HEADER SIGNALING PROTEIN, ELECTRON TRANSPORT 23-OCT-13 4NC3 TITLE CRYSTAL STRUCTURE OF THE 5-HT2B RECEPTOR SOLVED USING SERIAL TITLE 2 FEMTOSECOND CRYSTALLOGRAPHY IN LIPIDIC CUBIC PHASE. COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA PROTEIN OF HUMAN 5-HYDROXYTRYPTAMINE RECEPTOR 2B COMPND 3 AND E. COLI SOLUBLE CYTOCHROME B562; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: BRIL; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: HTR2B, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS SERIAL FEMTOSECOND CRYSTALLOGRAPHY, HUMAN 5HT2B RECEPTOR, ERGOTAMINE, KEYWDS 2 NOVEL PROTEIN ENGINEERING, GPCR NETWORK, MEMBRANE PROTEIN, LIPIDIC KEYWDS 3 CUBIC PHASE, PSI-BIOLOGY, FREE ELECTRON LASER, STRUCTURAL GENOMICS, KEYWDS 4 GPCR, MEMBRANE, SIGNALING PROTEIN, ELECTRON TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR W.LIU,D.WACKER,C.GATI,G.W.HAN,D.JAMES,D.WANG,G.NELSON,U.WEIERSTALL, AUTHOR 2 V.KATRITCH,A.BARTY,N.A.ZATSEPIN,D.LI,M.MESSERSCHMIDT,S.BOUTET, AUTHOR 3 G.J.WILLIAMS,J.E.KOGLIN,M.M.SEIBERT,C.WANG,S.T.A.SHAH,S.BASU, AUTHOR 4 R.FROMME,C.KUPITZ,K.N.RENDEK,I.GROTJOHANN,P.FROMME,R.A.KIRIAN, AUTHOR 5 K.R.BEYERLEIN,T.A.WHITE,H.N.CHAPMAN,M.CAFFREY,J.C.H.SPENCE, AUTHOR 6 R.C.STEVENS,V.CHEREZOV,GPCR NETWORK (GPCR) REVDAT 4 14-FEB-18 4NC3 1 REMARK REVDAT 3 07-JUN-17 4NC3 1 COMPND SOURCE REMARK REVDAT 2 22-JAN-14 4NC3 1 JRNL REVDAT 1 18-DEC-13 4NC3 0 JRNL AUTH W.LIU,D.WACKER,C.GATI,G.W.HAN,D.JAMES,D.WANG,G.NELSON, JRNL AUTH 2 U.WEIERSTALL,V.KATRITCH,A.BARTY,N.A.ZATSEPIN,D.LI, JRNL AUTH 3 M.MESSERSCHMIDT,S.BOUTET,G.J.WILLIAMS,J.E.KOGLIN, JRNL AUTH 4 M.M.SEIBERT,C.WANG,S.T.SHAH,S.BASU,R.FROMME,C.KUPITZ, JRNL AUTH 5 K.N.RENDEK,I.GROTJOHANN,P.FROMME,R.A.KIRIAN,K.R.BEYERLEIN, JRNL AUTH 6 T.A.WHITE,H.N.CHAPMAN,M.CAFFREY,J.C.SPENCE,R.C.STEVENS, JRNL AUTH 7 V.CHEREZOV JRNL TITL SERIAL FEMTOSECOND CRYSTALLOGRAPHY OF G PROTEIN-COUPLED JRNL TITL 2 RECEPTORS. JRNL REF SCIENCE V. 342 1521 2013 JRNL REFN ISSN 0036-8075 JRNL PMID 24357322 JRNL DOI 10.1126/SCIENCE.1244142 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.68 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 16025 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.229 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 814 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 34.6839 - 5.0836 1.00 2667 136 0.2491 0.2677 REMARK 3 2 5.0836 - 4.0370 1.00 2539 133 0.1784 0.2325 REMARK 3 3 4.0370 - 3.5272 1.00 2534 143 0.2153 0.2685 REMARK 3 4 3.5272 - 3.2050 1.00 2512 129 0.2629 0.3548 REMARK 3 5 3.2050 - 2.9754 1.00 2470 136 0.3072 0.3388 REMARK 3 6 2.9754 - 2.8001 1.00 2489 137 0.3409 0.3841 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.030 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 3179 REMARK 3 ANGLE : 0.601 4299 REMARK 3 CHIRALITY : 0.032 506 REMARK 3 PLANARITY : 0.002 499 REMARK 3 DIHEDRAL : 15.414 1157 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 48:400) OR CHAIN 'A' AND REMARK 3 (RESSEQ 1201:1201) REMARK 3 ORIGIN FOR THE GROUP (A): -21.7680 -18.1630 -2.1578 REMARK 3 T TENSOR REMARK 3 T11: 0.7326 T22: 0.6606 REMARK 3 T33: 0.6925 T12: 0.0302 REMARK 3 T13: -0.0022 T23: 0.0712 REMARK 3 L TENSOR REMARK 3 L11: 2.2400 L22: 2.0754 REMARK 3 L33: 1.2817 L12: -0.0261 REMARK 3 L13: 0.7117 L23: 0.1294 REMARK 3 S TENSOR REMARK 3 S11: 0.0474 S12: 0.0881 S13: -0.1327 REMARK 3 S21: -0.0432 S22: -0.0360 S23: -0.1061 REMARK 3 S31: 0.2515 S32: 0.0323 S33: -0.0016 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1001:1106) REMARK 3 ORIGIN FOR THE GROUP (A): -48.3730 -6.3246 -45.2049 REMARK 3 T TENSOR REMARK 3 T11: 1.0264 T22: 1.9875 REMARK 3 T33: 1.1809 T12: 0.0854 REMARK 3 T13: -0.1212 T23: 0.1200 REMARK 3 L TENSOR REMARK 3 L11: 0.1861 L22: 0.2899 REMARK 3 L33: 0.2845 L12: 0.1367 REMARK 3 L13: -0.1324 L23: -0.0075 REMARK 3 S TENSOR REMARK 3 S11: 0.3702 S12: -0.0559 S13: -0.0530 REMARK 3 S21: -0.0634 S22: -0.2081 S23: -0.3985 REMARK 3 S31: 0.1855 S32: -0.7574 S33: -0.0000 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 4NC3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-13. REMARK 100 THE DEPOSITION ID IS D_1000083014. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : MAR-13 REMARK 200 TEMPERATURE (KELVIN) : 294 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : CXI REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.3 REMARK 200 MONOCHROMATOR : K-B MIRRORS REMARK 200 OPTICS : K-B MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : CORNELL-SLAC PIXEL ARRAY REMARK 200 DETECTOR (CSPAD) REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16052 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 1150. REMARK 200 R MERGE (I) : 0.09500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 4IB4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.48 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS/HCL PH8.0, 20-80MM MGCL2 REMARK 280 AND 30% (V/V) PEG400 , LIPIDIC CUBIC PHASE (LCP), TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.25000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.25000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.75000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.10000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.75000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.10000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.25000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.75000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.10000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.25000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.75000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 61.10000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A 26 REMARK 465 TYR A 27 REMARK 465 LYS A 28 REMARK 465 ASP A 29 REMARK 465 ASP A 30 REMARK 465 ASP A 31 REMARK 465 ASP A 32 REMARK 465 GLY A 33 REMARK 465 ALA A 34 REMARK 465 PRO A 35 REMARK 465 THR A 36 REMARK 465 GLU A 37 REMARK 465 SER A 38 REMARK 465 ILE A 39 REMARK 465 PRO A 40 REMARK 465 GLU A 41 REMARK 465 GLU A 42 REMARK 465 MET A 43 REMARK 465 LYS A 44 REMARK 465 GLN A 45 REMARK 465 ILE A 46 REMARK 465 VAL A 47 REMARK 465 ASP A 198 REMARK 465 ALA A 1036 REMARK 465 ALA A 1037 REMARK 465 LEU A 1038 REMARK 465 ASP A 1039 REMARK 465 ALA A 1040 REMARK 465 GLN A 1041 REMARK 465 LYS A 1042 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 MET A 1058 REMARK 465 ALA A 401 REMARK 465 THR A 402 REMARK 465 LYS A 403 REMARK 465 SER A 404 REMARK 465 VAL A 405 REMARK 465 GLY A 406 REMARK 465 ARG A 407 REMARK 465 PRO A 408 REMARK 465 LEU A 409 REMARK 465 GLU A 410 REMARK 465 VAL A 411 REMARK 465 LEU A 412 REMARK 465 PHE A 413 REMARK 465 GLN A 414 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 GLU A 49 CG CD OE1 OE2 REMARK 470 LYS A 53 CD CE NZ REMARK 470 GLU A 118 CG CD OE1 OE2 REMARK 470 MET A 120 CG SD CE REMARK 470 LEU A 125 CD1 CD2 REMARK 470 ARG A 153 CD NE CZ NH1 NH2 REMARK 470 LYS A 159 CG CD CE NZ REMARK 470 ILE A 161 CG1 CG2 CD1 REMARK 470 GLN A 162 CG CD OE1 NE2 REMARK 470 TYR A 166 CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR A 197 OG1 CG2 REMARK 470 ILE A 205 CG1 CG2 CD1 REMARK 470 LYS A 211 CD CE NZ REMARK 470 GLU A1008 CG CD OE1 OE2 REMARK 470 VAL A1026 CG1 CG2 REMARK 470 LYS A1027 CG CD CE NZ REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 PHE A1065 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A1076 CG CD1 CD2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 ARG A 321 CD NE CZ NH1 NH2 REMARK 470 LYS A 324 CD CE NZ REMARK 470 LYS A 385 CG CD CE NZ REMARK 470 ARG A 400 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 VAL A 64 -57.68 -144.34 REMARK 500 GLU A 118 -159.57 57.60 REMARK 500 ASP A 200 -87.35 -118.31 REMARK 500 ASN A 204 58.43 -104.54 REMARK 500 PHE A 226 -54.34 -124.18 REMARK 500 CYS A 397 63.86 61.93 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 1204 REMARK 610 OLC A 1205 REMARK 610 OLC A 1208 REMARK 610 OLA A 1210 REMARK 610 OLA A 1212 REMARK 610 DGA A 1213 REMARK 610 DGA A 1214 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ERM A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGA A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGA A 1214 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4IB4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE CHIMERIC PROTEIN OF 5-HT2B-BRIL IN COMPLEX REMARK 900 WITH ERGOTAMINE REMARK 900 RELATED ID: GPCR-4 RELATED DB: TARGETTRACK DBREF 4NC3 A 36 248 UNP P41595 5HT2B_HUMAN 36 248 DBREF 4NC3 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 4NC3 A 314 405 UNP P41595 5HT2B_HUMAN 314 405 SEQADV 4NC3 ASP A 26 UNP P41595 EXPRESSION TAG SEQADV 4NC3 TYR A 27 UNP P41595 EXPRESSION TAG SEQADV 4NC3 LYS A 28 UNP P41595 EXPRESSION TAG SEQADV 4NC3 ASP A 29 UNP P41595 EXPRESSION TAG SEQADV 4NC3 ASP A 30 UNP P41595 EXPRESSION TAG SEQADV 4NC3 ASP A 31 UNP P41595 EXPRESSION TAG SEQADV 4NC3 ASP A 32 UNP P41595 EXPRESSION TAG SEQADV 4NC3 GLY A 33 UNP P41595 EXPRESSION TAG SEQADV 4NC3 ALA A 34 UNP P41595 EXPRESSION TAG SEQADV 4NC3 PRO A 35 UNP P41595 EXPRESSION TAG SEQADV 4NC3 TRP A 144 UNP P41595 MET 144 ENGINEERED MUTATION SEQADV 4NC3 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4NC3 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4NC3 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 4NC3 GLY A 406 UNP P41595 EXPRESSION TAG SEQADV 4NC3 ARG A 407 UNP P41595 EXPRESSION TAG SEQADV 4NC3 PRO A 408 UNP P41595 EXPRESSION TAG SEQADV 4NC3 LEU A 409 UNP P41595 EXPRESSION TAG SEQADV 4NC3 GLU A 410 UNP P41595 EXPRESSION TAG SEQADV 4NC3 VAL A 411 UNP P41595 EXPRESSION TAG SEQADV 4NC3 LEU A 412 UNP P41595 EXPRESSION TAG SEQADV 4NC3 PHE A 413 UNP P41595 EXPRESSION TAG SEQADV 4NC3 GLN A 414 UNP P41595 EXPRESSION TAG SEQRES 1 A 430 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO THR GLU SER SEQRES 2 A 430 ILE PRO GLU GLU MET LYS GLN ILE VAL GLU GLU GLN GLY SEQRES 3 A 430 ASN LYS LEU HIS TRP ALA ALA LEU LEU ILE LEU MET VAL SEQRES 4 A 430 ILE ILE PRO THR ILE GLY GLY ASN THR LEU VAL ILE LEU SEQRES 5 A 430 ALA VAL SER LEU GLU LYS LYS LEU GLN TYR ALA THR ASN SEQRES 6 A 430 TYR PHE LEU MET SER LEU ALA VAL ALA ASP LEU LEU VAL SEQRES 7 A 430 GLY LEU PHE VAL MET PRO ILE ALA LEU LEU THR ILE MET SEQRES 8 A 430 PHE GLU ALA MET TRP PRO LEU PRO LEU VAL LEU CYS PRO SEQRES 9 A 430 ALA TRP LEU PHE LEU ASP VAL LEU PHE SER THR ALA SER SEQRES 10 A 430 ILE TRP HIS LEU CYS ALA ILE SER VAL ASP ARG TYR ILE SEQRES 11 A 430 ALA ILE LYS LYS PRO ILE GLN ALA ASN GLN TYR ASN SER SEQRES 12 A 430 ARG ALA THR ALA PHE ILE LYS ILE THR VAL VAL TRP LEU SEQRES 13 A 430 ILE SER ILE GLY ILE ALA ILE PRO VAL PRO ILE LYS GLY SEQRES 14 A 430 ILE GLU THR ASP VAL ASP ASN PRO ASN ASN ILE THR CYS SEQRES 15 A 430 VAL LEU THR LYS GLU ARG PHE GLY ASP PHE MET LEU PHE SEQRES 16 A 430 GLY SER LEU ALA ALA PHE PHE THR PRO LEU ALA ILE MET SEQRES 17 A 430 ILE VAL THR TYR PHE LEU THR ILE HIS ALA LEU GLN LYS SEQRES 18 A 430 LYS ALA ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN SEQRES 19 A 430 ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA SEQRES 20 A 430 GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA SEQRES 21 A 430 LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP SEQRES 22 A 430 LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS SEQRES 23 A 430 GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU SEQRES 24 A 430 LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA SEQRES 25 A 430 ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE SEQRES 26 A 430 GLN LYS TYR LEU GLN THR ILE SER ASN GLU GLN ARG ALA SEQRES 27 A 430 SER LYS VAL LEU GLY ILE VAL PHE PHE LEU PHE LEU LEU SEQRES 28 A 430 MET TRP CYS PRO PHE PHE ILE THR ASN ILE THR LEU VAL SEQRES 29 A 430 LEU CYS ASP SER CYS ASN GLN THR THR LEU GLN MET LEU SEQRES 30 A 430 LEU GLU ILE PHE VAL TRP ILE GLY TYR VAL SER SER GLY SEQRES 31 A 430 VAL ASN PRO LEU VAL TYR THR LEU PHE ASN LYS THR PHE SEQRES 32 A 430 ARG ASP ALA PHE GLY ARG TYR ILE THR CYS ASN TYR ARG SEQRES 33 A 430 ALA THR LYS SER VAL GLY ARG PRO LEU GLU VAL LEU PHE SEQRES 34 A 430 GLN HET PLM A1201 17 HET ERM A1202 43 HET CLR A1203 28 HET OLC A1204 19 HET OLC A1205 16 HET PEG A1206 7 HET OLC A1207 25 HET OLC A1208 19 HET TRS A1209 8 HET OLA A1210 10 HET OLA A1211 20 HET OLA A1212 19 HET DGA A1213 26 HET DGA A1214 20 HETNAM PLM PALMITIC ACID HETNAM ERM ERGOTAMINE HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL HETNAM OLA OLEIC ACID HETNAM DGA DIACYL GLYCEROL HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN TRS TRIS BUFFER FORMUL 2 PLM C16 H32 O2 FORMUL 3 ERM C33 H35 N5 O5 FORMUL 4 CLR C27 H46 O FORMUL 5 OLC 4(C21 H40 O4) FORMUL 7 PEG C4 H10 O3 FORMUL 10 TRS C4 H12 N O3 1+ FORMUL 11 OLA 3(C18 H34 O2) FORMUL 14 DGA 2(C39 H76 O5) FORMUL 16 HOH *7(H2 O) HELIX 1 1 LYS A 53 VAL A 64 1 12 HELIX 2 2 VAL A 64 GLU A 82 1 19 HELIX 3 3 ALA A 88 VAL A 107 1 20 HELIX 4 4 VAL A 107 PHE A 117 1 11 HELIX 5 5 VAL A 126 LYS A 159 1 34 HELIX 6 6 ASN A 164 ILE A 188 1 25 HELIX 7 7 ILE A 188 GLY A 194 1 7 HELIX 8 8 THR A 210 PHE A 226 1 17 HELIX 9 9 PHE A 226 LYS A 1019 1 42 HELIX 10 10 ASN A 1022 LYS A 1032 1 11 HELIX 11 11 ASP A 1060 GLY A 1082 1 23 HELIX 12 12 LYS A 1083 MET A 336 1 47 HELIX 13 13 TRP A 337 CYS A 350 1 14 HELIX 14 14 ASN A 354 VAL A 375 1 22 HELIX 15 15 VAL A 375 LEU A 382 1 8 HELIX 16 16 ASN A 384 THR A 396 1 13 SSBOND 1 CYS A 128 CYS A 207 1555 1555 2.03 SSBOND 2 CYS A 350 CYS A 353 1555 1555 2.03 LINK SG CYS A 397 C1 PLM A1201 1555 1555 1.66 SITE 1 AC1 5 LEU A 62 CYS A 353 ILE A 395 THR A 396 SITE 2 AC1 5 CYS A 397 SITE 1 AC2 12 ASP A 135 SER A 139 THR A 140 VAL A 208 SITE 2 AC2 12 LEU A 209 PHE A 217 MET A 218 ALA A 225 SITE 3 AC2 12 PHE A 340 ASN A 344 GLN A 359 HOH A1302 SITE 1 AC3 5 ILE A 61 ILE A 69 GLY A 70 TYR A 394 SITE 2 AC3 5 TYR A 399 SITE 1 AC4 4 SER A 150 MET A 233 THR A 240 LEU A 326 SITE 1 AC5 1 TYR A 399 SITE 1 AC6 3 TYR A 87 TYR A 380 ASN A 384 SITE 1 AC7 2 LEU A 77 HOH A1305 SITE 1 AC8 4 LYS A 193 ASP A 216 PHE A 217 OLA A1212 SITE 1 AC9 1 ASP A 216 SITE 1 BC1 1 MET A 63 SITE 1 BC2 2 ILE A 174 OLC A1208 SITE 1 BC3 3 LEU A 239 HIS A 242 DGA A1214 SITE 1 BC4 4 HIS A 55 HIS A 242 DGA A1213 HOH A1306 CRYST1 61.500 122.200 168.500 90.00 90.00 90.00 C 2 2 21 8 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 0.016260 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008183 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005935 0.00000 ATOM 1 N GLU A 48 -16.523 -42.109 27.751 1.00140.52 N ANISOU 1 N GLU A 48 21564 15404 16423 -698 -3010 5650 N ATOM 2 CA GLU A 48 -17.227 -41.456 26.653 1.00140.16 C ANISOU 2 CA GLU A 48 21328 15443 16484 -711 -2752 5372 C ATOM 3 C GLU A 48 -16.445 -40.234 26.183 1.00147.41 C ANISOU 3 C GLU A 48 22090 16511 17409 -527 -2740 5042 C ATOM 4 O GLU A 48 -16.029 -39.405 26.993 1.00150.38 O ANISOU 4 O GLU A 48 22507 17108 17522 -484 -2771 5020 O ATOM 5 CB GLU A 48 -18.638 -41.054 27.092 1.00139.28 C ANISOU 5 CB GLU A 48 21243 15585 16092 -925 -2465 5453 C ATOM 6 CG GLU A 48 -19.554 -40.631 25.952 1.00140.33 C ANISOU 6 CG GLU A 48 21192 15760 16368 -971 -2214 5222 C ATOM 7 CD GLU A 48 -19.249 -39.239 25.432 1.00144.33 C ANISOU 7 CD GLU A 48 21537 16474 16829 -836 -2107 4882 C ATOM 8 OE1 GLU A 48 -18.632 -38.444 26.173 1.00147.63 O ANISOU 8 OE1 GLU A 48 21993 17080 17020 -757 -2164 4841 O ATOM 9 OE2 GLU A 48 -19.628 -38.940 24.280 1.00143.99 O ANISOU 9 OE2 GLU A 48 21332 16402 16977 -811 -1976 4659 O ATOM 10 N GLU A 49 -16.244 -40.128 24.873 1.00149.70 N ANISOU 10 N GLU A 49 22203 16679 17998 -422 -2697 4788 N ATOM 11 CA GLU A 49 -15.480 -39.021 24.309 1.00145.99 C ANISOU 11 CA GLU A 49 21572 16326 17573 -253 -2682 4485 C ATOM 12 C GLU A 49 -15.912 -38.706 22.882 1.00150.04 C ANISOU 12 C GLU A 49 21900 16808 18301 -228 -2501 4225 C ATOM 13 O GLU A 49 -16.507 -39.541 22.199 1.00148.29 O ANISOU 13 O GLU A 49 21668 16403 18273 -293 -2457 4258 O ATOM 14 CB GLU A 49 -13.984 -39.343 24.335 1.00144.08 C ANISOU 14 CB GLU A 49 21318 15911 17513 -58 -2968 4464 C ATOM 15 N GLN A 50 -15.601 -37.490 22.444 1.00153.70 N ANISOU 15 N GLN A 50 22221 17448 18728 -134 -2408 3970 N ATOM 16 CA GLN A 50 -15.932 -37.034 21.098 1.00150.58 C ANISOU 16 CA GLN A 50 21651 17054 18506 -99 -2241 3717 C ATOM 17 C GLN A 50 -15.436 -38.000 20.023 1.00151.79 C ANISOU 17 C GLN A 50 21743 16916 19013 0 -2344 3651 C ATOM 18 O GLN A 50 -16.135 -38.250 19.040 1.00150.90 O ANISOU 18 O GLN A 50 21564 16731 19042 -45 -2219 3556 O ATOM 19 CB GLN A 50 -15.355 -35.634 20.850 1.00152.49 C ANISOU 19 CB GLN A 50 21758 17493 18687 13 -2186 3476 C ATOM 20 CG GLN A 50 -13.832 -35.559 20.840 1.00157.27 C ANISOU 20 CG GLN A 50 22311 18015 19430 199 -2399 3402 C ATOM 21 CD GLN A 50 -13.224 -35.742 22.219 1.00157.49 C ANISOU 21 CD GLN A 50 22484 18070 19283 208 -2601 3596 C ATOM 22 OE1 GLN A 50 -13.687 -35.154 23.196 1.00157.29 O ANISOU 22 OE1 GLN A 50 22551 18254 18957 117 -2546 3672 O ATOM 23 NE2 GLN A 50 -12.188 -36.570 22.306 1.00155.50 N ANISOU 23 NE2 GLN A 50 22256 17608 19218 322 -2842 3672 N ATOM 24 N GLY A 51 -14.232 -38.536 20.208 1.00152.54 N ANISOU 24 N GLY A 51 21859 16846 19254 140 -2578 3690 N ATOM 25 CA GLY A 51 -13.659 -39.471 19.254 1.00148.20 C ANISOU 25 CA GLY A 51 21250 16015 19043 257 -2690 3614 C ATOM 26 C GLY A 51 -12.653 -38.823 18.319 1.00138.82 C ANISOU 26 C GLY A 51 19876 14848 18021 445 -2691 3339 C ATOM 27 O GLY A 51 -11.841 -37.999 18.742 1.00137.00 O ANISOU 27 O GLY A 51 19593 14756 17704 532 -2747 3280 O ATOM 28 N ASN A 52 -12.710 -39.201 17.044 1.00129.91 N ANISOU 28 N ASN A 52 18647 13585 17129 505 -2628 3169 N ATOM 29 CA ASN A 52 -11.785 -38.685 16.039 1.00117.21 C ANISOU 29 CA ASN A 52 16857 11990 15687 679 -2607 2911 C ATOM 30 C ASN A 52 -12.511 -38.406 14.727 1.00106.63 C ANISOU 30 C ASN A 52 15417 10689 14410 651 -2396 2711 C ATOM 31 O ASN A 52 -13.230 -39.264 14.217 1.00111.44 O ANISOU 31 O ASN A 52 16074 11142 15125 588 -2370 2731 O ATOM 32 CB ASN A 52 -10.647 -39.680 15.806 1.00117.28 C ANISOU 32 CB ASN A 52 16841 11741 15980 850 -2822 2899 C ATOM 33 CG ASN A 52 -9.595 -39.152 14.849 1.00118.05 C ANISOU 33 CG ASN A 52 16738 11870 16246 1035 -2797 2642 C ATOM 34 OD1 ASN A 52 -9.594 -37.971 14.497 1.00121.14 O ANISOU 34 OD1 ASN A 52 17018 12481 16527 1034 -2643 2499 O ATOM 35 ND2 ASN A 52 -8.687 -40.025 14.429 1.00118.26 N ANISOU 35 ND2 ASN A 52 16714 11674 16546 1195 -2947 2586 N ATOM 36 N LYS A 53 -12.312 -37.210 14.181 1.00 97.46 N ANISOU 36 N LYS A 53 14118 9727 13186 697 -2258 2524 N ATOM 37 CA LYS A 53 -13.060 -36.771 13.008 1.00 96.28 C ANISOU 37 CA LYS A 53 13882 9653 13048 659 -2055 2348 C ATOM 38 C LYS A 53 -12.170 -36.581 11.780 1.00 92.28 C ANISOU 38 C LYS A 53 13216 9118 12730 826 -2027 2114 C ATOM 39 O LYS A 53 -12.438 -35.722 10.939 1.00 91.67 O ANISOU 39 O LYS A 53 13036 9185 12608 822 -1862 1955 O ATOM 40 CB LYS A 53 -13.788 -35.460 13.319 1.00101.78 C ANISOU 40 CB LYS A 53 14558 10620 13497 550 -1889 2331 C ATOM 41 CG LYS A 53 -14.651 -35.512 14.570 1.00 98.81 C ANISOU 41 CG LYS A 53 14324 10317 12901 391 -1887 2546 C ATOM 42 N LEU A 54 -11.116 -37.383 11.676 1.00 93.05 N ANISOU 42 N LEU A 54 13288 9031 13037 972 -2187 2097 N ATOM 43 CA LEU A 54 -10.194 -37.292 10.546 1.00 94.90 C ANISOU 43 CA LEU A 54 13363 9240 13456 1141 -2157 1876 C ATOM 44 C LEU A 54 -10.887 -37.651 9.231 1.00 96.63 C ANISOU 44 C LEU A 54 13559 9404 13753 1129 -2024 1721 C ATOM 45 O LEU A 54 -10.650 -37.018 8.203 1.00 92.25 O ANISOU 45 O LEU A 54 12877 8959 13216 1194 -1890 1530 O ATOM 46 CB LEU A 54 -8.992 -38.214 10.765 1.00 96.05 C ANISOU 46 CB LEU A 54 13487 9179 13827 1304 -2367 1893 C ATOM 47 CG LEU A 54 -7.845 -38.095 9.763 1.00 82.10 C ANISOU 47 CG LEU A 54 11533 7403 12257 1497 -2344 1671 C ATOM 48 CD1 LEU A 54 -7.158 -36.747 9.884 1.00 80.72 C ANISOU 48 CD1 LEU A 54 11218 7460 11990 1528 -2276 1608 C ATOM 49 CD2 LEU A 54 -6.856 -39.229 9.973 1.00 84.70 C ANISOU 49 CD2 LEU A 54 11858 7489 12838 1654 -2560 1694 C ATOM 50 N HIS A 55 -11.743 -38.666 9.274 1.00 80.22 N ANISOU 50 N HIS A 55 11607 7154 11717 1041 -2067 1810 N ATOM 51 CA HIS A 55 -12.432 -39.148 8.081 1.00 83.38 C ANISOU 51 CA HIS A 55 12002 7473 12204 1026 -1976 1666 C ATOM 52 C HIS A 55 -13.402 -38.111 7.526 1.00 80.11 C ANISOU 52 C HIS A 55 11549 7283 11609 912 -1768 1588 C ATOM 53 O HIS A 55 -13.610 -38.034 6.316 1.00 76.84 O ANISOU 53 O HIS A 55 11072 6887 11237 949 -1665 1403 O ATOM 54 CB HIS A 55 -13.162 -40.465 8.371 1.00 91.83 C ANISOU 54 CB HIS A 55 13219 8297 13374 937 -2089 1800 C ATOM 55 CG HIS A 55 -14.208 -40.368 9.440 1.00 90.05 C ANISOU 55 CG HIS A 55 13115 8131 12968 732 -2077 2035 C ATOM 56 ND1 HIS A 55 -13.904 -40.350 10.785 1.00 87.18 N ANISOU 56 ND1 HIS A 55 12830 7783 12510 696 -2187 2253 N ATOM 57 CD2 HIS A 55 -15.558 -40.309 9.361 1.00 91.28 C ANISOU 57 CD2 HIS A 55 13324 8339 13021 554 -1965 2086 C ATOM 58 CE1 HIS A 55 -15.021 -40.270 11.487 1.00 86.36 C ANISOU 58 CE1 HIS A 55 12824 7751 12238 503 -2127 2427 C ATOM 59 NE2 HIS A 55 -16.039 -40.244 10.646 1.00 89.80 N ANISOU 59 NE2 HIS A 55 13236 8206 12676 414 -1991 2330 N ATOM 60 N TRP A 56 -13.995 -37.314 8.408 1.00 81.53 N ANISOU 60 N TRP A 56 11766 7630 11581 781 -1713 1723 N ATOM 61 CA TRP A 56 -14.868 -36.233 7.968 1.00 82.74 C ANISOU 61 CA TRP A 56 11870 7998 11570 685 -1527 1652 C ATOM 62 C TRP A 56 -14.041 -35.154 7.286 1.00 83.27 C ANISOU 62 C TRP A 56 11791 8226 11623 800 -1439 1483 C ATOM 63 O TRP A 56 -14.450 -34.596 6.269 1.00 82.64 O ANISOU 63 O TRP A 56 11644 8245 11509 792 -1303 1344 O ATOM 64 CB TRP A 56 -15.642 -35.632 9.143 1.00 77.62 C ANISOU 64 CB TRP A 56 11290 7491 10710 532 -1490 1826 C ATOM 65 CG TRP A 56 -16.673 -36.551 9.719 1.00 84.05 C ANISOU 65 CG TRP A 56 12235 8188 11511 383 -1528 1998 C ATOM 66 CD1 TRP A 56 -16.773 -36.960 11.017 1.00 87.62 C ANISOU 66 CD1 TRP A 56 12802 8605 11886 304 -1621 2221 C ATOM 67 CD2 TRP A 56 -17.749 -37.183 9.015 1.00 90.43 C ANISOU 67 CD2 TRP A 56 13070 8901 12387 288 -1475 1970 C ATOM 68 NE1 TRP A 56 -17.847 -37.805 11.166 1.00 87.04 N ANISOU 68 NE1 TRP A 56 12819 8420 11832 159 -1617 2344 N ATOM 69 CE2 TRP A 56 -18.462 -37.959 9.951 1.00 89.46 C ANISOU 69 CE2 TRP A 56 13069 8682 12239 145 -1534 2189 C ATOM 70 CE3 TRP A 56 -18.180 -37.168 7.684 1.00 96.18 C ANISOU 70 CE3 TRP A 56 13734 9619 13191 305 -1391 1784 C ATOM 71 CZ2 TRP A 56 -19.581 -38.712 9.599 1.00 90.96 C ANISOU 71 CZ2 TRP A 56 13304 8757 12500 15 -1511 2225 C ATOM 72 CZ3 TRP A 56 -19.291 -37.916 7.337 1.00 95.90 C ANISOU 72 CZ3 TRP A 56 13750 9470 13217 184 -1381 1808 C ATOM 73 CH2 TRP A 56 -19.979 -38.677 8.291 1.00 94.76 C ANISOU 73 CH2 TRP A 56 13713 9222 13069 38 -1441 2027 C ATOM 74 N ALA A 57 -12.873 -34.864 7.850 1.00 84.95 N ANISOU 74 N ALA A 57 11952 8461 11865 901 -1525 1505 N ATOM 75 CA ALA A 57 -11.980 -33.870 7.274 1.00 79.51 C ANISOU 75 CA ALA A 57 11111 7912 11185 1005 -1452 1363 C ATOM 76 C ALA A 57 -11.534 -34.313 5.888 1.00 72.61 C ANISOU 76 C ALA A 57 10153 6967 10468 1126 -1401 1174 C ATOM 77 O ALA A 57 -11.549 -33.528 4.942 1.00 80.23 O ANISOU 77 O ALA A 57 11024 8069 11391 1143 -1258 1041 O ATOM 78 CB ALA A 57 -10.777 -33.652 8.175 1.00 83.01 C ANISOU 78 CB ALA A 57 11512 8363 11667 1092 -1582 1427 C ATOM 79 N ALA A 58 -11.137 -35.576 5.774 1.00 74.46 N ANISOU 79 N ALA A 58 10426 6987 10880 1213 -1520 1163 N ATOM 80 CA ALA A 58 -10.750 -36.137 4.488 1.00 76.61 C ANISOU 80 CA ALA A 58 10632 7176 11299 1336 -1479 969 C ATOM 81 C ALA A 58 -11.905 -36.008 3.503 1.00 73.98 C ANISOU 81 C ALA A 58 10333 6899 10877 1245 -1340 876 C ATOM 82 O ALA A 58 -11.723 -35.570 2.367 1.00 77.29 O ANISOU 82 O ALA A 58 10664 7420 11285 1306 -1216 707 O ATOM 83 CB ALA A 58 -10.357 -37.591 4.649 1.00 77.44 C ANISOU 83 CB ALA A 58 10800 7013 11611 1426 -1648 984 C ATOM 84 N LEU A 59 -13.096 -36.390 3.952 1.00 89.00 N ANISOU 84 N LEU A 59 12362 8741 12715 1096 -1366 994 N ATOM 85 CA LEU A 59 -14.292 -36.335 3.121 1.00 89.44 C ANISOU 85 CA LEU A 59 12452 8833 12697 995 -1261 922 C ATOM 86 C LEU A 59 -14.513 -34.930 2.566 1.00 79.93 C ANISOU 86 C LEU A 59 11158 7881 11332 964 -1095 848 C ATOM 87 O LEU A 59 -14.728 -34.754 1.367 1.00 77.05 O ANISOU 87 O LEU A 59 10752 7571 10951 993 -1000 693 O ATOM 88 CB LEU A 59 -15.515 -36.767 3.934 1.00 94.62 C ANISOU 88 CB LEU A 59 13233 9420 13299 819 -1307 1097 C ATOM 89 CG LEU A 59 -16.756 -37.158 3.130 1.00102.96 C ANISOU 89 CG LEU A 59 14336 10430 14353 718 -1257 1031 C ATOM 90 CD1 LEU A 59 -16.547 -38.504 2.449 1.00107.96 C ANISOU 90 CD1 LEU A 59 15014 10817 15187 801 -1360 925 C ATOM 91 CD2 LEU A 59 -17.987 -37.189 4.023 1.00108.54 C ANISOU 91 CD2 LEU A 59 15125 11147 14969 523 -1255 1218 C ATOM 92 N LEU A 60 -14.454 -33.934 3.445 1.00 75.62 N ANISOU 92 N LEU A 60 10586 7482 10664 907 -1069 959 N ATOM 93 CA LEU A 60 -14.694 -32.547 3.059 1.00 74.91 C ANISOU 93 CA LEU A 60 10417 7613 10433 869 -929 911 C ATOM 94 C LEU A 60 -13.642 -32.047 2.072 1.00 78.05 C ANISOU 94 C LEU A 60 10687 8091 10878 1003 -857 759 C ATOM 95 O LEU A 60 -13.961 -31.326 1.127 1.00 70.88 O ANISOU 95 O LEU A 60 9728 7310 9892 989 -734 665 O ATOM 96 CB LEU A 60 -14.723 -31.654 4.301 1.00 79.52 C ANISOU 96 CB LEU A 60 11003 8314 10898 796 -940 1050 C ATOM 97 CG LEU A 60 -15.900 -31.902 5.249 1.00 83.33 C ANISOU 97 CG LEU A 60 11598 8778 11285 645 -964 1200 C ATOM 98 CD1 LEU A 60 -15.721 -31.130 6.547 1.00 75.52 C ANISOU 98 CD1 LEU A 60 10619 7899 10177 602 -990 1322 C ATOM 99 CD2 LEU A 60 -17.215 -31.531 4.580 1.00 86.44 C ANISOU 99 CD2 LEU A 60 11996 9250 11596 537 -848 1154 C ATOM 100 N ILE A 61 -12.388 -32.426 2.297 1.00 88.20 N ANISOU 100 N ILE A 61 11915 9306 12291 1131 -933 742 N ATOM 101 CA ILE A 61 -11.311 -32.085 1.374 1.00 87.38 C ANISOU 101 CA ILE A 61 11675 9272 12253 1265 -859 599 C ATOM 102 C ILE A 61 -11.607 -32.658 -0.009 1.00 82.94 C ANISOU 102 C ILE A 61 11121 8675 11717 1315 -783 433 C ATOM 103 O ILE A 61 -11.377 -32.005 -1.027 1.00 76.65 O ANISOU 103 O ILE A 61 10241 8015 10866 1352 -652 321 O ATOM 104 CB ILE A 61 -9.956 -32.634 1.863 1.00 94.21 C ANISOU 104 CB ILE A 61 12472 10035 13287 1404 -973 601 C ATOM 105 CG1 ILE A 61 -9.488 -31.883 3.111 1.00 93.10 C ANISOU 105 CG1 ILE A 61 12302 9963 13110 1370 -1046 739 C ATOM 106 CG2 ILE A 61 -8.908 -32.508 0.771 1.00 95.91 C ANISOU 106 CG2 ILE A 61 12539 10308 13593 1549 -880 433 C ATOM 107 CD1 ILE A 61 -8.275 -32.505 3.783 1.00 94.25 C ANISOU 107 CD1 ILE A 61 12400 9989 13423 1493 -1200 771 C ATOM 108 N LEU A 62 -12.123 -33.883 -0.032 1.00 82.03 N ANISOU 108 N LEU A 62 11114 8374 11681 1311 -873 422 N ATOM 109 CA LEU A 62 -12.401 -34.586 -1.280 1.00 84.82 C ANISOU 109 CA LEU A 62 11492 8664 12071 1365 -833 250 C ATOM 110 C LEU A 62 -13.596 -34.018 -2.043 1.00 80.83 C ANISOU 110 C LEU A 62 11027 8278 11406 1250 -727 211 C ATOM 111 O LEU A 62 -13.498 -33.744 -3.238 1.00 71.58 O ANISOU 111 O LEU A 62 9811 7205 10180 1304 -622 63 O ATOM 112 CB LEU A 62 -12.642 -36.073 -1.004 1.00 91.24 C ANISOU 112 CB LEU A 62 12413 9217 13037 1384 -983 255 C ATOM 113 CG LEU A 62 -11.399 -36.938 -0.785 1.00102.94 C ANISOU 113 CG LEU A 62 13851 10539 14721 1552 -1091 210 C ATOM 114 CD1 LEU A 62 -11.792 -38.322 -0.282 1.00113.45 C ANISOU 114 CD1 LEU A 62 15310 11595 16202 1537 -1264 270 C ATOM 115 CD2 LEU A 62 -10.590 -37.048 -2.068 1.00 97.34 C ANISOU 115 CD2 LEU A 62 13040 9876 14067 1718 -996 -24 C ATOM 116 N MET A 63 -14.721 -33.843 -1.355 1.00 84.84 N ANISOU 116 N MET A 63 11614 8784 11836 1094 -756 346 N ATOM 117 CA MET A 63 -15.980 -33.533 -2.028 1.00 82.52 C ANISOU 117 CA MET A 63 11364 8561 11427 984 -690 311 C ATOM 118 C MET A 63 -16.511 -32.127 -1.755 1.00 79.22 C ANISOU 118 C MET A 63 10904 8344 10851 880 -598 397 C ATOM 119 O MET A 63 -17.711 -31.886 -1.879 1.00 84.88 O ANISOU 119 O MET A 63 11663 9100 11489 762 -575 424 O ATOM 120 CB MET A 63 -17.048 -34.554 -1.628 1.00 85.45 C ANISOU 120 CB MET A 63 11851 8757 11857 878 -793 375 C ATOM 121 CG MET A 63 -16.670 -35.996 -1.924 1.00 85.98 C ANISOU 121 CG MET A 63 11975 8594 12101 969 -904 286 C ATOM 122 SD MET A 63 -18.077 -37.118 -1.808 1.00143.90 S ANISOU 122 SD MET A 63 19437 15728 19510 825 -1009 333 S ATOM 123 CE MET A 63 -18.608 -36.828 -0.123 1.00126.04 C ANISOU 123 CE MET A 63 17212 13480 17199 667 -1044 613 C ATOM 124 N VAL A 64 -15.634 -31.198 -1.391 1.00 75.18 N ANISOU 124 N VAL A 64 10303 7951 10310 926 -553 435 N ATOM 125 CA VAL A 64 -16.058 -29.816 -1.183 1.00 73.20 C ANISOU 125 CA VAL A 64 10007 7877 9926 841 -472 500 C ATOM 126 C VAL A 64 -14.991 -28.820 -1.626 1.00 74.31 C ANISOU 126 C VAL A 64 10029 8157 10049 923 -387 453 C ATOM 127 O VAL A 64 -15.242 -27.966 -2.475 1.00 74.40 O ANISOU 127 O VAL A 64 9999 8299 9970 904 -288 405 O ATOM 128 CB VAL A 64 -16.405 -29.540 0.293 1.00 63.82 C ANISOU 128 CB VAL A 64 8854 6687 8706 749 -530 662 C ATOM 129 CG1 VAL A 64 -16.948 -28.131 0.451 1.00 72.19 C ANISOU 129 CG1 VAL A 64 9871 7920 9640 668 -448 703 C ATOM 130 CG2 VAL A 64 -17.405 -30.559 0.807 1.00 70.18 C ANISOU 130 CG2 VAL A 64 9770 7358 9537 657 -605 734 C ATOM 131 N ILE A 65 -13.801 -28.931 -1.048 1.00 72.74 N ANISOU 131 N ILE A 65 9771 7925 9944 1008 -433 476 N ATOM 132 CA ILE A 65 -12.731 -27.980 -1.321 1.00 79.73 C ANISOU 132 CA ILE A 65 10524 8934 10836 1073 -361 450 C ATOM 133 C ILE A 65 -12.181 -28.127 -2.738 1.00 82.89 C ANISOU 133 C ILE A 65 10861 9382 11251 1170 -260 304 C ATOM 134 O ILE A 65 -12.059 -27.143 -3.468 1.00 84.08 O ANISOU 134 O ILE A 65 10941 9681 11324 1158 -147 280 O ATOM 135 CB ILE A 65 -11.583 -28.133 -0.311 1.00 79.34 C ANISOU 135 CB ILE A 65 10417 8829 10901 1142 -455 508 C ATOM 136 CG1 ILE A 65 -12.088 -27.829 1.102 1.00 73.36 C ANISOU 136 CG1 ILE A 65 9726 8059 10090 1044 -545 653 C ATOM 137 CG2 ILE A 65 -10.433 -27.204 -0.672 1.00 78.10 C ANISOU 137 CG2 ILE A 65 10103 8793 10779 1206 -380 474 C ATOM 138 CD1 ILE A 65 -11.072 -28.094 2.187 1.00 76.91 C ANISOU 138 CD1 ILE A 65 10145 8441 10635 1105 -670 721 C ATOM 139 N ILE A 66 -11.845 -29.354 -3.120 1.00 82.32 N ANISOU 139 N ILE A 66 10816 9185 11277 1267 -300 208 N ATOM 140 CA ILE A 66 -11.294 -29.613 -4.446 1.00 85.22 C ANISOU 140 CA ILE A 66 11128 9600 11650 1375 -201 48 C ATOM 141 C ILE A 66 -12.293 -29.254 -5.549 1.00 85.98 C ANISOU 141 C ILE A 66 11284 9795 11590 1309 -110 -14 C ATOM 142 O ILE A 66 -11.941 -28.555 -6.501 1.00 80.47 O ANISOU 142 O ILE A 66 10517 9248 10809 1336 17 -70 O ATOM 143 CB ILE A 66 -10.830 -31.078 -4.582 1.00 84.62 C ANISOU 143 CB ILE A 66 11082 9347 11722 1499 -280 -61 C ATOM 144 CG1 ILE A 66 -9.508 -31.271 -3.835 1.00 86.06 C ANISOU 144 CG1 ILE A 66 11158 9475 12068 1605 -341 -32 C ATOM 145 CG2 ILE A 66 -10.659 -31.456 -6.045 1.00 86.10 C ANISOU 145 CG2 ILE A 66 11256 9582 11875 1593 -175 -253 C ATOM 146 CD1 ILE A 66 -9.054 -32.708 -3.735 1.00 81.07 C ANISOU 146 CD1 ILE A 66 10555 8637 11611 1729 -453 -113 C ATOM 147 N PRO A 67 -13.542 -29.728 -5.429 1.00 81.20 N ANISOU 147 N PRO A 67 10804 9105 10943 1219 -179 5 N ATOM 148 CA PRO A 67 -14.563 -29.316 -6.398 1.00 79.05 C ANISOU 148 CA PRO A 67 10583 8927 10525 1148 -116 -42 C ATOM 149 C PRO A 67 -14.660 -27.797 -6.527 1.00 79.50 C ANISOU 149 C PRO A 67 10574 9169 10463 1079 -22 40 C ATOM 150 O PRO A 67 -14.703 -27.275 -7.640 1.00 82.13 O ANISOU 150 O PRO A 67 10890 9628 10687 1090 75 -22 O ATOM 151 CB PRO A 67 -15.854 -29.876 -5.800 1.00 74.03 C ANISOU 151 CB PRO A 67 10060 8170 9898 1036 -222 20 C ATOM 152 CG PRO A 67 -15.419 -31.060 -5.022 1.00 68.24 C ANISOU 152 CG PRO A 67 9361 7245 9322 1088 -335 31 C ATOM 153 CD PRO A 67 -14.055 -30.734 -4.482 1.00 70.29 C ANISOU 153 CD PRO A 67 9517 7535 9656 1180 -320 66 C ATOM 154 N THR A 68 -14.696 -27.104 -5.393 1.00 81.49 N ANISOU 154 N THR A 68 10797 9432 10734 1011 -57 178 N ATOM 155 CA THR A 68 -14.828 -25.650 -5.380 1.00 82.41 C ANISOU 155 CA THR A 68 10853 9695 10763 942 10 258 C ATOM 156 C THR A 68 -13.677 -24.978 -6.122 1.00 84.14 C ANISOU 156 C THR A 68 10958 10035 10977 1015 120 223 C ATOM 157 O THR A 68 -13.895 -24.182 -7.036 1.00 81.79 O ANISOU 157 O THR A 68 10642 9860 10572 987 209 216 O ATOM 158 CB THR A 68 -14.868 -25.100 -3.940 1.00 80.60 C ANISOU 158 CB THR A 68 10607 9446 10570 878 -55 388 C ATOM 159 OG1 THR A 68 -16.022 -25.609 -3.258 1.00 60.92 O ANISOU 159 OG1 THR A 68 8214 6869 8063 794 -133 436 O ATOM 160 CG2 THR A 68 -14.923 -23.576 -3.951 1.00 82.01 C ANISOU 160 CG2 THR A 68 10718 9758 10682 820 6 453 C ATOM 161 N ILE A 69 -12.453 -25.303 -5.722 1.00 79.94 N ANISOU 161 N ILE A 69 10344 9467 10564 1105 112 210 N ATOM 162 CA ILE A 69 -11.271 -24.702 -6.325 1.00 78.06 C ANISOU 162 CA ILE A 69 9970 9342 10346 1171 222 185 C ATOM 163 C ILE A 69 -11.174 -25.051 -7.807 1.00 80.03 C ANISOU 163 C ILE A 69 10227 9669 10513 1236 335 57 C ATOM 164 O ILE A 69 -11.035 -24.169 -8.653 1.00 83.77 O ANISOU 164 O ILE A 69 10652 10290 10889 1213 451 69 O ATOM 165 CB ILE A 69 -9.989 -25.152 -5.604 1.00 72.51 C ANISOU 165 CB ILE A 69 9168 8572 9812 1267 175 181 C ATOM 166 CG1 ILE A 69 -9.997 -24.646 -4.158 1.00 75.32 C ANISOU 166 CG1 ILE A 69 9515 8881 10223 1201 64 310 C ATOM 167 CG2 ILE A 69 -8.763 -24.630 -6.333 1.00 76.23 C ANISOU 167 CG2 ILE A 69 9480 9166 10318 1336 304 143 C ATOM 168 CD1 ILE A 69 -8.817 -25.110 -3.329 1.00 65.18 C ANISOU 168 CD1 ILE A 69 8145 7518 9102 1289 -19 318 C ATOM 169 N GLY A 70 -11.252 -26.340 -8.118 1.00 75.22 N ANISOU 169 N GLY A 70 9684 8956 9938 1315 297 -64 N ATOM 170 CA GLY A 70 -11.180 -26.791 -9.495 1.00 72.03 C ANISOU 170 CA GLY A 70 9302 8619 9446 1389 394 -213 C ATOM 171 C GLY A 70 -12.234 -26.140 -10.370 1.00 71.46 C ANISOU 171 C GLY A 70 9312 8659 9183 1298 442 -201 C ATOM 172 O GLY A 70 -11.933 -25.654 -11.460 1.00 76.03 O ANISOU 172 O GLY A 70 9858 9389 9641 1320 569 -242 O ATOM 173 N GLY A 71 -13.473 -26.125 -9.888 1.00 71.92 N ANISOU 173 N GLY A 71 9471 8643 9211 1194 339 -139 N ATOM 174 CA GLY A 71 -14.585 -25.592 -10.654 1.00 71.25 C ANISOU 174 CA GLY A 71 9465 8642 8966 1109 353 -130 C ATOM 175 C GLY A 71 -14.439 -24.114 -10.957 1.00 71.89 C ANISOU 175 C GLY A 71 9475 8884 8954 1049 444 -20 C ATOM 176 O GLY A 71 -14.528 -23.696 -12.111 1.00 72.61 O ANISOU 176 O GLY A 71 9582 9104 8902 1051 529 -50 O ATOM 177 N ASN A 72 -14.211 -23.319 -9.917 1.00 77.59 N ANISOU 177 N ASN A 72 10127 9596 9758 996 420 110 N ATOM 178 CA ASN A 72 -14.068 -21.876 -10.078 1.00 79.02 C ANISOU 178 CA ASN A 72 10238 9899 9886 932 486 223 C ATOM 179 C ASN A 72 -12.832 -21.521 -10.898 1.00 72.52 C ANISOU 179 C ASN A 72 9310 9201 9043 996 628 206 C ATOM 180 O ASN A 72 -12.842 -20.556 -11.661 1.00 74.05 O ANISOU 180 O ASN A 72 9482 9521 9133 952 710 267 O ATOM 181 CB ASN A 72 -14.013 -21.190 -8.712 1.00 81.48 C ANISOU 181 CB ASN A 72 10497 10157 10306 872 417 341 C ATOM 182 CG ASN A 72 -15.265 -21.428 -7.890 1.00 84.39 C ANISOU 182 CG ASN A 72 10957 10429 10677 800 302 369 C ATOM 183 OD1 ASN A 72 -15.191 -21.838 -6.733 1.00 93.09 O ANISOU 183 OD1 ASN A 72 12062 11435 11873 798 224 396 O ATOM 184 ND2 ASN A 72 -16.424 -21.173 -8.485 1.00 80.20 N ANISOU 184 ND2 ASN A 72 10499 9931 10042 739 291 369 N ATOM 185 N THR A 73 -11.766 -22.297 -10.732 1.00 69.39 N ANISOU 185 N THR A 73 8844 8768 8752 1099 656 129 N ATOM 186 CA THR A 73 -10.562 -22.119 -11.536 1.00 78.37 C ANISOU 186 CA THR A 73 9866 10030 9880 1171 805 92 C ATOM 187 C THR A 73 -10.892 -22.300 -13.015 1.00 79.94 C ANISOU 187 C THR A 73 10139 10349 9886 1196 906 2 C ATOM 188 O THR A 73 -10.466 -21.509 -13.858 1.00 75.65 O ANISOU 188 O THR A 73 9539 9964 9241 1178 1039 49 O ATOM 189 CB THR A 73 -9.456 -23.123 -11.144 1.00 87.94 C ANISOU 189 CB THR A 73 10993 11168 11252 1299 805 -7 C ATOM 190 OG1 THR A 73 -9.037 -22.884 -9.795 1.00 85.29 O ANISOU 190 OG1 THR A 73 10584 10737 11084 1277 706 85 O ATOM 191 CG2 THR A 73 -8.254 -22.985 -12.068 1.00 88.88 C ANISOU 191 CG2 THR A 73 10979 11432 11358 1379 980 -62 C ATOM 192 N LEU A 74 -11.653 -23.348 -13.321 1.00 79.42 N ANISOU 192 N LEU A 74 10202 10207 9767 1233 838 -123 N ATOM 193 CA LEU A 74 -12.066 -23.630 -14.692 1.00 76.52 C ANISOU 193 CA LEU A 74 9927 9943 9204 1261 905 -231 C ATOM 194 C LEU A 74 -12.880 -22.479 -15.278 1.00 75.80 C ANISOU 194 C LEU A 74 9889 9967 8944 1147 921 -111 C ATOM 195 O LEU A 74 -12.668 -22.082 -16.423 1.00 80.70 O ANISOU 195 O LEU A 74 10516 10750 9395 1156 1039 -121 O ATOM 196 CB LEU A 74 -12.880 -24.927 -14.750 1.00 77.64 C ANISOU 196 CB LEU A 74 10202 9947 9348 1301 786 -379 C ATOM 197 CG LEU A 74 -12.086 -26.237 -14.701 1.00 80.94 C ANISOU 197 CG LEU A 74 10597 10270 9886 1444 788 -549 C ATOM 198 CD1 LEU A 74 -13.025 -27.428 -14.575 1.00 75.82 C ANISOU 198 CD1 LEU A 74 10086 9448 9275 1453 638 -663 C ATOM 199 CD2 LEU A 74 -11.208 -26.382 -15.934 1.00 73.66 C ANISOU 199 CD2 LEU A 74 9630 9510 8849 1554 958 -681 C ATOM 200 N VAL A 75 -13.807 -21.942 -14.491 1.00 70.95 N ANISOU 200 N VAL A 75 9311 9272 8375 1044 802 2 N ATOM 201 CA VAL A 75 -14.647 -20.843 -14.954 1.00 68.72 C ANISOU 201 CA VAL A 75 9075 9074 7964 941 791 117 C ATOM 202 C VAL A 75 -13.796 -19.608 -15.231 1.00 69.95 C ANISOU 202 C VAL A 75 9120 9359 8098 908 913 251 C ATOM 203 O VAL A 75 -13.958 -18.949 -16.256 1.00 67.63 O ANISOU 203 O VAL A 75 8858 9199 7640 874 981 303 O ATOM 204 CB VAL A 75 -15.751 -20.492 -13.931 1.00 64.57 C ANISOU 204 CB VAL A 75 8584 8430 7520 847 646 203 C ATOM 205 CG1 VAL A 75 -16.510 -19.245 -14.365 1.00 64.05 C ANISOU 205 CG1 VAL A 75 8542 8443 7352 753 632 327 C ATOM 206 CG2 VAL A 75 -16.710 -21.664 -13.755 1.00 82.10 C ANISOU 206 CG2 VAL A 75 10912 10528 9755 857 529 90 C ATOM 207 N ILE A 76 -12.884 -19.304 -14.315 1.00 70.80 N ANISOU 207 N ILE A 76 9100 9426 8375 914 933 312 N ATOM 208 CA ILE A 76 -12.014 -18.145 -14.464 1.00 72.47 C ANISOU 208 CA ILE A 76 9188 9740 8607 872 1038 443 C ATOM 209 C ILE A 76 -11.151 -18.301 -15.710 1.00 75.67 C ANISOU 209 C ILE A 76 9554 10310 8889 933 1216 393 C ATOM 210 O ILE A 76 -11.021 -17.371 -16.504 1.00 75.50 O ANISOU 210 O ILE A 76 9514 10420 8751 875 1310 501 O ATOM 211 CB ILE A 76 -11.119 -17.950 -13.224 1.00 79.09 C ANISOU 211 CB ILE A 76 9890 10495 9667 878 1011 490 C ATOM 212 CG1 ILE A 76 -11.973 -17.557 -12.014 1.00 73.83 C ANISOU 212 CG1 ILE A 76 9263 9697 9091 805 853 558 C ATOM 213 CG2 ILE A 76 -10.070 -16.880 -13.489 1.00 77.67 C ANISOU 213 CG2 ILE A 76 9563 10420 9527 841 1130 608 C ATOM 214 CD1 ILE A 76 -11.233 -17.600 -10.692 1.00 72.92 C ANISOU 214 CD1 ILE A 76 9050 9486 9173 822 791 577 C ATOM 215 N LEU A 77 -10.570 -19.486 -15.879 1.00 85.42 N ANISOU 215 N LEU A 77 10774 11536 10145 1052 1263 229 N ATOM 216 CA LEU A 77 -9.759 -19.787 -17.055 1.00 91.30 C ANISOU 216 CA LEU A 77 11480 12444 10764 1130 1443 143 C ATOM 217 C LEU A 77 -10.568 -19.612 -18.334 1.00 95.44 C ANISOU 217 C LEU A 77 12147 13096 11018 1100 1479 133 C ATOM 218 O LEU A 77 -10.117 -18.974 -19.285 1.00 74.79 O ANISOU 218 O LEU A 77 9502 10660 8256 1078 1630 200 O ATOM 219 CB LEU A 77 -9.227 -21.221 -16.979 1.00 92.16 C ANISOU 219 CB LEU A 77 11576 12489 10951 1277 1451 -64 C ATOM 220 CG LEU A 77 -8.038 -21.462 -16.049 1.00 98.52 C ANISOU 220 CG LEU A 77 12208 13224 12002 1341 1465 -72 C ATOM 221 CD1 LEU A 77 -7.772 -22.953 -15.896 1.00105.43 C ANISOU 221 CD1 LEU A 77 13102 13989 12967 1486 1423 -276 C ATOM 222 CD2 LEU A 77 -6.804 -20.753 -16.579 1.00 99.05 C ANISOU 222 CD2 LEU A 77 12099 13463 12072 1347 1663 -8 C ATOM 223 N ALA A 78 -11.765 -20.189 -18.347 1.00 96.12 N ANISOU 223 N ALA A 78 12389 13091 11041 1095 1336 54 N ATOM 224 CA ALA A 78 -12.648 -20.118 -19.504 1.00 90.80 C ANISOU 224 CA ALA A 78 11864 12520 10117 1070 1330 29 C ATOM 225 C ALA A 78 -12.883 -18.671 -19.932 1.00 89.80 C ANISOU 225 C ALA A 78 11734 12505 9882 953 1364 241 C ATOM 226 O ALA A 78 -12.667 -18.314 -21.091 1.00 77.22 O ANISOU 226 O ALA A 78 10172 11090 8076 950 1484 269 O ATOM 227 CB ALA A 78 -13.973 -20.806 -19.195 1.00 79.83 C ANISOU 227 CB ALA A 78 10614 10983 8737 1055 1138 -55 C ATOM 228 N VAL A 79 -13.316 -17.841 -18.989 1.00 89.35 N ANISOU 228 N VAL A 79 11640 12340 9969 860 1257 389 N ATOM 229 CA VAL A 79 -13.621 -16.442 -19.277 1.00 89.11 C ANISOU 229 CA VAL A 79 11607 12374 9876 748 