA LEU A 218 12462 7630 6746 1680 1957 825 C ATOM 1605 C LEU A 218 -131.885-120.066 662.245 1.00 73.58 C ANISOU 1605 C LEU A 218 13095 7870 6991 1852 1960 927 C ATOM 1606 O LEU A 218 -132.531-120.634 663.130 1.00 72.95 O ANISOU 1606 O LEU A 218 13178 7683 6859 1805 2085 978 O ATOM 1607 CB LEU A 218 -133.045-119.746 660.030 1.00 73.74 C ANISOU 1607 CB LEU A 218 12825 7924 7268 1550 2090 789 C ATOM 1608 CG LEU A 218 -134.494-120.249 660.065 1.00 78.14 C ANISOU 1608 CG LEU A 218 13416 8372 7901 1330 2303 768 C ATOM 1609 CD1 LEU A 218 -135.452-119.147 659.633 1.00 77.52 C ANISOU 1609 CD1 LEU A 218 13078 8450 7928 1146 2300 663 C ATOM 1610 CD2 LEU A 218 -134.687-121.504 659.221 1.00 80.11 C ANISOU 1610 CD2 LEU A 218 13774 8438 8228 1266 2454 772 C ATOM 1611 N LYS A 219 -130.587-120.277 662.037 1.00 74.98 N ANISOU 1611 N LYS A 219 13298 8068 7122 2051 1818 950 N ATOM 1612 CA LYS A 219 -129.746-121.067 662.936 1.00 77.44 C ANISOU 1612 CA LYS A 219 13811 8301 7309 2244 1767 1030 C ATOM 1613 C LYS A 219 -129.900-120.602 664.378 1.00 75.64 C ANISOU 1613 C LYS A 219 13643 8132 6965 2275 1731 1060 C ATOM 1614 O LYS A 219 -130.292-121.367 665.258 1.00 77.87 O ANISOU 1614 O LYS A 219 14126 8289 7172 2274 1840 1130 O ATOM 1615 CB LYS A 219 -128.280-120.963 662.500 1.00 82.07 C ANISOU 1615 CB LYS A 219 14326 8981 7876 2448 1568 1016 C ATOM 1616 CG LYS A 219 -127.248-121.463 663.503 1.00 89.07 C ANISOU 1616 CG LYS A 219 15351 9859 8632 2661 1457 1072 C ATOM 1617 CD LYS A 219 -125.848-121.401 662.889 1.00 92.01 C ANISOU 1617 CD LYS A 219 15612 10334 9015 2836 1268 1037 C ATOM 1618 CE LYS A 219 -124.860-120.678 663.803 1.00 94.58 C ANISOU 1618 CE LYS A 219 15867 10826 9244 2986 1064 1016 C ATOM 1619 NZ LYS A 219 -123.437-120.909 663.415 1.00 95.64 N ANISOU 1619 NZ LYS A 219 15926 11039 9375 3167 894 988 N ATOM 1620 N THR A 220 -129.594-119.330 664.602 1.00 71.56 N ANISOU 1620 N THR A 220 12951 7805 6433 2297 1579 1005 N ATOM 1621 CA THR A 220 -129.674-118.728 665.923 1.00 69.38 C ANISOU 1621 CA THR A 220 12707 7607 6047 2327 1527 1020 C ATOM 1622 C THR A 220 -131.113-118.665 666.432 1.00 70.92 C ANISOU 1622 C THR A 220 12945 7750 6249 2137 1706 1028 C ATOM 1623 O THR A 220 -131.364-118.852 667.624 1.00 73.57 O ANISOU 1623 O THR A 220 13423 8056 6474 2159 1748 1081 O ATOM 1624 CB THR A 220 -129.058-117.313 665.908 1.00 66.20 C ANISOU 1624 CB THR A 220 12086 7419 5648 2371 1330 942 C ATOM 1625 OG1 THR A 220 -127.675-117.405 665.543 1.00 68.07 O ANISOU 1625 OG1 THR A 220 12278 7713 5871 2551 1160 929 O ATOM 1626 CG2 THR A 220 -129.172-116.643 667.267 1.00 64.70 C ANISOU 1626 CG2 THR A 220 11927 7312 5345 2394 1280 947 C ATOM 1627 N LEU A 221 -132.059-118.438 665.525 1.00 70.48 N ANISOU 1627 N LEU A 221 12764 7691 6325 1948 1813 971 N ATOM 1628 CA LEU A 221 -133.449-118.204 665.916 1.00 75.37 C ANISOU 1628 CA LEU A 221 13366 8301 6970 1755 1966 952 C ATOM 1629 C LEU A 221 -134.178-119.416 666.498 1.00 81.22 C ANISOU 1629 C LEU A 221 14332 8855 7671 1692 2164 1026 C ATOM 1630 O LEU A 221 -134.981-119.267 667.419 1.00 85.46 O ANISOU 1630 O LEU A 221 14920 9399 8153 1612 2250 1040 O ATOM 1631 CB LEU A 221 -134.248-117.676 664.727 1.00 73.21 C ANISOU 1631 CB LEU A 221 12876 8083 6857 1570 2019 859 C ATOM 1632 CG LEU A 221 -134.672-116.209 664.843 1.00 71.43 C ANISOU 1632 CG LEU A 221 12434 8048 6659 1492 1939 775 C ATOM 1633 CD1 LEU A 221 -135.893-115.937 663.972 1.00 70.36 C ANISOU 1633 CD1 LEU A 221 12129 7936 6670 1275 2053 692 C ATOM 1634 CD2 LEU A 221 -134.940-115.824 666.293 1.00 72.52 C ANISOU 1634 CD2 LEU A 221 12657 8229 6669 1519 1939 804 C ATOM 1635 N LEU A 222 -133.925-120.606 665.966 1.00 85.53 N ANISOU 1635 N LEU A 222 15013 9236 8246 1723 2240 1069 N ATOM 1636 CA LEU A 222 -134.618-121.794 666.465 1.00 88.67 C ANISOU 1636 CA LEU A 222 15630 9445 8615 1653 2435 1135 C ATOM 1637 C LEU A 222 -133.871-122.501 667.600 1.00 91.04 C ANISOU 1637 C LEU A 222 16170 9668 8753 1837 2398 1240 C ATOM 1638 O LEU A 222 -134.157-123.657 667.911 1.00 94.42 O ANISOU 1638 O LEU A 222 16806 9918 9149 1820 2539 1307 O ATOM 1639 CB LEU A 222 -134.895-122.783 665.325 1.00 91.76 C ANISOU 1639 CB LEU A 222 16054 9680 9129 1562 2565 1120 C ATOM 1640 CG LEU A 222 -136.061-122.418 664.396 1.00 91.70 C ANISOU 1640 CG LEU A 222 15857 9703 9282 1322 2677 1022 C ATOM 1641 CD1 LEU A 222 -135.608-121.562 663.224 1.00 89.56 C ANISOU 1641 CD1 LEU A 222 15349 9572 9108 1329 2545 942 C ATOM 1642 CD2 LEU A 222 -136.807-123.666 663.915 1.00 92.13 C ANISOU 1642 CD2 LEU A 222 16030 9556 9419 1179 2887 1023 C ATOM 1643 N ARG A 223 -132.930-121.804 668.228 1.00 83.18 N ANISOU 1643 N ARG A 223 15141 8807 7654 2008 2209 1249 N ATOM 1644 CA ARG A 223 -132.317-122.308 669.449 1.00 76.63 C ANISOU 1644 CA ARG A 223 14517 7938 6660 2172 2164 1339 C ATOM 1645 C ARG A 223 -133.345-122.185 670.579 1.00 74.13 C ANISOU 1645 C ARG A 223 14288 7615 6265 2060 2290 1372 C ATOM 1646 O ARG A 223 -134.329-121.461 670.438 1.00 73.69 O ANISOU 1646 O ARG A 223 14090 7633 6277 1886 2360 1309 O ATOM 1647 CB ARG A 223 -131.033-121.541 669.767 1.00 72.70 C ANISOU 1647 CB ARG A 223 13933 7603 6085 2372 1920 1322 C ATOM 1648 CG ARG A 223 -130.081-122.279 670.689 1.00 77.17 C ANISOU 1648 CG ARG A 223 14699 8119 6503 2581 1844 1408 C ATOM 1649 N MET A1001 -133.123-122.895 671.685 1.00 79.67 N ANISOU 1649 N MET A1001 16376 7035 6859 1429 3744 739 N ATOM 1650 CA MET A1001 -134.099-122.977 672.779 1.00 72.87 C ANISOU 1650 CA MET A1001 15381 6285 6023 1168 3437 675 C ATOM 1651 C MET A1001 -134.433-121.614 673.401 1.00 69.09 C ANISOU 1651 C MET A1001 14334 6232 5684 999 3110 745 C ATOM 1652 O MET A1001 -133.548-120.906 673.888 1.00 67.19 O ANISOU 1652 O MET A1001 13649 6226 5653 1199 3176 944 O ATOM 1653 CB MET A1001 -133.584-123.929 673.862 1.00 73.07 C ANISOU 1653 CB MET A1001 15388 6189 6185 1404 3638 787 C ATOM 1654 N LYS A1002 -135.717-121.259 673.401 1.00 67.82 N ANISOU 1654 N LYS A1002 14189 6162 5418 625 2754 604 N ATOM 1655 CA LYS A1002 -136.144-119.921 673.814 1.00 66.43 C ANISOU 1655 CA LYS A1002 13539 6348 5354 456 2453 661 C ATOM 1656 C LYS A1002 -136.456-119.782 675.316 1.00 66.39 C ANISOU 1656 C LYS A1002 13191 6511 5524 396 2272 746 C ATOM 1657 O LYS A1002 -137.114-120.632 675.913 1.00 66.36 O ANISOU 1657 O LYS A1002 13361 6375 5478 279 2193 674 O ATOM 1658 CB LYS A1002 -137.368-119.502 672.996 1.00 67.08 C ANISOU 1658 CB LYS A1002 13759 6466 5263 103 2170 509 C ATOM 1659 N LYS A1003 -135.986-118.687 675.910 1.00 65.43 N ANISOU 1659 N LYS A1003 12593 6672 5595 459 2196 901 N ATOM 1660 CA LYS A1003 -136.224-118.383 677.320 1.00 58.93 C ANISOU 1660 CA LYS A1003 11425 6017 4949 391 2013 995 C ATOM 1661 C LYS A1003 -137.628-117.841 677.584 1.00 61.13 C ANISOU 1661 C LYS A1003 11627 6416 5184 67 1666 893 C ATOM 1662 O LYS A1003 -138.122-116.991 676.843 1.00 63.16 O ANISOU 1662 O LYS A1003 11837 6786 5376 -71 1530 843 O ATOM 1663 CB LYS A1003 -135.191-117.374 677.818 1.00 53.27 C ANISOU 1663 CB LYS A1003 10255 5540 4446 545 2043 1205 C ATOM 1664 CG LYS A1003 -133.764-117.879 677.758 1.00 56.26 C ANISOU 1664 CG LYS A1003 10597 5851 4929 876 2368 1373 C ATOM 1665 CD LYS A1003 -132.779-116.795 678.142 1.00 57.37 C ANISOU 1665 CD LYS A1003 10272 6254 5272 969 2346 1594 C ATOM 1666 CE LYS A1003 -133.042-116.291 679.544 1.00 57.68 C ANISOU 1666 CE LYS A1003 9977 6469 5469 818 2096 1677 C ATOM 1667 NZ LYS A1003 -132.319-115.019 679.798 1.00 59.74 N ANISOU 1667 NZ LYS A1003 9839 6984 5875 804 1996 1845 N ATOM 1668 N TYR A1004 -138.260-118.324 678.652 1.00 59.33 N ANISOU 1668 N TYR A1004 11361 6171 5009 -40 1531 883 N ATOM 1669 CA TYR A1004 -139.613-117.895 679.003 1.00 53.16 C ANISOU 1669 CA TYR A1004 10480 5504 4215 -321 1221 816 C ATOM 1670 C TYR A1004 -139.669-117.267 680.391 1.00 48.77 C ANISOU 1670 C TYR A1004 9537 5132 3862 -333 1086 927 C ATOM 1671 O TYR A1004 -138.834-117.558 681.246 1.00 43.80 O ANISOU 1671 O TYR A1004 8784 4494 3362 -175 1199 1036 O ATOM 1672 CB TYR A1004 -140.587-119.072 678.922 1.00 52.64 C ANISOU 1672 CB TYR A1004 10759 5241 4000 -502 1141 685 C ATOM 1673 CG TYR A1004 -140.874-119.525 677.506 1.00 53.97 C ANISOU 1673 CG TYR A1004 11326 5236 3943 -598 1186 555 C ATOM 1674 CD1 TYR A1004 -139.977-120.331 676.819 1.00 55.26 C ANISOU 1674 CD1 TYR A1004 11832 5160 4004 -406 1479 516 C ATOM 1675 CD2 TYR A1004 -142.039-119.144 676.857 1.00 55.16 C ANISOU 1675 CD2 TYR A1004 11506 5457 3994 -880 943 488 C ATOM 1676 CE1 TYR A1004 -140.232-120.747 675.522 1.00 58.92 C ANISOU 1676 CE1 TYR A1004 12696 5436 4255 -509 1523 392 C ATOM 1677 CE2 TYR A1004 -142.303-119.554 675.557 1.00 57.70 C ANISOU 1677 CE2 TYR A1004 12196 5617 4112 -1004 963 382 C ATOM 1678 CZ TYR A1004 -141.396-120.355 674.896 1.00 60.58 C ANISOU 1678 CZ TYR A1004 12933 5722 4361 -827 1250 323 C ATOM 1679 OH TYR A1004 -141.653-120.766 673.607 1.00 66.85 O ANISOU 1679 OH TYR A1004 14126 6328 4947 -964 1273 217 O ATOM 1680 N THR A1005 -140.656-116.402 680.610 1.00 39.23 N ANISOU 1680 N THR A1005 8135 4085 2686 -517 850 911 N ATOM 1681 CA THR A1005 -140.785-115.714 681.888 1.00 37.04 C ANISOU 1681 CA THR A1005 7524 3964 2585 -535 728 1000 C ATOM 1682 C THR A1005 -142.218-115.783 682.409 1.00 41.48 C ANISOU 1682 C THR A1005 8048 4563 3148 -741 510 947 C ATOM 1683 O THR A1005 -143.178-115.743 681.640 1.00 43.34 O ANISOU 1683 O THR A1005 8385 4803 3280 -895 397 881 O ATOM 1684 CB THR A1005 -140.332-114.230 681.787 1.00 40.99 C ANISOU 1684 CB THR A1005 7741 4655 3177 -490 703 1082 C ATOM 1685 OG1 THR A1005 -140.486-113.579 683.055 1.00 37.42 O ANISOU 1685 OG1 THR A1005 7018 4321 2877 -522 592 1152 O ATOM 1686 CG2 THR A1005 -141.149-113.486 680.753 1.00 35.73 C ANISOU 1686 CG2 THR A1005 7092 4060 2423 -610 597 1021 C ATOM 1687 N CYS A1006 -142.353-115.911 683.722 1.00 35.01 N ANISOU 1687 N CYS A1006 7072 3776 2453 -746 451 995 N ATOM 1688 CA CYS A1006 -143.662-115.945 684.354 1.00 43.44 C ANISOU 1688 CA CYS A1006 8062 4894 3548 -910 267 973 C ATOM 1689 C CYS A1006 -144.289-114.556 684.330 1.00 44.81 C ANISOU 1689 C CYS A1006 7991 5243 3790 -957 160 1008 C ATOM 1690 O CYS A1006 -143.638-113.567 684.665 1.00 43.99 O ANISOU 1690 O CYS A1006 7701 5231 3784 -860 203 1065 O ATOM 1691 CB CYS A1006 -143.546-116.459 685.785 1.00 33.48 C ANISOU 1691 CB CYS A1006 6704 3613 2402 -884 257 1015 C ATOM 1692 SG CYS A1006 -145.102-116.492 686.667 1.00 32.65 S ANISOU 1692 SG CYS A1006 6477 3580 2348 -1054 60 1009 S ATOM 1693 N THR A1007 -145.550-114.477 683.920 1.00 49.49 N ANISOU 1693 N THR A1007 8590 5879 4336 -1109 25 991 N ATOM 1694 CA THR A1007 -146.227-113.189 683.796 1.00 51.65 C ANISOU 1694 CA THR A1007 8648 6304 4674 -1132 -50 1045 C ATOM 1695 C THR A1007 -146.650-112.640 685.152 1.00 51.88 C ANISOU 1695 C THR A1007 8455 6407 4850 -1100 -83 1102 C ATOM 1696 O THR A1007 -146.820-111.431 685.318 1.00 53.57 O ANISOU 1696 O THR A1007 8499 6714 5140 -1049 -77 1150 O ATOM 1697 CB THR A1007 -147.465-113.292 682.895 1.00 56.12 C ANISOU 1697 CB THR A1007 9266 6905 5151 -1305 -181 1052 C ATOM 1698 OG1 THR A1007 -148.315-114.344 683.374 1.00 58.22 O ANISOU 1698 OG1 THR A1007 9606 7121 5394 -1440 -281 1048 O ATOM 1699 CG2 THR A1007 -147.050-113.580 681.456 1.00 58.20 C ANISOU 1699 CG2 THR A1007 9757 7098 5257 -1344 -145 989 C ATOM 1700 N VAL A1008 -146.815-113.535 686.121 1.00 48.45 N ANISOU 1700 N VAL A1008 8048 5915 4446 -1127 -104 1093 N ATOM 1701 CA VAL A1008 -147.218-113.143 687.463 1.00 47.28 C ANISOU 1701 CA VAL A1008 7723 5820 4421 -1100 -123 1137 C ATOM 1702 C VAL A1008 -146.054-112.630 688.311 1.00 44.78 C ANISOU 1702 C VAL A1008 7324 5499 4190 -978 -32 1145 C ATOM 1703 O VAL A1008 -146.115-111.530 688.870 1.00 40.24 O ANISOU 1703 O VAL A1008 6612 4986 3692 -930 -15 1175 O ATOM 1704 CB VAL A1008 -147.876-114.313 688.205 1.00 50.04 C ANISOU 1704 CB VAL A1008 8124 6118 4771 -1189 -191 1132 C ATOM 1705 CG1 VAL A1008 -148.271-113.891 689.613 1.00 48.19 C ANISOU 1705 CG1 VAL A1008 7719 5936 4656 -1150 -192 1176 C ATOM 1706 CG2 VAL A1008 -149.084-114.812 687.431 1.00 55.35 C ANISOU 1706 CG2 VAL A1008 8862 6808 5359 -1348 -311 1148 C ATOM 1707 N CYS A1009 -144.996-113.429 688.411 1.00 43.50 N ANISOU 1707 N CYS A1009 7256 5258 4013 -931 31 1133 N ATOM 1708 CA CYS A1009 -143.925-113.131 689.352 1.00 38.34 C ANISOU 1708 CA CYS A1009 6503 4615 3450 -848 89 1177 C ATOM 1709 C CYS A1009 -142.626-112.742 688.657 1.00 38.17 C ANISOU 1709 C CYS A1009 6484 4604 3416 -756 182 1219 C ATOM 1710 O CYS A1009 -141.759-112.114 689.259 1.00 41.79 O ANISOU 1710 O CYS A1009 6820 5109 3949 -707 208 1282 O ATOM 1711 CB CYS A1009 -143.697-114.323 690.280 1.00 37.78 C ANISOU 1711 CB CYS A1009 6476 4469 3409 -856 91 1188 C ATOM 1712 SG CYS A1009 -142.675-115.635 689.605 1.00 30.23 S ANISOU 1712 SG CYS A1009 5716 3383 2386 -786 202 1205 S ATOM 1713 N GLY A1010 -142.486-113.106 687.390 1.00 36.63 N ANISOU 1713 N GLY A1010 6433 4366 3118 -740 230 1193 N ATOM 1714 CA GLY A1010 -141.363-112.620 686.605 1.00 36.04 C ANISOU 1714 CA GLY A1010 6349 4319 3026 -645 329 1244 C ATOM 1715 C GLY A1010 -140.176-113.559 686.597 1.00 37.71 C ANISOU 1715 C GLY A1010 6639 4451 3237 -537 462 1313 C ATOM 1716 O GLY A1010 -139.125-113.225 686.042 1.00 35.50 O ANISOU 1716 O GLY A1010 6324 4203 2960 -439 563 1392 O ATOM 1717 N TYR A1011 -140.341-114.723 687.227 1.00 37.47 N ANISOU 1717 N TYR A1011 6703 4320 3213 -546 471 1301 N ATOM 1718 CA TYR A1011 -139.350-115.791 687.153 1.00 36.39 C ANISOU 1718 CA TYR A1011 6678 4070 3077 -416 629 1369 C ATOM 1719 C TYR A1011 -138.988-116.079 685.700 1.00 39.82 C ANISOU 1719 C TYR A1011 7325 4415 3389 -322 778 1326 C ATOM 1720 O TYR A1011 -139.861-116.105 684.835 1.00 38.82 O ANISOU 1720 O TYR A1011 7369 4247 3133 -415 727 1202 O ATOM 1721 CB TYR A1011 -139.874-117.059 687.830 1.00 34.93 C ANISOU 1721 CB TYR A1011 6624 3759 2889 -456 610 1327 C ATOM 1722 CG TYR A1011 -139.072-118.306 687.533 1.00 35.57 C ANISOU 1722 CG TYR A1011 6894 3670 2949 -303 805 1367 C ATOM 1723 CD1 TYR A1011 -137.884-118.571 688.201 1.00 36.13 C ANISOU 1723 CD1 TYR A1011 6812 3758 3157 -159 914 1537 C ATOM 1724 CD2 TYR A1011 -139.510-119.224 686.589 1.00 37.10 C ANISOU 1724 CD2 TYR A1011 7423 3683 2989 -305 882 1247 C ATOM 1725 CE1 TYR A1011 -137.144-119.719 687.927 1.00 48.34 C ANISOU 1725 CE1 TYR A1011 8510 5144 4712 25 1127 1593 C ATOM 1726 CE2 TYR A1011 -138.784-120.373 686.311 1.00 49.48 C ANISOU 1726 CE2 TYR A1011 9202 5063 4536 -137 1099 1276 C ATOM 1727 CZ TYR A1011 -137.601-120.618 686.979 1.00 49.58 C ANISOU 1727 CZ TYR A1011 9034 5094 4710 50 1236 1453 C ATOM 1728 OH TYR A1011 -136.889-121.766 686.701 1.00 42.02 O ANISOU 1728 OH TYR A1011 8268 3945 3754 251 1480 1498 O ATOM 1729 N ILE A1012 -137.701-116.271 685.431 1.00 42.26 N ANISOU 1729 N ILE A1012 7610 4706 3743 -141 961 1443 N ATOM 1730 CA ILE A1012 -137.260-116.600 684.083 1.00 43.64 C ANISOU 1730 CA ILE A1012 7999 4779 3804 -15 1146 1407 C ATOM 1731 C ILE A1012 -136.847-118.060 683.998 1.00 45.24 C ANISOU 1731 C ILE A1012 8443 4769 3977 134 1350 1410 C ATOM 1732 O ILE A1012 -135.982-118.514 684.749 1.00 47.73 O ANISOU 1732 O ILE A1012 8620 5081 4433 272 1450 1560 O ATOM 1733 CB ILE A1012 -136.071-115.735 683.627 1.00 45.64 C ANISOU 1733 CB ILE A1012 8055 5160 4128 118 1248 1546 C ATOM 1734 CG1 ILE A1012 -136.318-114.259 683.943 1.00 42.66 C ANISOU 1734 CG1 ILE A1012 7422 4983 3803 -25 1051 1571 C ATOM 1735 CG2 ILE A1012 -135.801-115.947 682.130 1.00 40.03 C ANISOU 1735 CG2 ILE A1012 7582 4350 3278 231 1430 1481 C ATOM 1736 CD1 ILE A1012 -135.202-113.344 683.467 1.00 41.07 C ANISOU 1736 CD1 ILE A1012 7035 4911 3659 62 1114 1705 C ATOM 1737 N TYR A1013 -137.471-118.797 683.088 1.00 45.16 N ANISOU 1737 N TYR A1013 8799 4577 3784 94 1404 1251 N ATOM 1738 CA TYR A1013 -137.011-120.141 682.793 1.00 48.59 C ANISOU 1738 CA TYR A1013 9535 4768 4160 257 1644 1240 C ATOM 1739 C TYR A1013 -135.932-120.089 681.724 1.00 50.48 C ANISOU 1739 C TYR A1013 9857 4955 4367 493 1916 1297 C ATOM 1740 O TYR A1013 -136.200-119.766 680.568 1.00 50.23 O ANISOU 1740 O TYR A1013 10014 4893 4180 443 1931 1184 O ATOM 1741 CB TYR A1013 -138.154-121.044 682.336 1.00 44.75 C ANISOU 1741 CB TYR A1013 9455 4079 3470 80 1574 1041 C ATOM 1742 CG TYR A1013 -137.673-122.420 681.950 1.00 47.68 C ANISOU 1742 CG TYR A1013 10207 4157 3752 249 1845 1010 C ATOM 1743 CD1 TYR A1013 -137.385-123.373 682.922 1.00 54.60 C ANISOU 1743 CD1 TYR A1013 11079 4928 4739 349 1925 1087 C ATOM 1744 CD2 TYR A1013 -137.489-122.767 680.615 1.00 55.12 C ANISOU 1744 CD2 TYR A1013 11527 4914 4504 315 2032 906 C ATOM 1745 CE1 TYR A1013 -136.932-124.640 682.576 1.00 55.67 C ANISOU 1745 CE1 TYR A1013 11578 4774 4800 528 2200 1064 C ATOM 1746 CE2 TYR A1013 -137.040-124.030 680.258 1.00 59.10 C ANISOU 1746 CE2 TYR A1013 12426 5112 4915 487 2313 871 C ATOM 1747 CZ TYR A1013 -136.761-124.963 681.242 1.00 59.28 C ANISOU 1747 CZ TYR A1013 12441 5030 5054 603 2405 953 C ATOM 1748 OH TYR A1013 -136.314-126.219 680.893 1.00 61.50 O ANISOU 1748 OH TYR A1013 13128 4991 5248 794 2708 922 O ATOM 1749 N ASN A1014 -134.709-120.403 682.126 1.00 54.45 N ANISOU 1749 N ASN A1014 10193 5462 5033 748 2125 1489 N ATOM 1750 CA ASN A1014 -133.594-120.504 681.204 1.00 62.17 C ANISOU 1750 CA ASN A1014 11228 6383 6012 1019 2425 1581 C ATOM 1751 C ASN A1014 -133.416-121.949 680.746 1.00 72.56 C ANISOU 1751 C ASN A1014 12972 7374 7222 1202 2718 1519 C ATOM 1752 O ASN A1014 -132.993-122.796 681.527 1.00 75.70 O ANISOU 1752 O ASN A1014 13328 7691 7743 1343 2834 1630 O ATOM 1753 CB ASN A1014 -132.321-119.982 681.872 1.00 60.37 C ANISOU 1753 CB ASN A1014 10533 6367 6039 1191 2480 1862 C ATOM 1754 CG ASN A1014 -131.108-120.041 680.961 1.00 63.48 C ANISOU 1754 CG ASN A1014 10921 6733 6467 1491 2792 1999 C ATOM 1755 OD1 ASN A1014 -131.220-120.285 679.757 1.00 62.00 O ANISOU 1755 OD1 ASN A1014 11080 6378 6101 1565 2964 1867 O ATOM 1756 ND2 ASN A1014 -129.934-119.810 681.537 1.00 66.31 N ANISOU 1756 ND2 ASN A1014 10878 7261 7055 1653 2856 2272 N ATOM 1757 N PRO A1015 -133.743-122.235 679.474 1.00 80.83 N ANISOU 1757 N PRO A1015 14449 8226 8038 1192 2835 1341 N ATOM 1758 CA PRO A1015 -133.653-123.585 678.902 1.00 85.91 C ANISOU 1758 CA PRO A1015 15601 8510 8532 1339 3120 1245 C ATOM 1759 C PRO A1015 -132.275-124.213 679.066 1.00 89.78 C ANISOU 1759 C PRO A1015 16005 8916 9192 1748 3501 1467 C ATOM 1760 O PRO A1015 -132.176-125.435 679.131 1.00 95.52 O ANISOU 1760 O PRO A1015 17060 9364 9871 1891 3726 1439 O ATOM 1761 CB PRO A1015 -133.962-123.363 677.417 1.00 87.83 C ANISOU 1761 CB PRO A1015 16203 8631 8537 1264 3164 1068 C ATOM 1762 CG PRO A1015 -134.761-122.127 677.380 1.00 85.96 C ANISOU 1762 CG PRO A1015 15712 8667 8283 965 2804 1005 C ATOM 1763 CD PRO A1015 -134.241-121.260 678.490 1.00 82.36 C ANISOU 1763 CD PRO A1015 14681 8522 8093 1018 2688 1218 C ATOM 1764 N GLU A1016 -131.237-123.386 679.136 1.00 88.68 N ANISOU 1764 N GLU A1016 15421 9020 9252 1927 3565 1697 N ATOM 1765 CA GLU A1016 -129.869-123.876 679.247 1.00 89.75 C ANISOU 1765 CA GLU A1016 15394 9129 9580 2321 3914 1956 C ATOM 1766 C GLU A1016 -129.647-124.650 680.542 1.00 88.48 C ANISOU 1766 C GLU A1016 15042 8970 9607 2392 3921 2102 C ATOM 1767 O GLU A1016 -128.948-125.665 680.551 1.00 93.16 O ANISOU 1767 O GLU A1016 15755 9379 10264 2697 4258 2215 O ATOM 1768 CB GLU A1016 -128.874-122.716 679.157 1.00 88.14 C ANISOU 1768 CB GLU A1016 14687 9240 9563 2426 3895 2192 C ATOM 1769 N ASP A1017 -130.247-124.184 681.631 1.00 83.98 N ANISOU 1769 N ASP A1017 14181 8602 9125 2117 3560 2102 N ATOM 1770 CA ASP A1017 -130.043-124.832 682.926 1.00 86.26 C ANISOU 1770 CA ASP A1017 14246 8923 9605 2149 3519 2247 C ATOM 1771 C ASP A1017 -131.336-125.283 683.611 1.00 79.94 C ANISOU 1771 C ASP A1017 13647 8024 8704 1857 3260 2043 C ATOM 1772 O ASP A1017 -131.351-125.503 684.826 1.00 74.80 O ANISOU 1772 O ASP A1017 12736 7470 8217 1791 3111 2147 O ATOM 1773 CB ASP A1017 -129.265-123.905 683.863 1.00 88.13 C ANISOU 1773 CB ASP A1017 13853 9523 10109 2121 3334 2517 C ATOM 1774 CG ASP A1017 -129.682-122.457 683.732 1.00 86.22 C ANISOU 1774 CG ASP A1017 13419 9519 9823 1858 3031 2450 C ATOM 1775 OD1 ASP A1017 -130.858-122.200 683.409 1.00 84.99 O ANISOU 1775 OD1 ASP A1017 13525 9295 9473 1620 2854 2199 O ATOM 1776 OD2 ASP A1017 -128.828-121.575 683.950 1.00 86.30 O ANISOU 1776 OD2 ASP A1017 13013 9786 9991 1882 2964 2657 O ATOM 1777 N GLY A1018 -132.400-125.424 682.824 1.00 79.85 N ANISOU 1777 N GLY A1018 14089 7828 8423 1671 3195 1764 N ATOM 1778 CA GLY A1018 -133.671-125.957 683.283 1.00 79.79 C ANISOU 1778 CA GLY A1018 14326 7700 8289 1392 2966 1566 C ATOM 1779 C GLY A1018 -134.131-125.570 684.670 1.00 80.06 C ANISOU 1779 C GLY A1018 13977 7953 8489 1186 2641 1633 C ATOM 1780 O GLY A1018 -134.226-124.390 685.013 1.00 80.35 O ANISOU 1780 O GLY A1018 13666 8259 8604 1047 2416 1685 O ATOM 1781 N ASP A1019 -134.405-126.577 685.481 1.00 81.79 N ANISOU 1781 N ASP A1019 14277 8045 8755 1170 2627 1628 N ATOM 1782 CA ASP A1019 -134.910-126.350 686.822 1.00 80.87 C ANISOU 1782 CA ASP A1019 13849 8100 8775 970 2331 1676 C ATOM 1783 C ASP A1019 -134.780-127.688 687.533 1.00 86.99 C ANISOU 1783 C ASP A1019 14726 8697 9628 1070 2438 1720 C ATOM 1784 O ASP A1019 -135.692-128.521 687.451 1.00 87.75 O ANISOU 1784 O ASP A1019 15185 8584 9572 932 2385 1538 O ATOM 1785 CB ASP A1019 -136.358-125.874 686.797 1.00 73.36 C ANISOU 1785 CB ASP A1019 13015 7193 7666 622 2014 1466 C ATOM 1786 CG ASP A1019 -136.919-125.621 688.179 1.00 68.50 C ANISOU 1786 CG ASP A1019 12097 6746 7182 431 1734 1511 C ATOM 1787 OD1 ASP A1019 -136.133-125.589 689.141 1.00 69.31 O ANISOU 1787 OD1 ASP A1019 11870 6971 7493 536 1750 1707 O ATOM 1788 OD2 ASP A1019 -138.159-125.475 688.294 1.00 63.85 O ANISOU 1788 OD2 ASP A1019 11602 6174 6484 168 1496 1358 O ATOM 1789 N PRO A1020 -133.643-127.913 688.220 1.00 91.38 N ANISOU 1789 N PRO A1020 14957 9345 10420 1296 2577 1972 N ATOM 1790 CA PRO A1020 -133.278-129.205 688.821 1.00 93.39 C ANISOU 1790 CA PRO A1020 15270 9440 10775 1455 2737 2058 C ATOM 1791 C PRO A1020 -134.109-129.609 690.018 1.00 89.89 C ANISOU 1791 C PRO A1020 14758 9017 10380 1225 2469 2013 C ATOM 1792 O PRO A1020 -134.584-130.740 690.027 1.00 90.78 O ANISOU 1792 O PRO A1020 15199 8887 10407 1219 2534 1897 O ATOM 1793 CB PRO A1020 -131.808-129.022 689.225 1.00 96.82 C ANISOU 1793 CB PRO A1020 15262 10060 11465 1719 2902 2379 C ATOM 1794 CG PRO A1020 -131.493-127.579 689.013 1.00 94.93 C ANISOU 1794 CG PRO A1020 14711 10097 11262 1641 2762 2454 C ATOM 1795 CD PRO A1020 -132.687-126.851 688.546 1.00 91.63 C ANISOU 1795 CD PRO A1020 14500 9677 10638 1364 2536 2201 C ATOM 1796 N ASP A1021 -134.293-128.705 690.974 1.00 85.91 N ANISOU 1796 N ASP A1021 13865 8786 9991 1033 2180 2095 N ATOM 1797 CA ASP A1021 -134.950-129.044 692.229 1.00 82.29 C ANISOU 1797 CA ASP A1021 13291 8373 9601 839 1944 2091 C ATOM 1798 C ASP A1021 -136.452-129.266 692.081 1.00 75.93 C ANISOU 1798 C ASP A1021 12806 7444 8601 574 1753 1829 C ATOM 1799 O ASP A1021 -137.148-129.545 693.062 1.00 74.05 O ANISOU 1799 O ASP A1021 12495 7241 8400 397 1550 1806 O ATOM 1800 CB ASP A1021 -134.699-127.965 693.291 1.00 80.72 C ANISOU 1800 CB ASP A1021 12623 8493 9552 698 1703 2247 C ATOM 1801 CG ASP A1021 -133.649-128.380 694.314 1.00 84.13 C ANISOU 1801 CG ASP A1021 12725 9032 10208 817 1742 2509 C ATOM 1802 OD1 ASP A1021 -133.456-129.596 694.511 1.00 87.11 O ANISOU 1802 OD1 ASP A1021 13222 9238 10637 957 1893 2550 O ATOM 1803 OD2 ASP A1021 -133.031-127.484 694.931 1.00 84.03 O ANISOU 1803 OD2 ASP A1021 12345 9275 10307 750 1608 2669 O ATOM 1804 N ASN A1022 -136.945-129.146 690.855 1.00 71.09 N ANISOU 1804 N ASN A1022 12534 6702 7776 534 1807 1644 N ATOM 1805 CA ASN A1022 -138.340-129.434 690.565 1.00 62.53 C ANISOU 1805 CA ASN A1022 11763 5506 6490 266 1621 1411 C ATOM 1806 C ASN A1022 -138.473-130.425 689.409 1.00 56.85 C ANISOU 1806 C ASN A1022 11576 4470 5556 326 1823 1253 C ATOM 1807 O ASN A1022 -139.526-130.521 688.777 1.00 52.58 O ANISOU 1807 O ASN A1022 11341 3841 4796 91 1683 1060 O ATOM 1808 CB ASN A1022 -139.106-128.136 690.275 1.00 63.32 C ANISOU 1808 CB ASN A1022 11744 5809 6506 45 1388 1326 C ATOM 1809 CG ASN A1022 -139.326-127.302 691.532 1.00 66.61 C ANISOU 1809 CG ASN A1022 11732 6495 7082 -81 1155 1425 C ATOM 1810 OD1 ASN A1022 -138.396-126.677 692.041 1.00 71.15 O ANISOU 1810 OD1 ASN A1022 11984 7233 7817 36 1195 1600 O ATOM 1811 ND2 ASN A1022 -140.552-127.310 692.051 1.00 64.31 N ANISOU 1811 ND2 ASN A1022 11438 6254 6741 -329 910 1324 N ATOM 1812 N GLY A1023 -137.391-131.155 689.142 1.00 53.86 N ANISOU 1812 N GLY A1023 11301 3929 5233 634 2153 1348 N ATOM 1813 CA GLY A1023 -137.420-132.295 688.238 1.00 57.19 C ANISOU 1813 CA GLY A1023 12261 4014 5454 722 2390 1207 C ATOM 1814 C GLY A1023 -137.156-132.038 686.765 1.00 72.05 C ANISOU 1814 C GLY A1023 14484 5764 7127 814 2602 1105 C ATOM 1815 O GLY A1023 -137.280-132.951 685.942 1.00 72.66 O ANISOU 1815 O GLY A1023 15080 5549 6980 845 2790 958 O ATOM 1816 N VAL A1024 -136.790-130.805 686.421 1.00 67.55 N ANISOU 1816 N VAL A1024 13645 5408 6612 848 2574 1180 N ATOM 1817 CA VAL A1024 -136.591-130.443 685.021 1.00 65.10 C ANISOU 1817 CA VAL A1024 13631 4999 6104 913 2746 1085 C ATOM 1818 C VAL A1024 -135.118-130.484 684.637 1.00 70.25 C ANISOU 1818 C VAL A1024 14188 5625 6879 1328 3144 1269 C ATOM 1819 O VAL A1024 -134.319-129.640 685.063 1.00 67.96 O ANISOU 1819 O VAL A1024 13405 5599 6816 1462 3142 1483 O ATOM 1820 CB VAL A1024 -137.157-129.044 684.709 1.00 61.18 C ANISOU 1820 CB VAL A1024 12923 4757 5564 685 2474 1041 C ATOM 1821 CG1 VAL A1024 -136.796-128.622 683.292 1.00 57.56 C ANISOU 1821 CG1 VAL A1024 12713 4223 4932 779 2664 974 C ATOM 1822 CG2 VAL A1024 -138.665-129.030 684.913 1.00 61.20 C ANISOU 1822 CG2 VAL A1024 13038 4788 5427 285 2107 871 C ATOM 1823 N ASN A1025 -134.778-131.481 683.827 1.00 75.74 N ANISOU 1823 N ASN A1025 15364 6005 7408 1519 3485 1191 N ATOM 1824 CA ASN A1025 -133.428-131.665 683.318 1.00 81.01 C ANISOU 1824 CA ASN A1025 16012 6610 8158 1940 3923 1359 C ATOM 1825 C ASN A1025 -132.984-130.529 682.400 1.00 79.17 C ANISOU 1825 