1257 593 C ATOM 230 C VAL A 79 -12.366 -15.670 -19.684 1.00 92.56 C ANISOU 230 C VAL A 79 11914 12948 10305 728 1440 712 C ATOM 231 O VAL A 79 -12.418 -14.792 -20.546 1.00 93.33 O ANISOU 231 O VAL A 79 12038 13170 10251 662 1503 848 O ATOM 232 CB VAL A 79 -14.264 -15.745 -18.058 1.00 85.26 C ANISOU 232 CB VAL A 79 11091 11727 9576 667 1105 702 C ATOM 233 CG1 VAL A 79 -14.504 -14.272 -18.348 1.00 76.44 C ANISOU 233 CG1 VAL A 79 9963 10658 8423 562 1099 908 C ATOM 234 CG2 VAL A 79 -15.570 -16.432 -17.673 1.00 92.89 C ANISOU 234 CG2 VAL A 79 12172 12572 10549 671 937 605 C ATOM 235 N SER A 80 -11.238 -16.004 -19.065 1.00 89.08 N ANISOU 235 N SER A 80 11329 12483 10035 782 1520 668 N ATOM 236 CA SER A 80 -9.990 -15.290 -19.312 1.00 80.54 C ANISOU 236 CA SER A 80 10090 11518 8994 757 1690 780 C ATOM 237 C SER A 80 -9.382 -15.622 -20.673 1.00 78.74 C ANISOU 237 C SER A 80 9869 11504 8543 812 1892 722 C ATOM 238 O SER A 80 -8.837 -14.747 -21.342 1.00 90.68 O ANISOU 238 O SER A 80 11320 13162 9971 746 2031 872 O ATOM 239 CB SER A 80 -8.975 -15.599 -18.207 1.00 84.12 C ANISOU 239 CB SER A 80 10375 11876 9711 804 1698 738 C ATOM 240 OG SER A 80 -9.350 -14.997 -16.980 1.00 85.96 O ANISOU 240 OG SER A 80 10583 11946 10134 734 1539 830 O ATOM 241 N LEU A 81 -9.479 -16.883 -21.081 1.00 85.86 N ANISOU 241 N LEU A 81 10848 12427 9349 932 1909 505 N ATOM 242 CA LEU A 81 -8.814 -17.347 -22.295 1.00 96.07 C ANISOU 242 CA LEU A 81 12140 13927 10437 1011 2110 403 C ATOM 243 C LEU A 81 -9.675 -17.182 -23.547 1.00104.82 C ANISOU 243 C LEU A 81 13434 15172 11219 981 2115 415 C ATOM 244 O LEU A 81 -9.194 -16.717 -24.580 1.00108.59 O ANISOU 244 O LEU A 81 13904 15862 11495 959 2290 490 O ATOM 245 CB LEU A 81 -8.409 -18.815 -22.141 1.00 94.92 C ANISOU 245 CB LEU A 81 11979 13728 10358 1171 2124 140 C ATOM 246 CG LEU A 81 -7.270 -19.114 -21.162 1.00 94.26 C ANISOU 246 CG LEU A 81 11693 13557 10563 1233 2162 105 C ATOM 247 CD1 LEU A 81 -7.183 -20.607 -20.889 1.00 96.86 C ANISOU 247 CD1 LEU A 81 12048 13775 10979 1387 2106 -149 C ATOM 248 CD2 LEU A 81 -5.948 -18.596 -21.703 1.00 92.90 C ANISOU 248 CD2 LEU A 81 11336 13578 10382 1236 2405 174 C ATOM 249 N GLU A 82 -10.944 -17.565 -23.453 1.00108.38 N ANISOU 249 N GLU A 82 14050 15511 11620 975 1920 347 N ATOM 250 CA GLU A 82 -11.840 -17.535 -24.607 1.00110.62 C ANISOU 250 CA GLU A 82 14520 15909 11602 958 1886 333 C ATOM 251 C GLU A 82 -12.255 -16.116 -24.988 1.00102.41 C ANISOU 251 C GLU A 82 13512 14939 10460 818 1869 598 C ATOM 252 O GLU A 82 -12.883 -15.409 -24.200 1.00 90.72 O ANISOU 252 O GLU A 82 12021 13311 9137 731 1717 734 O ATOM 253 CB GLU A 82 -13.088 -18.378 -24.336 1.00118.36 C ANISOU 253 CB GLU A 82 15646 16731 12594 987 1667 181 C ATOM 254 CG GLU A 82 -12.850 -19.873 -24.420 1.00130.15 C ANISOU 254 CG GLU A 82 17169 18186 14097 1130 1679 -100 C ATOM 255 CD GLU A 82 -12.510 -20.324 -25.827 1.00145.43 C ANISOU 255 CD GLU A 82 19186 20339 15733 1212 1827 -238 C ATOM 256 OE1 GLU A 82 -13.099 -19.780 -26.786 1.00147.31 O ANISOU 256 OE1 GLU A 82 19549 20714 15708 1155 1818 -161 O ATOM 257 OE2 GLU A 82 -11.650 -21.217 -25.973 1.00153.21 O ANISOU 257 OE2 GLU A 82 20112 21360 16741 1338 1949 -428 O ATOM 258 N LYS A 83 -11.902 -15.712 -26.205 1.00104.00 N ANISOU 258 N LYS A 83 13756 15367 10394 801 2024 670 N ATOM 259 CA LYS A 83 -12.297 -14.410 -26.728 1.00 95.58 C ANISOU 259 CA LYS A 83 12740 14375 9200 671 2005 931 C ATOM 260 C LYS A 83 -13.812 -14.329 -26.880 1.00 90.51 C ANISOU 260 C LYS A 83 12277 13645 8467 635 1766 936 C ATOM 261 O LYS A 83 -14.417 -13.293 -26.605 1.00 86.81 O ANISOU 261 O LYS A 83 11820 13096 8069 531 1644 1135 O ATOM 262 CB LYS A 83 -11.634 -14.160 -28.083 1.00101.39 C ANISOU 262 CB LYS A 83 13506 15390 9627 668 2226 993 C ATOM 263 CG LYS A 83 -10.139 -13.906 -28.013 1.00113.43 C ANISOU 263 CG LYS A 83 14827 17025 11246 667 2478 1058 C ATOM 264 CD LYS A 83 -9.830 -12.523 -27.454 1.00120.34 C ANISOU 264 CD LYS A 83 15576 17831 12316 521 2472 1351 C ATOM 265 CE LYS A 83 -8.338 -12.215 -27.504 1.00128.84 C ANISOU 265 CE LYS A 83 16440 19036 13477 504 2728 1432 C ATOM 266 NZ LYS A 83 -7.800 -12.194 -28.896 1.00131.12 N ANISOU 266 NZ LYS A 83 16766 19621 13432 508 2969 1467 N ATOM 267 N LYS A 84 -14.417 -15.426 -27.323 1.00 90.37 N ANISOU 267 N LYS A 84 12393 13637 8308 724 1694 710 N ATOM 268 CA LYS A 84 -15.857 -15.469 -27.553 1.00 85.53 C ANISOU 268 CA LYS A 84 11943 12952 7603 697 1465 690 C ATOM 269 C LYS A 84 -16.648 -15.215 -26.276 1.00 83.60 C ANISOU 269 C LYS A 84 11648 12462 7656 645 1267 738 C ATOM 270 O LYS A 84 -17.764 -14.704 -26.325 1.00 89.47 O ANISOU 270 O LYS A 84 12473 13142 8379 582 1089 824 O ATOM 271 CB LYS A 84 -16.270 -16.820 -28.144 1.00 88.86 C ANISOU 271 CB LYS A 84 12496 13404 7863 806 1419 408 C ATOM 272 CG LYS A 84 -15.766 -17.068 -29.556 1.00 98.42 C ANISOU 272 CG LYS A 84 13801 14876 8718 862 1584 338 C ATOM 273 CD LYS A 84 -16.614 -18.116 -30.264 1.00106.74 C ANISOU 273 CD LYS A 84 15036 15945 9576 938 1454 94 C ATOM 274 CE LYS A 84 -16.062 -18.458 -31.643 1.00120.11 C ANISOU 274 CE LYS A 84 16829 17908 10899 1011 1626 -13 C ATOM 275 NZ LYS A 84 -16.051 -17.287 -32.568 1.00124.19 N ANISOU 275 NZ LYS A 84 17413 18631 11144 918 1694 239 N ATOM 276 N LEU A 85 -16.069 -15.570 -25.134 1.00 78.43 N ANISOU 276 N LEU A 85 10856 11673 7270 675 1297 680 N ATOM 277 CA LEU A 85 -16.780 -15.470 -23.864 1.00 88.31 C ANISOU 277 CA LEU A 85 12064 12704 8788 637 1124 699 C ATOM 278 C LEU A 85 -16.556 -14.131 -23.165 1.00 86.06 C ANISOU 278 C LEU A 85 11666 12359 8674 539 1119 931 C ATOM 279 O LEU A 85 -17.139 -13.872 -22.112 1.00 72.49 O ANISOU 279 O LEU A 85 9907 10473 7162 503 985 962 O ATOM 280 CB LEU A 85 -16.366 -16.618 -22.938 1.00 83.66 C ANISOU 280 CB LEU A 85 11405 11989 8393 720 1129 512 C ATOM 281 CG LEU A 85 -16.861 -18.008 -23.346 1.00 83.38 C ANISOU 281 CG LEU A 85 11485 11932 8264 809 1066 268 C ATOM 282 CD1 LEU A 85 -16.217 -19.086 -22.487 1.00 86.62 C ANISOU 282 CD1 LEU A 85 11815 12223 8873 895 1095 108 C ATOM 283 CD2 LEU A 85 -18.377 -18.084 -23.244 1.00 80.82 C ANISOU 283 CD2 LEU A 85 11269 11501 7940 759 847 252 C ATOM 284 N GLN A 86 -15.724 -13.277 -23.753 1.00 83.91 N ANISOU 284 N GLN A 86 11342 12223 8316 495 1267 1093 N ATOM 285 CA GLN A 86 -15.389 -12.003 -23.125 1.00 81.24 C ANISOU 285 CA GLN A 86 10890 11820 8157 401 1266 1310 C ATOM 286 C GLN A 86 -16.394 -10.905 -23.466 1.00 77.82 C ANISOU 286 C GLN A 86 10540 11360 7668 310 1125 1491 C ATOM 287 O GLN A 86 -16.077 -9.959 -24.186 1.00 83.02 O ANISOU 287 O GLN A 86 11204 12121 8220 241 1192 1684 O ATOM 288 CB GLN A 86 -13.977 -11.566 -23.516 1.00 90.30 C ANISOU 288 CB GLN A 86 11920 13107 9283 382 1489 1414 C ATOM 289 CG GLN A 86 -12.882 -12.358 -22.827 1.00 90.25 C ANISOU 289 CG GLN A 86 11772 13078 9440 460 1605 1275 C ATOM 290 CD GLN A 86 -11.494 -11.905 -23.232 1.00 97.84 C ANISOU 290 CD GLN A 86 12594 14186 10396 437 1829 1379 C ATOM 291 OE1 GLN A 86 -11.283 -10.743 -23.579 1.00 98.86 O ANISOU 291 OE1 GLN A 86 12690 14368 10504 331 1874 1603 O ATOM 292 NE2 GLN A 86 -10.538 -12.826 -23.195 1.00104.38 N ANISOU 292 NE2 GLN A 86 13332 15075 11254 535 1971 1220 N ATOM 293 N TYR A 87 -17.606 -11.039 -22.939 1.00 73.56 N ANISOU 293 N TYR A 87 10059 10681 7210 310 927 1433 N ATOM 294 CA TYR A 87 -18.610 -9.987 -23.049 1.00 82.46 C ANISOU 294 CA TYR A 87 11239 11747 8347 236 768 1590 C ATOM 295 C TYR A 87 -19.180 -9.652 -21.668 1.00 84.08 C ANISOU 295 C TYR A 87 11363 11747 8836 215 630 1584 C ATOM 296 O TYR A 87 -18.968 -10.387 -20.702 1.00 76.83 O ANISOU 296 O TYR A 87 10381 10743 8068 260 639 1446 O ATOM 297 CB TYR A 87 -19.720 -10.390 -24.024 1.00 83.22 C ANISOU 297 CB TYR A 87 11499 11907 8215 255 650 1530 C ATOM 298 CG TYR A 87 -20.193 -11.812 -23.862 1.00 90.65 C ANISOU 298 CG TYR A 87 12492 12815 9134 337 600 1278 C ATOM 299 CD1 TYR A 87 -19.600 -12.849 -24.570 1.00 95.34 C ANISOU 299 CD1 TYR A 87 13140 13539 9547 410 724 1124 C ATOM 300 CD2 TYR A 87 -21.235 -12.119 -23.002 1.00 97.59 C ANISOU 300 CD2 TYR A 87 13365 13533 10183 339 432 1192 C ATOM 301 CE1 TYR A 87 -20.033 -14.153 -24.422 1.00100.82 C ANISOU 301 CE1 TYR A 87 13886 14180 10243 482 663 892 C ATOM 302 CE2 TYR A 87 -21.675 -13.418 -22.848 1.00102.49 C ANISOU 302 CE2 TYR A 87 14031 14110 10800 399 382 977 C ATOM 303 CZ TYR A 87 -21.070 -14.432 -23.560 1.00101.89 C ANISOU 303 CZ TYR A 87 14014 14143 10556 470 489 828 C ATOM 304 OH TYR A 87 -21.503 -15.730 -23.412 1.00101.05 O ANISOU 304 OH TYR A 87 13956 13973 10467 528 425 613 O ATOM 305 N ALA A 88 -19.901 -8.539 -21.590 1.00 84.78 N ANISOU 305 N ALA A 88 11459 11760 8994 152 501 1734 N ATOM 306 CA ALA A 88 -20.311 -7.955 -20.314 1.00 73.77 C ANISOU 306 CA ALA A 88 9975 10187 7867 128 392 1753 C ATOM 307 C ALA A 88 -20.854 -8.963 -19.303 1.00 77.66 C ANISOU 307 C ALA A 88 10450 10580 8477 182 328 1556 C ATOM 308 O ALA A 88 -20.307 -9.104 -18.211 1.00 85.55 O ANISOU 308 O ALA A 88 11353 11500 9651 192 366 1508 O ATOM 309 CB ALA A 88 -21.335 -6.856 -20.550 1.00 72.90 C ANISOU 309 CB ALA A 88 9904 10011 7783 78 229 1892 C ATOM 310 N THR A 89 -21.931 -9.653 -19.660 1.00 77.79 N ANISOU 310 N THR A 89 10559 10600 8399 209 224 1450 N ATOM 311 CA THR A 89 -22.657 -10.471 -18.693 1.00 80.40 C ANISOU 311 CA THR A 89 10871 10821 8855 238 142 1295 C ATOM 312 C THR A 89 -21.806 -11.580 -18.071 1.00 80.44 C ANISOU 312 C THR A 89 10836 10815 8910 288 250 1159 C ATOM 313 O THR A 89 -22.129 -12.078 -16.993 1.00 78.90 O ANISOU 313 O THR A 89 10601 10516 8862 300 204 1071 O ATOM 314 CB THR A 89 -23.928 -11.098 -19.309 1.00 79.65 C ANISOU 314 CB THR A 89 10877 10736 8648 251 13 1203 C ATOM 315 OG1 THR A 89 -24.707 -11.713 -18.275 1.00 89.89 O ANISOU 315 OG1 THR A 89 12137 11917 10101 259 -69 1086 O ATOM 316 CG2 THR A 89 -23.569 -12.136 -20.350 1.00 73.38 C ANISOU 316 CG2 THR A 89 10182 10063 7636 297 81 1096 C ATOM 317 N ASN A 90 -20.726 -11.967 -18.743 1.00 85.19 N ANISOU 317 N ASN A 90 11448 11529 9392 321 393 1144 N ATOM 318 CA ASN A 90 -19.852 -13.014 -18.216 1.00 87.87 C ANISOU 318 CA ASN A 90 11742 11855 9790 381 490 1014 C ATOM 319 C ASN A 90 -18.875 -12.497 -17.165 1.00 83.97 C ANISOU 319 C ASN A 90 11114 11301 9488 367 554 1080 C ATOM 320 O ASN A 90 -18.216 -13.282 -16.484 1.00 84.38 O ANISOU 320 O ASN A 90 11116 11313 9633 415 602 984 O ATOM 321 CB ASN A 90 -19.079 -13.700 -19.345 1.00 90.11 C ANISOU 321 CB ASN A 90 12075 12285 9878 437 622 944 C ATOM 322 CG ASN A 90 -19.896 -14.769 -20.047 1.00 84.27 C ANISOU 322 CG ASN A 90 11462 11568 8988 481 552 787 C ATOM 323 OD1 ASN A 90 -20.966 -15.160 -19.578 1.00 81.07 O ANISOU 323 OD1 ASN A 90 11092 11056 8654 469 411 721 O ATOM 324 ND2 ASN A 90 -19.387 -15.257 -21.171 1.00 83.02 N ANISOU 324 ND2 ASN A 90 11369 11552 8623 530 653 720 N ATOM 325 N TYR A 91 -18.778 -11.178 -17.036 1.00 83.04 N ANISOU 325 N TYR A 91 10943 11169 9439 303 539 1242 N ATOM 326 CA TYR A 91 -17.911 -10.579 -16.028 1.00 80.06 C ANISOU 326 CA TYR A 91 10440 10725 9255 282 575 1303 C ATOM 327 C TYR A 91 -18.516 -10.731 -14.634 1.00 72.85 C ANISOU 327 C TYR A 91 9499 9669 8513 285 463 1235 C ATOM 328 O TYR A 91 -17.797 -10.753 -13.635 1.00 61.41 O ANISOU 328 O TYR A 91 7963 8162 7208 294 484 1219 O ATOM 329 CB TYR A 91 -17.644 -9.111 -16.357 1.00 78.83 C ANISOU 329 CB TYR A 91 10240 10583 9129 207 582 1496 C ATOM 330 CG TYR A 91 -16.813 -8.929 -17.605 1.00 90.09 C ANISOU 330 CG TYR A 91 11672 12162 10395 193 724 1586 C ATOM 331 CD1 TYR A 91 -15.669 -9.690 -17.817 1.00104.50 C ANISOU 331 CD1 TYR A 91 13444 14079 12183 242 880 1516 C ATOM 332 CD2 TYR A 91 -17.177 -8.013 -18.578 1.00 91.28 C ANISOU 332 CD2 TYR A 91 11881 12372 10429 133 705 1743 C ATOM 333 CE1 TYR A 91 -14.906 -9.533 -18.959 1.00107.91 C ANISOU 333 CE1 TYR A 91 13874 14672 12457 230 1031 1593 C ATOM 334 CE2 TYR A 91 -16.424 -7.849 -19.722 1.00101.50 C ANISOU 334 CE2 TYR A 91 13187 13823 11554 113 848 1839 C ATOM 335 CZ TYR A 91 -15.289 -8.611 -19.909 1.00108.80 C ANISOU 335 CZ TYR A 91 14052 14852 12436 161 1021 1759 C ATOM 336 OH TYR A 91 -14.533 -8.451 -21.049 1.00117.87 O ANISOU 336 OH TYR A 91 15204 16177 13406 142 1184 1849 O ATOM 337 N PHE A 92 -19.839 -10.841 -14.570 1.00 63.14 N ANISOU 337 N PHE A 92 8337 8390 7261 276 345 1197 N ATOM 338 CA PHE A 92 -20.497 -11.229 -13.332 1.00 63.98 C ANISOU 338 CA PHE A 92 8428 8387 7495 283 261 1114 C ATOM 339 C PHE A 92 -19.988 -12.598 -12.908 1.00 64.33 C ANISOU 339 C PHE A 92 8477 8419 7545 338 310 986 C ATOM 340 O PHE A 92 -19.547 -12.784 -11.775 1.00 67.59 O ANISOU 340 O PHE A 92 8833 8765 8084 349 309 960 O ATOM 341 CB PHE A 92 -22.011 -11.294 -13.516 1.00 71.32 C ANISOU 341 CB PHE A 92 9423 9288 8388 266 142 1082 C ATOM 342 CG PHE A 92 -22.676 -9.954 -13.551 1.00 80.31 C ANISOU 342 CG PHE A 92 10540 10395 9581 222 59 1191 C ATOM 343 CD1 PHE A 92 -23.055 -9.324 -12.378 1.00 84.08 C ANISOU 343 CD1 PHE A 92 10951 10777 10220 206 -2 1196 C ATOM 344 CD2 PHE A 92 -22.933 -9.327 -14.759 1.00 91.75 C ANISOU 344 CD2 PHE A 92 12039 11907 10915 201 36 1287 C ATOM 345 CE1 PHE A 92 -23.672 -8.088 -12.407 1.00 92.68 C ANISOU 345 CE1 PHE A 92 12015 11822 11377 177 -86 1281 C ATOM 346 CE2 PHE A 92 -23.550 -8.092 -14.796 1.00 96.47 C ANISOU 346 CE2 PHE A 92 12617 12457 11580 166 -58 1393 C ATOM 347 CZ PHE A 92 -23.920 -7.472 -13.618 1.00 97.95 C ANISOU 347 CZ PHE A 92 12729 12537 11951 158 -120 1384 C ATOM 348 N LEU A 93 -20.056 -13.552 -13.833 1.00 62.59 N ANISOU 348 N LEU A 93 8332 8260 7188 376 342 905 N ATOM 349 CA LEU A 93 -19.639 -14.921 -13.562 1.00 66.23 C ANISOU 349 CA LEU A 93 8810 8695 7660 436 375 774 C ATOM 350 C LEU A 93 -18.196 -14.978 -13.079 1.00 60.82 C ANISOU 350 C LEU A 93 8032 8015 7062 474 471 783 C ATOM 351 O LEU A 93 -17.875 -15.718 -12.151 1.00 69.61 O ANISOU 351 O LEU A 93 9120 9050 8278 506 456 719 O ATOM 352 CB LEU A 93 -19.805 -15.783 -14.813 1.00 61.98 C ANISOU 352 CB LEU A 93 8367 8233 6952 478 400 680 C ATOM 353 CG LEU A 93 -21.250 -16.110 -15.186 1.00 92.90 C ANISOU 353 CG LEU A 93 12374 12122 10801 451 280 629 C ATOM 354 CD1 LEU A 93 -21.314 -16.727 -16.570 1.00 99.05 C ANISOU 354 CD1 LEU A 93 13251 12997 11387 490 302 545 C ATOM 355 CD2 LEU A 93 -21.864 -17.044 -14.156 1.00 97.32 C ANISOU 355 CD2 LEU A 93 12939 12556 11483 449 202 542 C ATOM 356 N MET A 94 -17.325 -14.200 -13.710 1.00 61.73 N ANISOU 356 N MET A 94 8094 8221 7141 465 567 871 N ATOM 357 CA MET A 94 -15.924 -14.173 -13.312 1.00 70.80 C ANISOU 357 CA MET A 94 9130 9382 8388 495 660 886 C ATOM 358 C MET A 94 -15.792 -13.613 -11.901 1.00 71.04 C ANISOU 358 C MET A 94 9084 9307 8602 462 587 934 C ATOM 359 O MET A 94 -14.974 -14.083 -11.111 1.00 66.82 O ANISOU 359 O MET A 94 8483 8728 8178 502 599 892 O ATOM 360 CB MET A 94 -15.095 -13.340 -14.292 1.00 65.10 C ANISOU 360 CB MET A 94 8354 8785 7595 471 781 992 C ATOM 361 CG MET A 94 -13.634 -13.197 -13.884 1.00 66.89 C ANISOU 361 CG MET A 94 8438 9028 7949 491 877 1018 C ATOM 362 SD MET A 94 -12.521 -13.028 -15.289 1.00101.53 S ANISOU 362 SD MET A 94 12770 13601 12208 504 1078 1065 S ATOM 363 CE MET A 94 -10.960 -12.750 -14.456 1.00136.61 C ANISOU 363 CE MET A 94 17011 18021 16874 511 1148 1102 C ATOM 364 N SER A 95 -16.601 -12.606 -11.589 1.00 67.82 N ANISOU 364 N SER A 95 8686 8858 8225 396 505 1014 N ATOM 365 CA SER A 95 -16.574 -11.991 -10.269 1.00 65.44 C ANISOU 365 CA SER A 95 8323 8463 8079 368 431 1045 C ATOM 366 C SER A 95 -17.103 -12.951 -9.209 1.00 60.20 C ANISOU 366 C SER A 95 7699 7717 7458 396 359 946 C ATOM 367 O SER A 95 -16.594 -12.996 -8.091 1.00 63.98 O ANISOU 367 O SER A 95 8126 8138 8047 406 329 935 O ATOM 368 CB SER A 95 -17.403 -10.708 -10.262 1.00 69.71 C ANISOU 368 CB SER A 95 8870 8976 8643 302 358 1136 C ATOM 369 OG SER A 95 -17.344 -10.081 -8.994 1.00 67.64 O ANISOU 369 OG SER A 95 8548 8627 8525 282 289 1146 O ATOM 370 N LEU A 96 -18.130 -13.712 -9.568 1.00 61.65 N ANISOU 370 N LEU A 96 7976 7896 7553 403 324 882 N ATOM 371 CA LEU A 96 -18.706 -14.702 -8.669 1.00 59.44 C ANISOU 371 CA LEU A 96 7738 7538 7307 416 263 802 C ATOM 372 C LEU A 96 -17.723 -15.845 -8.466 1.00 61.15 C ANISOU 372 C LEU A 96 7945 7735 7553 483 303 735 C ATOM 373 O LEU A 96 -17.586 -16.374 -7.365 1.00 60.85 O ANISOU 373 O LEU A 96 7902 7624 7594 495 258 711 O ATOM 374 CB LEU A 96 -20.018 -15.236 -9.250 1.00 61.65 C ANISOU 374 CB LEU A 96 8109 7818 7498 399 216 753 C ATOM 375 CG LEU A 96 -20.698 -16.388 -8.508 1.00 56.79 C ANISOU 375 CG LEU A 96 7542 7122 6912 400 159 678 C ATOM 376 CD1 LEU A 96 -20.980 -16.014 -7.066 1.00 68.66 C ANISOU 376 CD1 LEU A 96 9010 8569 8510 366 113 710 C ATOM 377 CD2 LEU A 96 -21.983 -16.779 -9.219 1.00 73.62 C ANISOU 377 CD2 LEU A 96 9745 9258 8970 372 108 635 C ATOM 378 N ALA A 97 -17.040 -16.219 -9.543 1.00 70.97 N ANISOU 378 N ALA A 97 9188 9048 8730 529 387 703 N ATOM 379 CA ALA A 97 -16.083 -17.316 -9.506 1.00 68.58 C ANISOU 379 CA ALA A 97 8867 8727 8462 609 430 623 C ATOM 380 C ALA A 97 -14.941 -17.002 -8.547 1.00 73.74 C ANISOU 380 C ALA A 97 9412 9351 9252 627 436 664 C ATOM 381 O ALA A 97 -14.531 -17.854 -7.760 1.00 80.22 O ANISOU 381 O ALA A 97 10227 10098 10155 673 396 617 O ATOM 382 CB ALA A 97 -15.545 -17.590 -10.899 1.00 69.76 C ANISOU 382 CB ALA A 97 9023 8980 8504 659 537 576 C ATOM 383 N VAL A 98 -14.432 -15.777 -8.617 1.00 77.06 N ANISOU 383 N VAL A 98 9749 9824 9705 587 472 756 N ATOM 384 CA VAL A 98 -13.363 -15.344 -7.726 1.00 77.49 C ANISOU 384 CA VAL A 98 9691 9851 9900 593 462 797 C ATOM 385 C VAL A 98 -13.823 -15.397 -6.273 1.00 74.20 C ANISOU 385 C VAL A 98 9302 9336 9556 573 342 796 C ATOM 386 O VAL A 98 -13.085 -15.847 -5.398 1.00 70.35 O ANISOU 386 O VAL A 98 8771 8797 9162 612 302 777 O ATOM 387 CB VAL A 98 -12.897 -13.913 -8.062 1.00 72.57 C ANISOU 387 CB VAL A 98 8978 9285 9309 533 506 905 C ATOM 388 CG1 VAL A 98 -12.014 -13.360 -6.950 1.00 67.62 C ANISOU 388 CG1 VAL A 98 8243 8607 8844 523 455 942 C ATOM 389 CG2 VAL A 98 -12.163 -13.893 -9.397 1.00 74.04 C ANISOU 389 CG2 VAL A 98 9118 9587 9428 554 647 920 C ATOM 390 N ALA A 99 -15.044 -14.935 -6.024 1.00 71.04 N ANISOU 390 N ALA A 99 8970 8915 9109 514 284 817 N ATOM 391 CA ALA A 99 -15.604 -14.941 -4.679 1.00 56.58 C ANISOU 391 CA ALA A 99 7169 7012 7319 490 188 814 C ATOM 392 C ALA A 99 -15.667 -16.364 -4.130 1.00 64.70 C ANISOU 392 C ALA A 99 8258 7979 8347 533 152 754 C ATOM 393 O ALA A 99 -15.226 -16.625 -3.010 1.00 56.60 O ANISOU 393 O ALA A 99 7219 6902 7385 548 93 758 O ATOM 394 CB ALA A 99 -16.985 -14.312 -4.682 1.00 55.87 C ANISOU 394 CB ALA A 99 7132 6923 7173 429 152 831 C ATOM 395 N ASP A 100 -16.215 -17.279 -4.926 1.00 60.54 N ANISOU 395 N ASP A 100 7802 7451 7749 551 178 702 N ATOM 396 CA ASP A 100 -16.323 -18.679 -4.531 1.00 63.19 C ANISOU 396 CA ASP A 100 8201 7708 8098 587 137 647 C ATOM 397 C ASP A 100 -14.946 -19.327 -4.416 1.00 71.32 C ANISOU 397 C ASP A 100 9174 8712 9211 671 150 619 C ATOM 398 O ASP A 100 -14.723 -20.187 -3.563 1.00 77.54 O ANISOU 398 O ASP A 100 9989 9416 10057 701 84 609 O ATOM 399 CB ASP A 100 -17.169 -19.455 -5.539 1.00 62.06 C ANISOU 399 CB ASP A 100 8141 7565 7875 587 154 584 C ATOM 400 CG ASP A 100 -18.614 -19.003 -5.559 1.00 69.83 C ANISOU 400 CG ASP A 100 9175 8560 8798 507 121 606 C ATOM 401 OD1 ASP A 100 -19.120 -18.576 -4.501 1.00 73.92 O ANISOU 401 OD1 ASP A 100 9688 9055 9344 459 75 651 O ATOM 402 OD2 ASP A 100 -19.246 -19.078 -6.634 1.00 73.80 O ANISOU 402 OD2 ASP A 100 9717 9099 9223 498 139 570 O ATOM 403 N LEU A 101 -14.028 -18.919 -5.285 1.00 62.72 N ANISOU 403 N LEU A 101 8004 7696 8130 710 236 611 N ATOM 404 CA LEU A 101 -12.671 -19.448 -5.260 1.00 68.39 C ANISOU 404 CA LEU A 101 8639 8404 8943 797 260 577 C ATOM 405 C LEU A 101 -11.984 -19.097 -3.946 1.00 72.85 C ANISOU 405 C LEU A 101 9138 8923 9621 795 180 631 C ATOM 406 O LEU A 101 -11.276 -19.922 -3.366 1.00 71.61 O ANISOU 406 O LEU A 101 8961 8698 9551 861 127 605 O ATOM 407 CB LEU A 101 -11.857 -18.888 -6.429 1.00 81.45 C ANISOU 407 CB LEU A 101 10198 10169 10578 822 387 572 C ATOM 408 CG LEU A 101 -10.379 -19.292 -6.459 1.00 85.30 C ANISOU 408 CG LEU A 101 10563 10666 11181 913 433 536 C ATOM 409 CD1 LEU A 101 -10.228 -20.777 -6.754 1.00 81.45 C ANISOU 409 CD1 LEU A 101 10123 10119 10705 1014 431 419 C ATOM 410 CD2 LEU A 101 -9.614 -18.461 -7.476 1.00 82.62 C ANISOU 410 CD2 LEU A 101 10111 10457 10824 908 572 565 C ATOM 411 N LEU A 102 -12.189 -17.867 -3.486 1.00 77.27 N ANISOU 411 N LEU A 102 9665 9513 10180 723 159 701 N ATOM 412 CA LEU A 102 -11.524 -17.379 -2.284 1.00 78.23 C ANISOU 412 CA LEU A 102 9723 9601 10398 717 75 742 C ATOM 413 C LEU A 102 -12.061 -18.057 -1.028 1.00 79.83 C ANISOU 413 C LEU A 102 10021 9722 10589 711 -38 745 C ATOM 414 O LEU A 102 -11.327 -18.246 -0.057 1.00 80.75 O ANISOU 414 O LEU A 102 10106 9795 10781 742 -122 759 O ATOM 415 CB LEU A 102 -11.667 -15.861 -2.172 1.00 74.51 C ANISOU 415 CB LEU A 102 9201 9175 9934 641 76 801 C ATOM 416 CG LEU A 102 -10.901 -15.056 -3.225 1.00 67.30 C ANISOU 416 CG LEU A 102 8175 8338 9059 633 177 832 C ATOM 417 CD1 LEU A 102 -11.265 -13.583 -3.143 1.00 66.37 C ANISOU 417 CD1 LEU A 102 8030 8236 8950 550 161 897 C ATOM 418 CD2 LEU A 102 -9.403 -15.242 -3.058 1.00 63.32 C ANISOU 418 CD2 LEU A 102 7535 7835 8690 690 184 826 C ATOM 419 N VAL A 103 -13.340 -18.416 -1.043 1.00 71.40 N ANISOU 419 N VAL A 103 9067 8638 9425 668 -42 739 N ATOM 420 CA VAL A 103 -13.914 -19.183 0.056 1.00 68.83 C ANISOU 420 CA VAL A 103 8835 8241 9075 653 -130 754 C ATOM 421 C VAL A 103 -13.171 -20.508 0.181 1.00 71.02 C ANISOU 421 C VAL A 103 9125 8437 9421 733 -171 730 C ATOM 422 O VAL A 103 -12.856 -20.952 1.284 1.00 77.07 O ANISOU 422 O VAL A 103 9917 9143 10221 748 -267 765 O ATOM 423 CB VAL A 103 -15.415 -19.464 -0.157 1.00 66.46 C ANISOU 423 CB VAL A 103 8636 7937 8678 591 -112 749 C ATOM 424 CG1 VAL A 103 -15.948 -20.370 0.943 1.00 71.62 C ANISOU 424 CG1 VAL A 103 9381 8519 9311 568 -188 779 C ATOM 425 CG2 VAL A 103 -16.202 -18.165 -0.201 1.00 68.59 C ANISOU 425 CG2 VAL A 103 8890 8277 8896 522 -85 768 C ATOM 426 N GLY A 104 -12.886 -21.129 -0.960 1.00 71.05 N ANISOU 426 N GLY A 104 9113 8439 9444 790 -104 667 N ATOM 427 CA GLY A 104 -12.202 -22.409 -0.989 1.00 75.69 C ANISOU 427 CA GLY A 104 9707 8938 10114 881 -141 624 C ATOM 428 C GLY A 104 -10.745 -22.333 -0.569 1.00 75.42 C ANISOU 428 C GLY A 104 9556 8896 10205 958 -177 628 C ATOM 429 O GLY A 104 -10.198 -23.297 -0.034 1.00 79.17 O ANISOU 429 O GLY A 104 10041 9274 10765 1026 -262 623 O ATOM 430 N LEU A 105 -10.115 -21.187 -0.809 1.00 74.55 N ANISOU 430 N LEU A 105 9329 8877 10119 946 -123 643 N ATOM 431 CA LEU A 105 -8.696 -21.015 -0.509 1.00 76.56 C ANISOU 431 CA LEU A 105 9444 9134 10511 1012 -152 645 C ATOM 432 C LEU A 105 -8.436 -20.578 0.931 1.00 76.30 C ANISOU 432 C LEU A 105 9407 9068 10516 982 -289 711 C ATOM 433 O LEU A 105 -7.561 -21.126 1.602 1.00 79.66 O ANISOU 433 O LEU A 105 9790 9431 11046 1050 -388 715 O ATOM 434 CB LEU A 105 -8.072 -19.989 -1.459 1.00 69.37 C ANISOU 434 CB LEU A 105 8397 8336 9625 1002 -28 639 C ATOM 435 CG LEU A 105 -7.800 -20.449 -2.891 1.00 75.91 C ANISOU 435 CG LEU A 105 9185 9220 10437 1063 114 563 C ATOM 436 CD1 LEU A 105 -7.400 -19.265 -3.755 1.00 83.35 C ANISOU 436 CD1 LEU A 105 10015 10288 11367 1019 240 594 C ATOM 437 CD2 LEU A 105 -6.717 -21.516 -2.916 1.00 81.37 C ANISOU 437 CD2 LEU A 105 9798 9857 11260 1190 98 492 C ATOM 438 N PHE A 106 -9.194 -19.594 1.402 1.00 71.08 N ANISOU 438 N PHE A 106 8790 8448 9768 888 -302 756 N ATOM 439 CA PHE A 106 -8.886 -18.939 2.669 1.00 74.94 C ANISOU 439 CA PHE A 106 9264 8930 10280 859 -421 801 C ATOM 440 C PHE A 106 -9.856 -19.287 3.798 1.00 81.66 C ANISOU 440 C PHE A 106 10266 9741 11018 813 -510 839 C ATOM 441 O PHE A 106 -9.477 -19.269 4.969 1.00 81.70 O ANISOU 441 O PHE A 106 10288 9722 11033 818 -634 871 O ATOM 442 CB PHE A 106 -8.844 -17.422 2.463 1.00 71.26 C ANISOU 442 CB PHE A 106 8716 8539 9821 793 -378 813 C ATOM 443 CG PHE A 106 -7.745 -16.968 1.540 1.00 89.43 C ANISOU 443 CG PHE A 106 10853 10885 12244 822 -297 801 C ATOM 444 CD1 PHE A 106 -6.437 -17.376 1.748 1.00 95.91 C ANISOU 444 CD1 PHE A 106 11554 11680 13208 898 -346 788 C ATOM 445 CD2 PHE A 106 -8.021 -16.148 0.457 1.00 88.72 C ANISOU 445 CD2 PHE A 106 10721 10865 12124 774 -172 809 C ATOM 446 CE1 PHE A 106 -5.423 -16.966 0.901 1.00 94.51 C ANISOU 446 CE1 PHE A 106 11207 11556 13147 920 -255 779 C ATOM 447 CE2 PHE A 106 -7.010 -15.737 -0.394 1.00 86.57 C ANISOU 447 CE2 PHE A 106 10295 10646 11952 790 -82 814 C ATOM 448 CZ PHE A 106 -5.711 -16.146 -0.171 1.00 93.07 C ANISOU 448 CZ PHE A 106 10988 11452 12921 861 -115 797 C ATOM 449 N VAL A 107 -11.098 -19.612 3.452 1.00 79.25 N ANISOU 449 N VAL A 107 10069 9439 10605 765 -449 838 N ATOM 450 CA VAL A 107 -12.129 -19.830 4.462 1.00 74.11 C ANISOU 450 CA VAL A 107 9546 8772 9839 705 -504 880 C ATOM 451 C VAL A 107 -12.291 -21.306 4.847 1.00 79.88 C ANISOU 451 C VAL A 107 10376 9408 10566 732 -564 912 C ATOM 452 O VAL A 107 -12.272 -21.647 6.031 1.00 79.53 O ANISOU 452 O VAL A 107 10401 9332 10485 722 -667 970 O ATOM 453 CB VAL A 107 -13.490 -19.276 3.995 1.00 72.31 C ANISOU 453 CB VAL A 107 9365 8599 9508 626 -413 869 C ATOM 454 CG1 VAL A 107 -14.537 -19.437 5.088 1.00 69.89 C ANISOU 454 CG1 VAL A 107 9170 8296 9088 562 -453 909 C ATOM 455 CG2 VAL A 107 -13.355 -17.815 3.591 1.00 70.41 C ANISOU 455 CG2 VAL A 107 9034 8433 9286 600 -367 848 C ATOM 456 N MET A 108 -12.445 -22.176 3.853 1.00 73.54 N ANISOU 456 N MET A 108 9586 8557 9798 765 -507 874 N ATOM 457 CA MET A 108 -12.754 -23.582 4.115 1.00 69.67 C ANISOU 457 CA MET A 108 9198 7956 9317 779 -564 902 C ATOM 458 C MET A 108 -11.647 -24.312 4.881 1.00 70.57 C ANISOU 458 C MET A 108 9303 7980 9529 859 -693 938 C ATOM 459 O MET A 108 -11.933 -25.029 5.839 1.00 66.18 O ANISOU 459 O MET A 108 8851 7354 8941 836 -788 1018 O ATOM 460 CB MET A 108 -13.060 -24.323 2.809 1.00 73.90 C ANISOU 460 CB MET A 108 9743 8451 9886 808 -486 829 C ATOM 461 CG MET A 108 -14.336 -23.869 2.116 1.00 70.22 C ANISOU 461 CG MET A 108 9314 8050 9319 724 -390 805 C ATOM 462 SD MET A 108 -14.808 -24.960 0.756 1.00 76.73 S ANISOU 462 SD MET A 108 10182 8807 10165 753 -339 717 S ATOM 463 CE MET A 108 -16.031 -23.958 -0.084 1.00112.17 C ANISOU 463 CE MET A 108 14670 13411 14536 665 -237 692 C ATOM 464 N PRO A 109 -10.383 -24.142 4.459 1.00 75.54 N ANISOU 464 N PRO A 109 9805 8615 10283 952 -698 887 N ATOM 465 CA PRO A 109 -9.281 -24.848 5.127 1.00 69.51 C ANISOU 465 CA PRO A 109 9014 7761 9637 1042 -833 914 C ATOM 466 C PRO A 109 -9.130 -24.469 6.599 1.00 70.44 C ANISOU 466 C PRO A 109 9176 7891 9699 1006 -967 1004 C ATOM 467 O PRO A 109 -8.714 -25.304 7.400 1.00 71.67 O ANISOU 467 O PRO A 109 9385 7952 9895 1048 -1105 1066 O ATOM 468 CB PRO A 109 -8.045 -24.405 4.334 1.00 65.82 C ANISOU 468 CB PRO A 109 8366 7336 9305 1130 -781 835 C ATOM 469 CG PRO A 109 -8.572 -23.945 3.021 1.00 69.03 C ANISOU 469 CG PRO A 109 8742 7824 9661 1100 -610 764 C ATOM 470 CD PRO A 109 -9.903 -23.335 3.325 1.00 72.57 C ANISOU 470 CD PRO A 109 9297 8326 9949 978 -579 810 C ATOM 471 N ILE A 110 -9.452 -23.227 6.947 1.00 73.68 N ANISOU 471 N ILE A 110 9569 8411 10015 933 -935 1008 N ATOM 472 CA ILE A 110 -9.415 -22.803 8.340 1.00 79.54 C ANISOU 472 CA ILE A 110 10368 9181 10673 895 -1056 1074 C ATOM 473 C ILE A 110 -10.613 -23.404 9.067 1.00 75.91 C ANISOU 473 C ILE A 110 10080 8702 10059 818 -1069 1155 C ATOM 474 O ILE A 110 -10.491 -23.902 10.187 1.00 72.25 O ANISOU 474 O ILE A 110 9708 8202 9543 816 -1196 1240 O ATOM 475 CB ILE A 110 -9.447 -21.270 8.477 1.00 80.84 C ANISOU 475 CB ILE A 110 10464 9460 10792 844 -1020 1036 C ATOM 476 CG1 ILE A 110 -8.332 -20.630 7.646 1.00 79.85 C ANISOU 476 CG1 ILE A 110 10157 9357 10827 899 -985 970 C ATOM 477 CG2 ILE A 110 -9.309 -20.864 9.935 1.00 81.19 C ANISOU 477 CG2 ILE A 110 10568 9533 10746 819 -1159 1081 C ATOM 478 CD1 ILE A 110 -6.939 -21.080 8.033 1.00 85.67 C ANISOU 478 CD1 ILE A 110 10805 10034 11714 993 -1118 977 C ATOM 479 N ALA A 111 -11.772 -23.358 8.419 1.00 75.07 N ANISOU 479 N ALA A 111 10017 8626 9882 750 -939 1134 N ATOM 480 CA ALA A 111 -12.968 -24.000 8.948 1.00 76.41 C ANISOU 480 CA ALA A 111 10328 8777 9928 668 -928 1210 C ATOM 481 C ALA A 111 -12.682 -25.478 9.169 1.00 72.62 C ANISOU 481 C ALA A 111 9924 8152 9518 708 -1025 1281 C ATOM 482 O ALA A 111 -13.195 -26.089 10.105 1.00 70.04 O ANISOU 482 O ALA A 111 9719 7791 9101 652 -1086 1389 O ATOM 483 CB ALA A 111 -14.130 -23.828 7.986 1.00 80.48 C ANISOU 483 CB ALA A 111 10846 9328 10406 604 -783 1162 C ATOM 484 N LEU A 112 -11.851 -26.040 8.298 1.00 82.03 N ANISOU 484 N LEU A 112 11039 9257 10871 805 -1036 1221 N ATOM 485 CA LEU A 112 -11.489 -27.450 8.368 1.00 83.55 C ANISOU 485 CA LEU A 112 11289 9289 11169 864 -1136 1267 C ATOM 486 C LEU A 112 -10.539 -27.711 9.534 1.00 91.73 C ANISOU 486 C LEU A 112 12344 10276 12233 917 -1313 1353 C ATOM 487 O LEU A 112 -10.618 -28.749 10.190 1.00 92.91 O ANISOU 487 O LEU A 112 12602 10309 12389 915 -1425 1459 O ATOM 488 CB LEU A 112 -10.847 -27.889 7.050 1.00 82.34 C ANISOU 488 CB LEU A 112 11035 9071 11180 969 -1086 1148 C ATOM 489 CG LEU A 112 -10.475 -29.367 6.934 1.00 88.29 C ANISOU 489 CG LEU A 112 11834 9638 12073 1048 -1183 1161 C ATOM 490 CD1 LEU A 112 -11.704 -30.247 7.090 1.00 92.48 C ANISOU 490 CD1 LEU A 112 12515 10079 12544 953 -1186 1235 C ATOM 491 CD2 LEU A 112 -9.788 -29.638 5.604 1.00 86.33 C ANISOU 491 CD2 LEU A 112 11470 9359 11973 1164 -1114 1013 C ATOM 492 N LEU A 113 -9.640 -26.765 9.791 1.00 98.35 N ANISOU 492 N LEU A 113 13076 11198 13094 962 -1350 1314 N ATOM 493 CA LEU A 113 -8.732 -26.870 10.926 1.00101.64 C ANISOU 493 CA LEU A 113 13505 11585 13528 1010 -1534 1388 C ATOM 494 C LEU A 113 -9.521 -26.864 12.231 1.00103.57 C ANISOU 494 C LEU A 113 13913 11872 13566 909 -1596 1514 C ATOM 495 O LEU A 113 -9.358 -27.748 13.070 1.00105.27 O ANISOU 495 O LEU A 113 14234 11997 13766 920 -1738 1633 O ATOM 496 CB LEU A 113 -7.719 -25.722 10.919 1.00 96.64 C ANISOU 496 CB LEU A 113 12716 11044 12957 1057 -1555 1311 C ATOM 497 CG LEU A 113 -6.524 -25.865 9.974 1.00 92.53 C ANISOU 497 CG LEU A 113 12018 10476 12664 1178 -1548 1217 C ATOM 498 CD1 LEU A 113 -5.651 -24.620 10.031 1.00 92.02 C ANISOU 498 CD1 LEU A 113 11796 10511 12654 1193 -1560 1157 C ATOM 499 CD2 LEU A 113 -5.707 -27.101 10.315 1.00 90.82 C ANISOU 499 CD2 LEU A 113 11810 10107 12591 1286 -1711 1264 C ATOM 500 N THR A 114 -10.390 -25.870 12.390 1.00101.57 N ANISOU 500 N THR A 114 13681 11757 13152 814 -1486 1490 N ATOM 501 CA THR A 114 -11.185 -25.739 13.608 1.00 99.24 C ANISOU 501 CA THR A 114 13529 11536 12641 719 -1514 1590 C ATOM 502 C THR A 114 -11.945 -27.023 13.931 1.00100.46 C ANISOU 502 C THR A 114 13832 11594 12746 662 -1529 1724 C ATOM 503 O THR A 114 -12.336 -27.246 15.077 1.00105.68 O ANISOU 503 O THR A 114 14623 12287 13243 599 -1591 1846 O ATOM 504 CB THR A 114 -12.203 -24.578 13.512 1.00 94.53 C ANISOU 504 CB THR A 114 12923 11092 11903 630 -1359 1522 C ATOM 505 OG1 THR A 114 -13.091 -24.798 12.407 1.00 83.07 O ANISOU 505 OG1 THR A 114 11450 9621 10493 590 -1204 1479 O ATOM 506 CG2 THR A 114 -11.490 -23.241 13.342 1.00 93.43 C ANISOU 506 CG2 THR A 114 12652 11038 11809 671 -1361 1407 C ATOM 507 N ILE A 115 -12.153 -27.866 12.924 1.00100.45 N ANISOU 507 N ILE A 115 13811 11473 12882 681 -1475 1702 N ATOM 508 CA ILE A 115 -12.900 -29.104 13.114 1.00104.87 C ANISOU 508 CA ILE A 115 14500 11917 13429 619 -1491 1823 C ATOM 509 C ILE A 115 -12.036 -30.181 13.769 1.00104.38 C ANISOU 509 C ILE A 115 14505 11700 13454 688 -1691 1941 C ATOM 510 O ILE A 115 -12.536 -31.003 14.536 1.00107.19 O ANISOU 510 O ILE A 115 15004 11990 13735 617 -1755 2101 O ATOM 511 CB ILE A 115 -13.467 -29.630 11.773 1.00109.91 C ANISOU 511 CB ILE A 115 15099 12472 14191 614 -1376 1741 C ATOM 512 CG1 ILE A 115 -14.948 -29.985 11.924 1.00116.83 C ANISOU 512 CG1 ILE A 115 16076 13361 14954 470 -1282 1821 C ATOM 513 CG2 ILE A 115 -12.677 -30.837 11.283 1.00111.71 C ANISOU 513 CG2 ILE A 115 15318 12499 14627 720 -1485 1738 C ATOM 514 CD1 ILE A 115 -15.649 -30.257 10.607 1.00117.30 C ANISOU 514 CD1 ILE A 115 16090 13373 15106 451 -1164 1720 C ATOM 515 N MET A 116 -10.739 -30.167 13.472 1.00 99.28 N ANISOU 515 N MET A 116 13752 10997 12974 824 -1791 1868 N ATOM 516 CA MET A 116 -9.830 -31.197 13.969 1.00 96.45 C ANISOU 516 CA MET A 116 13433 10473 12739 913 -1995 1962 C ATOM 517 C MET A 116 -9.071 -30.774 15.226 1.00104.00 C ANISOU 517 C MET A 116 14420 11492 13602 938 -2164 2043 C ATOM 518 O MET A 116 -8.189 -31.495 15.692 1.00111.14 O ANISOU 518 O MET A 116 15342 12272 14614 1025 -2357 2118 O ATOM 519 CB MET A 116 -8.829 -31.587 12.880 1.00 89.50 C ANISOU 519 CB MET A 116 12406 9477 12122 1062 -2014 1829 C ATOM 520 CG MET A 116 -9.402 -32.503 11.815 1.00 81.26 C ANISOU 520 CG MET A 116 11377 8302 11196 1064 -1927 1777 C ATOM 521 SD MET A 116 -8.173 -33.017 10.600 1.00174.51 S ANISOU 521 SD MET A 116 23019 19987 23299 1255 -1948 1606 S ATOM 522 CE MET A 116 -7.740 -31.442 9.861 1.00107.39 C ANISOU 522 CE MET A 116 14328 11707 14767 1277 -1784 1441 C ATOM 523 N PHE A 117 -9.411 -29.614 15.777 1.00111.20 N ANISOU 523 N PHE A 117 15338 12593 14321 868 -2104 2021 N ATOM 524 CA PHE A 117 -8.745 -29.130 16.981 1.00124.01 C ANISOU 524 CA PHE A 117 16996 14290 15831 887 -2267 2078 C ATOM 525 C PHE A 117 -9.743 -28.525 17.964 1.00133.47 C ANISOU 525 C PHE A 117 18329 15654 16731 757 -2206 2147 C ATOM 526 O PHE A 117 -9.419 -27.590 18.697 1.00133.75 O ANISOU 526 O PHE A 117 18359 15818 16640 758 -2263 2111 O ATOM 527 CB PHE A 117 -7.668 -28.104 16.620 1.00130.16 C ANISOU 527 CB PHE A 117 17591 15134 16729 978 -2294 1925 C ATOM 528 CG PHE A 117 -6.537 -28.674 15.810 1.00139.41 C ANISOU 528 CG PHE A 117 18617 16165 18189 1117 -2366 1860 C ATOM 529 CD1 PHE A 117 -5.444 -29.252 16.433 1.00147.03 C ANISOU 529 CD1 PHE A 117 19573 17027 19264 1217 -2597 1927 C ATOM 530 CD2 PHE A 117 -6.568 -28.633 14.426 1.00142.35 C ANISOU 530 CD2 PHE A 117 18859 16512 18716 1153 -2202 1729 C ATOM 531 CE1 PHE A 117 -4.403 -29.778 15.690 1.00150.24 C ANISOU 531 CE1 PHE A 117 19829 17307 19949 1355 -2656 1855 C ATOM 532 CE2 PHE A 117 -5.530 -29.157 13.678 1.00145.84 C ANISOU 532 CE2 PHE A 117 19160 16840 19412 1287 -2250 1656 C ATOM 533 CZ PHE A 117 -4.447 -29.730 14.311 1.00147.66 C ANISOU 533 CZ PHE A 117 19369 16968 19768 1391 -2473 1714 C ATOM 534 N GLU A 118 -10.956 -29.069 17.976 1.00142.31 N ANISOU 534 N GLU A 118 19561 16767 17743 647 -2089 2236 N ATOM 535 CA GLU A 118 -11.990 -28.627 18.906 1.00150.64 C ANISOU 535 CA GLU A 118 20740 17982 18514 522 -2008 2309 C ATOM 536 C GLU A 118 -12.278 -27.135 18.758 1.00158.76 C ANISOU 536 C GLU A 118 21678 19197 19448 503 -1878 2144 C ATOM 537 O GLU A 118 -11.974 -26.530 17.729 1.00156.40 O ANISOU 537 O GLU A 118 21226 18893 19307 557 -1805 1990 O ATOM 538 CB GLU A 118 -11.571 -28.935 20.344 1.00153.65 C ANISOU 538 CB GLU A 118 21269 18386 18725 517 -2199 2468 C ATOM 539 N ALA A 119 -12.865 -26.548 19.796 1.00169.99 N ANISOU 539 N ALA A 119 23197 20781 20611 428 -1851 2177 N ATOM 540 CA ALA A 119 -13.205 -25.130 19.788 1.00180.89 C ANISOU 540 CA ALA A 119 24507 22330 21895 411 -1740 2020 C ATOM 541 C ALA A 119 -11.951 -24.257 19.826 1.00176.93 C ANISOU 541 C ALA A 119 23898 21841 21487 514 -1876 1899 C ATOM 542 O ALA A 119 -12.006 -23.066 19.519 1.00188.54 O ANISOU 542 O ALA A 119 25270 23402 22965 520 -1801 1748 O ATOM 543 CB ALA A 119 -14.114 -24.803 20.968 1.00193.72 C ANISOU 543 CB ALA A 119 26267 24124 23212 316 -1683 2079 C ATOM 544 N MET A 120 -10.824 -24.855 20.203 1.00168.35 N ANISOU 544 N MET A 120 22825 20655 20487 592 -2084 1969 N ATOM 545 CA MET A 120 -9.566 -24.123 20.310 1.00156.00 C ANISOU 545 CA MET A 120 21150 19093 19029 686 -2236 1869 C ATOM 546 C MET A 120 -9.177 -23.472 18.985 1.00145.08 C ANISOU 546 C MET A 120 19563 17677 17886 735 -2135 1711 C ATOM 547 O MET A 120 -9.558 -23.942 17.911 1.00145.18 O ANISOU 547 O MET A 120 19521 17616 18026 731 -2001 1700 O ATOM 548 CB MET A 120 -8.446 -25.057 20.771 1.00154.37 C ANISOU 548 CB MET A 120 20972 18758 18922 770 -2475 1979 C ATOM 549 N TRP A 121 -8.411 -22.389 19.074 1.00133.01 N ANISOU 549 N TRP A 121 17923 16202 16412 776 -2205 1593 N ATOM 550 CA TRP A 121 -7.962 -21.656 17.898 1.00119.83 C ANISOU 550 CA TRP A 121 16057 14514 14960 813 -2116 1458 C ATOM 551 C TRP A 121 -6.441 -21.709 17.809 1.00120.41 C ANISOU 551 C TRP A 121 15993 14506 15251 915 -2291 1434 C ATOM 552 O TRP A 121 -5.751 -20.941 18.479 1.00126.55 O ANISOU 552 O TRP A 121 16732 15331 16020 934 -2432 1383 O ATOM 553 CB TRP A 121 -8.438 -20.206 17.978 1.00107.22 C ANISOU 553 CB TRP A 121 14424 13043 13271 761 -2029 1334 C ATOM 554 CG TRP A 121 -8.072 -19.370 16.791 1.00 94.29 C ANISOU 554 CG TRP A 121 12596 11391 11838 780 -1931 1217 C ATOM 555 CD1 TRP A 121 -7.124 -18.391 16.741 1.00 89.96 C ANISOU 555 CD1 TRP A 121 11910 10851 11421 812 -2015 1125 C ATOM 556 CD2 TRP A 121 -8.654 -19.432 15.482 1.00 89.77 C ANISOU 556 CD2 TRP A 121 11956 10796 11359 760 -1734 1188 C ATOM 557 NE1 TRP A 121 -7.078 -17.840 15.483 1.00 86.88 N ANISOU 557 NE1 TRP A 121 11369 10445 11194 809 -1872 1054 N ATOM 558 CE2 TRP A 121 -8.007 -18.463 14.692 1.00 88.91 C ANISOU 558 CE2 TRP A 121 11673 10689 11421 781 -1701 1089 C ATOM 559 CE3 TRP A 121 -9.658 -20.215 14.902 1.00 85.56 C ANISOU 559 CE3 TRP A 121 11491 10238 10778 722 -1590 1238 C ATOM 560 CZ2 TRP A 121 -8.329 -18.254 13.353 1.00 90.12 C ANISOU 560 CZ2 TRP A 121 11732 10832 11678 769 -1527 1047 C ATOM 561 CZ3 TRP A 121 -9.977 -20.005 13.572 1.00 85.93 C ANISOU 561 CZ3 TRP A 121 11441 10272 10936 716 -1430 1180 C ATOM 562 CH2 TRP A 121 -9.314 -19.033 12.813 1.00 85.88 C ANISOU 562 CH2 TRP A 121 11274 10279 11078 741 -1398 1088 C ATOM 563 N PRO A 122 -5.911 -22.621 16.978 1.00113.62 N ANISOU 563 N PRO A 122 15052 13524 14596 984 -2285 1460 N ATOM 564 CA PRO A 122 -4.462 -22.840 16.904 1.00111.85 C ANISOU 564 CA PRO A 122 14685 13216 14596 1092 -2451 1444 C ATOM 565 C PRO A 122 -3.707 -21.664 16.291 1.00116.65 C ANISOU 565 C PRO A 122 15082 13869 15369 1111 -2417 1311 C ATOM 566 O PRO A 122 -2.569 -21.396 16.680 1.00123.27 O ANISOU 566 O PRO A 122 15813 14690 16333 1170 -2588 1288 O ATOM 567 CB PRO A 122 -4.342 -24.081 16.015 1.00107.79 C ANISOU 567 CB PRO A 122 14140 12568 14246 1156 -2398 1482 C ATOM 568 CG PRO A 122 -5.562 -24.056 15.169 1.00109.53 C ANISOU 568 CG PRO A 122 14405 12820 14389 1080 -2162 1456 C ATOM 569 CD PRO A 122 -6.647 -23.469 16.023 1.00109.87 C ANISOU 569 CD PRO A 122 14602 12981 14164 970 -2122 1489 C ATOM 570 N LEU A 123 -4.335 -20.972 15.346 1.00109.79 N ANISOU 570 N LEU A 123 14154 13056 14507 1057 -2205 1234 N ATOM 571 CA LEU A 123 -3.716 -19.823 14.696 1.00102.45 C ANISOU 571 CA LEU A 123 13031 12167 13729 1057 -2154 1127 C ATOM 572 C LEU A 123 -3.662 -18.617 15.631 1.00 96.68 C ANISOU 572 C LEU A 123 12316 11516 12900 1007 -2259 1077 C ATOM 573 O LEU A 123 -4.285 -18.621 16.692 1.00 98.60 O ANISOU 573 O LEU A 123 12732 11808 12922 968 -2331 1111 O ATOM 574 CB LEU A 123 -4.490 -19.455 13.430 1.00102.28 C ANISOU 574 CB LEU A 123 12964 12178 13721 1010 -1907 1077 C ATOM 575 CG LEU A 123 -4.181 -20.284 12.183 1.00105.55 C ANISOU 575 CG LEU A 123 13282 12524 14299 1072 -1794 1072 C ATOM 576 CD1 LEU A 123 -4.449 -21.762 12.426 1.00109.95 C ANISOU 576 CD1 LEU A 123 13969 12989 14818 1116 -1844 1153 C ATOM 577 CD2 LEU A 123 -4.996 -19.771 11.006 1.00105.71 C ANISOU 577 CD2 LEU A 123 13274 12596 14295 1016 -1567 1022 C ATOM 578 N PRO A 124 -2.900 -17.583 15.243 1.00 94.55 N ANISOU 578 N PRO A 124 11866 11261 12798 1006 -2269 993 N ATOM 579 CA PRO A 124 -2.876 -16.314 15.977 1.00 99.45 C ANISOU 579 CA PRO A 124 12488 11944 13356 954 -2359 920 C ATOM 580 C PRO A 124 -4.277 -15.733 16.140 1.00105.09 C ANISOU 580 C PRO A 124 13346 12736 13846 873 -2227 891 C ATOM 581 O PRO A 124 -5.101 -15.860 15.235 1.00109.95 O ANISOU 581 O PRO A 124 13973 13360 14444 843 -2027 899 O ATOM 582 CB PRO A 124 -2.024 -15.412 15.083 1.00 97.85 C ANISOU 582 CB PRO A 124 12049 11725 13407 951 -2315 852 C ATOM 583 CG PRO A 124 -1.124 -16.346 14.361 1.00 97.00 C ANISOU 583 CG PRO A 124 11804 11550 13501 1032 -2305 892 C ATOM 584 CD PRO A 124 -1.916 -17.604 14.146 1.00 97.21 C ANISOU 584 CD PRO A 124 11980 11551 13404 1058 -2212 964 C ATOM 585 N LEU A 125 -4.538 -15.102 17.281 1.00105.60 N ANISOU 585 N LEU A 125 13517 12861 13745 843 -2343 848 N ATOM 586 CA LEU A 125 -5.862 -14.565 17.577 1.00 98.84 C ANISOU 586 CA LEU A 125 12796 12089 12671 778 -2227 807 C ATOM 587 C LEU A 125 -6.335 -13.595 16.502 1.00 93.05 C ANISOU 587 C LEU A 125 11955 11359 12041 733 -2050 735 C ATOM 588 O LEU A 125 -7.519 -13.557 16.172 1.00 95.30 O ANISOU 588 O LEU A 125 12316 11685 12209 691 -1885 734 O ATOM 589 CB LEU A 125 -5.856 -13.855 18.932 1.00 97.33 C ANISOU 589 CB LEU A 125 12702 11964 12313 766 -2391 737 C ATOM 590 CG LEU A 125 -5.438 -14.712 20.127 1.00 98.35 C ANISOU 590 CG LEU A 125 12964 12108 12298 805 -2587 815 C ATOM 591 N VAL A 126 -5.407 -12.817 15.957 1.00 94.37 N ANISOU 591 N VAL A 126 11942 11481 12433 738 -2089 684 N ATOM 592 CA VAL A 126 -5.755 -11.748 15.027 1.00 95.47 C ANISOU 592 CA VAL A 126 11981 11617 12676 688 -1951 625 C ATOM 593 C VAL A 126 -6.424 -12.293 13.767 1.00 88.75 C ANISOU 593 C VAL A 126 11118 10762 11843 678 -1733 682 C ATOM 594 O VAL A 126 -7.215 -11.602 13.126 1.00 88.96 O ANISOU 594 O VAL A 126 11136 10807 11859 632 -1598 651 O ATOM 595 CB VAL A 126 -4.513 -10.926 14.625 1.00 99.74 C ANISOU 595 CB VAL A 126 12316 12102 13478 687 -2034 588 C ATOM 596 CG1 VAL A 126 -4.914 -9.754 13.739 1.00 97.06 C ANISOU 596 CG1 VAL A 126 11891 11753 13235 625 -1905 544 C ATOM 597 CG2 VAL A 126 -3.779 -10.427 15.863 1.00106.68 C ANISOU 597 CG2 VAL A 126 13200 12976 14357 698 -2277 523 C ATOM 598 N LEU A 127 -6.107 -13.534 13.417 1.00 81.98 N ANISOU 598 N LEU A 127 10261 9874 11014 725 -1711 760 N ATOM 599 CA LEU A 127 -6.652 -14.144 12.210 1.00 83.60 C ANISOU 599 CA LEU A 127 10456 10069 11239 724 -1522 802 C ATOM 600 C LEU A 127 -8.089 -14.619 12.405 1.00 82.43 C ANISOU 600 C LEU A 127 10480 9961 10880 688 -1424 826 C ATOM 601 O LEU A 127 -8.752 -15.019 11.447 1.00 87.75 O ANISOU 601 O LEU A 127 11161 10632 11548 675 -1272 847 O ATOM 602 CB LEU A 127 -5.784 -15.324 11.780 1.00 91.95 C ANISOU 602 CB LEU A 127 11450 11069 12418 796 -1542 857 C ATOM 603 CG LEU A 127 -4.295 -15.015 11.623 1.00102.00 C ANISOU 603 CG LEU A 127 12531 12307 13917 840 -1639 838 C ATOM 604 CD1 LEU A 127 -3.563 -16.220 11.053 1.00106.95 C ANISOU 604 CD1 LEU A 127 13087 12879 14669 924 -1627 878 C ATOM 605 CD2 LEU A 127 -4.085 -13.785 10.750 1.00100.49 C ANISOU 605 CD2 LEU A 127 12190 12135 13856 789 -1542 795 C ATOM 606 N CYS A 128 -8.564 -14.585 13.645 1.00 85.54 N ANISOU 606 N CYS A 128 11008 10399 11096 671 -1512 821 N ATOM 607 CA CYS A 128 -9.913 -15.050 13.954 1.00 82.64 C ANISOU 607 CA CYS A 128 10794 10081 10526 631 -1417 851 C ATOM 608 C CYS A 128 -10.989 -14.111 13.416 1.00 75.84 C ANISOU 608 C CYS A 128 9921 9267 9628 577 -1273 786 C ATOM 609 O CYS A 128 -11.865 -14.538 12.665 1.00 72.38 O ANISOU 609 O CYS A 128 9506 8831 9164 552 -1132 814 O ATOM 610 CB CYS A 128 -10.087 -15.234 15.460 1.00 73.29 C ANISOU 610 CB CYS A 128 9753 8949 9144 626 -1541 867 C ATOM 611 SG CYS A 128 -11.751 -15.739 15.928 1.00 78.27 S ANISOU 611 SG CYS A 128 10557 9660 9522 562 -1409 911 S ATOM 612 N PRO A 129 -10.937 -12.830 13.805 1.00 77.14 N ANISOU 612 N PRO A 129 10048 9460 9801 562 -1320 695 N ATOM 613 CA PRO A 129 -11.941 -11.915 13.256 1.00 80.34 C ANISOU 613 CA PRO A 129 10435 9895 10198 521 -1195 633 C ATOM 614 C PRO A 129 -11.771 -11.737 11.751 1.00 70.18 C ANISOU 614 C PRO A 129 9025 8557 9081 515 -1089 655 C ATOM 615 O PRO A 129 -12.742 -11.456 11.048 1.00 60.06 O ANISOU 615 O PRO A 129 7747 7293 7781 484 -964 645 O ATOM 616 CB PRO A 129 -11.660 -10.601 13.994 1.00 80.53 C ANISOU 616 CB PRO A 129 10432 9931 10235 519 -1303 525 C ATOM 617 CG PRO A 129 -10.248 -10.715 14.464 1.00 79.28 C ANISOU 617 CG PRO A 129 10220 9731 10171 554 -1474 535 C ATOM 618 CD PRO A 129 -10.045 -12.162 14.767 1.00 78.11 C ANISOU 618 CD PRO A 129 10152 9584 9943 583 -1499 636 C ATOM 619 N ALA A 130 -10.545 -11.908 11.268 1.00 63.43 N ANISOU 619 N ALA A 130 8063 7650 8388 545 -1139 685 N ATOM 620 CA ALA A 130 -10.263 -11.785 9.844 1.00 70.13 C ANISOU 620 CA ALA A 130 8795 8468 9382 541 -1031 711 C ATOM 621 C ALA A 130 -10.910 -12.929 9.069 1.00 76.68 C ANISOU 621 C ALA A 130 9681 9301 10153 549 -907 765 C ATOM 622 O ALA A 130 -11.540 -12.712 8.034 1.00 73.42 O ANISOU 622 O ALA A 130 9248 8898 9750 524 -784 768 O ATOM 623 CB ALA A 130 -8.765 -11.767 9.606 1.00 63.67 C ANISOU 623 CB ALA A 130 7838 7607 8747 575 -1105 727 C ATOM 624 N TRP A 131 -10.749 -14.147 9.576 1.00 72.35 N ANISOU 624 N TRP A 131 9207 8736 9546 583 -954 809 N ATOM 625 CA TRP A 131 -11.344 -15.321 8.952 1.00 73.34 C ANISOU 625 CA TRP A 131 9395 8845 9626 590 -861 854 C ATOM 626 C TRP A 131 -12.867 -15.221 8.971 1.00 74.11 C ANISOU 626 C TRP A 131 9589 8987 9581 532 -768 847 C ATOM 627 O TRP A 131 -13.535 -15.580 8.000 1.00 74.70 O ANISOU 627 O TRP A 131 9670 9058 9654 516 -659 856 O ATOM 628 CB TRP A 131 -10.876 -16.590 9.669 1.00 74.32 C ANISOU 628 CB TRP A 131 9589 8923 9725 634 -958 910 C ATOM 629 CG TRP A 131 -11.642 -17.822 9.294 1.00 76.97 C ANISOU 629 CG TRP A 131 10017 9227 10001 629 -887 957 C ATOM 630 CD1 TRP A 131 -11.680 -18.424 8.070 1.00 80.29 C ANISOU 630 CD1 TRP A 131 10401 9611 10496 651 -792 952 C ATOM 631 CD2 TRP A 131 -12.471 -18.610 10.155 1.00 74.76 C ANISOU 631 CD2 TRP A 131 9882 8946 9576 595 -910 1016 C ATOM 632 NE1 TRP A 131 -12.488 -19.535 8.114 1.00 75.18 N ANISOU 632 NE1 TRP A 131 9865 8925 9775 632 -767 996 N ATOM 633 CE2 TRP A 131 -12.985 -19.672 9.384 1.00 70.89 C ANISOU 633 CE2 TRP A 131 9430 8401 9102 592 -835 1045 C ATOM 634 CE3 TRP A 131 -12.832 -18.520 11.502 1.00 75.21 C ANISOU 634 CE3 TRP A 131 10042 9048 9484 562 -984 1046 C ATOM 635 CZ2 TRP A 131 -13.838 -20.634 9.914 1.00 71.88 C ANISOU 635 CZ2 TRP A 131 9684 8503 9124 549 -835 1116 C ATOM 636 CZ3 TRP A 131 -13.680 -19.477 12.027 1.00 76.47 C ANISOU 636 CZ3 TRP A 131 10332 9202 9520 520 -969 1124 C ATOM 637 CH2 TRP A 131 -14.174 -20.520 11.235 1.00 79.04 C ANISOU 637 CH2 TRP A 131 10684 9460 9888 509 -897 1164 C ATOM 638 N LEU A 132 -13.410 -14.729 10.080 1.00 66.93 N ANISOU 638 N LEU A 132 8751 8126 8554 502 -815 824 N ATOM 639 CA LEU A 132 -14.850 -14.540 10.205 1.00 71.55 C ANISOU 639 CA LEU A 132 9408 8766 9014 450 -725 807 C ATOM 640 C LEU A 132 -15.342 -13.458 9.248 1.00 73.07 C ANISOU 640 C LEU A 132 9520 8971 9274 429 -641 753 C ATOM 641 O LEU A 132 -16.460 -13.527 8.738 1.00 57.34 O ANISOU 641 O LEU A 132 7550 7000 7236 396 -543 751 O ATOM 642 CB LEU A 132 -15.214 -14.168 11.642 1.00 73.94 C ANISOU 642 CB LEU A 132 9792 9132 9169 434 -788 778 C ATOM 643 CG LEU A 132 -15.151 -15.303 12.666 1.00 65.56 C ANISOU 643 CG LEU A 132 8848 8078 7982 434 -851 854 C ATOM 644 CD1 LEU A 132 -15.244 -14.750 14.075 1.00 61.84 C ANISOU 644 CD1 LEU A 132 8450 7685 7361 428 -929 813 C ATOM 645 CD2 LEU A 132 -16.260 -16.305 12.411 1.00 66.04 C ANISOU 645 CD2 LEU A 132 8983 8144 7966 388 -744 921 C ATOM 646 N PHE A 133 -14.502 -12.454 9.018 1.00 73.37 N ANISOU 646 N PHE A 133 9460 8987 9430 444 -689 717 N ATOM 647 CA PHE A 133 -14.835 -11.366 8.107 1.00 67.88 C ANISOU 647 CA PHE A 133 8688 8288 8816 422 -627 685 C ATOM 648 C PHE A 133 -14.894 -11.871 6.669 1.00 69.73 C ANISOU 648 C PHE A 133 8884 8505 9104 421 -526 734 C ATOM 649 O PHE A 133 -15.891 -11.674 5.972 1.00 56.14 O ANISOU 649 O PHE A 133 7175 6801 7354 394 -445 731 O ATOM 650 CB PHE A 133 -13.802 -10.243 8.227 1.00 65.01 C ANISOU 650 CB PHE A 133 8227 7892 8583 429 -714 652 C ATOM 651 CG PHE A 133 -14.010 -9.122 7.250 1.00 60.98 C ANISOU 651 CG PHE A 133 7635 7359 8176 401 -663 644 C ATOM 652 CD1 PHE A 133 -14.990 -8.171 7.469 1.00 65.15 C ANISOU 652 CD1 PHE A 133 8183 7895 8676 380 -657 585 C ATOM 653 CD2 PHE A 133 -13.225 -9.018 6.113 1.00 61.39 C ANISOU 653 CD2 PHE A 133 7589 7384 8354 397 -620 700 C ATOM 654 CE1 PHE A 133 -15.185 -7.136 6.572 1.00 67.85 C ANISOU 654 CE1 PHE A 133 8456 8201 9123 355 -627 591 C ATOM 655 CE2 PHE A 133 -13.416 -7.985 5.214 1.00 57.33 C ANISOU 655 CE2 PHE A 133 7010 6849 7925 363 -578 715 C ATOM 656 CZ PHE A 133 -14.396 -7.044 5.444 1.00 58.10 C ANISOU 656 CZ PHE A 133 7136 6938 8002 342 -590 666 C ATOM 657 N LEU A 134 -13.817 -12.517 6.231 1.00 69.59 N ANISOU 657 N LEU A 134 8819 8458 9165 456 -537 771 N ATOM 658 CA LEU A 134 -13.745 -13.063 4.883 1.00 56.75 C ANISOU 658 CA LEU A 134 7159 6824 7577 467 -440 802 C ATOM 659 C LEU A 134 -14.871 -14.056 4.643 1.00 56.28 C ANISOU 659 C LEU A 134 7199 6772 7411 454 -378 811 C ATOM 660 O LEU A 134 -15.483 -14.064 3.577 1.00 55.78 O ANISOU 660 O LEU A 134 7135 6723 7337 438 -295 812 O ATOM 661 CB LEU A 134 -12.397 -13.745 4.653 1.00 57.45 C ANISOU 661 CB LEU A 134 7181 6885 7763 521 -464 823 C ATOM 662 CG LEU A 134 -11.171 -12.831 4.701 1.00 59.16 C ANISOU 662 CG LEU A 134 7269 7093 8118 528 -517 821 C ATOM 663 CD1 LEU A 134 -9.893 -13.638 4.553 1.00 65.02 C ANISOU 663 CD1 LEU A 134 7933 7810 8960 591 -540 835 C ATOM 664 CD2 LEU A 134 -11.262 -11.764 3.625 1.00 60.12 C ANISOU 664 CD2 LEU A 134 7311 7234 8298 487 -434 834 C ATOM 665 N ASP A 135 -15.134 -14.901 5.633 1.00 60.26 N ANISOU 665 N ASP A 135 7791 7267 7838 457 -426 823 N ATOM 666 CA ASP A 135 -16.210 -15.874 5.523 1.00 61.43 C ANISOU 666 CA ASP A 135 8030 7411 7899 431 -377 841 C ATOM 667 C ASP A 135 -17.537 -15.191 5.213 1.00 55.71 C ANISOU 667 C ASP A 135 7315 6732 7120 378 -310 815 C ATOM 668 O ASP A 135 -18.185 -15.504 4.217 1.00 56.36 O ANISOU 668 O ASP A 135 7401 6812 7199 363 -243 814 O ATOM 669 CB ASP A 135 -16.333 -16.686 6.810 1.00 67.98 C ANISOU 669 CB ASP A 135 8954 8230 8647 424 -443 877 C ATOM 670 CG ASP A 135 -17.524 -17.626 6.791 1.00 74.68 C ANISOU 670 CG ASP A 135 9889 9071 9415 378 -391 908 C ATOM 671 OD1 ASP A 135 -18.596 -17.213 6.309 1.00 73.34 O ANISOU 671 OD1 ASP A 135 9712 8940 9216 334 -317 882 O ATOM 672 OD2 ASP A 135 -17.392 -18.781 7.244 1.00 83.50 O ANISOU 672 OD2 ASP A 135 11076 10138 10512 382 -431 962 O ATOM 673 N VAL A 136 -17.947 -14.273 6.082 1.00 57.82 N ANISOU 673 N VAL A 136 7585 7040 7346 357 -335 784 N ATOM 674 CA VAL A 136 -19.209 -13.567 5.907 1.00 58.07 C ANISOU 674 CA VAL A 136 7612 7113 7341 318 -280 749 C ATOM 675 C VAL A 136 -19.192 -12.734 4.629 1.00 58.23 C ANISOU 675 C VAL A 136 7556 7122 7446 321 -245 739 C ATOM 676 O VAL A 136 -20.210 -12.603 3.947 1.00 54.45 O ANISOU 676 O VAL A 136 7076 6658 6953 296 -193 731 O ATOM 677 CB VAL A 136 -19.505 -12.643 7.105 1.00 55.74 C ANISOU 677 CB VAL A 136 7323 6861 6996 312 -318 696 C ATOM 678 CG1 VAL A 136 -20.766 -11.836 6.850 1.00 55.45 C ANISOU 678 CG1 VAL A 136 7259 6859 6950 288 -263 646 C ATOM 679 CG2 VAL A 136 -19.643 -13.456 8.384 1.00 56.47 C ANISOU 679 CG2 VAL A 136 7504 6984 6967 301 -343 717 C ATOM 680 N LEU A 137 -18.030 -12.173 4.311 1.00 57.50 N ANISOU 680 N LEU A 137 7398 7005 7444 347 -277 747 N ATOM 681 CA LEU A 137 -17.874 -11.334 3.129 1.00 57.97 C ANISOU 681 CA LEU A 137 7387 7057 7581 342 -244 760 C ATOM 682 C LEU A 137 -18.117 -12.122 1.848 1.00 61.40 C ANISOU 682 C LEU A 137 7837 7498 7994 343 -172 790 C ATOM 683 O LEU A 137 -19.041 -11.823 1.091 1.00 62.99 O ANISOU 683 O LEU A 137 8045 7716 8174 320 -135 790 O ATOM 684 CB LEU A 137 -16.470 -10.727 3.100 1.00 60.89 C ANISOU 684 CB LEU A 137 7675 7402 8059 360 -287 776 C ATOM 685 CG LEU A 137 -16.124 -9.872 1.879 1.00 59.22 C ANISOU 685 CG LEU A 137 7385 7184 7931 344 -247 816 C ATOM 686 CD1 LEU A 137 -17.085 -8.703 1.750 1.00 67.15 C ANISOU 686 CD1 LEU A 137 8385 8180 8948 313 -258 802 C ATOM 687 CD2 LEU A 137 -14.690 -9.379 1.969 1.00 58.74 C ANISOU 687 CD2 LEU A 137 7229 7100 7990 351 -286 838 C ATOM 688 N PHE A 138 -17.282 -13.129 1.612 1.00 62.12 N ANISOU 688 N PHE A 138 7934 7575 8094 376 -161 806 N ATOM 689 CA PHE A 138 -17.350 -13.914 0.386 1.00 59.85 C ANISOU 689 CA PHE A 138 7662 7294 7786 390 -96 814 C ATOM 690 C PHE A 138 -18.664 -14.683 0.267 1.00 57.88 C ANISOU 690 C PHE A 138 7494 7043 7456 362 -78 796 C ATOM 691 O PHE A 138 -19.242 -14.772 -0.818 1.00 59.57 O ANISOU 691 O PHE A 138 7719 7274 7640 352 -37 791 O ATOM 692 CB PHE A 138 -16.174 -14.888 0.317 1.00 55.34 C ANISOU 692 CB PHE A 138 7076 6697 7255 445 -97 815 C ATOM 693 CG PHE A 138 -14.832 -14.215 0.248 1.00 76.05 C ANISOU 693 CG PHE A 138 9594 9326 9975 469 -103 832 C ATOM 694 CD1 PHE A 138 -14.654 -13.057 -0.492 1.00 68.67 C ANISOU 694 CD1 PHE A 138 8589 8424 9080 442 -65 859 C ATOM 695 CD2 PHE A 138 -13.748 -14.739 0.932 1.00 80.60 C ANISOU 695 CD2 PHE A 138 10138 9871 10615 516 -156 831 C ATOM 696 CE1 PHE A 138 -13.418 -12.439 -0.552 1.00 67.75 C ANISOU 696 CE1 PHE A 138 8364 8310 9069 451 -68 885 C ATOM 697 CE2 PHE A 138 -12.512 -14.126 0.877 1.00 80.06 C ANISOU 697 CE2 PHE A 138 9954 9809 10656 533 -166 845 C ATOM 698 CZ PHE A 138 -12.347 -12.974 0.133 1.00 73.12 C ANISOU 698 CZ PHE A 138 8998 8963 9819 496 -117 873 C ATOM 699 N SER A 139 -19.129 -15.245 1.377 1.00 57.77 N ANISOU 699 N SER A 139 7533 7011 7404 347 -113 793 N ATOM 700 CA SER A 139 -20.369 -16.014 1.376 1.00 60.11 C ANISOU 700 CA SER A 139 7894 7303 7641 307 -96 786 C ATOM 701 C SER A 139 -21.550 -15.143 0.967 1.00 64.14 C ANISOU 701 C SER A 139 8382 7854 8134 268 -72 769 C ATOM 702 O SER A 139 -22.406 -15.565 0.189 1.00 61.92 O ANISOU 702 O SER A 139 8121 7574 7832 244 -50 758 O ATOM 703 CB SER A 139 -20.627 -16.617 2.758 1.00 58.89 C ANISOU 703 CB SER A 139 7796 7137 7444 285 -129 806 C ATOM 704 OG SER A 139 -19.629 -17.563 3.097 1.00 55.28 O ANISOU 704 OG SER A 139 7368 6626 7008 324 -169 831 O ATOM 705 N THR A 140 -21.593 -13.929 1.504 1.00 65.35 N ANISOU 705 N THR A 140 8491 8033 8308 264 -89 758 N ATOM 706 CA THR A 140 -22.671 -12.996 1.206 1.00 63.17 C ANISOU 706 CA THR A 140 8181 7783 8036 239 -80 737 C ATOM 707 C THR A 140 -22.569 -12.492 -0.231 1.00 66.64 C ANISOU 707 C THR A 140 8590 8222 8506 247 -68 756 C ATOM 708 O THR A 140 -23.582 -12.275 -0.896 1.00 59.90 O ANISOU 708 O THR A 140 7733 7383 7644 227 -64 749 O ATOM 709 CB THR A 140 -22.646 -11.799 2.169 1.00 61.58 C ANISOU 709 CB THR A 140 7941 7594 7862 246 -112 706 C ATOM 710 OG1 THR A 140 -22.841 -12.261 3.512 1.00 57.80 O ANISOU 710 OG1 THR A 140 7502 7136 7323 236 -117 687 O ATOM 711 CG2 THR A 140 -23.740 -10.802 1.817 1.00 63.33 C ANISOU 711 CG2 THR A 140 8119 7829 8114 234 -111 677 C ATOM 712 N ALA A 141 -21.340 -12.309 -0.704 1.00 68.02 N ANISOU 712 N ALA A 141 8741 8388 8715 275 -64 785 N ATOM 713 CA ALA A 141 -21.105 -11.849 -2.068 1.00 61.16 C ANISOU 713 CA ALA A 141 7849 7535 7856 279 -39 819 C ATOM 714 C ALA A 141 -21.648 -12.839 -3.095 1.00 63.25 C ANISOU 714 C ALA A 141 8166 7816 8050 277 -9 808 C ATOM 715 O ALA A 141 -22.235 -12.437 -4.098 1.00 66.32 O ANISOU 715 O ALA A 141 8558 8228 8412 264 -8 823 O ATOM 716 CB ALA A 141 -19.622 -11.618 -2.294 1.00 54.95 C ANISOU 716 CB ALA A 141 7014 6746 7117 304 -22 853 C ATOM 717 N SER A 142 -21.451 -14.131 -2.850 1.00 65.89 N ANISOU 717 N SER A 142 8547 8131 8358 292 1 781 N ATOM 718 CA SER A 142 -21.884 -15.149 -3.801 1.00 65.22 C ANISOU 718 CA SER A 142 8517 8047 8218 294 18 753 C ATOM 719 C SER A 142 -23.404 -15.163 -3.939 1.00 65.97 C ANISOU 719 C SER A 142 8633 8146 8287 248 -10 734 C ATOM 720 O SER A 142 -23.938 -15.452 -5.011 1.00 66.30 O ANISOU 720 O SER A 142 8704 8203 8285 242 -15 716 O ATOM 721 CB SER A 142 -21.357 -16.535 -3.405 1.00 60.48 C ANISOU 721 CB SER A 142 7960 7398 7621 321 19 725 C ATOM 722 OG SER A 142 -22.035 -17.078 -2.283 1.00 66.14 O ANISOU 722 OG SER A 142 8708 8077 8344 286 -14 725 O ATOM 723 N ILE A 143 -24.095 -14.823 -2.857 1.00 70.59 N ANISOU 723 N ILE A 143 9198 8725 8900 217 -30 734 N ATOM 724 CA ILE A 143 -25.551 -14.805 -2.856 1.00 67.90 C ANISOU 724 CA ILE A 143 8851 8392 8555 172 -49 714 C ATOM 725 C ILE A 143 -26.052 -13.571 -3.595 1.00 60.60 C ANISOU 725 C ILE A 143 7881 7497 7647 174 -73 726 C ATOM 726 O ILE A 143 -26.919 -13.662 -4.464 1.00 56.31 O ANISOU 726 O ILE A 143 7345 6965 7086 157 -100 715 O ATOM 727 CB ILE A 143 -26.107 -14.799 -1.418 1.00 63.38 C ANISOU 727 CB ILE A 143 8261 7821 7998 142 -44 706 C ATOM 728 CG1 ILE A 143 -25.698 -16.077 -0.683 1.00 60.89 C ANISOU 728 CG1 ILE A 143 8002 7470 7662 132 -34 717 C ATOM 729 CG2 ILE A 143 -27.620 -14.673 -1.432 1.00 64.54 C ANISOU 729 CG2 ILE A 143 8374 7989 8159 98 -52 683 C ATOM 730 CD1 ILE A 143 -25.944 -16.030 0.810 1.00 64.68 C ANISOU 730 CD1 ILE A 143 8480 7967 8129 107 -22 727 C ATOM 731 N TRP A 144 -25.491 -12.416 -3.254 1.00 54.48 N ANISOU 731 N TRP A 144 7062 6724 6913 193 -76 750 N ATOM 732 CA TRP A 144 -25.903 -11.161 -3.871 1.00 53.98 C ANISOU 732 CA TRP A 144 6957 6668 6886 196 -111 774 C ATOM 733 C TRP A 144 -25.506 -11.095 -5.343 1.00 59.79 C ANISOU 733 C TRP A 144 7720 7423 7574 204 -111 821 C ATOM 734 O TRP A 144 -26.120 -10.365 -6.122 1.00 63.17 O ANISOU 734 O TRP A 144 8137 7859 8006 198 -153 850 O ATOM 735 CB TRP A 144 -25.329 -9.964 -3.106 1.00 61.06 C ANISOU 735 CB TRP A 144 7803 7543 7856 211 -125 785 C ATOM 736 CG TRP A 144 -26.230 -9.492 -2.007 1.00 64.05 C ANISOU 736 CG TRP A 144 8141 7917 8277 208 -144 729 C ATOM 737 CD1 TRP A 144 -26.189 -9.863 -0.693 1.00 53.80 C ANISOU 737 CD1 TRP A 144 6848 6630 6965 207 -121 685 C ATOM 738 CD2 TRP A 144 -27.319 -8.567 -2.128 1.00 64.04 C ANISOU 738 CD2 TRP A 144 8088 7908 8335 212 -186 707 C ATOM 739 NE1 TRP A 144 -27.182 -9.224 0.010 1.00 60.66 N ANISOU 739 NE1 TRP A 144 7670 7510 7868 209 -131 629 N ATOM 740 CE2 TRP A 144 -27.889 -8.423 -0.849 1.00 65.85 C ANISOU 740 CE2 TRP A 144 8284 8151 8584 216 -172 635 C ATOM 741 CE3 TRP A 144 -27.864 -7.848 -3.198 1.00 54.57 C ANISOU 741 CE3 TRP A 144 6867 6694 7173 216 -238 742 C ATOM 742 CZ2 TRP A 144 -28.978 -7.587 -0.607 1.00 66.88 C ANISOU 742 CZ2 TRP A 144 8348 8280 8783 232 -200 583 C ATOM 743 CZ3 TRP A 144 -28.945 -7.019 -2.955 1.00 62.98 C ANISOU 743 CZ3 TRP A 144 7869 7744 8317 231 -284 701 C ATOM 744 CH2 TRP A 144 -29.490 -6.895 -1.671 1.00 64.94 C ANISOU 744 CH2 TRP A 144 8073 8005 8597 242 -260 614 C ATOM 745 N HIS A 145 -24.483 -11.854 -5.725 1.00 54.44 N ANISOU 745 N HIS A 145 7080 6759 6848 222 -64 827 N ATOM 746 CA HIS A 145 -24.099 -11.943 -7.129 1.00 55.02 C ANISOU 746 CA HIS A 145 7187 6872 6847 233 -44 859 C ATOM 747 C HIS A 145 -25.217 -12.573 -7.955 1.00 66.07 C ANISOU 747 C HIS A 145 8637 8289 8178 219 -83 822 C ATOM 748 O HIS A 145 -25.538 -12.095 -9.042 1.00 62.75 O ANISOU 748 O HIS A 145 8235 7903 7704 215 -111 857 O ATOM 749 CB HIS A 145 -22.810 -12.747 -7.296 1.00 57.28 C ANISOU 749 CB HIS A 145 7491 7173 7101 266 23 849 C ATOM 750 CG HIS A 145 -21.582 -11.899 -7.405 1.00 59.81 C ANISOU 750 CG HIS A 145 7756 7509 7458 277 65 914 C ATOM 751 ND1 HIS A 145 -20.853 -11.495 -6.307 1.00 62.83 N ANISOU 751 ND1 HIS A 145 8083 7856 7935 281 62 924 N ATOM 752 CD2 HIS A 145 -20.958 -11.371 -8.484 1.00 63.24 C ANISOU 752 CD2 HIS A 145 8181 7996 7849 277 109 979 C ATOM 753 CE1 HIS A 145 -19.832 -10.759 -6.705 1.00 65.80 C ANISOU 753 CE1 HIS A 145 8405 8251 8343 280 98 989 C ATOM 754 NE2 HIS A 145 -19.872 -10.667 -8.023 1.00 67.68 N ANISOU 754 NE2 HIS A 145 8670 8546 8498 275 135 1030 N ATOM 755 N LEU A 146 -25.808 -13.643 -7.434 1.00 55.20 N ANISOU 755 N LEU A 146 7284 6884 6806 206 -93 757 N ATOM 756 CA LEU A 146 -26.893 -14.328 -8.128 1.00 70.24 C ANISOU 756 CA LEU A 146 9228 8792 8669 184 -142 712 C ATOM 757 C LEU A 146 -28.143 -13.460 -8.212 1.00 68.90 C ANISOU 757 C LEU A 146 9011 8627 8540 157 -212 727 C ATOM 758 O LEU A 146 -28.942 -13.600 -9.137 1.00 72.21 O ANISOU 758 O LEU A 146 9454 9065 8919 145 -272 712 O ATOM 759 CB LEU A 146 -27.229 -15.648 -7.430 1.00 71.34 C ANISOU 759 CB LEU A 146 9391 8883 8831 163 -140 652 C ATOM 760 CG LEU A 146 -26.154 -16.738 -7.455 1.00 71.42 C ANISOU 760 CG LEU A 146 9455 8868 8814 197 -96 621 C ATOM 761 CD1 LEU A 146 -26.742 -18.054 -6.983 1.00 73.51 C ANISOU 761 CD1 LEU A 146 9754 9066 9109 165 -121 571 C ATOM 762 CD2 LEU A 146 -25.552 -16.887 -8.841 1.00 70.39 C ANISOU 762 CD2 LEU A 146 9373 8783 8590 239 -79 601 C ATOM 763 N CYS A 147 -28.317 -12.571 -7.240 1.00 69.14 N ANISOU 763 N CYS A 147 8973 8641 8655 153 -211 747 N ATOM 764 CA CYS A 147 -29.445 -11.649 -7.252 1.00 68.58 C ANISOU 764 CA CYS A 147 8841 8567 8647 143 -275 753 C ATOM 765 C CYS A 147 -29.250 -10.608 -8.350 1.00 69.58 C ANISOU 765 C CYS A 147 8977 8710 8751 161 -322 824 C ATOM 766 O CYS A 147 -30.199 -10.231 -9.041 1.00 56.60 O ANISOU 766 O CYS A 147 7322 7072 7114 156 -402 833 O ATOM 767 CB CYS A 147 -29.587 -10.959 -5.894 1.00 67.09 C ANISOU 767 CB CYS A 147 8581 8359 8552 146 -255 738 C ATOM 768 SG CYS A 147 -30.995 -9.828 -5.779 1.00 64.04 S ANISOU 768 SG CYS A 147 8099 7962 8269 151 -329 720 S ATOM 769 N ALA A 148 -28.011 -10.151 -8.504 1.00 63.69 N ANISOU 769 N ALA A 148 8247 7969 7982 178 -275 881 N ATOM 770 CA ALA A 148 -27.668 -9.177 -9.532 1.00 58.81 C ANISOU 770 CA ALA A 148 7643 7367 7336 184 -304 974 C ATOM 771 C ALA A 148 -27.842 -9.779 -10.923 1.00 57.38 C ANISOU 771 C ALA A 148 7540 7244 7017 182 -323 984 C ATOM 772 O ALA A 148 -28.305 -9.110 -11.844 1.00 67.76 O ANISOU 772 O ALA A 148 8873 8576 8297 178 -394 1047 O ATOM 773 CB ALA A 148 -26.241 -8.695 -9.341 1.00 56.46 C ANISOU 773 CB ALA A 148 7333 7067 7053 191 -235 1034 C ATOM 774 N ILE A 149 -27.466 -11.045 -11.067 1.00 57.32 N ANISOU 774 N ILE A 149 7585 7264 6929 188 -269 919 N ATOM 775 CA ILE A 149 -27.627 -11.752 -12.330 1.00 63.36 C ANISOU 775 CA ILE A 149 8434 8085 7554 193 -288 895 C ATOM 776 C ILE A 149 -29.110 -11.922 -12.662 1.00 68.18 C ANISOU 776 C ILE A 149 9047 8684 8173 173 -404 854 C ATOM 777 O ILE A 149 -29.529 -11.691 -13.796 1.00 71.78 O ANISOU 777 O ILE A 149 9553 9184 8537 173 -475 883 O ATOM 778 CB ILE A 149 -26.938 -13.131 -12.286 1.00 58.16 C ANISOU 778 CB ILE A 149 7825 7436 6838 213 -214 809 C ATOM 779 CG1 ILE A 149 -25.420 -12.958 -12.184 1.00 70.68 C ANISOU 779 CG1 ILE A 149 9398 9047 8410 241 -104 851 C ATOM 780 CG2 ILE A 149 -27.286 -13.941 -13.524 1.00 59.24 C ANISOU 780 CG2 ILE A 149 8051 7622 6836 223 -251 750 C ATOM 781 CD1 ILE A 149 -24.661 -14.245 -11.916 1.00 75.09 C ANISOU 781 CD1 ILE A 149 9983 9595 8954 274 -36 765 C ATOM 782 N SER A 150 -29.896 -12.323 -11.667 1.00 65.45 N ANISOU 782 N SER A 150 8645 8286 7936 153 -424 790 N ATOM 783 CA SER A 150 -31.333 -12.520 -11.846 1.00 62.87 C ANISOU 783 CA SER A 150 8291 7945 7650 127 -529 746 C ATOM 784 C SER A 150 -32.010 -11.275 -12.402 1.00 70.26 C ANISOU 784 C SER A 150 9192 8888 8615 134 -627 816 C ATOM 785 O SER A 150 -32.751 -11.342 -13.383 1.00 73.74 O ANISOU 785 O SER A 150 9665 9353 9001 129 -731 812 O ATOM 786 CB SER A 150 -31.990 -12.889 -10.516 1.00 62.90 C ANISOU 786 CB SER A 150 8213 7901 7783 99 -509 692 C ATOM 787 OG SER A 150 -31.496 -14.122 -10.031 1.00 73.54 O ANISOU 787 OG SER A 150 9601 9229 9111 86 -441 639 O ATOM 788 N VAL A 151 -31.762 -10.144 -11.753 1.00 69.98 N ANISOU 788 N VAL A 151 9093 8823 8674 148 -609 874 N ATOM 789 CA VAL A 151 -32.376 -8.884 -12.146 1.00 69.70 C ANISOU 789 CA VAL A 151 9015 8767 8699 162 -710 944 C ATOM 790 C VAL A 151 -31.834 -8.420 -13.492 1.00 77.48 C ANISOU 790 C VAL A 151 10090 9797 9552 168 -745 1048 C ATOM 791 O VAL A 151 -32.575 -7.892 -14.322 1.00 70.75 O ANISOU 791 O VAL A 151 9249 8949 8685 172 -867 1097 O ATOM 792 CB VAL A 151 -32.120 -7.793 -11.092 1.00 64.22 C ANISOU 792 CB VAL A 151 8239 8017 8147 180 -681 970 C ATOM 793 CG1 VAL A 151 -32.670 -6.453 -11.562 1.00 59.64 C ANISOU 793 CG1 VAL A 151 7621 7395 7646 201 -797 1047 C ATOM 794 CG2 VAL A 151 -32.740 -8.193 -9.762 1.00 58.10 C ANISOU 794 CG2 VAL A 151 7379 7219 7479 174 -642 868 C ATOM 795 N ASP A 152 -30.536 -8.615 -13.698 1.00 85.50 N ANISOU 795 N ASP A 152 11165 10851 10472 169 -638 1086 N ATOM 796 CA ASP A 152 -29.896 -8.234 -14.949 1.00 86.35 C ANISOU 796 CA ASP A 152 11357 11021 10432 169 -638 1191 C ATOM 797 C ASP A 152 -30.540 -8.966 -16.123 1.00 74.85 C ANISOU 797 C ASP A 152 9989 9631 8820 168 -715 1154 C ATOM 798 O ASP A 152 -30.772 -8.380 -17.180 1.00 80.51 O ANISOU 798 O ASP A 152 10761 10387 9441 166 -797 1245 O ATOM 799 CB ASP A 152 -28.400 -8.544 -14.894 1.00 96.54 C ANISOU 799 CB ASP A 152 12676 12354 11652 171 -488 1210 C ATOM 800 CG ASP A 152 -27.647 -8.005 -16.094 1.00108.00 C ANISOU 800 CG ASP A 152 14195 13881 12959 163 -458 1337 C ATOM 801 OD1 ASP A 152 -27.223 -6.831 -16.052 1.00110.10 O ANISOU 801 OD1 ASP A 152 14426 14116 13292 146 -459 1464 O ATOM 802 OD2 ASP A 152 -27.478 -8.754 -17.080 1.00112.96 O ANISOU 802 OD2 ASP A 152 14913 14602 13404 172 -433 1308 O ATOM 803 N ARG A 153 -30.829 -10.249 -15.927 1.00 68.73 N ANISOU 803 N ARG A 153 9231 8863 8021 167 -699 1022 N ATOM 804 CA ARG A 153 -31.421 -11.071 -16.976 1.00 69.79 C ANISOU 804 CA ARG A 153 9450 9050 8017 167 -780 957 C ATOM 805 C ARG A 153 -32.882 -10.711 -17.231 1.00 68.35 C ANISOU 805 C ARG A 153 9229 8838 7903 155 -954 955 C ATOM 806 O ARG A 153 -33.369 -10.838 -18.354 1.00 68.83 O ANISOU 806 O ARG A 153 9366 8951 7837 156 -1063 957 O ATOM 807 CB ARG A 153 -31.302 -12.553 -16.624 1.00 62.59 C ANISOU 807 CB ARG A 153 8562 8128 7093 166 -723 813 C ATOM 808 CG ARG A 153 -29.913 -13.130 -16.860 1.00 62.60 C ANISOU 808 CG ARG A 153 8630 8181 6976 193 -582 794 C ATOM 809 N TYR A 154 -33.580 -10.270 -16.191 1.00 62.93 N ANISOU 809 N TYR A 154 8420 8074 7415 148 -981 943 N ATOM 810 CA TYR A 154 -34.962 -9.837 -16.348 1.00 76.34 C ANISOU 810 CA TYR A 154 10052 9741 9213 144 -1141 939 C ATOM 811 C TYR A 154 -35.029 -8.602 -17.234 1.00 77.29 C ANISOU 811 C TYR A 154 10205 9874 9290 164 -1246 1076 C ATOM 812 O TYR A 154 -35.809 -8.544 -18.184 1.00 74.88 O ANISOU 812 O TYR A 154 9936 9594 8923 166 -1397 1092 O ATOM 813 CB TYR A 154 -35.594 -9.526 -14.993 1.00 78.50 C ANISOU 813 CB TYR A 154 10178 9942 9708 142 -1122 896 C ATOM 814 CG TYR A 154 -36.817 -8.643 -15.096 1.00 80.91 C ANISOU 814 CG TYR A 154 10387 10209 10147 158 -1273 919 C ATOM 815 CD1 TYR A 154 -37.974 -9.097 -15.713 1.00 64.70 C ANISOU 815 CD1 TYR A 154 8314 8167 8103 145 -1416 867 C ATOM 816 CD2 TYR A 154 -36.814 -7.355 -14.578 1.00 63.47 C ANISOU 816 CD2 TYR A 154 8102 7944 8070 191 -1283 985 C ATOM 817 CE1 TYR A 154 -39.091 -8.295 -15.812 1.00 65.64 C ANISOU 817 CE1 TYR A 154 8331 8249 8361 167 -1562 885 C ATOM 818 CE2 TYR A 154 -37.927 -6.548 -14.671 1.00 65.32 C ANISOU 818 CE2 TYR A 154 8240 8134 8444 219 -1426 997 C ATOM 819 CZ TYR A 154 -39.063 -7.023 -15.288 1.00 65.50 C ANISOU 819 CZ TYR A 154 8236 8174 8476 209 -1564 949 C ATOM 820 OH TYR A 154 -40.177 -6.221 -15.384 1.00 99.89 O ANISOU 820 OH TYR A 154 12481 12483 12988 244 -1716 959 O ATOM 821 N ILE A 155 -34.202 -7.614 -16.914 1.00 82.46 N ANISOU 821 N ILE A 155 10846 10502 9981 175 -1175 1181 N ATOM 822 CA ILE A 155 -34.176 -6.365 -17.661 1.00 81.35 C ANISOU 822 CA ILE A 155 10734 10353 9822 186 -1269 1336 C ATOM 823 C ILE A 155 -33.845 -6.628 -19.125 1.00 77.95 C ANISOU 823 C ILE A 155 10452 10026 9141 176 -1304 1404 C ATOM 824 O ILE A 155 -34.307 -5.913 -20.012 1.00 68.46 O ANISOU 824 O ILE A 155 9293 8832 7887 181 -1444 1513 O ATOM 825 CB ILE A 155 -33.149 -5.384 -17.070 1.00 73.59 C ANISOU 825 CB ILE A 155 9721 9321 8920 186 -1170 1435 C ATOM 826 CG1 ILE A 155 -33.533 -5.024 -15.632 1.00 68.23 C ANISOU 826 CG1 ILE A 155 8903 8545 8475 204 -1150 1357 C ATOM 827 CG2 ILE A 155 -33.062 -4.125 -17.923 1.00 70.51 C ANISOU 827 CG2 ILE A 155 9372 8911 8508 185 -1269 1616 C ATOM 828 CD1 ILE A 155 -32.445 -4.306 -14.870 1.00 65.04 C ANISOU 828 CD1 ILE A 155 8468 8092 8152 202 -1044 1410 C ATOM 829 N ALA A 156 -33.048 -7.662 -19.373 1.00 79.38 N ANISOU 829 N ALA A 156 10712 10287 9161 168 -1180 1337 N ATOM 830 CA ALA A 156 -32.672 -8.025 -20.733 1.00 80.10 C ANISOU 830 CA ALA A 156 10949 10496 8989 167 -1188 1373 C ATOM 831 C ALA A 156 -33.899 -8.461 -21.524 1.00 83.67 C ANISOU 831 C ALA A 156 11446 10973 9374 171 -1376 1311 C ATOM 832 O ALA A 156 -34.081 -8.067 -22.675 1.00 86.56 O ANISOU 832 O ALA A 156 11910 11405 9574 172 -1482 1403 O ATOM 833 CB ALA A 156 -31.632 -9.134 -20.714 1.00 74.53 C ANISOU 833 CB ALA A 156 10300 9860 8158 172 -1016 1276 C ATOM 834 N ILE A 157 -34.740 -9.275 -20.895 1.00 87.92 N ANISOU 834 N ILE A 157 11909 11456 10039 167 -1422 1160 N ATOM 835 CA ILE A 157 -35.949 -9.775 -21.534 1.00 94.30 C ANISOU 835 CA ILE A 157 12735 12274 10821 164 -1608 1081 C ATOM 836 C ILE A 157 -36.954 -8.646 -21.748 1.00 96.84 C ANISOU 836 C ILE A 157 12993 12546 11255 174 -1796 1184 C ATOM 837 O ILE A 157 -37.479 -8.470 -22.847 1.00 99.66 O ANISOU 837 O ILE A 157 13431 12952 11484 180 -1961 1230 O ATOM 838 CB ILE A 157 -36.604 -10.881 -20.685 1.00 98.04 C ANISOU 838 CB ILE A 157 13119 12687 11444 144 -1601 909 C ATOM 839 CG1 ILE A 157 -35.666 -12.086 -20.570 1.00 99.14 C ANISOU 839 CG1 ILE A 157 13333 12860 11476 140 -1446 803 C ATOM 840 CG2 ILE A 157 -37.929 -11.306 -21.295 1.00105.35 C ANISOU 840 CG2 ILE A 157 14035 13610 12384 131 -1810 832 C ATOM 841 CD1 ILE A 157 -36.151 -13.156 -19.614 1.00 97.04 C ANISOU 841 CD1 ILE A 157 12983 12519 11368 111 -1419 662 C ATOM 842 N LYS A 158 -37.212 -7.884 -20.691 1.00 95.53 N ANISOU 842 N LYS A 158 12685 12283 11329 182 -1776 1213 N ATOM 843 CA LYS A 158 -38.181 -6.795 -20.738 1.00 91.99 C ANISOU 843 CA LYS A 158 12151 11766 11035 205 -1950 1292 C ATOM 844 C LYS A 158 -37.723 -5.690 -21.689 1.00 95.47 C ANISOU 844 C LYS A 158 12693 12228 11352 217 -2019 1489 C ATOM 845 O LYS A 158 -38.476 -5.253 -22.562 1.00 91.00 O ANISOU 845 O LYS A 158 12161 11668 10747 231 -2219 1559 O ATOM 846 CB LYS A 158 -38.387 -6.220 -19.334 1.00 89.89 C ANISOU 846 CB LYS A 158 11717 11396 11040 221 -1883 1264 C ATOM 847 CG LYS A 158 -39.490 -5.178 -19.240 1.00100.66 C ANISOU 847 CG LYS A 158 12962 12676 12607 259 -2059 1307 C ATOM 848 CD LYS A 158 -40.865 -5.801 -19.428 1.00105.41 C ANISOU 848 CD LYS A 158 13482 13281 13286 257 -2212 1195 C ATOM 849 CE LYS A 158 -41.968 -4.764 -19.301 1.00106.99 C ANISOU 849 CE LYS A 158 13542 13396 13712 307 -2387 1226 C ATOM 850 NZ LYS A 158 -43.323 -5.381 -19.326 1.00106.72 N ANISOU 850 NZ LYS A 158 13389 13364 13795 302 -2521 1106 N ATOM 851 N LYS A 159 -36.485 -5.242 -21.510 1.00102.50 N ANISOU 851 N LYS A 159 13628 13129 12187 207 -1860 1585 N ATOM 852 CA LYS A 159 -35.920 -4.176 -22.329 1.00102.80 C ANISOU 852 CA LYS A 159 13758 13184 12119 201 -1896 1793 C ATOM 853 C LYS A 159 -34.853 -4.718 -23.275 1.00110.17 C ANISOU 853 C LYS A 159 14853 14261 12746 174 -1777 1840 C ATOM 854 O LYS A 159 -33.662 -4.673 -22.962 1.00100.16 O ANISOU 854 O LYS A 159 13596 13016 11443 156 -1588 1878 O ATOM 855 CB LYS A 159 -35.313 -3.093 -21.437 1.00 97.90 C ANISOU 855 CB LYS A 159 13049 12455 11692 202 -1813 1886 C ATOM 856 N PRO A 160 -35.277 -5.231 -24.441 1.00132.10 N ANISOU 856 N PRO A 160 17753 17141 15299 175 -1890 1828 N ATOM 857 CA PRO A 160 -34.341 -5.788 -25.425 1.00151.03 C ANISOU 857 CA PRO A 160 20311 19695 17379 160 -1779 1851 C ATOM 858 C PRO A 160 -33.409 -4.732 -26.013 1.00170.56 C ANISOU 858 C PRO A 160 22859 22214 19732 132 -1713 2088 C ATOM 859 O PRO A 160 -32.248 -5.028 -26.298 1.00176.19 O ANISOU 859 O PRO A 160 23639 23033 20273 115 -1522 2112 O ATOM 860 CB PRO A 160 -35.266 -6.355 -26.508 1.00148.89 C ANISOU 860 CB PRO A 160 20144 19502 16924 172 -1972 1790 C ATOM 861 CG PRO A 160 -36.531 -5.587 -26.371 1.00144.67 C ANISOU 861 CG PRO A 160 19521 18855 16593 187 -2208 1842 C ATOM 862 CD PRO A 160 -36.672 -5.298 -24.910 1.00137.24 C ANISOU 862 CD PRO A 160 18392 17769 15983 195 -2136 1786 C ATOM 863 N ILE A 161 -33.913 -3.515 -26.190 1.00177.02 N ANISOU 863 N ILE A 161 23657 22947 20654 128 -1871 2263 N ATOM 864 CA ILE A 161 -33.101 -2.424 -26.714 1.00178.72 C ANISOU 864 CA ILE A 161 23937 23181 20789 89 -1828 2514 C ATOM 865 C ILE A 161 -32.098 -1.957 -25.666 1.00180.86 C ANISOU 865 C ILE A 161 24098 23367 21252 66 -1639 2548 C ATOM 866 O ILE A 161 -32.156 -2.374 -24.509 1.00182.34 O ANISOU 866 O ILE A 161 24163 23476 21643 88 -1570 2384 O ATOM 867 CB ILE A 161 -33.971 -1.227 -27.142 1.00177.82 C ANISOU 867 CB ILE A 161 23828 22967 20767 93 -2075 2697 C ATOM 868 N GLN A 162 -31.176 -1.093 -26.078 1.00182.67 N ANISOU 868 N GLN A 162 24373 23618 21417 16 -1560 2765 N ATOM 869 CA GLN A 162 -30.152 -0.578 -25.177 1.00181.98 C ANISOU 869 CA GLN A 162 24184 23451 21510 -14 -1395 2812 C ATOM 870 C GLN A 162 -29.309 -1.720 -24.623 1.00176.78 C ANISOU 870 C GLN A 162 23491 22875 20801 -5 -1171 2628 C ATOM 871 O GLN A 162 -29.299 -1.969 -23.417 1.00172.11 O ANISOU 871 O GLN A 162 22780 22188 20427 18 -1121 2486 O ATOM 872 CB GLN A 162 -30.795 0.199 -24.027 1.00182.47 C ANISOU 872 CB GLN A 162 24100 23302 21930 12 -1509 2782 C ATOM 873 N ALA A 163 -28.605 -2.411 -25.513 1.00175.73 N ANISOU 873 N ALA A 163 23467 22924 20379 -18 -1040 2630 N ATOM 874 CA ALA A 163 -27.761 -3.533 -25.122 1.00171.83 C ANISOU 874 CA ALA A 163 22949 22513 19826 0 -834 2457 C ATOM 875 C ALA A 163 -26.357 -3.384 -25.704 1.00168.63 C ANISOU 875 C ALA A 163 22582 22241 19250 -44 -625 2585 C ATOM 876 O ALA A 163 -25.718 -4.372 -26.069 1.00169.15 O ANISOU 876 O ALA A 163 22693 22449 19128 -21 -473 2472 O ATOM 877 CB ALA A 163 -28.387 -4.845 -25.575 1.00170.03 C ANISOU 877 CB ALA A 163 22802 22379 19423 49 -876 2253 C ATOM 878 N ASN A 164 -25.885 -2.144 -25.794 1.00161.04 N ANISOU 878 N ASN A 164 21594 21228 18364 -106 -619 2819 N ATOM 879 CA ASN A 164 -24.547 -1.870 -26.304 1.00156.41 C ANISOU 879 CA ASN A 164 21019 20761 17648 -164 -415 2969 C ATOM 880 C ASN A 164 -23.487 -2.462 -25.387 1.00158.78 C ANISOU 880 C ASN A 164 21199 21060 18070 -151 -212 2834 C ATOM 881 O ASN A 164 -23.545 -2.293 -24.169 1.00163.49 O ANISOU 881 O ASN A 164 21674 21499 18946 -139 -242 2757 O ATOM 882 CB ASN A 164 -24.325 -0.365 -26.441 1.00153.38 C ANISOU 882 CB ASN A 164 20614 20283 17381 -246 -472 3255 C ATOM 883 CG ASN A 164 -25.373 0.302 -27.305 1.00157.15 C ANISOU 883 CG ASN A 164 21208 20740 17763 -256 -696 3410 C ATOM 884 OD1 ASN A 164 -26.464 -0.234 -27.502 1.00158.65 O ANISOU 884 OD1 ASN A 164 21457 20934 17889 -195 -851 3280 O ATOM 885 ND2 ASN A 164 -25.048 1.478 -27.828 1.00160.17 N ANISOU 885 ND2 ASN A 164 21619 21092 18145 -336 -724 3695 N ATOM 886 N GLN A 165 -22.517 -3.155 -25.974 1.00156.93 N ANISOU 886 N GLN A 165 20997 21006 17623 -148 -10 2801 N ATOM 887 CA GLN A 165 -21.455 -3.776 -25.195 1.00152.05 C ANISOU 887 CA GLN A 165 20263 20398 17112 -127 179 2673 C ATOM 888 C GLN A 165 -20.640 -2.713 -24.469 1.00150.83 C ANISOU 888 C GLN A 165 19972 20131 17207 -197 234 2829 C ATOM 889 O GLN A 165 -20.308 -2.871 -23.294 1.00149.80 O ANISOU 889 O GLN A 165 19720 19888 17309 -178 260 2719 O ATOM 890 CB GLN A 165 -20.547 -4.612 -26.099 1.00145.45 C ANISOU 890 CB GLN A 165 19482 19788 15996 -107 388 2622 C ATOM 891 CG GLN A 165 -19.476 -5.391 -25.347 1.00136.84 C ANISOU 891 CG GLN A 165 18269 18709 15014 -67 573 2468 C ATOM 892 CD GLN A 165 -20.046 -6.397 -24.358 1.00122.12 C ANISOU 892 CD GLN A 165 16373 16731 13294 12 493 2214 C ATOM 893 OE1 GLN A 165 -19.536 -6.539 -23.246 1.00108.98 O ANISOU 893 OE1 GLN A 165 14585 14967 11857 25 539 2143 O ATOM 894 NE2 GLN A 165 -21.095 -7.108 -24.760 1.00121.00 N ANISOU 894 NE2 GLN A 165 16346 16607 13022 61 369 2083 N ATOM 895 N TYR A 166 -20.329 -1.628 -25.172 1.00145.51 N ANISOU 895 N TYR A 166 19323 19481 16481 -282 241 3089 N ATOM 896 CA TYR A 166 -19.538 -0.540 -24.604 1.00135.03 C ANISOU 896 CA TYR A 166 17872 18040 15393 -364 281 3259 C ATOM 897 C TYR A 166 -20.135 -0.051 -23.286 1.00129.62 C ANISOU 897 C TYR A 166 17094 17115 15042 -345 116 3185 C ATOM 898 O TYR A 166 -19.418 0.135 -22.302 1.00128.20 O ANISOU 898 O TYR A 166 16782 16843 15087 -359 176 3147 O ATOM 899 CB TYR A 166 -19.445 0.622 -25.594 1.00131.22 C ANISOU 899 CB TYR A 166 17454 17584 14817 -464 253 3569 C ATOM 900 CG TYR A 166 -18.596 1.774 -25.106 1.00127.54 C ANISOU 900 CG TYR A 166 16862 16994 14604 -563 291 3761 C ATOM 901 N ASN A 167 -21.447 0.160 -23.276 1.00123.21 N ANISOU 901 N ASN A 167 16348 16209 14258 -309 -93 3160 N ATOM 902 CA ASN A 167 -22.143 0.575 -22.064 1.00116.91 C ANISOU 902 CA ASN A 167 15466 15200 13754 -278 -246 3067 C ATOM 903 C ASN A 167 -22.316 -0.587 -21.093 1.00115.09 C ANISOU 903 C ASN A 167 15185 14965 13580 -197 -208 2790 C ATOM 904 O ASN A 167 -22.213 -0.414 -19.879 1.00118.73 O ANISOU 904 O ASN A 167 15540 15296 14278 -183 -226 2701 O ATOM 905 CB ASN A 167 -23.514 1.159 -22.408 1.00117.94 C ANISOU 905 CB ASN A 167 15669 15241 13902 -259 -477 3125 C ATOM 906 CG ASN A 167 -23.419 2.433 -23.223 1.00124.31 C ANISOU 906 CG ASN A 167 16524 16008 14701 -339 -552 3416 C ATOM 907 OD1 ASN A 167 -22.433 2.666 -23.923 1.00124.64 O ANISOU 907 OD1 ASN A 167 16588 16155 14613 -414 -412 3587 O ATOM 908 ND2 ASN A 167 -24.448 3.268 -23.134 1.00127.27 N ANISOU 908 ND2 ASN A 167 16909 16227 15223 -325 -772 3480 N ATOM 909 N SER A 168 -22.578 -1.771 -21.635 1.00108.43 N ANISOU 909 N SER A 168 14423 14261 12514 -147 -162 2658 N ATOM 910 CA SER A 168 -22.816 -2.954 -20.817 1.00102.43 C ANISOU 910 CA SER A 168 13630 13493 11795 -76 -137 2409 C ATOM 911 C SER A 168 -21.615 -3.267 -19.932 1.00 93.98 C ANISOU 911 C SER A 168 12450 12413 10847 -76 19 2342 C ATOM 912 O SER A 168 -21.777 -3.719 -18.799 1.00 91.28 O ANISOU 912 O SER A 168 12041 11984 10657 -37 0 2188 O ATOM 913 CB SER A 168 -23.139 -4.158 -21.705 1.00109.72 C ANISOU 913 CB SER A 168 14667 14568 12452 -31 -107 2292 C ATOM 914 OG SER A 168 -24.338 -3.951 -22.432 1.00113.30 O ANISOU 914 OG SER A 168 15219 15025 12806 -25 -279 2330 O ATOM 915 N ARG A 169 -20.413 -3.025 -20.450 1.00 85.99 N ANISOU 915 N ARG A 169 11413 11493 9765 -122 172 2462 N ATOM 916 CA ARG A 169 -19.193 -3.292 -19.695 1.00 89.55 C ANISOU 916 CA ARG A 169 11746 11942 10336 -122 316 2409 C ATOM 917 C ARG A 169 -19.113 -2.391 -18.472 1.00 93.42 C ANISOU 917 C ARG A 169 12125 12249 11122 -151 233 2435 C ATOM 918 O ARG A 169 -18.929 -2.866 -17.351 1.00 94.97 O ANISOU 918 O ARG A 169 12249 12379 11457 -111 238 2288 O ATOM 919 CB ARG A 169 -17.959 -3.097 -20.576 1.00 92.89 C ANISOU 919 CB ARG A 169 12149 12509 10636 -174 498 2551 C ATOM 920 CG ARG A 169 -17.808 -4.159 -21.650 1.00112.36 C ANISOU 920 CG ARG A 169 14711 15176 12807 -128 619 2476 C ATOM 921 CD ARG A 169 -16.584 -3.927 -22.521 1.00127.51 C ANISOU 921 CD ARG A 169 16597 17255 14595 -180 820 2617 C ATOM 922 NE ARG A 169 -16.607 -4.774 -23.712 1.00141.72 N ANISOU 922 NE ARG A 169 18515 19258 16073 -136 918 2558 N ATOM 923 CZ ARG A 169 -16.211 -6.044 -23.746 1.00145.42 C ANISOU 923 CZ ARG A 169 18984 19823 16448 -49 1031 2351 C ATOM 924 NH1 ARG A 169 -15.750 -6.638 -22.653 1.00138.16 N ANISOU 924 NH1 ARG A 169 17952 18814 15729 1 1059 2198 N ATOM 925 NH2 ARG A 169 -16.277 -6.727 -24.881 1.00152.13 N ANISOU 925 NH2 ARG A 169 19950 20854 16997 -8 1108 2292 N ATOM 926 N ALA A 170 -19.252 -1.088 -18.693 1.00 91.04 N ANISOU 926 N ALA A 170 11816 11863 10914 -218 148 2623 N ATOM 927 CA ALA A 170 -19.248 -0.131 -17.597 1.00 86.61 C ANISOU 927 CA ALA A 170 11157 11115 10635 -242 49 2641 C ATOM 928 C ALA A 170 -20.351 -0.476 -16.608 1.00 79.51 C ANISOU 928 C ALA A 170 10260 10114 9836 -169 -81 2454 C ATOM 929 O ALA A 170 -20.106 -0.610 -15.410 1.00 84.92 O ANISOU 929 O ALA A 170 10865 10720 10681 -145 -83 2333 O ATOM 930 CB ALA A 170 -19.438 1.275 -18.125 1.00 90.76 C ANISOU 930 CB ALA A 170 11697 11550 11236 -318 -51 2868 C ATOM 931 N THR A 171 -21.567 -0.627 -17.123 1.00 74.41 N ANISOU 931 N THR A 171 9705 9479 9089 -137 -189 2434 N ATOM 932 CA THR A 171 -22.726 -0.923 -16.291 1.00 74.23 C ANISOU 932 CA THR A 171 9675 9371 9156 -75 -308 2271 C ATOM 933 C THR A 171 -22.479 -2.182 -15.474 1.00 74.70 C ANISOU 933 C THR A 171 9708 9476 9200 -25 -218 2073 C ATOM 934 O THR A 171 -22.858 -2.258 -14.305 1.00 74.86 O ANISOU 934 O THR A 171 9671 