C ASN A1025 15669 6511 7900 2013 3981 1396 C ATOM 1826 O ASN A1025 -133.668-130.211 681.422 1.00 73.24 O ANISOU 1826 O ASN A1025 15274 5661 6892 1820 3899 1185 O ATOM 1827 CB ASN A1025 -133.351-132.988 682.568 1.00 88.96 C ANISOU 1827 CB ASN A1025 17653 7231 8918 2089 4282 1222 C ATOM 1828 CG ASN A1025 -134.614-133.268 681.782 1.00 93.07 C ANISOU 1828 CG ASN A1025 18770 7537 9057 1731 4105 900 C ATOM 1829 OD1 ASN A1025 -135.674-132.714 682.090 1.00 90.84 O ANISOU 1829 OD1 ASN A1025 18380 7389 8746 1361 3681 794 O ATOM 1830 ND2 ASN A1025 -134.509-134.098 680.745 1.00 97.12 N ANISOU 1830 ND2 ASN A1025 19905 7745 9250 1820 4428 767 N ATOM 1831 N PRO A1026 -131.821-129.934 682.707 1.00 80.99 N ANISOU 1831 N PRO A1026 15392 6980 8399 2275 4107 1677 N ATOM 1832 CA PRO A1026 -131.252-128.806 681.961 1.00 77.98 C ANISOU 1832 CA PRO A1026 14806 6779 8045 2361 4151 1759 C ATOM 1833 C PRO A1026 -131.200-129.094 680.465 1.00 79.46 C ANISOU 1833 C PRO A1026 15553 6674 7963 2484 4447 1594 C ATOM 1834 O PRO A1026 -131.025-130.247 680.071 1.00 81.67 O ANISOU 1834 O PRO A1026 16293 6626 8111 2672 4778 1525 O ATOM 1835 CB PRO A1026 -129.843-128.676 682.544 1.00 82.37 C ANISOU 1835 CB PRO A1026 14829 7544 8922 2690 4345 2116 C ATOM 1836 CG PRO A1026 -129.946-129.267 683.916 1.00 83.15 C ANISOU 1836 CG PRO A1026 14686 7707 9203 2628 4201 2216 C ATOM 1837 CD PRO A1026 -130.926-130.395 683.785 1.00 82.59 C ANISOU 1837 CD PRO A1026 15184 7296 8899 2502 4220 1951 C ATOM 1838 N GLY A1027 -131.359-128.064 679.643 1.00 79.80 N ANISOU 1838 N GLY A1027 15574 6832 7916 2368 4329 1525 N ATOM 1839 CA GLY A1027 -131.372-128.250 678.205 1.00 71.08 C ANISOU 1839 CA GLY A1027 14996 5448 6564 2436 4551 1361 C ATOM 1840 C GLY A1027 -132.717-128.743 677.707 1.00 71.26 C ANISOU 1840 C GLY A1027 15600 5211 6266 2073 4355 1035 C ATOM 1841 O GLY A1027 -132.828-129.261 676.596 1.00 74.31 O ANISOU 1841 O GLY A1027 16553 5249 6433 2087 4530 888 O ATOM 1842 N THR A1028 -133.746-128.590 678.534 1.00 81.41 N ANISOU 1842 N THR A1028 16741 6650 7543 1727 3966 951 N ATOM 1843 CA THR A1028 -135.088-129.001 678.144 1.00 83.93 C ANISOU 1843 CA THR A1028 17530 6780 7579 1336 3717 678 C ATOM 1844 C THR A1028 -135.847-127.808 677.591 1.00 80.08 C ANISOU 1844 C THR A1028 16885 6527 7014 1016 3370 585 C ATOM 1845 O THR A1028 -135.967-126.777 678.255 1.00 72.02 O ANISOU 1845 O THR A1028 15332 5868 6164 927 3124 686 O ATOM 1846 CB THR A1028 -135.881-129.612 679.324 1.00 66.83 C ANISOU 1846 CB THR A1028 15309 4637 5446 1128 3481 646 C ATOM 1847 N ASP A1029 -136.342-127.942 676.365 1.00 88.56 N ANISOU 1847 N ASP A1029 18417 7387 7846 841 3349 409 N ATOM 1848 CA ASP A1029 -137.183-126.905 675.789 1.00 86.66 C ANISOU 1848 CA ASP A1029 18035 7369 7524 509 3003 320 C ATOM 1849 C ASP A1029 -138.418-126.766 676.669 1.00 84.16 C ANISOU 1849 C ASP A1029 17529 7233 7214 151 2592 267 C ATOM 1850 O ASP A1029 -138.929-127.754 677.190 1.00 84.42 O ANISOU 1850 O ASP A1029 17812 7084 7179 40 2547 204 O ATOM 1851 CB ASP A1029 -137.566-127.232 674.342 1.00 90.98 C ANISOU 1851 CB ASP A1029 19116 7632 7818 336 3025 172 C ATOM 1852 N PHE A1030 -138.871-125.531 676.849 1.00 81.53 N ANISOU 1852 N PHE A1030 16747 7256 6973 -12 2305 308 N ATOM 1853 CA PHE A1030 -140.031-125.231 677.679 1.00 77.75 C ANISOU 1853 CA PHE A1030 16019 6982 6540 -321 1923 295 C ATOM 1854 C PHE A1030 -141.251-126.062 677.268 1.00 83.11 C ANISOU 1854 C PHE A1030 17122 7455 7001 -681 1718 139 C ATOM 1855 O PHE A1030 -142.089-126.422 678.103 1.00 80.72 O ANISOU 1855 O PHE A1030 16751 7198 6721 -882 1493 134 O ATOM 1856 CB PHE A1030 -140.347-123.737 677.600 1.00 71.46 C ANISOU 1856 CB PHE A1030 14765 6542 5844 -431 1690 353 C ATOM 1857 CG PHE A1030 -141.379-123.279 678.586 1.00 68.16 C ANISOU 1857 CG PHE A1030 14007 6358 5532 -666 1352 388 C ATOM 1858 CD1 PHE A1030 -141.022-122.986 679.891 1.00 65.57 C ANISOU 1858 CD1 PHE A1030 13293 6194 5427 -537 1339 521 C ATOM 1859 CD2 PHE A1030 -142.702-123.129 678.206 1.00 68.57 C ANISOU 1859 CD2 PHE A1030 14108 6467 5479 -1016 1049 312 C ATOM 1860 CE1 PHE A1030 -141.967-122.557 680.802 1.00 65.85 C ANISOU 1860 CE1 PHE A1030 13031 6425 5565 -735 1051 554 C ATOM 1861 CE2 PHE A1030 -143.654-122.703 679.112 1.00 67.42 C ANISOU 1861 CE2 PHE A1030 13630 6538 5450 -1198 768 369 C ATOM 1862 CZ PHE A1030 -143.285-122.414 680.413 1.00 66.05 C ANISOU 1862 CZ PHE A1030 13103 6506 5486 -1049 780 479 C ATOM 1863 N LYS A1031 -141.335-126.371 675.977 1.00 88.87 N ANISOU 1863 N LYS A1031 18280 7956 7531 -776 1789 35 N ATOM 1864 CA LYS A1031 -142.401-127.216 675.461 1.00 91.08 C ANISOU 1864 CA LYS A1031 19002 8000 7605 -1143 1605 -75 C ATOM 1865 C LYS A1031 -142.216-128.647 675.947 1.00 95.64 C ANISOU 1865 C LYS A1031 19998 8227 8112 -1071 1781 -114 C ATOM 1866 O LYS A1031 -143.186-129.382 676.106 1.00 95.84 O ANISOU 1866 O LYS A1031 20260 8122 8032 -1388 1569 -160 O ATOM 1867 CB LYS A1031 -142.434-127.171 673.930 1.00 88.00 C ANISOU 1867 CB LYS A1031 18969 7438 7031 -1263 1655 -134 C ATOM 1868 N ASP A1032 -140.963-129.027 676.191 1.00103.32 N ANISOU 1868 N ASP A1032 21038 9058 9160 -649 2175 -68 N ATOM 1869 CA ASP A1032 -140.624-130.392 676.595 1.00104.30 C ANISOU 1869 CA ASP A1032 21579 8822 9229 -507 2417 -90 C ATOM 1870 C ASP A1032 -140.699-130.587 678.114 1.00 99.16 C ANISOU 1870 C ASP A1032 20575 8373 8727 -436 2337 -43 C ATOM 1871 O ASP A1032 -140.317-131.637 678.633 1.00101.04 O ANISOU 1871 O ASP A1032 21028 8425 8937 -262 2552 -54 O ATOM 1872 CB ASP A1032 -139.226-130.762 676.086 1.00108.00 C ANISOU 1872 CB ASP A1032 22239 9072 9723 -55 2909 -13 C ATOM 1873 N ILE A1033 -141.190-129.572 678.817 1.00 86.25 N ANISOU 1873 N ILE A1033 18369 7142 7259 -569 2030 43 N ATOM 1874 CA ILE A1033 -141.426-129.665 680.252 1.00 75.51 C ANISOU 1874 CA ILE A1033 16628 5973 6089 -574 1882 142 C ATOM 1875 C ILE A1033 -142.799-130.262 680.534 1.00 75.54 C ANISOU 1875 C ILE A1033 16799 5943 5960 -978 1544 43 C ATOM 1876 O ILE A1033 -143.789-129.827 679.941 1.00 77.44 O ANISOU 1876 O ILE A1033 17067 6262 6094 -1313 1260 -17 O ATOM 1877 CB ILE A1033 -141.336-128.288 680.925 1.00 62.85 C ANISOU 1877 CB ILE A1033 14358 4778 4743 -535 1714 293 C ATOM 1878 CG1 ILE A1033 -139.883-127.842 681.049 1.00 61.27 C ANISOU 1878 CG1 ILE A1033 13900 4644 4735 -125 2030 448 C ATOM 1879 CG2 ILE A1033 -141.978-128.310 682.290 1.00 58.08 C ANISOU 1879 CG2 ILE A1033 13405 4352 4309 -668 1461 367 C ATOM 1880 CD1 ILE A1033 -139.750-126.476 681.678 1.00 60.00 C ANISOU 1880 CD1 ILE A1033 13135 4861 4802 -112 1862 589 C ATOM 1881 N PRO A1034 -142.861-131.265 681.432 1.00 71.93 N ANISOU 1881 N PRO A1034 16411 5388 5530 -948 1568 53 N ATOM 1882 CA PRO A1034 -144.128-131.865 681.871 1.00 75.14 C ANISOU 1882 CA PRO A1034 16904 5813 5832 -1313 1239 -8 C ATOM 1883 C PRO A1034 -145.170-130.798 682.210 1.00 78.23 C ANISOU 1883 C PRO A1034 16830 6547 6347 -1592 845 59 C ATOM 1884 O PRO A1034 -144.842-129.826 682.882 1.00 78.98 O ANISOU 1884 O PRO A1034 16410 6905 6693 -1441 826 188 O ATOM 1885 CB PRO A1034 -143.719-132.662 683.110 1.00 70.22 C ANISOU 1885 CB PRO A1034 16127 5163 5390 -1120 1343 79 C ATOM 1886 CG PRO A1034 -142.304-133.055 682.834 1.00 69.19 C ANISOU 1886 CG PRO A1034 16160 4830 5299 -696 1798 114 C ATOM 1887 CD PRO A1034 -141.698-131.898 682.081 1.00 68.27 C ANISOU 1887 CD PRO A1034 15899 4813 5228 -554 1910 152 C ATOM 1888 N ASP A1035 -146.399-130.970 681.737 1.00 82.68 N ANISOU 1888 N ASP A1035 17568 7109 6738 -1993 544 -14 N ATOM 1889 CA ASP A1035 -147.399-129.909 681.815 1.00 87.54 C ANISOU 1889 CA ASP A1035 17746 8046 7468 -2238 211 71 C ATOM 1890 C ASP A1035 -147.826-129.598 683.249 1.00 88.63 C ANISOU 1890 C ASP A1035 17365 8464 7847 -2222 43 201 C ATOM 1891 O ASP A1035 -148.232-128.476 683.562 1.00 89.71 O ANISOU 1891 O ASP A1035 17035 8900 8150 -2250 -109 302 O ATOM 1892 CB ASP A1035 -148.621-130.279 680.976 1.00 95.19 C ANISOU 1892 CB ASP A1035 18996 8922 8249 -2685 -65 19 C ATOM 1893 CG ASP A1035 -149.255-129.073 680.313 1.00 98.67 C ANISOU 1893 CG ASP A1035 19117 9613 8760 -2853 -258 106 C ATOM 1894 OD1 ASP A1035 -148.953-127.932 680.732 1.00 97.22 O ANISOU 1894 OD1 ASP A1035 18454 9719 8764 -2650 -236 189 O ATOM 1895 OD2 ASP A1035 -150.051-129.268 679.369 1.00101.69 O ANISOU 1895 OD2 ASP A1035 19694 9928 9014 -3171 -420 122 O ATOM 1896 N ASP A1036 -147.718-130.593 684.121 1.00 88.43 N ANISOU 1896 N ASP A1036 17425 8329 7845 -2164 89 201 N ATOM 1897 CA ASP A1036 -148.086-130.435 685.524 1.00 85.51 C ANISOU 1897 CA ASP A1036 16599 8177 7714 -2149 -52 321 C ATOM 1898 C ASP A1036 -147.097-129.561 686.298 1.00 77.89 C ANISOU 1898 C ASP A1036 15210 7364 7022 -1823 116 429 C ATOM 1899 O ASP A1036 -147.298-129.277 687.479 1.00 77.22 O ANISOU 1899 O ASP A1036 14737 7461 7142 -1795 19 528 O ATOM 1900 CB ASP A1036 -148.201-131.807 686.186 1.00 92.34 C ANISOU 1900 CB ASP A1036 17682 8870 8532 -2177 -43 292 C ATOM 1901 CG ASP A1036 -147.043-132.721 685.832 1.00 99.09 C ANISOU 1901 CG ASP A1036 18947 9406 9296 -1916 306 216 C ATOM 1902 OD1 ASP A1036 -146.640-132.748 684.649 1.00102.31 O ANISOU 1902 OD1 ASP A1036 19734 9640 9499 -1884 466 120 O ATOM 1903 OD2 ASP A1036 -146.529-133.410 686.736 1.00101.40 O ANISOU 1903 OD2 ASP A1036 19173 9622 9732 -1732 433 262 O ATOM 1904 N TRP A1037 -146.030-129.145 685.624 1.00 71.51 N ANISOU 1904 N TRP A1037 14487 6480 6202 -1589 365 416 N ATOM 1905 CA TRP A1037 -145.013-128.275 686.204 1.00 64.02 C ANISOU 1905 CA TRP A1037 13157 5682 5485 -1301 518 532 C ATOM 1906 C TRP A1037 -145.547-126.851 686.348 1.00 59.33 C ANISOU 1906 C TRP A1037 12142 5408 4993 -1393 323 595 C ATOM 1907 O TRP A1037 -146.326-126.386 685.510 1.00 60.46 O ANISOU 1907 O TRP A1037 12336 5623 5013 -1591 174 547 O ATOM 1908 CB TRP A1037 -143.759-128.318 685.327 1.00 60.89 C ANISOU 1908 CB TRP A1037 12990 5114 5030 -1030 846 515 C ATOM 1909 CG TRP A1037 -142.613-127.409 685.685 1.00 57.50 C ANISOU 1909 CG TRP A1037 12195 4842 4811 -744 1011 652 C ATOM 1910 CD1 TRP A1037 -141.481-127.747 686.369 1.00 54.43 C ANISOU 1910 CD1 TRP A1037 11672 4406 4601 -460 1231 774 C ATOM 1911 CD2 TRP A1037 -142.460-126.032 685.315 1.00 46.42 C ANISOU 1911 CD2 TRP A1037 10514 3669 3455 -726 964 694 C ATOM 1912 NE1 TRP A1037 -140.644-126.660 686.467 1.00 49.95 N ANISOU 1912 NE1 TRP A1037 10756 4038 4183 -290 1304 900 N ATOM 1913 CE2 TRP A1037 -141.222-125.596 685.828 1.00 46.76 C ANISOU 1913 CE2 TRP A1037 10275 3797 3696 -446 1147 841 C ATOM 1914 CE3 TRP A1037 -143.251-125.125 684.608 1.00 45.63 C ANISOU 1914 CE3 TRP A1037 10356 3721 3262 -922 777 637 C ATOM 1915 CZ2 TRP A1037 -140.762-124.298 685.658 1.00 47.22 C ANISOU 1915 CZ2 TRP A1037 10030 4074 3838 -375 1142 916 C ATOM 1916 CZ3 TRP A1037 -142.794-123.835 684.444 1.00 48.65 C ANISOU 1916 CZ3 TRP A1037 10432 4312 3740 -824 791 705 C ATOM 1917 CH2 TRP A1037 -141.561-123.432 684.964 1.00 46.59 C ANISOU 1917 CH2 TRP A1037 9928 4120 3655 -561 969 835 C ATOM 1918 N VAL A1038 -145.139-126.177 687.424 1.00 54.74 N ANISOU 1918 N VAL A1038 11150 5012 4639 -1255 327 709 N ATOM 1919 CA VAL A1038 -145.554-124.798 687.703 1.00 49.34 C ANISOU 1919 CA VAL A1038 10072 4612 4064 -1303 182 769 C ATOM 1920 C VAL A1038 -144.354-123.890 687.983 1.00 44.78 C ANISOU 1920 C VAL A1038 9243 4137 3633 -1061 339 858 C ATOM 1921 O VAL A1038 -143.237-124.372 688.175 1.00 40.32 O ANISOU 1921 O VAL A1038 8735 3457 3127 -855 542 909 O ATOM 1922 CB VAL A1038 -146.513-124.723 688.913 1.00 48.11 C ANISOU 1922 CB VAL A1038 9638 4612 4030 -1436 -24 823 C ATOM 1923 CG1 VAL A1038 -147.810-125.472 688.626 1.00 49.42 C ANISOU 1923 CG1 VAL A1038 9982 4731 4063 -1705 -218 772 C ATOM 1924 CG2 VAL A1038 -145.828-125.256 690.172 1.00 46.01 C ANISOU 1924 CG2 VAL A1038 9255 4306 3919 -1294 61 890 C ATOM 1925 N CYS A1039 -144.591-122.580 688.008 1.00 37.85 N ANISOU 1925 N CYS A1039 8080 3480 2823 -1086 246 894 N ATOM 1926 CA CYS A1039 -143.551-121.601 688.341 1.00 36.57 C ANISOU 1926 CA CYS A1039 7660 3441 2796 -906 349 985 C ATOM 1927 C CYS A1039 -142.978-121.860 689.735 1.00 38.79 C ANISOU 1927 C CYS A1039 7746 3748 3246 -817 375 1085 C ATOM 1928 O CYS A1039 -143.714-121.856 690.723 1.00 34.86 O ANISOU 1928 O CYS A1039 7097 3330 2819 -924 232 1093 O ATOM 1929 CB CYS A1039 -144.114-120.179 688.261 1.00 34.95 C ANISOU 1929 CB CYS A1039 7200 3450 2629 -979 221 995 C ATOM 1930 SG CYS A1039 -143.003-118.880 688.830 1.00 33.40 S ANISOU 1930 SG CYS A1039 6686 3415 2590 -822 294 1104 S ATOM 1931 N PRO A1040 -141.659-122.094 689.823 1.00 39.41 N ANISOU 1931 N PRO A1040 7810 3767 3396 -618 563 1180 N ATOM 1932 CA PRO A1040 -141.045-122.427 691.116 1.00 39.46 C ANISOU 1932 CA PRO A1040 7626 3802 3566 -546 581 1304 C ATOM 1933 C PRO A1040 -141.247-121.357 692.190 1.00 34.10 C ANISOU 1933 C PRO A1040 6616 3337 3002 -630 427 1359 C ATOM 1934 O PRO A1040 -141.155-121.663 693.377 1.00 34.02 O ANISOU 1934 O PRO A1040 6468 3360 3097 -649 377 1428 O ATOM 1935 CB PRO A1040 -139.555-122.583 690.775 1.00 38.76 C ANISOU 1935 CB PRO A1040 7522 3662 3541 -309 812 1436 C ATOM 1936 CG PRO A1040 -139.389-122.042 689.418 1.00 38.01 C ANISOU 1936 CG PRO A1040 7558 3555 3329 -257 903 1375 C ATOM 1937 CD PRO A1040 -140.696-122.170 688.718 1.00 38.01 C ANISOU 1937 CD PRO A1040 7794 3492 3155 -445 777 1195 C ATOM 1938 N LEU A1041 -141.548-120.128 691.789 1.00 34.09 N ANISOU 1938 N LEU A1041 6507 3470 2975 -681 360 1323 N ATOM 1939 CA LEU A1041 -141.721-119.066 692.766 1.00 34.79 C ANISOU 1939 CA LEU A1041 6332 3729 3159 -740 250 1357 C ATOM 1940 C LEU A1041 -143.190-118.880 693.172 1.00 33.32 C ANISOU 1940 C LEU A1041 6120 3589 2950 -882 104 1261 C ATOM 1941 O LEU A1041 -143.485-118.768 694.359 1.00 29.73 O ANISOU 1941 O LEU A1041 5530 3193 2574 -923 38 1278 O ATOM 1942 CB LEU A1041 -141.143-117.750 692.231 1.00 30.89 C ANISOU 1942 CB LEU A1041 5718 3347 2670 -693 278 1391 C ATOM 1943 CG LEU A1041 -139.713-117.798 691.681 1.00 31.96 C ANISOU 1943 CG LEU A1041 5848 3467 2827 -549 427 1515 C ATOM 1944 CD1 LEU A1041 -139.223-116.401 691.308 1.00 40.03 C ANISOU 1944 CD1 LEU A1041 6720 4625 3863 -535 419 1558 C ATOM 1945 CD2 LEU A1041 -138.747-118.467 692.644 1.00 32.62 C ANISOU 1945 CD2 LEU A1041 5826 3542 3027 -483 477 1676 C ATOM 1946 N CYS A1042 -144.109-118.848 692.206 1.00 33.29 N ANISOU 1946 N CYS A1042 6240 3567 2842 -955 58 1178 N ATOM 1947 CA CYS A1042 -145.513-118.563 692.526 1.00 33.37 C ANISOU 1947 CA CYS A1042 6179 3651 2849 -1078 -72 1140 C ATOM 1948 C CYS A1042 -146.464-119.724 692.226 1.00 40.11 C ANISOU 1948 C CYS A1042 7205 4416 3618 -1201 -151 1097 C ATOM 1949 O CYS A1042 -147.597-119.742 692.705 1.00 43.78 O ANISOU 1949 O CYS A1042 7588 4946 4101 -1303 -260 1105 O ATOM 1950 CB CYS A1042 -145.991-117.309 691.782 1.00 33.43 C ANISOU 1950 CB CYS A1042 6108 3762 2830 -1090 -96 1127 C ATOM 1951 SG CYS A1042 -146.224-117.483 689.976 1.00 47.38 S ANISOU 1951 SG CYS A1042 8082 5477 4443 -1141 -95 1075 S ATOM 1952 N GLY A1043 -146.017-120.687 691.430 1.00 42.51 N ANISOU 1952 N GLY A1043 7762 4567 3824 -1192 -88 1060 N ATOM 1953 CA GLY A1043 -146.818-121.868 691.169 1.00 43.07 C ANISOU 1953 CA GLY A1043 8045 4523 3796 -1330 -167 1013 C ATOM 1954 C GLY A1043 -147.924-121.730 690.133 1.00 44.28 C ANISOU 1954 C GLY A1043 8290 4709 3826 -1499 -289 974 C ATOM 1955 O GLY A1043 -148.877-122.506 690.159 1.00 45.21 O ANISOU 1955 O GLY A1043 8499 4793 3884 -1665 -415 964 O ATOM 1956 N VAL A1044 -147.821-120.763 689.221 1.00 44.05 N ANISOU 1956 N VAL A1044 8226 4752 3759 -1475 -266 967 N ATOM 1957 CA VAL A1044 -148.763-120.726 688.098 1.00 44.87 C ANISOU 1957 CA VAL A1044 8437 4874 3736 -1647 -381 944 C ATOM 1958 C VAL A1044 -148.383-121.772 687.065 1.00 45.62 C ANISOU 1958 C VAL A1044 8930 4757 3649 -1702 -326 852 C ATOM 1959 O VAL A1044 -147.244-122.237 687.031 1.00 47.57 O ANISOU 1959 O VAL A1044 9342 4856 3876 -1544 -149 816 O ATOM 1960 CB VAL A1044 -148.816-119.365 687.391 1.00 46.51 C ANISOU 1960 CB VAL A1044 8486 5224 3962 -1609 -376 971 C ATOM 1961 CG1 VAL A1044 -149.266-118.282 688.343 1.00 47.88 C ANISOU 1961 CG1 VAL A1044 8321 5576 4295 -1549 -406 1056 C ATOM 1962 CG2 VAL A1044 -147.474-119.041 686.760 1.00 47.76 C ANISOU 1962 CG2 VAL A1044 8746 5314 4086 -1443 -204 929 C ATOM 1963 N GLY A1045 -149.339-122.132 686.215 1.00 44.96 N ANISOU 1963 N GLY A1045 9004 4650 3429 -1925 -468 826 N ATOM 1964 CA GLY A1045 -149.088-123.099 685.167 1.00 47.16 C ANISOU 1964 CA GLY A1045 9717 4701 3502 -2011 -422 722 C ATOM 1965 C GLY A1045 -148.298-122.487 684.029 1.00 48.75 C ANISOU 1965 C GLY A1045 10031 4869 3624 -1902 -282 674 C ATOM 1966 O GLY A1045 -148.106-121.270 683.983 1.00 47.48 O ANISOU 1966 O GLY A1045 9590 4884 3564 -1800 -264 728 O ATOM 1967 N LYS A1046 -147.844-123.332 683.105 1.00 50.96 N ANISOU 1967 N LYS A1046 10738 4908 3715 -1921 -171 569 N ATOM 1968 CA LYS A1046 -147.100-122.869 681.942 1.00 53.36 C ANISOU 1968 CA LYS A1046 11191 5158 3926 -1817 -21 517 C ATOM 1969 C LYS A1046 -147.975-121.947 681.111 1.00 56.50 C ANISOU 1969 C LYS A1046 11439 5731 4298 -2004 -203 550 C ATOM 1970 O LYS A1046 -147.474-121.124 680.347 1.00 55.21 O ANISOU 1970 O LYS A1046 11227 5627 4124 -1907 -118 546 O ATOM 1971 CB LYS A1046 -146.605-124.049 681.103 1.00 54.21 C ANISOU 1971 CB LYS A1046 11837 4940 3820 -1819 141 395 C ATOM 1972 CG LYS A1046 -145.788-125.065 681.895 1.00 58.57 C ANISOU 1972 CG LYS A1046 12558 5297 4400 -1620 344 382 C ATOM 1973 CD LYS A1046 -144.625-125.627 681.080 1.00 65.89 C ANISOU 1973 CD LYS A1046 13878 5956 5202 -1398 669 309 C ATOM 1974 CE LYS A1046 -145.100-126.399 679.852 1.00 70.06 C ANISOU 1974 CE LYS A1046 14934 6222 5464 -1616 652 173 C ATOM 1975 N ASP A1047 -149.288-122.082 681.292 1.00 62.43 N ANISOU 1975 N ASP A1047 12091 6577 5055 -2266 -449 605 N ATOM 1976 CA ASP A1047 -150.275-121.223 680.643 1.00 63.00 C ANISOU 1976 CA ASP A1047 11958 6842 5137 -2450 -635 687 C ATOM 1977 C ASP A1047 -150.036-119.725 680.887 1.00 59.89 C ANISOU 1977 C ASP A1047 11154 6687 4913 -2259 -591 773 C ATOM 1978 O ASP A1047 -150.424-118.889 680.068 1.00 59.99 O ANISOU 1978 O ASP A1047 11056 6822 4913 -2328 -658 821 O ATOM 1979 CB ASP A1047 -151.681-121.601 681.115 1.00 64.40 C ANISOU 1979 CB ASP A1047 12004 7116 5348 -2714 -883 784 C ATOM 1980 N GLN A1048 -149.399-119.387 682.006 1.00 54.81 N ANISOU 1980 N GLN A1048 10302 6098 4426 -2032 -479 798 N ATOM 1981 CA GLN A1048 -149.181-117.988 682.349 1.00 49.61 C ANISOU 1981 CA GLN A1048 9289 5635 3924 -1869 -439 876 C ATOM 1982 C GLN A1048 -147.748-117.522 682.051 1.00 47.04 C ANISOU 1982 C GLN A1048 9007 5263 3603 -1636 -230 830 C ATOM 1983 O GLN A1048 -147.312-116.483 682.543 1.00 44.97 O ANISOU 1983 O GLN A1048 8484 5127 3477 -1485 -174 886 O ATOM 1984 CB GLN A1048 -149.522-117.757 683.821 1.00 45.89 C ANISOU 1984 CB GLN A1048 8535 5270 3632 -1803 -471 955 C ATOM 1985 N PHE A1049 -147.026-118.292 681.240 1.00 47.01 N ANISOU 1985 N PHE A1049 9344 5070 3448 -1610 -107 736 N ATOM 1986 CA PHE A1049 -145.663-117.940 680.833 1.00 47.21 C ANISOU 1986 CA PHE A1049 9418 5051 3470 -1383 110 715 C ATOM 1987 C PHE A1049 -145.632-117.362 679.408 1.00 51.67 C ANISOU 1987 C PHE A1049 10074 5638 3920 -1426 119 684 C ATOM 1988 O PHE A1049 -146.422-117.757 678.550 1.00 54.79 O ANISOU 1988 O PHE A1049 10667 5976 4176 -1637 5 640 O ATOM 1989 CB PHE A1049 -144.741-119.166 680.913 1.00 48.95 C ANISOU 1989 CB PHE A1049 9952 5032 3613 -1257 307 653 C ATOM 1990 CG PHE A1049 -144.139-119.409 682.284 1.00 46.48 C ANISOU 1990 CG PHE A1049 9477 4725 3459 -1101 384 721 C ATOM 1991 CD1 PHE A1049 -144.896-119.962 683.308 1.00 44.93 C ANISOU 1991 CD1 PHE A1049 9220 4532 3322 -1213 251 736 C ATOM 1992 CD2 PHE A1049 -142.805-119.116 682.533 1.00 42.41 C ANISOU 1992 CD2 PHE A1049 8860 4215 3038 -852 586 788 C ATOM 1993 CE1 PHE A1049 -144.337-120.194 684.560 1.00 42.81 C ANISOU 1993 CE1 PHE A1049 8800 4266 3200 -1082 315 802 C ATOM 1994 CE2 PHE A1049 -142.242-119.345 683.782 1.00 41.19 C ANISOU 1994 CE2 PHE A1049 8540 4073 3039 -732 640 874 C ATOM 1995 CZ PHE A1049 -143.010-119.884 684.798 1.00 40.71 C ANISOU 1995 CZ PHE A1049 8431 4007 3030 -850 503 873 C ATOM 1996 N GLU A1050 -144.718-116.425 679.167 1.00 49.97 N ANISOU 1996 N GLU A1050 9708 5509 3767 -1244 243 721 N ATOM 1997 CA GLU A1050 -144.537-115.823 677.851 1.00 49.28 C ANISOU 1997 CA GLU A1050 9689 5451 3584 -1255 273 700 C ATOM 1998 C GLU A1050 -143.069-115.885 677.466 1.00 49.42 C ANISOU 1998 C GLU A1050 9815 5381 3579 -1014 530 689 C ATOM 1999 O GLU A1050 -142.231-116.246 678.288 1.00 51.09 O ANISOU 1999 O GLU A1050 9989 5543 3878 -839 670 727 O ATOM 2000 CB GLU A1050 -145.019-114.370 677.842 1.00 49.85 C ANISOU 2000 CB GLU A1050 9412 5758 3770 -1280 151 790 C ATOM 2001 CG GLU A1050 -146.434-114.181 677.331 1.00 52.41 C ANISOU 2001 CG GLU A1050 9703 6163 4048 -1524 -64 815 C ATOM 2002 N GLU A1051 -142.756-115.530 676.223 1.00 47.82 N ANISOU 2002 N GLU A1051 9729 5168 3271 -1002 597 658 N ATOM 2003 CA GLU A1051 -141.365-115.378 675.804 1.00 48.10 C ANISOU 2003 CA GLU A1051 9802 5165 3310 -756 846 683 C ATOM 2004 C GLU A1051 -140.770-114.099 676.405 1.00 45.32 C ANISOU 2004 C GLU A1051 9043 5034 3144 -627 843 811 C ATOM 2005 O GLU A1051 -141.481-113.113 676.617 1.00 44.86 O ANISOU 2005 O GLU A1051 8738 5147 3161 -736 663 851 O ATOM 2006 CB GLU A1051 -141.254-115.339 674.275 1.00 51.39 C ANISOU 2006 CB GLU A1051 10463 5509 3555 -792 912 614 C ATOM 2007 CG GLU A1051 -141.685-116.602 673.565 1.00 54.83 C ANISOU 2007 CG GLU A1051 11363 5684 3785 -926 940 485 C ATOM 2008 CD GLU A1051 -141.439-116.534 672.061 1.00 62.20 C ANISOU 2008 CD GLU A1051 12554 6529 4551 -949 1030 423 C ATOM 2009 OE1 GLU A1051 -141.256-115.415 671.527 1.00 55.33 O ANISOU 2009 OE1 GLU A1051 11462 5842 3717 -923 1000 480 O ATOM 2010 OE2 GLU A1051 -141.422-117.606 671.413 1.00 69.31 O ANISOU 2010 OE2 GLU A1051 13896 7161 5278 -996 1137 319 O ATOM 2011 N VAL A1052 -139.469-114.113 676.674 1.00 44.75 N ANISOU 2011 N VAL A1052 8904 4950 3151 -397 1047 891 N ATOM 2012 CA VAL A1052 -138.794-112.930 677.200 1.00 45.24 C ANISOU 2012 CA VAL A1052 8606 5207 3378 -303 1037 1026 C ATOM 2013 C VAL A1052 -138.742-111.821 676.141 1.00 46.99 C ANISOU 2013 C VAL A1052 8743 5552 3558 -329 1006 1038 C ATOM 2014 O VAL A1052 -138.726-112.102 674.941 1.00 41.47 O ANISOU 2014 O VAL A1052 8274 4771 2711 -335 1082 967 O ATOM 2015 CB VAL A1052 -137.368-113.269 677.697 1.00 43.85 C ANISOU 2015 CB VAL A1052 8353 5001 3306 -68 1252 1150 C ATOM 2016 CG1 VAL A1052 -137.431-114.264 678.852 1.00 40.21 C ANISOU 2016 CG1 VAL A1052 7927 4440 2911 -45 1266 1163 C ATOM 2017 CG2 VAL A1052 -136.519-113.820 676.574 1.00 42.84 C ANISOU 2017 CG2 VAL A1052 8457 4746 3076 104 1502 1140 C ATOM 2018 N GLU A1053 -138.724-110.568 676.593 1.00 44.96 N ANISOU 2018 N GLU A1053 8177 5480 3427 -349 896 1127 N ATOM 2019 CA GLU A1053 -138.844-109.407 675.704 1.00 45.69 C ANISOU 2019 CA GLU A1053 8164 5700 3496 -392 837 1147 C ATOM 2020 C GLU A1053 -137.798-109.399 674.603 1.00 45.01 C ANISOU 2020 C GLU A1053 8174 5596 3333 -264 1017 1171 C ATOM 2021 O GLU A1053 -138.106-109.098 673.449 1.00 44.24 O ANISOU 2021 O GLU A1053 8176 5511 3122 -324 1001 1122 O ATOM 2022 CB GLU A1053 -138.745-108.103 676.502 1.00 43.79 C ANISOU 2022 CB GLU A1053 7601 5625 3414 -396 735 1252 C ATOM 2023 N GLU A1054 -136.566-109.745 674.964 1.00 46.69 N ANISOU 2023 N GLU A1054 8344 5779 3616 -85 1193 1264 N ATOM 2024 CA GLU A1054 -135.448-109.702 674.028 1.00 49.66 C ANISOU 2024 CA GLU A1054 8764 6148 3957 76 1393 1323 C ATOM 2025 C GLU A1054 -135.628-110.706 672.895 1.00 56.02 C ANISOU 2025 C GLU A1054 9952 6762 4572 106 1537 1192 C ATOM 2026 O GLU A1054 -135.090-110.519 671.802 1.00 58.20 O ANISOU 2026 O GLU A1054 10315 7030 4770 185 1664 1197 O ATOM 2027 CB GLU A1054 -134.129-109.959 674.762 1.00 53.05 C ANISOU 2027 CB GLU A1054 9034 6589 4535 273 1552 1485 C ATOM 2028 CG GLU A1054 -134.037-111.334 675.386 1.00 63.85 C ANISOU 2028 CG GLU A1054 10566 7782 5911 375 1679 1465 C ATOM 2029 CD GLU A1054 -133.481-111.309 676.799 1.00 70.29 C ANISOU 2029 CD GLU A1054 11113 8675 6920 417 1640 1616 C ATOM 2030 OE1 GLU A1054 -134.211-110.867 677.713 1.00 69.03 O ANISOU 2030 OE1 GLU A1054 10827 8587 6813 247 1426 1593 O ATOM 2031 OE2 GLU A1054 -132.326-111.744 676.998 1.00 74.63 O ANISOU 2031 OE2 GLU A1054 11572 9211 7572 618 1825 1768 O ATOM 2032 N GLU A 227 -136.395-111.762 673.157 1.00 70.60 N ANISOU 2032 N GLU A 227 11778 10159 4889 27 1193 1151 N ATOM 2033 CA GLU A 227 -136.611-112.819 672.180 1.00 53.96 C ANISOU 2033 CA GLU A 227 9647 7860 2995 -25 1238 1285 C ATOM 2034 C GLU A 227 -137.733-112.457 671.218 1.00 52.29 C ANISOU 2034 C GLU A 227 9312 7606 2948 -69 1376 1173 C ATOM 2035 O GLU A 227 -137.625-112.695 670.015 1.00 50.08 O ANISOU 2035 O GLU A 227 8996 7145 2889 -78 1358 1161 O ATOM 2036 CB GLU A 227 -136.918-114.145 672.879 1.00 56.42 C ANISOU 2036 CB GLU A 227 10013 8200 3223 -98 1304 1532 C ATOM 2037 N LYS A 228 -138.809-111.880 671.739 1.00 53.46 N ANISOU 2037 N LYS A 228 9391 7932 2990 -95 1513 1091 N ATOM 2038 CA LYS A 228 -139.910-111.476 670.876 1.00 52.09 C ANISOU 2038 CA LYS A 228 9082 7740 2971 -131 1640 988 C ATOM 2039 C LYS A 228 -139.537-110.243 670.046 1.00 54.92 C ANISOU 2039 C LYS A 228 9385 8032 3449 -56 1561 770 C ATOM 2040 O LYS A 228 -139.946-110.122 668.895 1.00 53.43 O ANISOU 2040 O LYS A 228 9104 7733 3463 -78 1596 717 O ATOM 2041 CB LYS A 228 -141.174-111.208 671.690 1.00 54.29 C ANISOU 2041 CB LYS A 228 9286 8239 3103 -169 1811 969 C ATOM 2042 CG LYS A 228 -141.160-111.852 673.048 1.00 63.65 C ANISOU 2042 CG LYS A 228 10556 9582 4044 -198 1840 1124 C ATOM 2043 CD LYS A 228 -142.527-111.868 673.699 1.00 68.22 C ANISOU 2043 CD LYS A 228 11045 10369 4506 -257 2033 1153 C ATOM 2044 CE LYS A 228 -143.614-112.311 672.741 1.00 68.99 C ANISOU 2044 CE LYS A 228 11013 10386 4814 -337 2158 1202 C ATOM 2045 NZ LYS A 228 -144.848-112.640 673.514 1.00 73.33 N ANISOU 2045 NZ LYS A 228 11484 11144 5233 -408 2338 1302 N ATOM 2046 N LYS A 229 -138.755-109.334 670.624 1.00 52.10 N ANISOU 2046 N LYS A 229 9083 7744 2969 25 1449 649 N ATOM 2047 CA LYS A 229 -138.286-108.165 