9407 9365 7 -266 1950 O ATOM 935 CB THR A 171 -24.000 -1.123 -17.140 1.00 79.66 C ANISOU 935 CB THR A 171 10460 10097 9710 -48 -422 2272 C ATOM 936 OG1 THR A 171 -24.242 0.042 -17.940 1.00 78.86 O ANISOU 936 OG1 THR A 171 10394 9951 9617 -92 -522 2473 O ATOM 937 CG2 THR A 171 -25.207 -1.369 -16.244 1.00 88.59 C ANISOU 937 CG2 THR A 171 11558 11142 10962 8 -537 2110 C ATOM 938 N ALA A 172 -21.839 -3.168 -16.095 1.00 80.33 N ANISOU 938 N ALA A 172 10462 10327 9734 -16 -88 2043 N ATOM 939 CA ALA A 172 -21.517 -4.414 -15.414 1.00 76.21 C ANISOU 939 CA ALA A 172 9921 9839 9198 32 -7 1869 C ATOM 940 C ALA A 172 -20.568 -4.140 -14.257 1.00 72.39 C ANISOU 940 C ALA A 172 9327 9281 8896 24 40 1847 C ATOM 941 O ALA A 172 -20.864 -4.477 -13.113 1.00 68.59 O ANISOU 941 O ALA A 172 8810 8729 8522 56 1 1723 O ATOM 942 CB ALA A 172 -20.900 -5.399 -16.384 1.00 73.16 C ANISOU 942 CB ALA A 172 9594 9606 8600 49 122 1846 C ATOM 943 N PHE A 173 -19.431 -3.520 -14.560 1.00 70.29 N ANISOU 943 N PHE A 173 9007 9037 8664 -24 122 1973 N ATOM 944 CA PHE A 173 -18.456 -3.164 -13.536 1.00 76.15 C ANISOU 944 CA PHE A 173 9637 9707 9590 -41 151 1964 C ATOM 945 C PHE A 173 -19.114 -2.435 -12.367 1.00 78.31 C ANISOU 945 C PHE A 173 9872 9827 10056 -36 12 1914 C ATOM 946 O PHE A 173 -18.848 -2.741 -11.204 1.00 83.25 O ANISOU 946 O PHE A 173 10444 10403 10783 -8 6 1800 O ATOM 947 CB PHE A 173 -17.351 -2.289 -14.128 1.00 81.88 C ANISOU 947 CB PHE A 173 10300 10455 10355 -115 226 2143 C ATOM 948 CG PHE A 173 -16.332 -3.050 -14.932 1.00 97.48 C ANISOU 948 CG PHE A 173 12266 12589 12184 -113 402 2161 C ATOM 949 CD1 PHE A 173 -16.458 -4.414 -15.140 1.00 97.68 C ANISOU 949 CD1 PHE A 173 12348 12712 12053 -40 468 2016 C ATOM 950 CD2 PHE A 173 -15.236 -2.396 -15.470 1.00116.12 C ANISOU 950 CD2 PHE A 173 14553 14995 14573 -184 503 2320 C ATOM 951 CE1 PHE A 173 -15.514 -5.107 -15.877 1.00102.76 C ANISOU 951 CE1 PHE A 173 12976 13500 12568 -24 632 2012 C ATOM 952 CE2 PHE A 173 -14.290 -3.085 -16.204 1.00118.65 C ANISOU 952 CE2 PHE A 173 14849 15475 14759 -176 681 2326 C ATOM 953 CZ PHE A 173 -14.429 -4.441 -16.408 1.00110.31 C ANISOU 953 CZ PHE A 173 13851 14518 13544 -88 746 2164 C ATOM 954 N ILE A 174 -19.965 -1.464 -12.678 1.00 69.42 N ANISOU 954 N ILE A 174 8774 8628 8975 -57 -101 1997 N ATOM 955 CA ILE A 174 -20.666 -0.714 -11.646 1.00 62.23 C ANISOU 955 CA ILE A 174 7826 7574 8246 -41 -233 1937 C ATOM 956 C ILE A 174 -21.488 -1.649 -10.766 1.00 69.09 C ANISOU 956 C ILE A 174 8710 8449 9092 25 -254 1748 C ATOM 957 O ILE A 174 -21.422 -1.572 -9.540 1.00 59.92 O ANISOU 957 O ILE A 174 7497 7220 8050 46 -281 1646 O ATOM 958 CB ILE A 174 -21.591 0.349 -12.253 1.00 63.21 C ANISOU 958 CB ILE A 174 7983 7622 8414 -59 -360 2046 C ATOM 959 CG1 ILE A 174 -20.763 1.426 -12.956 1.00 64.88 C ANISOU 959 CG1 ILE A 174 8171 7796 8683 -138 -353 2254 C ATOM 960 CG2 ILE A 174 -22.447 0.982 -11.172 1.00 62.59 C ANISOU 960 CG2 ILE A 174 7862 7405 8515 -20 -489 1943 C ATOM 961 CD1 ILE A 174 -21.584 2.375 -13.797 1.00 66.19 C ANISOU 961 CD1 ILE A 174 8390 7900 8860 -160 -475 2398 C ATOM 962 N LYS A 175 -22.261 -2.529 -11.394 1.00 60.53 N ANISOU 962 N LYS A 175 7700 7448 7851 52 -245 1704 N ATOM 963 CA LYS A 175 -23.060 -3.504 -10.661 1.00 63.47 C ANISOU 963 CA LYS A 175 8087 7830 8197 100 -257 1543 C ATOM 964 C LYS A 175 -22.188 -4.398 -9.787 1.00 63.93 C ANISOU 964 C LYS A 175 8117 7914 8259 117 -168 1449 C ATOM 965 O LYS A 175 -22.495 -4.618 -8.617 1.00 60.81 O ANISOU 965 O LYS A 175 7694 7473 7936 141 -194 1343 O ATOM 966 CB LYS A 175 -23.883 -4.363 -11.622 1.00 74.75 C ANISOU 966 CB LYS A 175 9599 9344 9460 114 -262 1520 C ATOM 967 CG LYS A 175 -25.133 -3.678 -12.161 1.00 94.06 C ANISOU 967 CG LYS A 175 12067 11752 11921 115 -389 1564 C ATOM 968 CD LYS A 175 -26.264 -4.680 -12.355 1.00108.65 C ANISOU 968 CD LYS A 175 13959 13645 13680 141 -426 1459 C ATOM 969 CE LYS A 175 -27.568 -3.996 -12.724 1.00112.69 C ANISOU 969 CE LYS A 175 14466 14110 14241 150 -568 1485 C ATOM 970 NZ LYS A 175 -28.746 -4.802 -12.295 1.00107.82 N ANISOU 970 NZ LYS A 175 13834 13498 13634 174 -610 1350 N ATOM 971 N ILE A 176 -21.103 -4.914 -10.357 1.00 68.96 N ANISOU 971 N ILE A 176 8760 8627 8816 109 -63 1489 N ATOM 972 CA ILE A 176 -20.194 -5.772 -9.610 1.00 73.67 C ANISOU 972 CA ILE A 176 9323 9241 9425 133 11 1409 C ATOM 973 C ILE A 176 -19.725 -5.041 -8.361 1.00 70.79 C ANISOU 973 C ILE A 176 8879 8785 9231 124 -34 1392 C ATOM 974 O ILE A 176 -19.765 -5.582 -7.255 1.00 72.75 O ANISOU 974 O ILE A 176 9119 9010 9514 153 -47 1287 O ATOM 975 CB ILE A 176 -18.955 -6.171 -10.440 1.00 82.43 C ANISOU 975 CB ILE A 176 10420 10440 10459 127 132 1466 C ATOM 976 CG1 ILE A 176 -19.368 -6.906 -11.716 1.00 85.79 C ANISOU 976 CG1 ILE A 176 10935 10968 10694 142 178 1466 C ATOM 977 CG2 ILE A 176 -18.021 -7.046 -9.619 1.00 84.58 C ANISOU 977 CG2 ILE A 176 10647 10718 10773 163 190 1379 C ATOM 978 CD1 ILE A 176 -20.337 -8.038 -11.487 1.00 93.02 C ANISOU 978 CD1 ILE A 176 11919 11885 11540 183 140 1334 C ATOM 979 N THR A 177 -19.290 -3.799 -8.547 1.00 66.74 N ANISOU 979 N THR A 177 8316 8220 8823 81 -64 1498 N ATOM 980 CA THR A 177 -18.740 -3.008 -7.454 1.00 71.96 C ANISOU 980 CA THR A 177 8900 8787 9655 69 -118 1480 C ATOM 981 C THR A 177 -19.790 -2.790 -6.369 1.00 80.54 C ANISOU 981 C THR A 177 9999 9803 10802 102 -214 1366 C ATOM 982 O THR A 177 -19.493 -2.896 -5.180 1.00 80.34 O ANISOU 982 O THR A 177 9943 9744 10839 122 -237 1275 O ATOM 983 CB THR A 177 -18.222 -1.640 -7.941 1.00 70.56 C ANISOU 983 CB THR A 177 8669 8543 9596 7 -150 1623 C ATOM 984 OG1 THR A 177 -17.251 -1.829 -8.979 1.00 67.88 O ANISOU 984 OG1 THR A 177 8311 8290 9190 -31 -40 1739 O ATOM 985 CG2 THR A 177 -17.578 -0.877 -6.795 1.00 81.69 C ANISOU 985 CG2 THR A 177 9996 9847 11193 -7 -218 1587 C ATOM 986 N VAL A 178 -21.017 -2.490 -6.785 1.00 57.90 N ANISOU 986 N VAL A 178 7171 6920 7909 111 -270 1369 N ATOM 987 CA VAL A 178 -22.115 -2.297 -5.846 1.00 66.22 C ANISOU 987 CA VAL A 178 8223 7923 9015 147 -345 1256 C ATOM 988 C VAL A 178 -22.334 -3.551 -5.005 1.00 64.62 C ANISOU 988 C VAL A 178 8046 7778 8727 179 -297 1134 C ATOM 989 O VAL A 178 -22.512 -3.470 -3.791 1.00 64.33 O ANISOU 989 O VAL A 178 7989 7712 8742 201 -325 1037 O ATOM 990 CB VAL A 178 -23.422 -1.941 -6.577 1.00 57.72 C ANISOU 990 CB VAL A 178 7176 6835 7921 156 -408 1281 C ATOM 991 CG1 VAL A 178 -24.616 -2.078 -5.644 1.00 71.72 C ANISOU 991 CG1 VAL A 178 8936 8591 9723 199 -451 1146 C ATOM 992 CG2 VAL A 178 -23.345 -0.531 -7.144 1.00 83.81 C ANISOU 992 CG2 VAL A 178 10454 10047 11343 129 -489 1399 C ATOM 993 N VAL A 179 -22.316 -4.709 -5.655 1.00 67.56 N ANISOU 993 N VAL A 179 8469 8233 8967 181 -227 1140 N ATOM 994 CA VAL A 179 -22.505 -5.977 -4.960 1.00 66.40 C ANISOU 994 CA VAL A 179 8353 8128 8747 204 -187 1044 C ATOM 995 C VAL A 179 -21.439 -6.165 -3.884 1.00 60.96 C ANISOU 995 C VAL A 179 7635 7425 8104 213 -170 1008 C ATOM 996 O VAL A 179 -21.747 -6.542 -2.753 1.00 58.28 O ANISOU 996 O VAL A 179 7302 7079 7762 230 -184 925 O ATOM 997 CB VAL A 179 -22.459 -7.168 -5.942 1.00 61.33 C ANISOU 997 CB VAL A 179 7770 7559 7974 206 -123 1057 C ATOM 998 CG1 VAL A 179 -22.327 -8.482 -5.188 1.00 57.72 C ANISOU 998 CG1 VAL A 179 7341 7121 7469 225 -85 976 C ATOM 999 CG2 VAL A 179 -23.701 -7.179 -6.823 1.00 55.59 C ANISOU 999 CG2 VAL A 179 7081 6852 7188 200 -161 1066 C ATOM 1000 N TRP A 180 -20.187 -5.896 -4.241 1.00 64.42 N ANISOU 1000 N TRP A 180 8035 7860 8580 200 -142 1075 N ATOM 1001 CA TRP A 180 -19.077 -6.039 -3.307 1.00 65.99 C ANISOU 1001 CA TRP A 180 8193 8043 8838 209 -142 1047 C ATOM 1002 C TRP A 180 -19.176 -5.025 -2.176 1.00 69.57 C ANISOU 1002 C TRP A 180 8609 8424 9401 208 -228 998 C ATOM 1003 O TRP A 180 -18.780 -5.305 -1.046 1.00 73.06 O ANISOU 1003 O TRP A 180 9047 8858 9855 226 -254 930 O ATOM 1004 CB TRP A 180 -17.741 -5.878 -4.033 1.00 65.40 C ANISOU 1004 CB TRP A 180 8062 7986 8802 191 -89 1133 C ATOM 1005 CG TRP A 180 -17.336 -7.096 -4.794 1.00 66.06 C ANISOU 1005 CG TRP A 180 8175 8147 8780 213 3 1139 C ATOM 1006 CD1 TRP A 180 -17.412 -7.282 -6.141 1.00 69.48 C ANISOU 1006 CD1 TRP A 180 8634 8641 9124 205 71 1198 C ATOM 1007 CD2 TRP A 180 -16.796 -8.305 -4.250 1.00 67.69 C ANISOU 1007 CD2 TRP A 180 8391 8374 8956 255 31 1075 C ATOM 1008 NE1 TRP A 180 -16.949 -8.532 -6.473 1.00 73.01 N ANISOU 1008 NE1 TRP A 180 9103 9146 9490 244 145 1158 N ATOM 1009 CE2 TRP A 180 -16.565 -9.181 -5.330 1.00 68.66 C ANISOU 1009 CE2 TRP A 180 8541 8562 8985 276 118 1085 C ATOM 1010 CE3 TRP A 180 -16.484 -8.732 -2.957 1.00 71.82 C ANISOU 1010 CE3 TRP A 180 8908 8862 9516 279 -17 1010 C ATOM 1011 CZ2 TRP A 180 -16.036 -10.458 -5.154 1.00 68.50 C ANISOU 1011 CZ2 TRP A 180 8534 8559 8933 325 155 1027 C ATOM 1012 CZ3 TRP A 180 -15.960 -10.000 -2.784 1.00 76.40 C ANISOU 1012 CZ3 TRP A 180 9506 9461 10059 322 14 973 C ATOM 1013 CH2 TRP A 180 -15.741 -10.848 -3.877 1.00 73.93 C ANISOU 1013 CH2 TRP A 180 9213 9199 9677 347 98 978 C ATOM 1014 N LEU A 181 -19.701 -3.845 -2.486 1.00 71.85 N ANISOU 1014 N LEU A 181 8876 8657 9767 190 -282 1028 N ATOM 1015 CA LEU A 181 -19.900 -2.817 -1.474 1.00 73.34 C ANISOU 1015 CA LEU A 181 9032 8766 10066 199 -372 961 C ATOM 1016 C LEU A 181 -20.981 -3.251 -0.489 1.00 71.51 C ANISOU 1016 C LEU A 181 8840 8562 9769 237 -382 839 C ATOM 1017 O LEU A 181 -20.839 -3.072 0.721 1.00 66.97 O ANISOU 1017 O LEU A 181 8259 7970 9217 257 -422 748 O ATOM 1018 CB LEU A 181 -20.271 -1.486 -2.130 1.00 57.12 C ANISOU 1018 CB LEU A 181 6947 6630 8124 176 -434 1026 C ATOM 1019 CG LEU A 181 -19.122 -0.773 -2.844 1.00 57.98 C ANISOU 1019 CG LEU A 181 7003 6695 8333 124 -436 1153 C ATOM 1020 CD1 LEU A 181 -19.648 0.395 -3.659 1.00 58.83 C ANISOU 1020 CD1 LEU A 181 7100 6723 8529 97 -497 1246 C ATOM 1021 CD2 LEU A 181 -18.078 -0.302 -1.843 1.00 58.40 C ANISOU 1021 CD2 LEU A 181 6995 6687 8508 114 -491 1109 C ATOM 1022 N ILE A 182 -22.059 -3.825 -1.012 1.00 55.48 N ANISOU 1022 N ILE A 182 6848 6578 7653 243 -345 837 N ATOM 1023 CA ILE A 182 -23.131 -4.342 -0.172 1.00 60.77 C ANISOU 1023 CA ILE A 182 7544 7288 8259 267 -334 736 C ATOM 1024 C ILE A 182 -22.614 -5.468 0.721 1.00 57.76 C ANISOU 1024 C ILE A 182 7201 6958 7789 272 -293 698 C ATOM 1025 O ILE A 182 -23.035 -5.601 1.869 1.00 55.17 O ANISOU 1025 O ILE A 182 6885 6651 7425 288 -298 613 O ATOM 1026 CB ILE A 182 -24.301 -4.872 -1.019 1.00 64.03 C ANISOU 1026 CB ILE A 182 7979 7740 8608 262 -305 753 C ATOM 1027 CG1 ILE A 182 -24.986 -3.719 -1.757 1.00 62.81 C ANISOU 1027 CG1 ILE A 182 7789 7530 8544 267 -369 785 C ATOM 1028 CG2 ILE A 182 -25.307 -5.601 -0.137 1.00 54.71 C ANISOU 1028 CG2 ILE A 182 6815 6612 7361 272 -274 663 C ATOM 1029 CD1 ILE A 182 -25.987 -4.169 -2.800 1.00 56.91 C ANISOU 1029 CD1 ILE A 182 7062 6820 7741 259 -363 820 C ATOM 1030 N SER A 183 -21.703 -6.273 0.183 1.00 61.70 N ANISOU 1030 N SER A 183 7718 7478 8248 261 -253 761 N ATOM 1031 CA SER A 183 -21.134 -7.395 0.923 1.00 64.03 C ANISOU 1031 CA SER A 183 8050 7805 8474 271 -228 740 C ATOM 1032 C SER A 183 -20.219 -6.906 2.040 1.00 59.78 C ANISOU 1032 C SER A 183 7486 7239 7987 283 -286 703 C ATOM 1033 O SER A 183 -20.319 -7.360 3.178 1.00 54.76 O ANISOU 1033 O SER A 183 6888 6627 7291 296 -300 647 O ATOM 1034 CB SER A 183 -20.360 -8.315 -0.023 1.00 66.72 C ANISOU 1034 CB SER A 183 8404 8166 8782 270 -176 804 C ATOM 1035 OG SER A 183 -21.224 -8.907 -0.980 1.00 69.33 O ANISOU 1035 OG SER A 183 8772 8525 9045 260 -134 820 O ATOM 1036 N ILE A 184 -19.317 -5.990 1.705 1.00 62.20 N ANISOU 1036 N ILE A 184 7733 7497 8404 275 -324 740 N ATOM 1037 CA ILE A 184 -18.450 -5.370 2.700 1.00 65.49 C ANISOU 1037 CA ILE A 184 8115 7874 8894 282 -401 698 C ATOM 1038 C ILE A 184 -19.292 -4.734 3.801 1.00 55.92 C ANISOU 1038 C ILE A 184 6923 6653 7670 300 -454 590 C ATOM 1039 O ILE A 184 -18.997 -4.875 4.985 1.00 63.00 O ANISOU 1039 O ILE A 184 7845 7565 8527 318 -498 521 O ATOM 1040 CB ILE A 184 -17.553 -4.290 2.069 1.00 61.44 C ANISOU 1040 CB ILE A 184 7520 7294 8531 254 -438 760 C ATOM 1041 CG1 ILE A 184 -16.507 -4.936 1.157 1.00 58.88 C ANISOU 1041 CG1 ILE A 184 7160 6998 8215 241 -374 854 C ATOM 1042 CG2 ILE A 184 -16.864 -3.480 3.153 1.00 58.73 C ANISOU 1042 CG2 ILE A 184 7138 6894 8284 257 -543 694 C ATOM 1043 CD1 ILE A 184 -15.724 -3.948 0.326 1.00 57.04 C ANISOU 1043 CD1 ILE A 184 6841 6717 8114 198 -379 944 C ATOM 1044 N GLY A 185 -20.338 -4.024 3.397 1.00 67.15 N ANISOU 1044 N GLY A 185 8334 8055 9123 301 -451 571 N ATOM 1045 CA GLY A 185 -21.245 -3.401 4.340 1.00 68.38 C ANISOU 1045 CA GLY A 185 8498 8210 9275 329 -486 454 C ATOM 1046 C GLY A 185 -21.816 -4.394 5.333 1.00 74.45 C ANISOU 1046 C GLY A 185 9328 9070 9890 343 -437 392 C ATOM 1047 O GLY A 185 -21.775 -4.172 6.541 1.00 84.55 O ANISOU 1047 O GLY A 185 10628 10370 11128 366 -474 298 O ATOM 1048 N ILE A 186 -22.353 -5.495 4.819 1.00 73.57 N ANISOU 1048 N ILE A 186 9251 9013 9691 326 -358 447 N ATOM 1049 CA ILE A 186 -22.990 -6.508 5.654 1.00 69.07 C ANISOU 1049 CA ILE A 186 8738 8524 8983 323 -304 415 C ATOM 1050 C ILE A 186 -21.994 -7.219 6.576 1.00 71.36 C ANISOU 1050 C ILE A 186 9079 8835 9198 325 -329 424 C ATOM 1051 O ILE A 186 -22.344 -7.618 7.685 1.00 71.56 O ANISOU 1051 O ILE A 186 9155 8922 9114 328 -317 379 O ATOM 1052 CB ILE A 186 -23.713 -7.557 4.782 1.00 62.30 C ANISOU 1052 CB ILE A 186 7900 7697 8075 294 -229 480 C ATOM 1053 CG1 ILE A 186 -24.904 -6.920 4.062 1.00 55.01 C ANISOU 1053 CG1 ILE A 186 6928 6766 7208 295 -216 460 C ATOM 1054 CG2 ILE A 186 -24.182 -8.728 5.628 1.00 55.14 C ANISOU 1054 CG2 ILE A 186 7053 6857 7040 275 -177 476 C ATOM 1055 CD1 ILE A 186 -25.502 -7.792 2.980 1.00 75.10 C ANISOU 1055 CD1 ILE A 186 9485 9325 9724 266 -171 523 C ATOM 1056 N ALA A 187 -20.754 -7.364 6.120 1.00 67.98 N ANISOU 1056 N ALA A 187 8636 8363 8832 325 -366 487 N ATOM 1057 CA ALA A 187 -19.756 -8.149 6.839 1.00 62.70 C ANISOU 1057 CA ALA A 187 8007 7705 8112 333 -402 509 C ATOM 1058 C ALA A 187 -18.944 -7.322 7.835 1.00 63.06 C ANISOU 1058 C ALA A 187 8037 7729 8194 353 -505 444 C ATOM 1059 O ALA A 187 -18.247 -7.878 8.681 1.00 62.32 O ANISOU 1059 O ALA A 187 7984 7653 8042 365 -556 446 O ATOM 1060 CB ALA A 187 -18.818 -8.828 5.842 1.00 69.08 C ANISOU 1060 CB ALA A 187 8791 8480 8975 331 -386 598 C ATOM 1061 N ILE A 188 -19.033 -5.999 7.741 1.00 73.06 N ANISOU 1061 N ILE A 188 9248 8949 9562 359 -549 385 N ATOM 1062 CA ILE A 188 -18.130 -5.121 8.489 1.00 75.58 C ANISOU 1062 CA ILE A 188 9538 9223 9955 373 -664 322 C ATOM 1063 C ILE A 188 -18.344 -5.112 10.009 1.00 73.63 C ANISOU 1063 C ILE A 188 9361 9034 9580 399 -716 215 C ATOM 1064 O ILE A 188 -17.410 -4.831 10.761 1.00 70.70 O ANISOU 1064 O ILE A 188 8991 8643 9228 412 -824 174 O ATOM 1065 CB ILE A 188 -18.187 -3.661 7.969 1.00 69.66 C ANISOU 1065 CB ILE A 188 8712 8386 9369 368 -711 287 C ATOM 1066 CG1 ILE A 188 -16.886 -2.928 8.305 1.00 58.98 C ANISOU 1066 CG1 ILE A 188 7303 6958 8147 362 -832 270 C ATOM 1067 CG2 ILE A 188 -19.387 -2.919 8.545 1.00 58.59 C ANISOU 1067 CG2 ILE A 188 7329 6997 7935 396 -710 166 C ATOM 1068 CD1 ILE A 188 -15.689 -3.409 7.510 1.00 68.00 C ANISOU 1068 CD1 ILE A 188 8387 8077 9373 334 -824 391 C ATOM 1069 N PRO A 189 -19.569 -5.409 10.474 1.00 68.15 N ANISOU 1069 N PRO A 189 8723 8419 8751 406 -639 168 N ATOM 1070 CA PRO A 189 -19.769 -5.364 11.926 1.00 65.00 C ANISOU 1070 CA PRO A 189 8395 8096 8207 430 -674 65 C ATOM 1071 C PRO A 189 -18.865 -6.330 12.691 1.00 69.22 C ANISOU 1071 C PRO A 189 9000 8667 8633 428 -731 119 C ATOM 1072 O PRO A 189 -18.512 -6.049 13.835 1.00 77.20 O ANISOU 1072 O PRO A 189 10060 9712 9560 450 -817 38 O ATOM 1073 CB PRO A 189 -21.238 -5.770 12.092 1.00 64.64 C ANISOU 1073 CB PRO A 189 8382 8142 8037 424 -547 43 C ATOM 1074 CG PRO A 189 -21.871 -5.472 10.782 1.00 65.03 C ANISOU 1074 CG PRO A 189 8356 8137 8214 411 -487 83 C ATOM 1075 CD PRO A 189 -20.812 -5.747 9.760 1.00 69.43 C ANISOU 1075 CD PRO A 189 8881 8614 8886 390 -522 198 C ATOM 1076 N VAL A 190 -18.499 -7.448 12.071 1.00 69.18 N ANISOU 1076 N VAL A 190 9004 8652 8632 406 -693 248 N ATOM 1077 CA VAL A 190 -17.722 -8.482 12.753 1.00 66.14 C ANISOU 1077 CA VAL A 190 8687 8290 8154 409 -749 312 C ATOM 1078 C VAL A 190 -16.376 -7.961 13.273 1.00 72.11 C ANISOU 1078 C VAL A 190 9415 8999 8985 435 -905 276 C ATOM 1079 O VAL A 190 -16.114 -8.024 14.475 1.00 74.65 O ANISOU 1079 O VAL A 190 9809 9369 9184 452 -992 231 O ATOM 1080 CB VAL A 190 -17.506 -9.715 11.847 1.00 61.20 C ANISOU 1080 CB VAL A 190 8060 7635 7560 392 -690 443 C ATOM 1081 CG1 VAL A 190 -16.551 -10.703 12.499 1.00 62.13 C ANISOU 1081 CG1 VAL A 190 8233 7748 7624 408 -775 510 C ATOM 1082 CG2 VAL A 190 -18.838 -10.385 11.546 1.00 61.37 C ANISOU 1082 CG2 VAL A 190 8122 7705 7491 360 -559 477 C ATOM 1083 N PRO A 191 -15.518 -7.447 12.377 1.00 68.40 N ANISOU 1083 N PRO A 191 8837 8439 8712 433 -944 300 N ATOM 1084 CA PRO A 191 -14.217 -6.929 12.821 1.00 70.02 C ANISOU 1084 CA PRO A 191 8992 8593 9019 448 -1096 268 C ATOM 1085 C PRO A 191 -14.327 -5.709 13.733 1.00 62.41 C ANISOU 1085 C PRO A 191 8039 7628 8047 461 -1196 123 C ATOM 1086 O PRO A 191 -13.489 -5.531 14.614 1.00 73.42 O ANISOU 1086 O PRO A 191 9447 9016 9434 478 -1340 73 O ATOM 1087 CB PRO A 191 -13.522 -6.547 11.508 1.00 60.72 C ANISOU 1087 CB PRO A 191 7683 7330 8059 429 -1074 331 C ATOM 1088 CG PRO A 191 -14.622 -6.380 10.519 1.00 75.32 C ANISOU 1088 CG PRO A 191 9524 9183 9911 408 -935 353 C ATOM 1089 CD PRO A 191 -15.658 -7.383 10.913 1.00 70.47 C ANISOU 1089 CD PRO A 191 9019 8652 9106 412 -850 367 C ATOM 1090 N ILE A 192 -15.344 -4.882 13.522 1.00 82.24 N ANISOU 1090 N ILE A 192 10543 10139 10567 458 -1130 47 N ATOM 1091 CA ILE A 192 -15.527 -3.677 14.324 1.00 63.33 C ANISOU 1091 CA ILE A 192 8154 7729 8178 481 -1220 -113 C ATOM 1092 C ILE A 192 -15.920 -4.041 15.751 1.00 81.55 C ANISOU 1092 C ILE A 192 10589 10155 10244 511 -1247 -199 C ATOM 1093 O ILE A 192 -15.363 -3.516 16.715 1.00 84.54 O ANISOU 1093 O ILE A 192 10997 10534 10592 535 -1388 -307 O ATOM 1094 CB ILE A 192 -16.609 -2.764 13.721 1.00 62.93 C ANISOU 1094 CB ILE A 192 8062 7645 8202 483 -1140 -175 C ATOM 1095 CG1 ILE A 192 -16.188 -2.288 12.330 1.00 62.11 C ANISOU 1095 CG1 ILE A 192 7844 7426 8327 448 -1127 -80 C ATOM 1096 CG2 ILE A 192 -16.853 -1.569 14.623 1.00 80.13 C ANISOU 1096 CG2 ILE A 192 10255 9806 10386 520 -1234 -362 C ATOM 1097 CD1 ILE A 192 -17.268 -1.525 11.592 1.00 83.35 C ANISOU 1097 CD1 ILE A 192 10497 10078 11094 448 -1052 -106 C ATOM 1098 N LYS A 193 -16.884 -4.946 15.877 1.00 81.10 N ANISOU 1098 N LYS A 193 10606 10199 10009 504 -1113 -149 N ATOM 1099 CA LYS A 193 -17.347 -5.403 17.180 1.00 84.77 C ANISOU 1099 CA LYS A 193 11196 10795 10218 521 -1107 -201 C ATOM 1100 C LYS A 193 -16.237 -6.174 17.885 1.00 73.35 C ANISOU 1100 C LYS A 193 9815 9364 8692 523 -1234 -132 C ATOM 1101 O LYS A 193 -16.028 -6.023 19.089 1.00 73.22 O ANISOU 1101 O LYS A 193 9885 9417 8520 547 -1332 -216 O ATOM 1102 CB LYS A 193 -18.578 -6.295 17.016 1.00100.33 C ANISOU 1102 CB LYS A 193 13213 12859 12049 495 -927 -127 C ATOM 1103 CG LYS A 193 -19.239 -6.699 18.325 1.00115.50 C ANISOU 1103 CG LYS A 193 15257 14933 13695 500 -885 -172 C ATOM 1104 CD LYS A 193 -20.199 -5.632 18.826 1.00119.97 C ANISOU 1104 CD LYS A 193 15813 15564 14207 536 -832 -358 C ATOM 1105 CE LYS A 193 -21.526 -6.240 19.260 1.00118.51 C ANISOU 1105 CE LYS A 193 15680 15527 13822 514 -655 -344 C ATOM 1106 NZ LYS A 193 -22.274 -6.833 18.114 1.00108.02 N ANISOU 1106 NZ LYS A 193 14282 14164 12597 470 -519 -225 N ATOM 1107 N GLY A 194 -15.527 -6.998 17.121 1.00 71.47 N ANISOU 1107 N GLY A 194 9534 9062 8559 504 -1238 14 N ATOM 1108 CA GLY A 194 -14.435 -7.793 17.651 1.00 68.99 C ANISOU 1108 CA GLY A 194 9261 8743 8208 514 -1365 92 C ATOM 1109 C GLY A 194 -14.920 -8.979 18.459 1.00 76.35 C ANISOU 1109 C GLY A 194 10335 9779 8895 505 -1324 175 C ATOM 1110 O GLY A 194 -16.117 -9.129 18.710 1.00 78.90 O ANISOU 1110 O GLY A 194 10722 10193 9064 486 -1191 161 O ATOM 1111 N ILE A 195 -13.982 -9.825 18.871 1.00 84.79 N ANISOU 1111 N ILE A 195 11447 10832 9936 517 -1442 268 N ATOM 1112 CA ILE A 195 -14.308 -10.999 19.667 1.00 96.24 C ANISOU 1112 CA ILE A 195 13040 12364 11164 504 -1429 374 C ATOM 1113 C ILE A 195 -13.950 -10.776 21.129 1.00105.84 C ANISOU 1113 C ILE A 195 14370 13665 12178 527 -1579 311 C ATOM 1114 O ILE A 195 -12.964 -10.112 21.445 1.00112.38 O ANISOU 1114 O ILE A 195 15157 14451 13091 561 -1752 230 O ATOM 1115 CB ILE A 195 -13.576 -12.241 19.148 1.00101.03 C ANISOU 1115 CB ILE A 195 13633 12887 11867 507 -1465 536 C ATOM 1116 CG1 ILE A 195 -14.131 -12.631 17.779 1.00105.91 C ANISOU 1116 CG1 ILE A 195 14172 13445 12623 481 -1298 595 C ATOM 1117 CG2 ILE A 195 -13.733 -13.397 20.123 1.00107.63 C ANISOU 1117 CG2 ILE A 195 14627 13786 12483 494 -1500 655 C ATOM 1118 CD1 ILE A 195 -13.384 -13.747 17.130 1.00112.76 C ANISOU 1118 CD1 ILE A 195 15009 14219 13615 498 -1328 721 C ATOM 1119 N GLU A 196 -14.764 -11.336 22.018 1.00110.98 N ANISOU 1119 N GLU A 196 15165 14443 12560 503 -1513 352 N ATOM 1120 CA GLU A 196 -14.550 -11.194 23.453 1.00116.24 C ANISOU 1120 CA GLU A 196 15966 15219 12980 522 -1639 299 C ATOM 1121 C GLU A 196 -13.227 -11.834 23.866 1.00117.99 C ANISOU 1121 C GLU A 196 16223 15381 13228 550 -1859 396 C ATOM 1122 O GLU A 196 -13.066 -13.053 23.789 1.00115.56 O ANISOU 1122 O GLU A 196 15966 15042 12900 534 -1862 573 O ATOM 1123 CB GLU A 196 -15.702 -11.839 24.226 1.00120.39 C ANISOU 1123 CB GLU A 196 16636 15900 13206 479 -1497 364 C ATOM 1124 CG GLU A 196 -15.644 -11.612 25.731 1.00126.83 C ANISOU 1124 CG GLU A 196 17606 16864 13719 496 -1597 297 C ATOM 1125 CD GLU A 196 -16.341 -10.336 26.164 1.00132.71 C ANISOU 1125 CD GLU A 196 18343 17713 14370 523 -1531 67 C ATOM 1126 OE1 GLU A 196 -17.330 -9.941 25.511 1.00131.03 O ANISOU 1126 OE1 GLU A 196 18045 17506 14233 508 -1343 8 O ATOM 1127 OE2 GLU A 196 -15.897 -9.728 27.162 1.00139.48 O ANISOU 1127 OE2 GLU A 196 19277 18640 15080 564 -1677 -62 O ATOM 1128 N THR A 197 -12.281 -11.007 24.300 1.00124.76 N ANISOU 1128 N THR A 197 17046 16210 14145 593 -2054 275 N ATOM 1129 CA THR A 197 -10.975 -11.494 24.732 1.00129.67 C ANISOU 1129 CA THR A 197 17683 16775 14812 626 -2288 347 C ATOM 1130 C THR A 197 -10.956 -11.741 26.237 1.00141.10 C ANISOU 1130 C THR A 197 19323 18356 15934 636 -2418 350 C ATOM 1131 O THR A 197 -10.857 -10.804 27.030 1.00148.33 O ANISOU 1131 O THR A 197 20281 19341 16737 660 -2521 184 O ATOM 1132 CB THR A 197 -9.857 -10.497 24.375 1.00120.97 C ANISOU 1132 CB THR A 197 16425 15563 13976 660 -2451 224 C ATOM 1133 N VAL A 199 -7.810 -14.473 28.600 1.00144.91 N ANISOU 1133 N VAL A 199 20083 18772 16204 736 -3181 767 N ATOM 1134 CA VAL A 199 -6.424 -14.873 28.786 1.00147.96 C ANISOU 1134 CA VAL A 199 20420 19055 16745 794 -3459 829 C ATOM 1135 C VAL A 199 -6.028 -14.805 30.257 1.00159.88 C ANISOU 1135 C VAL A 199 22106 20674 17967 817 -3707 815 C ATOM 1136 O VAL A 199 -6.206 -13.780 30.918 1.00157.15 O ANISOU 1136 O VAL A 199 21812 20435 17464 817 -3753 634 O ATOM 1137 CB VAL A 199 -5.469 -13.971 27.983 1.00137.50 C ANISOU 1137 CB VAL A 199 18854 17607 15783 828 -3542 687 C ATOM 1138 CG1 VAL A 199 -4.012 -14.356 28.238 1.00140.98 C ANISOU 1138 CG1 VAL A 199 19223 17949 16392 891 -3838 740 C ATOM 1139 CG2 VAL A 199 -5.789 -14.051 26.504 1.00122.01 C ANISOU 1139 CG2 VAL A 199 16723 15544 14090 808 -3306 709 C ATOM 1140 N ASP A 200 -5.462 -15.897 30.761 1.00171.95 N ANISOU 1140 N ASP A 200 23730 22169 19433 841 -3882 1003 N ATOM 1141 CA ASP A 200 -4.956 -15.947 32.135 1.00182.42 C ANISOU 1141 CA ASP A 200 25230 23590 20493 869 -4155 1017 C ATOM 1142 C ASP A 200 -3.453 -16.211 32.082 1.00185.77 C ANISOU 1142 C ASP A 200 25532 23869 21185 942 -4462 1053 C ATOM 1143 O ASP A 200 -2.652 -15.276 32.063 1.00184.98 O ANISOU 1143 O ASP A 200 25296 23731 21257 977 -4622 880 O ATOM 1144 CB ASP A 200 -5.662 -17.024 32.972 1.00187.78 C ANISOU 1144 CB ASP A 200 26161 24376 20810 828 -4116 1232 C ATOM 1145 CG ASP A 200 -5.052 -17.178 34.353 1.00192.38 C ANISOU 1145 CG ASP A 200 26932 25051 21114 859 -4419 1276 C ATOM 1146 OD1 ASP A 200 -5.485 -16.459 35.275 1.00194.19 O ANISOU 1146 OD1 ASP A 200 27302 25462 21020 844 -4429 1147 O ATOM 1147 OD2 ASP A 200 -4.145 -18.017 34.511 1.00194.37 O ANISOU 1147 OD2 ASP A 200 27190 25194 21468 904 -4652 1434 O ATOM 1148 N ASN A 201 -3.075 -17.487 32.039 1.00189.35 N ANISOU 1148 N ASN A 201 26022 24230 21694 967 -4547 1276 N ATOM 1149 CA ASN A 201 -1.680 -17.866 31.810 1.00189.23 C ANISOU 1149 CA ASN A 201 25855 24057 21988 1047 -4809 1320 C ATOM 1150 C ASN A 201 -1.464 -18.249 30.341 1.00195.50 C ANISOU 1150 C ASN A 201 26417 24684 23181 1066 -4644 1351 C ATOM 1151 O ASN A 201 -0.577 -17.703 29.684 1.00196.03 O ANISOU 1151 O ASN A 201 26250 24656 23576 1107 -4711 1238 O ATOM 1152 CB ASN A 201 -1.250 -18.989 32.764 1.00180.27 C ANISOU 1152 CB ASN A 201 24900 22914 20679 1082 -5059 1533 C ATOM 1153 CG ASN A 201 0.215 -19.356 32.617 1.00171.10 C ANISOU 1153 CG ASN A 201 23576 21593 19841 1178 -5356 1568 C ATOM 1154 OD1 ASN A 201 0.796 -19.239 31.537 1.00167.21 O ANISOU 1154 OD1 ASN A 201 22828 20967 19739 1214 -5303 1506 O ATOM 1155 ND2 ASN A 201 0.820 -19.805 33.711 1.00170.15 N ANISOU 1155 ND2 ASN A 201 23599 21494 19555 1220 -5671 1670 N ATOM 1156 N PRO A 202 -2.272 -19.189 29.817 1.00199.03 N ANISOU 1156 N PRO A 202 26925 25097 23599 1032 -4427 1501 N ATOM 1157 CA PRO A 202 -2.267 -19.421 28.371 1.00195.47 C ANISOU 1157 CA PRO A 202 26272 24516 23484 1042 -4227 1495 C ATOM 1158 C PRO A 202 -3.386 -18.643 27.683 1.00191.15 C ANISOU 1158 C PRO A 202 25691 24043 22895 968 -3912 1376 C ATOM 1159 O PRO A 202 -3.989 -17.761 28.296 1.00187.53 O ANISOU 1159 O PRO A 202 25325 23724 22205 923 -3870 1264 O ATOM 1160 CB PRO A 202 -2.549 -20.916 28.274 1.00196.66 C ANISOU 1160 CB PRO A 202 26529 24581 23613 1047 -4197 1722 C ATOM 1161 CG PRO A 202 -3.485 -21.157 29.404 1.00199.94 C ANISOU 1161 CG PRO A 202 27220 25141 23606 978 -4181 1824 C ATOM 1162 CD PRO A 202 -3.036 -20.238 30.519 1.00202.58 C ANISOU 1162 CD PRO A 202 27625 25602 23745 991 -4397 1709 C ATOM 1163 N ASN A 203 -3.654 -18.972 26.423 1.00190.90 N ANISOU 1163 N ASN A 203 25529 23919 23088 962 -3702 1395 N ATOM 1164 CA ASN A 203 -4.768 -18.380 25.691 1.00187.27 C ANISOU 1164 CA ASN A 203 25040 23515 22598 894 -3406 1308 C ATOM 1165 C ASN A 203 -5.802 -19.433 25.306 1.00182.92 C ANISOU 1165 C ASN A 203 24592 22948 21961 847 -3204 1456 C ATOM 1166 O ASN A 203 -5.596 -20.206 24.369 1.00180.96 O ANISOU 1166 O ASN A 203 24251 22572 21933 874 -3143 1525 O ATOM 1167 CB ASN A 203 -4.265 -17.673 24.434 1.00185.05 C ANISOU 1167 CB ASN A 203 24506 23151 22653 915 -3319 1182 C ATOM 1168 CG ASN A 203 -5.396 -17.176 23.557 1.00183.61 C ANISOU 1168 CG ASN A 203 24291 23008 22465 851 -3024 1116 C ATOM 1169 OD1 ASN A 203 -6.435 -16.737 24.052 1.00182.74 O ANISOU 1169 OD1 ASN A 203 24308 23016 22111 794 -2917 1074 O ATOM 1170 ND2 ASN A 203 -5.206 -17.254 22.245 1.00183.61 N ANISOU 1170 ND2 ASN A 203 24120 22915 22730 865 -2893 1103 N ATOM 1171 N ASN A 204 -6.915 -19.456 26.033 1.00179.17 N ANISOU 1171 N ASN A 204 24305 22605 21169 775 -3101 1496 N ATOM 1172 CA ASN A 204 -7.990 -20.406 25.769 1.00170.98 C ANISOU 1172 CA ASN A 204 23367 21562 20034 711 -2909 1638 C ATOM 1173 C ASN A 204 -9.166 -19.726 25.076 1.00158.78 C ANISOU 1173 C ASN A 204 21772 20090 18469 646 -2627 1531 C ATOM 1174 O ASN A 204 -10.288 -19.738 25.581 1.00153.87 O ANISOU 1174 O ASN A 204 21279 19590 17595 574 -2488 1561 O ATOM 1175 CB ASN A 204 -8.453 -21.067 27.070 1.00175.31 C ANISOU 1175 CB ASN A 204 24159 22208 20243 666 -2980 1796 C ATOM 1176 CG ASN A 204 -8.883 -20.058 28.120 1.00178.19 C ANISOU 1176 CG ASN A 204 24631 22772 20300 635 -2985 1681 C ATOM 1177 OD1 ASN A 204 -8.404 -18.924 28.141 1.00178.52 O ANISOU 1177 OD1 ASN A 204 24577 22847 20403 674 -3054 1492 O ATOM 1178 ND2 ASN A 204 -9.788 -20.469 29.001 1.00179.64 N ANISOU 1178 ND2 ASN A 204 25013 23087 20153 564 -2909 1794 N ATOM 1179 N ILE A 205 -8.897 -19.134 23.915 1.00153.34 N ANISOU 1179 N ILE A 205 20888 19328 18047 673 -2545 1410 N ATOM 1180 CA ILE A 205 -9.917 -18.409 23.163 1.00139.45 C ANISOU 1180 CA ILE A 205 19063 17621 16302 622 -2302 1302 C ATOM 1181 C ILE A 205 -10.460 -19.237 22.003 1.00129.83 C ANISOU 1181 C ILE A 205 17792 16308 15228 598 -2128 1382 C ATOM 1182 O ILE A 205 -9.696 -19.783 21.205 1.00129.05 O ANISOU 1182 O ILE A 205 17590 16077 15366 650 -2174 1416 O ATOM 1183 CB ILE A 205 -9.362 -17.085 22.603 1.00126.65 C ANISOU 1183 CB ILE A 205 17267 15986 14867 656 -2318 1117 C ATOM 1184 N THR A 206 -11.784 -19.322 21.917 1.00119.31 N ANISOU 1184 N THR A 206 16526 15049 13756 522 -1930 1401 N ATOM 1185 CA THR A 206 -12.440 -20.050 20.837 1.00111.08 C ANISOU 1185 CA THR A 206 15442 13927 12836 488 -1764 1462 C ATOM 1186 C THR A 206 -12.953 -19.086 19.770 1.00 97.65 C ANISOU 1186 C THR A 206 13602 12243 11256 477 -1597 1318 C ATOM 1187 O THR A 206 -13.562 -18.062 20.079 1.00 97.34 O ANISOU 1187 O THR A 206 13562 12316 11106 451 -1525 1209 O ATOM 1188 CB THR A 206 -13.609 -20.926 21.351 1.00115.37 C ANISOU 1188 CB THR A 206 16138 14523 13173 400 -1657 1602 C ATOM 1189 OG1 THR A 206 -14.302 -21.500 20.236 1.00117.76 O ANISOU 1189 OG1 THR A 206 16385 14746 13611 363 -1500 1632 O ATOM 1190 CG2 THR A 206 -14.597 -20.112 22.183 1.00114.10 C ANISOU 1190 CG2 THR A 206 16052 14548 12753 341 -1552 1536 C ATOM 1191 N CYS A 207 -12.711 -19.428 18.510 1.00 84.13 N ANISOU 1191 N CYS A 207 11776 10418 9770 501 -1539 1316 N ATOM 1192 CA CYS A 207 -13.047 -18.549 17.400 1.00 77.47 C ANISOU 1192 CA CYS A 207 10799 9579 9056 497 -1402 1197 C ATOM 1193 C CYS A 207 -14.483 -18.798 16.940 1.00 75.45 C ANISOU 1193 C CYS A 207 10578 9360 8729 423 -1209 1217 C ATOM 1194 O CYS A 207 -14.731 -19.624 16.059 1.00 71.57 O ANISOU 1194 O CYS A 207 10067 8787 8340 413 -1139 1271 O ATOM 1195 CB CYS A 207 -12.065 -18.778 16.248 1.00 79.26 C ANISOU 1195 CB CYS A 207 10887 9686 9542 559 -1428 1183 C ATOM 1196 SG CYS A 207 -12.061 -17.500 14.972 1.00 89.35 S ANISOU 1196 SG CYS A 207 11991 10970 10987 563 -1310 1047 S ATOM 1197 N VAL A 208 -15.426 -18.090 17.556 1.00 76.92 N ANISOU 1197 N VAL A 208 10811 9670 8744 374 -1129 1162 N ATOM 1198 CA VAL A 208 -16.845 -18.252 17.240 1.00 75.21 C ANISOU 1198 CA VAL A 208 10614 9505 8457 302 -949 1175 C ATOM 1199 C VAL A 208 -17.669 -17.039 17.671 1.00 73.65 C ANISOU 1199 C VAL A 208 10403 9440 8142 280 -864 1051 C ATOM 1200 O VAL A 208 -17.380 -16.410 18.688 1.00 84.04 O ANISOU 1200 O VAL A 208 11766 10835 9328 301 -942 993 O ATOM 1201 CB VAL A 208 -17.424 -19.506 17.929 1.00 72.19 C ANISOU 1201 CB VAL A 208 10369 9134 7927 238 -931 1332 C ATOM 1202 CG1 VAL A 208 -17.394 -19.345 19.447 1.00 78.80 C ANISOU 1202 CG1 VAL A 208 11330 10090 8521 225 -1002 1361 C ATOM 1203 CG2 VAL A 208 -18.840 -19.788 17.441 1.00 69.52 C ANISOU 1203 CG2 VAL A 208 10022 8826 7565 157 -748 1353 C ATOM 1204 N LEU A 209 -18.701 -16.722 16.894 1.00 68.52 N ANISOU 1204 N LEU A 209 9687 8808 7540 245 -712 1002 N ATOM 1205 CA LEU A 209 -19.600 -15.622 17.223 1.00 68.25 C ANISOU 1205 CA LEU A 209 9627 8888 7417 232 -620 880 C ATOM 1206 C LEU A 209 -20.597 -16.083 18.279 1.00 72.02 C ANISOU 1206 C LEU A 209 10211 9493 7662 169 -534 935 C ATOM 1207 O LEU A 209 -21.216 -17.135 18.141 1.00 74.76 O ANISOU 1207 O LEU A 209 10597 9826 7982 105 -458 1058 O ATOM 1208 CB LEU A 209 -20.334 -15.133 15.970 1.00 69.82 C ANISOU 1208 CB LEU A 209 9709 9054 7767 222 -503 816 C ATOM 1209 CG LEU A 209 -19.450 -14.573 14.852 1.00 61.82 C ANISOU 1209 CG LEU A 209 8586 7933 6968 274 -562 767 C ATOM 1210 CD1 LEU A 209 -20.304 -14.158 13.667 1.00 73.10 C ANISOU 1210 CD1 LEU A 209 9922 9343 8508 257 -447 724 C ATOM 1211 CD2 LEU A 209 -18.615 -13.400 15.347 1.00 67.63 C ANISOU 1211 CD2 LEU A 209 9290 8679 7728 327 -673 660 C ATOM 1212 N THR A 210 -20.746 -15.292 19.335 1.00 81.73 N ANISOU 1212 N THR A 210 11484 10847 8723 185 -544 842 N ATOM 1213 CA THR A 210 -21.605 -15.665 20.451 1.00 86.81 C ANISOU 1213 CA THR A 210 12232 11639 9113 129 -455 890 C ATOM 1214 C THR A 210 -22.994 -15.045 20.319 1.00 89.85 C ANISOU 1214 C THR A 210 12545 12128 9466 99 -270 790 C ATOM 1215 O THR A 210 -23.148 -13.943 19.792 1.00 93.26 O ANISOU 1215 O THR A 210 12872 12546 10016 148 -253 636 O ATOM 1216 CB THR A 210 -20.989 -15.220 21.788 1.00 86.26 C ANISOU 1216 CB THR A 210 12268 11670 8839 168 -571 838 C ATOM 1217 OG1 THR A 210 -21.003 -13.789 21.868 1.00 87.60 O ANISOU 1217 OG1 THR A 210 12368 11883 9032 229 -581 628 O ATOM 1218 CG2 THR A 210 -19.550 -15.726 21.917 1.00 71.04 C ANISOU 1218 CG2 THR A 210 10391 9633 6967 208 -779 922 C ATOM 1219 N LYS A 211 -24.000 -15.769 20.800 1.00 86.32 N ANISOU 1219 N LYS A 211 12148 11780 8868 18 -135 887 N ATOM 1220 CA LYS A 211 -25.381 -15.302 20.779 1.00 82.76 C ANISOU 1220 CA LYS A 211 11620 11444 8380 -15 52 803 C ATOM 1221 C LYS A 211 -25.552 -14.055 21.650 1.00 87.26 C ANISOU 1221 C LYS A 211 12190 12156 8809 48 69 611 C ATOM 1222 O LYS A 211 -26.502 -13.290 21.476 1.00 85.18 O ANISOU 1222 O LYS A 211 11826 11961 8576 63 192 478 O ATOM 1223 CB LYS A 211 -26.310 -16.423 21.256 1.00 80.10 C ANISOU 1223 CB LYS A 211 11340 11191 7901 -127 187 967 C ATOM 1224 CG LYS A 211 -27.757 -16.004 21.453 1.00 72.41 C ANISOU 1224 CG LYS A 211 10283 10369 6860 -167 392 888 C ATOM 1225 N GLU A 212 -24.615 -13.843 22.571 1.00 93.30 N ANISOU 1225 N GLU A 212 13063 12957 9431 93 -66 586 N ATOM 1226 CA GLU A 212 -24.681 -12.709 23.491 1.00 95.92 C ANISOU 1226 CA GLU A 212 13416 13420 9609 158 -73 391 C ATOM 1227 C GLU A 212 -24.078 -11.449 22.877 1.00 87.93 C ANISOU 1227 C GLU A 212 12304 12297 8807 250 -186 207 C ATOM 1228 O GLU A 212 -24.500 -10.333 23.185 1.00 93.04 O ANISOU 1228 O GLU A 212 12907 13015 9431 306 -151 10 O ATOM 1229 CB GLU A 212 -23.960 -13.037 24.805 1.00103.49 C ANISOU 1229 CB GLU A 212 14546 14474 10301 162 -184 441 C ATOM 1230 CG GLU A 212 -24.667 -14.075 25.657 1.00113.63 C ANISOU 1230 CG GLU A 212 15943 15908 11322 69 -58 608 C ATOM 1231 CD GLU A 212 -24.368 -15.495 25.219 1.00117.44 C ANISOU 1231 CD GLU A 212 16473 16269 11881 -9 -95 866 C ATOM 1232 OE1 GLU A 212 -23.196 -15.787 24.899 1.00117.04 O ANISOU 1232 OE1 GLU A 212 16449 16068 11953 28 -284 925 O ATOM 1233 OE2 GLU A 212 -25.308 -16.320 25.192 1.00118.29 O ANISOU 1233 OE2 GLU A 212 16583 16425 11938 -106 62 1003 O ATOM 1234 N ARG A 213 -23.089 -11.634 22.010 1.00 80.72 N ANISOU 1234 N ARG A 213 11354 11209 8105 265 -319 273 N ATOM 1235 CA ARG A 213 -22.352 -10.518 21.432 1.00 77.22 C ANISOU 1235 CA ARG A 213 10822 10650 7868 337 -441 134 C ATOM 1236 C ARG A 213 -22.798 -10.217 20.002 1.00 79.56 C ANISOU 1236 C ARG A 213 10974 10833 8422 333 -369 125 C ATOM 1237 O ARG A 213 -22.654 -9.090 19.524 1.00 78.59 O ANISOU 1237 O ARG A 213 10761 10643 8457 384 -413 -9 O ATOM 1238 CB ARG A 213 -20.859 -10.834 21.437 1.00 80.72 C ANISOU 1238 CB ARG A 213 11306 10985 8378 359 -640 208 C ATOM 1239 CG ARG A 213 -19.972 -9.614 21.478 1.00 81.97 C ANISOU 1239 CG ARG A 213 11414 11077 8655 428 -796 48 C ATOM 1240 CD ARG A 213 -18.503 -10.007 21.469 1.00 79.47 C ANISOU 1240 CD ARG A 213 11117 10658 8420 444 -988 131 C ATOM 1241 NE ARG A 213 -17.627 -8.857 21.276 1.00 77.19 N ANISOU 1241 NE ARG A 213 10746 10277 8305 494 -1133 -3 N ATOM 1242 CZ ARG A 213 -17.369 -7.942 22.205 1.00 95.15 C ANISOU 1242 CZ ARG A 213 13060 12602 10492 536 -1242 -166 C ATOM 1243 NH1 ARG A 213 -17.924 -8.024 23.408 1.00100.03 N ANISOU 1243 NH1 ARG A 213 13805 13379 10824 542 -1212 -221 N ATOM 1244 NH2 ARG A 213 -16.557 -6.934 21.926 1.00103.63 N ANISOU 1244 NH2 ARG A 213 14047 13567 11763 570 -1379 -274 N ATOM 1245 N PHE A 214 -23.330 -11.229 19.321 1.00 77.97 N ANISOU 1245 N PHE A 214 10756 10606 8264 270 -269 271 N ATOM 1246 CA PHE A 214 -23.651 -11.114 17.902 1.00 74.59 C ANISOU 1246 CA PHE A 214 10208 10067 8065 263 -221 285 C ATOM 1247 C PHE A 214 -25.046 -11.634 17.547 1.00 73.94 C ANISOU 1247 C PHE A 214 10084 10043 7965 202 -48 331 C ATOM 1248 O PHE A 214 -25.319 -11.939 16.388 1.00 74.01 O ANISOU 1248 O PHE A 214 10022 9965 8134 179 -14 387 O ATOM 1249 CB PHE A 214 -22.592 -11.850 17.077 1.00 72.76 C ANISOU 1249 CB PHE A 214 9976 9696 7973 257 -318 412 C ATOM 1250 CG PHE A 214 -21.264 -11.148 17.039 1.00 71.19 C ANISOU 1250 CG PHE A 214 9757 9415 7877 316 -479 355 C ATOM 1251 CD1 PHE A 214 -21.040 -10.116 16.143 1.00 66.82 C ANISOU 1251 CD1 PHE A 214 9092 8775 7520 350 -507 269 C ATOM 1252 CD2 PHE A 214 -20.244 -11.514 17.901 1.00 73.24 C ANISOU 1252 CD2 PHE A 214 10104 9680 8044 333 -610 394 C ATOM 1253 CE1 PHE A 214 -19.824 -9.464 16.105 1.00 69.81 C ANISOU 1253 CE1 PHE A 214 9439 9076 8011 391 -651 225 C ATOM 1254 CE2 PHE A 214 -19.023 -10.864 17.867 1.00 75.68 C ANISOU 1254 CE2 PHE A 214 10376 9913 8468 382 -764 339 C ATOM 1255 CZ PHE A 214 -18.814 -9.838 16.967 1.00 73.67 C ANISOU 1255 CZ PHE A 214 10002 9573 8418 407 -779 255 C ATOM 1256 N GLY A 215 -25.929 -11.723 18.536 1.00 79.04 N ANISOU 1256 N GLY A 215 10770 10843 8418 175 62 305 N ATOM 1257 CA GLY A 215 -27.283 -12.196 18.300 1.00 77.14 C ANISOU 1257 CA GLY A 215 10474 10670 8166 110 232 347 C ATOM 1258 C GLY A 215 -28.020 -11.345 17.279 1.00 74.77 C ANISOU 1258 C GLY A 215 10027 10322 8062 142 281 238 C ATOM 1259 O GLY A 215 -28.682 -11.868 16.382 1.00 68.87 O ANISOU 1259 O GLY A 215 9213 9529 7427 93 345 309 O ATOM 1260 N ASP A 216 -27.905 -10.027 17.419 1.00 88.46 N ANISOU 1260 N ASP A 216 11712 12057 9842 225 236 64 N ATOM 1261 CA ASP A 216 -28.512 -9.093 16.473 1.00 96.99 C ANISOU 1261 CA ASP A 216 12658 13074 11121 267 253 -40 C ATOM 1262 C ASP A 216 -27.911 -9.258 15.081 1.00 84.37 C ANISOU 1262 C ASP A 216 11021 11310 9726 259 167 49 C ATOM 1263 O ASP A 216 -28.631 -9.475 14.107 1.00 73.84 O ANISOU 1263 O ASP A 216 9611 9938 8509 231 221 90 O ATOM 1264 CB ASP A 216 -28.314 -7.647 16.936 1.00112.14 C ANISOU 1264 CB ASP A 216 14547 14995 13064 361 190 -238 C ATOM 1265 CG ASP A 216 -29.153 -7.296 18.148 1.00123.22 C ANISOU 1265 CG ASP A 216 15959 16573 14285 386 300 -371 C ATOM 1266 OD1 ASP A 216 -30.113 -8.035 18.451 1.00122.22 O ANISOU 1266 OD1 ASP A 216 15822 16568 14048 327 452 -312 O ATOM 1267 OD2 ASP A 216 -28.855 -6.267 18.791 1.00132.64 O ANISOU 1267 OD2 ASP A 216 17164 17783 15449 464 237 -542 O ATOM 1268 N PHE A 217 -26.589 -9.141 14.993 1.00 81.80 N ANISOU 1268 N PHE A 217 10746 10895 9439 286 33 75 N ATOM 1269 CA PHE A 217 -25.895 -9.301 13.721 1.00 72.31 C ANISOU 1269 CA PHE A 217 9510 9553 8411 282 -38 157 C ATOM 1270 C PHE A 217 -26.309 -10.593 13.033 1.00 69.80 C ANISOU 1270 C PHE A 217 9202 9219 8100 213 29 299 C ATOM 1271 O PHE A 217 -26.468 -10.639 11.816 1.00 78.13 O ANISOU 1271 O PHE A 217 10197 10196 9293 205 31 334 O ATOM 1272 CB PHE A 217 -24.380 -9.300 13.918 1.00 63.98 C ANISOU 1272 CB PHE A 217 8510 8431 7370 306 -174 188 C ATOM 1273 CG PHE A 217 -23.625 -9.772 12.714 1.00 66.59 C ANISOU 1273 CG PHE A 217 8814 8644 7842 294 -220 293 C ATOM 1274 CD1 PHE A 217 -23.569 -8.993 11.572 1.00 68.53 C ANISOU 1274 CD1 PHE A 217 8970 8805 8261 314 -239 269 C ATOM 1275 CD2 PHE A 217 -22.987 -10.999 12.716 1.00 72.29 C ANISOU 1275 CD2 PHE A 217 9603 9343 8521 267 -242 416 C ATOM 1276 CE1 PHE A 217 -22.883 -9.428 10.456 1.00 67.03 C ANISOU 1276 CE1 PHE A 217 8759 8530 8180 304 -264 361 C ATOM 1277 CE2 PHE A 217 -22.296 -11.438 11.602 1.00 67.37 C ANISOU 1277 CE2 PHE A 217 8950 8622 8025 267 -273 493 C ATOM 1278 CZ PHE A 217 -22.245 -10.651 10.471 1.00 62.27 C ANISOU 1278 CZ PHE A 217 8216 7913 7531 285 -276 463 C ATOM 1279 N MET A 218 -26.484 -11.645 13.821 1.00 70.71 N ANISOU 1279 N MET A 218 9399 9405 8062 162 77 382 N ATOM 1280 CA MET A 218 -26.870 -12.942 13.285 1.00 78.37 C ANISOU 1280 CA MET A 218 10388 10347 9044 90 129 516 C ATOM 1281 C MET A 218 -28.283 -12.869 12.714 1.00 78.32 C ANISOU 1281 C MET A 218 10287 10374 9097 54 239 489 C ATOM 1282 O MET A 218 -28.577 -13.461 11.675 1.00 75.02 O ANISOU 1282 O MET A 218 9836 9885 8781 19 248 551 O ATOM 1283 CB MET A 218 -26.800 -14.008 14.382 1.00 84.65 C ANISOU 1283 CB MET A 218 11295 11207 9661 36 151 620 C ATOM 1284 CG MET A 218 -26.351 -15.376 13.900 1.00 98.88 C ANISOU 1284 CG MET A 218 13156 12912 11501 -11 114 772 C ATOM 1285 SD MET A 218 -24.779 -15.347 13.008 1.00 77.19 S ANISOU 1285 SD MET A 218 10411 10017 8902 59 -32 784 S ATOM 1286 CE MET A 218 -23.843 -14.164 13.977 1.00 78.42 C ANISOU 1286 CE MET A 218 10584 10219 8993 133 -127 681 C ATOM 1287 N LEU A 219 -29.152 -12.136 13.402 1.00 82.59 N ANISOU 1287 N LEU A 219 10779 11026 9577 68 318 385 N ATOM 1288 CA LEU A 219 -30.539 -11.975 12.977 1.00 83.28 C ANISOU 1288 CA LEU A 219 10756 11158 9730 42 422 344 C ATOM 1289 C LEU A 219 -30.668 -11.036 11.777 1.00 71.77 C ANISOU 1289 C LEU A 219 9197 9608 8462 97 367 270 C ATOM 1290 O LEU A 219 -31.170 -11.427 10.725 1.00 68.55 O ANISOU 1290 O LEU A 219 8738 9146 8163 64 373 319 O ATOM 1291 CB LEU A 219 -31.382 -11.442 14.136 1.00 86.01 C ANISOU 1291 CB LEU A 219 11070 11659 9951 54 531 240 C ATOM 1292 CG LEU A 219 -32.868 -11.242 13.835 1.00 94.32 C ANISOU 1292 CG LEU A 219 11985 12776 11078 33 648 185 C ATOM 1293 CD1 LEU A 219 -33.538 -12.574 13.532 1.00100.99 C ANISOU 1293 CD1 LEU A 219 12822 13626 11923 -81 723 330 C ATOM 1294 CD2 LEU A 219 -33.558 -10.536 14.993 1.00 94.95 C ANISOU 1294 CD2 LEU A 219 12023 13014 11038 70 756 50 C ATOM 1295 N PHE A 220 -30.222 -9.796 11.947 1.00 68.40 N ANISOU 1295 N PHE A 220 8749 9163 8075 179 303 154 N ATOM 1296 CA PHE A 220 -30.315 -8.790 10.893 1.00 69.85 C ANISOU 1296 CA PHE A 220 8845 9255 8439 231 241 93 C ATOM 1297 C PHE A 220 -29.342 -9.073 9.752 1.00 71.44 C ANISOU 1297 C PHE A 220 9077 9332 8734 224 149 192 C ATOM 1298 O PHE A 220 -29.625 -8.766 8.594 1.00 63.12 O ANISOU 1298 O PHE A 220 7964 8211 7809 230 121 205 O ATOM 1299 CB PHE A 220 -30.047 -7.401 11.472 1.00 71.23 C ANISOU 1299 CB PHE A 220 8997 9428 8640 315 189 -54 C ATOM 1300 CG PHE A 220 -31.037 -6.983 12.520 1.00 89.43 C ANISOU 1300 CG PHE A 220 11259 11860 10859 342 286 -183 C ATOM 1301 CD1 PHE A 220 -32.390 -7.224 12.346 1.00 91.31 C ANISOU 1301 CD1 PHE A 220 11404 12169 11122 316 397 -196 C ATOM 1302 CD2 PHE A 220 -30.616 -6.361 13.683 1.00101.43 C ANISOU 1302 CD2 PHE A 220 12827 13438 12273 394 267 -299 C ATOM 1303 CE1 PHE A 220 -33.305 -6.845 13.307 1.00 95.00 C ANISOU 1303 CE1 PHE A 220 11816 12768 11511 344 505 -321 C ATOM 1304 CE2 PHE A 220 -31.528 -5.981 14.650 1.00105.77 C ANISOU 1304 CE2 PHE A 220 13339 14122 12727 426 370 -433 C ATOM 1305 CZ PHE A 220 -32.874 -6.223 14.461 1.00103.44 C ANISOU 1305 CZ PHE A 220 12941 13903 12460 402 498 -442 C ATOM 1306 N GLY A 221 -28.191 -9.647 10.084 1.00 70.19 N ANISOU 1306 N GLY A 221 9011 9150 8508 214 100 259 N ATOM 1307 CA GLY A 221 -27.233 -10.051 9.073 1.00 68.37 C ANISOU 1307 CA GLY A 221 8804 8819 8355 209 32 349 C ATOM 1308 C GLY A 221 -27.815 -11.131 8.181 1.00 70.53 C ANISOU 1308 C GLY A 221 9076 9074 8649 154 78 436 C ATOM 1309 O GLY A 221 -27.632 -11.112 6.963 1.00 72.47 O ANISOU 1309 O GLY A 221 9296 9250 8989 158 46 469 O ATOM 1310 N SER A 222 -28.520 -12.079 8.791 1.00 70.47 N ANISOU 1310 N SER A 222 9097 9129 8547 97 152 474 N ATOM 1311 CA SER A 222 -29.211 -13.123 8.043 1.00 73.83 C ANISOU 1311 CA SER A 222 9515 9533 9003 34 190 546 C ATOM 1312 C SER A 222 -30.282 -12.510 7.148 1.00 73.33 C ANISOU 1312 C SER A 222 9348 9469 9045 38 208 492 C ATOM 1313 O SER A 222 -30.407 -12.873 5.979 1.00 72.17 O ANISOU 1313 O SER A 222 9189 9262 8971 23 178 528 O ATOM 1314 CB SER A 222 -29.845 -14.135 8.999 1.00 69.01 C ANISOU 1314 CB SER A 222 8944 8992 8283 -39 270 602 C ATOM 1315 OG SER A 222 -28.858 -14.814 9.758 1.00 75.44 O ANISOU 1315 OG SER A 222 9866 9795 9002 -45 235 672 O ATOM 1316 N LEU A 223 -31.054 -11.583 7.709 1.00 76.09 N ANISOU 1316 N LEU A 223 9625 9887 9399 64 249 400 N ATOM 1317 CA LEU A 223 -32.080 -10.871 6.955 1.00 77.21 C ANISOU 1317 CA LEU A 223 9656 10025 9656 82 250 340 C ATOM 1318 C LEU A 223 -31.472 -10.096 5.790 1.00 69.67 C ANISOU 1318 C LEU A 223 8689 8974 8808 134 151 340 C ATOM 1319 O LEU A 223 -32.082 -9.974 4.730 1.00 68.26 O ANISOU 1319 O LEU A 223 8458 8762 8718 130 122 349 O ATOM 1320 CB LEU A 223 -32.841 -9.907 7.870 1.00 81.39 C ANISOU 1320 CB LEU A 223 10107 10639 10179 124 305 221 C ATOM 1321 CG LEU A 223 -33.838 -10.527 8.853 1.00 92.00 C ANISOU 1321 CG LEU A 223 11420 12106 11431 68 432 212 C ATOM 1322 CD1 LEU A 223 -34.385 -9.462 9.789 1.00 95.41 C ANISOU 1322 CD1 LEU A 223 11781 12628 11843 131 488 70 C ATOM 1323 CD2 LEU A 223 -34.973 -11.219 8.118 1.00 85.94 C ANISOU 1323 CD2 LEU A 223 10572 11341 10742 1 471 256 C ATOM 1324 N ALA A 224 -30.265 -9.579 5.990 1.00 70.86 N ANISOU 1324 N ALA A 224 8890 9083 8949 176 94 338 N ATOM 1325 CA ALA A 224 -29.619 -8.729 4.996 1.00 68.82 C ANISOU 1325 CA ALA A 224 8617 8740 8792 217 10 348 C ATOM 1326 C ALA A 224 -28.927 -9.534 3.897 1.00 69.38 C ANISOU 1326 C ALA A 224 8739 8758 8863 191 -16 447 C ATOM 1327 O ALA A 224 -28.913 -9.128 2.735 1.00 72.34 O ANISOU 1327 O ALA A 224 9091 9086 9308 202 -59 475 O ATOM 1328 CB ALA A 224 -28.615 -7.805 5.673 1.00 66.77 C ANISOU 1328 CB ALA A 224 8374 8455 8542 265 -41 302 C ATOM 1329 N ALA A 225 -28.360 -10.677 4.266 1.00 63.08 N ANISOU 1329 N ALA A 225 8015 7969 7984 160 9 499 N ATOM 1330 CA ALA A 225 -27.508 -11.431 3.354 1.00 65.52 C ANISOU 1330 CA ALA A 225 8373 8226 8294 153 -15 571 C ATOM 1331 C ALA A 225 -28.250 -12.507 2.561 1.00 71.49 C ANISOU 1331 C ALA A 225 9144 8977 9042 107 7 605 C ATOM 1332 O ALA A 225 -27.795 -12.912 1.490 1.00 72.10 O ANISOU 1332 O ALA A 225 9248 9015 9133 112 -16 639 O ATOM 1333 CB ALA A 225 -26.357 -12.057 4.124 1.00 65.01 C ANISOU 1333 CB ALA A 225 8376 8153 8172 159 -23 603 C ATOM 1334 N PHE A 226 -29.383 -12.973 3.076 1.00 68.72 N ANISOU 1334 N PHE A 226 8772 8668 8670 61 52 590 N ATOM 1335 CA PHE A 226 -30.065 -14.108 2.464 1.00 65.14 C ANISOU 1335 CA PHE A 226 8332 8198 8219 6 63 621 C ATOM 1336 C PHE A 226 -31.519 -13.831 2.079 1.00 65.52 C ANISOU 1336 C PHE A 226 8293 8277 8325 -23 73 584 C ATOM 1337 O PHE A 226 -31.911 -14.033 0.929 1.00 67.74 O ANISOU 1337 O PHE A 226 8562 8527 8647 -32 30 588 O ATOM 1338 CB PHE A 226 -30.002 -15.316 3.399 1.00 64.83 C ANISOU 1338 CB PHE A 226 8353 8162 8115 -47 103 667 C ATOM 1339 CG PHE A 226 -30.592 -16.564 2.813 1.00 64.19 C ANISOU 1339 CG PHE A 226 8294 8039 8055 -110 101 702 C ATOM 1340 CD1 PHE A 226 -29.967 -17.213 1.761 1.00 60.96 C ANISOU 1340 CD1 PHE A 226 7940 7558 7666 -94 51 716 C ATOM 1341 CD2 PHE A 226 -31.769 -17.089 3.315 1.00 68.03 C ANISOU 1341 CD2 PHE A 226 8742 8560 8547 -188 151 714 C ATOM 1342 CE1 PHE A 226 -30.506 -18.361 1.221 1.00 62.57 C ANISOU 1342 CE1 PHE A 226 8168 7710 7897 -149 35 730 C ATOM 1343 CE2 PHE A 226 -32.314 -18.237 2.780 1.00 57.42 C ANISOU 1343 CE2 PHE A 226 7413 7162 7242 -255 136 744 C ATOM 1344 CZ PHE A 226 -31.683 -18.875 1.732 1.00 74.29 C ANISOU 1344 CZ PHE A 226 9613 9212 9400 -234 69 747 C ATOM 1345 N PHE A 227 -32.318 -13.374 3.036 1.00 59.78 N ANISOU 1345 N PHE A 227 7501 7616 7598 -32 126 542 N ATOM 1346 CA PHE A 227 -33.758 -13.258 2.823 1.00 63.07 C ANISOU 1346 CA PHE A 227 7814 8069 8080 -64 146 505 C ATOM 1347 C PHE A 227 -34.151 -12.092 1.913 1.00 68.69 C ANISOU 1347 C PHE A 227 8451 8762 8885 -7 78 458 C ATOM 1348 O PHE A 227 -35.147 -12.178 1.194 1.00 57.33 O ANISOU 1348 O PHE A 227 6945 7322 7516 -29 49 447 O ATOM 1349 CB PHE A 227 -34.483 -13.152 4.165 1.00 62.46 C ANISOU 1349 CB PHE A 227 7679 8083 7968 -88 242 469 C ATOM 1350 CG PHE A 227 -34.347 -14.380 5.019 1.00 71.88 C ANISOU 1350 CG PHE A 227 8942 9300 9071 -163 308 539 C ATOM 1351 CD1 PHE A 227 -35.222 -15.443 4.869 1.00 69.72 C ANISOU 1351 CD1 PHE A 227 8641 9025 8823 -256 340 585 C ATOM 1352 CD2 PHE A 227 -33.340 -14.474 5.965 1.00 74.65 C ANISOU 1352 CD2 PHE A 227 9383 9663 9315 -146 323 565 C ATOM 1353 CE1 PHE A 227 -35.096 -16.577 5.651 1.00 69.45 C ANISOU 1353 CE1 PHE A 227 8676 8998 8716 -333 392 668 C ATOM 1354 CE2 PHE A 227 -33.209 -15.605 6.750 1.00 66.91 C ANISOU 1354 CE2 PHE A 227 8477 8697 8251 -215 370 646 C ATOM 1355 CZ PHE A 227 -34.088 -16.657 6.593 1.00 64.26 C ANISOU 1355 CZ PHE A 227 8117 8353 7944 -311 407 704 C ATOM 1356 N THR A 228 -33.381 -11.009 1.944 1.00 68.77 N ANISOU 1356 N THR A 228 8473 8751 8906 62 43 437 N ATOM 1357 CA THR A 228 -33.663 -9.862 1.083 1.00 71.39 C ANISOU 1357 CA THR A 228 8746 9047 9333 115 -34 413 C ATOM 1358 C THR A 228 -33.488 -10.224 -0.394 1.00 74.36 C ANISOU 1358 C THR A 228 9165 9375 9715 102 -106 475 C ATOM 1359 O THR A 228 -34.418 -10.059 -1.185 1.00 70.15 O ANISOU 1359 O THR A 228 8575 8836 9243 99 -158 467 O ATOM 1360 CB THR A 228 -32.783 -8.642 1.428 1.00 65.67 C ANISOU 1360 CB THR A 228 8031 8290 8631 181 -65 389 C ATOM 1361 OG1 THR A 228 -33.028 -8.239 2.779 1.00 57.87 O ANISOU 1361 OG1 THR A 228 7005 7354 7629 202 -7 309 O ATOM 1362 CG2 THR A 228 -33.096 -7.477 0.497 1.00 64.97 C ANISOU 1362 CG2 THR A 228 7886 8146 8652 228 -155 385 C ATOM 1363 N PRO A 229 -32.296 -10.718 -0.773 1.00 55.49 N ANISOU 1363 N PRO A 229 6872 6954 7257 100 -111 531 N ATOM 1364 CA PRO A 229 -32.107 -11.138 -2.166 1.00 62.15 C ANISOU 1364 CA PRO A 229 7765 7769 8081 92 -164 576 C ATOM 1365 C PRO A 229 -33.049 -12.270 -2.572 1.00 60.58 C ANISOU 1365 C PRO A 229 7564 7579 7875 35 -170 567 C ATOM 1366 O PRO A 229 -33.425 -12.357 -3.741 1.00 62.13 O ANISOU 1366 O PRO A 229 7768 7764 8076 32 -237 576 O ATOM 1367 CB PRO A 229 -30.647 -11.605 -2.203 1.00 58.00 C ANISOU 1367 CB PRO A 229 7329 7223 7485 102 -140 618 C ATOM 1368 CG PRO A 229 -30.266 -11.839 -0.788 1.00 54.65 C ANISOU 1368 CG PRO A 229 6912 6813 7039 97 -82 601 C ATOM 1369 CD PRO A 229 -31.066 -10.875 0.019 1.00 55.04 C ANISOU 1369 CD PRO A 229 6878 6892 7142 112 -73 547 C ATOM 1370 N LEU A 230 -33.422 -13.122 -1.621 1.00 59.41 N ANISOU 1370 N LEU A 230 7407 7450 7715 -14 -107 553 N ATOM 1371 CA LEU A 230 -34.372 -14.194 -1.891 1.00 65.59 C ANISOU 1371 CA LEU A 230 8174 8230 8518 -82 -114 547 C ATOM 1372 C LEU A 230 -35.723 -13.612 -2.297 1.00 67.86 C ANISOU 1372 C LEU A 230 8347 8541 8896 -87 -160 509 C ATOM 1373 O LEU A 230 -36.338 -14.063 -3.264 1.00 62.85 O ANISOU 1373 O LEU A 230 7705 7888 8288 -115 -231 503 O ATOM 1374 CB LEU A 230 -34.536 -15.093 -0.664 1.00 64.93 C ANISOU 1374 CB LEU A 230 8094 8163 8412 -142 -30 560 C ATOM 1375 CG LEU A 230 -35.597 -16.192 -0.778 1.00 72.21 C ANISOU 1375 CG LEU A 230 8983 9075 9378 -232 -31 563 C ATOM 1376 CD1 LEU A 230 -35.298 -17.124 -1.944 1.00 74.45 C ANISOU 1376 CD1 LEU A 230 9349 9287 9651 -247 -107 571 C ATOM 1377 CD2 LEU A 230 -35.694 -16.975 0.521 1.00 64.21 C ANISOU 1377 CD2 LEU A 230 7978 8082 8336 -298 61 602 C ATOM 1378 N ALA A 231 -36.181 -12.613 -1.551 1.00 57.56 N ANISOU 1378 N ALA A 231 6950 7276 7645 -55 -129 472 N ATOM 1379 CA ALA A 231 -37.421 -11.925 -1.881 1.00 69.10 C ANISOU 1379 CA ALA A 231 8285 8756 9215 -42 -177 427 C ATOM 1380 C ALA A 231 -37.313 -11.272 -3.253 1.00 68.07 C ANISOU 1380 C ALA A 231 8177 8582 9105 5 -301 449 C ATOM 1381 O ALA A 231 -38.202 -11.417 -4.092 1.00 70.57 O ANISOU 1381 O ALA A 231 8445 8893 9475 -12 -383 440 O ATOM 1382 CB ALA A 231 -37.740 -10.882 -0.828 1.00 61.68 C ANISOU 1382 CB ALA A 231 7252 7859 8327 7 -120 369 C ATOM 1383 N ILE A 232 -36.218 -10.551 -3.471 1.00 60.95 N ANISOU 1383 N ILE A 232 7347 7652 8160 59 -317 483 N ATOM 1384 CA ILE A 232 -35.975 -9.884 -4.742 1.00 65.53 C ANISOU 1384 CA ILE A 232 7963 8198 8739 97 -422 527 C ATOM 1385 C ILE A 232 -36.021 -10.876 -5.905 1.00 72.57 C ANISOU 1385 C ILE A 232 8929 9086 9559 58 -477 553 C ATOM 1386 O ILE A 232 -36.603 -10.591 -6.951 1.00 73.33 O ANISOU 1386 O ILE A 232 9014 9176 9672 67 -583 565 O ATOM 1387 CB ILE A 232 -34.613 -9.166 -4.735 1.00 63.53 C ANISOU 1387 CB ILE A 232 7781 7916 8440 139 -408 576 C ATOM 1388 CG1 ILE A 232 -34.640 -7.998 -3.748 1.00 57.07 C ANISOU 1388 CG1 ILE A 232 6890 7085 7709 186 -389 536 C ATOM 1389 CG2 ILE A 232 -34.269 -8.657 -6.125 1.00 64.86 C ANISOU 1389 CG2 ILE A 232 8005 8061 8579 160 -499 647 C ATOM 1390 CD1 ILE A 232 -33.285 -7.390 -3.488 1.00 56.50 C ANISOU 1390 CD1 ILE A 232 6876 6980 7611 214 -370 573 C ATOM 1391 N MET A 233 -35.407 -12.040 -5.716 1.00 67.33 N ANISOU 1391 N MET A 233 8346 8423 8815 19 -416 556 N ATOM 1392 CA MET A 233 -35.356 -13.054 -6.763 1.00 62.53 C ANISOU 1392 CA MET A 233 7818 7805 8136 -10 -465 558 C ATOM 1393 C MET A 233 -36.721 -13.691 -6.998 1.00 64.74 C ANISOU 1393 C MET A 233 8030 8085 8484 -65 -525 513 C ATOM 1394 O MET A 233 -37.027 -14.114 -8.112 1.00 67.92 O ANISOU 1394 O MET A 233 8474 8481 8853 -77 -618 502 O ATOM 1395 CB MET A 233 -34.320 -14.126 -6.415 1.00 57.12 C ANISOU 1395 CB MET A 233 7228 7102 7373 -27 -388 563 C ATOM 1396 CG MET A 233 -32.885 -13.649 -6.586 1.00 73.10 C ANISOU 1396 CG MET A 233 9324 9128 9325 26 -351 606 C ATOM 1397 SD MET A 233 -31.661 -14.724 -5.819 1.00 66.54 S ANISOU 1397 SD MET A 233 8568 8271 8442 22 -261 608 S ATOM 1398 CE MET A 233 -31.555 -16.041 -7.025 1.00 80.73 C ANISOU 1398 CE MET A 233 10460 10046 10169 10 -302 574 C ATOM 1399 N ILE A 234 -37.538 -13.771 -5.953 1.00 63.44 N ANISOU 1399 N ILE A 234 7758 7935 8411 -101 -472 485 N ATOM 1400 CA ILE A 234 -38.898 -14.266 -6.109 1.00 66.69 C ANISOU 1400 CA ILE A 234 8072 8351 8916 -160 -524 446 C ATOM 1401 C ILE A 234 -39.697 -13.290 -6.956 1.00 60.62 C ANISOU 1401 C ILE A 234 7227 7590 8216 -117 -646 435 C ATOM 1402 O ILE A 234 -40.377 -13.688 -7.897 1.00 68.52 O ANISOU 1402 O ILE A 234 8220 8580 9235 -143 -760 418 O ATOM 1403 CB ILE A 234 -39.604 -14.460 -4.757 1.00 65.11 C ANISOU 1403 CB ILE A 234 7756 8183 8799 -209 -419 426 C ATOM 1404 CG1 ILE A 234 -39.038 -15.686 -4.037 1.00 70.73 C ANISOU 1404 CG1 ILE A 234 8547 8876 9451 -273 -327 451 C ATOM 1405 CG2 ILE A 234 -41.100 -14.638 -4.964 1.00 64.04 C ANISOU 1405 CG2 ILE A 234 7476 8062 8793 -260 -476 386 C ATOM 1406 CD1 ILE A 234 -39.526 -15.838 -2.615 1.00 68.66 C ANISOU 1406 CD1 ILE A 234 8197 8662 9229 -322 -203 454 C ATOM 1407 N VAL A 235 -39.614 -12.010 -6.613 1.00 60.42 N ANISOU 1407 N VAL A 235 7148 7576 8234 -50 -637 444 N ATOM 1408 CA VAL A 235 -40.304 -10.978 -7.373 1.00 71.85 C ANISOU 1408 CA VAL A 235 8527 9015 9759 2 -764 446 C ATOM 1409 C VAL A 235 -39.831 -11.004 -8.821 1.00 70.45 C ANISOU 1409 C VAL A 235 8474 8820 9474 18 -881 497 C ATOM 1410 O VAL A 235 -40.640 -10.984 -9.747 1.00 71.58 O ANISOU 1410 O VAL A 235 8590 8960 9647 15 -1017 492 O ATOM 1411 CB VAL A 235 -40.061 -9.575 -6.784 1.00 71.48 C ANISOU 1411 CB VAL A 235 8427 8958 9774 80 -740 450 C ATOM 1412 CG1 VAL A 235 -40.738 -8.518 -7.640 1.00 61.94 C ANISOU 1412 CG1 VAL A 235 7157 7720 8657 137 -892 466 C ATOM 1413 CG2 VAL A 235 -40.574 -9.503 -5.355 1.00 63.81 C ANISOU 1413 CG2 VAL A 235 7333 8022 8889 74 -621 382 C ATOM 1414 N THR A 236 -38.515 -11.057 -9.009 1.00 65.41 N ANISOU 1414 N THR A 236 7969 8177 8706 34 -827 545 N ATOM 1415 CA THR A 236 -37.938 -11.092 -10.347 1.00 67.89 C ANISOU 1415 CA THR A 236 8409 8495 8891 49 -906 595 C ATOM 1416 C THR A 236 -38.435 -12.318 -11.104 1.00 71.21 C ANISOU 1416 C THR A 236 8875 8923 9257 -1 -973 547 C ATOM 1417 O THR A 236 -38.748 -12.240 -12.291 1.00 72.06 O ANISOU 1417 O THR A 236 9030 9044 9306 9 -1101 560 O ATOM 1418 CB THR A 236 -36.400 -11.113 -10.304 1.00 59.71 C ANISOU 1418 CB THR A 236 7489 7463 7733 68 -807 643 C ATOM 1419 OG1 THR A 236 -35.918 -9.928 -9.662 1.00 59.21 O ANISOU 1419 OG1 THR A 236 7386 7383 7730 110 -765 686 O ATOM 1420 CG2 THR A 236 -35.825 -11.178 -11.713 1.00113.49 C ANISOU 1420 CG2 THR A 236 14425 14300 14395 83 -868 692 C ATOM 1421 N TYR A 237 -38.504 -13.451 -10.414 1.00 67.94 N ANISOU 1421 N TYR A 237 8452 8497 8864 -56 -897 494 N ATOM 1422 CA TYR A 237 -39.004 -14.676 -11.023 1.00 67.34 C ANISOU 1422 CA TYR A 237 8411 8407 8766 -112 -966 438 C ATOM 1423 C TYR A 237 -40.393 -14.452 -11.620 1.00 63.21 C ANISOU 1423 C TYR A 237 7791 7888 8340 -129 -1118 409 C ATOM 1424 O TYR A 237 -40.633 -14.770 -12.782 1.00 66.09 O ANISOU 1424 O TYR A 237 8221 8256 8634 -131 -1247 388 O ATOM 1425 CB TYR A 237 -39.044 -15.818 -10.003 1.00 61.61 C ANISOU 1425 CB TYR A 237 7664 7650 8095 -179 -866 402 C ATOM 1426 CG TYR A 237 -39.825 -17.020 -10.483 1.00 63.10 C ANISOU 1426 CG TYR A 237 7852 7802 8320 -252 -953 339 C ATOM 1427 CD1 TYR A 237 -41.193 -17.113 -10.264 1.00 63.70 C ANISOU 1427 CD1 TYR A 237 7783 7875 8547 -311 -1013 310 C ATOM 1428 CD2 TYR A 237 -39.198 -18.059 -11.161 1.00 62.92 C ANISOU 1428 CD2 TYR A 237 7966 7745 8195 -260 -979 301 C ATOM 1429 CE1 TYR A 237 -41.914 -18.203 -10.703 1.00 64.86 C ANISOU 1429 CE1 TYR A 237 7920 7978 8747 -387 -1104 253 C ATOM 1430 CE2 TYR A 237 -39.912 -19.155 -11.606 1.00 64.09 C ANISOU 1430 CE2 TYR A 237 8117 7843 8390 -327 -1074 232 C ATOM 1431 CZ TYR A 237 -41.270 -19.221 -11.375 1.00 84.95 C ANISOU 1431 CZ TYR A 237 10613 10476 11189 -396 -1141 213 C ATOM 1432 OH TYR A 237 -41.993 -20.306 -11.816 1.00 66.36 O ANISOU 1432 OH TYR A 237 8251 8061 8900 -474 -1247 145 O ATOM 1433 N PHE A 238 -41.301 -13.897 -10.823 1.00 82.44 N ANISOU 1433 N PHE A 238 10063 10326 10933 -136 -1105 401 N ATOM 1434 CA PHE A 238 -42.673 -13.673 -11.267 1.00 78.37 C ANISOU 1434 CA PHE A 238 9420 9812 10543 -150 -1247 369 C ATOM 1435 C PHE A 238 -42.754 -12.583 -12.334 1.00 80.50 C ANISOU 1435 C PHE A 238 9719 10090 10776 -77 -1394 415 C ATOM 1436 O PHE A 238 -43.554 -12.677 -13.265 1.00 66.74 O ANISOU 1436 O PHE A 238 7958 8347 9051 -85 -1562 396 O ATOM 1437 CB PHE A 238 -43.570 -13.329 -10.076 1.00 71.70 C ANISOU 1437 CB PHE A 238 8381 8980 9883 -166 -1171 341 C ATOM 1438 CG PHE A 238 -43.917 -14.518 -9.221 1.00 75.12 C ANISOU 1438 CG PHE A 238 8759 9409 10374 -264 -1069 304 C ATOM 1439 CD1 PHE A 238 -44.798 -15.481 -9.684 1.00 75.58 C ANISOU 1439 CD1 PHE A 238 8768 9445 10503 -345 -1163 261 C ATOM 1440 CD2 PHE A 238 -43.365 -14.675 -7.959 1.00 71.94 C ANISOU 1440 CD2 PHE A 238 8357 9021 9957 -280 -888 320 C ATOM 1441 CE1 PHE A 238 -45.121 -16.579 -8.908 1.00 75.66 C ANISOU 1441 CE1 PHE A 238 8728 9439 10579 -447 -1073 245 C ATOM 1442 CE2 PHE A 238 -43.686 -15.771 -7.177 1.00 68.70 C ANISOU 1442 CE2 PHE A 238 7905 8605 9592 -377 -798 309 C ATOM 1443 CZ PHE A 238 -44.565 -16.723 -7.653 1.00 74.53 C ANISOU 1443 CZ PHE A 238 8592 9313 10412 -465 -886 277 C ATOM 1444 N LEU A 239 -41.923 -11.554 -12.198 1.00 79.77 N ANISOU 1444 N LEU A 239 9675 10001 10635 -10 -1342 482 N ATOM 1445 CA LEU A 239 -41.844 -10.499 -13.203 1.00 70.93 C ANISOU 1445 CA LEU A 239 8603 8879 9467 52 -1474 555 C ATOM 1446 C LEU A 239 -41.394 -11.079 -14.538 1.00 70.92 C ANISOU 1446 C LEU A 239 8769 8906 9270 41 -1561 576 C ATOM 1447 O LEU A 239 -41.856 -10.658 -15.599 1.00 67.08 O ANISOU 1447 O LEU A 239 8312 8430 8745 64 -1728 611 O ATOM 1448 CB LEU A 239 -40.865 -9.409 -12.764 1.00 64.34 C ANISOU 1448 CB LEU A 239 7801 8030 8614 108 -1385 630 C ATOM 1449 CG LEU A 239 -41.321 -8.494 -11.627 1.00 76.24 C ANISOU 1449 CG LEU A 239 9154 9508 10308 146 -1336 607 C ATOM 1450 CD1 LEU A 239 -40.167 -7.619 -11.161 1.00 72.51 C ANISOU 1450 CD1 LEU A 239 8737 9011 9802 189 -1243 667 C ATOM 1451 CD2 LEU A 239 -42.501 -7.637 -12.056 1.00 73.90 C ANISOU 1451 CD2 LEU A 239 8736 9184 10160 191 -1503 608 C ATOM 1452 N THR A 240 -40.492 -12.053 -14.476 1.00 68.86 N ANISOU 1452 N THR A 240 8622 8660 8884 11 -1451 549 N ATOM 1453 CA THR A 240 -39.944 -12.673 -15.675 1.00 65.65 C ANISOU 1453 CA THR A 240 8379 8288 8276 9 -1505 546 C ATOM 1454 C THR A 240 -41.007 -13.525 -16.358 1.00 83.94 C ANISOU 1454 C THR A 240 10682 10600 10609 -33 -1661 460 C ATOM 1455 O THR A 240 -41.161 -13.479 -17.578 1.00 68.30 O ANISOU 1455 O THR A 240 8793 8656 8503 -17 -1803 468 O ATOM 1456 CB THR A 240 -38.716 -13.550 -15.345 1.00 64.59 C ANISOU 1456 CB THR A 240 8351 8159 8033 -1 -1344 519 C ATOM 1457 OG1 THR A 240 -37.711 -12.757 -14.700 1.00 65.64 O ANISOU 1457 OG1 THR A 240 8486 8294 8160 34 -1211 596 O ATOM 1458 CG2 THR A 240 -38.130 -14.152 -16.611 1.00 86.77 C ANISOU 1458 CG2 THR A 240 11324 11014 10629 11 -1388 498 C ATOM 1459 N ILE A 241 -41.741 -14.299 -15.566 1.00 85.92 N ANISOU 1459 N ILE A 241 10820 10812 11014 -93 -1637 383 N ATOM 1460 CA ILE A 241 -42.837 -15.105 -16.087 1.00 86.01 C ANISOU 1460 CA ILE A 241 10788 10805 11087 -148 -1789 299 C ATOM 1461 C ILE A 241 -43.844 -14.203 -16.791 1.00 87.50 C ANISOU 1461 C ILE A 241 10899 11009 11338 -117 -1983 327 C ATOM 1462 O ILE A 241 -44.272 -14.483 -17.911 1.00 84.15 O ANISOU 1462 O ILE A 241 10539 10601 10833 -121 -2161 295 O ATOM 1463 CB ILE A 241 -43.542 -15.887 -14.960 1.00 89.90 C ANISOU 1463 CB ILE A 241 11134 11250 11773 -228 -1717 239 C ATOM 1464 CG1 ILE A 241 -42.902 -17.264 -14.775 1.00 88.10 C ANISOU 1464 CG1 ILE A 241 11009 10983 11480 -280 -1633 182 C ATOM 1465 CG2 ILE A 241 -45.016 -16.068 -15.271 1.00101.68 C ANISOU 1465 CG2 ILE A 241 12484 12726 13424 -276 -1887 185 C ATOM 1466 CD1 ILE A 241 -41.437 -17.219 -14.422 1.00 93.86 C ANISOU 1466 CD1 ILE A 241 11864 11724 12074 -234 -1467 225 C ATOM 1467 N HIS A 242 -44.212 -13.114 -16.122 1.00 92.33 N ANISOU 1467 N HIS A 242 11374 11613 12094 -80 -1957 382 N ATOM 1468 CA HIS A 242 -45.158 -12.152 -16.670 1.00 91.54 C ANISOU 1468 CA HIS A 242 11182 11513 12087 -38 -2141 416 C ATOM 1469 C HIS A 242 -44.614 -11.530 -17.951 1.00 86.10 C ANISOU 1469 C HIS A 242 10661 10857 11196 18 -2262 502 C ATOM 1470 O HIS A 242 -45.330 -11.402 -18.944 1.00 83.35 O ANISOU 1470 O HIS A 242 10324 10520 10824 27 -2473 505 O ATOM 1471 CB HIS A 242 -45.445 -11.055 -15.644 1.00 98.66 C ANISOU 1471 CB HIS A 242 11920 12391 13173 8 -2065 450 C ATOM 1472 CG HIS A 242 -46.347 -9.975 -16.152 1.00115.72 C ANISOU 1472 CG HIS A 242 13980 14534 15452 68 -2255 488 C ATOM 1473 ND1 HIS A 242 -47.716 -10.119 -16.219 1.00126.51 N ANISOU 1473 ND1 HIS A 242 15173 15890 17006 51 -2395 423 N ATOM 1474 CD2 HIS A 242 -46.076 -8.734 -16.622 1.00120.22 C ANISOU 1474 CD2 HIS A 242 14595 15088 15996 146 -2336 590 C ATOM 1475 CE1 HIS A 242 -48.250 -9.013 -16.706 1.00130.31 C ANISOU 1475 CE1 HIS A 242 15595 16349 17570 125 -2561 478 C ATOM 1476 NE2 HIS A 242 -47.277 -8.157 -16.959 1.00125.39 N ANISOU 1476 NE2 HIS A 242 15108 15716 16818 182 -2531 584 N ATOM 1477 N ALA A 243 -43.343 -11.143 -17.917 1.00 88.04 N ANISOU 1477 N ALA A 243 11035 11123 11294 49 -2128 578 N ATOM 1478 CA ALA A 243 -42.697 -10.508 -19.061 1.00 88.22 C ANISOU 1478 CA ALA A 243 11219 11188 11112 93 -2205 683 C ATOM 1479 C ALA A 243 -42.776 -11.387 -20.307 1.00 83.58 C ANISOU 1479 C ALA A 243 10774 10655 10325 71 -2331 632 C ATOM 1480 O ALA A 243 -43.160 -10.922 -21.380 1.00 83.75 O ANISOU 1480 O ALA A 243 10860 10710 10253 96 -2517 687 O ATOM 1481 CB ALA A 243 -41.246 -10.186 -18.733 1.00 69.64 C ANISOU 1481 CB ALA A 243 8965 8852 8643 112 -2010 757 C ATOM 1482 N LEU A 244 -42.408 -12.655 -20.163 1.00 78.46 N ANISOU 1482 N LEU A 244 10185 10015 9612 27 -2240 524 N ATOM 1483 CA LEU A 244 -42.437 -13.585 -21.283 1.00 73.33 C ANISOU 1483 CA LEU A 244 9676 9411 8777 11 -2352 443 C ATOM 1484 C LEU A 244 -43.867 -13.794 -21.767 1.00102.41 C ANISOU 1484 C LEU A 244 13272 13072 12568 -15 -2593 378 C ATOM 1485 O LEU A 244 -44.143 -13.716 -22.963 1.00 76.84 O ANISOU 1485 O LEU A 244 10136 9883 9175 3 -2778 384 O ATOM 1486 CB LEU A 244 -41.807 -14.922 -20.884 1.00 72.51 C ANISOU 1486 CB LEU A 244 9630 9289 8633 -26 -2209 327 C ATOM 1487 CG LEU A 244 -40.290 -14.907 -20.673 1.00 82.32 C ANISOU 1487 CG LEU A 244 10984 10566 9728 7 -1996 372 C ATOM 1488 CD1 LEU A 244 -39.798 -16.265 -20.195 1.00 83.25 C ANISOU 1488 CD1 LEU A 244 11137 10644 9851 -25 -1879 251 C ATOM 1489 CD2 LEU A 244 -39.576 -14.506 -21.955 1.00 88.58 C ANISOU 1489 CD2 LEU A 244 11952 11459 10244 55 -2030 433 C ATOM 1490 N GLN A 245 -44.775 -14.056 -20.831 1.00103.40 N ANISOU 1490 N GLN A 245 13203 13129 12954 -60 -2592 320 N ATOM 1491 CA GLN A 245 -46.186 -14.227 -21.160 1.00100.40 C ANISOU 1491 CA GLN A 245 12697 12722 12726 -91 -2813 258 C ATOM 1492 C GLN A 245 -46.694 -13.030 -21.958 1.00 96.23 C ANISOU 1492 C GLN A 245 12163 12222 12179 -29 -3011 357 C ATOM 1493 O GLN A 245 -47.440 -13.185 -22.924 1.00 94.31 O ANISOU 1493 O GLN A 245 11943 11995 11895 -32 -3246 324 O ATOM 1494 CB GLN A 245 -47.019 -14.403 -19.885 1.00110.30 C ANISOU 1494 CB GLN A 245 13712 13913 14282 -143 -2739 213 C ATOM 1495 CG GLN A 245 -47.028 -15.824 -19.333 1.00121.36 C ANISOU 1495 CG GLN A 245 15097 15271 15742 -233 -2645 102 C ATOM 1496 CD GLN A 245 -47.911 -15.973 -18.104 1.00131.40 C ANISOU 1496 CD GLN A 245 16128 16497 17300 -294 -2567 76 C ATOM 1497 OE1 GLN A 245 -48.283 -14.987 -17.469 1.00135.67 O ANISOU 1497 OE1 GLN A 245 16522 17046 17980 -256 -2524 132 O ATOM 1498 NE2 GLN A 245 -48.251 -17.213 -17.766 1.00136.03 N ANISOU 1498 NE2 GLN A 245 16673 17035 17976 -391 -2547 -11 N ATOM 1499 N LYS A 246 -46.277 -11.836 -21.551 1.00102.64 N ANISOU 1499 N LYS A 246 12946 13029 13023 29 -2926 481 N ATOM 1500 CA LYS A 246 -46.689 -10.606 -22.216 1.00105.35 C ANISOU 1500 CA LYS A 246 13283 13376 13370 92 -3108 598 C ATOM 1501 C LYS A 246 -46.077 -10.527 -23.610 1.00102.85 C ANISOU 1501 C LYS A 246 13205 13137 12735 115 -3213 669 C ATOM 1502 O LYS A 246 -46.742 -10.141 -24.573 1.00 81.48 O ANISOU 1502 O LYS A 246 10529 10450 9979 139 -3456 711 O ATOM 1503 CB LYS A 246 -46.255 -9.394 -21.390 1.00106.17 C ANISOU 1503 CB LYS A 246 13313 13439 13589 145 -2976 708 C ATOM 1504 CG LYS A 246 -46.740 -8.058 -21.930 1.00114.55 C ANISOU 1504 CG LYS A 246 14343 14472 14709 214 -3167 833 C ATOM 1505 CD LYS A 246 -48.031 -7.617 -21.257 1.00127.75 C ANISOU 1505 CD LYS A 246 15757 16073 16709 238 -3264 781 C ATOM 1506 CE LYS A 246 -48.419 -6.207 -21.674 1.00137.84 C ANISOU 1506 CE LYS A 246 16997 17299 18076 322 -3444 909 C ATOM 1507 NZ LYS A 246 -49.417 -5.602 -20.750 1.00142.15 N ANISOU 1507 NZ LYS A 246 17278 17769 18962 367 -3468 854 N ATOM 1508 N LYS A 247 -44.805 -10.899 -23.708 1.00 99.22 N ANISOU 1508 N LYS A 247 12912 12730 12058 109 -3029 682 N ATOM 1509 CA LYS A 247 -44.075 -10.839 -24.968 1.00 88.27 C ANISOU 1509 CA LYS A 247 11755 11440 10343 130 -3077 750 C ATOM 1510 C LYS A 247 -44.739 -11.716 -26.023 1.00 86.99 C ANISOU 1510 C LYS A 247 11679 11325 10047 110 -3289 637 C ATOM 1511 O LYS A 247 -44.880 -11.316 -27.178 1.00 94.79 O ANISOU 1511 O LYS A 247 12795 12381 10841 136 -3469 708 O ATOM 1512 CB LYS A 247 -42.631 -11.298 -24.765 1.00 86.51 C ANISOU 1512 CB LYS A 247 11661 11266 9944 125 -2819 744 C ATOM 1513 CG LYS A 247 -41.594 -10.372 -25.369 1.00 86.20 C ANISOU 1513 CG LYS A 247 11763 11297 9690 160 -2749 917 C ATOM 1514 CD LYS A 247 -40.233 -11.039 -25.401 1.00 82.95 C ANISOU 1514 CD LYS A 247 11483 10956 9080 156 -2520 880 C ATOM 1515 CE LYS A 247 -39.126 -10.063 -25.058 1.00 88.06 C ANISOU 1515 CE LYS A 247 12144 11611 9703 172 -2342 1042 C ATOM 1516 NZ LYS A 247 -37.799 -10.733 -25.041 1.00 96.08 N ANISOU 1516 NZ LYS A 247 13259 12695 10550 171 -2115 999 N ATOM 1517 N ALA A 248 -45.143 -12.914 -25.612 1.00 89.60 N ANISOU 1517 N ALA A 248 11944 11616 10482 59 -3275 464 N ATOM 1518 CA ALA A 248 -45.738 -13.889 -26.519 1.00 83.30 C ANISOU 1518 CA ALA A 248 11224 10846 9580 31 -3471 326 C ATOM 1519 C ALA A 248 -47.038 -13.372 -27.128 1.00 85.41 C ANISOU 1519 C ALA A 248 11408 11101 9942 40 -3778 351 C ATOM 1520 O ALA A 248 -47.349 -13.660 -28.283 1.00 87.57 O ANISOU 1520 O ALA A 248 11812 11435 10026 46 -3990 308 O ATOM 1521 CB ALA A 248 -45.991 -15.198 -25.781 1.00 97.17 C ANISOU 1521 CB ALA A 248 12891 12528 11500 -36 -3396 152 C ATOM 1522 N ALA A1001 -47.793 -12.608 -26.345 1.00114.95 N ANISOU 1522 N ALA A1001 10845 20549 12281 -1959 -3145 1513 N ATOM 1523 CA ALA A1001 -49.111 -12.141 -26.763 1.00113.17 C ANISOU 1523 CA ALA A1001 10557 20613 11830 -1902 -3063 1475 C ATOM 1524 C ALA A1001 -49.026 -11.124 -27.896 1.00112.74 C ANISOU 1524 C ALA A1001 10473 20547 11818 -1642 -2885 1443 C ATOM 1525 O ALA A1001 -49.639 -11.304 -28.949 1.00132.12 O ANISOU 1525 O ALA A1001 12919 23103 14177 -1569 -2825 1423 O ATOM 1526 CB ALA A1001 -49.857 -11.544 -25.577 1.00113.39 C ANISOU 1526 CB ALA A1001 10527 20847 11710 -1990 -3085 1463 C ATOM 1527 N ASP A1002 -48.267 -10.056 -27.675 1.00112.29 N ANISOU 1527 N ASP A1002 10398 20365 11901 -1507 -2800 1437 N ATOM 1528 CA ASP A1002 -48.171 -8.970 -28.645 1.00111.88 C ANISOU 1528 CA ASP A1002 10315 20303 11891 -1257 -2626 1407 C ATOM 1529 C ASP A1002 -47.797 -9.492 -30.029 1.00111.74 C ANISOU 1529 C ASP A1002 10343 20157 11956 -1153 -2580 1407 C ATOM 1530 O ASP A1002 -48.303 -9.006 -31.041 1.00111.66 O ANISOU 1530 O ASP A1002 10306 20247 11873 -996 -2460 1380 O ATOM 1531 CB ASP A1002 -47.147 -7.929 -28.188 1.00111.40 C ANISOU 1531 CB ASP A1002 10248 20065 12014 -1144 -2560 1408 C ATOM 1532 CG ASP A1002 -47.428 -7.407 -26.792 1.00111.54 C ANISOU 1532 CG ASP A1002 10226 20192 11963 -1250 -2606 1407 C ATOM 1533 OD1 ASP A1002 -48.571 -7.567 -26.313 1.00111.97 O ANISOU 1533 OD1 ASP A1002 10242 20495 11806 -1363 -2650 1397 O ATOM 1534 OD2 ASP A1002 -46.508 -6.830 -26.174 1.00111.24 O ANISOU 1534 OD2 ASP A1002 10195 19990 12082 -1220 -2598 1416 O ATOM 1535 N LEU A1003 -46.909 -10.480 -30.068 1.00111.73 N ANISOU 1535 N LEU A1003 10413 19933 12107 -1241 -2674 1440 N ATOM 1536 CA LEU A1003 -46.487 -11.072 -31.332 1.00118.64 C ANISOU 1536 CA LEU A1003 11339 20669 13071 -1159 -2639 1442 C ATOM 1537 C LEU A1003 -47.664 -11.726 -32.043 1.00121.23 C ANISOU 1537 C LEU A1003 11659 21212 13190 -1206 -2648 1426 C ATOM 1538 O LEU A1003 -47.861 -11.529 -33.242 1.00124.56 O ANISOU 1538 O LEU A1003 12080 21656 13591 -1057 -2543 1404 O ATOM 1539 CB LEU A1003 -45.383 -12.104 -31.099 1.00117.00 C ANISOU 1539 CB LEU A1003 11207 20194 13053 -1273 -2755 1482 C ATOM 1540 CG LEU A1003 -44.930 -12.876 -32.340 1.00118.48 C ANISOU 1540 CG LEU A1003 11455 20228 13335 -1216 -2734 1486 C ATOM 1541 CD1 LEU A1003 -44.388 -11.930 -33.402 1.00121.69 C ANISOU 1541 CD1 LEU A1003 11854 20523 13859 -962 -2566 1462 C ATOM 1542 CD2 LEU A1003 -43.892 -13.920 -31.962 1.00120.36 C ANISOU 1542 CD2 LEU A1003 11764 20215 13753 -1346 -2860 1528 C ATOM 1543 N GLU A1004 -48.445 -12.503 -31.301 1.00119.88 N ANISOU 1543 N GLU A1004 11484 21202 12862 -1415 -2774 1436 N ATOM 1544 CA GLU A1004 -49.604 -13.178 -31.870 1.00121.40 C ANISOU 1544 CA GLU A1004 11668 21611 12847 -1482 -2795 1422 C ATOM 1545 C GLU A1004 -50.644 -12.152 -32.299 1.00119.68 C ANISOU 1545 C GLU A1004 11372 21646 12457 -1342 -2669 1383 C ATOM 1546 O GLU A1004 -51.378 -12.362 -33.264 1.00118.04 O ANISOU 1546 O GLU A1004 11153 21571 12125 -1292 -2621 1364 O ATOM 1547 CB GLU A1004 -50.219 -14.146 -30.860 1.00125.73 C ANISOU 1547 CB GLU A1004 12224 22283 13265 -1740 -2956 1441 C ATOM 1548 CG GLU A1004 -50.898 -15.347 -31.499 1.00135.45 C ANISOU 1548 CG GLU A1004 13488 23606 14370 -1851 -3021 1441 C ATOM 1549 CD GLU A1004 -51.758 -16.123 -30.520 1.00145.04 C ANISOU 1549 CD GLU A1004 14695 25003 15411 -2093 -3160 1452 C ATOM 1550 OE1 GLU A1004 -51.938 -15.647 -29.379 1.00151.19 O ANISOU 1550 OE1 GLU A1004 15436 25862 16147 -2164 -3196 1456 O ATOM 1551 OE2 GLU A1004 -52.252 -17.210 -30.892 1.00144.74 O ANISOU 1551 OE2 GLU A1004 14690 25026 15278 -2213 -3231 1456 O ATOM 1552 N ASP A1005 -50.703 -11.040 -31.572 1.00121.82 N ANISOU 1552 N ASP A1005 11587 21980 12719 -1281 -2615 1372 N ATOM 1553 CA ASP A1005 -51.634 -9.967 -31.892 1.00124.54 C ANISOU 1553 CA ASP A1005 11853 22554 12912 -1140 -2490 1337 C ATOM 1554 C ASP A1005 -51.284 -9.358 -33.245 1.00118.75 C ANISOU 1554 C ASP A1005 11125 21735 12262 -900 -2339 1319 C ATOM 1555 O ASP A1005 -52.154 -9.167 -34.095 1.00120.97 O ANISOU 1555 O ASP A1005 11371 22194 12398 -813 -2264 1296 O ATOM 1556 CB ASP A1005 -51.591 -8.886 -30.812 1.00134.51 C ANISOU 1556 CB ASP A1005 13065 23862 14181 -1119 -2459 1331 C ATOM 1557 CG ASP A1005 -52.905 -8.141 -30.682 1.00148.67 C ANISOU 1557 CG ASP A1005 14773 25965 15750 -1082 -2393 1300 C ATOM 1558 OD1 ASP A1005 -53.174 -7.254 -31.520 1.00154.45 O ANISOU 1558 OD1 ASP A1005 15465 26763 16454 -881 -2251 1276 O ATOM 1559 OD2 ASP A1005 -53.667 -8.442 -29.738 1.00152.09 O ANISOU 1559 OD2 ASP A1005 15177 26575 16035 -1253 -2483 1302 O ATOM 1560 N ASN A1006 -50.004 -9.053 -33.436 1.00113.53 N ANISOU 1560 N ASN A1006 10505 20799 11833 -796 -2296 1331 N ATOM 1561 CA ASN A1006 -49.529 -8.478 -34.688 1.00111.60 C ANISOU 1561 CA ASN A1006 10272 20440 11690 -568 -2154 1316 C ATOM 1562 C ASN A1006 -49.615 -9.477 -35.838 1.00114.87 C ANISOU 1562 C ASN A1006 10736 20819 12089 -576 -2169 1318 C ATOM 1563 O ASN A1006 -49.909 -9.100 -36.972 1.00111.72 O ANISOU 1563 O ASN A1006 10327 20472 11650 -416 -2055 1297 O ATOM 1564 CB ASN A1006 -48.094 -7.971 -34.533 1.00111.05 C ANISOU 1564 CB ASN A1006 10237 20077 11881 -472 -2113 1328 C ATOM 1565 CG ASN A1006 -47.990 -6.806 -33.565 1.00118.94 C ANISOU 1565 CG ASN A1006 11185 21109 12899 -426 -2069 1320 C ATOM 1566 OD1 ASN A1006 -48.962 -6.085 -33.341 1.00123.84 O ANISOU 1566 OD1 ASN A1006 11738 21964 13351 -390 -2014 1298 O ATOM 1567 ND2 ASN A1006 -46.808 -6.614 -32.991 1.00119.89 N ANISOU 1567 ND2 ASN A1006 11335 20993 13226 -427 -2090 1338 N ATOM 1568 N TRP A1007 -49.354 -10.747 -35.546 1.00112.03 N ANISOU 1568 N TRP A1007 10434 20369 11763 -763 -2308 1343 N ATOM 1569 CA TRP A1007 -49.565 -11.804 -36.526 1.00121.97 C ANISOU 1569 CA TRP A1007 11741 21619 12982 -803 -2337 1344 C ATOM 1570 C TRP A1007 -51.008 -11.736 -37.005 1.00118.88 C ANISOU 1570 C TRP A1007 11296 21539 12334 -796 -2303 1318 C ATOM 1571 O TRP A1007 -51.278 -11.705 -38.205 1.00122.58 O ANISOU 1571 O TRP A1007 11770 22044 12761 -676 -2218 1301 O ATOM 1572 CB TRP A1007 -49.285 -13.178 -35.913 1.00130.79 C ANISOU 1572 CB TRP A1007 12918 22642 14133 -1035 -2506 1375 C ATOM 1573 CG TRP A1007 -49.679 -14.334 -36.797 1.00143.39 C ANISOU 1573 CG TRP A1007 14561 24266 15654 -1107 -2548 1375 C ATOM 1574 CD1 TRP A1007 -50.916 -14.580 -37.327 1.00150.08 C ANISOU 1574 CD1 TRP A1007 15378 25368 16278 -1132 -2538 1353 C ATOM 1575 CD2 TRP A1007 -48.837 -15.408 -37.239 1.00146.50 C ANISOU 1575 CD2 TRP A1007 15040 24426 16196 -1167 -2609 1396 C ATOM 1576 NE1 TRP A1007 -50.891 -15.730 -38.076 1.00151.91 N ANISOU 1576 NE1 TRP A1007 15673 25538 16508 -1205 -2587 1359 N ATOM 1577 CE2 TRP A1007 -49.627 -16.259 -38.037 1.00151.55 C ANISOU 1577 CE2 TRP A1007 15700 25194 16689 -1227 -2630 1385 C ATOM 1578 CE3 TRP A1007 -47.491 -15.730 -37.038 1.00144.28 C ANISOU 1578 CE3 TRP A1007 14819 23840 16159 -1175 -2647 1424 C ATOM 1579 CZ2 TRP A1007 -49.118 -17.409 -38.635 1.00152.11 C ANISOU 1579 CZ2 TRP A1007 15851 25095 16848 -1294 -2684 1399 C ATOM 1580 CZ3 TRP A1007 -46.988 -16.875 -37.634 1.00146.60 C ANISOU 1580 CZ3 TRP A1007 15191 23967 16543 -1239 -2701 1440 C ATOM 1581 CH2 TRP A1007 -47.799 -17.699 -38.422 1.00150.42 C ANISOU 1581 CH2 TRP A1007 15696 24582 16875 -1298 -2718 1426 C ATOM 1582 N GLU A1008 -51.932 -11.710 -36.049 1.00118.07 N ANISOU 1582 N GLU A1008 11140 21660 12059 -928 -2369 1316 N ATOM 1583 CA GLU A1008 -53.357 -11.671 -36.350 1.00123.04 C ANISOU 1583 CA GLU A1008 11711 22601 12436 -944 -2350 1292 C ATOM 1584 C GLU A1008 -53.695 -10.488 -37.248 1.00113.31 C ANISOU 1584 C GLU A1008 10427 21464 11162 -703 -2181 1264 C ATOM 1585 O GLU A1008 -54.411 -10.636 -38.237 1.00115.47 O ANISOU 1585 O GLU A1008 10688 21873 11311 -645 -2133 1248 O ATOM 1586 CB GLU A1008 -54.170 -11.589 -35.056 1.00113.85 C ANISOU 1586 CB GLU A1008 10493 21646 11120 -1100 -2431 1293 C ATOM 1587 N THR A1009 -53.177 -9.314 -36.900 1.00112.87 N ANISOU 1587 N THR A1009 10341 21334 11210 -565 -2093 1260 N ATOM 1588 CA THR A1009 -53.458 -8.099 -37.660 1.00118.71 C ANISOU 1588 CA THR A1009 11031 22156 11918 -332 -1929 1235 C ATOM 1589 C THR A1009 -52.973 -8.238 -39.101 1.00112.47 C ANISOU 1589 C THR A1009 10289 21227 11218 -182 -1844 1230 C ATOM 1590 O THR A1009 -53.724 -7.988 -40.044 1.00112.66 O ANISOU 1590 O THR A1009 10283 21408 11115 -75 -1763 1211 O ATOM 1591 CB THR A1009 -52.796 -6.861 -37.021 1.00112.19 C ANISOU 1591 CB THR A1009 10177 21230 11220 -214 -1850 1232 C ATOM 1592 OG1 THR A1009 -53.317 -6.661 -35.701 1.00112.40 O ANISOU 1592 OG1 THR A1009 10155 21402 11148 -347 -1919 1234 O ATOM 1593 CG2 THR A1009 -53.067 -5.618 -37.854 1.00111.99 C ANISOU 1593 CG2 THR A1009 10104 21281 11166 33 -1677 1208 C ATOM 1594 N LEU A1010 -51.716 -8.639 -39.262 1.00112.12 N ANISOU 1594 N LEU A1010 10318 20889 11394 -175 -1864 1247 N ATOM 1595 CA LEU A1010 -51.137 -8.841 -40.585 1.00111.93 C ANISOU 1595 CA LEU A1010 10349 20704 11476 -44 -1789 1244 C ATOM 1596 C LEU A1010 -51.964 -9.835 -41.391 1.00112.43 C ANISOU 1596 C LEU A1010 10430 20907 11383 -123 -1832 1238 C ATOM 1597 O LEU A1010 -52.397 -9.536 -42.502 1.00112.51 O ANISOU 1597 O LEU A1010 10427 21001 11318 16 -1733 1220 O ATOM 1598 CB LEU A1010 -49.697 -9.344 -40.462 1.00111.57 C ANISOU 1598 CB LEU A1010 10382 20327 11684 -74 -1834 1267 C ATOM 1599 CG LEU A1010 -48.671 -8.324 -39.966 1.00114.28 C ANISOU 1599 CG LEU A1010 10718 20484 12220 44 -1767 1271 C ATOM 1600 CD1 LEU A1010 -47.347 -9.004 -39.657 1.00110.78 C ANISOU 1600 CD1 LEU A1010 10348 19735 12009 -32 -1844 1298 C ATOM 1601 CD2 LEU A1010 -48.477 -7.220 -40.992 1.00110.67 C ANISOU 1601 CD2 LEU A1010 10245 19994 11812 301 -1591 1249 C ATOM 1602 N ASN A1011 -52.179 -11.016 -40.824 1.00112.80 N ANISOU 1602 N ASN A1011 10506 20977 11377 -347 -1980 1254 N ATOM 1603 CA ASN A1011 -52.951 -12.057 -41.491 1.00113.32 C ANISOU 1603 CA ASN A1011 10593 21170 11294 -446 -2035 1248 C ATOM 1604 C ASN A1011 -54.326 -11.556 -41.916 1.00113.69 C ANISOU 1604 C ASN A1011 10563 21534 11099 -386 -1973 1224 C ATOM 1605 O ASN A1011 -54.738 -11.748 -43.058 1.00113.88 O ANISOU 1605 O ASN A1011 10597 21626 11048 -313 -1918 1210 O ATOM 1606 CB ASN A1011 -53.092 -13.278 -40.580 1.00131.80 C ANISOU 1606 CB ASN A1011 12965 23520 13594 -709 -2208 1269 C ATOM 1607 CG ASN A1011 -51.974 -14.287 -40.777 1.00132.78 C ANISOU 1607 CG ASN A1011 13184 23355 13911 -781 -2276 1292 C ATOM 1608 OD1 ASN A1011 -52.225 -15.486 -40.901 1.00137.11 O ANISOU 1608 OD1 ASN A1011 13777 23916 14402 -938 -2374 1300 O ATOM 1609 ND2 ASN A1011 -50.735 -13.806 -40.822 1.00129.83 N ANISOU 1609 ND2 ASN A1011 12843 22720 13768 -664 -2221 1302 N ATOM 1610 N ASP A1012 -55.031 -10.908 -40.994 1.00122.25 N ANISOU 1610 N ASP A1012 11572 22814 12064 -418 -1980 1218 N ATOM 1611 CA ASP A1012 -56.365 -10.390 -41.275 1.00125.81 C ANISOU 1611 CA ASP A1012 11941 23577 12285 -366 -1925 1196 C ATOM 1612 C ASP A1012 -56.348 -9.428 -42.459 1.00127.97 C ANISOU 1612 C ASP A1012 12195 23854 12574 -112 -1761 1179 C ATOM 1613 O ASP A1012 -57.126 -9.575 -43.401 1.00125.13 O ANISOU 1613 O ASP A1012 11819 23652 12074 -64 -1722 1165 O ATOM 1614 CB ASP A1012 -56.934 -9.688 -40.040 1.00125.86 C ANISOU 1614 CB ASP A1012 11870 23752 12198 -417 -1943 1193 C ATOM 1615 CG ASP A1012 -57.467 -10.664 -39.010 1.00128.23 C ANISOU 1615 CG ASP A1012 12171 24162 12389 -677 -2102 1204 C ATOM 1616 OD1 ASP A1012 -57.148 -11.868 -39.105 1.00127.74 O ANISOU 1616 OD1 ASP A1012 12178 23990 12368 -821 -2204 1219 O ATOM 1617 OD2 ASP A1012 -58.205 -10.226 -38.101 1.00130.10 O ANISOU 1617 OD2 ASP A1012 12340 24593 12500 -739 -2122 1198 O ATOM 1618 N ASN A1013 -55.454 -8.447 -42.408 1.00128.56 N ANISOU 1618 N ASN A1013 12272 23755 12819 48 -1666 1180 N ATOM 1619 CA ASN A1013 -55.359 -7.447 -43.465 1.00128.74 C ANISOU 1619 CA ASN A1013 12278 23766 12871 297 -1505 1165 C ATOM 1620 C ASN A1013 -54.946 -8.064 -44.797 1.00113.13 C ANISOU 1620 C ASN A1013 10371 21656 10958 360 -1472 1164 C ATOM 1621 O ASN A1013 -55.434 -7.660 -45.848 1.00113.26 O ANISOU 1621 O ASN A1013 10367 21776 10889 505 -1373 1149 O ATOM 1622 CB ASN A1013 -54.384 -6.341 -43.059 1.00130.85 C ANISOU 1622 CB ASN A1013 12542 23850 13326 439 -1418 1167 C ATOM 1623 CG ASN A1013 -54.840 -5.598 -41.818 1.00134.60 C ANISOU 1623 CG ASN A1013 12944 24467 13729 397 -1431 1165 C ATOM 1624 OD1 ASN A1013 -55.612 -6.127 -41.018 1.00135.34 O ANISOU 1624 OD1 ASN A1013 13008 24735 13680 217 -1538 1167 O ATOM 