669.885 1.00 47.74 C ANISOU 2047 CA LYS A 229 8487 7120 2531 95 1355 456 C ATOM 2048 C LYS A 229 -137.418-108.615 668.717 1.00 49.93 C ANISOU 2048 C LYS A 229 8779 7185 3008 104 1241 513 C ATOM 2049 O LYS A 229 -137.511-108.079 667.611 1.00 48.75 O ANISOU 2049 O LYS A 229 8545 6939 3037 115 1233 414 O ATOM 2050 CB LYS A 229 -137.507-107.210 670.792 1.00 48.81 C ANISOU 2050 CB LYS A 229 8695 7357 2495 169 1235 330 C ATOM 2051 N ARG A 230 -136.583-109.617 668.970 1.00 48.46 N ANISOU 2051 N ARG A 230 8694 6932 2787 101 1157 679 N ATOM 2052 CA ARG A 230 -135.765-110.203 667.923 1.00 44.05 C ANISOU 2052 CA ARG A 230 8151 6177 2408 114 1061 749 C ATOM 2053 C ARG A 230 -136.624-110.847 666.835 1.00 42.81 C ANISOU 2053 C ARG A 230 7918 5906 2441 38 1181 791 C ATOM 2054 O ARG A 230 -136.348-110.683 665.659 1.00 40.64 O ANISOU 2054 O ARG A 230 7596 5503 2342 51 1140 736 O ATOM 2055 CB ARG A 230 -134.797-111.225 668.507 1.00 45.37 C ANISOU 2055 CB ARG A 230 8434 6304 2501 131 960 930 C ATOM 2056 CG ARG A 230 -134.220-112.170 667.477 1.00 56.13 C ANISOU 2056 CG ARG A 230 9811 7462 4055 132 909 1036 C ATOM 2057 CD ARG A 230 -132.828-112.588 667.864 1.00 44.64 C ANISOU 2057 CD ARG A 230 8439 5964 2558 204 739 1140 C ATOM 2058 NE ARG A 230 -132.781-112.930 669.272 1.00 59.23 N ANISOU 2058 NE ARG A 230 10363 7952 4191 193 732 1249 N ATOM 2059 CZ ARG A 230 -131.670-112.937 669.995 1.00 58.92 C ANISOU 2059 CZ ARG A 230 10386 7958 4043 255 578 1310 C ATOM 2060 NH1 ARG A 230 -130.510-112.624 669.426 1.00 57.15 N ANISOU 2060 NH1 ARG A 230 10147 7647 3918 334 418 1274 N ATOM 2061 NH2 ARG A 230 -131.722-113.255 671.282 1.00 56.81 N ANISOU 2061 NH2 ARG A 230 10184 7835 3565 234 581 1414 N ATOM 2062 N HIS A 231 -137.671-111.569 667.222 1.00 51.85 N ANISOU 2062 N HIS A 231 9047 7106 3549 -48 1326 888 N ATOM 2063 CA HIS A 231 -138.566-112.169 666.233 1.00 46.81 C ANISOU 2063 CA HIS A 231 8329 6369 3088 -136 1436 923 C ATOM 2064 C HIS A 231 -139.226-111.093 665.377 1.00 48.94 C ANISOU 2064 C HIS A 231 8462 6661 3474 -133 1485 747 C ATOM 2065 O HIS A 231 -139.382-111.256 664.167 1.00 49.80 O ANISOU 2065 O HIS A 231 8509 6645 3767 -168 1492 725 O ATOM 2066 CB HIS A 231 -139.636-113.025 666.909 1.00 45.68 C ANISOU 2066 CB HIS A 231 8177 6307 2872 -233 1580 1060 C ATOM 2067 N ARG A 232 -139.608-109.991 666.011 1.00 49.69 N ANISOU 2067 N ARG A 232 8509 6914 3457 -89 1516 620 N ATOM 2068 CA ARG A 232 -140.253-108.890 665.310 1.00 47.11 C ANISOU 2068 CA ARG A 232 8047 6616 3235 -73 1561 453 C ATOM 2069 C ARG A 232 -139.291-108.230 664.330 1.00 46.23 C ANISOU 2069 C ARG A 232 7929 6383 3253 -10 1424 355 C ATOM 2070 O ARG A 232 -139.637-107.992 663.174 1.00 42.76 O ANISOU 2070 O ARG A 232 7389 5872 2988 -34 1445 302 O ATOM 2071 CB ARG A 232 -140.776-107.865 666.313 1.00 47.53 C ANISOU 2071 CB ARG A 232 8067 6860 3132 -25 1617 333 C ATOM 2072 CG ARG A 232 -142.222-107.468 666.097 1.00 48.15 C ANISOU 2072 CG ARG A 232 7991 7035 3267 -61 1775 273 C ATOM 2073 CD ARG A 232 -142.888-107.190 667.428 1.00 45.46 C ANISOU 2073 CD ARG A 232 7651 6903 2717 -44 1877 253 C ATOM 2074 NE ARG A 232 -141.929-106.659 668.392 1.00 53.39 N ANISOU 2074 NE ARG A 232 8777 7966 3541 33 1770 182 N ATOM 2075 CZ ARG A 232 -142.021-106.814 669.712 1.00 55.53 C ANISOU 2075 CZ ARG A 232 9119 8400 3582 36 1811 218 C ATOM 2076 NH1 ARG A 232 -143.038-107.486 670.243 1.00 56.06 N ANISOU 2076 NH1 ARG A 232 9144 8591 3568 -30 1964 331 N ATOM 2077 NH2 ARG A 232 -141.093-106.293 670.503 1.00 54.32 N ANISOU 2077 NH2 ARG A 232 9074 8292 3274 99 1695 143 N ATOM 2078 N ASP A 233 -138.077-107.952 664.798 1.00 47.56 N ANISOU 2078 N ASP A 233 8200 6539 3332 66 1280 340 N ATOM 2079 CA ASP A 233 -137.059-107.297 663.980 1.00 43.18 C ANISOU 2079 CA ASP A 233 7642 5885 2882 132 1136 259 C ATOM 2080 C ASP A 233 -136.602-108.170 662.801 1.00 41.18 C ANISOU 2080 C ASP A 233 7390 5464 2791 105 1100 353 C ATOM 2081 O ASP A 233 -136.152-107.664 661.769 1.00 35.32 O ANISOU 2081 O ASP A 233 6596 4646 2180 136 1032 285 O ATOM 2082 CB ASP A 233 -135.860-106.911 664.851 1.00 45.55 C ANISOU 2082 CB ASP A 233 8048 6219 3038 212 980 243 C ATOM 2083 N VAL A 234 -136.719-109.482 662.946 1.00 42.63 N ANISOU 2083 N VAL A 234 7636 5593 2970 49 1148 507 N ATOM 2084 CA VAL A 234 -136.390-110.365 661.837 1.00 39.18 C ANISOU 2084 CA VAL A 234 7206 4992 2690 20 1129 581 C ATOM 2085 C VAL A 234 -137.573-110.438 660.867 1.00 38.37 C ANISOU 2085 C VAL A 234 6983 4866 2730 -73 1255 542 C ATOM 2086 O VAL A 234 -137.379-110.514 659.655 1.00 40.12 O ANISOU 2086 O VAL A 234 7159 4984 3100 -84 1231 515 O ATOM 2087 CB VAL A 234 -135.995-111.788 662.322 1.00 39.49 C ANISOU 2087 CB VAL A 234 7363 4953 2688 0 1119 759 C ATOM 2088 CG1 VAL A 234 -135.856-112.739 661.145 1.00 38.33 C ANISOU 2088 CG1 VAL A 234 7220 4631 2714 -38 1124 816 C ATOM 2089 CG2 VAL A 234 -134.690-111.745 663.115 1.00 37.04 C ANISOU 2089 CG2 VAL A 234 7154 4658 2263 97 969 808 C ATOM 2090 N ARG A 235 -138.797-110.389 661.384 1.00 36.74 N ANISOU 2090 N ARG A 235 6715 4767 2476 -139 1385 538 N ATOM 2091 CA ARG A 235 -139.970-110.449 660.512 1.00 41.14 C ANISOU 2091 CA ARG A 235 7141 5319 3170 -231 1495 509 C ATOM 2092 C ARG A 235 -140.026-109.235 659.586 1.00 44.78 C ANISOU 2092 C ARG A 235 7479 5796 3741 -193 1466 359 C ATOM 2093 O ARG A 235 -140.437-109.331 658.426 1.00 46.14 O ANISOU 2093 O ARG A 235 7558 5908 4065 -251 1490 337 O ATOM 2094 CB ARG A 235 -141.260-110.542 661.331 1.00 46.99 C ANISOU 2094 CB ARG A 235 7823 6198 3831 -295 1636 541 C ATOM 2095 CG ARG A 235 -142.521-110.624 660.478 1.00 50.57 C ANISOU 2095 CG ARG A 235 8127 6661 4429 -393 1741 524 C ATOM 2096 CD ARG A 235 -143.790-110.547 661.320 1.00 60.34 C ANISOU 2096 CD ARG A 235 9283 8061 5582 -437 1879 551 C ATOM 2097 NE ARG A 235 -144.987-110.577 660.479 1.00 69.07 N ANISOU 2097 NE ARG A 235 10228 9183 6833 -527 1965 540 N ATOM 2098 CZ ARG A 235 -146.232-110.449 660.931 1.00 75.96 C ANISOU 2098 CZ ARG A 235 10987 10198 7675 -568 2089 561 C ATOM 2099 NH1 ARG A 235 -146.459-110.279 662.229 1.00 80.42 N ANISOU 2099 NH1 ARG A 235 11586 10910 8061 -526 2154 587 N ATOM 2100 NH2 ARG A 235 -147.254-110.490 660.081 1.00 74.97 N ANISOU 2100 NH2 ARG A 235 10709 10080 7695 -649 2147 558 N ATOM 2101 N LEU A 236 -139.597-108.092 660.107 1.00 44.47 N ANISOU 2101 N LEU A 236 7440 5837 3621 -99 1406 257 N ATOM 2102 CA LEU A 236 -139.631-106.849 659.354 1.00 42.08 C ANISOU 2102 CA LEU A 236 7024 5550 3415 -55 1373 117 C ATOM 2103 C LEU A 236 -138.666-106.885 658.175 1.00 36.94 C ANISOU 2103 C LEU A 236 6377 4773 2884 -33 1266 114 C ATOM 2104 O LEU A 236 -139.049-106.660 657.032 1.00 35.78 O ANISOU 2104 O LEU A 236 6117 4596 2881 -71 1288 74 O ATOM 2105 CB LEU A 236 -139.296-105.670 660.270 1.00 41.27 C ANISOU 2105 CB LEU A 236 6946 5543 3194 42 1320 4 C ATOM 2106 CG LEU A 236 -139.266-104.309 659.582 1.00 37.86 C ANISOU 2106 CG LEU A 236 6408 5113 2865 97 1275 -145 C ATOM 2107 CD1 LEU A 236 -140.639-103.996 659.010 1.00 35.17 C ANISOU 2107 CD1 LEU A 236 5901 4824 2637 46 1406 -187 C ATOM 2108 CD2 LEU A 236 -138.822-103.235 660.559 1.00 41.46 C ANISOU 2108 CD2 LEU A 236 6915 5637 3200 189 1205 -262 C ATOM 2109 N ILE A 237 -137.411-107.182 658.473 1.00 36.50 N ANISOU 2109 N ILE A 237 6447 4658 2763 31 1148 163 N ATOM 2110 CA ILE A 237 -136.355-107.140 657.477 1.00 40.95 C ANISOU 2110 CA ILE A 237 7018 5123 3417 76 1035 163 C ATOM 2111 C ILE A 237 -136.574-108.219 656.405 1.00 42.70 C ANISOU 2111 C ILE A 237 7224 5239 3762 -1 1086 236 C ATOM 2112 O ILE A 237 -136.243-108.028 655.230 1.00 43.16 O ANISOU 2112 O ILE A 237 7221 5246 3933 5 1049 204 O ATOM 2113 CB ILE A 237 -134.968-107.279 658.165 1.00 59.62 C ANISOU 2113 CB ILE A 237 9515 7462 5677 168 890 216 C ATOM 2114 CG1 ILE A 237 -134.399-105.893 658.495 1.00 58.76 C ANISOU 2114 CG1 ILE A 237 9388 7418 5521 252 777 98 C ATOM 2115 CG2 ILE A 237 -133.979-108.015 657.289 1.00 61.56 C ANISOU 2115 CG2 ILE A 237 9799 7586 6004 198 810 296 C ATOM 2116 CD1 ILE A 237 -135.244-105.060 659.443 1.00 59.87 C ANISOU 2116 CD1 ILE A 237 9500 7676 5571 247 844 -2 C ATOM 2117 N PHE A 238 -137.172-109.335 656.803 1.00 44.27 N ANISOU 2117 N PHE A 238 7474 5409 3936 -77 1173 330 N ATOM 2118 CA PHE A 238 -137.442-110.419 655.865 1.00 44.93 C ANISOU 2118 CA PHE A 238 7558 5381 4133 -160 1220 388 C ATOM 2119 C PHE A 238 -138.523-110.023 654.879 1.00 40.80 C ANISOU 2119 C PHE A 238 6876 4894 3734 -247 1298 312 C ATOM 2120 O PHE A 238 -138.373-110.209 653.674 1.00 42.31 O ANISOU 2120 O PHE A 238 7023 5016 4038 -276 1281 290 O ATOM 2121 CB PHE A 238 -137.839-111.694 656.614 1.00 50.49 C ANISOU 2121 CB PHE A 238 8360 6040 4783 -225 1286 510 C ATOM 2122 CG PHE A 238 -138.169-112.850 655.711 1.00 59.64 C ANISOU 2122 CG PHE A 238 9533 7067 6060 -320 1332 559 C ATOM 2123 CD1 PHE A 238 -137.201-113.398 654.880 1.00 62.46 C ANISOU 2123 CD1 PHE A 238 9957 7287 6489 -276 1260 577 C ATOM 2124 CD2 PHE A 238 -139.448-113.388 655.691 1.00 64.06 C ANISOU 2124 CD2 PHE A 238 10037 7643 6659 -450 1443 585 C ATOM 2125 CE1 PHE A 238 -137.501-114.463 654.048 1.00 63.97 C ANISOU 2125 CE1 PHE A 238 10173 7347 6784 -362 1301 604 C ATOM 2126 CE2 PHE A 238 -139.757-114.451 654.862 1.00 66.15 C ANISOU 2126 CE2 PHE A 238 10321 7780 7033 -547 1474 618 C ATOM 2127 CZ PHE A 238 -138.783-114.989 654.037 1.00 66.18 C ANISOU 2127 CZ PHE A 238 10405 7636 7103 -503 1404 620 C ATOM 2128 N THR A 239 -139.605-109.466 655.406 1.00 37.70 N ANISOU 2128 N THR A 239 6392 4619 3314 -284 1380 273 N ATOM 2129 CA THR A 239 -140.735-109.052 654.596 1.00 36.44 C ANISOU 2129 CA THR A 239 6062 4512 3269 -362 1451 212 C ATOM 2130 C THR A 239 -140.316-108.003 653.578 1.00 38.25 C ANISOU 2130 C THR A 239 6191 4752 3593 -311 1382 115 C ATOM 2131 O THR A 239 -140.664-108.104 652.409 1.00 41.17 O ANISOU 2131 O THR A 239 6462 5097 4085 -376 1390 95 O ATOM 2132 CB THR A 239 -141.861-108.518 655.484 1.00 36.57 C ANISOU 2132 CB THR A 239 6000 4669 3228 -375 1546 191 C ATOM 2133 OG1 THR A 239 -142.256-109.550 656.394 1.00 44.12 O ANISOU 2133 OG1 THR A 239 7043 5627 4095 -430 1613 298 O ATOM 2134 CG2 THR A 239 -143.062-108.101 654.659 1.00 32.54 C ANISOU 2134 CG2 THR A 239 5301 4220 2844 -446 1611 143 C ATOM 2135 N ILE A 240 -139.546-107.013 654.018 1.00 36.60 N ANISOU 2135 N ILE A 240 6007 4578 3322 -200 1308 56 N ATOM 2136 CA ILE A 240 -139.054-105.971 653.122 1.00 36.12 C ANISOU 2136 CA ILE A 240 5857 4522 3346 -145 1236 -28 C ATOM 2137 C ILE A 240 -138.266-106.567 651.954 1.00 31.30 C ANISOU 2137 C ILE A 240 5263 3817 2814 -157 1174 8 C ATOM 2138 O ILE A 240 -138.528-106.260 650.786 1.00 28.30 O ANISOU 2138 O ILE A 240 4735 3445 2572 -193 1155 -30 O ATOM 2139 CB ILE A 240 -138.162-104.965 653.877 1.00 23.02 C ANISOU 2139 CB ILE A 240 4260 2890 1596 -22 1141 -89 C ATOM 2140 CG1 ILE A 240 -139.008-104.094 654.805 1.00 29.17 C ANISOU 2140 CG1 ILE A 240 4991 3772 2322 0 1203 -167 C ATOM 2141 CG2 ILE A 240 -137.417-104.093 652.914 1.00 21.51 C ANISOU 2141 CG2 ILE A 240 3957 2677 1540 34 1007 -146 C ATOM 2142 CD1 ILE A 240 -138.195-103.152 655.683 1.00 24.49 C ANISOU 2142 CD1 ILE A 240 4477 3202 1627 110 1104 -244 C ATOM 2143 N MET A 241 -137.312-107.432 652.288 1.00 29.03 N ANISOU 2143 N MET A 241 5125 3446 2461 -117 1118 85 N ATOM 2144 CA MET A 241 -136.430-108.054 651.307 1.00 27.27 C ANISOU 2144 CA MET A 241 4903 3130 2330 -97 1032 117 C ATOM 2145 C MET A 241 -137.194-108.905 650.298 1.00 34.60 C ANISOU 2145 C MET A 241 5790 4009 3347 -216 1115 127 C ATOM 2146 O MET A 241 -136.954-108.811 649.093 1.00 33.58 O ANISOU 2146 O MET A 241 5559 3868 3332 -220 1063 90 O ATOM 2147 CB MET A 241 -135.374-108.914 652.004 1.00 26.10 C ANISOU 2147 CB MET A 241 4930 2896 2090 -27 975 209 C ATOM 2148 CG MET A 241 -134.497-109.705 651.055 1.00 27.66 C ANISOU 2148 CG MET A 241 5143 2989 2380 6 909 245 C ATOM 2149 SD MET A 241 -133.251-108.695 650.227 1.00 53.18 S ANISOU 2149 SD MET A 241 8235 6260 5713 122 744 193 S ATOM 2150 CE MET A 241 -131.801-109.057 651.224 1.00 31.38 C ANISOU 2150 CE MET A 241 5613 3451 2857 254 627 284 C ATOM 2151 N ILE A 242 -138.115-109.736 650.769 1.00 22.52 N ANISOU 2151 N ILE A 242 4326 2457 1774 -317 1232 177 N ATOM 2152 CA ILE A 242 -138.802-110.602 649.828 1.00 31.03 C ANISOU 2152 CA ILE A 242 5369 3476 2944 -440 1288 181 C ATOM 2153 C ILE A 242 -139.912-109.855 649.092 1.00 30.80 C ANISOU 2153 C ILE A 242 5140 3555 3010 -521 1324 108 C ATOM 2154 O ILE A 242 -140.184-110.155 647.934 1.00 34.30 O ANISOU 2154 O ILE A 242 5514 3976 3540 -598 1325 81 O ATOM 2155 CB ILE A 242 -139.372-111.878 650.506 1.00 42.40 C ANISOU 2155 CB ILE A 242 6917 4839 4353 -524 1356 263 C ATOM 2156 CG1 ILE A 242 -140.674-111.600 651.237 1.00 45.11 C ANISOU 2156 CG1 ILE A 242 7169 5293 4678 -595 1437 266 C ATOM 2157 CG2 ILE A 242 -138.338-112.519 651.409 1.00 44.27 C ANISOU 2157 CG2 ILE A 242 7337 4986 4495 -433 1313 350 C ATOM 2158 CD1 ILE A 242 -141.866-112.136 650.492 1.00 48.97 C ANISOU 2158 CD1 ILE A 242 7559 5781 5265 -743 1497 257 C ATOM 2159 N VAL A 243 -140.546-108.877 649.727 1.00 26.73 N ANISOU 2159 N VAL A 243 4526 3154 2475 -498 1349 76 N ATOM 2160 CA VAL A 243 -141.510-108.078 648.982 1.00 29.04 C ANISOU 2160 CA VAL A 243 4619 3546 2870 -550 1368 16 C ATOM 2161 C VAL A 243 -140.765-107.338 647.869 1.00 32.80 C ANISOU 2161 C VAL A 243 5016 4032 3415 -502 1291 -37 C ATOM 2162 O VAL A 243 -141.282-107.191 646.753 1.00 36.40 O ANISOU 2162 O VAL A 243 5331 4526 3972 -572 1282 -64 O ATOM 2163 CB VAL A 243 -142.275-107.092 649.879 1.00 25.15 C ANISOU 2163 CB VAL A 243 4042 3167 2348 -511 1416 -14 C ATOM 2164 CG1 VAL A 243 -143.020-106.080 649.042 1.00 23.88 C ANISOU 2164 CG1 VAL A 243 3672 3096 2304 -528 1414 -73 C ATOM 2165 CG2 VAL A 243 -143.250-107.842 650.745 1.00 27.10 C ANISOU 2165 CG2 VAL A 243 4319 3435 2544 -581 1507 45 C ATOM 2166 N TYR A 244 -139.536-106.913 648.156 1.00 30.05 N ANISOU 2166 N TYR A 244 4729 3655 3035 -375 1188 -43 N ATOM 2167 CA TYR A 244 -138.699-106.325 647.119 1.00 24.34 C ANISOU 2167 CA TYR A 244 3905 2936 2405 -312 1062 -74 C ATOM 2168 C TYR A 244 -138.529-107.287 645.949 1.00 20.50 C ANISOU 2168 C TYR A 244 3423 2394 1972 -375 1050 -61 C ATOM 2169 O TYR A 244 -138.684-106.892 644.801 1.00 21.38 O ANISOU 2169 O TYR A 244 3394 2558 2172 -403 1012 -92 O ATOM 2170 CB TYR A 244 -137.327-105.921 647.664 1.00 27.36 C ANISOU 2170 CB TYR A 244 4361 3287 2747 -176 946 -66 C ATOM 2171 CG TYR A 244 -136.404-105.422 646.571 1.00 25.00 C ANISOU 2171 CG TYR A 244 3955 2996 2546 -119 824 -77 C ATOM 2172 CD1 TYR A 244 -135.556-106.296 645.901 1.00 25.62 C ANISOU 2172 CD1 TYR A 244 4088 3012 2636 -98 783 -43 C ATOM 2173 CD2 TYR A 244 -136.399-104.082 646.187 1.00 21.90 C ANISOU 2173 CD2 TYR A 244 3405 2675 2240 -85 755 -116 C ATOM 2174 CE1 TYR A 244 -134.725-105.855 644.873 1.00 25.54 C ANISOU 2174 CE1 TYR A 244 3969 3030 2706 -46 686 -47 C ATOM 2175 CE2 TYR A 244 -135.566-103.630 645.157 1.00 20.53 C ANISOU 2175 CE2 TYR A 244 3125 2520 2156 -43 648 -107 C ATOM 2176 CZ TYR A 244 -134.733-104.525 644.511 1.00 25.24 C ANISOU 2176 CZ TYR A 244 3771 3074 2746 -24 619 -71 C ATOM 2177 OH TYR A 244 -133.896-104.107 643.500 1.00 31.83 O ANISOU 2177 OH TYR A 244 4494 3943 3655 20 527 -54 O ATOM 2178 N PHE A 245 -138.207-108.547 646.231 1.00 25.56 N ANISOU 2178 N PHE A 245 4229 2927 2557 -393 1082 -16 N ATOM 2179 CA PHE A 245 -138.054-109.546 645.164 1.00 24.34 C ANISOU 2179 CA PHE A 245 4102 2698 2447 -448 1077 -21 C ATOM 2180 C PHE A 245 -139.367-109.847 644.456 1.00 27.00 C ANISOU 2180 C PHE A 245 4354 3071 2835 -609 1153 -49 C ATOM 2181 O PHE A 245 -139.370-110.268 643.308 1.00 31.69 O ANISOU 2181 O PHE A 245 4911 3650 3478 -661 1129 -86 O ATOM 2182 CB PHE A 245 -137.478-110.853 645.705 1.00 28.56 C ANISOU 2182 CB PHE A 245 4842 3086 2924 -428 1098 36 C ATOM 2183 CG PHE A 245 -136.040-110.762 646.105 1.00 34.16 C ANISOU 2183 CG PHE A 245 5625 3753 3601 -269 1003 69 C ATOM 2184 CD1 PHE A 245 -135.154-109.990 645.379 1.00 34.40 C ANISOU 2184 CD1 PHE A 245 5544 3842 3685 -174 901 37 C ATOM 2185 CD2 PHE A 245 -135.578-111.437 647.225 1.00 37.58 C ANISOU 2185 CD2 PHE A 245 6230 4099 3951 -219 1014 146 C ATOM 2186 CE1 PHE A 245 -133.830-109.903 645.754 1.00 37.15 C ANISOU 2186 CE1 PHE A 245 5941 4161 4011 -35 810 76 C ATOM 2187 CE2 PHE A 245 -134.256-111.353 647.607 1.00 37.77 C ANISOU 2187 CE2 PHE A 245 6308 4094 3947 -74 917 186 C ATOM 2188 CZ PHE A 245 -133.378-110.585 646.868 1.00 38.58 C ANISOU 2188 CZ PHE A 245 6289 4257 4112 17 814 148 C ATOM 2189 N LEU A 246 -140.488-109.647 645.133 1.00 26.90 N ANISOU 2189 N LEU A 246 4306 3112 2802 -689 1245 -33 N ATOM 2190 CA LEU A 246 -141.774-109.854 644.479 1.00 28.96 C ANISOU 2190 CA LEU A 246 4451 3426 3128 -837 1291 -53 C ATOM 2191 C LEU A 246 -142.012-108.796 643.412 1.00 27.73 C ANISOU 2191 C LEU A 246 4089 3392 3054 -836 1233 -102 C ATOM 2192 O LEU A 246 -142.532-109.088 642.329 1.00 29.06 O ANISOU 2192 O LEU A 246 4173 3588 3279 -930 1209 -130 O ATOM 2193 CB LEU A 246 -142.913-109.833 645.494 1.00 32.04 C ANISOU 2193 CB LEU A 246 4803 3863 3506 -877 1353 -20 C ATOM 2194 CG LEU A 246 -142.957-111.031 646.441 1.00 39.24 C ANISOU 2194 CG LEU A 246 5892 4668 4351 -915 1412 46 C ATOM 2195 CD1 LEU A 246 -144.243-111.024 647.281 1.00 42.12 C ANISOU 2195 CD1 LEU A 246 6184 5110 4709 -972 1481 84 C ATOM 2196 CD2 LEU A 246 -142.800-112.339 645.661 1.00 40.28 C ANISOU 2196 CD2 LEU A 246 6129 4666 4510 -1012 1411 47 C ATOM 2197 N PHE A 247 -141.614-107.566 643.715 1.00 22.57 N ANISOU 2197 N PHE A 247 3358 2809 2408 -725 1195 -113 N ATOM 2198 CA PHE A 247 -141.923-106.454 642.834 1.00 23.73 C ANISOU 2198 CA PHE A 247 3301 3071 2646 -718 1138 -141 C ATOM 2199 C PHE A 247 -140.882-106.225 641.754 1.00 22.86 C ANISOU 2199 C PHE A 247 3151 2964 2572 -654 1021 -155 C ATOM 2200 O PHE A 247 -141.196-105.629 640.728 1.00 24.67 O ANISOU 2200 O PHE A 247 3219 3284 2870 -685 975 -164 O ATOM 2201 CB PHE A 247 -142.106-105.173 643.651 1.00 24.19 C ANISOU 2201 CB PHE A 247 3281 3193 2720 -628 1142 -149 C ATOM 2202 CG PHE A 247 -143.470-105.039 644.262 1.00 28.72 C ANISOU 2202 CG PHE A 247 3783 3821 3308 -674 1215 -141 C ATOM 2203 CD1 PHE A 247 -143.803-105.738 645.412 1.00 27.29 C ANISOU 2203 CD1 PHE A 247 3727 3598 3042 -689 1293 -115 C ATOM 2204 CD2 PHE A 247 -144.423-104.218 643.682 1.00 29.87 C ANISOU 2204 CD2 PHE A 247 3730 4064 3555 -688 1189 -143 C ATOM 2205 CE1 PHE A 247 -145.059-105.612 645.976 1.00 29.02 C ANISOU 2205 CE1 PHE A 247 3867 3884 3274 -721 1357 -99 C ATOM 2206 CE2 PHE A 247 -145.688-104.093 644.243 1.00 33.08 C ANISOU 2206 CE2 PHE A 247 4065 4527 3978 -710 1250 -126 C ATOM 2207 CZ PHE A 247 -146.003-104.790 645.391 1.00 31.44 C ANISOU 2207 CZ PHE A 247 3976 4288 3682 -729 1341 -106 C ATOM 2208 N TRP A 248 -139.655-106.695 641.970 1.00 24.04 N ANISOU 2208 N TRP A 248 3437 3024 2672 -564 975 -146 N ATOM 2209 CA TRP A 248 -138.541-106.343 641.073 1.00 23.66 C ANISOU 2209 CA TRP A 248 3340 2996 2655 -479 869 -149 C ATOM 2210 C TRP A 248 -137.853-107.525 640.364 1.00 23.02 C ANISOU 2210 C TRP A 248 3365 2840 2542 -483 860 -163 C ATOM 2211 O TRP A 248 -137.221-107.342 639.321 1.00 23.63 O ANISOU 2211 O TRP A 248 3371 2964 2642 -446 797 -173 O ATOM 2212 CB TRP A 248 -137.481-105.557 641.843 1.00 15.00 C ANISOU 2212 CB TRP A 248 2266 1884 1551 -338 797 -127 C ATOM 2213 CG TRP A 248 -137.742-104.094 641.925 1.00 20.10 C ANISOU 2213 CG TRP A 248 2757 2612 2266 -303 751 -131 C ATOM 2214 CD1 TRP A 248 -138.055-103.376 643.042 1.00 18.78 C ANISOU 2214 CD1 TRP A 248 2601 2445 2090 -264 770 -143 C ATOM 2215 CD2 TRP A 248 -137.695-103.153 640.843 1.00 17.83 C ANISOU 2215 CD2 TRP A 248 2287 2414 2072 -300 677 -122 C ATOM 2216 NE1 TRP A 248 -138.208-102.042 642.723 1.00 17.62 N ANISOU 2216 NE1 TRP A 248 2292 2363 2039 -233 710 -151 N ATOM 2217 CE2 TRP A 248 -138.002-101.883 641.378 1.00 14.93 C ANISOU 2217 CE2 TRP A 248 1827 2078 1766 -257 651 -127 C ATOM 2218 CE3 TRP A 248 -137.439-103.265 639.471 1.00 18.57 C ANISOU 2218 CE3 TRP A 248 2290 2568 2198 -328 632 -108 C ATOM 2219 CZ2 TRP A 248 -138.051-100.731 640.591 1.00 13.23 C ANISOU 2219 CZ2 TRP A 248 1431 1935 1660 -244 576 -105 C ATOM 2220 CZ3 TRP A 248 -137.495-102.117 638.689 1.00 20.58 C ANISOU 2220 CZ3 TRP A 248 2360 2917 2542 -319 561 -80 C ATOM 2221 CH2 TRP A 248 -137.798-100.867 639.253 1.00 21.04 C ANISOU 2221 CH2 TRP A 248 2328 2988 2678 -279 530 -71 C ATOM 2222 N ALA A 249 -137.943-108.727 640.921 1.00 20.95 N ANISOU 2222 N ALA A 249 3275 2458 2226 -519 926 -159 N ATOM 2223 CA ALA A 249 -137.372-109.881 640.233 1.00 17.21 C ANISOU 2223 CA ALA A 249 2911 1894 1736 -519 924 -185 C ATOM 2224 C ALA A 249 -138.019-110.131 638.871 1.00 29.11 C ANISOU 2224 C ALA A 249 4332 3462 3269 -634 926 -246 C ATOM 2225 O ALA A 249 -137.329-110.550 637.952 1.00 29.49 O ANISOU 2225 O ALA A 249 4398 3498 3308 -595 892 -285 O ATOM 2226 CB ALA A 249 -137.474-111.126 641.090 1.00 18.58 C ANISOU 2226 CB ALA A 249 3284 1910 1864 -550 994 -162 C ATOM 2227 N PRO A 250 -139.344-109.902 638.729 1.00 29.21 N ANISOU 2227 N PRO A 250 4245 3545 3307 -774 965 -255 N ATOM 2228 CA PRO A 250 -139.853-110.129 637.371 1.00 18.00 C ANISOU 2228 CA PRO A 250 2742 2196 1901 -881 944 -311 C ATOM 2229 C PRO A 250 -139.200-109.224 636.326 1.00 28.85 C ANISOU 2229 C PRO A 250 3972 3702 3289 -803 858 -317 C ATOM 2230 O PRO A 250 -138.831-109.700 635.257 1.00 26.20 O ANISOU 2230 O PRO A 250 3647 3383 2923 -813 832 -369 O ATOM 2231 CB PRO A 250 -141.351-109.823 637.504 1.00 18.45 C ANISOU 2231 CB PRO A 250 2683 2331 1994 -1030 989 -298 C ATOM 2232 CG PRO A 250 -141.663-110.115 638.923 1.00 18.94 C ANISOU 2232 CG PRO A 250 2850 2304 2042 -1032 1069 -252 C ATOM 2233 CD PRO A 250 -140.447-109.728 639.698 1.00 18.17 C ANISOU 2233 CD PRO A 250 2831 2157 1916 -856 1039 -220 C ATOM 2234 N TYR A 251 -139.039-107.945 636.639 1.00 26.18 N ANISOU 2234 N TYR A 251 3504 3452 2993 -726 817 -264 N ATOM 2235 CA TYR A 251 -138.394-107.025 635.707 1.00 24.71 C ANISOU 2235 CA TYR A 251 3174 3386 2830 -656 732 -244 C ATOM 2236 C TYR A 251 -136.959-107.441 635.338 1.00 23.33 C ANISOU 2236 C TYR A 251 3079 3170 2614 -536 699 -252 C ATOM 2237 O TYR A 251 -136.596-107.439 634.162 1.00 22.98 O ANISOU 2237 O TYR A 251 2970 3213 2549 -532 664 -271 O ATOM 2238 CB TYR A 251 -138.383-105.604 636.277 1.00 24.26 C ANISOU 2238 CB TYR A 251 2987 3389 2841 -587 690 -182 C ATOM 2239 CG TYR A 251 -137.612-104.651 635.402 1.00 26.98 C ANISOU 2239 CG TYR A 251 3190 3840 3222 -515 599 -140 C ATOM 2240 CD1 TYR A 251 -138.125-104.242 634.184 1.00 28.81 C ANISOU 2240 CD1 TYR A 251 3268 4208 3472 -586 563 -128 C ATOM 2241 CD2 TYR A 251 -136.362-104.185 635.780 1.00 27.88 C ANISOU 2241 CD2 TYR A 251 3320 3924 3348 -382 544 -101 C ATOM 2242 CE1 TYR A 251 -137.433-103.386 633.371 1.00 33.72 C ANISOU 2242 CE1 TYR A 251 3757 4932 4121 -527 483 -71 C ATOM 2243 CE2 TYR A 251 -135.653-103.327 634.972 1.00 33.58 C ANISOU 2243 CE2 TYR A 251 3904 4744 4110 -328 463 -47 C ATOM 2244 CZ TYR A 251 -136.193-102.925 633.763 1.00 41.01 C ANISOU 2244 CZ TYR A 251 4695 5820 5067 -400 436 -28 C ATOM 2245 OH TYR A 251 -135.492-102.059 632.937 1.00 48.55 O ANISOU 2245 OH TYR A 251 5508 6882 6058 -352 358 46 O ATOM 2246 N ASN A 252 -136.144-107.778 636.335 1.00 21.11 N ANISOU 2246 N ASN A 252 2930 2771 2318 -434 709 -233 N ATOM 2247 CA ASN A 252 -134.773-108.234 636.085 1.00 22.21 C ANISOU 2247 CA ASN A 252 3142 2867 2429 -307 683 -232 C ATOM 2248 C ASN A 252 -134.747-109.440 635.151 1.00 26.22 C ANISOU 2248 C ASN A 252 3741 3334 2887 -347 723 -311 C ATOM 2249 O ASN A 252 -133.934-109.517 634.236 1.00 28.43 O ANISOU 2249 O ASN A 252 3989 3671 3144 -277 699 -330 O ATOM 2250 CB ASN A 252 -134.067-108.595 637.396 1.00 21.64 C ANISOU 2250 CB ASN A 252 3215 2662 2345 -209 691 -195 C ATOM 2251 CG ASN A 252 -133.750-107.387 638.243 1.00 23.29 C ANISOU 2251 CG ASN A 252 3344 2913 2590 -141 632 -131 C ATOM 2252 OD1 ASN A 252 -132.673-106.807 638.138 1.00 26.49 O ANISOU 2252 OD1 ASN A 252 3688 3359 3019 -34 559 -89 O ATOM 2253 ND2 ASN A 252 -134.690-106.998 639.094 1.00 28.45 N ANISOU 2253 ND2 ASN A 252 3999 3559 3251 -204 663 -128 N ATOM 2254 N ILE A 253 -135.641-110.390 635.392 1.00 26.15 N ANISOU 2254 N ILE A 253 3850 3224 2862 -461 786 -361 N ATOM 2255 CA ILE A 253 -135.685-111.592 634.572 1.00 29.47 C ANISOU 2255 CA ILE A 253 4379 3575 3241 -511 820 -453 C ATOM 2256 C ILE A 253 -136.022-111.246 633.123 1.00 31.61 C ANISOU 2256 C ILE A 253 4516 4011 3485 -581 787 -507 C ATOM 2257 O ILE A 253 -135.313-111.652 632.203 1.00 33.47 O ANISOU 2257 O ILE A 253 4774 4271 3673 -521 781 -565 O ATOM 2258 CB ILE A 253 -136.700-112.611 635.122 1.00 25.19 C ANISOU 2258 CB ILE A 253 3978 2891 2703 -650 885 -486 C ATOM 2259 CG1 ILE A 253 -136.184-113.187 636.440 1.00 24.74 C ANISOU 2259 CG1 ILE A 253 4086 2663 2653 -567 920 -430 C ATOM 2260 CG2 ILE A 253 -136.914-113.719 634.122 1.00 25.22 C ANISOU 2260 CG2 ILE A 253 4074 2832 2674 -731 904 -599 C ATOM 2261 CD1 ILE A 253 -137.258-113.842 637.265 1.00 27.98 C ANISOU 2261 CD1 ILE A 253 4594 2963 3073 -705 985 -413 C ATOM 2262 N VAL A 254 -137.086-110.473 632.931 1.00 30.20 N ANISOU 2262 N VAL A 254 4190 3953 3332 -698 766 -482 N ATOM 2263 CA VAL A 254 -137.496-110.032 631.601 1.00 30.08 C ANISOU 2263 CA VAL A 254 4029 4114 3288 -773 722 -509 C ATOM 2264 C VAL A 254 -136.386-109.203 630.942 1.00 26.28 C ANISOU 2264 C VAL A 254 3432 3763 2791 -639 668 -461 C ATOM 2265 O VAL A 254 -136.232-109.200 629.720 1.00 25.75 O ANISOU 2265 O VAL A 254 3302 3820 2661 -654 644 -498 O ATOM 2266 CB VAL A 254 -138.821-109.224 631.669 1.00 21.55 C ANISOU 2266 CB VAL A 254 2790 3139 2258 -904 704 -462 C ATOM 2267 CG1 VAL A 254 -139.221-108.714 630.301 1.00 24.60 C ANISOU 2267 CG1 VAL A 254 3014 3719 2613 -977 645 -469 C ATOM 2268 CG2 VAL A 254 -139.931-110.094 632.232 1.00 20.97 C ANISOU 2268 CG2 VAL A 254 2813 2956 2198 -1051 763 -502 C ATOM 2269 N LEU A 255 -135.585-108.533 631.761 1.00 22.16 N ANISOU 2269 N LEU A 255 2886 3213 2319 -511 649 -378 N ATOM 2270 CA LEU A 255 -134.467-107.746 631.259 1.00 22.82 C ANISOU 2270 CA LEU A 