1625 ND2 ASN A1013 -54.368 -4.368 -41.650 1.00138.52 N ANISOU 1625 ND2 ASN A1013 13416 24892 14325 562 -1321 1158 N ATOM 1626 N LEU A1014 -54.052 -9.046 -44.751 1.00113.01 N ANISOU 1626 N LEU A1014 10437 21411 11089 251 -1555 1179 N ATOM 1627 CA LEU A1014 -53.641 -9.753 -45.959 1.00113.04 C ANISOU 1627 CA LEU A1014 10514 21281 11156 289 -1535 1178 C ATOM 1628 C LEU A1014 -54.817 -10.530 -46.544 1.00113.68 C ANISOU 1628 C LEU A1014 10583 21596 11015 198 -1580 1167 C ATOM 1629 O LEU A1014 -54.996 -10.574 -47.761 1.00113.81 O ANISOU 1629 O LEU A1014 10618 21631 10992 304 -1506 1155 O ATOM 1630 CB LEU A1014 -52.473 -10.699 -45.668 1.00112.83 C ANISOU 1630 CB LEU A1014 10575 20966 11331 173 -1625 1198 C ATOM 1631 CG LEU A1014 -51.099 -10.059 -45.442 1.00112.19 C ANISOU 1631 CG LEU A1014 10523 20598 11505 287 -1568 1208 C ATOM 1632 CD1 LEU A1014 -50.078 -11.124 -45.074 1.00112.10 C ANISOU 1632 CD1 LEU A1014 10592 20331 11670 144 -1677 1231 C ATOM 1633 CD2 LEU A1014 -50.639 -9.286 -46.670 1.00111.87 C ANISOU 1633 CD2 LEU A1014 10498 20454 11553 528 -1408 1193 C ATOM 1634 N LYS A1015 -55.619 -11.140 -45.676 1.00118.31 N ANISOU 1634 N LYS A1015 11138 22361 11452 -1 -1701 1172 N ATOM 1635 CA LYS A1015 -56.817 -11.846 -46.115 1.00122.38 C ANISOU 1635 CA LYS A1015 11634 23123 11743 -100 -1749 1161 C ATOM 1636 C LYS A1015 -57.756 -10.867 -46.811 1.00122.59 C ANISOU 1636 C LYS A1015 11583 23383 11611 70 -1629 1141 C ATOM 1637 O LYS A1015 -58.280 -11.152 -47.887 1.00117.20 O ANISOU 1637 O LYS A1015 10908 22797 10825 115 -1594 1130 O ATOM 1638 CB LYS A1015 -57.529 -12.509 -44.932 1.00128.41 C ANISOU 1638 CB LYS A1015 12367 24047 12374 -336 -1892 1168 C ATOM 1639 CG LYS A1015 -56.828 -13.747 -44.382 1.00130.90 C ANISOU 1639 CG LYS A1015 12763 24172 12801 -536 -2028 1189 C ATOM 1640 CD LYS A1015 -57.720 -14.497 -43.400 1.00132.69 C ANISOU 1640 CD LYS A1015 12961 24593 12860 -772 -2167 1194 C ATOM 1641 CE LYS A1015 -56.917 -15.160 -42.288 1.00133.39 C ANISOU 1641 CE LYS A1015 13101 24494 13086 -943 -2290 1220 C ATOM 1642 NZ LYS A1015 -56.728 -14.256 -41.117 1.00130.11 N ANISOU 1642 NZ LYS A1015 12635 24086 12716 -928 -2286 1227 N ATOM 1643 N VAL A1016 -57.955 -9.708 -46.191 1.00128.40 N ANISOU 1643 N VAL A1016 12247 24208 12331 166 -1567 1138 N ATOM 1644 CA VAL A1016 -58.799 -8.663 -46.759 1.00114.88 C ANISOU 1644 CA VAL A1016 10457 22710 10481 340 -1448 1122 C ATOM 1645 C VAL A1016 -58.289 -8.251 -48.138 1.00114.64 C ANISOU 1645 C VAL A1016 10465 22553 10539 551 -1319 1116 C ATOM 1646 O VAL A1016 -59.067 -8.101 -49.079 1.00114.99 O ANISOU 1646 O VAL A1016 10481 22768 10441 638 -1259 1104 O ATOM 1647 CB VAL A1016 -58.839 -7.418 -45.845 1.00114.60 C ANISOU 1647 CB VAL A1016 10351 22730 10461 425 -1391 1121 C ATOM 1648 CG1 VAL A1016 -59.486 -6.243 -46.562 1.00114.67 C ANISOU 1648 CG1 VAL A1016 10291 22907 10372 642 -1247 1107 C ATOM 1649 CG2 VAL A1016 -59.577 -7.731 -44.548 1.00129.79 C ANISOU 1649 CG2 VAL A1016 12224 24834 12257 226 -1506 1124 C ATOM 1650 N ILE A1017 -56.975 -8.079 -48.247 1.00149.16 N ANISOU 1650 N ILE A1017 14902 26626 15145 631 -1279 1123 N ATOM 1651 CA ILE A1017 -56.349 -7.644 -49.490 1.00113.77 C ANISOU 1651 CA ILE A1017 10462 21993 10773 834 -1152 1117 C ATOM 1652 C ILE A1017 -56.523 -8.672 -50.602 1.00128.73 C ANISOU 1652 C ILE A1017 12416 23883 12614 790 -1177 1113 C ATOM 1653 O ILE A1017 -56.910 -8.329 -51.720 1.00122.40 O ANISOU 1653 O ILE A1017 11606 23163 11738 931 -1082 1101 O ATOM 1654 CB ILE A1017 -54.841 -7.395 -49.293 1.00113.10 C ANISOU 1654 CB ILE A1017 10440 21572 10961 900 -1120 1127 C ATOM 1655 CG1 ILE A1017 -54.612 -6.123 -48.477 1.00112.71 C ANISOU 1655 CG1 ILE A1017 10333 21517 10973 1005 -1053 1128 C ATOM 1656 CG2 ILE A1017 -54.140 -7.275 -50.638 1.00112.88 C ANISOU 1656 CG2 ILE A1017 10473 21364 11050 1070 -1012 1121 C ATOM 1657 CD1 ILE A1017 -53.171 -5.917 -48.055 1.00112.09 C ANISOU 1657 CD1 ILE A1017 10308 21123 11156 1039 -1042 1139 C ATOM 1658 N GLU A1018 -56.236 -9.931 -50.291 1.00129.97 N ANISOU 1658 N GLU A1018 12632 23942 12807 592 -1304 1121 N ATOM 1659 CA GLU A1018 -56.203 -10.977 -51.308 1.00132.70 C ANISOU 1659 CA GLU A1018 13048 24233 13137 542 -1329 1117 C ATOM 1660 C GLU A1018 -57.590 -11.280 -51.879 1.00135.17 C ANISOU 1660 C GLU A1018 13316 24851 13191 501 -1342 1103 C ATOM 1661 O GLU A1018 -57.703 -11.896 -52.938 1.00136.96 O ANISOU 1661 O GLU A1018 13590 25070 13378 507 -1330 1095 O ATOM 1662 CB GLU A1018 -55.555 -12.250 -50.747 1.00134.60 C ANISOU 1662 CB GLU A1018 13364 24294 13484 334 -1465 1131 C ATOM 1663 CG GLU A1018 -56.523 -13.388 -50.452 1.00142.04 C ANISOU 1663 CG GLU A1018 14301 25429 14239 109 -1597 1130 C ATOM 1664 CD GLU A1018 -55.836 -14.592 -49.830 1.00153.04 C ANISOU 1664 CD GLU A1018 15768 26633 15747 -92 -1730 1147 C ATOM 1665 OE1 GLU A1018 -55.979 -15.705 -50.378 1.00159.16 O ANISOU 1665 OE1 GLU A1018 16601 27395 16479 -204 -1789 1144 O ATOM 1666 OE2 GLU A1018 -55.158 -14.427 -48.793 1.00152.15 O ANISOU 1666 OE2 GLU A1018 15657 26385 15767 -140 -1775 1164 O ATOM 1667 N LYS A1019 -58.638 -10.839 -51.188 1.00135.20 N ANISOU 1667 N LYS A1019 13228 25122 13020 461 -1365 1100 N ATOM 1668 CA LYS A1019 -60.004 -11.039 -51.669 1.00131.87 C ANISOU 1668 CA LYS A1019 12752 25007 12347 428 -1375 1088 C ATOM 1669 C LYS A1019 -60.639 -9.737 -52.158 1.00131.14 C ANISOU 1669 C LYS A1019 12577 25093 12155 640 -1243 1079 C ATOM 1670 O LYS A1019 -61.811 -9.715 -52.537 1.00129.96 O ANISOU 1670 O LYS A1019 12369 25215 11795 637 -1239 1070 O ATOM 1671 CB LYS A1019 -60.882 -11.649 -50.572 1.00130.03 C ANISOU 1671 CB LYS A1019 12471 24975 11958 204 -1510 1090 C ATOM 1672 CG LYS A1019 -61.196 -10.704 -49.420 1.00130.23 C ANISOU 1672 CG LYS A1019 12412 25117 11954 221 -1501 1094 C ATOM 1673 CD LYS A1019 -62.596 -10.939 -48.875 1.00132.03 C ANISOU 1673 CD LYS A1019 12559 25672 11936 83 -1575 1087 C ATOM 1674 CE LYS A1019 -62.768 -12.356 -48.355 1.00132.74 C ANISOU 1674 CE LYS A1019 12692 25768 11976 -180 -1732 1092 C ATOM 1675 NZ LYS A1019 -64.166 -12.622 -47.917 1.00132.84 N ANISOU 1675 NZ LYS A1019 12626 26105 11741 -313 -1800 1083 N ATOM 1676 N AALA A1020 -59.864 -8.658 -52.147 0.49133.06 N ANISOU 1676 N AALA A1020 12818 25184 12552 823 -1135 1083 N ATOM 1677 N BALA A1020 -59.864 -8.658 -52.147 0.51133.02 N ANISOU 1677 N BALA A1020 12814 25180 12548 823 -1135 1083 N ATOM 1678 CA ALA A1020 -60.363 -7.351 -52.560 1.00138.39 C ANISOU 1678 CA ALA A1020 13421 26006 13156 1034 -1003 1077 C ATOM 1679 C ALA A1020 -60.667 -7.321 -54.055 1.00144.27 C ANISOU 1679 C ALA A1020 14183 26804 13830 1168 -918 1068 C ATOM 1680 O AALA A1020 -59.911 -7.857 -54.865 0.49143.75 O ANISOU 1680 O AALA A1020 14204 26536 13878 1190 -902 1067 O ATOM 1681 O BALA A1020 -59.912 -7.858 -54.865 0.51143.74 O ANISOU 1681 O BALA A1020 14202 26535 13877 1190 -902 1067 O ATOM 1682 CB ALA A1020 -59.353 -6.270 -52.211 1.00141.45 C ANISOU 1682 CB ALA A1020 13813 26189 13741 1191 -909 1082 C ATOM 1683 N ASP A1021 -61.781 -6.688 -54.411 1.00149.10 N ANISOU 1683 N ASP A1021 14712 27688 14251 1257 -862 1063 N ATOM 1684 CA ASP A1021 -62.176 -6.547 -55.807 1.00151.51 C ANISOU 1684 CA ASP A1021 15024 28075 14470 1394 -776 1056 C ATOM 1685 C ASP A1021 -61.797 -5.162 -56.325 1.00152.54 C ANISOU 1685 C ASP A1021 15134 28142 14682 1659 -616 1058 C ATOM 1686 O ASP A1021 -61.371 -5.012 -57.471 1.00153.25 O ANISOU 1686 O ASP A1021 15274 28122 14831 1800 -527 1056 O ATOM 1687 CB ASP A1021 -63.684 -6.766 -55.960 1.00148.62 C ANISOU 1687 CB ASP A1021 14577 28058 13833 1326 -818 1051 C ATOM 1688 CG ASP A1021 -64.118 -8.158 -55.540 1.00143.48 C ANISOU 1688 CG ASP A1021 13948 27480 13087 1064 -973 1047 C ATOM 1689 OD1 ASP A1021 -63.322 -9.106 -55.701 1.00140.06 O ANISOU 1689 OD1 ASP A1021 13609 26832 12776 964 -1030 1047 O ATOM 1690 OD2 ASP A1021 -65.258 -8.304 -55.049 1.00141.80 O ANISOU 1690 OD2 ASP A1021 13658 27541 12681 958 -1036 1044 O ATOM 1691 N ASN A1022 -61.946 -4.157 -55.468 1.00149.82 N ANISOU 1691 N ASN A1022 14718 27865 14342 1724 -577 1062 N ATOM 1692 CA ASN A1022 -61.681 -2.773 -55.846 1.00148.52 C ANISOU 1692 CA ASN A1022 14525 27664 14242 1972 -424 1064 C ATOM 1693 C ASN A1022 -60.412 -2.239 -55.192 1.00144.06 C ANISOU 1693 C ASN A1022 13999 26820 13916 2027 -387 1068 C ATOM 1694 O ASN A1022 -59.762 -2.939 -54.415 1.00147.17 O ANISOU 1694 O ASN A1022 14439 27058 14422 1871 -483 1070 O ATOM 1695 CB ASN A1022 -62.873 -1.889 -55.477 1.00155.69 C ANISOU 1695 CB ASN A1022 15316 28873 14964 2034 -387 1064 C ATOM 1696 CG ASN A1022 -63.229 -1.978 -54.007 1.00161.61 C ANISOU 1696 CG ASN A1022 16011 29721 15672 1872 -483 1064 C ATOM 1697 OD1 ASN A1022 -62.778 -1.170 -53.196 1.00163.93 O ANISOU 1697 OD1 ASN A1022 16283 29934 16068 1927 -443 1066 O ATOM 1698 ND2 ASN A1022 -64.039 -2.969 -53.655 1.00163.61 N ANISOU 1698 ND2 ASN A1022 16243 30149 15772 1667 -609 1061 N ATOM 1699 N ALA A1023 -60.065 -0.995 -55.508 1.00139.12 N ANISOU 1699 N ALA A1023 13357 26135 13367 2249 -246 1068 N ATOM 1700 CA ALA A1023 -58.815 -0.407 -55.040 1.00133.66 C ANISOU 1700 CA ALA A1023 12706 25170 12909 2325 -193 1071 C ATOM 1701 C ALA A1023 -58.948 0.216 -53.652 1.00132.06 C ANISOU 1701 C ALA A1023 12438 25028 12711 2279 -217 1072 C ATOM 1702 O ALA A1023 -57.974 0.281 -52.902 1.00128.41 O ANISOU 1702 O ALA A1023 12011 24352 12427 2242 -237 1075 O ATOM 1703 CB ALA A1023 -58.318 0.629 -56.038 1.00133.88 C ANISOU 1703 CB ALA A1023 12753 25089 13027 2584 -28 1070 C ATOM 1704 N ALA A1024 -60.149 0.676 -53.314 1.00135.18 N ANISOU 1704 N ALA A1024 12738 25714 12910 2281 -214 1071 N ATOM 1705 CA ALA A1024 -60.380 1.314 -52.021 1.00141.03 C ANISOU 1705 CA ALA A1024 13412 26536 13637 2242 -230 1070 C ATOM 1706 C ALA A1024 -60.081 0.355 -50.871 1.00141.09 C ANISOU 1706 C ALA A1024 13445 26472 13691 1998 -382 1072 C ATOM 1707 O ALA A1024 -59.461 0.738 -49.879 1.00113.66 O ANISOU 1707 O ALA A1024 9971 22876 10338 1971 -391 1074 O ATOM 1708 CB ALA A1024 -61.811 1.821 -51.930 1.00148.34 C ANISOU 1708 CB ALA A1024 14232 27803 14329 2271 -210 1067 C ATOM 1709 N GLN A1025 -60.526 -0.891 -51.010 1.00143.30 N ANISOU 1709 N GLN A1025 13746 26830 13872 1819 -500 1073 N ATOM 1710 CA GLN A1025 -60.289 -1.907 -49.990 1.00146.50 C ANISOU 1710 CA GLN A1025 14180 27173 14310 1578 -651 1077 C ATOM 1711 C GLN A1025 -58.796 -2.153 -49.808 1.00139.91 C ANISOU 1711 C GLN A1025 13436 25993 13731 1568 -662 1084 C ATOM 1712 O GLN A1025 -58.303 -2.227 -48.683 1.00133.77 O ANISOU 1712 O GLN A1025 12665 25117 13047 1460 -728 1089 O ATOM 1713 CB GLN A1025 -60.985 -3.218 -50.362 1.00154.48 C ANISOU 1713 CB GLN A1025 15208 28314 15175 1405 -764 1076 C ATOM 1714 CG GLN A1025 -62.504 -3.149 -50.333 1.00162.36 C ANISOU 1714 CG GLN A1025 16111 29665 15912 1367 -783 1070 C ATOM 1715 CD GLN A1025 -63.149 -4.518 -50.442 1.00167.37 C ANISOU 1715 CD GLN A1025 16763 30420 16411 1157 -914 1069 C ATOM 1716 OE1 GLN A1025 -63.429 -5.001 -51.539 1.00165.32 O ANISOU 1716 OE1 GLN A1025 16530 30202 16083 1183 -902 1065 O ATOM 1717 NE2 GLN A1025 -63.387 -5.151 -49.298 1.00171.41 N ANISOU 1717 NE2 GLN A1025 17261 30985 16880 945 -1040 1071 N ATOM 1718 N VAL A1026 -58.083 -2.284 -50.922 1.00140.72 N ANISOU 1718 N VAL A1026 13608 25913 13946 1679 -598 1084 N ATOM 1719 CA VAL A1026 -56.643 -2.503 -50.888 1.00139.05 C ANISOU 1719 CA VAL A1026 13483 25367 13984 1687 -597 1090 C ATOM 1720 C VAL A1026 -55.949 -1.349 -50.175 1.00141.04 C ANISOU 1720 C VAL A1026 13715 25495 14380 1799 -521 1091 C ATOM 1721 O VAL A1026 -55.142 -1.562 -49.272 1.00139.15 O ANISOU 1721 O VAL A1026 13505 25082 14285 1703 -584 1098 O ATOM 1722 CB VAL A1026 -56.061 -2.637 -52.308 1.00135.01 C ANISOU 1722 CB VAL A1026 13041 24696 13559 1822 -514 1087 C ATOM 1723 N LYS A1027 -56.274 -0.127 -50.583 1.00146.52 N ANISOU 1723 N LYS A1027 14357 26281 15031 2003 -385 1084 N ATOM 1724 CA LYS A1027 -55.686 1.063 -49.984 1.00149.51 C ANISOU 1724 CA LYS A1027 14713 26558 15534 2127 -297 1083 C ATOM 1725 C LYS A1027 -56.076 1.184 -48.514 1.00155.73 C ANISOU 1725 C LYS A1027 15444 27461 16267 1986 -379 1084 C ATOM 1726 O LYS A1027 -55.287 1.644 -47.689 1.00153.63 O ANISOU 1726 O LYS A1027 15187 27037 16148 1987 -372 1085 O ATOM 1727 CB LYS A1027 -56.130 2.314 -50.743 1.00148.65 C ANISOU 1727 CB LYS A1027 14557 26562 15362 2367 -136 1076 C ATOM 1728 N ASP A1028 -57.295 0.762 -48.193 1.00163.61 N ANISOU 1728 N ASP A1028 16382 28731 17049 1862 -455 1082 N ATOM 1729 CA ASP A1028 -57.811 0.863 -46.832 1.00169.83 C ANISOU 1729 CA ASP A1028 17110 29658 17757 1725 -532 1081 C ATOM 1730 C ASP A1028 -57.126 -0.136 -45.904 1.00168.51 C ANISOU 1730 C ASP A1028 16997 29332 17697 1508 -676 1091 C ATOM 1731 O ASP A1028 -56.801 0.187 -44.760 1.00169.47 O ANISOU 1731 O ASP A1028 17104 29405 17883 1443 -709 1093 O ATOM 1732 CB ASP A1028 -59.324 0.628 -46.820 1.00175.63 C ANISOU 1732 CB ASP A1028 17768 30733 18229 1650 -574 1077 C ATOM 1733 CG ASP A1028 -59.915 0.694 -45.423 1.00180.48 C ANISOU 1733 CG ASP A1028 18321 31504 18751 1501 -654 1074 C ATOM 1734 OD1 ASP A1028 -59.916 -0.343 -44.725 1.00180.83 O ANISOU 1734 OD1 ASP A1028 18389 31538 18780 1281 -795 1080 O ATOM 1735 OD2 ASP A1028 -60.387 1.780 -45.026 1.00182.71 O ANISOU 1735 OD2 ASP A1028 18532 31917 18973 1602 -573 1067 O ATOM 1736 N ALA A1029 -56.899 -1.346 -46.405 1.00165.64 N ANISOU 1736 N ALA A1029 16698 28884 17352 1396 -761 1098 N ATOM 1737 CA ALA A1029 -56.326 -2.417 -45.598 1.00160.60 C ANISOU 1737 CA ALA A1029 16113 28107 16801 1180 -906 1111 C ATOM 1738 C ALA A1029 -54.800 -2.388 -45.622 1.00152.50 C ANISOU 1738 C ALA A1029 15165 26737 16042 1231 -885 1119 C ATOM 1739 O ALA A1029 -54.149 -3.355 -45.225 1.00150.09 O ANISOU 1739 O ALA A1029 14918 26269 15838 1076 -995 1132 O ATOM 1740 CB ALA A1029 -56.833 -3.766 -46.086 1.00163.37 C ANISOU 1740 CB ALA A1029 16496 28535 17042 1026 -1011 1114 C ATOM 1741 N LEU A1030 -54.233 -1.278 -46.085 1.00147.15 N ANISOU 1741 N LEU A1030 14486 25948 15477 1447 -742 1113 N ATOM 1742 CA LEU A1030 -52.785 -1.145 -46.185 1.00141.63 C ANISOU 1742 CA LEU A1030 13856 24924 15032 1516 -706 1119 C ATOM 1743 C LEU A1030 -52.254 -0.157 -45.151 1.00141.90 C ANISOU 1743 C LEU A1030 13861 24880 15175 1559 -670 1119 C ATOM 1744 O LEU A1030 -51.178 -0.357 -44.586 1.00140.18 O ANISOU 1744 O LEU A1030 13690 24429 15144 1502 -714 1129 O ATOM 1745 CB LEU A1030 -52.397 -0.686 -47.590 1.00138.23 C ANISOU 1745 CB LEU A1030 13459 24392 14671 1732 -568 1112 C ATOM 1746 CG LEU A1030 -51.208 -1.399 -48.238 1.00136.46 C ANISOU 1746 CG LEU A1030 13330 23873 14645 1733 -579 1119 C ATOM 1747 CD1 LEU A1030 -51.473 -2.892 -48.389 1.00130.77 C ANISOU 1747 CD1 LEU A1030 12652 23175 13859 1538 -714 1127 C ATOM 1748 CD2 LEU A1030 -50.896 -0.770 -49.587 1.00136.86 C ANISOU 1748 CD2 LEU A1030 13405 23843 14752 1963 -426 1109 C ATOM 1749 N THR A1031 -53.010 0.909 -44.909 1.00143.16 N ANISOU 1749 N THR A1031 13945 25234 15217 1658 -588 1107 N ATOM 1750 CA THR A1031 -52.620 1.910 -43.925 1.00143.25 C ANISOU 1750 CA THR A1031 13924 25195 15310 1701 -546 1104 C ATOM 1751 C THR A1031 -52.624 1.303 -42.526 1.00148.27 C ANISOU 1751 C THR A1031 14553 25845 15937 1471 -694 1113 C ATOM 1752 O THR A1031 -51.820 1.680 -41.673 1.00150.97 O ANISOU 1752 O THR A1031 14907 26034 16423 1451 -703 1117 O ATOM 1753 CB THR A1031 -53.569 3.121 -43.946 1.00140.55 C ANISOU 1753 CB THR A1031 13497 25085 14820 1844 -432 1089 C ATOM 1754 OG1 THR A1031 -53.748 3.570 -45.295 1.00138.77 O ANISOU 1754 OG1 THR A1031 13275 24884 14568 2043 -306 1082 O ATOM 1755 CG2 THR A1031 -53.009 4.257 -43.100 1.00138.79 C ANISOU 1755 CG2 THR A1031 13252 24772 14709 1922 -363 1082 C ATOM 1756 N LYS A1032 -53.533 0.360 -42.298 1.00148.96 N ANISOU 1756 N LYS A1032 14623 26121 15855 1296 -810 1117 N ATOM 1757 CA LYS A1032 -53.618 -0.329 -41.017 1.00151.57 C ANISOU 1757 CA LYS A1032 14951 26479 16159 1064 -960 1128 C ATOM 1758 C LYS A1032 -52.364 -1.159 -40.761 1.00158.27 C ANISOU 1758 C LYS A1032 15883 27037 17215 960 -1049 1147 C ATOM 1759 O LYS A1032 -51.888 -1.245 -39.630 1.00163.33 O ANISOU 1759 O LYS A1032 16530 27593 17934 840 -1127 1157 O ATOM 1760 CB LYS A1032 -54.854 -1.229 -40.976 1.00149.79 C ANISOU 1760 CB LYS A1032 14695 26510 15708 904 -1060 1128 C ATOM 1761 CG LYS A1032 -56.171 -0.473 -40.996 1.00150.13 C ANISOU 1761 CG LYS A1032 14646 26862 15534 973 -994 1111 C ATOM 1762 CD LYS A1032 -57.351 -1.421 -41.136 1.00151.31 C ANISOU 1762 CD LYS A1032 14769 27254 15467 825 -1088 1111 C ATOM 1763 CE LYS A1032 -58.663 -0.664 -41.210 1.00151.25 C ANISOU 1763 CE LYS A1032 14666 27555 15247 901 -1018 1095 C ATOM 1764 NZ LYS A1032 -59.796 -1.553 -41.571 1.00152.62 N ANISOU 1764 NZ LYS A1032 14814 27960 15213 784 -1094 1093 N ATOM 1765 N MET A1033 -51.834 -1.772 -41.816 1.00159.91 N ANISOU 1765 N MET A1033 16154 27094 17510 1004 -1038 1152 N ATOM 1766 CA MET A1033 -50.609 -2.558 -41.705 1.00157.15 C ANISOU 1766 CA MET A1033 15885 26458 17367 923 -1112 1170 C ATOM 1767 C MET A1033 -49.432 -1.650 -41.375 1.00156.72 C ANISOU 1767 C MET A1033 15845 26172 17529 1042 -1036 1171 C ATOM 1768 O MET A1033 -48.451 -2.084 -40.770 1.00159.61 O ANISOU 1768 O MET A1033 16258 26325 18063 949 -1112 1188 O ATOM 1769 CB MET A1033 -50.323 -3.305 -43.008 1.00154.20 C ANISOU 1769 CB MET A1033 15574 25977 17037 969 -1096 1172 C ATOM 1770 CG MET A1033 -51.430 -4.247 -43.443 1.00152.68 C ANISOU 1770 CG MET A1033 15373 25999 16638 855 -1167 1170 C ATOM 1771 SD MET A1033 -50.952 -5.292 -44.832 1.00128.77 S ANISOU 1771 SD MET A1033 12433 22812 13683 871 -1169 1173 S ATOM 1772 CE MET A1033 -49.739 -6.359 -44.059 1.00110.86 C ANISOU 1772 CE MET A1033 10242 20259 11622 689 -1309 1199 C ATOM 1773 N ARG A1034 -49.536 -0.389 -41.779 1.00152.31 N ANISOU 1773 N ARG A1034 15248 25656 16967 1248 -886 1154 N ATOM 1774 CA ARG A1034 -48.483 0.588 -41.535 1.00151.07 C ANISOU 1774 CA ARG A1034 15101 25295 17006 1378 -796 1151 C ATOM 1775 C ARG A1034 -48.575 1.122 -40.107 1.00157.07 C ANISOU 1775 C ARG A1034 15816 26115 17750 1292 -838 1151 C ATOM 1776 O ARG A1034 -48.765 2.319 -39.892 1.00161.16 O ANISOU 1776 O ARG A1034 16285 26702 18246 1420 -732 1136 O ATOM 1777 CB ARG A1034 -48.593 1.737 -42.538 1.00146.26 C ANISOU 1777 CB ARG A1034 14470 24712 16391 1633 -615 1132 C ATOM 1778 CG ARG A1034 -47.310 2.527 -42.729 1.00145.34 C ANISOU 1778 CG ARG A1034 14388 24326 16509 1789 -512 1130 C ATOM 1779 CD ARG A1034 -47.345 3.332 -44.020 1.00143.77 C ANISOU 1779 CD ARG A1034 14189 24123 16313 2030 -345 1115 C ATOM 1780 NE ARG A1034 -46.049 3.934 -44.329 1.00144.43 N ANISOU 1780 NE ARG A1034 14316 23928 16631 2172 -250 1113 N ATOM 1781 CZ ARG A1034 -45.658 5.143 -43.933 1.00147.91 C ANISOU 1781 CZ ARG A1034 14732 24315 17153 2296 -150 1102 C ATOM 1782 NH1 ARG A1034 -46.458 5.911 -43.203 1.00149.53 N ANISOU 1782 NH1 ARG A1034 14868 24722 17224 2299 -127 1093 N ATOM 1783 NH2 ARG A1034 -44.457 5.590 -44.272 1.00146.89 N ANISOU 1783 NH2 ARG A1034 14647 23926 17240 2416 -69 1100 N ATOM 1784 N ALA A1035 -48.439 0.224 -39.136 1.00151.89 N ANISOU 1784 N ALA A1035 15177 25431 17103 1074 -993 1169 N ATOM 1785 CA ALA A1035 -48.533 0.591 -37.728 1.00135.92 C ANISOU 1785 CA ALA A1035 13116 23466 15059 965 -1050 1171 C ATOM 1786 C ALA A1035 -47.595 -0.270 -36.892 1.00130.19 C ANISOU 1786 C ALA A1035 12445 22538 14485 787 -1189 1196 C ATOM 1787 O ALA A1035 -46.478 -0.574 -37.313 1.00129.15 O ANISOU 1787 O ALA A1035 12373 22149 14550 825 -1187 1208 O ATOM 1788 CB ALA A1035 -49.962 0.440 -37.240 1.00109.82 C ANISOU 1788 CB ALA A1035 9748 20479 11500 854 -1103 1163 C ATOM 1789 N LYS A1059 -30.335 -1.245 -34.615 1.00128.83 N ANISOU 1789 N LYS A1059 12779 18766 17404 888 -1415 1412 N ATOM 1790 CA LYS A1059 -29.994 -1.188 -36.031 1.00124.81 C ANISOU 1790 CA LYS A1059 12300 18144 16978 1062 -1291 1395 C ATOM 1791 C LYS A1059 -30.713 -2.287 -36.801 1.00128.81 C ANISOU 1791 C LYS A1059 12839 18744 17360 1003 -1338 1401 C ATOM 1792 O LYS A1059 -31.415 -2.019 -37.777 1.00130.65 O ANISOU 1792 O LYS A1059 13068 19100 17474 1120 -1233 1374 O ATOM 1793 CB LYS A1059 -28.482 -1.326 -36.219 1.00121.03 C ANISOU 1793 CB LYS A1059 11857 17345 16785 1110 -1284 1412 C ATOM 1794 N ASP A1060 -30.537 -3.526 -36.355 1.00130.52 N ANISOU 1794 N ASP A1060 13085 18901 17604 818 -1498 1436 N ATOM 1795 CA ASP A1060 -31.149 -4.671 -37.016 1.00137.22 C ANISOU 1795 CA ASP A1060 13970 19822 18346 742 -1556 1444 C ATOM 1796 C ASP A1060 -32.655 -4.696 -36.768 1.00141.48 C ANISOU 1796 C ASP A1060 14474 20682 18600 666 -1585 1431 C ATOM 1797 O ASP A1060 -33.417 -5.235 -37.571 1.00144.02 O ANISOU 1797 O ASP A1060 14810 21122 18787 667 -1574 1421 O ATOM 1798 CB ASP A1060 -30.517 -5.970 -36.515 1.00142.59 C ANISOU 1798 CB ASP A1060 14692 20344 19140 560 -1722 1488 C ATOM 1799 CG ASP A1060 -30.670 -7.111 -37.501 1.00149.90 C ANISOU 1799 CG ASP A1060 15671 21234 20049 532 -1748 1494 C ATOM 1800 OD1 ASP A1060 -30.571 -6.863 -38.722 1.00153.83 O ANISOU 1800 OD1 ASP A1060 16188 21682 20579 694 -1619 1469 O ATOM 1801 OD2 ASP A1060 -30.888 -8.258 -37.056 1.00152.23 O ANISOU 1801 OD2 ASP A1060 15991 21549 20299 347 -1895 1523 O ATOM 1802 N PHE A1061 -33.076 -4.110 -35.652 1.00141.33 N ANISOU 1802 N PHE A1061 14408 20802 18490 598 -1621 1430 N ATOM 1803 CA PHE A1061 -34.488 -4.057 -35.296 1.00137.46 C ANISOU 1803 CA PHE A1061 13878 20619 17733 523 -1648 1417 C ATOM 1804 C PHE A1061 -35.247 -3.135 -36.243 1.00133.52 C ANISOU 1804 C PHE A1061 13348 20276 17107 712 -1483 1377 C ATOM 1805 O PHE A1061 -36.293 -3.501 -36.779 1.00132.13 O ANISOU 1805 O PHE A1061 13166 20295 16743 697 -1480 1366 O ATOM 1806 CB PHE A1061 -34.650 -3.569 -33.855 1.00135.74 C ANISOU 1806 CB PHE A1061 13617 20491 17468 414 -1716 1424 C ATOM 1807 CG PHE A1061 -36.081 -3.460 -33.407 1.00138.17 C ANISOU 1807 CG PHE A1061 13880 21113 17506 334 -1742 1410 C ATOM 1808 CD1 PHE A1061 -36.747 -4.562 -32.896 1.00139.73 C ANISOU 1808 CD1 PHE A1061 14088 21433 17571 128 -1893 1432 C ATOM 1809 CD2 PHE A1061 -36.758 -2.254 -33.490 1.00140.05 C ANISOU 1809 CD2 PHE A1061 14064 21522 17624 465 -1615 1375 C ATOM 1810 CE1 PHE A1061 -38.062 -4.464 -32.480 1.00141.33 C ANISOU 1810 CE1 PHE A1061 14247 21925 17527 53 -1915 1418 C ATOM 1811 CE2 PHE A1061 -38.073 -2.150 -33.076 1.00140.48 C ANISOU 1811 CE2 PHE A1061 14075 21867 17435 393 -1637 1362 C ATOM 1812 CZ PHE A1061 -38.726 -3.256 -32.570 1.00141.90 C ANISOU 1812 CZ PHE A1061 14264 22168 17485 186 -1788 1383 C ATOM 1813 N ARG A1062 -34.709 -1.937 -36.445 1.00131.37 N ANISOU 1813 N ARG A1062 13056 19919 16939 890 -1346 1356 N ATOM 1814 CA ARG A1062 -35.354 -0.939 -37.290 1.00134.24 C ANISOU 1814 CA ARG A1062 13389 20419 17195 1082 -1182 1319 C ATOM 1815 C ARG A1062 -35.326 -1.341 -38.763 1.00139.87 C ANISOU 1815 C ARG A1062 14143 21074 17927 1196 -1105 1310 C ATOM 1816 O ARG A1062 -36.105 -0.826 -39.566 1.00141.42 O ANISOU 1816 O ARG A1062 14319 21426 17988 1323 -995 1284 O ATOM 1817 CB ARG A1062 -34.677 0.422 -37.111 1.00130.95 C ANISOU 1817 CB ARG A1062 12948 19901 16905 1240 -1056 1301 C ATOM 1818 N HIS A1063 -34.431 -2.259 -39.116 1.00139.75 N ANISOU 1818 N HIS A1063 14185 20836 18078 1151 -1163 1331 N ATOM 1819 CA HIS A1063 -34.300 -2.696 -40.501 1.00136.67 C ANISOU 1819 CA HIS A1063 13839 20366 17722 1252 -1094 1323 C ATOM 1820 C HIS A1063 -35.587 -3.362 -40.980 1.00133.13 C ANISOU 1820 C HIS A1063 13388 20157 17036 1186 -1129 1316 C ATOM 1821 O HIS A1063 -36.098 -3.044 -42.053 1.00135.31 O ANISOU 1821 O HIS A1063 13664 20522 17225 1323 -1017 1293 O ATOM 1822 CB HIS A1063 -33.123 -3.659 -40.657 1.00136.60 C ANISOU 1822 CB HIS A1063 13891 20076 17932 1190 -1167 1349 C ATOM 1823 CG HIS A1063 -32.738 -3.912 -42.081 1.00137.06 C ANISOU 1823 CG HIS A1063 13998 20005 18073 1323 -1071 1337 C ATOM 1824 ND1 HIS A1063 -32.374 -2.902 -42.947 1.00135.22 N ANISOU 1824 ND1 HIS A1063 13763 19699 17915 1543 -900 1310 N ATOM 1825 CD2 HIS A1063 -32.661 -5.061 -42.795 1.00137.08 C ANISOU 1825 CD2 HIS A1063 14056 19936 18094 1264 -1121 1347 C ATOM 1826 CE1 HIS A1063 -32.090 -3.416 -44.127 1.00133.71 C ANISOU 1826 CE1 HIS A1063 13623 19398 17783 1613 -849 1304 C ATOM 1827 NE2 HIS A1063 -32.256 -4.726 -44.064 1.00134.09 N ANISOU 1827 NE2 HIS A1063 13706 19444 17798 1448 -980 1326 N ATOM 1828 N GLY A1064 -36.105 -4.287 -40.179 1.00129.90 N ANISOU 1828 N GLY A1064 12978 19855 16523 975 -1286 1338 N ATOM 1829 CA GLY A1064 -37.358 -4.946 -40.499 1.00129.74 C ANISOU 1829 CA GLY A1064 12952 20074 16271 891 -1332 1333 C ATOM 1830 C GLY A1064 -38.479 -3.940 -40.667 1.00131.21 C ANISOU 1830 C GLY A1064 13075 20523 16254 997 -1230 1303 C ATOM 1831 O GLY A1064 -39.357 -4.110 -41.512 1.00130.47 O ANISOU 1831 O GLY A1064 12978 20591 16003 1039 -1188 1288 O ATOM 1832 N PHE A1065 -38.448 -2.886 -39.859 1.00135.25 N ANISOU 1832 N PHE A1065 13539 21080 16772 1040 -1190 1295 N ATOM 1833 CA PHE A1065 -39.451 -1.831 -39.941 1.00137.79 C ANISOU 1833 CA PHE A1065 13799 21640 16915 1148 -1087 1268 C ATOM 1834 C PHE A1065 -39.333 -1.082 -41.264 1.00141.41 C ANISOU 1834 C PHE A1065 14264 22059 17407 1385 -912 1243 C ATOM 1835 O PHE A1065 -40.326 -0.880 -41.961 1.00142.99 O ANISOU 1835 O PHE A1065 14441 22459 17431 1457 -848 1226 O ATOM 1836 CB PHE A1065 -39.299 -0.857 -38.771 1.00135.54 C ANISOU 1836 CB PHE A1065 13466 21378 16653 1145 -1077 1265 C ATOM 1837 N ASP A1066 -38.115 -0.671 -41.605 1.00140.43 N ANISOU 1837 N ASP A1066 14172 21675 17508 1505 -836 1243 N ATOM 1838 CA ASP A1066 -37.870 0.036 -42.856 1.00139.12 C ANISOU 1838 CA ASP A1066 14021 21442 17398 1731 -669 1221 C ATOM 1839 C ASP A1066 -38.327 -0.794 -44.049 1.00135.26 C ANISOU 1839 C ASP A1066 13568 20999 16824 1742 -664 1218 C ATOM 1840 O ASP A1066 -39.005 -0.290 -44.944 1.00137.40 O ANISOU 1840 O ASP A1066 13824 21406 16977 1879 -554 1198 O ATOM 1841 CB ASP A1066 -36.385 0.374 -42.998 1.00144.16 C ANISOU 1841 CB ASP A1066 14696 21768 18309 1826 -612 1225 C ATOM 1842 CG ASP A1066 -35.938 1.446 -42.026 1.00153.04 C ANISOU 1842 CG ASP A1066 15782 22850 19515 1864 -576 1220 C ATOM 1843 OD1 ASP A1066 -36.543 1.551 -40.938 1.00155.18 O ANISOU 1843 OD1 ASP A1066 16011 23282 19670 1744 -654 1225 O ATOM 1844 OD2 ASP A1066 -34.984 2.184 -42.351 1.00157.11 O ANISOU 1844 OD2 ASP A1066 16312 23173 20210 2011 -469 1211 O ATOM 1845 N ILE A1067 -37.950 -2.069 -44.054 1.00128.25 N ANISOU 1845 N ILE A1067 12732 19998 16001 1596 -784 1239 N ATOM 1846 CA ILE A1067 -38.324 -2.974 -45.132 1.00124.13 C ANISOU 1846 CA ILE A1067 12252 19504 15409 1585 -792 1237 C ATOM 1847 C ILE A1067 -39.840 -3.075 -45.268 1.00122.19 C ANISOU 1847 C ILE A1067 11963 19579 14882 1542 -808 1226 C ATOM 1848 O ILE A1067 -40.390 -2.828 -46.340 1.00119.66 O ANISOU 1848 O ILE A1067 11643 19359 14464 1666 -709 1208 O ATOM 1849 CB ILE A1067 -37.733 -4.379 -44.909 1.00106.97 C ANISOU 1849 CB ILE A1067 10135 17169 13338 1407 -936 1264 C ATOM 1850 CG1 ILE A1067 -36.261 -4.397 -45.328 1.00126.11 C ANISOU 1850 CG1 ILE A1067 12613 19264 16038 1493 -888 1270 C ATOM 1851 CG2 ILE A1067 -38.514 -5.420 -45.698 1.00107.38 C ANISOU 1851 CG2 ILE A1067 10218 17339 13243 1335 -981 1262 C ATOM 1852 CD1 ILE A1067 -35.547 -5.697 -45.026 1.00106.78 C ANISOU 1852 CD1 ILE A1067 10220 16632 13721 1327 -1026 1300 C ATOM 1853 N LEU A1068 -40.510 -3.435 -44.178 1.00123.55 N ANISOU 1853 N LEU A1068 12100 19915 14928 1365 -931 1238 N ATOM 1854 CA LEU A1068 -41.957 -3.612 -44.201 1.00126.43 C ANISOU 1854 CA LEU A1068 12422 20588 15027 1302 -961 1229 C ATOM 1855 C LEU A1068 -42.650 -2.318 -44.609 1.00129.96 C ANISOU 1855 C LEU A1068 12812 21210 15356 1488 -814 1204 C ATOM 1856 O LEU A1068 -43.446 -2.305 -45.546 1.00131.68 O ANISOU 1856 O LEU A1068 13021 21581 15430 1562 -754 1190 O ATOM 1857 CB LEU A1068 -42.467 -4.069 -42.833 1.00127.17 C ANISOU 1857 CB LEU A1068 12485 20814 15021 1087 -1111 1245 C ATOM 1858 CG LEU A1068 -43.575 -5.122 -42.878 1.00126.37 C ANISOU 1858 CG LEU A1068 12380 20923 14710 925 -1218 1249 C ATOM 1859 CD1 LEU A1068 -43.014 -6.465 -43.325 1.00129.32 C ANISOU 1859 CD1 LEU A1068 12831 21125 15179 818 -1306 1267 C ATOM 1860 CD2 LEU A1068 -44.258 -5.245 -41.525 1.00126.17 C ANISOU 1860 CD2 LEU A1068 12307 21075 14555 747 -1334 1259 C ATOM 1861 N VAL A1069 -42.344 -1.234 -43.905 1.00130.91 N ANISOU 1861 N VAL A1069 12893 21308 15539 1561 -757 1199 N ATOM 1862 CA VAL A1069 -42.934 0.065 -44.206 1.00129.89 C ANISOU 1862 CA VAL A1069 12708 21330 15312 1741 -614 1176 C ATOM 1863 C VAL A1069 -42.668 0.450 -45.659 1.00131.20 C ANISOU 1863 C VAL A1069 12905 21414 15530 1948 -469 1161 C ATOM 1864 O VAL A1069 -43.539 0.999 -46.335 1.00128.11 O ANISOU 1864 O VAL A1069 12480 21209 14985 2065 -378 1145 O ATOM 1865 CB VAL A1069 -42.382 1.161 -43.276 1.00122.08 C ANISOU 1865 CB VAL A1069 11688 20270 14429 1796 -567 1172 C ATOM 1866 CG1 VAL A1069 -42.817 2.537 -43.755 1.00125.57 C ANISOU 1866 CG1 VAL A1069 12083 20823 14804 2010 -399 1148 C ATOM 1867 CG2 VAL A1069 -42.840 0.924 -41.844 1.00114.70 C ANISOU 1867 CG2 VAL A1069 10713 19462 13405 1602 -697 1183 C ATOM 1868 N GLY A1070 -41.461 0.162 -46.132 1.00130.05 N ANISOU 1868 N GLY A1070 12824 20988 15602 1992 -450 1167 N ATOM 1869 CA GLY A1070 -41.102 0.428 -47.512 1.00130.02 C ANISOU 1869 CA GLY A1070 12858 20879 15664 2177 -318 1154 C ATOM 1870 C GLY A1070 -41.988 -0.344 -48.471 1.00126.84 C ANISOU 1870 C GLY A1070 12471 20629 15093 2152 -335 1150 C ATOM 1871 O GLY A1070 -42.465 0.200 -49.466 1.00128.26 O ANISOU 1871 O GLY A1070 12642 20904 15188 2309 -217 1135 O ATOM 1872 N GLN A1071 -42.209 -1.618 -48.167 1.00124.11 N ANISOU 1872 N GLN A1071 12148 20308 14699 1952 -482 1165 N ATOM 1873 CA GLN A1071 -43.055 -2.470 -48.993 1.00107.98 C ANISOU 1873 CA GLN A1071 10123 18411 12494 1900 -515 1162 C ATOM 1874 C GLN A1071 -44.509 -2.015 -48.938 1.00128.88 C ANISOU 1874 C GLN A1071 12698 21392 14879 1912 -496 1151 C ATOM 1875 O GLN A1071 -45.209 -2.030 -49.949 1.00128.10 O ANISOU 1875 O GLN A1071 12598 21427 14650 1990 -436 1140 O ATOM 1876 CB GLN A1071 -42.941 -3.926 -48.543 1.00108.24 C ANISOU 1876 CB GLN A1071 10197 18391 12539 1671 -682 1182 C ATOM 1877 CG GLN A1071 -41.595 -4.559 -48.853 1.00108.00 C ANISOU 1877 CG GLN A1071 10245 18039 12752 1662 -699 1193 C ATOM 1878 CD GLN A1071 -41.449 -5.940 -48.250 1.00108.26 C ANISOU 1878 CD GLN A1071 10315 18015 12806 1431 -870 1215 C ATOM 1879 OE1 GLN A1071 -42.125 -6.278 -47.280 1.00124.02 O ANISOU 1879 OE1 GLN A1071 12275 20173 14676 1270 -983 1226 O ATOM 1880 NE2 GLN A1071 -40.564 -6.749 -48.824 1.00108.23 N ANISOU 1880 NE2 GLN A1071 10384 17777 12960 1413 -888 1223 N ATOM 1881 N ILE A1072 -44.963 -1.612 -47.756 1.00108.37 N ANISOU 1881 N ILE A1072 10040 18930 12206 1833 -548 1155 N ATOM 1882 CA ILE A1072 -46.319 -1.103 -47.601 1.00122.05 C ANISOU 1882 CA ILE A1072 11697 20978 13699 1846 -528 1144 C ATOM 1883 C ILE A1072 -46.500 0.138 -48.468 1.00123.64 C ANISOU 1883 C ILE A1072 11871 21229 13876 2092 -351 1126 C ATOM 1884 O ILE A1072 -47.523 0.302 -49.135 1.00118.15 O ANISOU 1884 O ILE A1072 11144 20751 12997 2153 -304 1117 O ATOM 1885 CB ILE A1072 -46.624 -0.737 -46.138 1.00121.95 C ANISOU 1885 CB ILE A1072 11626 21072 13637 1737 -597 1149 C ATOM 1886 CG1 ILE A1072 -46.621 -1.989 -45.255 1.00108.95 C ANISOU 1886 CG1 ILE A1072 10001 19413 11980 1482 -779 1168 C ATOM 1887 CG2 ILE A1072 -47.966 -0.029 -46.039 1.00109.04 C ANISOU 1887 CG2 ILE A1072 9910 19751 11770 1783 -551 1136 C ATOM 1888 CD1 ILE A1072 -47.729 -2.976 -45.568 1.00157.09 C ANISOU 1888 CD1 ILE A1072 16093 25726 17870 1353 -865 1169 C ATOM 1889 N ASP A1073 -45.496 1.010 -48.454 1.00130.82 N ANISOU 1889 N ASP A1073 12795 21936 14973 2232 -253 1123 N ATOM 1890 CA ASP A1073 -45.523 2.228 -49.254 1.00132.44 C ANISOU 1890 CA ASP A1073 12983 22156 15183 2472 -80 1107 C ATOM 1891 C ASP A1073 -45.461 1.889 -50.740 1.00121.74 C ANISOU 1891 C ASP A1073 11678 20748 13828 2578 -10 1101 C ATOM 1892 O ASP A1073 -46.115 2.534 -51.559 1.00118.63 O ANISOU 1892 O ASP A1073 11258 20496 13318 2728 98 1091 O ATOM 1893 CB ASP A1073 -44.355 3.142 -48.876 1.00139.99 C ANISOU 1893 CB ASP A1073 13952 22882 16358 2582 1 1104 C ATOM 1894 CG ASP A1073 -44.472 3.688 -47.463 1.00143.49 C ANISOU 1894 CG ASP A1073 14339 23391 16787 2505 -44 1106 C ATOM 1895 OD1 ASP A1073 -45.610 3.918 -47.002 1.00141.98 O ANISOU 1895 OD1 ASP A1073 14084 23464 16397 2460 -67 1103 O ATOM 1896 OD2 ASP A1073 -43.424 3.889 -46.815 1.00147.28 O ANISOU 1896 OD2 ASP A1073 14841 23662 17458 2489 -55 1111 O ATOM 1897 N ASP A1074 -44.671 0.876 -51.080 1.00118.19 N ANISOU 1897 N ASP A1074 11301 20095 13510 2499 -72 1109 N ATOM 1898 CA ASP A1074 -44.561 0.422 -52.462 1.00119.05 C ANISOU 1898 CA ASP A1074 11467 20141 13627 2578 -17 1104 C ATOM 1899 C ASP A1074 -45.909 -0.079 -52.971 1.00117.91 C ANISOU 1899 C ASP A1074 11296 20275 13231 2525 -52 1100 C ATOM 1900 O ASP A1074 -46.334 0.265 -54.075 1.00108.76 O ANISOU 1900 O ASP A1074 10138 19196 11988 2666 48 1090 O ATOM 1901 CB ASP A1074 -43.512 -0.686 -52.579 1.00123.32 C ANISOU 1901 CB ASP A1074 12088 20420 14349 2472 -95 1114 C ATOM 1902 CG ASP A1074 -42.093 -0.157 -52.499 1.00129.20 C ANISOU 1902 CG ASP A1074 12868 20864 15357 2572 -26 1114 C ATOM 1903 OD1 ASP A1074 -41.892 0.933 -51.922 1.00134.96 O ANISOU 1903 OD1 ASP A1074 13556 21587 16134 2662 39 1110 O ATOM 1904 OD2 ASP A1074 -41.177 -0.832 -53.014 1.00128.37 O ANISOU 1904 OD2 ASP A1074 12834 20528 15413 2560 -36 1118 O ATOM 1905 N ALA A1075 -46.580 -0.887 -52.157 1.00119.50 N ANISOU 1905 N ALA A1075 11471 20624 13309 2319 -197 1109 N ATOM 1906 CA ALA A1075 -47.881 -1.434 -52.519 1.00120.60 C ANISOU 1906 CA ALA A1075 11582 21035 13205 2245 -246 1106 C ATOM 1907 C ALA A1075 -48.939 -0.338 -52.515 1.00125.22 C ANISOU 1907 C ALA A1075 12083 21884 13612 2363 -161 1097 C ATOM 1908 O ALA A1075 -49.853 -0.341 -53.340 1.00127.30 O ANISOU 1908 O ALA A1075 12326 22338 13704 2417 -123 1091 O ATOM 1909 CB ALA A1075 -48.267 -2.550 -51.563 1.00109.79 C ANISOU 1909 CB ALA A1075 10208 19745 11762 1991 -422 1118 C ATOM 1910 N LEU A1076 -48.810 0.601 -51.583 1.00131.39 N ANISOU 1910 N LEU A1076 12816 22675 14434 2402 -131 1097 N ATOM 1911 CA LEU A1076 -49.740 1.721 -51.494 1.00136.95 C ANISOU 1911 CA LEU A1076 13438 23612 14985 2521 -45 1089 C ATOM 1912 C LEU A1076 -49.587 2.636 -52.706 1.00138.26 C ANISOU 1912 C LEU A1076 13615 23738 15179 2769 125 1080 C ATOM 1913 O LEU A1076 -50.563 3.209 -53.190 1.00131.86 O ANISOU 1913 O LEU A1076 12752 23149 14198 2871 195 1074 O ATOM 1914 CB LEU A1076 -49.506 2.511 -50.205 1.00137.09 C ANISOU 1914 CB LEU A1076 13410 23616 15061 2506 -48 1090 C ATOM 1915 N LYS A1077 -48.357 2.768 -53.194 1.00144.33 N ANISOU 1915 N LYS A1077 14451 24225 16164 2865 192 1078 N ATOM 1916 CA LYS A1077 -48.088 3.586 -54.370 1.00146.32 C ANISOU 1916 CA LYS A1077 14724 24410 16463 3098 353 1070 C ATOM 1917 C LYS A1077 -48.821 3.001 -55.572 1.00142.02 C ANISOU 1917 C LYS A1077 14196 23996 15768 3116 361 1068 C ATOM 1918 O LYS A1077 -49.306 3.731 -56.435 1.00143.81 O ANISOU 1918 O LYS A1077 14404 24331 15908 3287 478 1063 O ATOM 1919 CB LYS A1077 -46.584 3.651 -54.645 1.00148.35 C ANISOU 1919 CB LYS A1077 15056 24325 16986 3169 407 1069 C ATOM 1920 CG LYS A1077 -46.168 4.790 -55.565 1.00154.80 C ANISOU 1920 CG LYS A1077 15886 25052 17880 3421 587 1059 C ATOM 1921 CD LYS A1077 -44.672 4.769 -55.840 1.00164.22 C ANISOU 1921 CD LYS A1077 17154 25905 19338 3479 634 1057 C ATOM 1922 CE LYS A1077 -44.219 6.030 -56.563 1.00170.87 C ANISOU 1922 CE LYS A1077 18004 26653 20266 3727 815 1047 C ATOM 1923 NZ LYS A1077 -44.951 6.252 -57.840 1.00174.64 N ANISOU 1923 NZ LYS A1077 18483 27272 20600 3864 908 1043 N ATOM 1924 N LEU A1078 -48.899 1.674 -55.615 1.00137.12 N ANISOU 1924 N LEU A1078 13614 23367 15119 2937 236 1073 N ATOM 1925 CA LEU A1078 -49.635 0.980 -56.664 1.00133.40 C ANISOU 1925 CA LEU A1078 13161 23030 14496 2922 224 1070 C ATOM 1926 C LEU A1078 -51.137 1.084 -56.419 1.00129.19 C ANISOU 1926 C LEU A1078 12543 22845 13698 2874 186 1070 C ATOM 1927 O LEU A1078 -51.924 1.181 -57.362 1.00134.35 O ANISOU 1927 O LEU A1078 13182 23665 14201 2955 239 1067 O ATOM 1928 CB LEU A1078 -49.218 -0.491 -56.723 1.00132.44 C ANISOU 1928 CB LEU A1078 13108 22780 14431 2736 99 1074 C ATOM 1929 CG LEU A1078 -47.787 -0.762 -57.187 1.00109.71 C ANISOU 1929 CG LEU A1078 10320 19562 11803 2782 135 1073 C ATOM 1930 CD1 LEU A1078 -47.418 -2.218 -56.953 1.00109.83 C ANISOU 1930 CD1 LEU A1078 10393 19463 11873 2572 -6 1080 C ATOM 1931 CD2 LEU A1078 -47.623 -0.397 -58.654 1.00109.74 C ANISOU 1931 CD2 LEU A1078 10365 19509 11821 2972 272 1063 C ATOM 1932 N ALA A1079 -51.529 1.063 -55.148 1.00127.33 N ANISOU 1932 N ALA A1079 12253 22720 13408 2740 95 1075 N ATOM 1933 CA ALA A1079 -52.932 1.200 -54.773 1.00133.28 C ANISOU 1933 CA ALA A1079 12919 23802 13918 2686 57 1075 C ATOM 1934 C ALA A1079 -53.459 2.566 -55.197 1.00143.06 C ANISOU 1934 C ALA A1079 14098 25180 15078 2905 204 1070 C ATOM 1935 O ALA A1079 -54.607 2.696 -55.622 1.00111.70 O ANISOU 1935 O ALA A1079 10073 21467 10903 2936 219 1069 O ATOM 1936 CB ALA A1079 -53.100 1.006 -53.271 1.00141.96 C ANISOU 1936 CB ALA A1079 13975 24960 15001 2510 -58 1080 C ATOM 1937 N ASN A1080 -52.609 3.582 -55.079 1.00146.36 N ANISOU 1937 N ASN A1080 14525 25424 15661 3057 311 1068 N ATOM 1938 CA ASN A1080 -52.956 4.929 -55.513 1.00146.37 C ANISOU 1938 CA ASN A1080 14480 25520 15615 3280 462 1065 C ATOM 1939 C ASN A1080 -53.153 4.975 -57.023 1.00143.02 C ANISOU 1939 C ASN A1080 14087 25117 15138 3427 554 1064 C ATOM 1940 O ASN A1080 -54.056 5.646 -57.522 1.00145.21 O ANISOU 1940 O ASN A1080 14310 25604 15261 3549 630 1065 O ATOM 1941 CB ASN A1080 -51.866 5.920 -55.099 1.00148.92 C ANISOU 1941 CB ASN A1080 14819 25617 16147 3402 555 1061 C ATOM 1942 CG ASN A1080 -51.777 6.096 -53.596 1.00151.70 C ANISOU 1942 CG ASN A1080 15130 25977 16533 3281 482 1062 C ATOM 1943 OD1 ASN A1080 -52.424 5.376 -52.835 1.00152.89 O ANISOU 1943 OD1 ASN A1080 15248 26275 16567 3092 353 1066 O ATOM 1944 ND2 ASN A1080 -50.967 7.055 -53.159 1.00153.89 N ANISOU 1944 ND2 ASN A1080 15410 26093 16967 3388 566 1058 N ATOM 1945 N GLU A1081 -52.299 4.256 -57.746 1.00139.69 N ANISOU 1945 N GLU A1081 13754 24477 14846 3414 547 1062 N ATOM 1946 CA GLU A1081 -52.388 4.185 -59.199 1.00133.94 C ANISOU 1946 CA GLU A1081 13066 23744 14079 3539 628 1060 C ATOM 1947 C GLU A1081 -53.729 3.599 -59.621 1.00137.65 C ANISOU 1947 C GLU A1081 13495 24506 14298 3463 566 1062 C ATOM 1948 O GLU A1081 -54.279 3.965 -60.659 1.00138.27 O ANISOU 1948 O GLU A1081 13565 24703 14268 3598 651 1063 O ATOM 1949 CB GLU A1081 -51.256 3.320 -59.756 1.00128.68 C ANISOU 1949 CB GLU A1081 12503 22795 13594 3496 607 1057 C ATOM 1950 CG GLU A1081 -51.169 3.310 -61.273 1.00131.60 C ANISOU 1950 CG GLU A1081 12928 23120 13954 3636 704 1052 C ATOM 1951 CD GLU A1081 -50.265 2.210 -61.796 1.00127.86 C ANISOU 1951 CD GLU A1081 12552 22409 13620 3551 657 1048 C ATOM 1952 OE1 GLU A1081 -50.011 2.175 -63.020 1.00124.93 O ANISOU 1952 OE1 GLU A1081 12237 21958 13272 3663 739 1043 O ATOM 1953 OE2 GLU A1081 -49.811 1.378 -60.983 1.00123.77 O ANISOU 1953 OE2 GLU A1081 12056 21784 13187 3372 539 1050 O ATOM 1954 N GLY A1082 -54.248 2.684 -58.808 1.00140.89 N ANISOU 1954 N GLY A1082 13881 25033 14617 3244 418 1064 N ATOM 1955 CA GLY A1082 -55.481 1.988 -59.124 1.00144.05 C ANISOU 1955 CA GLY A1082 14246 25702 14786 3142 343 1065 C ATOM 1956 C GLY A1082 -55.205 0.609 -59.696 1.00147.93 C ANISOU 1956 C GLY A1082 14816 26095 15296 3004 256 1062 C ATOM 1957 O GLY A1082 -56.081 -0.006 -60.306 1.00149.95 O ANISOU 1957 O GLY A1082 15062 26534 15378 2947 215 1060 O ATOM 1958 N LYS A1083 -53.980 0.127 -59.504 1.00146.65 N ANISOU 1958 N LYS A1083 14732 25642 15348 2950 228 1061 N ATOM 1959 CA LYS A1083 -53.579 -1.183 -60.004 1.00142.45 C ANISOU 1959 CA LYS A1083 14282 24982 14862 2820 149 1058 C ATOM 1960 C LYS A1083 -53.704 -2.247 -58.920 1.00140.59 C ANISOU 1960 C LYS A1083 14043 24768 14606 2566 -19 1062 C ATOM 1961 O LYS A1083 -52.708 -2.658 -58.323 1.00140.96 O ANISOU 1961 O LYS A1083 14139 24585 14836 2483 -71 1066 O ATOM 1962 CB