255 2857 3407 2405 -387 597 -315 C ATOM 2271 C LEU A 255 -133.395-108.664 630.690 1.00 25.90 C ANISOU 2271 C LEU A 255 3349 3765 2725 -288 626 -374 C ATOM 2272 O LEU A 255 -132.731-108.340 629.700 1.00 28.07 O ANISOU 2272 O LEU A 255 3528 4178 2960 -232 604 -359 O ATOM 2273 CB LEU A 255 -133.887-106.879 632.376 1.00 25.26 C ANISOU 2273 CB LEU A 255 3131 3674 2792 -288 560 -221 C ATOM 2274 CG LEU A 255 -133.155-105.594 632.005 1.00 25.06 C ANISOU 2274 CG LEU A 255 2927 3779 2815 -213 482 -121 C ATOM 2275 CD1 LEU A 255 -134.104-104.614 631.333 1.00 18.42 C ANISOU 2275 CD1 LEU A 255 1909 3079 2011 -314 441 -80 C ATOM 2276 CD2 LEU A 255 -132.566-104.991 633.262 1.00 25.47 C ANISOU 2276 CD2 LEU A 255 2995 3747 2936 -123 445 -58 C ATOM 2277 N LEU A 256 -133.227-109.821 631.320 1.00 26.10 N ANISOU 2277 N LEU A 256 3570 3609 2738 -260 682 -436 N ATOM 2278 CA LEU A 256 -132.266-110.800 630.835 1.00 24.32 C ANISOU 2278 CA LEU A 256 3458 3325 2459 -154 721 -505 C ATOM 2279 C LEU A 256 -132.758-111.421 629.532 1.00 26.67 C ANISOU 2279 C LEU A 256 3775 3690 2671 -245 744 -625 C ATOM 2280 O LEU A 256 -131.981-111.637 628.606 1.00 24.59 O ANISOU 2280 O LEU A 256 3497 3505 2340 -159 758 -670 O ATOM 2281 CB LEU A 256 -132.028-111.876 631.888 1.00 18.77 C ANISOU 2281 CB LEU A 256 2961 2391 1778 -104 768 -529 C ATOM 2282 CG LEU A 256 -131.142-111.434 633.048 1.00 21.78 C ANISOU 2282 CG LEU A 256 3343 2717 2215 29 739 -419 C ATOM 2283 CD1 LEU A 256 -131.243-112.408 634.176 1.00 22.83 C ANISOU 2283 CD1 LEU A 256 3673 2636 2365 37 780 -422 C ATOM 2284 CD2 LEU A 256 -129.713-111.343 632.575 1.00 18.92 C ANISOU 2284 CD2 LEU A 256 2928 2418 1844 201 724 -390 C ATOM 2285 N LEU A 257 -134.056-111.703 629.469 1.00 26.74 N ANISOU 2285 N LEU A 257 3811 3674 2674 -419 749 -680 N ATOM 2286 CA LEU A 257 -134.646-112.289 628.275 1.00 28.67 C ANISOU 2286 CA LEU A 257 4078 3983 2834 -532 755 -802 C ATOM 2287 C LEU A 257 -134.522-111.359 627.073 1.00 31.04 C ANISOU 2287 C LEU A 257 4186 4540 3069 -534 706 -770 C ATOM 2288 O LEU A 257 -134.277-111.808 625.958 1.00 33.92 O ANISOU 2288 O LEU A 257 4572 4988 3328 -531 717 -865 O ATOM 2289 CB LEU A 257 -136.114-112.629 628.520 1.00 30.28 C ANISOU 2289 CB LEU A 257 4315 4128 3062 -735 755 -839 C ATOM 2290 CG LEU A 257 -136.411-113.984 629.158 1.00 36.05 C ANISOU 2290 CG LEU A 257 5270 4612 3815 -787 811 -922 C ATOM 2291 CD1 LEU A 257 -137.879-114.087 629.518 1.00 37.35 C ANISOU 2291 CD1 LEU A 257 5420 4749 4021 -994 808 -918 C ATOM 2292 CD2 LEU A 257 -136.032-115.093 628.197 1.00 41.07 C ANISOU 2292 CD2 LEU A 257 6047 5187 4371 -774 836 -1080 C ATOM 2293 N ASN A 258 -134.691-110.060 627.306 1.00 28.92 N ANISOU 2293 N ASN A 258 3734 4394 2861 -539 652 -635 N ATOM 2294 CA ASN A 258 -134.666-109.084 626.226 1.00 28.53 C ANISOU 2294 CA ASN A 258 3489 4586 2766 -554 597 -573 C ATOM 2295 C ASN A 258 -133.258-108.894 625.689 1.00 29.34 C ANISOU 2295 C ASN A 258 3551 4778 2820 -390 606 -540 C ATOM 2296 O ASN A 258 -133.048-108.834 624.479 1.00 35.46 O ANISOU 2296 O ASN A 258 4259 5726 3488 -393 601 -565 O ATOM 2297 CB ASN A 258 -135.232-107.744 626.701 1.00 30.81 C ANISOU 2297 CB ASN A 258 3600 4948 3158 -596 535 -432 C ATOM 2298 CG ASN A 258 -135.175-106.669 625.628 1.00 36.56 C ANISOU 2298 CG ASN A 258 4119 5914 3857 -607 470 -338 C ATOM 2299 OD1 ASN A 258 -136.060-106.587 624.778 1.00 45.63 O ANISOU 2299 OD1 ASN A 258 5194 7191 4950 -733 438 -357 O ATOM 2300 ND2 ASN A 258 -134.141-105.834 625.668 1.00 33.20 N ANISOU 2300 ND2 ASN A 258 3593 5549 3472 -483 444 -226 N ATOM 2301 N THR A 259 -132.299-108.805 626.602 1.00 24.05 N ANISOU 2301 N THR A 259 2916 3999 2223 -250 621 -479 N ATOM 2302 CA THR A 259 -130.908-108.550 626.260 1.00 24.36 C ANISOU 2302 CA THR A 259 2893 4120 2242 -88 628 -423 C ATOM 2303 C THR A 259 -130.325-109.700 625.452 1.00 31.11 C ANISOU 2303 C THR A 259 3869 4970 2981 -16 701 -557 C ATOM 2304 O THR A 259 -129.494-109.502 624.563 1.00 32.66 O ANISOU 2304 O THR A 259 3979 5326 3104 72 717 -538 O ATOM 2305 CB THR A 259 -130.078-108.321 627.532 1.00 25.18 C ANISOU 2305 CB THR A 259 3023 4090 2455 35 617 -337 C ATOM 2306 OG1 THR A 259 -130.561-107.146 628.192 1.00 25.41 O ANISOU 2306 OG1 THR A 259 2932 4139 2583 -22 547 -223 O ATOM 2307 CG2 THR A 259 -128.604-108.143 627.213 1.00 18.08 C ANISOU 2307 CG2 THR A 259 2052 3271 1545 202 625 -273 C ATOM 2308 N PHE A 260 -130.782-110.906 625.754 1.00 32.56 N ANISOU 2308 N PHE A 260 4254 4968 3149 -57 749 -694 N ATOM 2309 CA PHE A 260 -130.330-112.075 625.026 1.00 35.15 C ANISOU 2309 CA PHE A 260 4723 5256 3377 8 820 -848 C ATOM 2310 C PHE A 260 -131.463-112.677 624.208 1.00 36.12 C ANISOU 2310 C PHE A 260 4919 5399 3406 -164 820 -995 C ATOM 2311 O PHE A 260 -131.594-113.899 624.124 1.00 32.79 O ANISOU 2311 O PHE A 260 4690 4817 2950 -175 869 -1151 O ATOM 2312 CB PHE A 260 -129.766-113.104 625.999 1.00 35.11 C ANISOU 2312 CB PHE A 260 4911 4991 3438 120 873 -894 C ATOM 2313 CG PHE A 260 -128.712-112.549 626.905 1.00 31.55 C ANISOU 2313 CG PHE A 260 4392 4513 3080 275 858 -748 C ATOM 2314 CD1 PHE A 260 -127.419-112.381 626.454 1.00 29.09 C ANISOU 2314 CD1 PHE A 260 3999 4309 2744 448 882 -706 C ATOM 2315 CD2 PHE A 260 -129.016-112.193 628.205 1.00 28.24 C ANISOU 2315 CD2 PHE A 260 3988 3974 2768 243 817 -653 C ATOM 2316 CE1 PHE A 260 -126.449-111.872 627.279 1.00 24.62 C ANISOU 2316 CE1 PHE A 260 3361 3724 2268 578 854 -569 C ATOM 2317 CE2 PHE A 260 -128.045-111.680 629.037 1.00 24.70 C ANISOU 2317 CE2 PHE A 260 3482 3507 2395 376 788 -527 C ATOM 2318 CZ PHE A 260 -126.761-111.520 628.573 1.00 22.47 C ANISOU 2318 CZ PHE A 260 3113 3326 2098 538 800 -483 C ATOM 2319 N GLN A 261 -132.283-111.819 623.605 1.00 39.11 N ANISOU 2319 N GLN A 261 5141 5969 3748 -301 757 -942 N ATOM 2320 CA GLN A 261 -133.460-112.298 622.892 1.00 41.71 C ANISOU 2320 CA GLN A 261 5518 6334 3996 -486 735 -1064 C ATOM 2321 C GLN A 261 -133.053-113.079 621.660 1.00 48.09 C ANISOU 2321 C GLN A 261 6407 7203 4662 -443 765 -1207 C ATOM 2322 O GLN A 261 -133.759-113.991 621.239 1.00 51.30 O ANISOU 2322 O GLN A 261 6942 7524 5026 -550 756 -1348 O ATOM 2323 CB GLN A 261 -134.389-111.142 622.518 1.00 37.77 C ANISOU 2323 CB GLN A 261 4813 6037 3502 -626 650 -950 C ATOM 2324 CG GLN A 261 -133.845-110.165 621.503 1.00 38.26 C ANISOU 2324 CG GLN A 261 4684 6374 3480 -572 618 -853 C ATOM 2325 CD GLN A 261 -134.830-109.042 621.223 1.00 41.62 C ANISOU 2325 CD GLN A 261 4912 6969 3934 -710 527 -727 C ATOM 2326 OE1 GLN A 261 -135.283-108.863 620.091 1.00 42.71 O ANISOU 2326 OE1 GLN A 261 4969 7305 3955 -800 484 -741 O ATOM 2327 NE2 GLN A 261 -135.167-108.277 622.259 1.00 37.66 N ANISOU 2327 NE2 GLN A 261 4331 6386 3590 -719 495 -600 N ATOM 2328 N GLU A 262 -131.901-112.734 621.093 1.00 54.88 N ANISOU 2328 N GLU A 262 7189 8186 5477 -276 787 -1148 N ATOM 2329 CA GLU A 262 -131.368-113.471 619.951 1.00 60.40 C ANISOU 2329 CA GLU A 262 7969 8920 6061 -195 820 -1259 C ATOM 2330 C GLU A 262 -130.988-114.887 620.385 1.00 62.21 C ANISOU 2330 C GLU A 262 8440 8885 6311 -101 890 -1414 C ATOM 2331 O GLU A 262 -131.169-115.840 619.633 1.00 65.90 O ANISOU 2331 O GLU A 262 9043 9297 6701 -113 899 -1566 O ATOM 2332 CB GLU A 262 -130.163-112.744 619.342 1.00 63.98 C ANISOU 2332 CB GLU A 262 8276 9556 6479 -40 841 -1138 C ATOM 2333 CG GLU A 262 -129.448-113.528 618.251 1.00 68.64 C ANISOU 2333 CG GLU A 262 8960 10172 6949 68 903 -1249 C ATOM 2334 CD GLU A 262 -128.666-112.642 617.292 1.00 70.47 C ANISOU 2334 CD GLU A 262 9005 10650 7121 135 900 -1122 C ATOM 2335 OE1 GLU A 262 -128.344-111.484 617.652 1.00 67.71 O ANISOU 2335 OE1 GLU A 262 8464 10410 6854 148 857 -934 O ATOM 2336 OE2 GLU A 262 -128.380-113.108 616.170 1.00 73.87 O ANISOU 2336 OE2 GLU A 262 9483 11160 7426 170 936 -1209 O ATOM 2337 N PHE A 263 -130.483-115.015 621.610 1.00 59.49 N ANISOU 2337 N PHE A 263 8150 8373 6079 -8 932 -1372 N ATOM 2338 CA PHE A 263 -130.121-116.314 622.179 1.00 56.97 C ANISOU 2338 CA PHE A 263 8050 7781 5815 87 987 -1490 C ATOM 2339 C PHE A 263 -131.338-117.215 622.378 1.00 54.52 C ANISOU 2339 C PHE A 263 7895 7281 5539 -95 953 -1606 C ATOM 2340 O PHE A 263 -131.236-118.430 622.254 1.00 58.31 O ANISOU 2340 O PHE A 263 8547 7579 6030 -52 972 -1738 O ATOM 2341 CB PHE A 263 -129.387-116.122 623.514 1.00 57.40 C ANISOU 2341 CB PHE A 263 8111 7706 5992 207 1027 -1387 C ATOM 2342 CG PHE A 263 -129.190-117.397 624.299 1.00 61.12 C ANISOU 2342 CG PHE A 263 8794 7870 6558 275 1059 -1462 C ATOM 2343 CD1 PHE A 263 -128.094-118.209 624.068 1.00 64.51 C ANISOU 2343 CD1 PHE A 263 9287 8231 6995 472 1107 -1528 C ATOM 2344 CD2 PHE A 263 -130.097-117.773 625.279 1.00 62.73 C ANISOU 2344 CD2 PHE A 263 9113 7865 6856 137 1039 -1451 C ATOM 2345 CE1 PHE A 263 -127.908-119.376 624.791 1.00 66.14 C ANISOU 2345 CE1 PHE A 263 9667 8153 7310 528 1124 -1575 C ATOM 2346 CE2 PHE A 263 -129.918-118.938 626.001 1.00 65.68 C ANISOU 2346 CE2 PHE A 263 9671 7960 7326 192 1060 -1490 C ATOM 2347 CZ PHE A 263 -128.820-119.740 625.757 1.00 66.39 C ANISOU 2347 CZ PHE A 263 9822 7973 7431 388 1098 -1548 C ATOM 2348 N PHE A 264 -132.484-116.626 622.702 1.00 52.80 N ANISOU 2348 N PHE A 264 7605 7105 5351 -298 901 -1551 N ATOM 2349 CA PHE A 264 -133.701-117.409 622.893 1.00 54.21 C ANISOU 2349 CA PHE A 264 7906 7122 5568 -493 871 -1641 C ATOM 2350 C PHE A 264 -134.548-117.419 621.631 1.00 58.80 C ANISOU 2350 C PHE A 264 8436 7865 6039 -645 808 -1725 C ATOM 2351 O PHE A 264 -135.649-117.972 621.621 1.00 62.63 O ANISOU 2351 O PHE A 264 8989 8260 6546 -831 769 -1795 O ATOM 2352 CB PHE A 264 -134.526-116.863 624.054 1.00 51.27 C ANISOU 2352 CB PHE A 264 7495 6692 5295 -631 860 -1537 C ATOM 2353 CG PHE A 264 -133.853-116.984 625.386 1.00 49.50 C ANISOU 2353 CG PHE A 264 7353 6276 5178 -505 915 -1457 C ATOM 2354 CD1 PHE A 264 -133.727-118.216 626.002 1.00 49.40 C ANISOU 2354 CD1 PHE A 264 7545 5982 5243 -468 947 -1512 C ATOM 2355 CD2 PHE A 264 -133.357-115.860 626.033 1.00 49.01 C ANISOU 2355 CD2 PHE A 264 7133 6315 5173 -409 896 -1279 C ATOM 2356 CE1 PHE A 264 -133.114-118.328 627.241 1.00 50.20 C ANISOU 2356 CE1 PHE A 264 7721 5913 5438 -350 987 -1419 C ATOM 2357 CE2 PHE A 264 -132.739-115.966 627.274 1.00 47.47 C ANISOU 2357 CE2 PHE A 264 7002 5954 5081 -289 921 -1183 C ATOM 2358 CZ PHE A 264 -132.620-117.203 627.878 1.00 47.73 C ANISOU 2358 CZ PHE A 264 7256 5717 5162 -259 969 -1253 C ATOM 2359 N GLY A 265 -134.033-116.800 620.572 1.00 57.01 N ANISOU 2359 N GLY A 265 8085 7881 5696 -569 795 -1704 N ATOM 2360 CA GLY A 265 -134.753-116.706 619.315 1.00 52.86 C ANISOU 2360 CA GLY A 265 7498 7536 5051 -700 731 -1764 C ATOM 2361 C GLY A 265 -135.999-115.843 619.392 1.00 50.19 C ANISOU 2361 C GLY A 265 7002 7337 4730 -919 656 -1676 C ATOM 2362 O GLY A 265 -136.960-116.056 618.655 1.00 55.38 O ANISOU 2362 O GLY A 265 7649 8065 5328 -1085 593 -1742 O ATOM 2363 N LEU A 266 -135.985-114.858 620.281 1.00 41.79 N ANISOU 2363 N LEU A 266 5812 6318 3749 -914 659 -1527 N ATOM 2364 CA LEU A 266 -137.128-113.974 620.437 1.00 37.63 C ANISOU 2364 CA LEU A 266 5125 5927 3246 -1100 592 -1435 C ATOM 2365 C LEU A 266 -136.960-112.689 619.634 1.00 39.53 C ANISOU 2365 C LEU A 266 5132 6470 3418 -1077 539 -1300 C ATOM 2366 O LEU A 266 -137.774-111.774 619.762 1.00 44.14 O ANISOU 2366 O LEU A 266 5552 7191 4027 -1197 479 -1193 O ATOM 2367 CB LEU A 266 -137.339-113.638 621.914 1.00 36.31 C ANISOU 2367 CB LEU A 266 4956 5620 3221 -1111 620 -1341 C ATOM 2368 CG LEU A 266 -138.249-114.523 622.771 1.00 39.40 C ANISOU 2368 CG LEU A 266 5492 5768 3708 -1249 633 -1403 C ATOM 2369 CD1 LEU A 266 -138.085-115.991 622.427 1.00 45.62 C ANISOU 2369 CD1 LEU A 266 6508 6363 4464 -1247 665 -1581 C ATOM 2370 CD2 LEU A 266 -137.945-114.301 624.244 1.00 35.17 C ANISOU 2370 CD2 LEU A 266 4977 5061 3324 -1154 677 -1279 C ATOM 2371 N ASN A 267 -135.914-112.614 618.809 1.00 39.78 N ANISOU 2371 N ASN A 267 5143 6604 3369 -921 559 -1293 N ATOM 2372 CA ASN A 267 -135.607-111.361 618.106 1.00 40.34 C ANISOU 2372 CA ASN A 267 4989 6942 3397 -884 513 -1133 C ATOM 2373 C ASN A 267 -136.256-111.247 616.724 1.00 39.01 C ANISOU 2373 C ASN A 267 4741 6981 3102 -1001 442 -1157 C ATOM 2374 O ASN A 267 -135.578-111.166 615.701 1.00 37.41 O ANISOU 2374 O ASN A 267 4505 6913 2798 -913 448 -1151 O ATOM 2375 CB ASN A 267 -134.084-111.153 617.991 1.00 38.95 C ANISOU 2375 CB ASN A 267 4797 6788 3215 -658 572 -1070 C ATOM 2376 CG ASN A 267 -133.398-112.237 617.199 1.00 44.68 C ANISOU 2376 CG ASN A 267 5683 7459 3834 -556 631 -1223 C ATOM 2377 OD1 ASN A 267 -133.723-113.420 617.326 1.00 49.28 O ANISOU 2377 OD1 ASN A 267 6463 7857 4404 -589 658 -1393 O ATOM 2378 ND2 ASN A 267 -132.443-111.839 616.361 1.00 45.43 N ANISOU 2378 ND2 ASN A 267 5693 7711 3857 -432 651 -1159 N ATOM 2379 N ASN A 268 -137.584-111.235 616.716 1.00 37.69 N ANISOU 2379 N ASN A 268 4537 6843 2942 -1202 375 -1175 N ATOM 2380 CA ASN A 268 -138.358-110.887 615.536 1.00 39.95 C ANISOU 2380 CA ASN A 268 4700 7349 3128 -1331 290 -1151 C ATOM 2381 C ASN A 268 -139.463-109.944 615.981 1.00 41.83 C ANISOU 2381 C ASN A 268 4759 7685 3448 -1479 215 -1011 C ATOM 2382 O ASN A 268 -139.615-109.701 617.174 1.00 43.60 O ANISOU 2382 O ASN A 268 4983 7795 3789 -1483 235 -966 O ATOM 2383 CB ASN A 268 -138.926-112.129 614.857 1.00 46.43 C ANISOU 2383 CB ASN A 268 5688 8091 3860 -1432 279 -1347 C ATOM 2384 CG ASN A 268 -139.850-112.914 615.764 1.00 50.24 C ANISOU 2384 CG ASN A 268 6295 8352 4441 -1570 278 -1440 C ATOM 2385 OD1 ASN A 268 -141.046-112.639 615.836 1.00 53.50 O ANISOU 2385 OD1 ASN A 268 6613 8822 4892 -1746 211 -1393 O ATOM 2386 ND2 ASN A 268 -139.295-113.896 616.469 1.00 49.64 N ANISOU 2386 ND2 ASN A 268 6426 8018 4418 -1484 356 -1557 N ATOM 2387 N CYS A 269 -140.231-109.408 615.041 1.00 41.43 N ANISOU 2387 N CYS A 269 4559 7845 3339 -1590 134 -937 N ATOM 2388 CA CYS A 269 -141.206-108.375 615.373 1.00 44.84 C ANISOU 2388 CA CYS A 269 4798 8376 3864 -1689 68 -765 C ATOM 2389 C CYS A 269 -142.287-108.878 616.330 1.00 47.84 C ANISOU 2389 C CYS A 269 5245 8576 4356 -1817 64 -820 C ATOM 2390 O CYS A 269 -142.526-108.278 617.380 1.00 51.04 O ANISOU 2390 O CYS A 269 5584 8901 4906 -1797 71 -715 O ATOM 2391 CB CYS A 269 -141.853-107.824 614.106 1.00 31.78 C ANISOU 2391 CB CYS A 269 2999 6948 2129 -1762 0 -667 C ATOM 2392 SG CYS A 269 -142.827-106.335 614.397 1.00 56.40 S ANISOU 2392 SG CYS A 269 5935 10123 5373 -1760 -45 -393 S ATOM 2393 N SER A 270 -142.927-109.983 615.971 1.00 50.37 N ANISOU 2393 N SER A 270 5699 8812 4628 -1935 57 -974 N ATOM 2394 CA SER A 270 -144.018-110.524 616.775 1.00 53.15 C ANISOU 2394 CA SER A 270 6109 8994 5093 -2064 55 -1010 C ATOM 2395 C SER A 270 -143.567-110.961 618.173 1.00 53.63 C ANISOU 2395 C SER A 270 6299 8816 5264 -2019 131 -1069 C ATOM 2396 O SER A 270 -144.218-110.632 619.166 1.00 55.51 O ANISOU 2396 O SER A 270 6479 8963 5647 -2053 140 -980 O ATOM 2397 CB SER A 270 -144.675-111.697 616.043 1.00 57.65 C ANISOU 2397 CB SER A 270 6808 9512 5584 -2194 26 -1168 C ATOM 2398 OG SER A 270 -143.797-112.807 615.965 1.00 61.05 O ANISOU 2398 OG SER A 270 7460 9785 5950 -2130 84 -1357 O ATOM 2399 N SER A 271 -142.458-111.695 618.250 1.00 50.99 N ANISOU 2399 N SER A 271 6146 8358 4868 -1908 200 -1201 N ATOM 2400 CA SER A 271 -141.952-112.179 619.535 1.00 45.30 C ANISOU 2400 CA SER A 271 5579 7393 4240 -1841 284 -1252 C ATOM 2401 C SER A 271 -141.528-111.035 620.446 1.00 38.76 C ANISOU 2401 C SER A 271 4615 6573 3538 -1711 306 -1065 C ATOM 2402 O SER A 271 -141.825-111.035 621.644 1.00 36.31 O ANISOU 2402 O SER A 271 4328 6090 3378 -1709 345 -1012 O ATOM 2403 CB SER A 271 -140.768-113.126 619.334 1.00 45.25 C ANISOU 2403 CB SER A 271 5780 7240 4172 -1683 362 -1383 C ATOM 2404 OG SER A 271 -141.145-114.273 618.604 1.00 47.73 O ANISOU 2404 OG SER A 271 6234 7471 4429 -1762 346 -1534 O ATOM 2405 N SER A 272 -140.822-110.065 619.879 1.00 35.49 N ANISOU 2405 N SER A 272 4060 6350 3074 -1595 283 -956 N ATOM 2406 CA SER A 272 -140.282-108.984 620.684 1.00 35.93 C ANISOU 2406 CA SER A 272 3998 6391 3264 -1454 300 -779 C ATOM 2407 C SER A 272 -141.400-108.068 621.152 1.00 34.29 C ANISOU 2407 C SER A 272 3607 6231 3189 -1550 243 -640 C ATOM 2408 O SER A 272 -141.248-107.363 622.139 1.00 30.59 O ANISOU 2408 O SER A 272 3081 5680 2864 -1464 264 -528 O ATOM 2409 CB SER A 272 -139.227-108.193 619.908 1.00 35.53 C ANISOU 2409 CB SER A 272 3838 6530 3132 -1319 286 -688 C ATOM 2410 OG SER A 272 -139.825-107.403 618.899 1.00 38.81 O ANISOU 2410 OG SER A 272 4064 7202 3481 -1411 195 -597 O ATOM 2411 N ASN A 273 -142.533-108.087 620.460 1.00 36.83 N ANISOU 2411 N ASN A 273 3847 6680 3467 -1714 172 -649 N ATOM 2412 CA ASN A 273 -143.663-107.285 620.904 1.00 36.29 C ANISOU 2412 CA ASN A 273 3715 6539 3535 -1660 137 -489 C ATOM 2413 C ASN A 273 -144.294-107.875 622.141 1.00 40.09 C ANISOU 2413 C ASN A 273 4285 6811 4137 -1706 191 -532 C ATOM 2414 O ASN A 273 -144.713-107.142 623.036 1.00 41.47 O ANISOU 2414 O ASN A 273 4425 6876 4455 -1597 188 -416 O ATOM 2415 CB ASN A 273 -144.698-107.146 619.803 1.00 39.26 C ANISOU 2415 CB ASN A 273 4026 7050 3840 -1739 64 -452 C ATOM 2416 CG ASN A 273 -144.456-105.927 618.957 1.00 49.83 C ANISOU 2416 CG ASN A 273 5252 8535 5148 -1626 2 -295 C ATOM 2417 OD1 ASN A 273 -143.489-105.193 619.180 1.00 53.56 O ANISOU 2417 OD1 ASN A 273 5700 8995 5654 -1484 8 -216 O ATOM 2418 ND2 ASN A 273 -145.314-105.706 617.965 1.00 52.84 N ANISOU 2418 ND2 ASN A 273 5568 9042 5466 -1690 -59 -245 N ATOM 2419 N ARG A 274 -144.367-109.202 622.188 1.00 41.28 N ANISOU 2419 N ARG A 274 4568 6884 4231 -1863 235 -704 N ATOM 2420 CA ARG A 274 -144.831-109.886 623.383 1.00 40.52 C ANISOU 2420 CA ARG A 274 4582 6573 4240 -1912 301 -741 C ATOM 2421 C ARG A 274 -143.822-109.680 624.500 1.00 36.08 C ANISOU 2421 C ARG A 274 4066 5889 3756 -1805 380 -720 C ATOM 2422 O ARG A 274 -144.191-109.494 625.656 1.00 33.59 O ANISOU 2422 O ARG A 274 3768 5440 3556 -1747 422 -647 O ATOM 2423 CB ARG A 274 -145.045-111.372 623.116 1.00 46.65 C ANISOU 2423 CB ARG A 274 5539 7239 4945 -2076 320 -926 C ATOM 2424 CG ARG A 274 -146.222-111.662 622.200 1.00 52.74 C ANISOU 2424 CG ARG A 274 6265 8103 5669 -2193 250 -931 C ATOM 2425 CD ARG A 274 -146.565-113.145 622.198 1.00 61.38 C ANISOU 2425 CD ARG A 274 7553 9026 6744 -2329 271 -1085 C ATOM 2426 NE ARG A 274 -145.452-113.942 621.693 1.00 67.71 N ANISOU 2426 NE ARG A 274 8538 9756 7433 -2294 294 -1256 N ATOM 2427 CZ ARG A 274 -145.218-114.170 620.402 1.00 72.77 C ANISOU 2427 CZ ARG A 274 9195 10519 7935 -2298 244 -1343 C ATOM 2428 NH1 ARG A 274 -146.023-113.659 619.476 1.00 71.77 N ANISOU 2428 NH1 ARG A 274 8910 10601 7758 -2372 160 -1277 N ATOM 2429 NH2 ARG A 274 -144.173-114.903 620.036 1.00 75.73 N ANISOU 2429 NH2 ARG A 274 9749 10802 8225 -2199 282 -1483 N ATOM 2430 N LEU A 275 -142.544-109.687 624.141 1.00 35.54 N ANISOU 2430 N LEU A 275 4070 5823 3612 -1652 394 -746 N ATOM 2431 CA LEU A 275 -141.479-109.442 625.101 1.00 31.65 C ANISOU 2431 CA LEU A 275 3643 5198 3183 -1465 455 -694 C ATOM 2432 C LEU A 275 -141.615-108.040 625.664 1.00 30.14 C ANISOU 2432 C LEU A 275 3263 5082 3107 -1400 429 -530 C ATOM 2433 O LEU A 275 -141.458-107.827 626.866 1.00 28.30 O ANISOU 2433 O LEU A 275 3066 4715 2970 -1326 475 -482 O ATOM 2434 CB LEU A 275 -140.110-109.628 624.447 1.00 32.54 C ANISOU 2434 CB LEU A 275 3828 5342 3195 -1318 466 -739 C ATOM 2435 CG LEU A 275 -138.912-109.866 625.363 1.00 35.15 C ANISOU 2435 CG LEU A 275 4287 5500 3568 -1138 533 -731 C ATOM 2436 CD1 LEU A 275 -139.299-110.769 626.508 1.00 36.51 C ANISOU 2436 CD1 LEU A 275 4628 5433 3809 -1180 594 -781 C ATOM 2437 CD2 LEU A 275 -137.788-110.500 624.562 1.00 38.07 C ANISOU 2437 CD2 LEU A 275 4760 5885 3821 -1031 559 -826 C ATOM 2438 N ASP A 276 -141.930-107.090 624.787 1.00 26.07 N ANISOU 2438 N ASP A 276 2584 4742 2577 -1386 337 -440 N ATOM 2439 CA ASP A 276 -142.079-105.695 625.181 1.00 23.72 C ANISOU 2439 CA ASP A 276 2203 4407 2403 -1216 269 -278 C ATOM 2440 C ASP A 276 -143.272-105.493 626.113 1.00 26.23 C ANISOU 2440 C ASP A 276 2524 4600 2843 -1216 273 -237 C ATOM 2441 O ASP A 276 -143.192-104.705 627.053 1.00 27.04 O ANISOU 2441 O ASP A 276 2611 4600 3063 -1097 276 -162 O ATOM 2442 CB ASP A 276 -142.217-104.797 623.946 1.00 32.77 C ANISOU 2442 CB ASP A 276 3244 5700 3507 -1171 173 -185 C ATOM 2443 CG ASP A 276 -140.894-104.607 623.194 1.00 44.99 C ANISOU 2443 CG ASP A 276 4762 7369 4961 -1108 164 -172 C ATOM 2444 OD1 ASP A 276 -139.815-104.726 623.816 1.00 47.52 O ANISOU 2444 OD1 ASP A 276 5119 7631 5306 -1032 216 -186 O ATOM 2445 OD2 ASP A 276 -140.937-104.339 621.971 1.00 52.67 O ANISOU 2445 OD2 ASP A 276 5674 8507 5832 -1130 111 -139 O ATOM 2446 N GLN A 277 -144.375-106.191 625.856 1.00 20.75 N ANISOU 2446 N GLN A 277 1843 3922 2120 -1352 274 -290 N ATOM 2447 CA GLN A 277 -145.521-106.140 626.760 1.00 20.93 C ANISOU 2447 CA GLN A 277 1858 3842 2252 -1359 293 -255 C ATOM 2448 C GLN A 277 -145.126-106.607 628.147 1.00 20.28 C ANISOU 2448 C GLN A 277 1877 3610 2217 -1343 385 -289 C ATOM 2449 O GLN A 277 -145.399-105.934 629.140 1.00 22.44 O ANISOU 2449 O GLN A 277 2123 3807 2598 -1247 401 -218 O ATOM 2450 CB GLN A 277 -146.676-106.991 626.229 1.00 32.94 C ANISOU 2450 CB GLN A 277 3382 5404 3728 -1523 282 -310 C ATOM 2451 CG GLN A 277 -147.305-106.434 624.959 1.00 33.77 C ANISOU 2451 CG GLN A 277 3377 5658 3796 -1538 190 -256 C ATOM 2452 CD GLN A 277 -148.407-107.319 624.409 1.00 39.80 C ANISOU 2452 CD GLN A 277 4142 6469 4511 -1710 171 -314 C ATOM 2453 OE1 GLN A 277 -148.935-108.185 625.109 1.00 42.19 O ANISOU 2453 OE1 GLN A 277 4511 6672 4846 -1802 222 -367 O ATOM 2454 NE2 GLN A 277 -148.756-107.109 623.145 1.00 41.84 N ANISOU 2454 NE2 GLN A 277 4330 6878 4688 -1758 95 -296 N ATOM 2455 N ALA A 278 -144.471-107.761 628.210 1.00 26.79 N ANISOU 2455 N ALA A 278 2831 4387 2960 -1444 455 -402 N ATOM 2456 CA ALA A 278 -143.967-108.289 629.474 1.00 26.71 C ANISOU 2456 CA ALA A 278 2948 4219 2980 -1432 556 -430 C ATOM 2457 C ALA A 278 -143.031-107.291 630.163 1.00 26.24 C ANISOU 2457 C ALA A 278 2855 4139 2976 -1256 556 -352 C ATOM 2458 O ALA A 278 -143.118-107.078 631.374 1.00 26.61 O ANISOU 2458 O ALA A 278 2936 4087 3086 -1197 600 -314 O ATOM 2459 CB ALA A 278 -143.250-109.603 629.242 1.00 25.74 C ANISOU 2459 CB ALA A 278 2996 4013 2770 -1538 630 -559 C ATOM 2460 N MET A 279 -142.146-106.679 629.382 1.00 22.23 N ANISOU 2460 N MET A 279 2278 3731 2436 -1177 503 -326 N ATOM 2461 CA MET A 279 -141.171-105.734 629.915 1.00 23.17 C ANISOU 2461 CA MET A 279 2362 3832 2610 -1017 487 -249 C ATOM 2462 C MET A 279 -141.851-104.543 630.555 1.00 25.44 C ANISOU 2462 C MET A 279 2565 4081 3020 -923 436 -152 C ATOM 2463 O MET A 279 -141.470-104.122 631.645 1.00 20.24 O ANISOU 2463 O MET A 279 1929 3344 2418 -846 467 -124 O ATOM 2464 CB MET A 279 -140.225-105.248 628.820 1.00 26.06 C ANISOU 2464 CB MET A 279 2653 4322 2927 -951 426 -219 C ATOM 2465 CG MET A 279 -138.969-104.581 629.360 1.00 31.18 C ANISOU 2465 CG MET A 279 3290 4941 3617 -806 422 -157 C ATOM 2466 SD MET A 279 -138.060-103.679 628.091 1.00 55.91 S ANISOU 2466 SD MET A 279 6311 8206 6728 -707 323 -71 S ATOM 2467 CE MET A 279 -138.036-104.882 626.764 1.00 55.61 C ANISOU 2467 CE MET A 279 6294 8321 6515 -829 368 -183 C ATOM 2468 N GLN A 280 -142.866-104.009 629.884 1.00 16.78 N ANISOU 2468 N GLN A 280 1376 3038 1961 -934 371 -107 N ATOM 2469 CA GLN A 280 -143.533-102.820 630.379 1.00 16.47 C ANISOU 2469 CA GLN A 280 1257 2951 2051 -844 342 -25 C ATOM 2470 C GLN A 280 -144.375-103.138 631.608 1.00 26.13 C ANISOU 2470 C GLN A 280 2510 4098 3320 -875 416 -40 C ATOM 2471 O GLN A 280 -144.499-102.312 632.520 1.00 23.12 O ANISOU 2471 O GLN A 280 2098 3659 3028 -794 433 2 O ATOM 2472 CB GLN A 280 -144.414-102.194 629.306 1.00 24.33 C ANISOU 2472 CB GLN A 280 2156 4012 3078 -850 271 24 C ATOM 2473 CG GLN A 280 -144.928-100.828 629.706 1.00 23.57 C ANISOU 2473 CG GLN A 280 1979 3847 3129 -751 252 90 C ATOM 2474 CD GLN A 280 -143.797 -99.923 630.145 1.00 25.18 C ANISOU 2474 CD GLN A 280 2193 3988 3386 -642 237 115 C ATOM 2475 OE1 GLN A 280 -142.923 -99.579 629.349 1.00 26.68 O ANISOU 2475 OE1 GLN A 280 2383 4217 3539 -606 184 138 O ATOM 2476 NE2 GLN A 280 -143.794 -99.547 631.420 1.00 24.38 N ANISOU 2476 NE2 GLN A 280 2100 3801 3362 -595 284 110 N ATOM 2477 N VAL A 281 -144.964-104.328 631.630 1.00 21.70 N ANISOU 2477 N VAL A 281 2012 3537 2695 -1001 464 -102 N ATOM 2478 CA VAL A 281 -145.794-104.700 632.758 1.00 21.03 C ANISOU 2478 CA VAL A 281 1959 3386 2645 -1037 538 -106 C ATOM 2479 C VAL A 281 -144.912-104.836 633.984 1.00 24.35 C ANISOU 2479 C VAL A 281 2484 3721 3048 -989 611 -126 C ATOM 2480 O VAL A 281 -145.228-104.297 635.042 1.00 24.24 O ANISOU 2480 O VAL A 281 2453 3671 3085 -932 651 -94 O ATOM 2481 CB VAL A 281 -146.573-106.004 632.502 1.00 22.03 C ANISOU 2481 CB VAL A 281 2144 3511 2715 -1195 572 -166 C ATOM 2482 CG1 VAL A 281 -147.196-106.523 633.786 1.00 22.83 C ANISOU 2482 CG1 VAL A 281 2305 3529 2838 -1232 663 -164 C ATOM 2483 CG2 VAL A 281 -147.662-105.765 631.478 1.00 25.43 C ANISOU 2483 CG2 VAL A 281 2458 4032 3174 -1242 502 -135 C ATOM 2484 N THR A 282 -143.783-105.521 633.839 1.00 21.70 N ANISOU 2484 N THR A 282 2256 3356 2635 -1009 637 -182 N ATOM 2485 CA THR A 282 -142.934-105.788 634.994 1.00 19.78 C ANISOU 2485 CA THR A 282 2137 3015 2366 -968 717 -199 C ATOM 2486 C THR A 282 -142.117-104.572 635.417 1.00 16.18 C ANISOU 2486 C THR A 282 1619 2575 1956 -832 682 -151 C ATOM 2487 O THR A 282 -141.778-104.426 636.595 1.00 15.71 O ANISOU 2487 O THR A 282 1626 2450 1892 -784 742 -151 O ATOM 2488 CB THR A 282 -141.981-106.964 634.743 1.00 16.86 C ANISOU 2488 CB THR A 282 1922 2579 1904 -1025 777 -266 C ATOM 2489 OG1 THR A 282 -141.122-106.665 633.636 1.00 16.39 O ANISOU 2489 OG1 THR A 282 1803 2608 1818 -985 716 -272 O ATOM 2490 CG2 THR A 282 -142.761-108.211 634.452 1.00 18.12 C ANISOU 2490 CG2 THR A 282 2168 2689 2028 -1179 820 -324 C ATOM 2491 N GLU A 283 -141.781-103.712 634.467 1.00 15.10 N ANISOU 2491 N GLU A 283 1362 2517 1856 -774 586 -109 N ATOM 2492 CA GLU A 283 -141.138-102.446 634.802 1.00 14.28 C ANISOU 2492 CA GLU A 283 1184 2419 1823 -657 537 -55 C ATOM 2493 C GLU A 283 -142.095-101.613 635.647 1.00 22.19 C ANISOU 2493 C GLU A 283 2126 3395 2908 -624 552 -26 C ATOM 2494 O GLU A 283 -141.704-101.026 636.656 1.00 17.36 O ANISOU 2494 O GLU A 283 1522 2754 2321 -566 580 -30 O ATOM 2495 CB GLU A 283 -140.732-101.692 633.534 1.00 13.96 C ANISOU 2495 CB GLU A 283 1043 2443 1819 -606 430 0 C ATOM 2496 CG GLU A 283 -140.077-100.352 633.768 1.00 21.47 C ANISOU 2496 CG GLU A 283 1925 3369 2864 -497 367 57 C ATOM 2497 CD GLU A 283 -139.995 -99.530 632.500 1.00 26.66 C ANISOU 2497 CD GLU A 283 2512 4051 3568 -459 274 104 C ATOM 2498 OE1 GLU A 283 -140.817 -98.604 632.322 1.00 26.94 O ANISOU 2498 OE1 GLU A 283 2486 4054 3694 -440 244 122 O ATOM 2499 OE2 GLU A 283 -139.118 -99.824 631.662 1.00 36.54 O ANISOU 2499 OE2 GLU A 283 3772 5360 4752 -453 241 116 O ATOM 2500 N THR A 284 -143.360-101.596 635.235 1.00 20.28 N ANISOU 2500 N THR A 284 1823 3175 2705 -665 542 -5 N ATOM 2501 CA THR A 284 -144.398-100.838 635.912 1.00 16.92 C ANISOU 2501 CA THR A 284 1324 2741 2365 -635 567 28 C ATOM 2502 C THR A 284 -144.635-101.364 637.330 1.00 18.53 C ANISOU 2502 C THR A 284 1614 2911 2513 -660 678 -17 C ATOM 2503 O THR A 284 -144.764-100.592 638.276 1.00 23.93 O ANISOU 2503 O THR A 284 2271 3588 3232 -600 717 -19 O ATOM 2504 CB THR A 284 -145.706-100.881 635.100 1.00 20.65 C ANISOU 2504 CB THR A 284 1713 3245 2887 -683 542 60 C ATOM 2505 OG1 THR A 284 -145.505-100.207 633.855 1.00 21.18 O ANISOU 2505 OG1 THR A 284 1711 3329 3007 -649 451 89 O ATOM 2506 CG2 THR A 284 -146.845-100.211 635.851 1.00 23.41 C ANISOU 2506 CG2 THR A 284 1978 3590 3325 -655 589 96 C ATOM 2507 N LEU A 285 -144.690-102.681 637.471 1.00 16.80 N ANISOU 2507 N LEU A 285 1511 2663 2208 -749 736 -61 N ATOM 2508 CA LEU A 285 -144.787-103.304 638.779 1.00 20.38 C ANISOU 2508 CA LEU A 285 2085 3057 2602 -772 846 -94 C ATOM 2509 C LEU A 285 -143.666-102.813 639.684 1.00 25.24 C ANISOU 2509 C LEU A 285 2773 3627 3189 -687 879 -119 C ATOM 2510 O LEU A 285 -143.914-102.373 640.802 1.00 28.45 O ANISOU 2510 O LEU A 285 3198 4021 3592 -643 946 -132 O ATOM 2511 CB LEU A 285 -144.738-104.822 638.652 1.00 17.48 C ANISOU 2511 CB LEU A 285 1856 2630 2156 -879 890 -128 C ATOM 2512 CG LEU A 285 -144.761-105.615 639.956 1.00 21.29 C ANISOU 2512 CG LEU A 285 2493 3024 2571 -903 999 -139 C ATOM 2513 CD1 LEU A 285 -146.066-105.401 640.708 1.00 19.84 C ANISOU 2513 CD1 LEU A 285 2241 2880 2417 -918 1053 -108 C ATOM 2514 CD2 LEU A 285 -144.555-107.089 639.654 1.00 24.07 C ANISOU 2514 CD2 LEU A 285 2992 3291 2864 -1006 1029 -165 C ATOM 2515 N GLY A 286 -142.438-102.872 639.178 1.00 21.56 N ANISOU 2515 N GLY A 286 2345 3146 2701 -661 835 -129 N ATOM 2516 CA GLY A 286 -141.277-102.374 639.898 1.00 21.22 C ANISOU 2516 CA GLY A 286 2372 3049 2640 -550 817 -138 C ATOM 2517 C GLY A 286 -141.432-100.918 640.296 1.00 21.39 C ANISOU 2517 C GLY A 286 2274 3103 2751 -467 781 -133 C ATOM 2518 O GLY A 286 -141.056-100.516 641.398 1.00 27.62 O ANISOU 2518 O GLY A 286 3145 3833 3518 -380 786 -156 O ATOM 2519 N MET A 287 -142.000-100.128 639.397 1.00 15.53 N ANISOU 2519 N MET A 287 1343 2448 2109 -490 735 -102 N ATOM 2520 CA MET A 287 -142.248 -98.718 639.658 1.00 19.71 C ANISOU 2520 CA MET A 287 1746 2994 2749 -413 698 -93 C ATOM 2521 C MET A 287 -143.187 -98.496 640.831 1.00 25.14 C ANISOU 2521 C MET A 287 2448 3668 3435 -396 808 -140 C ATOM 2522 O MET A 287 -142.997 -97.561 641.607 1.00 28.14 O ANISOU 2522 O MET A 287 2829 4005 3856 -297 796 -174 O ATOM 2523 CB MET A 287 -142.831 -98.043 638.422 1.00 24.69 C ANISOU 2523 CB MET A 287 2241 3671 3471 -403 584 2 C ATOM 2524 CG MET A 287 -143.165 -96.582 638.640 1.00 29.51 C ANISOU 2524 CG MET A 287 2733 4290 4190 -324 539 31 C ATOM 2525 SD MET A 287 -141.780 -95.491 638.296 1.00 66.66 S ANISOU 2525 SD MET A 287 7392 8987 8949 -251 405 51 S ATOM 2526 CE MET A 287 -141.728 -95.607 636.517 1.00 30.24 C ANISOU 2526 CE MET A 287 2796 4327 4367 -296 328 16 C ATOM 2527 N THR A 288 -144.202 -99.348 640.966 1.00 22.80 N ANISOU 2527 N THR A 288 2194 3388 3082 -466 871 -125 N ATOM 2528 CA THR A 288 -145.171 -99.168 642.042 1.00 22.93 C ANISOU 2528 CA THR A 288 2212 3413 3088 -448 976 -153 C ATOM 2529 C THR A 288 -144.574 -99.477 643.409 1.00 23.21 C ANISOU 2529 C THR A 288 2414 3388 3017 -413 1084 -223 C ATOM 2530 O THR A 288 -145.146 -99.099 644.437 1.00 21.18 O ANISOU 2530 O THR A 288 2171 3139 2739 -365 1172 -261 O ATOM 2531 CB THR A 288 -146.420-100.046 641.850 1.00 24.64 C ANISOU 2531 CB THR A 288 2415 3667 3279 -536 1010 -105 C ATOM 2532 OG1 THR A 288 -146.079-101.427 642.030 1.00 21.75 O ANISOU 2532 OG1 THR A 288 2205 3250 2809 -615 1050 -114 O ATOM 2533 CG2 THR A 288 -147.022 -99.830 640.463 1.00 26.00 C ANISOU 2533 CG2 THR A 288 2451 3891 3538 -565 905 -28 C ATOM 2534 N HIS A 289 -143.422-100.147 643.426 1.00 20.97 N ANISOU 2534 N HIS A 289 2283 3034 2652 -405 1033 -219 N ATOM 2535 CA HIS A 289 -142.815-100.568 644.690 1.00 21.97 C ANISOU 2535 CA HIS A 289 2609 3087 2652 -348 1068 -246 C ATOM 2536 C HIS A 289 -142.375 -99.404 645.584 1.00 23.63 C ANISOU 2536 C HIS A 289 2838 3268 2870 -217 1025 -301 C ATOM 2537 O HIS A 289 -142.280 -99.555 646.803 1.00 26.34 O ANISOU 2537 O HIS A 289 3320 3586 3103 -173 1082 -336 O ATOM 2538 CB HIS A 289 -141.613-101.474 644.444 1.00 20.09 C ANISOU 2538 CB HIS A 289 2514 2775 2343 -348 999 -219 C ATOM 2539 CG HIS A 289 -140.990-101.983 645.706 1.00 26.88 C ANISOU 2539 CG HIS A 289 3575 3565 3072 -294 1024 -226 C ATOM 2540 ND1 HIS A 289 -139.925-101.357 646.313 1.00 25.87 N ANISOU 2540 ND1 HIS A 289 3516 3395 2920 -180 931 -248 N ATOM 2541 CD2 HIS A 289 -141.303-103.045 646.488 1.00 30.93 C ANISOU 2541 CD2 HIS A 289 4232 4047 3471 -345 1126 -206 C ATOM 2542 CE1 HIS A 289 -139.600-102.016 647.414 1.00 29.18 C ANISOU 2542 CE1 HIS A 289 4113 3769 3204 -158 971 -242 C ATOM 2543 NE2 HIS A 289 -140.416-103.044 647.540 1.00 30.87 N ANISOU 2543 NE2 HIS A 289 4378 3988 3363 -254 1092 -211 N ATOM 2544 N CYS A 290 -142.122 -98.240 644.999 1.00 16.76 N ANISOU 2544 N CYS A 290 1835 2403 2129 -158 924 -309 N ATOM 2545 CA CYS A 290 -141.662 -97.109 645.798 1.00 24.93 C ANISOU 2545 CA CYS A 290 2895 3390 3188 -41 867 -371 C ATOM 2546 C CYS A 290 -142.738 -96.542 646.738 1.00 26.96 C ANISOU 2546 C CYS A 290 3129 3677 3439 1 985 -443 C ATOM 2547 O CYS A 290 -142.515 -95.517 647.389 1.00 26.47 O ANISOU 2547 O CYS A 290 3081 3572 3406 101 946 -517 O ATOM 2548 CB CYS A 290 -141.147 -95.998 644.886 1.00 26.01 C ANISOU 2548 CB CYS A 290 2889 3510 3484 1 725 -348 C ATOM 2549 SG CYS A 290 -142.422 -95.225 643.881 1.00 25.31 S ANISOU 2549 SG CYS A 290 2550 3498 3569 -32 752 -315 S ATOM 2550 N CYS A 291 -143.896 -97.198 646.808 1.00 26.92 N ANISOU 2550 N CYS A 291 3085 3744 3398 -75 1130 -425 N ATOM 2551 CA CYS A 291 -144.942 -96.804 647.750 1.00 31.35 C ANISOU 2551 CA CYS A 291 3624 4354 3935 -34 1269 -486 C ATOM 2552 C CYS A 291 -145.273 -97.958 648.697 1.00 30.66 C ANISOU 2552 C CYS A 291 3686 4296 3667 -91 1408 -474 C ATOM 2553 O CYS A 291 -146.074 -97.816 649.616 1.00 31.78 O ANISOU 2553 O CYS A 291 3838 4489 3749 -58 1520 -508 O ATOM 2554 CB CYS A 291 -146.209 -96.341 647.005 1.00 32.04 C ANISOU 2554 CB CYS A 291 3480 4522 4170 -67 1328 -460 C ATOM 2555 SG CYS A 291 -147.281 -97.663 646.336 1.00 29.70 S ANISOU 2555 SG CYS A 291 3133 4307 3843 -225 1362 -337 S ATOM 2556 N ILE A 292 -144.632 -99.099 648.482 1.00 29.67 N ANISOU 2556 N ILE A 292 3681 4133 3459 -167 1376 -412 N ATOM 2557 CA ILE A 292 -144.990-100.308 649.212 1.00 29.23 C ANISOU 2557 CA ILE A 292 3754 4089 3263 -236 1468 -362 C ATOM 2558 C ILE A 292 -144.401-100.382 650.622 1.00 30.08 C ANISOU 2558 C ILE A 292 4057 4171 3202 -158 1491 -399 C ATOM 2559 O ILE A 292 -145.061-100.876 651.538 1.00 28.67 O ANISOU 2559 O ILE A 292 3928 4038 2926 -173 1570 -370 O ATOM 2560 CB ILE A 292 -144.572-101.550 648.416 1.00 26.98 C ANISOU 2560 CB ILE A 292 3526 3755 2971 -342 1421 -282 C ATOM 2561 CG1 ILE A 292 -145.457-101.683 647.179 1.00 24.64 C ANISOU 2561 CG1 ILE A 292 3049 3507 2808 -435 1396 -238 C ATOM 2562 CG2 ILE A 292 -144.708-102.814 649.263 1.00 30.31 C ANISOU 2562 CG2 ILE A 292 4103 4151 3264 -394 1475 -222 C ATOM 2563 CD1 ILE A 292 -146.898-102.025 647.515 1.00 26.86 C ANISOU 2563 CD1 ILE A 292 3252 3857 3094 -490 1474 -196 C ATOM 2564 N ASN A 293 -143.179 -99.884 650.810 1.00 31.06 N ANISOU 2564 N ASN A 293 4276 4228 3298 -71 1383 -447 N ATOM 2565 CA ASN A 293 -142.508-100.018 652.114 1.00 30.91 C ANISOU 2565 CA ASN A 293 4456 4188 3101 -4 1379 -476 C ATOM 2566 C ASN A 293 -143.235 -99.343 653.283 1.00 29.48 C ANISOU 2566 C ASN A 293 4282 4077 2842 67 1465 -554 C ATOM 2567 O ASN A 293 -143.252 -99.884 654.384 1.00 29.47 O ANISOU 2567 O ASN A 293 4403 4109 2685 73 1497 -530 O ATOM 2568 CB ASN A 293 -141.067 -99.493 652.042 1.00 31.48 C ANISOU 2568 CB ASN A 293 4590 4180 3192 79 1188 -502 C ATOM 2569 CG ASN A 293 -140.118-100.476 651.360 1.00 32.63 C ANISOU 2569 CG ASN A 293 4794 4262 3342 33 1098 -408 C ATOM 2570 OD1 ASN A 293 -140.261-101.693 651.487 1.00 31.12 O ANISOU 2570 OD1 ASN A 293 4695 4062 3067 -37 1172 -333 O ATOM 2571 ND2 ASN A 293 -139.150 -99.946 650.622 1.00 31.01 N ANISOU 2571 ND2 ASN A 293 4530 4009 3242 74 941 -408 N ATOM 2572 N PRO A 294 -143.828 -98.162 653.071 1.00 29.92 N ANISOU 2572 N PRO A 294 4196 4158 3012 127 1490 -644 N ATOM 2573 CA PRO A 294 -144.590 -97.692 654.232 1.00 33.09 C ANISOU 2573 CA PRO A 294 4608 4636 3328 198 1571 -708 C ATOM 2574 C PRO A 294 -145.799 -98.582 654.531 1.00 35.23 C ANISOU 2574 C PRO A 294 4825 5008 3551 119 1696 -612 C ATOM 2575 O PRO A 294 -146.125 -98.806 655.697 1.00 37.36 O ANISOU 2575 O PRO A 294 5173 5350 3673 146 1762 -618 O ATOM 2576 CB PRO A 294 -145.021 -96.279 653.817 1.00 32.60 C ANISOU 2576 CB PRO A 294 4394 4563 3431 285 1570 -815 C ATOM 2577 CG PRO A 294 -143.954 -95.836 652.870 1.00 28.43 C ANISOU 2577 CG PRO A 294 3841 3928 3032 291 1409 -821 C ATOM 2578 CD PRO A 294 -143.602 -97.084 652.091 1.00 28.56 C ANISOU 2578 CD PRO A 294 3875 3938 3040 171 1380 -686 C ATOM 2579 N ILE A 295 -146.443 -99.097 653.489 1.00 35.36 N ANISOU 2579 N ILE A 295 4708 5037 3692 17 1719 -524 N ATOM 2580 CA ILE A 295 -147.556-100.019 653.672 1.00 37.50 C ANISOU 2580 CA ILE A 295 4926 5389 3934 -74 1817 -425 C ATOM 2581 C ILE A 295 -147.115-101.237 654.479 1.00 40.65 C ANISOU 2581 C ILE A 295 5504 5773 4170 -128 1829 -350 C ATOM 2582 O ILE A 295 -147.824-101.687 655.376 1.00 47.12 O ANISOU 2582 O ILE A 295 6341 6676 4889 -142 1924 -308 O ATOM 2583 CB ILE A 295 -148.142-100.467 652.328 1.00 36.43 C ANISOU 2583 CB ILE A 295 4638 5248 3954 -188 1798 -344 C ATOM 2584 CG1 ILE A 295 -148.661 -99.249 651.563 1.00 34.14 C ANISOU 2584 CG1 ILE A 295 4155 4986 3831 -133 1782 -398 C ATOM 2585 CG2 ILE A 295 -149.259-101.464 652.550 1.00 41.95 C ANISOU 2585 CG2 ILE A 295 5294 6020 4626 -287 1886 -242 C ATOM 2586 CD1 ILE A 295 -149.061 -99.544 650.137 1.00 35.07 C ANISOU 2586 CD1 ILE A 295 4125 5104 4098 -234 1722 -323 C ATOM 2587 N ILE A 296 -145.927-101.748 654.184 1.00 37.25 N ANISOU 2587 N ILE A 296 5201 5240 3714 -149 1733 -327 N ATOM 2588 CA ILE A 296 -145.388-102.868 654.941 1.00 39.39 C ANISOU 2588 CA ILE A 296 5646 5480 3842 -185 1729 -250 C ATOM 2589 C ILE A 296 -145.260-102.509 656.419 1.00 41.75 C ANISOU 2589 C ILE A 296 6050 5847 3968 -96 1760 -296 C ATOM 2590 O ILE A 296 -145.594-103.315 657.279 1.00 47.53 O ANISOU 2590 O ILE A 296 6850 6629 4582 -134 1827 -221 O ATOM 2591 CB ILE A 296 -144.015-103.322 654.400 1.00 40.49 C ANISOU 2591 CB ILE A 296 5905 5495 3983 -190 1610 -227 C ATOM 2592 CG1 ILE A 296 -144.125-103.685 652.920 1.00 42.37 C ANISOU 2592 CG1 ILE A 296 6041 5679 4378 -277 1579 -192 C ATOM 2593 CG2 ILE A 296 -143.485-104.514 655.191 1.00 37.73 C ANISOU 2593 CG2 ILE A 296 5731 5103 3499 -220 1605 -133 C ATOM 2594 CD1 ILE A 296 -142.875-104.297 652.355 1.00 43.48 C ANISOU 2594 CD1 ILE A 296 6294 5708 4517 -284 1483 -159 C ATOM 2595 N TYR A 297 -144.803-101.298 656.717 1.00 37.31 N ANISOU 2595 N TYR A 297 5497 5290 3389 19 1711 -422 N ATOM 2596 CA TYR A 297 -144.595-100.909 658.107 1.00 39.11 C ANISOU 2596 CA TYR A 297 5833 5585 3443 103 1720 -488 C ATOM 2597 C TYR A 297 -145.925-100.845 658.841 1.00 48.29 C ANISOU 2597 C TYR A 297 6911 6888 4549 108 1868 -489 C ATOM 2598 O TYR A 297 -145.986-101.029 660.058 1.00 52.93 O ANISOU 2598 O TYR A 297 7587 7562 4962 135 1913 -491 O ATOM 2599 CB TYR A 297 -143.879 -99.559 658.213 1.00 35.67 C ANISOU 2599 CB TYR A 297 5420 5112 3022 221 1625 -643 C ATOM 2600 CG TYR A 297 -142.551 -99.476 657.491 1.00 36.24 C ANISOU 2600 CG TYR A 297 5561 5057 3153 229 1474 -644 C ATOM 2601 CD1 TYR A 297 -141.814-100.620 657.199 1.00 39.75 C ANISOU 2601 CD1 TYR A 297 6099 5438 3567 162 1421 -522 C ATOM 2602 CD2 TYR A 297 -142.029 -98.249 657.109 1.00 34.43 C ANISOU 2602 CD2 TYR A 297 5302 4765 3014 312 1384 -767 C ATOM 2603 CE1 TYR A 297 -140.601-100.541 656.537 1.00 38.97 C ANISOU 2603 CE1 TYR A 297 6056 5237 3515 182 1287 -519 C ATOM 2604 CE2 TYR A 297 -140.820 -98.159 656.453 1.00 35.70 C ANISOU 2604 CE2 TYR A 297 5519 4820 3225 323 1245 -761 C ATOM 2605 CZ TYR A 297 -140.109 -99.307 656.165 1.00 38.10 C ANISOU 2605 CZ TYR A 297 5909 5083 3485 261 1199 -635 C ATOM 2606 OH TYR A 297 -138.905 -99.212 655.503 1.00 34.64 O ANISOU 2606 OH TYR A 297 5490 4556 3116 281 1038 -614 O ATOM 2607 N ALA A 298 -146.992-100.593 658.092 1.00 51.39 N ANISOU 2607 N ALA A 298 7125 7315 5084 81 1942 -480 N ATOM 2608 CA ALA A 298 -148.307-100.383 658.687 1.00 53.91 C ANISOU 2608 CA ALA A 298 7336 7776 5370 103 2083 -485 C ATOM 2609 C ALA A 298 -149.003-101.699 659.033 1.00 59.99 C ANISOU 2609 C ALA A 298 8108 8614 6072 -12 2177 -332 C ATOM 2610 O ALA A 298 -149.905-101.731 659.874 1.00 64.73 O ANISOU 2610 O ALA A 298 8664 9353 6578 5 2297 -316 O ATOM 2611 CB ALA A 298 -149.180 -99.553 657.746 1.00 51.60 C ANISOU 2611 CB ALA A 298 6841 7496 5269 127 2115 -524 C ATOM 2612 N PHE A 299 -148.582-102.782 658.390 1.00 60.73 N ANISOU 2612 N PHE A 299 8252 8608 6213 -126 2123 -221 N ATOM 2613 CA PHE A 299 -149.238-104.073 658.575 1.00 66.11 C ANISOU 2613 CA PHE A 299 8932 9322 6863 -247 2200 -72 C ATOM 2614 C PHE A 299 -148.331-105.092 659.249 1.00 71.20 C ANISOU 2614 C PHE A 299 9774 9907 7371 -284 2159 9 C ATOM 2615 O PHE A 299 -148.789-106.144 659.692 1.00 76.08 O ANISOU 2615 O PHE A 299 10420 10556 7932 -370 2228 134 O ATOM 2616 CB PHE A 299 -149.720-104.624 657.232 1.00 65.38 C ANISOU 2616 CB PHE A 299 8724 9163 6957 -365 2180 -2 C ATOM 2617 CG PHE A 299 -150.919-103.911 656.681 1.00 68.41 C ANISOU 2617 CG PHE A 299 8891 9636 7466 -356 2241 -27 C ATOM 2618 CD1 PHE A 299 -151.853-103.339 657.533 1.00 72.94 C ANISOU 2618 CD1 PHE A 299 9380 10362 7972 -286 2359 -50 C ATOM 2619 CD2 PHE A 299 -151.113-103.809 655.314 1.00 68.24 C ANISOU 2619 CD2 PHE A 299 8747 9554 7625 -413 2178 -23 C ATOM 2620 CE1 PHE A 299 -152.963-102.678 657.030 1.00 74.23 C ANISOU 2620 CE1 PHE A 299 9338 10608 8256 -266 2415 -63 C ATOM 2621 CE2 PHE A 299 -152.218-103.149 654.802 1.00 69.95 C ANISOU 2621 CE2 PHE A 299 8759 9857 7961 -402 2221 -31 C ATOM 2622 CZ PHE A 299 -153.144-102.583 655.662 1.00 72.86 C ANISOU 2622 CZ PHE A 299 9044 10369 8272 -326 2341 -47 C ATOM 2623 N VAL A 300 -147.044-104.779 659.327 1.00 72.99 N ANISOU 2623 N VAL A 300 10132 10047 7552 -216 2044 -53 N ATOM 2624 CA VAL A 300 -146.076-105.702 659.907 1.00 76.17 C ANISOU 2624 CA VAL A 300 10720 10384 7837 -237 1987 29 C ATOM 2625 C VAL A 300 -145.486-105.149 661.200 1.00 80.76 C ANISOU 2625 C VAL A 300 11417 11042 8226 -134 1964 -35 C ATOM 2626 O VAL A 300 -145.456-105.839 662.220 1.00 86.73 O ANISOU 2626 O VAL A 300 12271 11857 8827 -154 2003 49 O ATOM 2627 CB VAL A 300 -144.941-106.017 658.909 1.00 74.58 C ANISOU 2627 CB VAL A 300 10588 10014 7734 -253 1856 39 C ATOM 2628 CG1 VAL A 300 -143.818-106.783 659.591 1.00 76.03 C ANISOU 2628 CG1 VAL A 300 10965 10131 7791 -238 1783 113 C ATOM 2629 CG2 VAL A 300 -145.489-106.797 657.720 1.00 73.05 C ANISOU 2629 CG2 VAL A 300 10306 9745 7703 -372 1876 109 C ATOM 2630 N GLY A 301 -145.028-103.903 661.160 1.00 78.47 N ANISOU 2630 N GLY A 301 11115 10754 7946 -30 1897 -185 N ATOM 2631 CA GLY A 301 -144.421-103.280 662.323 1.00 77.50 C ANISOU 2631 CA GLY A 301 11102 10697 7649 64 1854 -273 C ATOM 2632 C GLY A 301 -145.432-102.820 663.355 1.00 78.98 C ANISOU 2632 C GLY A 301 11235 11062 7713 104 1984 -331 C ATOM 2633 O GLY A 301 -146.387-102.112 663.033 1.00 79.04 O ANISOU 2633 O GLY A 301 11094 11128 7808 134 2065 -405 O ATOM 2634 N GLU A 302 -145.230-103.229 664.602 1.00 80.68 N ANISOU 2634 N GLU A 302 11565 11371 7720 108 2005 -292 N ATOM 2635 CA GLU A 302 -146.071-102.756 665.694 1.00 81.18 C ANISOU 2635 CA GLU A 302 11591 11621 7631 154 2125 -362 C ATOM 2636 C GLU A 302 -145.666-101.344 666.084 1.00 79.01 C ANISOU 2636 C GLU A 302 11336 11368 7316 271 2063 -579 C ATOM 2637 O GLU A 302 -146.497-100.548 666.527 1.00 78.08 O ANISOU 2637 O GLU A 302 11134 11371 7164 333 2160 -699 O ATOM 2638 CB GLU A 302 -145.972-103.693 666.900 1.00 81.37 C ANISOU 2638 CB GLU A 302 11732 11750 7434 109 2168 -240 C ATOM 2639 N GLU A 303 -144.380-101.047 665.911 1.00 81.69 N ANISOU 2639 N GLU A 303 11787 11585 7668 301 1897 -629 N ATOM 2640 CA GLU A 303 -143.820 -99.754 666.287 1.00 86.78 C ANISOU 2640 CA GLU A 303 12471 12219 8282 396 1808 -832 C ATOM 2641 C GLU A 303 -144.478 -98.637 665.464 1.00 85.34 C ANISOU 2641 C GLU A 303 12135 12000 8292 457 1840 -970 C ATOM 2642 O GLU A 303 -144.864 -97.605 666.007 1.00 87.34 O ANISOU 2642 O GLU A 303 12357 12318 8510 534 1879 -1143 O ATOM 2643 CB GLU A 303 -142.280 -99.763 666.122 1.00 91.97 C ANISOU 2643 CB GLU A 303 13265 12742 8938 402 1609 -825 C ATOM 2644 CG GLU A 303 -141.712 -99.290 664.771 1.00 97.51 C ANISOU 2644 CG GLU A 303 13912 13274 9864 416 1497 -855 C ATOM 2645 CD GLU A 303 -141.201-100.429 663.887 1.00 97.97 C ANISOU 2645 CD GLU A 303 13991 13225 10007 343 1449 -673 C ATOM 2646 OE1 GLU A 303 -141.975-101.380 663.645 1.00101.68 O ANISOU 2646 OE1 GLU A 303 14409 13723 10501 270 1564 -544 O ATOM 2647 OE2 GLU A 303 -140.047-100.355 663.404 1.00 96.10 O ANISOU 2647 OE2 GLU A 303 13818 12873 9823 357 1297 -665 O ATOM 2648 N PHE A 304 -144.663 -98.876 664.168 1.00 77.89 N ANISOU 2648 N PHE A 304 11090 10955 7549 419 1834 -891 N ATOM 2649 CA PHE A 304 -145.178 -97.865 663.244 1.00 70.21 C ANISOU 2649 CA PHE A 304 9970 9930 6777 476 1844 -994 C ATOM 2650 C PHE A 304 -146.664 -97.592 663.459 1.00 64.04 C ANISOU 2650 C PHE A 304 9040 9284 6007 508 2017 -1020 C ATOM 2651 O PHE A 304 -147.086 -96.437 663.578 1.00 60.88 O ANISOU 2651 O PHE A 304 8568 8906 5656 610 2041 -1180 O ATOM 2652 CB PHE A 304 -144.931 -98.315 661.799 1.00 68.16 C ANISOU 2652 CB PHE A 304 9648 9539 6711 409 1790 -884 C ATOM 2653 CG PHE A 304 -145.180 -97.251 660.769 1.00 69.28 C ANISOU 2653 CG PHE A 304 9655 9606 7062 466 1765 -978 C ATOM 2654 CD1 PHE A 304 -144.293 -96.197 660.618 1.00 68.75 C ANISOU 2654 CD1 PHE A 304 9631 9437 7054 542 1633 -1115 C ATOM 2655 CD2 PHE A 304 -146.282 -97.321 659.927 1.00 71.50 C ANISOU 2655 CD2 PHE A 304 9763 9913 7492 434 1866 -917 C ATOM 2656 CE1 PHE A 304 -144.509 -95.221 659.657 1.00 69.74 C ANISOU 2656 CE1 PHE A 304 9631 9483 7385 595 1608 -1187 C ATOM 2657 CE2 PHE A 304 -146.505 -96.345 658.958 1.00 71.26 C ANISOU 2657 CE2 PHE A 304 9601 9812 7662 486 1840 -985 C ATOM 2658 CZ PHE A 304 -145.619 -95.294 658.825 1.00 70.58 C ANISOU 2658 CZ PHE A 304 9563 9620 7636 571 1715 -1118 C ATOM 2659 N ARG A 305 -147.445 -98.668 663.506 1.00 62.16 N ANISOU 2659 N ARG A 305 8754 9131 5731 422 2132 -859 N ATOM 2660 CA ARG A 305 -148.892 -98.586 663.668 1.00 65.81 C ANISOU 2660 CA ARG A 305 9064 9736 6205 437 2299 -844 C ATOM 2661 C ARG A 305 -149.276 -97.864 664.959 1.00 67.51 C ANISOU 2661 C ARG A 305 9300 10104 6248 535 2378 -992 C ATOM 2662 O ARG A 305 -150.286 -97.162 665.005 1.00 67.00 O ANISOU 2662 O ARG A 305 9098 10128 6229 613 2483 -1071 O ATOM 2663 CB ARG A 305 -149.497 -99.994 663.633 1.00 71.19 C ANISOU 2663 CB ARG A 305 9718 10476 6855 306 2390 -634 C ATOM 2664 CG ARG A 305 -150.922-100.058 663.099 1.00 73.96 C ANISOU 2664 CG ARG A 305 9866 10909 7328 279 2522 -566 C ATOM 2665 CD ARG A 305 -151.346-101.490 662.783 1.00 74.01 C ANISOU 2665 CD ARG A 305 9848 10916 7355 123 2569 -355 C ATOM 2666 NE ARG A 305 -150.555-102.486 663.503 1.00 76.22 N ANISOU 2666 NE ARG A 305 10307 11179 7474 60 2532 -265 N ATOM 2667 CZ ARG A 305 -150.923-103.044 664.653 1.00 80.91 C ANISOU 2667 CZ ARG A 305 10946 11918 7877 39 2629 -196 C ATOM 2668 NH1 ARG A 305 -152.068-102.699 665.226 1.00 86.06 N ANISOU 2668 NH1 ARG A 305 11476 12755 8468 77 2776 -216 N ATOM 2669 NH2 ARG A 305 -150.141-103.943 665.236 1.00 79.81 N ANISOU 2669 NH2 ARG A 305 10971 11747 7607 -17 2581 -101 N ATOM 2670 N ASN A 306 -148.464 -98.031 666.002 1.00 68.68 N ANISOU 2670 N ASN A 306 9615 10285 6196 531 2327 -1033 N ATOM 2671 CA ASN A 306 -148.711 -97.354 667.275 1.00 67.40 C ANISOU 2671 CA ASN A 306 9491 10266 5852 603 2395 -1196 C ATOM 2672 C ASN A 306 -148.341 -95.881 667.208 1.00 60.52 C ANISOU 2672 C ASN A 306 8621 9307 5067 712 2316 -1439 C ATOM 2673 O ASN A 306 -149.102 -95.022 667.654 1.00 54.26 O ANISOU 2673 O ASN A 306 7756 8578 4284 789 2404 -1582 O ATOM 2674 CB ASN A 306 -147.936 -98.025 668.413 1.00 72.30 C ANISOU 2674 CB ASN A 306 10296 10949 6226 548 2358 -1151 C ATOM 2675 CG ASN A 306 -148.510 -99.376 668.801 1.00 75.78 C ANISOU 2675 CG ASN A 306 10729 11513 6549 451 2471 -933 C ATOM 2676 OD1 ASN A 306 -149.665 -99.683 668.503 1.00 78.91 O ANISOU 2676 OD1 ASN A 306 10977 11995 7010 429 2607 -849 O ATOM 2677 ND2 ASN A 306 -147.708-100.184 669.484 1.00 74.74 N ANISOU 2677 ND2 ASN A 306 10756 11391 6250 392 2411 -832 N ATOM 2678 N TYR A 307 -147.167 -95.599 666.648 1.00 62.38 N ANISOU 2678 N TYR A 307 8943 9363 5394 707 2141 -1469 N ATOM 2679 CA TYR A 307 -146.701 -94.226 666.490 1.00 69.69 C ANISOU 2679 CA TYR A 307 9878 10168 6434 788 2048 -1685 C ATOM 2680 C TYR A 307 -147.599 -93.456 665.533 1.00 68.70 C ANISOU 2680 C TYR A 307 9565 9991 6547 869 2093 -1723 C ATOM 2681 O TYR A 307 -147.762 -92.240 665.651 1.00 68.41 O ANISOU 2681 O TYR A 307 9495 9887 6609 951 2082 -1903 O ATOM 2682 CB TYR A 307 -145.252 -94.204 666.003 1.00 73.56 C ANISOU 2682 CB TYR A 307 10489 10478 6982 754 1847 -1666 C ATOM 2683 CG TYR A 307 -144.261 -94.473 667.113 1.00 80.90 C ANISOU 2683 CG TYR A 307 11616 11433 7690 719 1763 -1682 C ATOM 2684 CD1 TYR A 307 -144.437 -93.910 668.371 1.00 86.50 C ANISOU 2684 CD1 TYR A 307 12402 12237 8228 747 1822 -1840 C ATOM 2685 CD2 TYR A 307 -143.156 -95.289 666.909 1.00 81.89 C ANISOU 2685 CD2 TYR A 307 11852 11489 7774 660 1628 -1537 C ATOM 2686 CE1 TYR A 307 -143.543 -94.151 669.397 1.00 90.84 C ANISOU 2686 CE1 TYR A 307 13132 12823 8561 718 1737 -1845 C ATOM 2687 CE2 TYR A 307 -142.256 -95.540 667.933 1.00 85.41 C ANISOU 2687 CE2 TYR A 307 12469 11970 8014 640 1539 -1536 C ATOM 2688 CZ TYR A 307 -142.452 -94.965 669.172 1.00 91.14 C ANISOU 2688 CZ TYR A 307 13265 12801 8563 668 1589 -1688 C ATOM 2689 OH TYR A 307 -141.560 -95.207 670.194 1.00 95.89 O ANISOU 2689 OH TYR A 307 14034 13450 8949 647 1493 -1681 O ATOM 2690 N LEU A 308 -148.186 -94.184 664.592 1.00 66.03 N ANISOU 2690 N LEU A 308 9110 9672 6305 836 2147 -1544 N ATOM 2691 CA LEU A 308 -149.178 -93.624 663.687 1.00 63.47 C ANISOU 2691 CA LEU A 308 8603 9326 6186 908 2209 -1529 C ATOM 2692 C LEU A 308 -150.434 -93.225 664.468 1.00 64.98 C ANISOU 2692 C LEU A 308 8702 9671 6318 986 2367 -1592 C ATOM 2693 O LEU A 308 -151.046 -92.194 664.197 1.00 64.58 O ANISOU 2693 O LEU A 308 8549 9585 6403 1110 2390 -1681 O ATOM 2694 CB LEU A 308 -149.516 -94.638 662.591 1.00 60.23 C ANISOU 2694 CB LEU A 308 8103 8894 5888 797 2240 -1308 C ATOM 2695 CG LEU A 308 -149.799 -94.157 661.168 1.00 58.07 C ANISOU 2695 CG LEU A 308 7684 8501 5878 809 2208 -1267 C ATOM 2696 CD1 LEU A 308 -148.592 -93.459 660.563 1.00 55.66 C ANISOU 2696 CD1 LEU A 308 7452 8012 5684 841 2034 -1352 C ATOM 2697 CD2 LEU A 308 -150.203 -95.339 660.311 1.00 56.74 C ANISOU 2697 CD2 LEU A 308 7431 8343 5783 655 2249 -1062 C ATOM 2698 N LEU A 309 -150.810 -94.044 665.447 1.00 65.06 N ANISOU 2698 N LEU A 309 8749 9849 6122 921 2477 -1535 N ATOM 2699 CA LEU A 309 -151.969 -93.750 666.278 1.00 65.71 C ANISOU 2699 CA LEU A 309 8744 10099 6124 979 2638 -1596 C ATOM 2700 C LEU A 309 -151.717 -92.523 667.146 1.00 68.24 C ANISOU 2700 C LEU A 309 9131 10392 6404 1065 2618 -1863 C ATOM 2701 O LEU A 309 -152.625 -91.725 667.378 1.00 70.83 O ANISOU 2701 O LEU A 309 9350 10775 6787 1159 2715 -1978 O ATOM 2702 CB LEU A 309 -152.331 -94.951 667.155 1.00 68.42 C ANISOU 2702 CB LEU A 309 9124 10624 6247 870 2755 -1464 C ATOM 2703 CG LEU A 309 -153.703 -95.589 666.912 1.00 70.57 C ANISOU 2703 CG LEU A 309 9220 11039 6556 833 2916 -1298 C ATOM 2704 CD1 LEU A 309 -154.018 -96.630 667.976 1.00 72.29 C ANISOU 2704 CD1 LEU A 309 9487 11437 6543 732 3029 -1192 C ATOM 2705 CD2 LEU A 309 -154.793 -94.526 666.866 1.00 73.91 C ANISOU 2705 CD2 LEU A 309 9476 11517 7088 961 3012 -1416 C ATOM 2706 N VAL A 310 -150.486 -92.376 667.629 1.00 65.42 N ANISOU 2706 N VAL A 310 8958 9938 5961 1014 2502 -1963 N ATOM 2707 CA VAL A 310 -150.121 -91.202 668.417 1.00 64.97 C ANISOU 2707 CA VAL A 310 9006 9786 5894 1041 2499 -2220 C ATOM 2708 C VAL A 310 -150.073 -89.976 667.517 1.00 66.98 C ANISOU 2708 C VAL A 310 9182 9833 6433 1116 2426 -2340 C ATOM 2709 O VAL A 310 -150.339 -88.857 667.958 1.00 69.69 O ANISOU 2709 O VAL A 310 9574 10043 6862 1142 2523 -2527 O ATOM 2710 CB VAL A 310 -148.762 -91.374 669.120 1.00 61.15 C ANISOU 2710 CB VAL A 310 8762 9234 5239 968 2385 -2261 C ATOM 2711 N PHE A 311 -149.735 -90.203 666.250 1.00 68.20 N ANISOU 2711 N PHE A 311 9257 9916 6741 1145 2288 -2204 N ATOM 2712 CA PHE A 311 -149.688 -89.141 665.249 1.00 70.57 C ANISOU 2712 CA PHE A 311 9463 10047 7302 1247 2184 -2264 C ATOM 2713 C PHE A 311 -151.067 -88.503 665.077 1.00 71.91 C ANISOU 2713 C PHE A 311 9502 10305 7516 