LYS A1083 -52.137 -1.138 -60.514 1.00140.03 C ANISOU 1962 CB LYS A1083 14066 24335 14806 2913 220 1055 C ATOM 1963 N VAL A1084 -54.931 -2.698 -58.679 1.00136.25 N ANISOU 1963 N VAL A1084 13436 24496 13835 2444 -103 1062 N ATOM 1964 CA VAL A1084 -55.186 -3.714 -57.666 1.00128.69 C ANISOU 1964 CA VAL A1084 12472 23590 12833 2198 -264 1067 C ATOM 1965 C VAL A1084 -54.442 -5.007 -57.980 1.00128.09 C ANISOU 1965 C VAL A1084 12494 23305 12869 2065 -343 1066 C ATOM 1966 O VAL A1084 -53.934 -5.669 -57.077 1.00127.76 O ANISOU 1966 O VAL A1084 12478 23142 12923 1905 -448 1073 O ATOM 1967 CB VAL A1084 -56.692 -4.018 -57.533 1.00126.21 C ANISOU 1967 CB VAL A1084 12084 23622 12249 2096 -332 1065 C ATOM 1968 CG1 VAL A1084 -57.433 -2.813 -56.968 1.00124.94 C ANISOU 1968 CG1 VAL A1084 11820 23668 11982 2196 -274 1067 C ATOM 1969 CG2 VAL A1084 -57.275 -4.440 -58.873 1.00132.62 C ANISOU 1969 CG2 VAL A1084 12918 24541 12929 2139 -301 1058 C ATOM 1970 N LYS A1085 -54.374 -5.362 -59.259 1.00124.97 N ANISOU 1970 N LYS A1085 12156 22866 12462 2132 -291 1058 N ATOM 1971 CA LYS A1085 -53.692 -6.583 -59.668 1.00121.14 C ANISOU 1971 CA LYS A1085 11765 22183 12077 2016 -355 1056 C ATOM 1972 C LYS A1085 -52.224 -6.537 -59.256 1.00124.92 C ANISOU 1972 C LYS A1085 12305 22328 12831 2034 -344 1062 C ATOM 1973 O LYS A1085 -51.637 -7.559 -58.898 1.00128.56 O ANISOU 1973 O LYS A1085 12823 22631 13393 1878 -443 1067 O ATOM 1974 CB LYS A1085 -53.807 -6.779 -61.180 1.00117.79 C ANISOU 1974 CB LYS A1085 11392 21759 11605 2117 -277 1045 C ATOM 1975 N GLU A1086 -51.639 -5.345 -59.299 1.00126.60 N ANISOU 1975 N GLU A1086 12503 22437 13164 2225 -223 1062 N ATOM 1976 CA GLU A1086 -50.235 -5.170 -58.951 1.00128.56 C ANISOU 1976 CA GLU A1086 12802 22370 13675 2263 -198 1067 C ATOM 1977 C GLU A1086 -50.060 -5.166 -57.437 1.00116.77 C ANISOU 1977 C GLU A1086 11270 20863 12236 2132 -296 1079 C ATOM 1978 O GLU A1086 -49.101 -5.732 -56.911 1.00112.14 O ANISOU 1978 O GLU A1086 10733 20051 11825 2036 -361 1088 O ATOM 1979 CB GLU A1086 -49.699 -3.859 -59.533 1.00141.44 C ANISOU 1979 CB GLU A1086 14429 23902 15410 2514 -30 1062 C ATOM 1980 CG GLU A1086 -49.993 -3.660 -61.013 1.00149.53 C ANISOU 1980 CG GLU A1086 15481 24974 16360 2665 80 1051 C ATOM 1981 CD GLU A1086 -49.309 -4.688 -61.894 1.00156.10 C ANISOU 1981 CD GLU A1086 16413 25606 17291 2620 66 1045 C ATOM 1982 OE1 GLU A1086 -48.443 -5.430 -61.385 1.00159.07 O ANISOU 1982 OE1 GLU A1086 16840 25771 17828 2500 -11 1050 O ATOM 1983 OE2 GLU A1086 -49.639 -4.752 -63.098 1.00157.09 O ANISOU 1983 OE2 GLU A1086 16567 25787 17334 2706 134 1035 O ATOM 1984 N ALA A1087 -50.993 -4.521 -56.743 1.00115.20 N ANISOU 1984 N ALA A1087 10981 20907 11882 2128 -305 1081 N ATOM 1985 CA ALA A1087 -50.931 -4.400 -55.292 1.00111.39 C ANISOU 1985 CA ALA A1087 10455 20439 11430 2013 -389 1091 C ATOM 1986 C ALA A1087 -51.090 -5.760 -54.617 1.00111.67 C ANISOU 1986 C ALA A1087 10514 20487 11429 1757 -560 1100 C ATOM 1987 O ALA A1087 -50.328 -6.105 -53.715 1.00111.39 O ANISOU 1987 O ALA A1087 10502 20284 11537 1649 -637 1112 O ATOM 1988 CB ALA A1087 -52.001 -3.441 -54.801 1.00111.57 C ANISOU 1988 CB ALA A1087 10377 20739 11276 2067 -356 1089 C ATOM 1989 N GLN A1088 -52.086 -6.524 -55.055 1.00112.25 N ANISOU 1989 N GLN A1088 10581 20761 11308 1659 -618 1095 N ATOM 1990 CA GLN A1088 -52.339 -7.850 -54.499 1.00112.59 C ANISOU 1990 CA GLN A1088 10648 20834 11296 1414 -777 1102 C ATOM 1991 C GLN A1088 -51.144 -8.767 -54.725 1.00112.37 C ANISOU 1991 C GLN A1088 10719 20501 11474 1349 -819 1109 C ATOM 1992 O GLN A1088 -50.892 -9.678 -53.938 1.00112.42 O ANISOU 1992 O GLN A1088 10753 20437 11526 1159 -947 1121 O ATOM 1993 CB GLN A1088 -53.588 -8.471 -55.129 1.00113.27 C ANISOU 1993 CB GLN A1088 10715 21181 11141 1342 -814 1093 C ATOM 1994 CG GLN A1088 -54.884 -7.731 -54.825 1.00113.60 C ANISOU 1994 CG GLN A1088 10652 21548 10961 1375 -795 1088 C ATOM 1995 CD GLN A1088 -56.093 -8.399 -55.449 1.00132.95 C ANISOU 1995 CD GLN A1088 13085 24253 13178 1296 -837 1079 C ATOM 1996 OE1 GLN A1088 -56.134 -9.620 -55.594 1.00136.21 O ANISOU 1996 OE1 GLN A1088 13550 24639 13565 1133 -935 1079 O ATOM 1997 NE2 GLN A1088 -57.085 -7.598 -55.826 1.00133.74 N ANISOU 1997 NE2 GLN A1088 13109 24601 13106 1411 -764 1072 N ATOM 1998 N ALA A1089 -50.413 -8.525 -55.808 1.00112.14 N ANISOU 1998 N ALA A1089 10746 20292 11569 1506 -709 1101 N ATOM 1999 CA ALA A1089 -49.214 -9.298 -56.105 1.00111.92 C ANISOU 1999 CA ALA A1089 10812 19960 11751 1469 -731 1106 C ATOM 2000 C ALA A1089 -48.071 -8.849 -55.201 1.00111.33 C ANISOU 2000 C ALA A1089 10744 19654 11902 1488 -732 1119 C ATOM 2001 O ALA A1089 -47.274 -9.665 -54.738 1.00111.22 O ANISOU 2001 O ALA A1089 10783 19442 12035 1363 -820 1132 O ATOM 2002 CB ALA A1089 -48.832 -9.140 -57.568 1.00111.88 C ANISOU 2002 CB ALA A1089 10863 19846 11801 1636 -606 1092 C ATOM 2003 N ALA A1090 -48.002 -7.546 -54.951 1.00141.80 N ANISOU 2003 N ALA A1090 14548 23541 15788 1644 -635 1117 N ATOM 2004 CA ALA A1090 -46.991 -6.984 -54.064 1.00110.44 C ANISOU 2004 CA ALA A1090 10573 19373 12017 1672 -629 1128 C ATOM 2005 C ALA A1090 -47.241 -7.436 -52.630 1.00110.53 C ANISOU 2005 C ALA A1090 10551 19456 11990 1468 -775 1144 C ATOM 2006 O ALA A1090 -46.306 -7.597 -51.847 1.00110.22 O ANISOU 2006 O ALA A1090 10534 19217 12127 1404 -829 1158 O ATOM 2007 CB ALA A1090 -46.998 -5.464 -54.151 1.00125.40 C ANISOU 2007 CB ALA A1090 12414 21311 13923 1884 -487 1119 C ATOM 2008 N ALA A1091 -48.511 -7.641 -52.294 1.00110.99 N ANISOU 2008 N ALA A1091 10553 19802 11815 1366 -839 1141 N ATOM 2009 CA ALA A1091 -48.891 -8.082 -50.958 1.00111.14 C ANISOU 2009 CA ALA A1091 10538 19921 11771 1167 -978 1155 C ATOM 2010 C ALA A1091 -48.479 -9.533 -50.735 1.00115.30 C ANISOU 2010 C ALA A1091 11133 20314 12361 964 -1116 1169 C ATOM 2011 O ALA A1091 -48.232 -9.951 -49.605 1.00114.14 O ANISOU 2011 O ALA A1091 10985 20121 12263 809 -1229 1187 O ATOM 2012 CB ALA A1091 -50.391 -7.920 -50.757 1.00111.62 C ANISOU 2012 CB ALA A1091 10520 20330 11561 1119 -1002 1146 C ATOM 2013 N GLU A1092 -48.406 -10.296 -51.821 1.00120.69 N ANISOU 2013 N GLU A1092 11878 20936 13044 967 -1104 1162 N ATOM 2014 CA GLU A1092 -48.031 -11.705 -51.749 1.00126.67 C ANISOU 2014 CA GLU A1092 12706 21563 13858 784 -1225 1175 C ATOM 2015 C GLU A1092 -46.581 -11.852 -51.299 1.00133.07 C ANISOU 2015 C GLU A1092 13570 22049 14941 776 -1246 1192 C ATOM 2016 O GLU A1092 -46.229 -12.805 -50.604 1.00135.84 O ANISOU 2016 O GLU A1092 13955 22302 15355 598 -1373 1211 O ATOM 2017 CB GLU A1092 -48.214 -12.377 -53.111 1.00129.16 C ANISOU 2017 CB GLU A1092 13080 21872 14124 812 -1187 1160 C ATOM 2018 CG GLU A1092 -48.193 -13.895 -53.056 1.00135.28 C ANISOU 2018 CG GLU A1092 13918 22591 14891 603 -1318 1169 C ATOM 2019 CD GLU A1092 -49.425 -14.468 -52.383 1.00142.13 C ANISOU 2019 CD GLU A1092 14740 23734 15529 415 -1437 1171 C ATOM 2020 OE1 GLU A1092 -50.364 -13.694 -52.101 1.00145.86 O ANISOU 2020 OE1 GLU A1092 15130 24453 15836 458 -1409 1163 O ATOM 2021 OE2 GLU A1092 -49.455 -15.692 -52.135 1.00143.77 O ANISOU 2021 OE2 GLU A1092 14994 23908 15723 225 -1557 1181 O ATOM 2022 N GLN A1093 -45.745 -10.903 -51.708 1.00137.66 N ANISOU 2022 N GLN A1093 14156 22464 15683 971 -1120 1187 N ATOM 2023 CA GLN A1093 -44.336 -10.901 -51.332 1.00141.89 C ANISOU 2023 CA GLN A1093 14736 22691 16484 988 -1124 1202 C ATOM 2024 C GLN A1093 -44.172 -10.647 -49.836 1.00139.39 C ANISOU 2024 C GLN A1093 14375 22378 16207 885 -1212 1221 C ATOM 2025 O GLN A1093 -43.160 -11.019 -49.242 1.00138.59 O ANISOU 2025 O GLN A1093 14309 22051 16296 817 -1274 1241 O ATOM 2026 CB GLN A1093 -43.581 -9.833 -52.127 1.00145.36 C ANISOU 2026 CB GLN A1093 15184 22979 17068 1229 -959 1188 C ATOM 2027 CG GLN A1093 -42.114 -9.693 -51.747 1.00149.66 C ANISOU 2027 CG GLN A1093 15766 23208 17891 1264 -951 1202 C ATOM 2028 CD GLN A1093 -41.395 -8.639 -52.569 1.00153.96 C ANISOU 2028 CD GLN A1093 16320 23607 18572 1503 -783 1187 C ATOM 2029 OE1 GLN A1093 -41.911 -8.162 -53.579 1.00154.39 O ANISOU 2029 OE1 GLN A1093 16367 23769 18524 1641 -673 1167 O ATOM 2030 NE2 GLN A1093 -40.195 -8.268 -52.134 1.00155.11 N ANISOU 2030 NE2 GLN A1093 16480 23507 18947 1551 -763 1197 N ATOM 2031 N LEU A1094 -45.174 -10.016 -49.231 1.00136.23 N ANISOU 2031 N LEU A1094 13897 22236 15627 874 -1216 1216 N ATOM 2032 CA LEU A1094 -45.120 -9.673 -47.814 1.00134.25 C ANISOU 2032 CA LEU A1094 13600 22016 15394 783 -1290 1231 C ATOM 2033 C LEU A1094 -45.232 -10.907 -46.922 1.00134.90 C ANISOU 2033 C LEU A1094 13706 22102 15449 531 -1467 1253 C ATOM 2034 O LEU A1094 -44.855 -10.866 -45.751 1.00137.26 O ANISOU 2034 O LEU A1094 13989 22344 15820 435 -1546 1272 O ATOM 2035 CB LEU A1094 -46.229 -8.680 -47.458 1.00131.79 C ANISOU 2035 CB LEU A1094 13199 21990 14886 840 -1242 1216 C ATOM 2036 CG LEU A1094 -45.748 -7.371 -46.831 1.00123.08 C ANISOU 2036 CG LEU A1094 12050 20832 13881 965 -1162 1215 C ATOM 2037 CD1 LEU A1094 -44.995 -6.538 -47.854 1.00119.51 C ANISOU 2037 CD1 LEU A1094 11621 20215 13573 1200 -1002 1201 C ATOM 2038 CD2 LEU A1094 -46.914 -6.587 -46.247 1.00118.80 C ANISOU 2038 CD2 LEU A1094 11420 20584 13134 971 -1147 1204 C ATOM 2039 N LYS A1095 -45.754 -12.000 -47.470 1.00133.71 N ANISOU 2039 N LYS A1095 13592 22019 15193 423 -1529 1252 N ATOM 2040 CA LYS A1095 -45.871 -13.242 -46.711 1.00137.82 C ANISOU 2040 CA LYS A1095 14141 22540 15684 182 -1695 1273 C ATOM 2041 C LYS A1095 -44.490 -13.808 -46.403 1.00147.60 C ANISOU 2041 C LYS A1095 15446 23456 17178 132 -1750 1298 C ATOM 2042 O LYS A1095 -44.171 -14.103 -45.252 1.00155.01 O ANISOU 2042 O LYS A1095 16382 24339 18175 -5 -1860 1322 O ATOM 2043 CB LYS A1095 -46.690 -14.279 -47.478 1.00133.96 C ANISOU 2043 CB LYS A1095 13683 22181 15033 89 -1738 1264 C ATOM 2044 CG LYS A1095 -48.107 -13.843 -47.809 1.00127.25 C ANISOU 2044 CG LYS A1095 12768 21660 13922 122 -1695 1241 C ATOM 2045 CD LYS A1095 -48.990 -15.047 -48.092 1.00125.47 C ANISOU 2045 CD LYS A1095 12565 21586 13521 -46 -1789 1238 C ATOM 2046 CE LYS A1095 -50.164 -14.684 -48.984 1.00123.56 C ANISOU 2046 CE LYS A1095 12280 21607 13061 41 -1711 1211 C ATOM 2047 NZ LYS A1095 -50.966 -15.881 -49.359 1.00118.54 N ANISOU 2047 NZ LYS A1095 11672 21105 12264 -119 -1797 1206 N ATOM 2048 N THR A1096 -43.673 -13.954 -47.441 1.00149.41 N ANISOU 2048 N THR A1096 15735 23474 17559 246 -1673 1292 N ATOM 2049 CA THR A1096 -42.312 -14.457 -47.282 1.00156.23 C ANISOU 2049 CA THR A1096 16662 24020 18677 219 -1710 1315 C ATOM 2050 C THR A1096 -41.461 -13.495 -46.456 1.00151.84 C ANISOU 2050 C THR A1096 16074 23330 18288 295 -1682 1326 C ATOM 2051 O THR A1096 -40.395 -13.865 -45.964 1.00153.36 O ANISOU 2051 O THR A1096 16303 23285 18681 242 -1740 1350 O ATOM 2052 CB THR A1096 -41.628 -14.691 -48.649 1.00161.49 C ANISOU 2052 CB THR A1096 17396 24493 19471 347 -1614 1302 C ATOM 2053 OG1 THR A1096 -41.528 -13.453 -49.366 1.00163.16 O ANISOU 2053 OG1 THR A1096 17579 24712 19704 577 -1450 1278 O ATOM 2054 CG2 THR A1096 -42.411 -15.706 -49.478 1.00161.73 C ANISOU 2054 CG2 THR A1096 17465 24641 19345 263 -1645 1290 C ATOM 2055 N THR A1097 -41.938 -12.263 -46.304 1.00142.54 N ANISOU 2055 N THR A1097 14827 22305 17025 418 -1592 1309 N ATOM 2056 CA THR A1097 -41.233 -11.259 -45.515 1.00129.41 C ANISOU 2056 CA THR A1097 13129 20541 15499 494 -1557 1316 C ATOM 2057 C THR A1097 -41.598 -11.360 -44.036 1.00125.07 C ANISOU 2057 C THR A1097 12538 20105 14879 321 -1685 1336 C ATOM 2058 O THR A1097 -40.723 -11.328 -43.172 1.00125.54 O ANISOU 2058 O THR A1097 12604 19994 15100 270 -1741 1358 O ATOM 2059 CB THR A1097 -41.544 -9.836 -46.012 1.00125.64 C ANISOU 2059 CB THR A1097 12599 20169 14971 712 -1395 1288 C ATOM 2060 OG1 THR A1097 -41.104 -9.691 -47.368 1.00124.32 O ANISOU 2060 OG1 THR A1097 12474 19877 14886 879 -1272 1271 O ATOM 2061 CG2 THR A1097 -40.845 -8.800 -45.145 1.00120.93 C ANISOU 2061 CG2 THR A1097 11966 19473 14509 780 -1361 1294 C ATOM 2062 N ARG A1098 -42.891 -11.479 -43.745 1.00124.14 N ANISOU 2062 N ARG A1098 12376 20274 14518 229 -1731 1327 N ATOM 2063 CA ARG A1098 -43.351 -11.606 -42.366 1.00122.80 C ANISOU 2063 CA ARG A1098 12166 20233 14258 57 -1852 1344 C ATOM 2064 C ARG A1098 -42.900 -12.939 -41.783 1.00127.92 C ANISOU 2064 C ARG A1098 12872 20751 14983 -153 -2012 1376 C ATOM 2065 O ARG A1098 -42.528 -13.022 -40.614 1.00134.07 O ANISOU 2065 O ARG A1098 13643 21473 15825 -269 -2107 1400 O ATOM 2066 CB ARG A1098 -44.875 -11.492 -42.280 1.00122.08 C ANISOU 2066 CB ARG A1098 12016 20483 13885 7 -1861 1326 C ATOM 2067 CG ARG A1098 -45.626 -12.629 -42.952 1.00128.30 C ANISOU 2067 CG ARG A1098 12837 21383 14528 -100 -1919 1322 C ATOM 2068 CD ARG A1098 -47.119 -12.563 -42.670 1.00137.42 C ANISOU 2068 CD ARG A1098 13928 22878 15407 -176 -1948 1308 C ATOM 2069 NE ARG A1098 -47.861 -13.574 -43.422 1.00144.80 N ANISOU 2069 NE ARG A1098 14892 23927 16198 -261 -1989 1300 N ATOM 2070 CZ ARG A1098 -47.971 -14.851 -43.067 1.00148.06 C ANISOU 2070 CZ ARG A1098 15348 24327 16580 -468 -2128 1318 C ATOM 2071 NH1 ARG A1098 -47.386 -15.297 -41.963 1.00151.54 N ANISOU 2071 NH1 ARG A1098 15809 24645 17125 -613 -2243 1347 N ATOM 2072 NH2 ARG A1098 -48.669 -15.688 -43.821 1.00147.10 N ANISOU 2072 NH2 ARG A1098 15251 24316 16323 -531 -2152 1308 N ATOM 2073 N ASN A1099 -42.932 -13.980 -42.609 1.00126.84 N ANISOU 2073 N ASN A1099 12793 20563 14837 -203 -2040 1377 N ATOM 2074 CA ASN A1099 -42.517 -15.310 -42.180 1.00128.57 C ANISOU 2074 CA ASN A1099 13073 20652 15127 -397 -2186 1407 C ATOM 2075 C ASN A1099 -41.044 -15.342 -41.783 1.00132.52 C ANISOU 2075 C ASN A1099 13611 20837 15904 -382 -2208 1434 C ATOM 2076 O ASN A1099 -40.604 -16.241 -41.068 1.00136.62 O ANISOU 2076 O ASN A1099 14166 21243 16500 -548 -2340 1466 O ATOM 2077 CB ASN A1099 -42.781 -16.335 -43.286 1.00127.79 C ANISOU 2077 CB ASN A1099 13032 20545 14976 -428 -2190 1399 C ATOM 2078 CG ASN A1099 -44.256 -16.656 -43.448 1.00130.94 C ANISOU 2078 CG ASN A1099 13400 21255 15095 -513 -2219 1381 C ATOM 2079 OD1 ASN A1099 -45.121 -15.895 -43.014 1.00131.73 O ANISOU 2079 OD1 ASN A1099 13428 21586 15036 -494 -2195 1367 O ATOM 2080 ND2 ASN A1099 -44.550 -17.791 -44.074 1.00132.99 N ANISOU 2080 ND2 ASN A1099 13714 21521 15295 -610 -2269 1380 N ATOM 2081 N ALA A1100 -40.286 -14.354 -42.248 1.00133.60 N ANISOU 2081 N ALA A1100 13739 20833 16189 -183 -2078 1422 N ATOM 2082 CA ALA A1100 -38.858 -14.288 -41.962 1.00135.17 C ANISOU 2082 CA ALA A1100 13969 20731 16658 -147 -2083 1444 C ATOM 2083 C ALA A1100 -38.587 -13.631 -40.611 1.00140.80 C ANISOU 2083 C ALA A1100 14635 21445 17416 -193 -2133 1461 C ATOM 2084 O ALA A1100 -37.627 -13.983 -39.925 1.00147.48 O ANISOU 2084 O ALA A1100 15507 22089 18440 -269 -2214 1492 O ATOM 2085 CB ALA A1100 -38.136 -13.535 -43.072 1.00131.33 C ANISOU 2085 CB ALA A1100 13497 20086 16316 85 -1920 1422 C ATOM 2086 N TYR A1101 -39.434 -12.680 -40.228 1.00138.40 N ANISOU 2086 N TYR A1101 14263 21370 16954 -149 -2085 1441 N ATOM 2087 CA TYR A1101 -39.229 -11.932 -38.991 1.00135.61 C ANISOU 2087 CA TYR A1101 13862 21032 16632 -178 -2115 1451 C ATOM 2088 C TYR A1101 -40.054 -12.491 -37.834 1.00134.29 C ANISOU 2088 C TYR A1101 13672 21053 16299 -397 -2262 1468 C ATOM 2089 O TYR A1101 -39.617 -12.466 -36.684 1.00138.26 O ANISOU 2089 O TYR A1101 14166 21493 16873 -499 -2350 1493 O ATOM 2090 CB TYR A1101 -39.542 -10.448 -39.207 1.00132.42 C ANISOU 2090 CB TYR A1101 13397 20741 16176 15 -1964 1419 C ATOM 2091 CG TYR A1101 -38.495 -9.724 -40.026 1.00130.79 C ANISOU 2091 CG TYR A1101 13209 20312 16174 225 -1826 1407 C ATOM 2092 CD1 TYR A1101 -37.144 -9.984 -39.845 1.00136.68 C ANISOU 2092 CD1 TYR A1101 13998 20764 17171 223 -1856 1431 C ATOM 2093 CD2 TYR A1101 -38.857 -8.789 -40.986 1.00130.82 C ANISOU 2093 CD2 TYR A1101 13188 20400 16119 427 -1666 1373 C ATOM 2094 CE1 TYR A1101 -36.182 -9.331 -40.590 1.00141.52 C ANISOU 2094 CE1 TYR A1101 14627 21172 17972 412 -1729 1419 C ATOM 2095 CE2 TYR A1101 -37.900 -8.130 -41.739 1.00134.24 C ANISOU 2095 CE2 TYR A1101 13640 20628 16737 617 -1538 1362 C ATOM 2096 CZ TYR A1101 -36.565 -8.405 -41.535 1.00140.18 C ANISOU 2096 CZ TYR A1101 14434 21090 17738 608 -1569 1384 C ATOM 2097 OH TYR A1101 -35.608 -7.754 -42.279 1.00141.77 O ANISOU 2097 OH TYR A1101 14655 21087 18126 796 -1441 1372 O ATOM 2098 N ILE A1102 -41.244 -12.995 -38.136 1.00127.62 N ANISOU 2098 N ILE A1102 12818 20439 15232 -472 -2290 1456 N ATOM 2099 CA ILE A1102 -42.064 -13.642 -37.120 1.00128.90 C ANISOU 2099 CA ILE A1102 12964 20781 15230 -690 -2432 1471 C ATOM 2100 C ILE A1102 -41.397 -14.929 -36.650 1.00129.81 C ANISOU 2100 C ILE A1102 13145 20717 15461 -871 -2582 1511 C ATOM 2101 O ILE A1102 -41.418 -15.253 -35.464 1.00127.69 O ANISOU 2101 O ILE A1102 12870 20471 15176 -1037 -2705 1537 O ATOM 2102 CB ILE A1102 -43.471 -13.968 -37.651 1.00131.03 C ANISOU 2102 CB ILE A1102 13213 21332 15241 -729 -2426 1447 C ATOM 2103 CG1 ILE A1102 -44.424 -12.802 -37.391 1.00111.05 C ANISOU 2103 CG1 ILE A1102 10599 19057 12537 -647 -2345 1419 C ATOM 2104 CG2 ILE A1102 -44.016 -15.212 -36.981 1.00111.65 C ANISOU 2104 CG2 ILE A1102 10782 18967 12674 -976 -2591 1470 C ATOM 2105 CD1 ILE A1102 -43.976 -11.497 -38.002 1.00135.29 C ANISOU 2105 CD1 ILE A1102 13641 22059 15702 -402 -2177 1396 C ATOM 2106 N GLN A1103 -40.808 -15.661 -37.591 1.00136.00 N ANISOU 2106 N GLN A1103 13991 21320 16361 -839 -2569 1516 N ATOM 2107 CA GLN A1103 -40.143 -16.922 -37.282 1.00139.21 C ANISOU 2107 CA GLN A1103 14465 21542 16887 -998 -2702 1554 C ATOM 2108 C GLN A1103 -38.828 -16.681 -36.541 1.00137.76 C ANISOU 2108 C GLN A1103 14292 21103 16947 -992 -2737 1585 C ATOM 2109 O GLN A1103 -38.297 -17.583 -35.892 1.00139.39 O ANISOU 2109 O GLN A1103 14540 21177 17247 -1146 -2867 1623 O ATOM 2110 CB GLN A1103 -39.891 -17.716 -38.567 1.00142.77 C ANISOU 2110 CB GLN A1103 14980 21872 17395 -953 -2665 1547 C ATOM 2111 CG GLN A1103 -39.451 -19.155 -38.338 1.00147.20 C ANISOU 2111 CG GLN A1103 15611 22283 18034 -1133 -2805 1584 C ATOM 2112 CD GLN A1103 -39.426 -19.968 -39.620 1.00150.80 C ANISOU 2112 CD GLN A1103 16129 22666 18504 -1101 -2767 1572 C ATOM 2113 OE1 GLN A1103 -39.710 -19.452 -40.701 1.00154.36 O ANISOU 2113 OE1 GLN A1103 16571 23172 18908 -943 -2637 1537 O ATOM 2114 NE2 GLN A1103 -39.090 -21.247 -39.503 1.00151.33 N ANISOU 2114 NE2 GLN A1103 16260 22606 18633 -1254 -2882 1601 N ATOM 2115 N LYS A1104 -38.309 -15.462 -36.643 1.00135.88 N ANISOU 2115 N LYS A1104 14019 20799 16811 -814 -2618 1569 N ATOM 2116 CA LYS A1104 -37.088 -15.079 -35.940 1.00131.59 C ANISOU 2116 CA LYS A1104 13477 20029 16492 -793 -2638 1594 C ATOM 2117 C LYS A1104 -37.416 -14.576 -34.538 1.00124.83 C ANISOU 2117 C LYS A1104 12570 19301 15558 -895 -2710 1605 C ATOM 2118 O LYS A1104 -36.767 -14.953 -33.562 1.00115.00 O ANISOU 2118 O LYS A1104 11340 17932 14424 -1019 -2824 1642 O ATOM 2119 CB LYS A1104 -36.352 -13.988 -36.720 1.00137.95 C ANISOU 2119 CB LYS A1104 14271 20697 17448 -553 -2473 1569 C ATOM 2120 CG LYS A1104 -35.154 -13.394 -35.992 1.00145.33 C ANISOU 2120 CG LYS A1104 15196 21421 18602 -514 -2476 1589 C ATOM 2121 CD LYS A1104 -34.621 -12.167 -36.717 1.00149.10 C ANISOU 2121 CD LYS A1104 15651 21810 19190 -273 -2302 1559 C ATOM 2122 CE LYS A1104 -33.874 -12.543 -37.989 1.00149.78 C ANISOU 2122 CE LYS A1104 15793 21687 19432 -155 -2225 1554 C ATOM 2123 NZ LYS A1104 -34.073 -11.546 -39.077 1.00146.69 N ANISOU 2123 NZ LYS A1104 15381 21343 19013 68 -2043 1512 N ATOM 2124 N TYR A1105 -38.427 -13.717 -34.450 1.00134.62 N ANISOU 2124 N TYR A1105 13749 20792 16608 -842 -2641 1573 N ATOM 2125 CA TYR A1105 -38.829 -13.116 -33.184 1.00142.91 C ANISOU 2125 CA TYR A1105 14747 21985 17568 -922 -2689 1576 C ATOM 2126 C TYR A1105 -39.463 -14.161 -32.273 1.00142.16 C ANISOU 2126 C TYR A1105 14664 22011 17339 -1170 -2859 1603 C ATOM 2127 O TYR A1105 -39.297 -14.122 -31.053 1.00145.72 O ANISOU 2127 O TYR A1105 15102 22462 17804 -1292 -2954 1626 O ATOM 2128 CB TYR A1105 -39.815 -11.973 -33.435 1.00147.21 C ANISOU 2128 CB TYR A1105 15225 22774 17936 -795 -2564 1533 C ATOM 2129 CG TYR A1105 -39.978 -11.027 -32.265 1.00153.73 C ANISOU 2129 CG TYR A1105 15993 23698 18718 -816 -2568 1530 C ATOM 2130 CD1 TYR A1105 -39.047 -10.026 -32.023 1.00157.07 C ANISOU 2130 CD1 TYR A1105 16401 23965 19314 -690 -2492 1527 C ATOM 2131 CD2 TYR A1105 -41.068 -11.128 -31.409 1.00157.81 C ANISOU 2131 CD2 TYR A1105 16472 24466 19021 -961 -2644 1528 C ATOM 2132 CE1 TYR A1105 -39.192 -9.156 -30.958 1.00160.27 C ANISOU 2132 CE1 TYR A1105 16756 24459 19679 -710 -2493 1523 C ATOM 2133 CE2 TYR A1105 -41.222 -10.262 -30.342 1.00162.15 C ANISOU 2133 CE2 TYR A1105 16972 25106 19530 -982 -2644 1523 C ATOM 2134 CZ TYR A1105 -40.281 -9.278 -30.121 1.00163.44 C ANISOU 2134 CZ TYR A1105 17123 25110 19868 -856 -2569 1520 C ATOM 2135 OH TYR A1105 -40.430 -8.414 -29.060 1.00164.77 O ANISOU 2135 OH TYR A1105 17245 25366 19995 -878 -2567 1514 O ATOM 2136 N LEU A1106 -40.190 -15.095 -32.877 1.00136.64 N ANISOU 2136 N LEU A1106 13993 21415 16510 -1245 -2896 1599 N ATOM 2137 CA LEU A1106 -40.841 -16.168 -32.137 1.00133.31 C ANISOU 2137 CA LEU A1106 13587 21110 15952 -1480 -3052 1622 C ATOM 2138 C LEU A1106 -39.809 -17.182 -31.654 1.00135.22 C ANISOU 2138 C LEU A1106 13893 21105 16379 -1611 -3183 1671 C ATOM 2139 O LEU A1106 -40.090 -18.000 -30.778 1.00135.76 O ANISOU 2139 O LEU A1106 13978 21224 16379 -1815 -3328 1699 O ATOM 2140 CB LEU A1106 -41.877 -16.861 -33.026 1.00125.79 C ANISOU 2140 CB LEU A1106 12649 20331 14816 -1510 -3044 1602 C ATOM 2141 CG LEU A1106 -42.769 -17.911 -32.364 1.00119.61 C ANISOU 2141 CG LEU A1106 11878 19716 13854 -1747 -3190 1618 C ATOM 2142 CD1 LEU A1106 -43.664 -17.277 -31.315 1.00120.91 C ANISOU 2142 CD1 LEU A1106 11976 20125 13840 -1819 -3216 1608 C ATOM 2143 CD2 LEU A1106 -43.603 -18.632 -33.409 1.00117.63 C ANISOU 2143 CD2 LEU A1106 11649 19589 13457 -1759 -3171 1597 C ATOM 2144 N GLN A 314 -38.612 -17.120 -32.229 1.00113.73 N ANISOU 2144 N GLN A 314 16536 15524 11153 266 -2791 -17 N ATOM 2145 CA GLN A 314 -37.549 -18.066 -31.902 1.00117.61 C ANISOU 2145 CA GLN A 314 17061 16016 11610 296 -2557 -162 C ATOM 2146 C GLN A 314 -36.723 -17.594 -30.708 1.00117.18 C ANISOU 2146 C GLN A 314 16871 15895 11756 288 -2303 -34 C ATOM 2147 O GLN A 314 -36.183 -18.408 -29.958 1.00112.78 O ANISOU 2147 O GLN A 314 16262 15259 11332 295 -2151 -150 O ATOM 2148 CB GLN A 314 -36.634 -18.271 -33.111 1.00125.47 C ANISOU 2148 CB GLN A 314 18272 17210 12192 358 -2471 -213 C ATOM 2149 CG GLN A 314 -35.587 -19.357 -32.919 1.00134.06 C ANISOU 2149 CG GLN A 314 19401 18302 13235 407 -2256 -402 C ATOM 2150 CD GLN A 314 -36.200 -20.738 -32.772 1.00141.50 C ANISOU 2150 CD GLN A 314 20338 19112 14313 402 -2390 -673 C ATOM 2151 OE1 GLN A 314 -37.359 -20.955 -33.127 1.00145.87 O ANISOU 2151 OE1 GLN A 314 20899 19617 14909 367 -2654 -745 O ATOM 2152 NE2 GLN A 314 -35.424 -21.678 -32.244 1.00139.52 N ANISOU 2152 NE2 GLN A 314 20070 18794 14147 435 -2218 -821 N ATOM 2153 N THR A 315 -36.620 -16.280 -30.539 1.00122.05 N ANISOU 2153 N THR A 315 17435 16539 12400 275 -2269 203 N ATOM 2154 CA THR A 315 -35.836 -15.713 -29.449 1.00124.68 C ANISOU 2154 CA THR A 315 17644 16813 12914 267 -2046 330 C ATOM 2155 C THR A 315 -36.493 -15.981 -28.099 1.00129.54 C ANISOU 2155 C THR A 315 18070 17246 13904 227 -2064 282 C ATOM 2156 O THR A 315 -35.816 -16.322 -27.130 1.00132.13 O ANISOU 2156 O THR A 315 18321 17508 14375 227 -1878 254 O ATOM 2157 CB THR A 315 -35.653 -14.193 -29.615 1.00121.99 C ANISOU 2157 CB THR A 315 17293 16525 12533 258 -2035 595 C ATOM 2158 OG1 THR A 315 -35.028 -13.916 -30.875 1.00119.06 O ANISOU 2158 OG1 THR A 315 17101 16337 11798 284 -2006 666 O ATOM 2159 CG2 THR A 315 -34.793 -13.632 -28.490 1.00122.71 C ANISOU 2159 CG2 THR A 315 17259 16551 12813 249 -1813 708 C ATOM 2160 N ILE A 316 -37.812 -15.820 -28.038 1.00128.78 N ANISOU 2160 N ILE A 316 17894 17075 13961 193 -2287 278 N ATOM 2161 CA ILE A 316 -38.539 -16.019 -26.789 1.00123.29 C ANISOU 2161 CA ILE A 316 17008 16225 13612 148 -2302 241 C ATOM 2162 C ILE A 316 -38.407 -17.459 -26.303 1.00115.76 C ANISOU 2162 C ILE A 316 16045 15193 12744 132 -2238 42 C ATOM 2163 O ILE A 316 -38.406 -17.715 -25.100 1.00117.48 O ANISOU 2163 O ILE A 316 16132 15304 13201 101 -2134 31 O ATOM 2164 CB ILE A 316 -40.035 -15.658 -26.923 1.00128.67 C ANISOU 2164 CB ILE A 316 17595 16852 14442 117 -2562 255 C ATOM 2165 CG1 ILE A 316 -40.727 -16.569 -27.938 1.00139.47 C ANISOU 2165 CG1 ILE A 316 19064 18249 15679 110 -2776 92 C ATOM 2166 CG2 ILE A 316 -40.195 -14.198 -27.320 1.00131.00 C ANISOU 2166 CG2 ILE A 316 17889 17196 14690 138 -2641 463 C ATOM 2167 CD1 ILE A 316 -42.233 -16.450 -27.922 1.00146.55 C ANISOU 2167 CD1 ILE A 316 19833 19072 16776 70 -3032 72 C ATOM 2168 N SER A 317 -38.295 -18.394 -27.241 1.00108.55 N ANISOU 2168 N SER A 317 15278 14333 11632 153 -2305 -115 N ATOM 2169 CA SER A 317 -38.110 -19.799 -26.899 1.00 98.17 C ANISOU 2169 CA SER A 317 13976 12933 10391 145 -2259 -312 C ATOM 2170 C SER A 317 -36.798 -19.994 -26.151 1.00 98.84 C ANISOU 2170 C SER A 317 14053 13007 10495 177 -1990 -294 C ATOM 2171 O SER A 317 -36.752 -20.664 -25.119 1.00 99.70 O ANISOU 2171 O SER A 317 14070 12991 10820 148 -1914 -349 O ATOM 2172 CB SER A 317 -38.114 -20.662 -28.159 1.00 94.59 C ANISOU 2172 CB SER A 317 13700 12549 9689 179 -2379 -493 C ATOM 2173 OG SER A 317 -37.745 -21.995 -27.854 1.00104.94 O ANISOU 2173 OG SER A 317 15036 13769 11066 184 -2317 -683 O ATOM 2174 N ASN A 318 -35.730 -19.408 -26.682 1.00 96.96 N ANISOU 2174 N ASN A 318 13908 12901 10030 233 -1850 -210 N ATOM 2175 CA ASN A 318 -34.423 -19.485 -26.047 1.00 95.69 C ANISOU 2175 CA ASN A 318 13730 12744 9882 269 -1600 -182 C ATOM 2176 C ASN A 318 -34.427 -18.764 -24.706 1.00 86.83 C ANISOU 2176 C ASN A 318 12442 11531 9019 230 -1510 -36 C ATOM 2177 O ASN A 318 -33.863 -19.251 -23.726 1.00 88.38 O ANISOU 2177 O ASN A 318 12573 11646 9362 230 -1374 -66 O ATOM 2178 CB ASN A 318 -33.349 -18.891 -26.959 1.00107.14 C ANISOU 2178 CB ASN A 318 15298 14371 11041 326 -1473 -104 C ATOM 2179 CG ASN A 318 -33.250 -19.612 -28.288 1.00124.78 C ANISOU 2179 CG ASN A 318 17709 16719 12984 375 -1538 -263 C ATOM 2180 OD1 ASN A 318 -33.657 -20.768 -28.412 1.00133.07 O ANISOU 2180 OD1 ASN A 318 18798 17697 14067 381 -1634 -467 O ATOM 2181 ND2 ASN A 318 -32.705 -18.934 -29.291 1.00130.09 N ANISOU 2181 ND2 ASN A 318 18492 17570 13366 408 -1486 -170 N ATOM 2182 N GLU A 319 -35.069 -17.601 -24.667 1.00 81.75 N ANISOU 2182 N GLU A 319 11733 10900 8429 202 -1595 119 N ATOM 2183 CA GLU A 319 -35.192 -16.841 -23.431 1.00 85.33 C ANISOU 2183 CA GLU A 319 12028 11269 9122 171 -1530 242 C ATOM 2184 C GLU A 319 -35.921 -17.662 -22.376 1.00 85.98 C ANISOU 2184 C GLU A 319 11996 11214 9460 123 -1561 143 C ATOM 2185 O GLU A 319 -35.556 -17.646 -21.199 1.00 86.21 O ANISOU 2185 O GLU A 319 11929 11174 9654 109 -1431 176 O ATOM 2186 CB GLU A 319 -35.943 -15.534 -23.680 1.00 73.01 C ANISOU 2186 CB GLU A 319 10420 9730 7590 157 -1658 395 C ATOM 2187 CG GLU A 319 -35.127 -14.476 -24.401 1.00 73.64 C ANISOU 2187 CG GLU A 319 10584 9923 7473 189 -1594 555 C ATOM 2188 CD GLU A 319 -35.923 -13.217 -24.669 1.00 83.90 C ANISOU 2188 CD GLU A 319 11841 11219 8817 178 -1748 710 C ATOM 2189 OE1 GLU A 319 -35.361 -12.267 -25.255 1.00 84.26 O ANISOU 2189 OE1 GLU A 319 11952 11342 8720 191 -1718 867 O ATOM 2190 OE2 GLU A 319 -37.113 -13.179 -24.294 1.00 84.62 O ANISOU 2190 OE2 GLU A 319 11828 11228 9096 154 -1900 677 O ATOM 2191 N GLN A 320 -36.953 -18.377 -22.810 1.00 85.61 N ANISOU 2191 N GLN A 320 11958 11129 9440 91 -1738 26 N ATOM 2192 CA GLN A 320 -37.756 -19.191 -21.909 1.00 86.44 C ANISOU 2192 CA GLN A 320 11950 11105 9788 28 -1781 -59 C ATOM 2193 C GLN A 320 -36.944 -20.366 -21.379 1.00 85.34 C ANISOU 2193 C GLN A 320 11849 10900 9678 33 -1648 -163 C ATOM 2194 O GLN A 320 -36.948 -20.639 -20.179 1.00 84.55 O ANISOU 2194 O GLN A 320 11646 10707 9771 -5 -1560 -144 O ATOM 2195 CB GLN A 320 -39.003 -19.700 -22.630 1.00 88.67 C ANISOU 2195 CB GLN A 320 12236 11363 10089 -11 -2017 -162 C ATOM 2196 CG GLN A 320 -40.180 -19.967 -21.712 1.00 98.00 C ANISOU 2196 CG GLN A 320 13243 12432 11559 -93 -2090 -179 C ATOM 2197 CD GLN A 320 -41.506 -19.904 -22.442 1.00112.63 C ANISOU 2197 CD GLN A 320 15057 14286 13451 -127 -2340 -221 C ATOM 2198 OE1 GLN A 320 -41.582 -20.187 -23.638 1.00121.58 O ANISOU 2198 OE1 GLN A 320 16323 15475 14398 -102 -2482 -300 O ATOM 2199 NE2 GLN A 320 -42.557 -19.517 -21.729 1.00114.40 N ANISOU 2199 NE2 GLN A 320 15095 14457 13914 -180 -2398 -174 N ATOM 2200 N ARG A 321 -36.247 -21.058 -22.275 1.00 72.96 N ANISOU 2200 N ARG A 321 10429 9378 7913 84 -1636 -273 N ATOM 2201 CA ARG A 321 -35.413 -22.188 -21.884 1.00 72.68 C ANISOU 2201 CA ARG A 321 10438 9274 7903 107 -1523 -383 C ATOM 2202 C ARG A 321 -34.336 -21.731 -20.911 1.00 76.98 C ANISOU 2202 C ARG A 321 10927 9820 8502 134 -1312 -271 C ATOM 2203 O ARG A 321 -34.125 -22.347 -19.866 1.00 73.66 O ANISOU 2203 O ARG A 321 10447 9292 8249 110 -1237 -287 O ATOM 2204 CB ARG A 321 -34.763 -22.825 -23.113 1.00102.74 C ANISOU 2204 CB ARG A 321 14415 13158 11465 180 -1533 -524 C ATOM 2205 CG ARG A 321 -35.755 -23.376 -24.128 1.00106.93 C ANISOU 2205 CG ARG A 321 15021 13687 11921 160 -1756 -662 C ATOM 2206 N ALA A 322 -33.661 -20.641 -21.262 1.00 71.29 N ANISOU 2206 N ALA A 322 10228 9218 7642 177 -1225 -153 N ATOM 2207 CA ALA A 322 -32.602 -20.089 -20.428 1.00 71.78 C ANISOU 2207 CA ALA A 322 10234 9290 7750 202 -1039 -44 C ATOM 2208 C ALA A 322 -33.133 -19.718 -19.049 1.00 78.22 C ANISOU 2208 C ALA A 322 10903 10009 8806 143 -1025 41 C ATOM 2209 O ALA A 322 -32.552 -20.089 -18.031 1.00 87.49 O ANISOU 2209 O ALA A 322 12032 11117 10093 143 -914 45 O ATOM 2210 CB ALA A 322 -31.988 -18.873 -21.101 1.00 71.51 C ANISOU 2210 CB ALA A 322 10235 9391 7545 238 -979 86 C ATOM 2211 N SER A 323 -34.239 -18.982 -19.022 1.00 74.03 N ANISOU 2211 N SER A 323 10300 9478 8349 100 -1141 105 N ATOM 2212 CA SER A 323 -34.821 -18.532 -17.764 1.00 75.13 C ANISOU 2212 CA SER A 323 10294 9547 8703 51 -1122 177 C ATOM 2213 C SER A 323 -35.250 -19.713 -16.896 1.00 74.94 C ANISOU 2213 C SER A 323 10223 9411 8841 -4 -1122 91 C ATOM 2214 O SER A 323 -35.213 -19.635 -15.668 1.00 74.93 O ANISOU 2214 O SER A 323 10131 9358 8981 -32 -1035 140 O ATOM 2215 CB SER A 323 -36.005 -17.593 -18.022 1.00 78.60 C ANISOU 2215 CB SER A 323 10660 10007 9199 25 -1261 239 C ATOM 2216 OG SER A 323 -37.037 -18.232 -18.755 1.00 82.08 O ANISOU 2216 OG SER A 323 11120 10432 9634 -7 -1433 143 O ATOM 2217 N LYS A 324 -35.648 -20.809 -17.532 1.00 66.98 N ANISOU 2217 N LYS A 324 9280 8362 7806 -22 -1222 -35 N ATOM 2218 CA LYS A 324 -36.037 -22.005 -16.797 1.00 88.85 C ANISOU 2218 CA LYS A 324 12015 11009 10734 -83 -1234 -109 C ATOM 2219 C LYS A 324 -34.810 -22.628 -16.147 1.00 84.55 C ANISOU 2219 C LYS A 324 11516 10419 10191 -47 -1086 -118 C ATOM 2220 O LYS A 324 -34.826 -22.967 -14.964 1.00 91.12 O ANISOU 2220 O LYS A 324 12279 11172 11169 -91 -1020 -79 O ATOM 2221 CB LYS A 324 -36.719 -23.015 -17.723 1.00 68.87 C ANISOU 2221 CB LYS A 324 9551 8433 8182 -110 -1396 -252 C ATOM 2222 CG LYS A 324 -38.116 -22.606 -18.158 1.00 69.82 C ANISOU 2222 CG LYS A 324 9597 8570 8362 -164 -1568 -251 C ATOM 2223 N VAL A 325 -33.741 -22.764 -16.923 1.00 75.04 N ANISOU 2223 N VAL A 325 10423 9269 8818 36 -1034 -167 N ATOM 2224 CA VAL A 325 -32.500 -23.324 -16.411 1.00 74.44 C ANISOU 2224 CA VAL A 325 10385 9156 8745 87 -901 -183 C ATOM 2225 C VAL A 325 -31.992 -22.493 -15.240 1.00 72.65 C ANISOU 2225 C VAL A 325 10067 8941 8596 84 -775 -44 C ATOM 2226 O VAL A 325 -31.700 -23.026 -14.171 1.00 79.03 O ANISOU 2226 O VAL A 325 10840 9663 9523 64 -716 -26 O ATOM 2227 CB VAL A 325 -31.419 -23.380 -17.505 1.00 73.25 C ANISOU 2227 CB VAL A 325 10346 9095 8390 185 -846 -251 C ATOM 2228 CG1 VAL A 325 -30.070 -23.752 -16.905 1.00 75.22 C ANISOU 2228 CG1 VAL A 325 10600 9317 8662 246 -699 -250 C ATOM 2229 CG2 VAL A 325 -31.816 -24.372 -18.586 1.00 68.86 C ANISOU 2229 CG2 VAL A 325 9896 8518 7752 198 -968 -421 C ATOM 2230 N LEU A 326 -31.895 -21.184 -15.443 1.00 63.79 N ANISOU 2230 N LEU A 326 8912 7922 7406 102 -745 56 N ATOM 2231 CA LEU A 326 -31.420 -20.289 -14.399 1.00 62.32 C ANISOU 2231 CA LEU A 326 8642 7747 7289 103 -641 175 C ATOM 2232 C LEU A 326 -32.310 -20.398 -13.167 1.00 68.89 C ANISOU 2232 C LEU A 326 9374 8503 8298 28 -658 208 C ATOM 2233 O LEU A 326 -31.826 -20.373 -12.037 1.00 74.36 O ANISOU 2233 O LEU A 326 10023 9162 9067 24 -570 258 O ATOM 2234 CB LEU A 326 -31.388 -18.845 -14.904 1.00 74.21 C ANISOU 2234 CB LEU A 326 10127 9354 8716 123 -640 274 C ATOM 2235 CG LEU A 326 -30.853 -17.804 -13.917 1.00 79.31 C ANISOU 2235 CG LEU A 326 10691 10008 9435 128 -546 387 C ATOM 2236 CD1 LEU A 326 -30.113 -16.706 -14.659 1.00 79.08 C ANISOU 2236 CD1 LEU A 326 10686 10071 9290 170 -506 471 C ATOM 2237 CD2 LEU A 326 -31.981 -17.208 -13.087 1.00 86.41 C ANISOU 2237 CD2 LEU A 326 11483 10874 10476 76 -598 430 C ATOM 2238 N GLY A 327 -33.613 -20.519 -13.392 1.00 66.28 N ANISOU 2238 N GLY A 327 9004 8152 8028 -31 -772 179 N ATOM 2239 CA GLY A 327 -34.559 -20.659 -12.301 1.00 69.51 C ANISOU 2239 CA GLY A 327 9306 8504 8602 -109 -780 205 C ATOM 2240 C GLY A 327 -34.262 -21.881 -11.452 1.00 70.78 C ANISOU 2240 C GLY A 327 9485 8565 8842 -145 -731 180 C ATOM 2241 O GLY A 327 -34.128 -21.784 -10.234 1.00 68.86 O ANISOU 2241 O GLY A 327 9185 8302 8676 -170 -647 246 O ATOM 2242 N ILE A 328 -34.158 -23.035 -12.103 1.00 76.66 N ANISOU 2242 N ILE A 328 10317 9245 9567 -145 -792 84 N ATOM 2243 CA ILE A 328 -33.884 -24.287 -11.409 1.00 75.41 C ANISOU 2243 CA ILE A 328 10188 8967 9498 -177 -770 59 C ATOM 2244 C ILE A 328 -32.552 -24.224 -10.675 1.00 74.73 C ANISOU 2244 C ILE A 328 10131 8879 9385 -115 -647 112 C ATOM 2245 O ILE A 328 -32.476 -24.513 -9.483 1.00 73.12 O ANISOU 2245 O ILE A 328 9891 8621 9270 -156 -593 177 O ATOM 2246 CB ILE A 328 -33.839 -25.471 -12.388 1.00 77.84 C ANISOU 2246 CB ILE A 328 10598 9197 9781 -164 -866 -75 C ATOM 2247 CG1 ILE A 328 -35.210 -25.683 -13.033 1.00 93.95 C ANISOU 2247 CG1 ILE A 328 12606 11219 11872 -238 -1013 -135 C ATOM 2248 CG2 ILE A 328 -33.402 -26.734 -11.665 1.00 80.28 C ANISOU 2248 CG2 ILE A 328 10946 9362 10194 -184 -847 -92 C ATOM 2249 CD1 ILE A 328 -35.227 -26.751 -14.109 1.00101.93 C ANISOU 2249 CD1 ILE A 328 13724 12159 12844 -221 -1130 -289 C ATOM 2250 N VAL A 329 -31.501 -23.856 -11.400 1.00 71.36 N ANISOU 2250 N VAL A 329 9765 8517 8832 -19 -604 85 N ATOM 2251 CA VAL A 329 -30.162 -23.811 -10.832 1.00 65.47 C ANISOU 2251 CA VAL A 329 9036 7772 8068 47 -498 123 C ATOM 2252 C VAL A 329 -30.101 -22.865 -9.636 1.00 61.94 C ANISOU 2252 C VAL A 329 8502 7363 7669 23 -424 243 C ATOM 2253 O VAL A 329 -29.630 -23.242 -8.564 1.00 66.34 O ANISOU 2253 O VAL A 329 9051 7865 8291 16 -376 288 O ATOM 2254 CB VAL A 329 -29.122 -23.377 -11.880 1.00 72.01 C ANISOU 2254 CB VAL A 329 9917 8691 8751 145 -451 85 C ATOM 2255 CG1 VAL A 329 -27.761 -23.168 -11.227 1.00 79.38 C ANISOU 2255 CG1 VAL A 329 10837 9635 9690 208 -341 136 C ATOM 2256 CG2 VAL A 329 -29.029 -24.409 -12.992 1.00 63.05 C ANISOU 2256 CG2 VAL A 329 8879 7523 7553 186 -510 -57 C ATOM 2257 N PHE A 330 -30.571 -21.637 -9.824 1.00 59.57 N ANISOU 2257 N PHE A 330 8145 7153 7337 16 -425 292 N ATOM 2258 CA PHE A 330 -30.552 -20.653 -8.748 1.00 67.53 C ANISOU 2258 CA PHE A 330 9071 8197 8390 2 -364 384 C ATOM 2259 C PHE A 330 -31.408 -21.102 -7.567 1.00 61.40 C ANISOU 2259 C PHE A 330 8239 7367 7722 -80 -363 412 C ATOM 2260 O PHE A 330 -31.072 -20.840 -6.412 1.00 59.87 O ANISOU 2260 O PHE A 330 8013 7175 7559 -85 -298 471 O ATOM 2261 CB PHE A 330 -31.020 -19.284 -9.249 1.00 68.17 C ANISOU 2261 CB PHE A 330 9100 8364 8438 11 -386 420 C ATOM 2262 CG PHE A 330 -29.983 -18.543 -10.045 1.00 67.08 C ANISOU 2262 CG PHE A 330 8999 8292 8196 83 -351 443 C ATOM 2263 CD1 PHE A 330 -28.894 -19.210 -10.585 1.00 71.28 C ANISOU 2263 CD1 PHE A 330 9607 8822 8655 137 -310 401 C ATOM 2264 CD2 PHE A 330 -30.088 -17.178 -10.240 1.00 64.53 C ANISOU 2264 CD2 PHE A 330 8629 8029 7859 95 -355 508 C ATOM 2265 CE1 PHE A 330 -27.939 -18.530 -11.313 1.00 70.39 C ANISOU 2265 CE1 PHE A 330 9515 8784 8446 193 -260 430 C ATOM 2266 CE2 PHE A 330 -29.132 -16.493 -10.964 1.00 71.86 C ANISOU 2266 CE2 PHE A 330 9588 9017 8698 145 -317 549 C ATOM 2267 CZ PHE A 330 -28.057 -17.170 -11.502 1.00 72.86 C ANISOU 2267 CZ PHE A 330 9783 9157 8742 190 -262 513 C ATOM 2268 N PHE A 331 -32.517 -21.772 -7.858 1.00 59.37 N ANISOU 2268 N PHE A 331 7969 7067 7520 -147 -437 372 N ATOM 2269 CA PHE A 331 -33.381 -22.298 -6.808 1.00 70.10 C ANISOU 2269 CA PHE A 331 9269 8379 8985 -240 -427 406 C ATOM 2270 C PHE A 331 -32.636 -23.320 -5.953 1.00 65.58 C ANISOU 2270 C PHE A 331 8756 7721 8439 -250 -385 436 C ATOM 2271 O PHE A 331 -32.713 -23.284 -4.726 1.00 63.07 O ANISOU 2271 O PHE A 331 8402 7406 8156 -291 -323 509 O ATOM 2272 CB PHE A 331 -34.634 -22.933 -7.411 1.00 74.69 C ANISOU 2272 CB PHE A 331 9823 8919 9636 -316 -525 353 C ATOM 2273 CG PHE A 331 -35.523 -23.598 -6.400 1.00 78.84 C ANISOU 2273 CG PHE A 331 10282 9393 10281 -427 -508 397 C ATOM 2274 CD1 PHE A 331 -36.211 -22.846 -5.464 1.00 79.82 C ANISOU 2274 CD1 PHE A 331 10291 9588 10448 -469 -442 456 C ATOM 2275 CD2 PHE A 331 -35.674 -24.975 -6.387 1.00 86.04 C ANISOU 2275 CD2 PHE A 331 11244 10185 11264 -492 -556 378 C ATOM 2276 CE1 PHE A 331 -37.030 -23.454 -4.533 1.00 81.31 C ANISOU 2276 CE1 PHE A 331 10412 9748 10732 -577 -407 505 C ATOM 2277 CE2 PHE A 331 -36.493 -25.587 -5.459 1.00 89.79 C ANISOU 2277 CE2 PHE A 331 11654 10613 11850 -609 -534 439 C ATOM 2278 CZ PHE A 331 -37.172 -24.824 -4.531 1.00 87.62 C ANISOU 2278 CZ PHE A 331 11262 10430 11601 -654 -451 507 C ATOM 2279 N LEU A 332 -31.922 -24.232 -6.605 1.00 67.40 N ANISOU 2279 N LEU A 332 9080 7877 8650 -208 -422 377 N ATOM 2280 CA LEU A 332 -31.117 -25.220 -5.892 1.00 74.70 C ANISOU 2280 CA LEU A 332 10067 8703 9612 -200 -401 403 C ATOM 2281 C LEU A 332 -30.081 -24.540 -5.003 1.00 74.42 C ANISOU 2281 C LEU A 332 10023 8720 9534 -144 -316 474 C ATOM 2282 O LEU A 332 -29.873 -24.947 -3.861 1.00 77.28 O ANISOU 2282 O LEU A 332 10392 9039 9933 -175 -288 547 O ATOM 2283 CB LEU A 332 -30.422 -26.165 -6.877 1.00 76.00 C ANISOU 2283 CB LEU A 332 10327 8787 9763 -135 -455 302 C ATOM 2284 CG LEU A 332 -31.139 -27.485 -7.172 1.00 78.04 C ANISOU 2284 CG LEU A 332 10626 8909 10116 -204 -550 244 C ATOM 2285 CD1 LEU A 332 -31.268 -28.325 -5.908 1.00 77.60 C ANISOU 2285 CD1 LEU A 332 10573 8743 10170 -283 -543 339 C ATOM 2286 CD2 LEU A 332 -32.504 -27.240 -7.797 1.00 89.86 C ANISOU 2286 CD2 LEU A 332 12069 10441 11633 -280 -619 208 C ATOM 2287 N PHE A 333 -29.435 -23.506 -5.533 1.00 71.60 N ANISOU 2287 N PHE A 333 9652 8454 9098 -66 -283 459 N ATOM 2288 CA PHE A 333 -28.461 -22.737 -4.770 1.00 69.04 C ANISOU 2288 CA PHE A 333 9307 8181 8745 -15 -216 518 C ATOM 2289 C PHE A 333 -29.103 -22.162 -3.514 1.00 65.66 C ANISOU 2289 C PHE A 333 8815 7792 8341 -77 -180 592 C ATOM 2290 O PHE A 333 -28.581 -22.314 -2.410 1.00 57.25 O ANISOU 2290 O PHE A 333 7761 6711 7281 -78 -149 649 O ATOM 2291 CB PHE A 333 -27.900 -21.603 -5.626 1.00 66.91 C ANISOU 2291 CB PHE A 333 9016 8003 8402 55 -192 500 C ATOM 2292 CG PHE A 333 -27.081 -20.609 -4.855 1.00 73.01 C ANISOU 2292 CG PHE A 333 9747 8828 9164 91 -136 560 C ATOM 2293 CD1 PHE A 333 -27.691 -19.569 -4.175 1.00 75.60 C ANISOU 2293 CD1 PHE A 333 10009 9211 9505 57 -121 602 C ATOM 2294 CD2 PHE A 333 -25.703 -20.712 -4.815 1.00 79.02 C ANISOU 2294 CD2 PHE A 333 10528 9580 9915 162 -106 563 C ATOM 2295 CE1 PHE A 333 -26.941 -18.652 -3.466 1.00 69.53 C ANISOU 2295 CE1 PHE A 333 9205 8480 8733 91 -84 642 C ATOM 2296 CE2 PHE A 333 -24.949 -19.800 -4.110 1.00 77.57 C ANISOU 2296 CE2 PHE A 333 10301 9438 9736 189 -70 613 C ATOM 2297 CZ PHE A 333 -25.568 -18.767 -3.433 1.00 77.82 C ANISOU 2297 CZ PHE A 333 10277 9516 9774 151 -64 651 C ATOM 2298 N LEU A 334 -30.237 -21.496 -3.695 1.00 67.70 N ANISOU 2298 N LEU A 334 9006 