1500 2267 -2224 C ATOM 2714 O PHE A 311 -151.192 -87.279 664.979 1.00 72.51 O ANISOU 2714 O PHE A 311 9862 10046 7641 1793 2328 -2115 O ATOM 2715 CB PHE A 311 -149.170 -89.699 663.917 1.00 69.37 C ANISOU 2715 CB PHE A 311 9304 9810 7244 1268 2053 -2046 C ATOM 2716 CG PHE A 311 -149.050 -88.674 662.823 1.00 68.22 C ANISOU 2716 CG PHE A 311 9190 9420 7310 1440 1967 -1984 C ATOM 2717 CD1 PHE A 311 -147.975 -87.798 662.788 1.00 68.36 C ANISOU 2717 CD1 PHE A 311 9531 9025 7416 1419 1958 -1983 C ATOM 2718 CD2 PHE A 311 -149.997 -88.605 661.812 1.00 66.56 C ANISOU 2718 CD2 PHE A 311 8818 9186 7287 1454 2083 -1865 C ATOM 2719 CE1 PHE A 311 -147.857 -86.860 661.775 1.00 66.65 C ANISOU 2719 CE1 PHE A 311 9196 8661 7467 1444 1885 -2038 C ATOM 2720 CE2 PHE A 311 -149.884 -87.672 660.795 1.00 64.33 C ANISOU 2720 CE2 PHE A 311 8483 8697 7261 1496 2040 -1869 C ATOM 2721 CZ PHE A 311 -148.813 -86.798 660.777 1.00 64.47 C ANISOU 2721 CZ PHE A 311 8661 8475 7358 1509 1918 -1966 C ATOM 2722 N PHE A 312 -152.100 -89.341 665.061 1.00 70.91 N ANISOU 2722 N PHE A 312 9274 10345 7324 1475 2431 -2066 N ATOM 2723 CA PHE A 312 -153.471 -88.862 664.927 1.00 69.65 C ANISOU 2723 CA PHE A 312 8980 10248 7236 1625 2582 -2019 C ATOM 2724 C PHE A 312 -154.000 -88.309 666.244 1.00 73.51 C ANISOU 2724 C PHE A 312 9445 10892 7594 1677 2671 -2247 C ATOM 2725 O PHE A 312 -154.815 -87.388 666.249 1.00 77.63 O ANISOU 2725 O PHE A 312 9953 11374 8168 1916 2746 -2243 O ATOM 2726 CB PHE A 312 -154.387 -89.977 664.419 1.00 68.00 C ANISOU 2726 CB PHE A 312 8604 10186 7047 1499 2717 -1813 C ATOM 2727 CG PHE A 312 -154.045 -90.456 663.039 1.00 64.95 C ANISOU 2727 CG PHE A 312 8164 9677 6838 1394 2646 -1650 C ATOM 2728 CD1 PHE A 312 -154.018 -89.571 661.974 1.00 62.61 C ANISOU 2728 CD1 PHE A 312 7797 9206 6785 1468 2586 -1652 C ATOM 2729 CD2 PHE A 312 -153.757 -91.791 662.804 1.00 66.61 C ANISOU 2729 CD2 PHE A 312 8387 9946 6976 1212 2643 -1499 C ATOM 2730 CE1 PHE A 312 -153.701 -90.006 660.698 1.00 62.60 C ANISOU 2730 CE1 PHE A 312 7714 9124 6946 1350 2517 -1529 C ATOM 2731 CE2 PHE A 312 -153.438 -92.236 661.527 1.00 65.65 C ANISOU 2731 CE2 PHE A 312 8207 9723 7013 1109 2575 -1371 C ATOM 2732 CZ PHE A 312 -153.410 -91.340 660.473 1.00 62.89 C ANISOU 2732 CZ PHE A 312 7766 9231 6899 1174 2511 -1394 C ATOM 2733 N GLN A 313 -153.544 -88.870 667.359 1.00 72.86 N ANISOU 2733 N GLN A 313 9444 10875 7364 1414 2751 -2401 N ATOM 2734 CA GLN A 313 -153.934 -88.355 668.669 1.00 76.44 C ANISOU 2734 CA GLN A 313 10008 11271 7763 1299 2997 -2624 C ATOM 2735 C GLN A 313 -153.369 -86.956 668.862 1.00 80.70 C ANISOU 2735 C GLN A 313 10832 11356 8473 1317 3094 -2767 C ATOM 2736 O GLN A 313 -153.994 -86.101 669.494 1.00 86.41 O ANISOU 2736 O GLN A 313 11660 11965 9207 1430 3288 -2858 O ATOM 2737 CB GLN A 313 -153.455 -89.279 669.789 1.00 72.83 C ANISOU 2737 CB GLN A 313 9737 10942 6995 1195 3040 -2581 C ATOM 2738 CG GLN A 313 -154.192 -90.601 669.854 1.00 70.55 C ANISOU 2738 CG GLN A 313 9318 10944 6544 1162 3101 -2363 C ATOM 2739 CD GLN A 313 -153.393 -91.671 670.565 1.00 68.96 C ANISOU 2739 CD GLN A 313 9295 10822 6085 1049 3064 -2254 C ATOM 2740 OE1 GLN A 313 -152.423 -91.372 671.257 1.00 73.37 O ANISOU 2740 OE1 GLN A 313 10064 11284 6530 1018 3005 -2371 O ATOM 2741 NE2 GLN A 313 -153.791 -92.927 670.392 1.00 64.72 N ANISOU 2741 NE2 GLN A 313 8686 10447 5460 989 3097 -2013 N ATOM 2742 N LYS A 314 -152.182 -86.730 668.305 1.00 79.91 N ANISOU 2742 N LYS A 314 10880 11041 8444 1309 2918 -2727 N ATOM 2743 CA LYS A 314 -151.536 -85.427 668.375 1.00 81.95 C ANISOU 2743 CA LYS A 314 11381 10990 8767 1463 2871 -2806 C ATOM 2744 C LYS A 314 -152.246 -84.430 667.466 1.00 86.75 C ANISOU 2744 C LYS A 314 11956 11396 9609 1699 2921 -2703 C ATOM 2745 O LYS A 314 -152.086 -83.222 667.622 1.00 92.70 O ANISOU 2745 O LYS A 314 12785 12007 10430 1841 2877 -2850 O ATOM 2746 CB LYS A 314 -150.055 -85.531 668.001 1.00 79.98 C ANISOU 2746 CB LYS A 314 11238 10648 8502 1398 2615 -2798 C ATOM 2747 N HIS A 315 -153.034 -84.934 666.521 1.00 81.11 N ANISOU 2747 N HIS A 315 11115 10738 8964 1814 2952 -2431 N ATOM 2748 CA HIS A 315 -153.866 -84.063 665.696 1.00 80.16 C ANISOU 2748 CA HIS A 315 10820 10635 9002 2088 2910 -2374 C ATOM 2749 C HIS A 315 -155.093 -83.584 666.485 1.00 83.06 C ANISOU 2749 C HIS A 315 11157 11052 9351 2199 3162 -2442 C ATOM 2750 O HIS A 315 -155.657 -82.531 666.188 1.00 86.94 O ANISOU 2750 O HIS A 315 11548 11486 9999 2371 3176 -2510 O ATOM 2751 CB HIS A 315 -154.293 -84.777 664.410 1.00 76.79 C ANISOU 2751 CB HIS A 315 10091 10441 8646 2127 2763 -2187 C ATOM 2752 N ILE A 316 -155.499 -84.353 667.494 1.00 80.42 N ANISOU 2752 N ILE A 316 10877 10799 8880 2019 3391 -2471 N ATOM 2753 CA ILE A 316 -156.590 -83.945 668.379 1.00 80.22 C ANISOU 2753 CA ILE A 316 10781 10830 8869 2017 3659 -2631 C ATOM 2754 C ILE A 316 -156.046 -83.350 669.673 1.00 79.60 C ANISOU 2754 C ILE A 316 10848 10749 8646 1954 3678 -2964 C ATOM 2755 O ILE A 316 -155.845 -82.138 669.778 1.00 80.49 O ANISOU 2755 O ILE A 316 11067 10695 8820 2134 3637 -3090 O ATOM 2756 CB ILE A 316 -157.519 -85.121 668.724 1.00 71.06 C ANISOU 2756 CB ILE A 316 9337 9962 7701 1708 3823 -2697 C TER 2757 ILE A 316 HETATM 2758 N PCA B 0 -132.580-101.655 629.507 1.00 35.11 N ANISOU 2758 N PCA B 0 3587 6102 3651 -183 -19 -453 N HETATM 2759 CA PCA B 0 -131.733-101.259 630.630 1.00 31.53 C ANISOU 2759 CA PCA B 0 3131 5659 3190 -129 -65 -477 C HETATM 2760 CB PCA B 0 -130.411-102.011 630.591 1.00 31.51 C ANISOU 2760 CB PCA B 0 3131 5721 3119 13 -111 -478 C HETATM 2761 CG PCA B 0 -130.291-102.606 629.195 1.00 33.50 C ANISOU 2761 CG PCA B 0 3356 6008 3366 22 -82 -445 C HETATM 2762 CD PCA B 0 -131.690-102.453 628.654 1.00 38.36 C ANISOU 2762 CD PCA B 0 3980 6576 4018 -99 -29 -429 C HETATM 2763 OE PCA B 0 -132.035-102.980 627.591 1.00 44.00 O ANISOU 2763 OE PCA B 0 4681 7313 4725 -121 4 -414 O HETATM 2764 C PCA B 0 -131.466 -99.769 630.523 1.00 33.38 C ANISOU 2764 C PCA B 0 3320 5837 3527 -187 -61 -456 C HETATM 2765 O PCA B 0 -130.473 -99.336 629.932 1.00 39.49 O ANISOU 2765 O PCA B 0 4057 6625 4323 -167 -72 -435 O ATOM 2766 N GLY B 1 -132.372 -98.984 631.091 1.00 26.51 N ANISOU 2766 N GLY B 1 2465 4879 2728 -264 -46 -468 N ATOM 2767 CA GLY B 1 -132.345 -97.542 630.960 1.00 20.97 C ANISOU 2767 CA GLY B 1 1741 4077 2150 -314 -46 -439 C ATOM 2768 C GLY B 1 -133.592 -96.945 631.583 1.00 20.21 C ANISOU 2768 C GLY B 1 1668 3880 2133 -376 -25 -461 C ATOM 2769 O GLY B 1 -134.249 -97.589 632.394 1.00 25.61 O ANISOU 2769 O GLY B 1 2383 4585 2761 -398 -5 -524 O ATOM 2770 N PRO B 2 -133.935 -95.710 631.202 1.00 17.64 N ANISOU 2770 N PRO B 2 1317 3448 1936 -408 -21 -418 N ATOM 2771 CA PRO B 2 -135.071 -95.046 631.846 1.00 18.29 C ANISOU 2771 CA PRO B 2 1408 3434 2108 -450 -1 -447 C ATOM 2772 C PRO B 2 -136.368 -95.775 631.497 1.00 19.22 C ANISOU 2772 C PRO B 2 1561 3542 2202 -453 16 -464 C ATOM 2773 O PRO B 2 -136.380 -96.594 630.586 1.00 13.68 O ANISOU 2773 O PRO B 2 870 2897 1432 -427 12 -437 O ATOM 2774 CB PRO B 2 -135.029 -93.636 631.251 1.00 16.79 C ANISOU 2774 CB PRO B 2 1159 3164 2057 -466 -1 -385 C ATOM 2775 CG PRO B 2 -134.441 -93.841 629.893 1.00 14.69 C ANISOU 2775 CG PRO B 2 872 2951 1761 -439 -14 -312 C ATOM 2776 CD PRO B 2 -133.447 -94.963 630.028 1.00 17.24 C ANISOU 2776 CD PRO B 2 1223 3377 1950 -406 -26 -342 C ATOM 2777 N PRO B 3 -137.444 -95.508 632.234 1.00 19.02 N ANISOU 2777 N PRO B 3 1550 3452 2225 -490 43 -527 N ATOM 2778 CA PRO B 3 -138.682 -96.249 631.963 1.00 19.95 C ANISOU 2778 CA PRO B 3 1694 3574 2312 -505 75 -582 C ATOM 2779 C PRO B 3 -139.299 -96.010 630.575 1.00 22.82 C ANISOU 2779 C PRO B 3 2011 3938 2722 -465 47 -524 C ATOM 2780 O PRO B 3 -138.977 -95.033 629.878 1.00 21.57 O ANISOU 2780 O PRO B 3 1794 3757 2644 -433 8 -435 O ATOM 2781 CB PRO B 3 -139.630 -95.763 633.061 1.00 19.59 C ANISOU 2781 CB PRO B 3 1662 3455 2325 -552 115 -671 C ATOM 2782 CG PRO B 3 -138.964 -94.606 633.701 1.00 20.27 C ANISOU 2782 CG PRO B 3 1720 3490 2492 -553 94 -639 C ATOM 2783 CD PRO B 3 -137.510 -94.739 633.485 1.00 17.73 C ANISOU 2783 CD PRO B 3 1386 3232 2117 -528 62 -582 C ATOM 2784 N LEU B 4 -140.173 -96.942 630.190 1.00 22.72 N ANISOU 2784 N LEU B 4 2018 3969 2646 -477 76 -591 N ATOM 2785 CA LEU B 4 -140.945 -96.880 628.948 1.00 23.82 C ANISOU 2785 CA LEU B 4 2105 4144 2800 -439 52 -574 C ATOM 2786 C LEU B 4 -140.104 -97.100 627.693 1.00 26.94 C ANISOU 2786 C LEU B 4 2486 4608 3144 -394 15 -472 C ATOM 2787 O LEU B 4 -140.515 -96.726 626.596 1.00 29.41 O ANISOU 2787 O LEU B 4 2740 4961 3472 -353 -20 -429 O ATOM 2788 CB LEU B 4 -141.687 -95.547 628.840 1.00 21.74 C ANISOU 2788 CB LEU B 4 1762 3832 2668 -411 15 -553 C ATOM 2789 CG LEU B 4 -142.540 -95.177 630.052 1.00 23.77 C ANISOU 2789 CG LEU B 4 2026 4019 2985 -452 53 -658 C ATOM 2790 CD1 LEU B 4 -143.311 -93.889 629.792 1.00 26.42 C ANISOU 2790 CD1 LEU B 4 2259 4329 3449 -412 10 -645 C ATOM 2791 CD2 LEU B 4 -143.478 -96.325 630.399 1.00 21.04 C ANISOU 2791 CD2 LEU B 4 1730 3708 2554 -501 125 -811 C ATOM 2792 N MET B 5 -138.941 -97.725 627.834 1.00 27.26 N ANISOU 2792 N MET B 5 2569 4679 3109 -398 24 -443 N ATOM 2793 CA MET B 5 -138.172 -98.078 626.648 1.00 21.56 C ANISOU 2793 CA MET B 5 1839 4029 2324 -362 3 -369 C ATOM 2794 C MET B 5 -138.872 -99.196 625.898 1.00 18.89 C ANISOU 2794 C MET B 5 1511 3770 1895 -370 30 -431 C ATOM 2795 O MET B 5 -138.674 -99.361 624.706 1.00 20.55 O ANISOU 2795 O MET B 5 1700 4047 2060 -341 14 -382 O ATOM 2796 CB MET B 5 -136.746 -98.479 627.014 1.00 23.48 C ANISOU 2796 CB MET B 5 2109 4303 2510 -355 4 -344 C ATOM 2797 CG MET B 5 -135.797 -97.280 627.102 1.00 29.78 C ANISOU 2797 CG MET B 5 2871 5057 3385 -346 -24 -274 C ATOM 2798 SD MET B 5 -134.166 -97.671 627.763 1.00 38.72 S ANISOU 2798 SD MET B 5 4012 6245 4454 -330 -27 -289 S ATOM 2799 CE MET B 5 -133.636 -98.962 626.652 1.00 26.04 C ANISOU 2799 CE MET B 5 2417 4749 2727 -291 -20 -275 C ATOM 2800 N ALA B 6 -139.723 -99.944 626.588 1.00 20.98 N ANISOU 2800 N ALA B 6 1807 4034 2131 -423 82 -557 N ATOM 2801 CA ALA B 6 -140.478-101.019 625.941 1.00 27.05 C ANISOU 2801 CA ALA B 6 2583 4876 2819 -457 122 -658 C ATOM 2802 C ALA B 6 -141.401-100.490 624.850 1.00 23.90 C ANISOU 2802 C ALA B 6 2114 4522 2445 -415 91 -653 C ATOM 2803 O ALA B 6 -141.798-101.222 623.947 1.00 24.27 O ANISOU 2803 O ALA B 6 2147 4660 2416 -423 107 -712 O ATOM 2804 CB ALA B 6 -141.289-101.796 626.971 1.00 30.53 C ANISOU 2804 CB ALA B 6 3076 5287 3237 -558 197 -826 C ATOM 2805 N LEU B 7 -141.734 -99.210 624.923 1.00 23.71 N ANISOU 2805 N LEU B 7 2036 4448 2523 -371 42 -593 N ATOM 2806 CA LEU B 7 -142.733 -98.640 624.016 1.00 23.45 C ANISOU 2806 CA LEU B 7 1916 4480 2513 -320 0 -604 C ATOM 2807 C LEU B 7 -142.113 -98.239 622.684 1.00 24.28 C ANISOU 2807 C LEU B 7 1980 4663 2582 -257 -56 -473 C ATOM 2808 O LEU B 7 -142.814 -97.805 621.767 1.00 27.86 O ANISOU 2808 O LEU B 7 2356 5206 3024 -198 -102 -467 O ATOM 2809 CB LEU B 7 -143.415 -97.433 624.674 1.00 22.01 C ANISOU 2809 CB LEU B 7 1680 4226 2457 -296 -35 -609 C ATOM 2810 CG LEU B 7 -144.624 -97.680 625.591 1.00 24.45 C ANISOU 2810 CG LEU B 7 1989 4510 2792 -344 18 -780 C ATOM 2811 CD1 LEU B 7 -144.554 -99.012 626.322 1.00 24.52 C ANISOU 2811 CD1 LEU B 7 2094 4506 2715 -440 118 -900 C ATOM 2812 CD2 LEU B 7 -144.780 -96.550 626.593 1.00 20.70 C ANISOU 2812 CD2 LEU B 7 1493 3929 2443 -341 0 -763 C ATOM 2813 N GLN B 8 -140.799 -98.413 622.579 1.00 18.28 N ANISOU 2813 N GLN B 8 1269 3887 1790 -267 -49 -380 N ATOM 2814 CA GLN B 8 -140.036 -97.947 621.422 1.00 19.89 C ANISOU 2814 CA GLN B 8 1441 4161 1954 -227 -85 -255 C ATOM 2815 C GLN B 8 -139.873 -99.006 620.344 1.00 19.04 C ANISOU 2815 C GLN B 8 1344 4172 1717 -230 -59 -276 C ATOM 2816 O GLN B 8 -139.840-100.203 620.634 1.00 19.97 O ANISOU 2816 O GLN B 8 1512 4297 1778 -274 -9 -370 O ATOM 2817 CB GLN B 8 -138.657 -97.460 621.868 1.00 17.52 C ANISOU 2817 CB GLN B 8 1173 3794 1692 -245 -83 -164 C ATOM 2818 CG GLN B 8 -138.710 -96.224 622.721 1.00 20.69 C ANISOU 2818 CG GLN B 8 1542 4099 2221 -246 -105 -135 C ATOM 2819 CD GLN B 8 -137.338 -95.720 623.070 1.00 30.60 C ANISOU 2819 CD GLN B 8 2810 5312 3505 -276 -92 -71 C ATOM 2820 OE1 GLN B 8 -136.706 -96.198 624.016 1.00 33.01 O ANISOU 2820 OE1 GLN B 8 3172 5561 3811 -302 -68 -118 O ATOM 2821 NE2 GLN B 8 -136.850 -94.761 622.291 1.00 31.74 N ANISOU 2821 NE2 GLN B 8 2891 5511 3659 -272 -106 35 N ATOM 2822 N SER B 9 -139.750 -98.548 619.102 1.00 18.72 N ANISOU 2822 N SER B 9 1250 4240 1624 -187 -92 -190 N ATOM 2823 CA SER B 9 -139.708 -99.437 617.947 1.00 21.53 C ANISOU 2823 CA SER B 9 1597 4731 1854 -190 -66 -216 C ATOM 2824 C SER B 9 -138.297 -99.883 617.603 1.00 19.51 C ANISOU 2824 C SER B 9 1384 4490 1540 -221 -36 -153 C ATOM 2825 O SER B 9 -137.332 -99.185 617.894 1.00 20.29 O ANISOU 2825 O SER B 9 1494 4533 1683 -227 -49 -60 O ATOM 2826 CB SER B 9 -140.340 -98.751 616.740 1.00 26.30 C ANISOU 2826 CB SER B 9 2112 5473 2409 -118 -117 -160 C ATOM 2827 OG SER B 9 -141.676 -98.383 617.036 1.00 32.46 O ANISOU 2827 OG SER B 9 2841 6254 3239 -70 -157 -242 O ATOM 2828 N CYS B 10 -138.199-101.048 616.968 1.00 22.14 N ANISOU 2828 N CYS B 10 1730 4910 1771 -246 5 -223 N ATOM 2829 CA CYS B 10 -136.923-101.666 616.641 1.00 22.36 C ANISOU 2829 CA CYS B 10 1797 4923 1777 -268 18 -193 C ATOM 2830 C CYS B 10 -136.907-102.125 615.191 1.00 24.62 C ANISOU 2830 C CYS B 10 2043 5304 2008 -268 22 -190 C ATOM 2831 O CYS B 10 -137.961-102.289 614.580 1.00 21.06 O ANISOU 2831 O CYS B 10 1543 4944 1516 -255 26 -245 O ATOM 2832 CB CYS B 10 -136.650-102.850 617.564 1.00 21.43 C ANISOU 2832 CB CYS B 10 1744 4678 1718 -294 31 -287 C ATOM 2833 SG CYS B 10 -136.504-102.417 619.311 1.00 28.13 S ANISOU 2833 SG CYS B 10 2634 5429 2625 -297 32 -296 S ATOM 2834 N CYS B 11 -135.707-102.325 614.645 1.00 23.51 N ANISOU 2834 N CYS B 11 1914 5160 1859 -282 19 -142 N ATOM 2835 CA CYS B 11 -135.549-102.751 613.255 1.00 21.92 C ANISOU 2835 CA CYS B 11 1674 5053 1600 -291 24 -141 C ATOM 2836 C CYS B 11 -135.082-104.197 613.187 1.00 22.17 C ANISOU 2836 C CYS B 11 1748 5020 1657 -319 20 -241 C ATOM 2837 O CYS B 11 -134.284-104.631 614.013 1.00 22.42 O ANISOU 2837 O CYS B 11 1817 4962 1740 -322 13 -261 O ATOM 2838 CB CYS B 11 -134.548-101.852 612.528 1.00 21.85 C ANISOU 2838 CB CYS B 11 1628 5125 1551 -301 15 -20 C ATOM 2839 SG CYS B 11 -135.044-100.121 612.420 1.00 28.32 S ANISOU 2839 SG CYS B 11 2365 6069 2328 -273 3 132 S ATOM 2840 N PHE B 12 -135.571-104.939 612.202 1.00 21.40 N ANISOU 2840 N PHE B 12 1618 4992 1521 -339 17 -305 N ATOM 2841 CA PHE B 12 -135.178-106.334 612.034 1.00 19.64 C ANISOU 2841 CA PHE B 12 1383 4739 1341 -383 4 -403 C ATOM 2842 C PHE B 12 -134.707-106.583 610.618 1.00 22.25 C ANISOU 2842 C PHE B 12 1653 5180 1621 -407 -4 -398 C ATOM 2843 O PHE B 12 -134.330-107.699 610.265 1.00 20.11 O ANISOU 2843 O PHE B 12 1361 4916 1363 -447 13 -479 O ATOM 2844 CB PHE B 12 -136.333-107.253 612.396 1.00 23.24 C ANISOU 2844 CB PHE B 12 1830 5170 1831 -423 22 -528 C ATOM 2845 CG PHE B 12 -136.703-107.176 613.840 1.00 28.61 C ANISOU 2845 CG PHE B 12 2556 5744 2569 -421 33 -550 C ATOM 2846 CD1 PHE B 12 -136.157-108.060 614.752 1.00 31.60 C ANISOU 2846 CD1 PHE B 12 2954 6050 3003 -450 59 -600 C ATOM 2847 CD2 PHE B 12 -137.554-106.183 614.299 1.00 30.69 C ANISOU 2847 CD2 PHE B 12 2840 6008 2814 -387 34 -523 C ATOM 2848 CE1 PHE B 12 -136.473-107.976 616.092 1.00 31.48 C ANISOU 2848 CE1 PHE B 12 2973 5954 3032 -456 73 -620 C ATOM 2849 CE2 PHE B 12 -137.877-106.093 615.645 1.00 30.10 C ANISOU 2849 CE2 PHE B 12 2802 5838 2795 -396 44 -550 C ATOM 2850 CZ PHE B 12 -137.336-106.992 616.537 1.00 30.43 C ANISOU 2850 CZ PHE B 12 2861 5800 2903 -435 59 -595 C ATOM 2851 N ALA B 13 -134.723-105.516 609.822 1.00 21.00 N ANISOU 2851 N ALA B 13 1459 5125 1396 -387 -21 -303 N ATOM 2852 CA ALA B 13 -134.237-105.530 608.450 1.00 21.63 C ANISOU 2852 CA ALA B 13 1444 5337 1437 -417 -29 -278 C ATOM 2853 C ALA B 13 -133.632-104.171 608.120 1.00 22.96 C ANISOU 2853 C ALA B 13 1553 5586 1584 -409 -30 -136 C ATOM 2854 O ALA B 13 -134.035-103.164 608.698 1.00 22.77 O ANISOU 2854 O ALA B 13 1513 5554 1585 -373 10 -53 O ATOM 2855 CB ALA B 13 -135.359-105.857 607.495 1.00 24.05 C ANISOU 2855 CB ALA B 13 1644 5774 1720 -423 -14 -332 C ATOM 2856 N TYR B 14 -132.674-104.144 607.199 1.00 22.81 N ANISOU 2856 N TYR B 14 1497 5664 1508 -455 -26 -111 N ATOM 2857 CA TYR B 14 -132.096-102.892 606.725 1.00 29.00 C ANISOU 2857 CA TYR B 14 2223 6570 2224 -479 -25 22 C ATOM 2858 C TYR B 14 -132.334-102.723 605.227 1.00 31.49 C ANISOU 2858 C TYR B 14 2429 7113 2421 -505 -17 66 C ATOM 2859 O TYR B 14 -132.321-103.702 604.479 1.00 25.78 O ANISOU 2859 O TYR B 14 1686 6431 1678 -535 -11 -29 O ATOM 2860 CB TYR B 14 -130.591-102.844 606.984 1.00 28.50 C ANISOU 2860 CB TYR B 14 2204 6464 2161 -534 -27 12 C ATOM 2861 CG TYR B 14 -130.136-103.017 608.419 1.00 25.90 C ANISOU 2861 CG TYR B 14 1972 5960 1910 -501 -26 -33 C ATOM 2862 CD1 TYR B 14 -130.570-102.167 609.432 1.00 23.52 C ANISOU 2862 CD1 TYR B 14 1706 5588 1642 -465 -33 31 C ATOM 2863 CD2 TYR B 14 -129.262-104.034 608.752 1.00 24.60 C ANISOU 2863 CD2 TYR B 14 1845 5729 1774 -503 -10 -139 C ATOM 2864 CE1 TYR B 14 -130.131-102.325 610.729 1.00 20.27 C ANISOU 2864 CE1 TYR B 14 1367 5047 1287 -439 -21 -13 C ATOM 2865 CE2 TYR B 14 -128.820-104.206 610.046 1.00 23.89 C ANISOU 2865 CE2 TYR B 14 1813 5524 1741 -463 -2 -175 C ATOM 2866 CZ TYR B 14 -129.251-103.354 611.028 1.00 23.91 C ANISOU 2866 CZ TYR B 14 1851 5460 1774 -434 -7 -114 C ATOM 2867 OH TYR B 14 -128.794-103.555 612.309 1.00 19.90 O ANISOU 2867 OH TYR B 14 1386 4860 1317 -396 3 -156 O ATOM 2868 N ILE B 15 -132.538-101.489 604.782 1.00 26.56 N ANISOU 2868 N ILE B 15 1729 6662 1700 -495 -23 219 N ATOM 2869 CA ILE B 15 -132.723-101.252 603.362 1.00 31.17 C ANISOU 2869 CA ILE B 15 2301 7406 2138 -491 -17 280 C ATOM 2870 C ILE B 15 -131.424-101.593 602.619 1.00 36.32 C ANISOU 2870 C ILE B 15 2981 8068 2752 -602 6 249 C ATOM 2871 O ILE B 15 -130.328-101.383 603.135 1.00 35.98 O ANISOU 2871 O ILE B 15 2998 7918 2755 -664 25 246 O ATOM 2872 CB ILE B 15 -133.164 -99.800 603.079 1.00 32.70 C ANISOU 2872 CB ILE B 15 2635 7577 2212 -399 -31 470 C ATOM 2873 CG1 ILE B 15 -133.779 -99.702 601.681 1.00 36.47 C ANISOU 2873 CG1 ILE B 15 3138 8197 2521 -336 -54 514 C ATOM 2874 CG2 ILE B 15 -132.000 -98.824 603.256 1.00 32.33 C ANISOU 2874 CG2 ILE B 15 2731 7406 2147 -465 14 590 C ATOM 2875 CD1 ILE B 15 -134.552 -98.435 601.437 1.00 38.97 C ANISOU 2875 CD1 ILE B 15 3599 8494 2714 -189 -110 684 C ATOM 2876 N ALA B 16 -131.550-102.148 601.416 1.00 40.49 N ANISOU 2876 N ALA B 16 3465 8729 3190 -627 15 206 N ATOM 2877 CA ALA B 16 -130.388-102.672 600.694 1.00 44.26 C ANISOU 2877 CA ALA B 16 3952 9225 3638 -737 45 139 C ATOM 2878 C ALA B 16 -129.506-101.567 600.120 1.00 32.18 C ANISOU 2878 C ALA B 16 2573 7651 2002 -786 114 271 C ATOM 2879 O ALA B 16 -128.285-101.604 600.254 1.00 45.39 O ANISOU 2879 O ALA B 16 4283 9253 3711 -878 164 223 O ATOM 2880 CB ALA B 16 -130.837-103.614 599.584 1.00 31.73 C ANISOU 2880 CB ALA B 16 2266 7803 1988 -760 40 44 C ATOM 2881 N ARG B 17 -130.131-100.586 599.487 1.00 33.87 N ANISOU 2881 N ARG B 17 2895 7898 2076 -717 122 428 N ATOM 2882 CA ARG B 17 -129.397 -99.537 598.798 1.00 46.82 C ANISOU 2882 CA ARG B 17 4723 9482 3585 -766 207 566 C ATOM 2883 C ARG B 17 -129.697 -98.174 599.401 1.00 43.49 C ANISOU 2883 C ARG B 17 4462 8926 3136 -691 221 743 C ATOM 2884 O ARG B 17 -130.742 -97.987 600.019 1.00 43.90 O ANISOU 2884 O ARG B 17 4481 8977 3222 -568 139 779 O ATOM 2885 CB ARG B 17 -129.731 -99.544 597.300 1.00 38.11 C ANISOU 2885 CB ARG B 17 3677 8515 2287 -748 212 615 C ATOM 2886 CG ARG B 17 -129.006-100.622 596.523 1.00 46.28 C ANISOU 2886 CG ARG B 17 4606 9653 3323 -871 246 463 C ATOM 2887 CD ARG B 17 -127.508-100.621 596.805 1.00 46.72 C ANISOU 2887 CD ARG B 17 4692 9602 3459 -1014 341 397 C ATOM 2888 NE ARG B 17 -126.814 -99.525 596.135 1.00 50.53 N ANISOU 2888 NE ARG B 17 5380 10014 3806 -1079 465 528 N ATOM 2889 N PRO B 18 -128.770 -97.220 599.229 1.00 45.47 N ANISOU 2889 N PRO B 18 4890 9055 3332 -773 340 844 N ATOM 2890 CA PRO B 18 -128.968 -95.862 599.737 1.00 48.23 C ANISOU 2890 CA PRO B 18 5424 9251 3652 -720 383 1023 C ATOM 2891 C PRO B 18 -130.237 -95.229 599.194 1.00 52.57 C ANISOU 2891 C PRO B 18 6099 9832 4043 -538 296 1187 C ATOM 2892 O PRO B 18 -130.523 -95.356 598.009 1.00 56.02 O ANISOU 2892 O PRO B 18 6598 10372 4316 -498 276 1222 O ATOM 2893 CB PRO B 18 -127.734 -95.113 599.225 1.00 49.93 C ANISOU 2893 CB PRO B 18 5819 9349 3803 -866 567 1080 C ATOM 2894 CG PRO B 18 -126.709 -96.164 599.031 1.00 48.55 C ANISOU 2894 CG PRO B 18 5483 9252 3711 -1004 601 877 C ATOM 2895 CD PRO B 18 -127.458 -97.370 598.574 1.00 46.97 C ANISOU 2895 CD PRO B 18 5116 9234 3496 -933 464 779 C ATOM 2896 N LEU B 19 -130.991 -94.569 600.063 1.00 54.42 N ANISOU 2896 N LEU B 19 6366 9984 4326 -421 235 1276 N ATOM 2897 CA LEU B 19 -132.139 -93.779 599.644 1.00 56.63 C ANISOU 2897 CA LEU B 19 6792 10262 4464 -223 144 1440 C ATOM 2898 C LEU B 19 -131.677 -92.504 598.962 1.00 59.88 C ANISOU 2898 C LEU B 19 7532 10512 4706 -227 261 1657 C ATOM 2899 O LEU B 19 -130.564 -92.045 599.218 1.00 61.92 O ANISOU 2899 O LEU B 19 7892 10624 5010 -390 432 1680 O ATOM 2900 CB LEU B 19 -132.998 -93.432 600.848 1.00 55.70 C ANISOU 2900 CB LEU B 19 6609 10087 4468 -102 53 1458 C ATOM 2901 CG LEU B 19 -133.664 -94.610 601.525 1.00 52.66 C ANISOU 2901 CG LEU B 19 5941 9836 4231 -81 -46 1252 C ATOM 2902 CD1 LEU B 19 -133.682 -94.320 602.997 1.00 51.66 C ANISOU 2902 CD1 LEU B 19 5763 9593 4270 -91 -44 1240 C ATOM 2903 CD2 LEU B 19 -135.063 -94.763 600.982 1.00 54.64 C ANISOU 2903 CD2 LEU B 19 6143 10221 4398 106 -181 1235 C ATOM 2904 N PRO B 20 -132.528 -91.920 598.100 1.00 62.30 N ANISOU 2904 N PRO B 20 8015 10836 4818 -49 179 1805 N ATOM 2905 CA PRO B 20 -132.186 -90.613 597.529 1.00 66.18 C ANISOU 2905 CA PRO B 20 8877 11128 5141 -36 296 2038 C ATOM 2906 C PRO B 20 -131.953 -89.603 598.643 1.00 65.99 C ANISOU 2906 C PRO B 20 8967 10865 5240 -58 389 2147 C ATOM 2907 O PRO B 20 -132.888 -89.325 599.399 1.00 64.23 O ANISOU 2907 O PRO B 20 8679 10626 5098 106 258 2183 O ATOM 2908 CB PRO B 20 -133.423 -90.242 596.708 1.00 68.04 C ANISOU 2908 CB PRO B 20 9231 11437 5184 215 123 2158 C ATOM 2909 CG PRO B 20 -134.125 -91.527 596.461 1.00 65.80 C ANISOU 2909 CG PRO B 20 8632 11433 4935 268 -30 1954 C ATOM 2910 CD PRO B 20 -133.846 -92.396 597.643 1.00 60.84 C ANISOU 2910 CD PRO B 20 7710 10842 4565 146 -15 1758 C ATOM 2911 N ARG B 21 -130.731 -89.085 598.754 1.00 65.62 N ANISOU 2911 N ARG B 21 9068 10641 5223 -265 624 2177 N ATOM 2912 CA ARG B 21 -130.390 -88.128 599.804 1.00 62.67 C ANISOU 2912 CA ARG B 21 8794 10033 4985 -329 754 2259 C ATOM 2913 C ARG B 21 -131.408 -86.992 599.841 1.00 64.65 C ANISOU 2913 C ARG B 21 9283 10129 5153 -109 673 2492 C ATOM 2914 O ARG B 21 -131.788 -86.517 600.911 1.00 64.99 O ANISOU 2914 O ARG B 21 9281 10067 5346 -46 647 2533 O ATOM 2915 CB ARG B 21 -128.975 -87.580 599.594 1.00 61.16 C ANISOU 2915 CB ARG B 21 8781 9658 4797 -577 1056 2261 C ATOM 2916 CG ARG B 21 -128.577 -86.472 600.562 1.00 61.01 C ANISOU 2916 CG ARG B 21 8895 9371 4917 -670 1237 2340 C ATOM 2917 CD ARG B 21 -128.705 -86.910 602.013 1.00 57.33 C ANISOU 2917 CD ARG B 21 8115 8968 4699 -689 1143 2198 C ATOM 2918 NE ARG B 21 -128.469 -85.814 602.953 1.00 55.86 N ANISOU 2918 NE ARG B 21 8045 8529 4650 -765 1301 2276 N ATOM 2919 CZ ARG B 21 -129.425 -85.054 603.483 1.00 53.83 C ANISOU 2919 CZ ARG B 21 7889 8147 4416 -596 1217 2446 C ATOM 2920 NH1 ARG B 21 -130.700 -85.259 603.169 1.00 52.94 N ANISOU 2920 NH1 ARG B 21 7764 8151 4201 -315 967 2542 N ATOM 2921 NH2 ARG B 21 -129.107 -84.084 604.331 1.00 53.40 N ANISOU 2921 NH2 ARG B 21 7931 7848 4510 -698 1387 2496 N ATOM 2922 N ALA B 22 -131.870 -86.593 598.661 1.00 66.32 N ANISOU 2922 N ALA B 22 9733 10335 5131 18 617 2638 N ATOM 2923 CA ALA B 22 -132.880 -85.552 598.522 1.00 67.76 C ANISOU 2923 CA ALA B 22 10134 10388 5226 259 502 2857 C ATOM 2924 C ALA B 22 -134.167 -85.833 599.310 1.00 65.10 C ANISOU 2924 C ALA B 22 9544 10172 5017 514 258 2798 C ATOM 2925 O ALA B 22 -134.845 -84.904 599.744 1.00 65.63 O ANISOU 2925 O ALA B 22 9729 10079 5127 696 204 2941 O ATOM 2926 CB ALA B 22 -133.208 -85.357 597.052 1.00 71.58 C ANISOU 2926 CB ALA B 22 10842 10927 5429 357 434 2980 C ATOM 2927 N HIS B 23 -134.502 -87.106 599.502 1.00 61.61 N ANISOU 2927 N HIS B 23 8758 10002 4650 519 124 2575 N ATOM 2928 CA HIS B 23 -135.806 -87.457 600.062 1.00 60.75 C ANISOU 2928 CA HIS B 23 8414 10034 4634 741 -100 2484 C ATOM 2929 C HIS B 23 -135.787 -87.638 601.587 1.00 62.70 C ANISOU 2929 C HIS B 23 8453 10242 5131 683 -87 2382 C ATOM 2930 O HIS B 23 -136.820 -87.923 602.196 1.00 63.62 O ANISOU 2930 O HIS B 23 8373 10455 5344 835 -247 2284 O ATOM 2931 CB HIS B 23 -136.338 -88.731 599.392 1.00 54.78 C ANISOU 2931 CB HIS B 23 7407 9585 3821 771 -242 2284 C ATOM 2932 CG HIS B 23 -136.644 -88.570 597.934 1.00 56.41 C ANISOU 2932 CG HIS B 23 7782 9873 3777 878 -302 2375 C ATOM 2933 N ILE B 24 -134.625 -87.458 602.206 1.00 61.23 N ANISOU 2933 N ILE B 24 8305 9914 5046 452 112 2390 N ATOM 2934 CA ILE B 24 -134.486 -87.720 603.639 1.00 58.67 C ANISOU 2934 CA ILE B 24 7771 9576 4945 365 130 2282 C ATOM 2935 C ILE B 24 -134.504 -86.442 604.475 1.00 63.14 C ANISOU 2935 C ILE B 24 8510 9870 5610 409 224 2457 C ATOM 2936 O ILE B 24 -133.783 -85.486 604.182 1.00 69.58 O ANISOU 2936 O ILE B 24 9598 10453 6385 316 418 2611 O ATOM 2937 CB ILE B 24 -133.199 -88.496 603.926 1.00 53.92 C ANISOU 2937 CB ILE B 24 7032 9025 4431 75 274 2121 C ATOM 2938 CG1 ILE B 24 -133.294 -89.884 603.298 1.00 51.21 C ANISOU 2938 CG1 ILE B 24 6477 8936 4044 51 171 1925 C ATOM 2939 CG2 ILE B 24 -132.960 -88.606 605.422 1.00 54.74 C ANISOU 2939 CG2 ILE B 24 6962 9088 4749 -25 307 2029 C ATOM 2940 CD1 ILE B 24 -132.136 -90.787 603.626 1.00 49.32 C ANISOU 2940 CD1 ILE B 24 6071 8754 3915 -187 272 1738 C ATOM 2941 N LYS B 25 -135.327 -86.439 605.521 1.00 58.06 N ANISOU 2941 N LYS B 25 7711 9242 5108 537 106 2416 N ATOM 2942 CA LYS B 25 -135.562 -85.242 606.321 1.00 58.61 C ANISOU 2942 CA LYS B 25 7927 9051 5291 627 172 2578 C ATOM 2943 C LYS B 25 -134.817 -85.245 607.658 1.00 55.88 C ANISOU 2943 C LYS B 25 7453 8555 5226 388 304 2415 C ATOM 2944 O LYS B 25 -134.146 -84.277 608.007 1.00 58.87 O ANISOU 2944 O LYS B 25 8006 8649 5713 266 503 2483 O ATOM 2945 CB LYS B 25 -137.057 -85.084 606.573 1.00 60.14 C ANISOU 2945 CB LYS B 25 8042 9294 5512 939 -58 2569 C ATOM 2946 CG LYS B 25 -137.438 -83.787 607.244 1.00 63.71 C ANISOU 2946 CG LYS B 25 8669 9439 6099 1080 -7 2715 C ATOM 2947 CD LYS B 25 -138.657 -83.986 608.120 1.00 63.69 C ANISOU 2947 CD LYS B 25 8436 9513 6249 1263 -207 2564 C ATOM 2948 CE LYS B 25 -139.756 -84.718 607.374 1.00 64.11 C ANISOU 2948 CE LYS B 25 8336 9869 6155 1465 -447 2455 C ATOM 2949 NZ LYS B 25 -140.697 -85.371 608.324 1.00 62.21 N ANISOU 2949 NZ LYS B 25 7787 9784 6067 1519 -600 2218 N ATOM 2950 N GLU B 26 -134.965 -86.326 608.416 1.00 52.21 N ANISOU 2950 N GLU B 26 6688 8270 4880 322 197 2180 N ATOM 2951 CA GLU B 26 -134.306 -86.460 609.713 1.00 49.24 C ANISOU 2951 CA GLU B 26 6171 7786 4753 118 288 1996 C ATOM 2952 C GLU B 26 -133.775 -87.874 609.894 1.00 43.82 C ANISOU 2952 C GLU B 26 5243 7338 4069 -34 253 1785 C ATOM 2953 O GLU B 26 -133.929 -88.728 609.022 1.00 40.91 O ANISOU 2953 O GLU B 26 4814 7203 3525 3 172 1774 O ATOM 2954 CB GLU B 26 -135.266 -86.138 610.867 1.00 50.26 C ANISOU 2954 CB GLU B 26 6208 7812 5077 244 186 1924 C ATOM 2955 CG GLU B 26 -136.230 -84.986 610.623 1.00 55.36 C ANISOU 2955 CG GLU B 26 7043 8289 5703 495 138 2112 C ATOM 2956 CD GLU B 26 -137.531 -85.139 611.394 1.00 56.33 C ANISOU 2956 CD GLU B 26 6997 8468 5940 682 -48 2001 C ATOM 2957 OE1 GLU B 26 -137.730 -86.195 612.026 1.00 53.76 O ANISOU 2957 OE1 GLU B 26 6426 8318 5684 608 -133 1790 O ATOM 2958 OE2 GLU B 26 -138.363 -84.207 611.362 1.00 61.53 O ANISOU 2958 OE2 GLU B 26 7775 8988 6615 905 -100 2120 O ATOM 2959 N TYR B 27 -133.166 -88.123 611.043 1.00 40.32 N ANISOU 2959 N TYR B 27 4664 6836 3818 -191 311 1614 N ATOM 2960 CA TYR B 27 -132.768 -89.474 611.401 1.00 38.23 C ANISOU 2960 CA TYR B 27 4181 6770 3574 -291 262 1412 C ATOM 2961 C TYR B 27 -132.811 -89.651 612.910 1.00 36.93 C ANISOU 2961 C TYR B 27 3878 6533 3622 -336 239 1246 C ATOM 2962 O TYR B 27 -132.681 -88.676 613.652 1.00 33.14 O ANISOU 2962 O TYR B 27 3460 5847 3284 -371 317 1265 O ATOM 2963 CB TYR B 27 -131.364 -89.783 610.883 1.00 37.70 C ANISOU 2963 CB TYR B 27 4116 6763 3444 -491 407 1369 C ATOM 2964 CG TYR B 27 -130.272 -89.236 611.769 1.00 42.81 C ANISOU 2964 CG TYR B 27 4750 7259 4258 -674 563 1277 C ATOM 2965 CD1 TYR B 27 -129.841 -87.922 611.641 1.00 48.13 C ANISOU 2965 CD1 TYR B 27 5611 7712 4965 -753 734 1390 C ATOM 2966 CD2 TYR B 27 -129.673 -90.030 612.739 1.00 42.57 C ANISOU 2966 CD2 TYR B 27 4526 7307 4343 -765 546 1066 C ATOM 2967 CE1 TYR B 27 -128.844 -87.414 612.449 1.00 48.03 C ANISOU 2967 CE1 TYR B 27 5563 7581 5103 -941 890 1269 C ATOM 2968 CE2 TYR B 27 -128.676 -89.528 613.557 1.00 44.17 C ANISOU 2968 CE2 TYR B 27 4690 7410 4682 -922 675 956 C ATOM 2969 CZ TYR B 27 -128.265 -88.221 613.406 1.00 47.58 C ANISOU 2969 CZ TYR B 27 5280 7644 5153 -1021 849 1044 C ATOM 2970 OH TYR B 27 -127.271 -87.717 614.214 1.00 50.87 O ANISOU 2970 OH TYR B 27 5637 7984 5708 -1197 991 899 O ATOM 2971 N PHE B 28 -132.985 -90.895 613.356 1.00 35.97 N ANISOU 2971 N PHE B 28 3583 6571 3512 -339 145 1083 N ATOM 2972 CA PHE B 28 -132.786 -91.243 614.759 1.00 35.74 C ANISOU 2972 CA PHE B 28 3436 6496 3648 -402 139 919 C ATOM 2973 C PHE B 28 -132.268 -92.676 614.906 1.00 34.34 C ANISOU 2973 C PHE B 28 3125 6489 3432 -461 111 762 C ATOM 2974 O PHE B 28 -132.453 -93.500 614.009 1.00 37.02 O ANISOU 2974 O PHE B 28 3439 6990 3636 -429 68 761 O ATOM 2975 CB PHE B 28 -134.080 -91.043 615.566 1.00 31.77 C ANISOU 2975 CB PHE B 28 2903 5927 3242 -279 36 892 C ATOM 2976 CG PHE B 28 -135.221 -91.962 615.176 1.00 32.80 C ANISOU 2976 CG PHE B 28 2955 6229 3280 -158 -98 843 C ATOM 2977 CD1 PHE B 28 -135.401 -93.183 615.810 1.00 21.70 C ANISOU 2977 CD1 PHE B 28 1429 4923 1894 -191 -141 672 C ATOM 2978 CD2 PHE B 28 -136.141 -91.579 614.212 1.00 28.78 C ANISOU 2978 CD2 PHE B 28 2499 5778 2659 -7 -174 958 C ATOM 2979 CE1 PHE B 28 -136.456 -94.007 615.474 1.00 21.52 C ANISOU 2979 CE1 PHE B 28 1372 5003 1801 -111 -214 588 C ATOM 2980 CE2 PHE B 28 -137.200 -92.402 613.872 1.00 25.25 C ANISOU 2980 CE2 PHE B 28 1950 5516 2128 93 -293 874 C ATOM 2981 CZ PHE B 28 -137.356 -93.618 614.508 1.00 25.06 C ANISOU 2981 CZ PHE B 28 1822 5550 2149 20 -293 674 C ATOM 2982 N TYR B 29 -131.595 -92.949 616.026 1.00 28.17 N ANISOU 2982 N TYR B 29 2268 5673 2764 -540 139 628 N ATOM 2983 CA TYR B 29 -131.141 -94.296 616.381 1.00 24.92 C ANISOU 2983 CA TYR B 29 1896 5237 2337 -510 70 449 C ATOM 2984 C TYR B 29 -132.225 -95.029 617.168 1.00 26.31 C ANISOU 2984 C TYR B 29 2109 5352 2537 -419 -5 368 C ATOM 2985 O TYR B 29 -132.888 -94.428 618.010 1.00 26.01 O ANISOU 2985 O TYR B 29 2060 5224 2598 -399 -18 369 O ATOM 2986 CB TYR B 29 -129.856 -94.246 617.222 1.00 20.04 C ANISOU 2986 CB TYR B 29 1302 4506 1806 -569 113 327 C ATOM 2987 CG TYR B 29 -128.596 -93.935 616.443 1.00 30.11 C ANISOU 2987 CG TYR B 29 2567 5820 3052 -665 199 324 C ATOM 2988 CD1 TYR B 29 -128.183 -92.621 616.248 1.00 33.87 C ANISOU 2988 CD1 TYR B 29 3049 6241 3578 -774 325 399 C ATOM 2989 CD2 TYR B 29 -127.810 -94.956 615.917 1.00 25.36 C ANISOU 2989 CD2 TYR B 29 1970 5289 2377 -658 178 237 C ATOM 2990 CE1 TYR B 29 -127.026 -92.333 615.538 1.00 38.16 C ANISOU 2990 CE1 TYR B 29 3610 6792 4096 -879 432 372 C ATOM 2991 CE2 TYR B 29 -126.659 -94.680 615.212 1.00 33.74 C ANISOU 2991 CE2 TYR B 29 3017 6382 3420 -751 261 209 C ATOM 2992 CZ TYR B 29 -126.271 -93.366 615.021 1.00 41.01 C ANISOU 2992 CZ TYR B 29 3950 7241 4390 -866 391 270 C ATOM 2993 OH TYR B 29 -125.123 -93.087 614.315 1.00 49.29 O ANISOU 2993 OH TYR B 29 5005 8303 5421 -974 499 223 O ATOM 2994 N THR B 30 -132.404 -96.323 616.915 1.00 18.37 N ANISOU 2994 N THR B 30 1156 4376 1450 -378 -27 286 N ATOM 2995 CA THR B 30 -133.359 -97.100 617.696 1.00 24.14 C ANISOU 2995 CA THR B 30 1943 5018 2211 -324 -43 193 C ATOM 2996 C THR B 30 -132.819 -97.331 619.104 1.00 25.64 C ANISOU 2996 C THR B 30 2183 5069 2490 -329 -33 106 C ATOM 2997 O THR B 30 -131.611 -97.284 619.345 1.00 26.44 O ANISOU 2997 O THR B 30 2282 5160 2603 -355 -17 83 O ATOM 2998 CB THR B 30 -133.682 -98.452 617.040 1.00 17.15 C ANISOU 2998 CB THR B 30 1091 4204 1220 -303 -31 127 C ATOM 2999 OG1 THR B 30 -132.465 -99.122 616.729 1.00 17.09 O ANISOU 2999 OG1 THR B 30 1101 4232 1159 -327 -15 94 O ATOM 3000 CG2 THR B 30 -134.469 -98.250 615.765 1.00 18.13 C ANISOU 3000 CG2 THR B 30 1157 4479 1253 -283 -39 191 C ATOM 3001 N SER B 31 -133.734 -97.585 620.028 1.00 26.12 N ANISOU 3001 N SER B 31 2278 5042 2604 -303 -42 49 N ATOM 3002 CA SER B 31 -133.428 -97.707 621.447 1.00 21.08 C ANISOU 3002 CA SER B 31 1676 4298 2034 -304 -37 -18 C ATOM 3003 C SER B 31 -132.411 -98.794 621.753 1.00 16.95 C ANISOU 3003 C SER B 31 1186 3803 1450 -289 -22 -79 C ATOM 3004 O SER B 31 -132.300 -99.773 621.019 1.00 14.95 O ANISOU 3004 O SER B 31 944 3625 1109 -276 -10 -96 O ATOM 3005 CB SER B 31 -134.722 -97.975 622.221 1.00 21.71 C ANISOU 3005 CB SER B 31 1784 4315 2152 -290 -41 -75 C ATOM 3006 OG SER B 31 -134.464 -98.311 623.566 1.00 25.52 O ANISOU 3006 OG SER B 31 2302 4732 2660 -294 -32 -139 O ATOM 3007 N GLY B 32 -131.677 -98.615 622.849 1.00 14.82 N ANISOU 3007 N GLY B 32 917 3490 1222 -286 -23 -118 N ATOM 3008 CA GLY B 32 -130.724 -99.604 623.303 1.00 18.48 C ANISOU 3008 CA GLY B 32 1389 4009 1625 -246 -18 -181 C ATOM 3009 C GLY B 32 -131.388-100.906 623.698 1.00 18.89 C ANISOU 3009 C GLY B 32 1479 4088 1612 -214 -4 -232 C ATOM 3010 O GLY B 32 -130.729-101.942 623.775 1.00 20.31 O ANISOU 3010 O GLY B 32 1651 4347 1721 -164 5 -277 O ATOM 3011 N LYS B 33 -132.692-100.858 623.955 1.00 20.87 N ANISOU 3011 N LYS B 33 1756 4288 1887 -241 1 -238 N ATOM 3012 CA LYS B 33 -133.456-102.064 624.246 1.00 20.26 C ANISOU 3012 CA LYS B 33 1704 4251 1743 -244 26 -310 C ATOM 3013 C LYS B 33 -133.477-103.027 623.058 1.00 20.62 C ANISOU 3013 C LYS B 33 1748 4333 1752 -241 30 -317 C ATOM 3014 O LYS B 33 -133.680-104.230 623.221 1.00 25.58 O ANISOU 3014 O LYS B 33 2375 4955 2388 -244 26 -375 O ATOM 3015 CB LYS B 33 -134.894-101.712 624.626 1.00 20.49 C ANISOU 3015 CB LYS B 33 1752 4213 1822 -292 34 -341 C ATOM 3016 CG LYS B 33 -135.832-101.637 623.429 1.00 26.38 C ANISOU 3016 CG LYS B 33 2487 4975 2564 -308 35 -333 C ATOM 3017 CD LYS B 33 -137.251-101.948 623.824 1.00 32.85 C ANISOU 3017 CD LYS B 33 3316 5774 3391 -353 59 -431 C ATOM 3018 CE LYS B 33 -138.177-101.944 622.619 1.00 35.10 C ANISOU 3018 CE LYS B 33 3568 6114 3653 -352 58 -448 C ATOM 3019 NZ LYS B 33 -137.915-103.097 621.722 1.00 40.84 N ANISOU 3019 NZ LYS B 33 4301 6892 4324 -363 65 -476 N ATOM 3020 N CYS B 34 -133.287-102.491 621.859 1.00 17.41 N ANISOU 3020 N CYS B 34 1323 3969 1321 -247 25 -261 N ATOM 3021 CA CYS B 34 -133.468-103.274 620.653 1.00 17.24 C ANISOU 3021 CA CYS B 34 1296 3973 1280 -253 25 -271 C ATOM 3022 C CYS B 34 -132.334-104.272 620.467 1.00 20.60 C ANISOU 3022 C CYS B 34 1709 4425 1693 -219 20 -297 C ATOM 3023 O CYS B 34 -131.176-103.992 620.794 1.00 16.87 O ANISOU 3023 O CYS B 34 1219 3983 1210 -182 18 -282 O ATOM 3024 CB CYS B 34 -133.569-102.356 619.433 1.00 19.03 C ANISOU 3024 CB CYS B 34 1494 4265 1472 -267 20 -198 C ATOM 3025 SG CYS B 34 -134.911-101.150 619.502 1.00 24.46 S ANISOU 3025 SG CYS B 34 2160 4943 2191 -277 10 -160 S ATOM 3026 N SER B 35 -132.686-105.436 619.932 1.00 23.69 N ANISOU 3026 N SER B 35 2081 4832 2088 -237 14 -352 N ATOM 3027 CA SER B 35 -131.733-106.502 619.661 1.00 25.39 C ANISOU 3027 CA SER B 35 2249 5108 2290 -202 16 -391 C ATOM 3028 C SER B 35 -130.680-106.072 618.652 1.00 26.90 C ANISOU 3028 C SER B 35 2432 5346 2444 -188 6 -350 C ATOM 3029 O SER B 35 -129.524-106.487 618.730 1.00 29.12 O ANISOU 3029 O SER B 35 2678 5681 2705 -135 1 -376 O ATOM 3030 CB SER B 35 -132.471-107.737 619.140 1.00 32.62 C ANISOU 3030 CB SER B 35 3152 6042 3199 -253 50 -473 C ATOM 3031 OG SER B 35 -131.634-108.880 619.156 1.00 41.73 O ANISOU 3031 OG SER B 35 4362 7151 4341 -183 117 -502 O ATOM 3032 N ASN B 36 -131.100-105.249 617.696 1.00 23.43 N ANISOU 3032 N ASN B 36 2006 4914 1983 -232 11 -297 N ATOM 3033 CA ASN B 36 -130.241-104.792 616.609 1.00 19.93 C ANISOU 3033 CA ASN B 36 1533 4544 1498 -247 12 -261 C ATOM 3034 C ASN B 36 -129.960-103.304 616.715 1.00 21.72 C ANISOU 3034 C ASN B 36 1750 4793 1711 -268 14 -185 C ATOM 3035 O ASN B 36 -130.860-102.513 617.026 1.00 20.99 O ANISOU 3035 O ASN B 36 1671 4674 1631 -280 12 -138 O ATOM 3036 CB ASN B 36 -130.885-105.074 615.247 1.00 20.62 C ANISOU 3036 CB ASN B 36 1602 4677 1557 -287 8 -260 C ATOM 3037 CG ASN B 36 -131.121-106.550 615.000 1.00 22.27 C ANISOU 3037 CG ASN B 36 1790 4892 1780 -295 10 -351 C ATOM 3038 OD1 ASN B 36 -130.231-107.373 615.194 1.00 27.11 O ANISOU 3038 OD1 ASN B 36 2375 5531 2393 -270 16 -403 O ATOM 3039 ND2 ASN B 36 -132.331-106.891 614.575 1.00 21.64 N ANISOU 3039 ND2 ASN B 36 1707 4813 1703 -330 15 -385 N ATOM 3040 N PRO B 37 -128.711-102.911 616.461 1.00 19.15 N ANISOU 3040 N PRO B 37 1385 4537 1353 -283 15 -186 N ATOM 3041 CA PRO B 37 -128.436-101.483 616.296 1.00 21.59 C ANISOU 3041 CA PRO B 37 1664 4906 1634 -337 12 -118 C ATOM 3042 C PRO B 37 -129.044-101.034 614.968 1.00 28.83 C ANISOU 3042 C PRO B 37 2556 5891 2508 -382 3 -38 C ATOM 3043 O PRO B 37 -129.106-101.843 614.044 1.00 27.90 O ANISOU 3043 O PRO B 37 2432 5799 2371 -381 3 -66 O ATOM 3044 CB PRO B 37 -126.909-101.421 616.274 1.00 24.17 C ANISOU 3044 CB PRO B 37 1941 5268 1974 -352 26 -177 C ATOM 3045 CG PRO B 37 -126.501-102.750 615.698 1.00 21.79 C ANISOU 3045 CG PRO B 37 1633 5029 1618 -320 23 -252 C ATOM 3046 CD PRO B 37 -127.530-103.748 616.178 1.00 22.34 C ANISOU 3046 CD PRO B 37 1756 4998 1736 -262 18 -261 C ATOM 3047 N ALA B 38 -129.495 -99.792 614.864 1.00 18.43 N ANISOU 3047 N ALA B 38 1212 4595 1194 -414 -2 60 N ATOM 3048 CA ALA B 38 -130.128 -99.353 613.634 1.00 20.77 C ANISOU 3048 CA ALA B 38 1464 5012 1415 -439 -19 153 C ATOM 3049 C ALA B 38 -130.281 -97.853 613.577 1.00 25.39 C ANISOU 3049 C ALA B 38 1998 5616 2034 -476 -8 284 C ATOM 3050 O ALA B 38 -130.464 -97.188 614.601 1.00 26.74 O ANISOU 3050 O ALA B 38 2181 5675 2304 -467 5 296 O ATOM 3051 CB ALA B 38 -131.490-100.013 613.469 1.00 21.65 C ANISOU 3051 CB ALA B 38 1603 5078 1543 -379 -17 131 C ATOM 3052 N VAL B 39 -130.197 -97.330 612.360 1.00 29.86 N ANISOU 3052 N VAL B 39 2507 6304 2534 -519 5 384 N ATOM 3053 CA VAL B 39 -130.522 -95.944 612.082 1.00 29.47 C ANISOU 3053 CA VAL B 39 2449 6263 2484 -540 64 552 C ATOM 3054 C VAL B 39 -131.875 -95.912 611.394 1.00 33.37 C ANISOU 3054 C VAL B 39 2910 6894 2877 -449 11 651 C ATOM 3055 O VAL B 39 -132.151 -96.747 610.533 1.00 37.31 O ANISOU 3055 O VAL B 39 3359 7496 3322 -426 -27 598 O ATOM 3056 CB VAL B 39 -129.474 -95.291 611.187 1.00 31.23 C ANISOU 3056 CB VAL B 39 2731 6466 2670 -638 174 613 C ATOM 3057 CG1 VAL B 39 -129.890 -93.877 610.838 1.00 31.13 C ANISOU 3057 CG1 VAL B 39 2822 6404 2602 -640 258 820 C ATOM 3058 CG2 VAL B 39 -128.108 -95.312 611.872 1.00 32.02 C ANISOU 3058 CG2 VAL B 39 2829 6460 2876 -721 230 477 C ATOM 3059 N VAL B 40 -132.729 -94.972 611.776 1.00 30.81 N ANISOU 3059 N VAL B 40 2620 6551 2536 -383 9 775 N ATOM 3060 CA VAL B 40 -133.995 -94.822 611.086 1.00 29.97 C ANISOU 3060 CA VAL B 40 2535 6506 2347 -243 -87 838 C ATOM 3061 C VAL B 40 -134.055 -93.485 610.391 1.00 35.73 C ANISOU 3061 C VAL B 40 3425 7172 2978 -183 -65 1060 C ATOM 3062 O VAL B 40 -133.949 -92.440 611.032 1.00 40.52 O ANISOU 3062 O VAL B 40 4116 7575 3705 -182 -19 1133 O ATOM 3063 CB VAL B 40 -135.185 -94.953 612.034 1.00 29.16 C ANISOU 3063 CB VAL B 40 2373 6351 2355 -153 -165 747 C ATOM 3064 CG1 VAL B 40 -136.484 -94.628 611.292 1.00 34.28 C ANISOU 3064 CG1 VAL B 40 3049 7028 2948 5 -242 783 C ATOM 3065 CG2 VAL B 40 -135.239 -96.367 612.612 1.00 26.44 C ANISOU 3065 CG2 VAL B 40 2002 5958 2085 -206 -102 531 C ATOM 3066 N PHE B 41 -134.211 -93.519 609.071 1.00 33.32 N ANISOU 3066 N PHE B 41 3178 6929 2552 -129 -80 1115 N ATOM 3067 CA PHE B 41 -134.394 -92.293 608.314 1.00 30.62 C ANISOU 3067 CA PHE B 41 3030 6510 2095 -36 -65 1335 C ATOM 3068 C PHE B 41 -135.873 -92.000 608.134 1.00 35.57 C ANISOU 3068 C PHE B 41 3655 7168 2690 188 -212 1365 C ATOM 3069 O PHE B 41 -136.669 -92.904 607.873 1.00 31.25 O ANISOU 3069 O PHE B 41 2975 6745 2154 243 -292 1202 O ATOM 3070 CB PHE B 41 -133.706 -92.384 606.951 1.00 32.18 C ANISOU 3070 CB PHE B 41 3324 6739 2164 -95 4 1377 C ATOM 3071 CG PHE B 41 -132.215 -92.416 607.032 1.00 35.39 C ANISOU 3071 CG PHE B 41 3754 7077 2615 -306 162 1339 C ATOM 3072 CD1 PHE B 41 -131.505 -91.267 607.345 1.00 34.97 C ANISOU 3072 CD1 PHE B 41 3853 6842 2589 -396 310 1463 C ATOM 3073 CD2 PHE B 41 -131.521 -93.590 606.794 1.00 30.68 C ANISOU 3073 CD2 PHE B 41 3022 6578 2055 -414 171 1156 C ATOM 3074 CE1 PHE B 41 -130.136 -91.286 607.423 1.00 32.65 C ANISOU 3074 CE1 PHE B 41 3557 6482 2365 -596 462 1371 C ATOM 3075 CE2 PHE B 41 -130.151 -93.620 606.869 1.00 33.08 C ANISOU 3075 CE2 PHE B 41 3333 6817 2418 -583 295 1084 C ATOM 3076 CZ PHE B 41 -129.452 -92.463 607.184 1.00 34.71 C ANISOU 3076 CZ PHE B 41 3672 6857 2657 -677 441 1176 C ATOM 3077 N VAL B 42 -136.245 -90.735 608.290 1.00 39.63 N ANISOU 3077 N VAL B 42 4321 7551 3186 314 -224 1558 N ATOM 3078 CA VAL B 42 -137.607 -90.331 607.996 1.00 47.79 C ANISOU 3078 CA VAL B 42 5368 8601 4190 556 -368 1581 C ATOM 3079 C VAL B 42 -137.587 -89.481 606.730 1.00 53.91 C ANISOU 3079 C VAL B 42 6377 9317 4788 674 -354 1786 C ATOM 3080 O VAL B 42 -136.658 -88.702 606.498 1.00 56.56 O ANISOU 3080 O VAL B 42 6920 9498 5072 592 -211 1968 O ATOM 3081 CB VAL B 42 -138.256 -89.571 609.169 1.00 51.82 C ANISOU 3081 CB VAL B 42 5862 8993 4835 666 -423 1622 C ATOM 3082 CG1 VAL B 42 -138.116 -90.381 610.459 1.00 47.82 C ANISOU 3082 CG1 VAL B 42 5160 8482 4526 509 -405 1398 C ATOM 3083 CG2 VAL B 42 -137.634 -88.203 609.339 1.00 55.71 C ANISOU 3083 CG2 VAL B 42 6592 9181 5393 651 -285 1822 C ATOM 3084 N THR B 43 -138.599 -89.663 605.894 1.00 55.05 N ANISOU 3084 N THR B 43 6499 9579 4840 848 -483 1736 N ATOM 3085 CA THR B 43 -138.626 -89.005 604.598 1.00 60.82 C ANISOU 3085 CA THR B 43 7451 10282 5376 965 -491 1909 C ATOM 3086 C THR B 43 -139.442 -87.721 604.629 1.00 67.81 C ANISOU 3086 C THR B 43 8512 11014 6240 1220 -567 2083 C ATOM 3087 O THR B 43 -140.035 -87.371 605.653 1.00 67.00 O ANISOU 3087 O THR B 43 8333 10839 6285 1310 -620 2053 O ATOM 3088 CB THR B 43 -139.204 -89.933 603.518 1.00 56.98 C ANISOU 3088 CB THR B 43 6847 10029 4773 1008 -584 1763 C ATOM 3089 OG1 THR B 43 -140.571 -90.234 603.828 1.00 55.60 O ANISOU 3089 OG1 THR B 43 6493 9968 4664 1162 -728 1602 O ATOM 3090 CG2 THR B 43 -138.412 -91.224 603.457 1.00 52.26 C ANISOU 3090 CG2 THR B 43 6084 9557 4215 771 -498 1590 C ATOM 3091 N ARG B 44 -139.458 -87.022 603.498 1.00 72.74 N ANISOU 3091 N ARG B 44 9379 11578 6680 1338 -571 2261 N ATOM 3092 CA ARG B 44 -140.350 -85.889 603.317 1.00 77.17 C ANISOU 3092 CA ARG B 44 10110 12010 7200 1616 -667 2412 C ATOM 3093 C ARG B 44 -141.784 -86.385 603.452 1.00 78.70 C ANISOU 3093 C ARG B 44 10050 12410 7442 1799 -871 2205 C ATOM 3094 O ARG B 44 -142.636 -85.716 604.041 1.00 78.72 O ANISOU 3094 O ARG B 44 10043 12327 7540 1991 -958 2215 O ATOM 3095 CB ARG B 44 -140.123 -85.236 601.955 1.00 81.92 C ANISOU 3095 CB ARG B 44 11012 12544 7569 1694 -643 2616 C ATOM 3096 CG ARG B 44 -138.703 -85.384 601.441 1.00 81.77 C ANISOU 3096 CG ARG B 44 11151 12459 7459 1426 -442 2695 C ATOM 3097 CD ARG B 44 -137.758 -84.433 602.159 1.00 82.25 C ANISOU 3097 CD ARG B 44 11429 12199 7621 1291 -223 2859 C ATOM 3098 NE ARG B 44 -138.220 -83.051 602.092 1.00 86.23 N ANISOU 3098 NE ARG B 44 12218 12439 8108 1501 -218 3080 N ATOM 3099 N LYS B 45 -142.026 -87.579 602.917 1.00 78.92 N ANISOU 3099 N LYS B 45 9870 12701 7416 1721 -925 2001 N ATOM 3100 CA LYS B 45 -143.321 -88.242 603.013 1.00 80.28 C ANISOU 3100 CA LYS B 45 9782 13084 7636 1828 -1068 1758 C ATOM 3101 C LYS B 45 -143.509 -88.944 604.365 1.00 81.08 C ANISOU 3101 C LYS B 45 9643 13198 7964 1692 -1040 1536 C ATOM 3102 O LYS B 45 -144.497 -89.653 604.570 1.00 81.81 O ANISOU 3102 O LYS B 45 9518 13449 8117 1713 -1109 1298 O ATOM 3103 CB LYS B 45 -143.479 -89.246 601.871 1.00 79.45 C ANISOU 3103 CB LYS B 45 9568 13234 7383 1782 -1096 1629 C ATOM 3104 N ASN B 46 -142.550 -88.743 605.271 1.00 79.85 N ANISOU 3104 N ASN B 46 9540 12875 7925 1540 -925 1614 N ATOM 3105 CA ASN B 46 -142.599 -89.254 606.648 1.00 75.71 C ANISOU 3105 CA ASN B 46 8830 12326 7610 1410 -892 1441 C ATOM 3106 C ASN B 46 -142.670 -90.770 606.779 1.00 71.27 C ANISOU 3106 C ASN B 46 8044 11936 7100 1223 -856 1169 C ATOM 3107 O ASN B 46 -143.170 -91.295 607.776 1.00 69.70 O ANISOU 3107 O ASN B 46 7693 11736 7054 1157 -852 976 O ATOM 3108 CB ASN B 46 -143.772 -88.632 607.408 1.00 77.19 C ANISOU 3108 CB ASN B 46 8955 12454 7918 1594 -999 1380 C ATOM 3109 CG ASN B 46 -143.498 -87.205 607.821 1.00 80.12 C ANISOU 3109 CG ASN B 46 9533 12579 8330 1729 -981 1633 C ATOM 3110 OD1 ASN B 46 -142.358 -86.743 607.765 1.00 80.39 O ANISOU 3110 OD1 ASN B 46 9750 12469 8326 1638 -856 1842 O ATOM 3111 ND2 ASN B 46 -144.536 -86.503 608.260 1.00 81.57 N ANISOU 3111 ND2 ASN B 46 9694 12697 8601 1935 -1082 1607 N ATOM 3112 N ARG B 47 -142.164 -91.473 605.776 1.00 69.80 N ANISOU 3112 N ARG B 47 7860 11872 6788 1133 -810 1156 N ATOM 3113 CA ARG B 47 -141.944 -92.902 605.910 1.00 66.80 C ANISOU 3113 CA ARG B 47 7310 11606 6466 937 -730 937 C ATOM 3114 C ARG B 47 -140.739 -93.106 606.815 1.00 58.03 C ANISOU 3114 C ARG B 47 6208 10374 5468 740 -615 962 C ATOM 3115 O ARG B 47 -139.875 -92.236 606.907 1.00 58.33 O ANISOU 3115 O ARG B 47 6391 10291 5482 726 -577 1165 O ATOM 3116 CB ARG B 47 -141.717 -93.558 604.547 1.00 74.95 C ANISOU 3116 CB ARG B 47 8334 12804 7341 907 -713 919 C ATOM 3117 CG ARG B 47 -142.946 -94.223 603.957 1.00 84.42 C ANISOU 3117 CG ARG B 47 9390 14201 8483 994 -778 731 C ATOM 3118 CD ARG B 47 -143.802 -94.879 605.027 1.00 89.96 C ANISOU 3118 CD ARG B 47 9935 14906 9339 948 -759 497 C ATOM 3119 NE ARG B 47 -145.103 -95.264 604.492 1.00 98.54 N ANISOU 3119 NE ARG B 47 10899 16183 10357 1057 -824 326 N ATOM 3120 CZ ARG B 47 -146.216 -94.560 604.668 1.00104.83 C ANISOU 3120 CZ ARG B 47 11674 16999 11156 1240 -940 299 C ATOM 3121 NH1 ARG B 47 -146.185 -93.436 605.373 1.00104.47 N ANISOU 3121 NH1 ARG B 47 11730 16775 11188 1338 -1001 442 N ATOM 3122 NH2 ARG B 47 -147.359 -94.979 604.141 1.00109.87 N ANISOU 3122 NH2 ARG B 47 12180 17844 11721 1330 -989 119 N ATOM 3123 N GLN B 48 -140.685 -94.246 607.491 1.00 49.43 N ANISOU 3123 N GLN B 48 4982 9308 4491 589 -545 759 N ATOM 3124 CA GLN B 48 -139.531 -94.570 608.316 1.00 42.14 C ANISOU 3124 CA GLN B 48 4055 8292 3664 410 -444 759 C ATOM 3125 C GLN B 48 -138.854 -95.806 607.752 1.00 38.30 C ANISOU 3125 C GLN B 48 3503 7901 3148 266 -352 654 C ATOM 3126 O GLN B 48 -139.496 -96.832 607.529 1.00 40.57 O ANISOU 3126 O GLN B 48 3699 8279 3435 250 -329 480 O ATOM 3127 CB GLN B 48 -139.937 -94.799 609.770 1.00 37.57 C ANISOU 3127 CB GLN B 48 3415 7606 3253 366 -430 625 C ATOM 3128 CG GLN B 48 -140.502 -93.581 610.468 1.00 39.79 C ANISOU 3128 CG GLN B 48 3736 7782 3601 493 -514 718 C ATOM 3129 CD GLN B 48 -140.702 -93.822 611.951 1.00 42.78 C ANISOU 3129 CD GLN B 48 4060 8038 4155 412 -484 582 C ATOM 3130 OE1 GLN B 48 -140.271 -94.843 612.486 1.00 45.27 O ANISOU 3130 OE1 GLN B 48 4355 8322 4525 265 -395 450 O ATOM 3131 NE2 GLN B 48 -141.350 -92.883 612.623 1.00 41.33 N ANISOU 3131 NE2 GLN B 48 3875 7769 4058 519 -555 617 N ATOM 3132 N VAL B 49 -137.556 -95.711 607.510 1.00 33.45 N ANISOU 3132 N VAL B 49 2939 7266 2506 159 -290 753 N ATOM 3133 CA VAL B 49 -136.836 -96.832 606.940 1.00 35.46 C ANISOU 3133 CA VAL B 49 3122 7605 2747 33 -213 654 C ATOM 3134 C VAL B 49 -135.580 -97.146 607.744 1.00 33.83 C ANISOU 3134 C VAL B 49 2895 7320 2639 -116 -136 630 C ATOM 3135 O VAL B 49 -134.752 -96.268 608.018 1.00 32.82 O ANISOU 3135 O VAL B 49 2852 7113 2505 -157 -121 758 O ATOM 3136 CB VAL B 49 -136.491 -96.565 605.455 1.00 43.09 C ANISOU 3136 CB VAL B 49 4158 8662 3551 53 -225 761 C ATOM 3137 CG1 VAL B 49 -136.045 -95.139 605.269 1.00 47.40 C ANISOU 3137 CG1 VAL B 49 4894 9104 4012 101 -234 991 C ATOM 3138 CG2 VAL B 49 -135.424 -97.536 604.956 1.00 38.34 C ANISOU 3138 CG2 VAL B 49 3493 8117 2958 -100 -147 679 C ATOM 3139 N CYS B 50 -135.469 -98.410 608.144 1.00 32.44 N ANISOU 3139 N CYS B 50 2623 7159 2543 -192 -72 459 N ATOM 3140 CA CYS B 50 -134.325 -98.900 608.892 1.00 29.52 C ANISOU 3140 CA CYS B 50 2248 6700 2270 -300 -25 401 C ATOM 3141 C CYS B 50 -133.110 -99.039 608.002 1.00 29.34 C ANISOU 3141 C CYS B 50 2197 6746 2205 -386 -36 424 C ATOM 3142 O CYS B 50 -133.207 -99.579 606.904 1.00 31.57 O ANISOU 3142 O CYS B 50 2442 7135 2420 -393 -33 393 O ATOM 3143 CB CYS B 50 -134.644-100.249 609.533 1.00 30.29 C ANISOU 3143 CB CYS B 50 2438 6620 2449 -300 5 214 C ATOM 3144 SG CYS B 50 -136.070-100.232 610.653 1.00 31.32 S ANISOU 3144 SG CYS B 50 2612 6689 2601 -233 6 144 S ATOM 3145 N ALA B 51 -131.967 -98.563 608.487 1.00 30.02 N ANISOU 3145 N ALA B 51 2339 6753 2314 -455 -40 457 N ATOM 3146 CA ALA B 51 -130.708 -98.685 607.765 1.00 34.01 C ANISOU 3146 CA ALA B 51 2895 7254 2774 -543 -4 441 C ATOM 3147 C ALA B 51 -129.598 -99.198 608.680 1.00 35.32 C ANISOU 3147 C ALA B 51 3089 7320 3011 -592 -11 317 C ATOM 3148 O ALA B 51 -129.684 -99.086 609.907 1.00 33.93 O ANISOU 3148 O ALA B 51 2948 7048 2894 -560 -33 291 O ATOM 3149 CB ALA B 51 -130.319 -97.353 607.151 1.00 26.55 C ANISOU 3149 CB ALA B 51 2079 6268 1742 -573 79 607 C ATOM 3150 N ASN B 52 -128.559 -99.767 608.073 1.00 38.53 N ANISOU 3150 N ASN B 52 3503 7742 3396 -653 20 236 N ATOM 3151 CA ASN B 52 -127.417-100.313 608.803 1.00 34.30 C ANISOU 3151 CA ASN B 52 3000 7120 2910 -670 35 109 C ATOM 3152 C ASN B 52 -126.420 -99.230 609.151 1.00 33.54 C ANISOU 3152 C ASN B 52 2932 6948 2863 -739 126 136 C ATOM 3153 O ASN B 52 -125.837 -98.633 608.262 1.00 39.22 O ANISOU 3153 O ASN B 52 3664 7695 3544 -826 211 179 O ATOM 3154 CB ASN B 52 -126.731-101.391 607.970 1.00 37.09 C ANISOU 3154 CB ASN B 52 3330 7539 3226 -701 38 -2 C ATOM 3155 CG ASN B 52 -125.754-102.213 608.770 1.00 41.45 C ANISOU 3155 CG ASN B 52 3906 8022 3822 -672 46 -140 C ATOM 3156 OD1 ASN B 52 -125.205-101.753 609.766 1.00 42.07 O ANISOU 3156 OD1 ASN B 52 4006 8020 3959 -658 72 -156 O ATOM 3157 ND2 ASN B 52 -125.532-103.448 608.336 1.00 46.41 N ANISOU 3157 ND2 ASN B 52 4522 8680 4433 -656 36 -241 N ATOM 3158 N PRO B 53 -126.205 -98.987 610.450 1.00 34.60 N ANISOU 3158 N PRO B 53 3086 6978 3081 -708 125 98 N ATOM 3159 CA PRO B 53 -125.288 -97.942 610.927 1.00 36.28 C ANISOU 3159 CA PRO B 53 3303 7114 3368 -782 215 92 C ATOM 3160 C PRO B 53 -123.827 -98.194 610.554 1.00 36.49 C ANISOU 3160 C PRO B 53 3297 7168 3399 -854 279 -34 C ATOM 3161 O PRO B 53 -122.993 -97.291 610.674 1.00 35.48 O ANISOU 3161 O PRO B 53 3162 6997 3322 -946 377 -59 O ATOM 3162 CB PRO B 53 -125.453 -97.990 612.451 1.00 35.37 C ANISOU 3162 CB PRO B 53 3199 6900 3341 -709 173 42 C ATOM 3163 CG PRO B 53 -126.693 -98.761 612.698 1.00 36.07 C ANISOU 3163 CG PRO B 53 3319 6995 3391 -610 86 68 C ATOM 3164 CD PRO B 53 -126.849 -99.705 611.561 1.00 35.43 C ANISOU 3164 CD PRO B 53 3223 7023 3216 -607 55 48 C ATOM 3165 N GLU B 54 -123.521 -99.413 610.123 1.00 35.45 N ANISOU 3165 N GLU B 54 3142 7108 3219 -817 233 -128 N ATOM 3166 CA GLU B 54 -122.150 -99.772 609.791 1.00 36.23 C ANISOU 3166 CA GLU B 54 3194 7254 3319 -870 284 -266 C ATOM 3167 C GLU B 54 -121.807 -99.349 608.367 1.00 41.44 C ANISOU 3167 C GLU B 54 3853 7978 3916 -994 370 -230 C ATOM 3168 O GLU B 54 -120.644 -99.115 608.049 1.00 46.85 O ANISOU 3168 O GLU B 54 4505 8685 4612 -1085 455 -327 O ATOM 3169 CB GLU B 54 -121.928-101.278 609.969 1.00 32.86 C ANISOU 3169 CB GLU B 54 2749 6869 2869 -773 217 -383 C ATOM 3170 N LYS B 55 -122.824 -99.244 607.516 1.00 40.41 N ANISOU 3170 N LYS B 55 3760 7882 3710 -995 354 -96 N ATOM 3171 CA LYS B 55 -122.630 -98.871 606.115 1.00 39.90 C ANISOU 3171 CA LYS B 55 3727 7876 3558 -1097 442 -38 C ATOM 3172 C LYS B 55 -122.078 -97.460 605.964 1.00 43.30 C ANISOU 3172 C LYS B 55 4228 8228 3996 -1216 596 30 C ATOM 3173 O LYS B 55 -122.444 -96.551 606.707 1.00 45.38 O ANISOU 3173 O LYS B 55 4536 8395 4310 -1209 624 113 O ATOM 3174 CB LYS B 55 -123.942 -98.992 605.345 1.00 41.30 C ANISOU 3174 CB LYS B 55 3933 8116 3644 -1044 385 97 C ATOM 3175 CG LYS B 55 -124.400-100.422 605.120 1.00 43.62 C ANISOU 3175 CG LYS B 55 4157 8495 3921 -971 273 8 C ATOM 3176 CD LYS B 55 -123.450-101.141 604.186 1.00 49.45 C ANISOU 3176 CD LYS B 55 4862 9306 4620 -1044 314 -109 C ATOM 3177 CE LYS B 55 -123.811-102.611 604.037 1.00 53.02 C ANISOU 3177 CE LYS B 55 5259 9816 5068 -980 224 -213 C ATOM 3178 NZ LYS B 55 -122.975-103.273 602.984 1.00 56.25 N ANISOU 3178 NZ LYS B 55 5634 10307 5431 -1056 269 -319 N ATOM 3179 N LYS B 56 -121.194 -97.286 604.988 1.00 45.43 N ANISOU 3179 N LYS B 56 4519 8529 4214 -1336 709 -13 N ATOM 3180 CA LYS B 56 -120.555 -95.999 604.750 1.00 47.51 C ANISOU 3180 CA LYS B 56 4874 8701 4478 -1473 890 33 C ATOM 3181 C LYS B 56 -121.567 -94.942 604.328 1.00 47.78 C ANISOU 3181 C LYS B 56 5077 8653 4423 -1463 957 275 C ATOM 3182 O LYS B 56 -121.489 -93.800 604.778 1.00 51.52 O ANISOU 3182 O LYS B 56 5642 8994 4940 -1516 1071 348 O ATOM 3183 CB LYS B 56 -119.456 -96.125 603.685 1.00 48.92 C ANISOU 3183 CB LYS B 56 5049 8936 4601 -1607 1003 -68 C ATOM 3184 N TRP B 57 -122.516 -95.312 603.471 1.00 45.32 N ANISOU 3184 N TRP B 57 4816 8420 3984 -1385 885 394 N ATOM 3185 CA TRP B 57 -123.501 -94.340 603.000 1.00 46.58 C ANISOU 3185 CA TRP B 57 5160 8516 4023 -1336 928 631 C ATOM 3186 C TRP B 57 -124.395 -93.846 604.139 1.00 48.15 C ANISOU 3186 C TRP B 57 5363 8638 4294 -1237 858 720 C ATOM 3187 O TRP B 57 -124.830 -92.694 604.136 1.00 52.97 O ANISOU 3187 O TRP B 57 6145 9127 4853 -1226 942 897 O ATOM 3188 CB TRP B 57 -124.351 -94.918 601.857 1.00 43.69 C ANISOU 3188 CB TRP B 57 4824 8280 3497 -1249 838 712 C ATOM 3189 CG TRP B 57 -125.396 -95.953 602.222 1.00 41.52 C ANISOU 3189 CG TRP B 57 4399 8124 3252 -1109 638 668 C ATOM 3190 CD1 TRP B 57 -125.266 -97.315 602.148 1.00 41.33 C ANISOU 3190 CD1 TRP B 57 4208 8220 3276 -1098 539 501 C ATOM 3191 CD2 TRP B 57 -126.743 -95.705 602.649 1.00 39.63 C ANISOU 3191 CD2 TRP B 57 4174 7890 2994 -962 529 788 C ATOM 3192 NE1 TRP B 57 -126.440 -97.927 602.526 1.00 37.40 N ANISOU 3192 NE1 TRP B 57 3623 7788 2801 -971 396 504 N ATOM 3193 CE2 TRP B 57 -127.361 -96.961 602.837 1.00 36.00 C ANISOU 3193 CE2 TRP B 57 3539 7555 2586 -886 384 669 C ATOM 3194 CE3 TRP B 57 -127.485 -94.545 602.900 1.00 43.07 C ANISOU 3194 CE3 TRP B 57 4759 8228 3378 -885 546 978 C ATOM 3195 CZ2 TRP B 57 -128.681 -97.086 603.271 1.00 36.19 C ANISOU 3195 CZ2 TRP B 57 3510 7620 2619 -750 268 713 C ATOM 3196 CZ3 TRP B 57 -128.801 -94.673 603.328 1.00 41.72 C ANISOU 3196 CZ3 TRP B 57 4534 8109 3208 -726 402 1030 C ATOM 3197 CH2 TRP B 57 -129.383 -95.934 603.511 1.00 38.63 C ANISOU 3197 CH2 TRP B 57 3946 7854 2877 -667 272 887 C ATOM 3198 N VAL B 58 -124.644 -94.700 605.126 1.00 40.50 N ANISOU 3198 N VAL B 58 4224 7724 3439 -1163 714 599 N ATOM 3199 CA VAL B 58 -125.502 -94.311 606.236 1.00 38.61 C ANISOU 3199 CA VAL B 58 3974 7425 3272 -1073 646 666 C ATOM 3200 C VAL B 58 -124.804 -93.303 607.144 1.00 43.04 C ANISOU 3200 C VAL B 58 4570 7832 3952 -1167 772 646 C ATOM 3201 O VAL B 58 -125.410 -92.316 607.576 1.00 45.40 O ANISOU 3201 O VAL B 58 4965 8026 4261 -1146 814 787 O ATOM 3202 CB VAL B 58 -125.937 -95.527 607.063 1.00 33.69 C ANISOU 3202 CB VAL B 58 3187 6883 2730 -974 476 536 C ATOM 3203 CG1 VAL B 58 -126.621 -95.083 608.351 1.00 35.69 C ANISOU 3203 CG1 VAL B 58 3423 7060 3076 -907 429 575 C ATOM 3204 CG2 VAL B 58 -126.849 -96.417 606.240 1.00 29.46 C ANISOU 3204 CG2 VAL B 58 2611 6485 2098 -885 365 555 C ATOM 3205 N ARG B 59 -123.528 -93.544 607.427 1.00 43.41 N ANISOU 3205 N ARG B 59 4535 7869 4091 -1266 830 461 N ATOM 3206 CA ARG B 59 -122.773 -92.645 608.290 1.00 48.75 C ANISOU 3206 CA ARG B 59 5212 8416 4894 -1362 948 394 C ATOM 3207 C ARG B 59 -122.523 -91.307 607.601 1.00 50.71 C ANISOU 3207 C ARG B 59 5647 8529 5091 -1486 1164 528 C ATOM 3208 O ARG B 59 -122.471 -90.265 608.256 1.00 51.38 O ANISOU 3208 O ARG B 59 5793 8465 5262 -1543 1272 565 O ATOM 3209 CB ARG B 59 -121.456 -93.290 608.710 1.00 53.99 C ANISOU 3209 CB ARG B 59 5734 9133 5646 -1412 935 147 C ATOM 3210 CG ARG B 59 -121.651 -94.497 609.610 1.00 58.98 C ANISOU 3210 CG ARG B 59 6239 9843 6326 -1273 744 31 C ATOM 3211 CD ARG B 59 -120.340 -95.176 609.931 1.00 64.89 C ANISOU 3211 CD ARG B 59 6880 10655 7119 -1291 726 -194 C ATOM 3212 NE ARG B 59 -119.579 -95.482 608.726 1.00 72.25 N ANISOU 3212 NE ARG B 59 7808 11668 7977 -1380 796 -250 N ATOM 3213 CZ ARG B 59 -118.547 -96.317 608.693 1.00 77.43 C ANISOU 3213 CZ ARG B 59 8368 12417 8634 -1379 765 -438 C ATOM 3214 NH1 ARG B 59 -118.169 -96.943 609.803 1.00 79.82 N ANISOU 3214 NH1 ARG B 59 8590 12744 8994 -1276 666 -572 N ATOM 3215 NH2 ARG B 59 -117.905 -96.537 607.552 1.00 78.26 N ANISOU 3215 NH2 ARG B 59 8470 12594 8673 -1473 837 -490 N ATOM 3216 N GLU B 60 -122.384 -91.346 606.279 1.00 50.20 N ANISOU 3216 N GLU B 60 5688 8501 4884 -1524 1233 602 N ATOM 3217 CA GLU B 60 -122.223 -90.135 605.487 1.00 52.94 C ANISOU 3217 CA GLU B 60 6267 8703 5145 -1618 1444 761 C ATOM 3218 C GLU B 60 -123.520 -89.333 605.497 1.00 55.76 C ANISOU 3218 C GLU B 60 6818 8954 5415 -1504 1434 1024 C ATOM 3219 O GLU B 60 -123.507 -88.104 605.638 1.00 57.36 O ANISOU 3219 O GLU B 60 7199 8960 5634 -1558 1600 1149 O ATOM 3220 CB GLU B 60 -121.812 -90.478 604.055 1.00 51.82 C ANISOU 3220 CB GLU B 60 6199 8639 4851 -1666 1502 777 C ATOM 3221 N TYR B 61 -124.637 -90.041 605.348 1.00 54.61 N ANISOU 3221 N TYR B 61 6632 8940 5180 -1338 1234 1101 N ATOM 3222 CA TYR B 61 -125.959 -89.430 605.413 1.00 55.34 C ANISOU 3222 CA TYR B 61 6868 8976 5184 -1185 1162 1331 C ATOM 3223 C TYR B 61 -126.194 -88.744 606.758 1.00 59.20 C ANISOU 3223 C TYR B 61 7326 9335 5832 -1194 1183 1342 C ATOM 3224 O TYR B 61 -126.721 -87.631 606.817 1.00 60.12 O ANISOU 3224 O TYR B 61 7645 9283 5915 -1156 1259 1541 O ATOM 3225 CB TYR B 61 -127.037 -90.484 605.160 1.00 49.63 C ANISOU 3225 CB TYR B 61 6024 8456 4380 -1005 921 1337 C ATOM 3226 CG TYR B 61 -127.411 -90.629 603.705 1.00 54.23 C ANISOU 3226 CG TYR B 61 6739 9115 4749 -930 893 1446 C ATOM 3227 CD1 TYR B 61 -126.452 -90.539 602.706 1.00 58.29 C ANISOU 3227 CD1 TYR B 61 7360 9607 5182 -1059 1047 1424 C ATOM 3228 CD2 TYR B 61 -128.725 -90.858 603.327 1.00 56.25 C ANISOU 3228 CD2 TYR B 61 7006 9476 4892 -726 712 1549 C ATOM 3229 CE1 TYR B 61 -126.792 -90.668 601.370 1.00 61.25 C ANISOU 3229 CE1 TYR B 61 7866 10056 5352 -991 1024 1520 C ATOM 3230 CE2 TYR B 61 -129.076 -90.991 601.995 1.00 60.36 C ANISOU 3230 CE2 TYR B 61 7639 10078 5218 -649 675 1626 C ATOM 3231 CZ TYR B 61 -128.106 -90.893 601.022 1.00 62.43 C ANISOU 3231 CZ TYR B 61 8024 10310 5385 -785 832 1620 C ATOM 3232 OH TYR B 61 -128.452 -91.025 599.699 1.00 64.17 O ANISOU 3232 OH TYR B 61 8366 10616 5400 -711 798 1695 O ATOM 3233 N ILE B 62 -125.794 -89.418 607.833 1.00 59.92 N ANISOU 3233 N ILE B 62 7178 9493 6094 -1231 1110 1127 N ATOM 3234 CA ILE B 62 -125.915 -88.882 609.185 1.00 60.89 C ANISOU 3234 CA ILE B 62 7239 9511 6385 -1251 1124 1090 C ATOM 3235 C ILE B 62 -125.092 -87.602 609.343 1.00 64.46 C ANISOU 3235 C ILE B 62 7828 9742 6923 -1417 1369 1094 C ATOM 3236 O ILE B 62 -125.597 -86.595 609.845 1.00 65.04 O ANISOU 3236 O ILE B 62 8019 9648 7043 -1419 1443 1224 O ATOM 3237 CB ILE B 62 -125.478 -89.925 610.236 1.00 58.88 C ANISOU 3237 CB ILE B 62 6728 9364 6280 -1243 996 836 C ATOM 3238 CG1 ILE B 62 -126.508 -91.055 610.316 1.00 56.11 C ANISOU 3238 CG1 ILE B 62 6268 9177 5873 -1075 777 845 C ATOM 3239 CG2 ILE B 62 -125.292 -89.279 611.600 1.00 58.42 C ANISOU 3239 CG2 ILE B 62 6613 9182 6404 -1293 1041 752 C ATOM 3240 CD1 ILE B 62 -126.108 -92.191 611.232 1.00 52.82 C ANISOU 3240 CD1 ILE B 62 5667 8834 5567 -1041 652 621 C ATOM 3241 N ASN B 63 -123.836 -87.646 608.896 1.00 64.87 N ANISOU 3241 N ASN B 63 7859 9790 6999 -1555 1496 950 N ATOM 3242 CA ASN B 63 -122.953 -86.480 608.920 1.00 63.90 C ANISOU 3242 CA ASN B 63 7846 9475 6958 -1720 1735 928 C ATOM 3243 C ASN B 63 -123.521 -85.288 608.167 1.00 62.78 C ANISOU 3243 C ASN B 63 8025 9130 6699 -1713 1895 1215 C ATOM 3244 O ASN B 63 -123.332 -84.143 608.574 1.00 65.73 O ANISOU 3244 O ASN B 63 8512 9294 7169 -1801 2053 1256 O ATOM 3245 CB ASN B 63 -121.579 -86.822 608.335 1.00 69.47 C ANISOU 3245 CB ASN B 63 8471 10258 7666 -1854 1816 739 C ATOM 3246 CG ASN B 63 -120.743 -87.684 609.259 1.00 72.20 C ANISOU 3246 CG ASN B 63 8540 10744 8148 -1869 1693 442 C ATOM 3247 OD1 ASN B 63 -120.966 -87.718 610.470 1.00 72.78 O ANISOU 3247 OD1 ASN B 63 8499 10808 8346 -1818 1602 361 O ATOM 3248 ND2 ASN B 63 -119.759 -88.376 608.692 1.00 73.36 N ANISOU 3248 ND2 ASN B 63 8592 11020 8261 -1929 1687 280 N ATOM 3249 N SER B 64 -124.201 -85.559 607.059 1.00 59.73 N ANISOU 3249 N SER B 64 7793 8804 6099 -1593 1837 1408 N ATOM 3250 CA SER B 64 -124.807 -84.501 606.261 1.00 62.70 C ANISOU 3250 CA SER B 64 8509 8992 6323 -1522 1951 1711 C ATOM 3251 C SER B 64 -125.921 -83.785 607.017 1.00 65.25 C ANISOU 3251 C SER B 64 8950 9163 6677 -1405 1899 1887 C ATOM 3252 O SER B 64 -126.015 -82.558 607.000 1.00 69.19 O ANISOU 3252 O SER B 64 9675 9417 7196 -1422 2045 2057 O ATOM 3253 CB SER B 64 -125.356 -85.070 604.955 1.00 62.32 C ANISOU 3253 CB SER B 64 8585 9074 6020 -1376 1848 1848 C ATOM 3254 OG SER B 64 -126.105 -84.093 604.252 1.00 66.10 O ANISOU 3254 OG SER B 64 9410 9377 6328 -1235 1908 2156 O ATOM 3255 N LEU B 65 -126.761 -84.563 607.688 1.00 64.48 N ANISOU 3255 N LEU B 65 8659 9238 6603 -1281 1655 1848 N ATOM 3256 CA LEU B 65 -127.926 -84.019 608.366 1.00 65.49 C ANISOU 3256 CA LEU B 65 8840 9255 6787 -1101 1540 2005 C ATOM 3257 C LEU B 65 -127.554 -83.142 609.561 1.00 73.59 C ANISOU 3257 C LEU B 65 9858 10042 8063 -1232 1688 1897 C ATOM 3258 O LEU B 65 -128.377 -82.365 610.044 1.00 78.55 O ANISOU 3258 O LEU B 65 10600 10462 8782 -1082 1653 2005 O ATOM 3259 CB LEU B 65 -128.844 -85.157 608.804 1.00 57.07 C ANISOU 3259 CB LEU B 65 7513 8426 5744 -902 1236 1920 C ATOM 3260 CG LEU B 65 -129.464 -85.917 607.633 1.00 54.04 C ANISOU 3260 CG LEU B 65 7146 8271 5115 -740 1078 2030 C ATOM 3261 CD1 LEU B 65 -129.860 -87.315 608.045 1.00 54.00 C ANISOU 3261 CD1 LEU B 65 6836 8538 5143 -672 861 1849 C ATOM 3262 CD2 LEU B 65 -130.672 -85.169 607.119 1.00 54.12 C ANISOU 3262 CD2 LEU B 65 7383 8171 5011 -465 980 2282 C ATOM 3263 N GLU B 66 -126.314 -83.257 610.028 1.00 75.39 N ANISOU 3263 N GLU B 66 9937 10306 8403 -1500 1849 1663 N ATOM 3264 CA GLU B 66 -125.843 -82.426 611.132 1.00 77.26 C ANISOU 3264 CA GLU B 66 10133 10344 8878 -1633 1990 1518 C ATOM 3265 C GLU B 66 -125.516 -81.009 610.654 1.00 81.00 C ANISOU 3265 C GLU B 66 10900 10509 9366 -1707 2218 1639 C ATOM 3266 O GLU B 66 -125.922 -80.024 611.274 1.00 83.53 O ANISOU 3266 O GLU B 66 11354 10574 9809 -1694 2297 1691 O ATOM 3267 CB GLU B 66 -124.613 -83.053 611.793 1.00 78.89 C ANISOU 3267 CB GLU B 66 10027 10709 9240 -1764 1973 1175 C ATOM 3268 CG GLU B 66 -124.709 -84.555 612.016 1.00 78.35 C ANISOU 3268 CG GLU B 66 9697 10933 9140 -1668 1739 1038 C ATOM 3269 CD GLU B 66 -125.468 -84.934 613.274 1.00 79.06 C ANISOU 3269 CD GLU B 66 9614 11087 9338 -1580 1569 975 C ATOM 3270 OE1 GLU B 66 -126.519 -84.324 613.557 1.00 78.92 O ANISOU 3270 OE1 GLU B 66 9713 10932 9340 -1479 1536 1142 O ATOM 3271 OE2 GLU B 66 -125.011 -85.854 613.983 1.00 79.59 O ANISOU 3271 OE2 GLU B 66 9448 11306 9488 -1553 1433 749 O ATOM 3272 N MET B 67 -124.784 -80.915 609.547 1.00 80.02 N ANISOU 3272 N MET B 67 10878 10405 9122 -1781 2318 1669 N ATOM 3273 CA MET B 67 -124.363 -79.625 609.005 1.00 77.67 C ANISOU 3273 CA MET B 67 10862 9833 8816 -1879 2533 1755 C ATOM 3274 C MET B 67 -125.555 -78.802 608.516 1.00 77.46 C ANISOU 3274 C MET B 67 11191 9567 8672 -1675 2521 2087 C ATOM 3275 O MET B 67 -126.674 -79.309 608.404 1.00 75.45 O ANISOU 3275 O MET B 67 10965 9397 8305 -1443 2330 2258 O ATOM 3276 CB MET B 67 -123.358 -79.828 607.866 1.00 73.30 C ANISOU 3276 CB MET B 67 10336 9377 8139 -2001 2635 1709 C TER 3277 MET B 67 HETATM 3278 ZN ZN A1101 -144.259-116.972 688.920 0.85 35.30 ZN HETATM 3279 C9 OLC A1102 -121.171-104.816 637.704 1.00 30.77 C HETATM 3280 C8 OLC A1102 -120.780-104.626 636.252 1.00 30.38 C HETATM 3281 C24 OLC A1102 -119.114-108.377 624.118 1.00 77.46 C HETATM 3282 C7 OLC A1102 -121.060-105.887 635.456 1.00 34.75 C HETATM 3283 C6 OLC A1102 -120.212-105.879 634.199 1.00 37.41 C HETATM 3284 C5 OLC A1102 -120.650-106.963 633.240 1.00 41.15 C HETATM 3285 C4 OLC A1102 -119.772-106.911 632.006 1.00 47.61 C HETATM 3286 C3 OLC A1102 -120.289-107.849 630.932 1.00 51.42 C HETATM 3287 C2 OLC A1102 -119.257-107.934 629.827 1.00 56.28 C HETATM 3288 C21 OLC A1102 -119.949-109.124 626.327 1.00 71.14 C HETATM 3289 C1 OLC A1102 -119.784-108.710 628.638 1.00 62.75 C HETATM 3290 C22 OLC A1102 -118.806-109.217 625.340 1.00 76.26 C HETATM 3291 O19 OLC A1102 -120.347-109.774 628.795 1.00 66.71 O HETATM 3292 O25 OLC A1102 -118.069-108.505 623.179 1.00 78.28 O HETATM 3293 O23 OLC A1102 -117.618-108.760 625.950 1.00 79.01 O HETATM 3294 O20 OLC A1102 -119.615-108.205 627.341 1.00 66.89 O HETATM 3295 C24 OLC A1103 -146.044 -81.426 632.699 1.00 70.21 C HETATM 3296 C6 OLC A1103 -142.375 -83.319 642.815 1.00 47.08 C HETATM 3297 C5 OLC A1103 -142.386 -82.566 641.502 1.00 49.37 C HETATM 3298 C4 OLC A1103 -143.609 -82.962 640.704 1.00 53.65 C HETATM 3299 C3 OLC A1103 -143.495 -82.429 639.288 1.00 58.45 C HETATM 3300 C2 OLC A1103 -144.833 -82.556 638.581 1.00 63.18 C HETATM 3301 C21 OLC A1103 -145.518 -82.503 634.879 1.00 67.88 C HETATM 3302 C1 OLC A1103 -144.654 -82.426 637.081 1.00 64.91 C HETATM 3303 C22 OLC A1103 -146.620 -81.939 634.003 1.00 70.94 C HETATM 3304 O19 OLC A1103 -143.546 -82.537 636.604 1.00 65.76 O HETATM 3305 O25 OLC A1103 -147.083 -81.034 631.823 1.00 69.30 O HETATM 3306 O23 OLC A1103 -147.564 -82.947 633.724 1.00 74.98 O HETATM 3307 O20 OLC A1103 -145.751 -82.180 636.233 1.00 66.58 O HETATM 3308 C10 OLC A1104 -140.545-115.047 639.760 1.00 65.35 C HETATM 3309 C9 OLC A1104 -141.013-115.321 638.523 1.00 61.76 C HETATM 3310 C11 OLC A1104 -140.878-113.742 640.454 1.00 66.75 C HETATM 3311 C8 OLC A1104 -141.883-114.331 637.781 1.00 56.28 C HETATM 3312 C24 OLC A1104 -142.531-113.475 624.620 1.00 64.61 C HETATM 3313 C12 OLC A1104 -140.003-113.590 641.682 1.00 65.92 C HETATM 3314 C7 OLC A1104 -141.175-113.930 636.506 1.00 50.36 C HETATM 3315 C13 OLC A1104 -140.407-114.585 642.747 1.00 64.04 C HETATM 3316 C6 OLC A1104 -142.187-113.671 635.414 1.00 46.14 C HETATM 3317 C14 OLC A1104 -139.690-114.257 644.039 1.00 64.81 C HETATM 3318 C5 OLC A1104 -141.432-113.503 634.118 1.00 45.11 C HETATM 3319 C4 OLC A1104 -142.387-113.143 633.000 1.00 46.59 C HETATM 3320 C3 OLC A1104 -141.900-113.800 631.724 1.00 49.73 C HETATM 3321 C2 OLC A1104 -142.363-113.014 630.516 1.00 55.57 C HETATM 3322 C21 OLC A1104 -142.168-113.132 627.051 1.00 59.67 C HETATM 3323 C1 OLC A1104 -142.344-113.895 629.284 1.00 60.46 C HETATM 3324 C22 OLC A1104 -142.301-114.158 625.950 1.00 62.20 C HETATM 3325 O19 OLC A1104 -141.747-114.954 629.302 1.00 63.03 O HETATM 3326 O25 OLC A1104 -142.447-114.420 623.573 1.00 65.49 O HETATM 3327 O23 OLC A1104 -141.112-114.909 625.886 1.00 64.31 O HETATM 3328 O20 OLC A1104 -143.015-113.493 628.115 1.00 61.22 O HETATM 3329 C9 OLC A1105 -144.770-111.860 640.968 1.00 42.17 C HETATM 3330 C8 OLC A1105 -145.313-112.400 639.662 1.00 42.82 C HETATM 3331 C24 OLC A1105 -148.953-109.231 628.208 1.00 60.25 C HETATM 3332 C7 OLC A1105 -145.682-111.264 638.728 1.00 43.85 C HETATM 3333 C6 OLC A1105 -145.326-111.646 637.303 1.00 44.17 C HETATM 3334 C5 OLC A1105 -145.888-110.640 636.315 1.00 41.41 C HETATM 3335 C4 OLC A1105 -145.432-111.005 634.917 1.00 38.56 C HETATM 3336 C3 OLC A1105 -146.491-110.612 633.910 1.00 39.18 C HETATM 3337 C2 OLC A1105 -145.850-110.158 632.613 1.00 42.25 C HETATM 3338 C21 OLC A1105 -146.981-110.395 629.190 1.00 55.59 C HETATM 3339 C1 OLC A1105 -146.500-110.875 631.445 1.00 50.97 C HETATM 3340 C22 OLC A1105 -148.212-110.552 628.319 1.00 59.34 C HETATM 3341 O19 OLC A1105 -146.298-112.064 631.281 1.00 56.83 O HETATM 3342 O25 OLC A1105 -149.692-108.959 629.385 1.00 57.53 O HETATM 3343 O23 OLC A1105 -147.816-111.001 627.037 1.00 58.67 O HETATM 3344 O20 OLC A1105 -147.337-110.191 630.540 1.00 52.54 O HETATM 3345 C24 OLC A1106 -149.305 -86.233 633.517 1.00 71.60 C HETATM 3346 C6 OLC A1106 -151.778 -84.250 643.507 1.00 61.44 C HETATM 3347 C5 OLC A1106 -151.371 -84.466 642.066 1.00 63.22 C HETATM 3348 C4 OLC A1106 -150.338 -85.570 641.997 1.00 64.53 C HETATM 3349 C3 OLC A1106 -149.517 -85.433 640.734 1.00 66.01 C HETATM 3350 C2 OLC A1106 -150.221 -86.110 639.578 1.00 69.88 C HETATM 3351 C21 OLC A1106 -149.014 -85.991 635.976 1.00 74.98 C HETATM 3352 C1 OLC A1106 -149.469 -85.769 638.308 1.00 74.96 C HETATM 3353 C22 OLC A1106 -149.925 -85.716 634.796 1.00 74.58 C HETATM 3354 O19 OLC A1106 -148.591 -84.931 638.351 1.00 76.43 O HETATM 3355 O25 OLC A1106 -149.912 -85.621 632.397 1.00 68.97 O HETATM 3356 O23 OLC A1106 -151.169 -86.346 634.998 1.00 76.31 O HETATM 3357 O20 OLC A1106 -149.782 -86.405 637.088 1.00 76.32 O HETATM 3358 C10 OLC A1107 -150.573-102.045 634.144 1.00 36.19 C HETATM 3359 C9 OLC A1107 -150.361-101.522 632.923 1.00 35.92 C HETATM 3360 C17 OLC A1107 -149.922-104.531 640.971 1.00 46.66 C HETATM 3361 C11 OLC A1107 -149.597-103.022 634.759 1.00 42.88 C HETATM 3362 C8 OLC A1107 -149.151-101.877 632.087 1.00 38.92 C HETATM 3363 C24 OLC A1107 -153.512-105.318 621.967 1.00 72.25 C HETATM 3364 C16 OLC A1107 -149.508-103.117 640.609 1.00 47.37 C HETATM 3365 C12 OLC A1107 -149.880-103.135 636.246 1.00 44.66 C HETATM 3366 C7 OLC A1107 -149.233-101.125 630.773 1.00 38.99 C HETATM 3367 C15 OLC A1107 -149.544-102.897 639.108 1.00 44.31 C HETATM 3368 C13 OLC A1107 -148.714-103.796 636.951 1.00 43.81 C HETATM 3369 C6 OLC A1107 -148.485-101.871 629.692 1.00 40.66 C HETATM 3370 C14 OLC A1107 -149.087-104.143 638.377 1.00 42.66 C HETATM 3371 C5 OLC A1107 -149.451-102.291 628.608 1.00 43.43 C HETATM 3372 C4 OLC A1107 -149.459-103.798 628.471 1.00 46.27 C HETATM 3373 C3 OLC A1107 -149.978-104.142 627.094 1.00 52.82 C HETATM 3374 C2 OLC A1107 -150.436-105.584 627.036 1.00 63.50 C HETATM 3375 C21 OLC A1107 -152.068-105.728 623.948 1.00 76.82 C HETATM 3376 C1 OLC A1107 -151.747-105.614 626.280 1.00 72.84 C HETATM 3377 C22 OLC A1107 -153.428-105.979 623.327 1.00 76.06 C HETATM 3378 O19 OLC A1107 -152.646-104.887 626.643 1.00 76.83 O HETATM 3379 O25 OLC A1107 -154.863-105.198 621.571 1.00 69.50 O HETATM 3380 O23 OLC A1107 -153.648-107.365 623.193 1.00 78.05 O HETATM 3381 O20 OLC A1107 -151.943-106.443 625.161 1.00 76.30 O HETATM 3382 C1 OLA A1108 -147.686-109.831 655.845 1.00 73.21 C HETATM 3383 O1 OLA A1108 -146.559-110.378 655.714 1.00 75.26 O HETATM 3384 O2 OLA A1108 -148.261-109.848 656.967 1.00 73.03 O HETATM 3385 C2 OLA A1108 -148.339-109.159 654.654 1.00 70.60 C HETATM 3386 C3 OLA A1108 -147.276-108.535 653.773 1.00 67.33 C HETATM 3387 C4 OLA A1108 -147.454-107.032 653.745 1.00 63.55 C HETATM 3388 C5 OLA A1108 -148.453-106.658 652.672 1.00 59.94 C HETATM 3389 C6 OLA A1108 -147.739-106.570 651.342 1.00 56.89 C HETATM 3390 C7 OLA A1108 -148.475-105.593 650.453 1.00 52.75 C HETATM 3391 C8 OLA A1108 -148.191-105.928 649.007 1.00 48.68 C HETATM 3392 C9 OLA A1108 -149.350-105.460 648.152 1.00 46.03 C HETATM 3393 C10 OLA A1108 -149.942-104.271 648.390 1.00 44.75 C HETATM 3394 C1 OLA A1109 -144.620-112.101 652.403 1.00 77.77 C HETATM 3395 O1 OLA A1109 -144.500-113.264 651.932 1.00 78.85 O HETATM 3396 O2 OLA A1109 -143.983-111.778 653.441 1.00 77.19 O HETATM 3397 C2 OLA A1109 -145.526-111.101 651.715 1.00 76.24 C HETATM 3398 C3 OLA A1109 -146.314-111.801 650.629 1.00 75.44 C HETATM 3399 C4 OLA A1109 -147.044-110.773 649.793 1.00 76.25 C HETATM 3400 C5 OLA A1109 -148.105-110.088 650.628 1.00 76.55 C HETATM 3401 C6 OLA A1109 -149.438-110.777 650.423 1.00 75.85 C HETATM 3402 O HOH A1201 -133.453-108.893 671.155 1.00 40.45 O HETATM 3403 O HOH A1202 -130.866-100.250 618.618 1.00 19.08 O HETATM 3404 O HOH A1203 -141.916-125.732 689.749 1.00 41.19 O HETATM 3405 O HOH A1204 -140.214 -99.970 629.455 1.00 22.19 O HETATM 3406 O HOH A1205 -135.492-106.474 619.393 1.00 32.16 O HETATM 3407 O HOH A1206 -134.486 -91.078 623.224 1.00 28.53 O HETATM 3408 O HOH A1207 -135.843 -96.660 646.254 1.00 22.98 O HETATM 3409 O HOH A1208 -126.950 -96.426 619.238 1.00 27.65 O HETATM 3410 O HOH A1209 -128.901 -97.073 630.300 1.00 16.96 O HETATM 3411 O HOH A1210 -138.023 -94.578 627.363 1.00 31.99 O HETATM 3412 O HOH A1211 -130.382-109.945 616.985 1.00 36.70 O HETATM 3413 O HOH A1212 -137.066 -99.215 630.075 1.00 17.69 O HETATM 3414 O HOH A1213 -146.847-110.569 618.721 1.00 54.11 O HETATM 3415 O HOH A1214 -139.855-103.983 650.177 1.00 22.33 O HETATM 3416 O HOH A1215 -137.890 -82.866 624.964 1.00 33.79 O HETATM 3417 O HOH A1216 -138.069 -96.443 655.004 1.00 20.77 O HETATM 3418 O HOH A1217 -129.385-108.124 621.469 1.00 49.51 O HETATM 3419 O HOH A1218 -122.412-105.390 619.264 1.00 33.86 O HETATM 3420 O HOH A1219 -138.594 -99.663 644.614 1.00 41.20 O HETATM 3421 O HOH A1220 -141.428 -98.335 649.112 1.00 25.64 O HETATM 3422 O HOH A1221 -140.958-106.716 638.194 1.00 14.82 O HETATM 3423 O HOH A1222 -125.965-110.499 618.811 1.00 39.29 O HETATM 3424 O HOH A1223 -146.409 -95.178 650.737 1.00 28.49 O HETATM 3425 O HOH A1224 -140.192 -98.321 636.667 1.00 21.94 O HETATM 3426 O HOH A1225 -132.556-132.465 688.875 1.00 58.06 O HETATM 3427 O HOH A1226 -133.425 -85.335 618.106 1.00 42.10 O HETATM 3428 O HOH A1227 -139.973 -98.183 642.758 1.00 23.00 O HETATM 3429 O HOH A1228 -141.690-114.665 613.744 1.00 60.61 O HETATM 3430 O HOH A1229 -120.232 -96.728 617.631 1.00 29.87 O HETATM 3431 O HOH A1230 -114.859-109.456 626.939 1.00 50.54 O HETATM 3432 O HOH A1231 -143.247-110.526 684.487 1.00 53.22 O HETATM 3433 O HOH A1232 -152.053-107.182 630.527 1.00 50.52 O HETATM 3434 O HOH A1233 -138.195-112.866 690.092 1.00 42.01 O HETATM 3435 O HOH A1234 -126.000 -83.564 632.254 1.00 51.22 O HETATM 3436 O HOH A1235 -125.828 -81.756 630.387 1.00 52.88 O HETATM 3437 O HOH A1236 -126.212 -93.617 619.509 1.00 37.35 O HETATM 3438 O HOH B 101 -143.262 -98.256 618.918 1.00 49.59 O HETATM 3439 O HOH B 102 -142.130 -92.943 615.131 1.00 36.60 O HETATM 3440 O HOH B 103 -133.282-101.656 616.087 1.00 5.50 O HETATM 3441 O HOH B 104 -133.657-109.639 612.130 1.00 28.79 O HETATM 3442 O HOH B 105 -128.710-100.489 605.225 1.00 33.54 O HETATM 3443 O HOH B 106 -133.942-104.793 617.136 1.00 26.38 O HETATM 3444 O HOH B 107 -136.615 -96.588 619.055 1.00 22.74 O HETATM 3445 O HOH B 108 -129.018 -97.996 620.725 1.00 9.14 O CONECT 35 2392 CONECT 679 1275 CONECT 1275 679 CONECT 1692 3278 CONECT 1712 3278 CONECT 1930 3278 CONECT 1951 3278 CONECT 2392 35 CONECT 2758 2759 2762 CONECT 2759 2758 2760 2764 CONECT 2760 2759 2761 CONECT 2761 2760 2762 CONECT 2762 2758 2761 2763 CONECT 2763 2762 CONECT 2764 2759 2765 2766 CONECT 2765 2764 CONECT 2766 2764 CONECT 2833 3025 CONECT 2839 3144 CONECT 3025 2833 CONECT 3144 2839 CONECT 3278 1692 1712 1930 1951 CONECT 3279 3280 CONECT 3280 3279 3282 CONECT 3281 3290 3292 CONECT 3282 3280 3283 CONECT 3283 3282 3284 CONECT 3284 3283 3285 CONECT 3285 3284 3286 CONECT 3286 3285 3287 CONECT 3287 3286 3289 CONECT 3288 3290 3294 CONECT 3289 3287 3291 3294 CONECT 3290 3281 3288 3293 CONECT 3291 3289 CONECT 3292 3281 CONECT 3293 3290 CONECT 3294 3288 3289 CONECT 3295 3303 3305 CONECT 3296 3297 CONECT 3297 3296 3298 CONECT 3298 3297 3299 CONECT 3299 3298 3300 CONECT 3300 3299 3302 CONECT 3301 3303 3307 CONECT 3302 3300 3304 3307 CONECT 3303 3295 3301 3306 CONECT 3304 3302 CONECT 3305 3295 CONECT 3306 3303 CONECT 3307 3301 3302 CONECT 3308 3309 3310 CONECT 3309 3308 3311 CONECT 3310 3308 3313 CONECT 3311 3309 3314 CONECT 3312 3324 3326 CONECT 3313 3310 3315 CONECT 3314 3311 3316 CONECT 3315 3313 3317 CONECT 3316 3314 3318 CONECT 3317 3315 CONECT 3318 3316 3319 CONECT 3319 3318 3320 CONECT 3320 3319 3321 CONECT 3321 3320 3323 CONECT 3322 3324 3328 CONECT 3323 3321 3325 3328 CONECT 3324 3312 3322 3327 CONECT 3325 3323 CONECT 3326 3312 CONECT 3327 3324 CONECT 3328 3322 3323 CONECT 3329 3330 CONECT 3330 3329 3332 CONECT 3331 3340 3342 CONECT 3332 3330 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3339 CONECT 3338 3340 3344 CONECT 3339 3337 3341 3344 CONECT 3340 3331 3338 3343 CONECT 3341 3339 CONECT 3342 3331 CONECT 3343 3340 CONECT 3344 3338 3339 CONECT 3345 3353 3355 CONECT 3346 3347 CONECT 3347 3346 3348 CONECT 3348 3347 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3352 CONECT 3351 3353 3357 CONECT 3352 3350 3354 3357 CONECT 3353 3345 3351 3356 CONECT 3354 3352 CONECT 3355 3345 CONECT 3356 3353 CONECT 3357 3351 3352 CONECT 3358 3359 3361 CONECT 3359 3358 3362 CONECT 3360 3364 CONECT 3361 3358 3365 CONECT 3362 3359 3366 CONECT 3363 3377 3379 CONECT 3364 3360 3367 CONECT 3365 3361 3368 CONECT 3366 3362 3369 CONECT 3367 3364 3370 CONECT 3368 3365 3370 CONECT 3369 3366 3371 CONECT 3370 3367 3368 CONECT 3371 3369 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 CONECT 3374 3373 3376 CONECT 3375 3377 3381 CONECT 3376 3374 3378 3381 CONECT 3377 3363 3375 3380 CONECT 3378 3376 CONECT 3379 3363 CONECT 3380 3377 CONECT 3381 3375 3376 CONECT 3382 3383 3384 3385 CONECT 3383 3382 CONECT 3384 3382 CONECT 3385 3382 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 CONECT 3394 3395 3396 3397 CONECT 3395 3394 CONECT 3396 3394 CONECT 3397 3394 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3401 CONECT 3401 3400 MASTER 468 0 10 18 8 0 11 6 3437 2 145 38 END