8107 8609 -123 -188 586 N ATOM 2299 CA LEU A 334 -30.958 -20.883 -2.588 1.00 63.22 C ANISOU 2299 CA LEU A 334 8365 7594 8064 -174 -143 633 C ATOM 2300 C LEU A 334 -31.436 -21.941 -1.600 1.00 65.37 C ANISOU 2300 C LEU A 334 8650 7811 8378 -259 -127 683 C ATOM 2301 O LEU A 334 -31.443 -21.722 -0.389 1.00 73.14 O ANISOU 2301 O LEU A 334 9614 8831 9343 -283 -70 739 O ATOM 2302 CB LEU A 334 -32.154 -20.092 -3.119 1.00 60.59 C ANISOU 2302 CB LEU A 334 7945 7319 7757 -200 -166 603 C ATOM 2303 CG LEU A 334 -31.817 -18.868 -3.974 1.00 61.07 C ANISOU 2303 CG LEU A 334 7988 7436 7779 -127 -185 581 C ATOM 2304 CD1 LEU A 334 -33.065 -18.340 -4.663 1.00 71.61 C ANISOU 2304 CD1 LEU A 334 9250 8805 9154 -152 -241 552 C ATOM 2305 CD2 LEU A 334 -31.178 -17.779 -3.128 1.00 56.00 C ANISOU 2305 CD2 LEU A 334 7314 6842 7119 -83 -131 614 C ATOM 2306 N LEU A 335 -31.836 -23.092 -2.128 1.00 71.91 N ANISOU 2306 N LEU A 335 9516 8551 9257 -307 -180 662 N ATOM 2307 CA LEU A 335 -32.366 -24.176 -1.307 1.00 76.21 C ANISOU 2307 CA LEU A 335 10072 9024 9859 -406 -175 723 C ATOM 2308 C LEU A 335 -31.314 -24.725 -0.345 1.00 67.69 C ANISOU 2308 C LEU A 335 9072 7894 8754 -384 -153 795 C ATOM 2309 O LEU A 335 -31.609 -25.002 0.817 1.00 60.34 O ANISOU 2309 O LEU A 335 8137 6969 7820 -453 -110 882 O ATOM 2310 CB LEU A 335 -32.890 -25.303 -2.201 1.00 83.57 C ANISOU 2310 CB LEU A 335 11036 9846 10870 -455 -261 675 C ATOM 2311 CG LEU A 335 -33.573 -26.475 -1.494 1.00 83.02 C ANISOU 2311 CG LEU A 335 10972 9683 10890 -578 -270 745 C ATOM 2312 CD1 LEU A 335 -34.839 -26.017 -0.786 1.00 86.94 C ANISOU 2312 CD1 LEU A 335 11350 10268 11416 -679 -206 797 C ATOM 2313 CD2 LEU A 335 -33.887 -27.585 -2.485 1.00 82.20 C ANISOU 2313 CD2 LEU A 335 10913 9446 10875 -610 -377 676 C ATOM 2314 N MET A 336 -30.087 -24.872 -0.833 1.00 67.14 N ANISOU 2314 N MET A 336 9068 7780 8661 -287 -184 759 N ATOM 2315 CA MET A 336 -29.013 -25.469 -0.044 1.00 71.46 C ANISOU 2315 CA MET A 336 9687 8263 9202 -252 -188 818 C ATOM 2316 C MET A 336 -28.475 -24.526 1.031 1.00 71.10 C ANISOU 2316 C MET A 336 9619 8314 9083 -222 -131 874 C ATOM 2317 O MET A 336 -27.607 -24.909 1.814 1.00 72.29 O ANISOU 2317 O MET A 336 9822 8424 9219 -194 -143 932 O ATOM 2318 CB MET A 336 -27.869 -25.914 -0.961 1.00 70.68 C ANISOU 2318 CB MET A 336 9646 8093 9118 -148 -235 746 C ATOM 2319 CG MET A 336 -28.165 -27.178 -1.761 1.00 66.36 C ANISOU 2319 CG MET A 336 9152 7413 8648 -168 -307 689 C ATOM 2320 SD MET A 336 -26.760 -27.743 -2.745 1.00 99.84 S ANISOU 2320 SD MET A 336 13457 11579 12900 -28 -346 585 S ATOM 2321 CE MET A 336 -25.595 -28.188 -1.461 1.00105.11 C ANISOU 2321 CE MET A 336 14161 12178 13597 14 -352 683 C ATOM 2322 N TRP A 337 -28.987 -23.299 1.071 1.00 71.30 N ANISOU 2322 N TRP A 337 9567 8457 9068 -222 -83 852 N ATOM 2323 CA TRP A 337 -28.560 -22.330 2.079 1.00 65.72 C ANISOU 2323 CA TRP A 337 8837 7840 8295 -193 -38 883 C ATOM 2324 C TRP A 337 -29.596 -22.134 3.187 1.00 65.93 C ANISOU 2324 C TRP A 337 8823 7939 8289 -279 23 933 C ATOM 2325 O TRP A 337 -29.318 -21.486 4.197 1.00 63.23 O ANISOU 2325 O TRP A 337 8477 7671 7879 -263 60 956 O ATOM 2326 CB TRP A 337 -28.264 -20.977 1.433 1.00 68.54 C ANISOU 2326 CB TRP A 337 9135 8272 8635 -121 -28 818 C ATOM 2327 CG TRP A 337 -26.827 -20.767 1.093 1.00 71.18 C ANISOU 2327 CG TRP A 337 9498 8584 8961 -29 -52 803 C ATOM 2328 CD1 TRP A 337 -26.285 -20.688 -0.156 1.00 73.51 C ANISOU 2328 CD1 TRP A 337 9796 8863 9273 30 -71 752 C ATOM 2329 CD2 TRP A 337 -25.741 -20.603 2.014 1.00 73.51 C ANISOU 2329 CD2 TRP A 337 9817 8883 9231 15 -58 840 C ATOM 2330 NE1 TRP A 337 -24.929 -20.486 -0.072 1.00 55.72 N ANISOU 2330 NE1 TRP A 337 7551 6603 7017 104 -75 757 N ATOM 2331 CE2 TRP A 337 -24.570 -20.430 1.249 1.00 71.72 C ANISOU 2331 CE2 TRP A 337 9588 8635 9027 97 -77 808 C ATOM 2332 CE3 TRP A 337 -25.644 -20.587 3.410 1.00 76.14 C ANISOU 2332 CE3 TRP A 337 10171 9241 9517 -8 -51 895 C ATOM 2333 CZ2 TRP A 337 -23.318 -20.243 1.832 1.00 69.26 C ANISOU 2333 CZ2 TRP A 337 9281 8319 8718 155 -98 829 C ATOM 2334 CZ3 TRP A 337 -24.399 -20.401 3.986 1.00 75.02 C ANISOU 2334 CZ3 TRP A 337 10051 9093 9362 53 -84 914 C ATOM 2335 CH2 TRP A 337 -23.254 -20.232 3.199 1.00 72.39 C ANISOU 2335 CH2 TRP A 337 9700 8730 9076 133 -111 880 C ATOM 2336 N CYS A 338 -30.788 -22.690 2.994 1.00 76.46 N ANISOU 2336 N CYS A 338 10123 9256 9672 -370 35 942 N ATOM 2337 CA CYS A 338 -31.881 -22.512 3.948 1.00 81.10 C ANISOU 2337 CA CYS A 338 10649 9928 10237 -457 113 984 C ATOM 2338 C CYS A 338 -31.578 -23.102 5.327 1.00 78.65 C ANISOU 2338 C CYS A 338 10406 9622 9854 -504 148 1093 C ATOM 2339 O CYS A 338 -31.788 -22.438 6.343 1.00 70.59 O ANISOU 2339 O CYS A 338 9359 8714 8747 -512 220 1108 O ATOM 2340 CB CYS A 338 -33.173 -23.122 3.399 1.00 69.29 C ANISOU 2340 CB CYS A 338 9092 8401 8833 -555 110 980 C ATOM 2341 SG CYS A 338 -33.982 -22.132 2.133 1.00 75.56 S ANISOU 2341 SG CYS A 338 9776 9246 9689 -520 83 865 S ATOM 2342 N PRO A 339 -31.089 -24.352 5.370 1.00 79.84 N ANISOU 2342 N PRO A 339 10651 9649 10037 -532 92 1166 N ATOM 2343 CA PRO A 339 -30.856 -24.991 6.670 1.00 89.23 C ANISOU 2343 CA PRO A 339 11915 10834 11155 -586 111 1292 C ATOM 2344 C PRO A 339 -30.048 -24.112 7.618 1.00 86.08 C ANISOU 2344 C PRO A 339 11542 10535 10629 -513 132 1294 C ATOM 2345 O PRO A 339 -30.340 -24.067 8.813 1.00 93.56 O ANISOU 2345 O PRO A 339 12508 11569 11473 -567 193 1369 O ATOM 2346 CB PRO A 339 -30.064 -26.250 6.304 1.00 89.23 C ANISOU 2346 CB PRO A 339 12016 10659 11230 -572 9 1339 C ATOM 2347 CG PRO A 339 -30.459 -26.548 4.907 1.00 88.20 C ANISOU 2347 CG PRO A 339 11848 10448 11216 -569 -35 1247 C ATOM 2348 CD PRO A 339 -30.670 -25.214 4.251 1.00 77.37 C ANISOU 2348 CD PRO A 339 10386 9193 9820 -505 1 1132 C ATOM 2349 N PHE A 340 -29.044 -23.422 7.087 1.00 74.70 N ANISOU 2349 N PHE A 340 10101 9087 9195 -397 82 1213 N ATOM 2350 CA PHE A 340 -28.192 -22.572 7.908 1.00 71.05 C ANISOU 2350 CA PHE A 340 9658 8702 8635 -326 79 1203 C ATOM 2351 C PHE A 340 -28.951 -21.383 8.489 1.00 74.26 C ANISOU 2351 C PHE A 340 9989 9260 8965 -336 166 1148 C ATOM 2352 O PHE A 340 -29.101 -21.272 9.704 1.00 78.59 O ANISOU 2352 O PHE A 340 10567 9896 9398 -367 212 1194 O ATOM 2353 CB PHE A 340 -26.997 -22.062 7.103 1.00 61.17 C ANISOU 2353 CB PHE A 340 8402 7406 7435 -211 11 1128 C ATOM 2354 CG PHE A 340 -26.121 -21.113 7.866 1.00 62.61 C ANISOU 2354 CG PHE A 340 8587 7658 7542 -142 -7 1106 C ATOM 2355 CD1 PHE A 340 -25.136 -21.589 8.715 1.00 67.76 C ANISOU 2355 CD1 PHE A 340 9321 8278 8148 -116 -71 1174 C ATOM 2356 CD2 PHE A 340 -26.289 -19.745 7.744 1.00 65.19 C ANISOU 2356 CD2 PHE A 340 8838 8073 7859 -104 26 1016 C ATOM 2357 CE1 PHE A 340 -24.330 -20.718 9.425 1.00 59.48 C ANISOU 2357 CE1 PHE A 340 8273 7291 7036 -56 -104 1146 C ATOM 2358 CE2 PHE A 340 -25.486 -18.868 8.451 1.00 68.78 C ANISOU 2358 CE2 PHE A 340 9295 8578 8259 -45 -4 985 C ATOM 2359 CZ PHE A 340 -24.505 -19.356 9.292 1.00 63.46 C ANISOU 2359 CZ PHE A 340 8700 7879 7533 -23 -70 1047 C ATOM 2360 N PHE A 341 -29.429 -20.501 7.616 1.00 72.38 N ANISOU 2360 N PHE A 341 9657 9054 8791 -305 185 1047 N ATOM 2361 CA PHE A 341 -30.035 -19.243 8.044 1.00 73.57 C ANISOU 2361 CA PHE A 341 9725 9329 8898 -287 250 971 C ATOM 2362 C PHE A 341 -31.312 -19.428 8.865 1.00 78.27 C ANISOU 2362 C PHE A 341 10278 10021 9440 -380 356 1001 C ATOM 2363 O PHE A 341 -31.593 -18.631 9.761 1.00 75.20 O ANISOU 2363 O PHE A 341 9859 9750 8964 -365 420 958 O ATOM 2364 CB PHE A 341 -30.309 -18.347 6.834 1.00 77.87 C ANISOU 2364 CB PHE A 341 10181 9865 9541 -237 231 873 C ATOM 2365 CG PHE A 341 -29.065 -17.785 6.209 1.00 57.37 C ANISOU 2365 CG PHE A 341 7608 7217 6975 -144 156 837 C ATOM 2366 CD1 PHE A 341 -28.360 -16.770 6.835 1.00 64.17 C ANISOU 2366 CD1 PHE A 341 8467 8123 7793 -80 142 796 C ATOM 2367 CD2 PHE A 341 -28.596 -18.273 5.000 1.00 64.73 C ANISOU 2367 CD2 PHE A 341 8558 8058 7978 -122 102 839 C ATOM 2368 CE1 PHE A 341 -27.211 -16.251 6.267 1.00 67.55 C ANISOU 2368 CE1 PHE A 341 8899 8502 8264 -8 77 773 C ATOM 2369 CE2 PHE A 341 -27.447 -17.758 4.426 1.00 57.27 C ANISOU 2369 CE2 PHE A 341 7621 7080 7058 -42 52 813 C ATOM 2370 CZ PHE A 341 -26.754 -16.746 5.060 1.00 61.31 C ANISOU 2370 CZ PHE A 341 8120 7634 7542 9 41 788 C ATOM 2371 N ILE A 342 -32.084 -20.467 8.563 1.00 81.26 N ANISOU 2371 N ILE A 342 10647 10353 9876 -475 377 1068 N ATOM 2372 CA ILE A 342 -33.284 -20.759 9.340 1.00 85.03 C ANISOU 2372 CA ILE A 342 11072 10922 10314 -580 488 1116 C ATOM 2373 C ILE A 342 -32.899 -21.230 10.736 1.00 84.84 C ANISOU 2373 C ILE A 342 11148 10952 10136 -620 527 1222 C ATOM 2374 O ILE A 342 -33.407 -20.725 11.735 1.00 86.51 O ANISOU 2374 O ILE A 342 11329 11308 10232 -639 629 1211 O ATOM 2375 CB ILE A 342 -34.154 -21.837 8.670 1.00 85.97 C ANISOU 2375 CB ILE A 342 11156 10959 10551 -686 486 1173 C ATOM 2376 CG1 ILE A 342 -34.758 -21.297 7.373 1.00 86.11 C ANISOU 2376 CG1 ILE A 342 11065 10953 10701 -655 451 1064 C ATOM 2377 CG2 ILE A 342 -35.260 -22.285 9.614 1.00 79.22 C ANISOU 2377 CG2 ILE A 342 10251 10197 9652 -813 609 1256 C ATOM 2378 CD1 ILE A 342 -35.562 -22.320 6.603 1.00 85.32 C ANISOU 2378 CD1 ILE A 342 10930 10761 10726 -752 421 1099 C ATOM 2379 N THR A 343 -32.004 -22.209 10.795 1.00 80.87 N ANISOU 2379 N THR A 343 10766 10335 9628 -628 442 1323 N ATOM 2380 CA THR A 343 -31.507 -22.712 12.066 1.00 83.75 C ANISOU 2380 CA THR A 343 11245 10733 9846 -659 448 1441 C ATOM 2381 C THR A 343 -30.778 -21.603 12.811 1.00 81.18 C ANISOU 2381 C THR A 343 10944 10513 9388 -560 441 1364 C ATOM 2382 O THR A 343 -30.762 -21.563 14.042 1.00 85.76 O ANISOU 2382 O THR A 343 11585 11201 9801 -585 488 1418 O ATOM 2383 CB THR A 343 -30.539 -23.873 11.848 1.00 90.14 C ANISOU 2383 CB THR A 343 12171 11372 10706 -657 326 1545 C ATOM 2384 OG1 THR A 343 -31.138 -24.837 10.975 1.00 96.74 O ANISOU 2384 OG1 THR A 343 12983 12085 11691 -732 308 1582 O ATOM 2385 CG2 THR A 343 -30.189 -24.537 13.171 1.00 91.46 C ANISOU 2385 CG2 THR A 343 12460 11563 10726 -709 322 1698 C ATOM 2386 N ASN A 344 -30.169 -20.704 12.049 1.00 78.51 N ANISOU 2386 N ASN A 344 10563 10143 9124 -452 377 1240 N ATOM 2387 CA ASN A 344 -29.444 -19.579 12.616 1.00 80.68 C ANISOU 2387 CA ASN A 344 10850 10494 9312 -358 350 1152 C ATOM 2388 C ASN A 344 -30.383 -18.676 13.409 1.00 78.54 C ANISOU 2388 C ASN A 344 10512 10391 8938 -368 469 1073 C ATOM 2389 O ASN A 344 -30.146 -18.403 14.584 1.00 75.56 O ANISOU 2389 O ASN A 344 10197 10118 8397 -358 490 1075 O ATOM 2390 CB ASN A 344 -28.767 -18.786 11.498 1.00 81.17 C ANISOU 2390 CB ASN A 344 10857 10480 9503 -259 271 1044 C ATOM 2391 CG ASN A 344 -27.637 -17.920 12.000 1.00 78.44 C ANISOU 2391 CG ASN A 344 10545 10156 9104 -167 198 985 C ATOM 2392 OD1 ASN A 344 -27.153 -18.097 13.118 1.00 81.55 O ANISOU 2392 OD1 ASN A 344 11024 10597 9365 -168 175 1031 O ATOM 2393 ND2 ASN A 344 -27.200 -16.981 11.168 1.00 77.47 N ANISOU 2393 ND2 ASN A 344 10356 9994 9083 -93 153 888 N ATOM 2394 N ILE A 345 -31.454 -18.223 12.763 1.00 80.87 N ANISOU 2394 N ILE A 345 10682 10717 9329 -384 542 997 N ATOM 2395 CA ILE A 345 -32.426 -17.351 13.415 1.00 86.03 C ANISOU 2395 CA ILE A 345 11247 11526 9915 -382 661 903 C ATOM 2396 C ILE A 345 -33.155 -18.084 14.535 1.00 77.07 C ANISOU 2396 C ILE A 345 10142 10509 8633 -488 785 1004 C ATOM 2397 O ILE A 345 -33.549 -17.474 15.527 1.00 76.96 O ANISOU 2397 O ILE A 345 10111 10651 8479 -476 881 943 O ATOM 2398 CB ILE A 345 -33.469 -16.791 12.417 1.00 92.81 C ANISOU 2398 CB ILE A 345 11951 12380 10935 -376 700 809 C ATOM 2399 CG1 ILE A 345 -34.242 -17.930 11.743 1.00110.45 C ANISOU 2399 CG1 ILE A 345 14148 14548 13269 -484 723 908 C ATOM 2400 CG2 ILE A 345 -32.790 -15.915 11.375 1.00 82.65 C ANISOU 2400 CG2 ILE A 345 10638 10995 9771 -273 587 715 C ATOM 2401 CD1 ILE A 345 -35.406 -17.465 10.891 1.00118.65 C ANISOU 2401 CD1 ILE A 345 15028 15599 14454 -491 760 825 C ATOM 2402 N THR A 346 -33.331 -19.391 14.372 1.00 74.35 N ANISOU 2402 N THR A 346 9842 10090 8319 -593 784 1158 N ATOM 2403 CA THR A 346 -34.026 -20.197 15.368 1.00 79.84 C ANISOU 2403 CA THR A 346 10566 10882 8887 -715 902 1289 C ATOM 2404 C THR A 346 -33.183 -20.328 16.630 1.00 87.29 C ANISOU 2404 C THR A 346 11663 11894 9610 -702 880 1362 C ATOM 2405 O THR A 346 -33.698 -20.260 17.746 1.00 82.06 O ANISOU 2405 O THR A 346 11015 11398 8765 -750 1003 1391 O ATOM 2406 CB THR A 346 -34.341 -21.604 14.833 1.00 80.83 C ANISOU 2406 CB THR A 346 10710 10875 9126 -835 880 1446 C ATOM 2407 OG1 THR A 346 -35.179 -21.505 13.675 1.00 84.61 O ANISOU 2407 OG1 THR A 346 11049 11298 9801 -852 889 1374 O ATOM 2408 CG2 THR A 346 -35.051 -22.432 15.895 1.00 82.70 C ANISOU 2408 CG2 THR A 346 10978 11210 9236 -977 1005 1606 C ATOM 2409 N LEU A 347 -31.881 -20.519 16.445 1.00 93.43 N ANISOU 2409 N LEU A 347 12549 12549 10401 -634 723 1389 N ATOM 2410 CA LEU A 347 -30.960 -20.645 17.566 1.00 92.60 C ANISOU 2410 CA LEU A 347 12592 12489 10103 -611 663 1456 C ATOM 2411 C LEU A 347 -30.896 -19.343 18.360 1.00 93.66 C ANISOU 2411 C LEU A 347 12713 12788 10086 -526 704 1300 C ATOM 2412 O LEU A 347 -30.539 -19.340 19.538 1.00101.80 O ANISOU 2412 O LEU A 347 13852 13925 10901 -526 704 1340 O ATOM 2413 CB LEU A 347 -29.569 -21.029 17.061 1.00 82.73 C ANISOU 2413 CB LEU A 347 11428 11064 8943 -541 477 1492 C ATOM 2414 CG LEU A 347 -28.498 -21.276 18.123 1.00 84.22 C ANISOU 2414 CG LEU A 347 11768 11268 8962 -511 375 1574 C ATOM 2415 CD1 LEU A 347 -28.969 -22.296 19.148 1.00 77.14 C ANISOU 2415 CD1 LEU A 347 10975 10436 7900 -633 438 1768 C ATOM 2416 CD2 LEU A 347 -27.209 -21.740 17.465 1.00 85.57 C ANISOU 2416 CD2 LEU A 347 11989 11252 9272 -442 197 1606 C ATOM 2417 N VAL A 348 -31.246 -18.238 17.709 1.00 92.42 N ANISOU 2417 N VAL A 348 12427 12646 10043 -452 728 1122 N ATOM 2418 CA VAL A 348 -31.265 -16.935 18.363 1.00 95.31 C ANISOU 2418 CA VAL A 348 12765 13146 10303 -364 761 948 C ATOM 2419 C VAL A 348 -32.581 -16.700 19.099 1.00101.30 C ANISOU 2419 C VAL A 348 13450 14098 10940 -416 957 906 C ATOM 2420 O VAL A 348 -32.589 -16.236 20.239 1.00104.83 O ANISOU 2420 O VAL A 348 13950 14705 11176 -391 1014 847 O ATOM 2421 CB VAL A 348 -31.069 -15.795 17.343 1.00 94.52 C ANISOU 2421 CB VAL A 348 12556 12963 10395 -259 693 778 C ATOM 2422 CG1 VAL A 348 -31.259 -14.441 18.013 1.00 97.69 C ANISOU 2422 CG1 VAL A 348 12915 13489 10713 -172 731 586 C ATOM 2423 CG2 VAL A 348 -29.695 -15.886 16.694 1.00 86.85 C ANISOU 2423 CG2 VAL A 348 11647 11826 9527 -201 515 805 C ATOM 2424 N LEU A 349 -33.690 -17.025 18.442 1.00100.08 N ANISOU 2424 N LEU A 349 13169 13937 10920 -487 1061 930 N ATOM 2425 CA LEU A 349 -35.016 -16.709 18.967 1.00 97.63 C ANISOU 2425 CA LEU A 349 12743 13808 10545 -529 1256 869 C ATOM 2426 C LEU A 349 -35.573 -17.793 19.887 1.00 96.50 C ANISOU 2426 C LEU A 349 12656 13780 10230 -671 1390 1051 C ATOM 2427 O LEU A 349 -36.148 -17.490 20.932 1.00 97.64 O ANISOU 2427 O LEU A 349 12789 14128 10180 -686 1542 1013 O ATOM 2428 CB LEU A 349 -35.996 -16.465 17.817 1.00 95.57 C ANISOU 2428 CB LEU A 349 12296 13489 10528 -536 1296 799 C ATOM 2429 CG LEU A 349 -35.630 -15.344 16.841 1.00 90.42 C ANISOU 2429 CG LEU A 349 11573 12730 10054 -406 1178 631 C ATOM 2430 CD1 LEU A 349 -36.742 -15.152 15.823 1.00 88.32 C ANISOU 2430 CD1 LEU A 349 11125 12430 10001 -421 1223 576 C ATOM 2431 CD2 LEU A 349 -35.341 -14.042 17.572 1.00 86.75 C ANISOU 2431 CD2 LEU A 349 11112 12365 9486 -284 1180 447 C ATOM 2432 N CYS A 350 -35.410 -19.054 19.501 1.00 95.98 N ANISOU 2432 N CYS A 350 12650 13583 10234 -776 1337 1250 N ATOM 2433 CA CYS A 350 -35.982 -20.154 20.271 1.00101.83 C ANISOU 2433 CA CYS A 350 13440 14406 10846 -930 1456 1452 C ATOM 2434 C CYS A 350 -35.209 -20.394 21.564 1.00104.23 C ANISOU 2434 C CYS A 350 13935 14804 10863 -934 1435 1550 C ATOM 2435 O CYS A 350 -34.085 -20.895 21.545 1.00105.27 O ANISOU 2435 O CYS A 350 14213 14802 10983 -911 1266 1644 O ATOM 2436 CB CYS A 350 -36.016 -21.438 19.441 1.00101.41 C ANISOU 2436 CB CYS A 350 13399 14155 10978 -1039 1383 1629 C ATOM 2437 SG CYS A 350 -36.954 -22.775 20.212 1.00 85.85 S ANISOU 2437 SG CYS A 350 11446 12259 8915 -1256 1539 1886 S ATOM 2438 N ASP A 351 -35.825 -20.034 22.685 1.00107.94 N ANISOU 2438 N ASP A 351 14400 15512 11100 -958 1607 1522 N ATOM 2439 CA ASP A 351 -35.206 -20.205 23.994 1.00113.83 C ANISOU 2439 CA ASP A 351 15332 16384 11535 -964 1599 1609 C ATOM 2440 C ASP A 351 -35.389 -21.631 24.513 1.00116.71 C ANISOU 2440 C ASP A 351 15803 16742 11801 -1136 1642 1907 C ATOM 2441 O ASP A 351 -34.560 -22.134 25.272 1.00121.36 O ANISOU 2441 O ASP A 351 16582 17328 12202 -1150 1545 2048 O ATOM 2442 CB ASP A 351 -35.806 -19.215 24.996 1.00119.70 C ANISOU 2442 CB ASP A 351 16033 17402 12045 -915 1774 1444 C ATOM 2443 CG ASP A 351 -35.487 -17.769 24.657 1.00122.94 C ANISOU 2443 CG ASP A 351 16371 17808 12534 -737 1704 1152 C ATOM 2444 OD1 ASP A 351 -34.367 -17.501 24.172 1.00117.97 O ANISOU 2444 OD1 ASP A 351 15810 17011 12001 -644 1494 1105 O ATOM 2445 OD2 ASP A 351 -36.355 -16.900 24.881 1.00127.27 O ANISOU 2445 OD2 ASP A 351 16785 18515 13056 -691 1860 970 O ATOM 2446 N SER A 352 -36.478 -22.274 24.105 1.00113.38 N ANISOU 2446 N SER A 352 15255 16310 11516 -1271 1776 2007 N ATOM 2447 CA SER A 352 -36.807 -23.611 24.590 1.00112.11 C ANISOU 2447 CA SER A 352 15173 16141 11284 -1455 1836 2298 C ATOM 2448 C SER A 352 -36.107 -24.717 23.803 1.00109.27 C ANISOU 2448 C SER A 352 14899 15487 11131 -1498 1633 2464 C ATOM 2449 O SER A 352 -36.089 -25.871 24.230 1.00113.89 O ANISOU 2449 O SER A 352 15593 16016 11664 -1633 1622 2720 O ATOM 2450 CB SER A 352 -38.320 -23.829 24.541 1.00116.12 C ANISOU 2450 CB SER A 352 15492 16767 11860 -1593 2074 2335 C ATOM 2451 OG SER A 352 -38.820 -23.631 23.230 1.00116.58 O ANISOU 2451 OG SER A 352 15366 16684 12245 -1570 2043 2212 O ATOM 2452 N CYS A 353 -35.540 -24.367 22.654 1.00102.53 N ANISOU 2452 N CYS A 353 13997 14446 10514 -1382 1474 2320 N ATOM 2453 CA CYS A 353 -34.860 -25.347 21.813 1.00 95.28 C ANISOU 2453 CA CYS A 353 13145 13251 9804 -1400 1284 2437 C ATOM 2454 C CYS A 353 -33.516 -25.767 22.395 1.00 90.58 C ANISOU 2454 C CYS A 353 12762 12575 9078 -1348 1105 2549 C ATOM 2455 O CYS A 353 -32.817 -24.970 23.020 1.00 93.52 O ANISOU 2455 O CYS A 353 13207 13055 9270 -1236 1060 2450 O ATOM 2456 CB CYS A 353 -34.646 -24.789 20.408 1.00 90.97 C ANISOU 2456 CB CYS A 353 12484 12556 9525 -1286 1182 2240 C ATOM 2457 SG CYS A 353 -36.166 -24.497 19.479 1.00105.66 S ANISOU 2457 SG CYS A 353 14096 14448 11600 -1348 1333 2130 S ATOM 2458 N ASN A 354 -33.164 -27.029 22.180 1.00 88.76 N ANISOU 2458 N ASN A 354 12626 12147 8954 -1427 990 2753 N ATOM 2459 CA ASN A 354 -31.875 -27.551 22.605 1.00 89.02 C ANISOU 2459 CA ASN A 354 12846 12063 8913 -1374 794 2869 C ATOM 2460 C ASN A 354 -30.760 -26.947 21.760 1.00 86.01 C ANISOU 2460 C ASN A 354 12450 11550 8679 -1195 617 2682 C ATOM 2461 O ASN A 354 -30.659 -27.222 20.565 1.00 82.25 O ANISOU 2461 O ASN A 354 11900 10888 8462 -1168 545 2625 O ATOM 2462 CB ASN A 354 -31.867 -29.074 22.481 1.00 91.59 C ANISOU 2462 CB ASN A 354 13256 12183 9360 -1502 713 3124 C ATOM 2463 CG ASN A 354 -30.637 -29.703 23.098 1.00 99.11 C ANISOU 2463 CG ASN A 354 14409 13028 10222 -1459 516 3279 C ATOM 2464 OD1 ASN A 354 -29.526 -29.186 22.969 1.00107.01 O ANISOU 2464 OD1 ASN A 354 15451 13985 11223 -1303 366 3158 O ATOM 2465 ND2 ASN A 354 -30.829 -30.825 23.778 1.00103.35 N ANISOU 2465 ND2 ASN A 354 15065 13516 10688 -1601 509 3555 N ATOM 2466 N GLN A 355 -29.923 -26.125 22.384 1.00 91.64 N ANISOU 2466 N GLN A 355 13232 12363 9222 -1077 549 2587 N ATOM 2467 CA GLN A 355 -28.885 -25.402 21.659 1.00 97.99 C ANISOU 2467 CA GLN A 355 14003 13070 10157 -913 401 2403 C ATOM 2468 C GLN A 355 -27.756 -26.314 21.191 1.00 95.08 C ANISOU 2468 C GLN A 355 13720 12461 9943 -870 191 2503 C ATOM 2469 O GLN A 355 -27.133 -26.058 20.160 1.00 88.58 O ANISOU 2469 O GLN A 355 12830 11505 9322 -769 96 2377 O ATOM 2470 CB GLN A 355 -28.315 -24.275 22.521 1.00 99.87 C ANISOU 2470 CB GLN A 355 14287 13478 10179 -809 377 2273 C ATOM 2471 CG GLN A 355 -29.279 -23.123 22.738 1.00107.54 C ANISOU 2471 CG GLN A 355 15145 14662 11054 -800 563 2096 C ATOM 2472 CD GLN A 355 -28.590 -21.880 23.259 1.00118.75 C ANISOU 2472 CD GLN A 355 16586 16193 12342 -667 501 1909 C ATOM 2473 OE1 GLN A 355 -27.547 -21.960 23.910 1.00119.77 O ANISOU 2473 OE1 GLN A 355 16847 16309 12350 -616 350 1954 O ATOM 2474 NE2 GLN A 355 -29.165 -20.717 22.968 1.00123.11 N ANISOU 2474 NE2 GLN A 355 17005 16842 12929 -610 604 1695 N ATOM 2475 N THR A 356 -27.494 -27.375 21.945 1.00 92.42 N ANISOU 2475 N THR A 356 13531 12071 9515 -944 121 2731 N ATOM 2476 CA THR A 356 -26.429 -28.304 21.592 1.00 94.87 C ANISOU 2476 CA THR A 356 13925 12145 9978 -897 -87 2832 C ATOM 2477 C THR A 356 -26.691 -28.916 20.221 1.00 93.31 C ANISOU 2477 C THR A 356 13631 11742 10082 -911 -98 2800 C ATOM 2478 O THR A 356 -25.827 -28.894 19.343 1.00 87.97 O ANISOU 2478 O THR A 356 12919 10916 9589 -797 -223 2697 O ATOM 2479 CB THR A 356 -26.304 -29.434 22.626 1.00 95.36 C ANISOU 2479 CB THR A 356 14160 12170 9903 -995 -153 3111 C ATOM 2480 OG1 THR A 356 -26.168 -28.872 23.937 1.00 98.60 O ANISOU 2480 OG1 THR A 356 14671 12798 9995 -992 -130 3143 O ATOM 2481 CG2 THR A 356 -25.097 -30.307 22.319 1.00100.72 C ANISOU 2481 CG2 THR A 356 14921 12600 10747 -919 -390 3196 C ATOM 2482 N THR A 357 -27.890 -29.461 20.046 1.00 93.01 N ANISOU 2482 N THR A 357 13547 11704 10091 -1055 34 2884 N ATOM 2483 CA THR A 357 -28.276 -30.074 18.783 1.00 96.84 C ANISOU 2483 CA THR A 357 13944 12001 10848 -1084 23 2850 C ATOM 2484 C THR A 357 -28.325 -29.036 17.668 1.00 99.77 C ANISOU 2484 C THR A 357 14165 12402 11342 -979 60 2595 C ATOM 2485 O THR A 357 -27.900 -29.303 16.545 1.00101.29 O ANISOU 2485 O THR A 357 14316 12426 11743 -913 -30 2512 O ATOM 2486 CB THR A 357 -29.650 -30.759 18.889 1.00 98.99 C ANISOU 2486 CB THR A 357 14179 12289 11143 -1272 164 2985 C ATOM 2487 OG1 THR A 357 -30.633 -29.806 19.313 1.00101.79 O ANISOU 2487 OG1 THR A 357 14436 12893 11345 -1318 364 2906 O ATOM 2488 CG2 THR A 357 -29.601 -31.906 19.885 1.00103.45 C ANISOU 2488 CG2 THR A 357 14898 12793 11615 -1392 118 3268 C ATOM 2489 N LEU A 358 -28.843 -27.852 17.980 1.00 75.07 N ANISOU 2489 N LEU A 358 10958 9487 8080 -962 192 2471 N ATOM 2490 CA LEU A 358 -28.921 -26.777 17.001 1.00 72.82 C ANISOU 2490 CA LEU A 358 10534 9234 7899 -866 224 2243 C ATOM 2491 C LEU A 358 -27.534 -26.402 16.486 1.00 71.54 C ANISOU 2491 C LEU A 358 10392 8975 7814 -710 68 2139 C ATOM 2492 O LEU A 358 -27.346 -26.179 15.291 1.00 78.62 O ANISOU 2492 O LEU A 358 11206 9781 8886 -644 35 2016 O ATOM 2493 CB LEU A 358 -29.603 -25.552 17.607 1.00 72.93 C ANISOU 2493 CB LEU A 358 10475 9486 7747 -861 372 2133 C ATOM 2494 CG LEU A 358 -31.121 -25.642 17.770 1.00 81.51 C ANISOU 2494 CG LEU A 358 11469 10687 8812 -995 558 2167 C ATOM 2495 CD1 LEU A 358 -31.639 -24.430 18.524 1.00 83.38 C ANISOU 2495 CD1 LEU A 358 11648 11166 8867 -966 696 2049 C ATOM 2496 CD2 LEU A 358 -31.805 -25.753 16.416 1.00 78.66 C ANISOU 2496 CD2 LEU A 358 10975 10222 8692 -1016 575 2085 C ATOM 2497 N GLN A 359 -26.566 -26.328 17.392 1.00 73.46 N ANISOU 2497 N GLN A 359 10742 9246 7923 -653 -28 2191 N ATOM 2498 CA GLN A 359 -25.192 -26.039 17.005 1.00 81.33 C ANISOU 2498 CA GLN A 359 11748 10150 9002 -512 -181 2109 C ATOM 2499 C GLN A 359 -24.629 -27.182 16.172 1.00 81.74 C ANISOU 2499 C GLN A 359 11825 9972 9259 -493 -297 2170 C ATOM 2500 O GLN A 359 -24.015 -26.960 15.129 1.00 85.09 O ANISOU 2500 O GLN A 359 12181 10307 9844 -397 -352 2049 O ATOM 2501 CB GLN A 359 -24.319 -25.812 18.239 1.00 88.32 C ANISOU 2501 CB GLN A 359 12744 11112 9700 -466 -275 2164 C ATOM 2502 CG GLN A 359 -24.617 -24.515 18.976 1.00 91.41 C ANISOU 2502 CG GLN A 359 13110 11722 9901 -445 -189 2048 C ATOM 2503 CD GLN A 359 -23.734 -24.317 20.190 1.00 97.87 C ANISOU 2503 CD GLN A 359 14048 12614 10526 -398 -303 2093 C ATOM 2504 OE1 GLN A 359 -22.722 -24.999 20.354 1.00 95.90 O ANISOU 2504 OE1 GLN A 359 13879 12242 10316 -356 -467 2190 O ATOM 2505 NE2 GLN A 359 -24.114 -23.379 21.051 1.00104.33 N ANISOU 2505 NE2 GLN A 359 14874 13632 11136 -398 -224 2014 N ATOM 2506 N MET A 360 -24.845 -28.406 16.640 1.00 87.29 N ANISOU 2506 N MET A 360 12627 10581 9956 -584 -333 2360 N ATOM 2507 CA MET A 360 -24.382 -29.590 15.931 1.00 87.58 C ANISOU 2507 CA MET A 360 12697 10383 10196 -569 -450 2420 C ATOM 2508 C MET A 360 -24.924 -29.593 14.506 1.00 80.21 C ANISOU 2508 C MET A 360 11649 9374 9453 -567 -393 2287 C ATOM 2509 O MET A 360 -24.233 -29.994 13.570 1.00 80.76 O ANISOU 2509 O MET A 360 11701 9290 9696 -482 -486 2217 O ATOM 2510 CB MET A 360 -24.824 -30.853 16.674 1.00 94.17 C ANISOU 2510 CB MET A 360 13649 11132 10998 -699 -475 2656 C ATOM 2511 CG MET A 360 -24.259 -32.144 16.103 1.00 99.28 C ANISOU 2511 CG MET A 360 14351 11513 11859 -676 -625 2728 C ATOM 2512 SD MET A 360 -25.313 -32.891 14.845 1.00197.53 S ANISOU 2512 SD MET A 360 26718 23809 24527 -766 -564 2686 S ATOM 2513 CE MET A 360 -26.637 -33.552 15.856 1.00 87.65 C ANISOU 2513 CE MET A 360 12862 9945 10497 -990 -458 2923 C ATOM 2514 N LEU A 361 -26.161 -29.136 14.345 1.00 77.27 N ANISOU 2514 N LEU A 361 11196 9118 9043 -657 -243 2245 N ATOM 2515 CA LEU A 361 -26.773 -29.041 13.026 1.00 77.38 C ANISOU 2515 CA LEU A 361 11101 9082 9217 -660 -194 2116 C ATOM 2516 C LEU A 361 -26.112 -27.933 12.221 1.00 67.44 C ANISOU 2516 C LEU A 361 9758 7870 7994 -522 -206 1924 C ATOM 2517 O LEU A 361 -25.752 -28.128 11.062 1.00108.09 O ANISOU 2517 O LEU A 361 14869 12908 13294 -457 -256 1831 O ATOM 2518 CB LEU A 361 -28.273 -28.766 13.147 1.00 75.72 C ANISOU 2518 CB LEU A 361 10814 8997 8961 -789 -38 2124 C ATOM 2519 CG LEU A 361 -29.138 -29.920 13.659 1.00 77.45 C ANISOU 2519 CG LEU A 361 11082 9155 9192 -953 -5 2311 C ATOM 2520 CD1 LEU A 361 -30.543 -29.431 13.963 1.00 76.26 C ANISOU 2520 CD1 LEU A 361 10832 9176 8969 -1070 170 2309 C ATOM 2521 CD2 LEU A 361 -29.175 -31.056 12.648 1.00 75.92 C ANISOU 2521 CD2 LEU A 361 10897 8729 9221 -979 -99 2322 C ATOM 2522 N LEU A 362 -25.955 -26.771 12.844 1.00 68.98 N ANISOU 2522 N LEU A 362 9928 8232 8049 -479 -159 1866 N ATOM 2523 CA LEU A 362 -25.336 -25.628 12.186 1.00 65.20 C ANISOU 2523 CA LEU A 362 9368 7800 7604 -362 -170 1701 C ATOM 2524 C LEU A 362 -23.966 -25.982 11.619 1.00 76.96 C ANISOU 2524 C LEU A 362 10880 9154 9208 -249 -300 1674 C ATOM 2525 O LEU A 362 -23.620 -25.569 10.513 1.00 73.29 O ANISOU 2525 O LEU A 362 10341 8658 8850 -176 -305 1554 O ATOM 2526 CB LEU A 362 -25.206 -24.456 13.159 1.00 72.95 C ANISOU 2526 CB LEU A 362 10344 8954 8421 -332 -133 1659 C ATOM 2527 CG LEU A 362 -26.332 -23.422 13.125 1.00 77.30 C ANISOU 2527 CG LEU A 362 10799 9655 8917 -368 3 1563 C ATOM 2528 CD1 LEU A 362 -26.160 -22.437 14.266 1.00 86.01 C ANISOU 2528 CD1 LEU A 362 11921 10915 9845 -339 26 1526 C ATOM 2529 CD2 LEU A 362 -26.362 -22.691 11.789 1.00 77.30 C ANISOU 2529 CD2 LEU A 362 10687 9626 9055 -305 12 1418 C ATOM 2530 N GLU A 363 -23.191 -26.757 12.371 1.00 80.13 N ANISOU 2530 N GLU A 363 11380 9478 9586 -234 -405 1790 N ATOM 2531 CA GLU A 363 -21.841 -27.111 11.950 1.00 86.34 C ANISOU 2531 CA GLU A 363 12176 10140 10490 -117 -533 1764 C ATOM 2532 C GLU A 363 -21.863 -27.916 10.652 1.00 85.39 C ANISOU 2532 C GLU A 363 12026 9865 10552 -96 -548 1713 C ATOM 2533 O GLU A 363 -20.890 -27.922 9.899 1.00 81.01 O ANISOU 2533 O GLU A 363 11431 9240 10109 14 -606 1628 O ATOM 2534 CB GLU A 363 -21.127 -27.896 13.049 1.00 93.27 C ANISOU 2534 CB GLU A 363 13170 10952 11318 -111 -657 1913 C ATOM 2535 CG GLU A 363 -19.654 -28.135 12.769 1.00108.70 C ANISOU 2535 CG GLU A 363 15114 12794 13392 23 -797 1879 C ATOM 2536 CD GLU A 363 -18.867 -28.424 14.030 1.00122.82 C ANISOU 2536 CD GLU A 363 16999 14575 15092 47 -929 2003 C ATOM 2537 OE1 GLU A 363 -17.669 -28.072 14.075 1.00126.72 O ANISOU 2537 OE1 GLU A 363 17457 15057 15635 158 -1030 1951 O ATOM 2538 OE2 GLU A 363 -19.445 -29.001 14.975 1.00126.93 O ANISOU 2538 OE2 GLU A 363 17629 15105 15493 -50 -935 2159 O ATOM 2539 N ILE A 364 -22.976 -28.595 10.395 1.00 83.27 N ANISOU 2539 N ILE A 364 11774 9549 10314 -202 -496 1759 N ATOM 2540 CA ILE A 364 -23.153 -29.327 9.147 1.00 81.53 C ANISOU 2540 CA ILE A 364 11531 9191 10257 -191 -512 1691 C ATOM 2541 C ILE A 364 -23.696 -28.401 8.066 1.00 86.90 C ANISOU 2541 C ILE A 364 12104 9963 10950 -178 -418 1540 C ATOM 2542 O ILE A 364 -23.187 -28.369 6.945 1.00 63.43 O ANISOU 2542 O ILE A 364 9089 6939 8071 -92 -437 1425 O ATOM 2543 CB ILE A 364 -24.130 -30.504 9.319 1.00 75.71 C ANISOU 2543 CB ILE A 364 10855 8344 9568 -321 -515 1808 C ATOM 2544 CG1 ILE A 364 -23.656 -31.428 10.441 1.00 78.00 C ANISOU 2544 CG1 ILE A 364 11263 8536 9836 -347 -614 1987 C ATOM 2545 CG2 ILE A 364 -24.266 -31.280 8.013 1.00 78.13 C ANISOU 2545 CG2 ILE A 364 11144 8494 10048 -301 -553 1716 C ATOM 2546 CD1 ILE A 364 -24.671 -32.479 10.832 1.00 70.70 C ANISOU 2546 CD1 ILE A 364 10401 7521 8939 -501 -606 2139 C ATOM 2547 N PHE A 365 -24.733 -27.648 8.417 1.00 63.81 N ANISOU 2547 N PHE A 365 9137 7181 7929 -260 -316 1543 N ATOM 2548 CA PHE A 365 -25.396 -26.760 7.473 1.00 76.14 C ANISOU 2548 CA PHE A 365 10598 8826 9503 -257 -237 1417 C ATOM 2549 C PHE A 365 -24.433 -25.718 6.913 1.00 74.85 C ANISOU 2549 C PHE A 365 10378 8719 9342 -135 -245 1305 C ATOM 2550 O PHE A 365 -24.603 -25.252 5.785 1.00 77.31 O ANISOU 2550 O PHE A 365 10625 9046 9702 -103 -218 1201 O ATOM 2551 CB PHE A 365 -26.597 -26.086 8.142 1.00 79.20 C ANISOU 2551 CB PHE A 365 10941 9360 9790 -353 -131 1443 C ATOM 2552 CG PHE A 365 -27.679 -27.050 8.554 1.00 73.19 C ANISOU 2552 CG PHE A 365 10209 8559 9041 -491 -99 1553 C ATOM 2553 CD1 PHE A 365 -27.844 -28.252 7.886 1.00 69.71 C ANISOU 2553 CD1 PHE A 365 9802 7952 8732 -529 -160 1578 C ATOM 2554 CD2 PHE A 365 -28.527 -26.759 9.608 1.00 75.16 C ANISOU 2554 CD2 PHE A 365 10447 8936 9175 -584 -6 1628 C ATOM 2555 CE1 PHE A 365 -28.832 -29.143 8.259 1.00 77.10 C ANISOU 2555 CE1 PHE A 365 10758 8838 9700 -669 -138 1689 C ATOM 2556 CE2 PHE A 365 -29.519 -27.651 9.985 1.00 79.92 C ANISOU 2556 CE2 PHE A 365 11064 9507 9797 -724 35 1743 C ATOM 2557 CZ PHE A 365 -29.669 -28.842 9.310 1.00 79.52 C ANISOU 2557 CZ PHE A 365 11043 9277 9893 -772 -35 1781 C ATOM 2558 N VAL A 366 -23.424 -25.355 7.698 1.00 61.27 N ANISOU 2558 N VAL A 366 8681 7028 7569 -73 -290 1332 N ATOM 2559 CA VAL A 366 -22.390 -24.448 7.218 1.00 69.86 C ANISOU 2559 CA VAL A 366 9709 8153 8682 35 -308 1241 C ATOM 2560 C VAL A 366 -21.706 -25.050 5.994 1.00 68.68 C ANISOU 2560 C VAL A 366 9544 7894 8657 110 -345 1177 C ATOM 2561 O VAL A 366 -21.517 -24.376 4.981 1.00 71.63 O ANISOU 2561 O VAL A 366 9849 8306 9063 158 -308 1082 O ATOM 2562 CB VAL A 366 -21.329 -24.164 8.302 1.00 65.65 C ANISOU 2562 CB VAL A 366 9206 7645 8094 87 -377 1286 C ATOM 2563 CG1 VAL A 366 -20.062 -23.597 7.676 1.00 71.27 C ANISOU 2563 CG1 VAL A 366 9849 8346 8884 199 -417 1206 C ATOM 2564 CG2 VAL A 366 -21.877 -23.207 9.346 1.00 61.56 C ANISOU 2564 CG2 VAL A 366 8686 7268 7437 40 -330 1298 C ATOM 2565 N TRP A 367 -21.340 -26.323 6.094 1.00 70.02 N ANISOU 2565 N TRP A 367 9783 7928 8895 121 -418 1231 N ATOM 2566 CA TRP A 367 -20.637 -27.003 5.012 1.00 71.86 C ANISOU 2566 CA TRP A 367 10006 8050 9248 206 -457 1157 C ATOM 2567 C TRP A 367 -21.539 -27.273 3.813 1.00 75.01 C ANISOU 2567 C TRP A 367 10391 8425 9685 170 -410 1078 C ATOM 2568 O TRP A 367 -21.085 -27.234 2.671 1.00 73.92 O ANISOU 2568 O TRP A 367 10216 8274 9597 245 -398 972 O ATOM 2569 CB TRP A 367 -20.008 -28.303 5.516 1.00 66.68 C ANISOU 2569 CB TRP A 367 9428 7237 8670 235 -564 1231 C ATOM 2570 CG TRP A 367 -18.740 -28.063 6.260 1.00 63.09 C ANISOU 2570 CG TRP A 367 8965 6790 8218 320 -636 1266 C ATOM 2571 CD1 TRP A 367 -18.579 -28.018 7.611 1.00 63.75 C ANISOU 2571 CD1 TRP A 367 9103 6897 8222 289 -692 1383 C ATOM 2572 CD2 TRP A 367 -17.451 -27.810 5.692 1.00 80.89 C ANISOU 2572 CD2 TRP A 367 11144 9036 10555 448 -660 1180 C ATOM 2573 NE1 TRP A 367 -17.266 -27.761 7.923 1.00 91.13 N ANISOU 2573 NE1 TRP A 367 12536 10363 11727 392 -769 1372 N ATOM 2574 CE2 TRP A 367 -16.552 -27.628 6.762 1.00 86.80 C ANISOU 2574 CE2 TRP A 367 11898 9793 11288 488 -746 1250 C ATOM 2575 CE3 TRP A 367 -16.967 -27.724 4.382 1.00 80.15 C ANISOU 2575 CE3 TRP A 367 10976 8937 10540 530 -615 1053 C ATOM 2576 CZ2 TRP A 367 -15.197 -27.367 6.562 1.00 86.42 C ANISOU 2576 CZ2 TRP A 367 11768 9741 11327 606 -792 1196 C ATOM 2577 CZ3 TRP A 367 -15.623 -27.464 4.186 1.00 82.77 C ANISOU 2577 CZ3 TRP A 367 11228 9275 10946 645 -641 1003 C ATOM 2578 CH2 TRP A 367 -14.753 -27.289 5.270 1.00 86.08 C ANISOU 2578 CH2 TRP A 367 11639 9695 11373 681 -730 1074 C ATOM 2579 N ILE A 368 -22.811 -27.557 4.069 1.00 61.39 N ANISOU 2579 N ILE A 368 8693 6700 7932 54 -384 1128 N ATOM 2580 CA ILE A 368 -23.777 -27.692 2.986 1.00 84.01 C ANISOU 2580 CA ILE A 368 11534 9555 10829 9 -350 1051 C ATOM 2581 C ILE A 368 -23.861 -26.373 2.219 1.00 82.06 C ANISOU 2581 C ILE A 368 11204 9445 10529 45 -282 960 C ATOM 2582 O ILE A 368 -24.028 -26.359 0.997 1.00 59.64 O ANISOU 2582 O ILE A 368 8344 6602 7715 72 -273 865 O ATOM 2583 CB ILE A 368 -25.170 -28.084 3.509 1.00 61.83 C ANISOU 2583 CB ILE A 368 8744 6741 8009 -133 -328 1130 C ATOM 2584 CG1 ILE A 368 -25.142 -29.512 4.055 1.00 86.08 C ANISOU 2584 CG1 ILE A 368 11903 9647 11155 -181 -405 1228 C ATOM 2585 CG2 ILE A 368 -26.196 -27.981 2.399 1.00 64.95 C ANISOU 2585 CG2 ILE A 368 9092 7151 8434 -177 -301 1041 C ATOM 2586 CD1 ILE A 368 -26.470 -29.988 4.605 1.00 84.71 C ANISOU 2586 CD1 ILE A 368 11741 9462 10982 -336 -378 1327 C ATOM 2587 N GLY A 369 -23.741 -25.267 2.945 1.00 66.98 N ANISOU 2587 N GLY A 369 9253 7653 8543 46 -242 990 N ATOM 2588 CA GLY A 369 -23.714 -23.955 2.331 1.00 63.29 C ANISOU 2588 CA GLY A 369 8709 7299 8039 81 -190 920 C ATOM 2589 C GLY A 369 -22.437 -23.750 1.541 1.00 68.66 C ANISOU 2589 C GLY A 369 9364 7969 8754 191 -202 858 C ATOM 2590 O GLY A 369 -22.463 -23.220 0.430 1.00 67.02 O ANISOU 2590 O GLY A 369 9116 7806 8544 220 -169 788 O ATOM 2591 N TYR A 370 -21.314 -24.166 2.117 1.00 71.31 N ANISOU 2591 N TYR A 370 9720 8251 9122 250 -249 890 N ATOM 2592 CA TYR A 370 -20.028 -24.058 1.440 1.00 71.46 C ANISOU 2592 CA TYR A 370 9698 8262 9192 356 -254 833 C ATOM 2593 C TYR A 370 -20.060 -24.796 0.105 1.00 77.08 C ANISOU 2593 C TYR A 370 10424 8919 9946 395 -242 746 C ATOM 2594 O TYR A 370 -19.577 -24.288 -0.908 1.00 81.13 O ANISOU 2594 O TYR A 370 10886 9488 10453 451 -195 677 O ATOM 2595 CB TYR A 370 -18.907 -24.618 2.316 1.00 71.60 C ANISOU 2595 CB TYR A 370 9735 8211 9261 415 -326 881 C ATOM 2596 CG TYR A 370 -18.445 -23.694 3.425 1.00 71.25 C ANISOU 2596 CG TYR A 370 9661 8239 9173 412 -346 936 C ATOM 2597 CD1 TYR A 370 -18.679 -22.324 3.372 1.00 60.54 C ANISOU 2597 CD1 TYR A 370 8243 6998 7764 390 -293 913 C ATOM 2598 CD2 TYR A 370 -17.765 -24.198 4.525 1.00 70.79 C ANISOU 2598 CD2 TYR A 370 9641 8126 9128 435 -432 1006 C ATOM 2599 CE1 TYR A 370 -18.251 -21.487 4.386 1.00 63.30 C ANISOU 2599 CE1 TYR A 370 8569 7403 8079 390 -323 944 C ATOM 2600 CE2 TYR A 370 -17.335 -23.371 5.541 1.00 72.77 C ANISOU 2600 CE2 TYR A 370 9873 8445 9330 435 -465 1042 C ATOM 2601 CZ TYR A 370 -17.579 -22.017 5.469 1.00 75.59 C ANISOU 2601 CZ TYR A 370 10168 8914 9638 413 -410 1003 C ATOM 2602 OH TYR A 370 -17.151 -21.192 6.483 1.00 78.60 O ANISOU 2602 OH TYR A 370 10534 9356 9976 415 -454 1022 O ATOM 2603 N VAL A 371 -20.621 -26.001 0.112 1.00 73.20 N ANISOU 2603 N VAL A 371 10004 8315 9494 361 -288 750 N ATOM 2604 CA VAL A 371 -20.796 -26.770 -1.114 1.00 66.42 C ANISOU 2604 CA VAL A 371 9172 7393 8672 391 -292 651 C ATOM 2605 C VAL A 371 -21.641 -25.988 -2.115 1.00 75.97 C ANISOU 2605 C VAL A 371 10352 8706 9810 354 -236 593 C ATOM 2606 O VAL A 371 -21.263 -25.830 -3.276 1.00 59.50 O ANISOU 2606 O VAL A 371 8247 6658 7701 417 -203 503 O ATOM 2607 CB VAL A 371 -21.487 -28.116 -0.837 1.00 61.17 C ANISOU 2607 CB VAL A 371 8588 6579 8073 333 -364 674 C ATOM 2608 CG1 VAL A 371 -21.854 -28.806 -2.139 1.00 90.77 C ANISOU 2608 CG1 VAL A 371 12367 10268 11852 353 -378 552 C ATOM 2609 CG2 VAL A 371 -20.590 -29.010 0.004 1.00129.18 C ANISOU 2609 CG2 VAL A 371 17243 15068 16770 383 -439 732 C ATOM 2610 N SER A 372 -22.786 -25.498 -1.650 1.00 78.91 N ANISOU 2610 N SER A 372 10717 9126 10142 253 -225 648 N ATOM 2611 CA SER A 372 -23.717 -24.763 -2.498 1.00 79.90 C ANISOU 2611 CA SER A 372 10810 9337 10212 213 -192 605 C ATOM 2612 C SER A 372 -23.004 -23.652 -3.260 1.00 82.25 C ANISOU 2612 C SER A 372 11053 9741 10457 281 -139 570 C ATOM 2613 O SER A 372 -23.032 -23.611 -4.489 1.00 87.76 O ANISOU 2613 O SER A 372 11756 10470 11121 313 -126 496 O ATOM 2614 CB SER A 372 -24.847 -24.173 -1.653 1.00 86.21 C ANISOU 2614 CB SER A 372 11579 10189 10987 113 -177 675 C ATOM 2615 OG SER A 372 -25.762 -23.445 -2.453 1.00 86.07 O ANISOU 2615 OG SER A 372 11522 10247 10936 82 -161 636 O ATOM 2616 N SER A 373 -22.364 -22.752 -2.522 1.00 90.69 N ANISOU 2616 N SER A 373 12072 10867 11518 300 -113 625 N ATOM 2617 CA SER A 373 -21.647 -21.637 -3.129 1.00 89.98 C ANISOU 2617 CA SER A 373 11921 10869 11398 350 -65 613 C ATOM 2618 C SER A 373 -20.414 -22.119 -3.876 1.00 87.79 C ANISOU 2618 C SER A 373 11639 10577 11142 443 -43 559 C ATOM 2619 O SER A 373 -19.984 -21.504 -4.851 1.00 91.85 O ANISOU 2619 O SER A 373 12117 11166 11616 479 10 531 O ATOM 2620 CB SER A 373 -21.245 -20.617 -2.061 1.00 84.10 C ANISOU 2620 CB SER A 373 11124 10170 10661 341 -59 677 C ATOM 2621 OG SER A 373 -22.383 -19.904 -1.612 1.00 70.03 O ANISOU 2621 OG SER A 373 9329 8431 8850 270 -59 704 O ATOM 2622 N GLY A 374 -19.854 -23.228 -3.412 1.00 86.82 N ANISOU 2622 N GLY A 374 11549 10356 11082 483 -81 548 N ATOM 2623 CA GLY A 374 -18.626 -23.752 -3.972 1.00 81.64 C ANISOU 2623 CA GLY A 374 10874 9678 10469 586 -62 487 C ATOM 2624 C GLY A 374 -18.732 -24.158 -5.428 1.00 80.77 C ANISOU 2624 C GLY A 374 10790 9588 10312 627 -24 381 C ATOM 2625 O GLY A 374 -17.923 -23.731 -6.252 1.00 88.27 O ANISOU 2625 O GLY A 374 11689 10618 11230 689 47 342 O ATOM 2626 N VAL A 375 -19.730 -24.977 -5.751 1.00 75.04 N ANISOU 2626 N VAL A 375 10141 8794 9576 587 -72 335 N ATOM 2627 CA VAL A 375 -19.837 -25.554 -7.089 1.00 82.86 C ANISOU 2627 CA VAL A 375 11175 9788 10521 633 -59 212 C ATOM 2628 C VAL A 375 -20.927 -24.910 -7.942 1.00 81.25 C ANISOU 2628 C VAL A 375 10991 9672 10210 568 -51 199 C ATOM 2629 O VAL A 375 -21.322 -25.464 -8.967 1.00 73.32 O ANISOU 2629 O VAL A 375 10043 8661 9155 584 -69 98 O ATOM 2630 CB VAL A 375 -20.119 -27.072 -7.027 1.00 87.30 C ANISOU 2630 CB VAL A 375 11817 10190 11165 645 -142 141 C ATOM 2631 CG1 VAL A 375 -19.033 -27.783 -6.237 1.00 94.75 C ANISOU 2631 CG1 VAL A 375 12745 11030 12224 720 -168 155 C ATOM 2632 CG2 VAL A 375 -21.492 -27.342 -6.425 1.00 61.63 C ANISOU 2632 CG2 VAL A 375 8610 6870 7936 523 -215 201 C ATOM 2633 N ASN A 376 -21.410 -23.743 -7.528 1.00 80.41 N ANISOU 2633 N ASN A 376 10839 9642 10071 501 -36 295 N ATOM 2634 CA ASN A 376 -22.518 -23.100 -8.231 1.00 82.80 C ANISOU 2634 CA ASN A 376 11152 10014 10293 440 -49 295 C ATOM 2635 C ASN A 376 -22.160 -22.611 -9.637 1.00 80.17 C ANISOU 2635 C ASN A 376 10826 9792 9845 489 4 245 C ATOM 2636 O ASN A 376 -22.799 -23.010 -10.612 1.00 78.60 O ANISOU 2636 O ASN A 376 10686 9603 9575 485 -31 167 O ATOM 2637 CB ASN A 376 -23.102 -21.957 -7.397 1.00 83.35 C ANISOU 2637 CB ASN A 376 11165 10128 10375 369 -49 401 C ATOM 2638 CG ASN A 376 -23.993 -21.041 -8.211 1.00 89.45 C ANISOU 2638 CG ASN A 376 11929 10986 11073 329 -58 410 C ATOM 2639 OD1 ASN A 376 -23.602 -19.931 -8.573 1.00 87.72 O ANISOU 2639 OD1 ASN A 376 11668 10852 10809 344 -16 456 O ATOM 2640 ND2 ASN A 376 -25.198 -21.511 -8.515 1.00 85.68 N ANISOU 2640 ND2 ASN A 376 11485 10477 10593 275 -124 372 N ATOM 2641 N PRO A 377 -21.136 -21.752 -9.753 1.00 74.53 N ANISOU 2641 N PRO A 377 10050 9163 9105 531 86 293 N ATOM 2642 CA PRO A 377 -20.769 -21.224 -11.073 1.00 78.38 C ANISOU 2642 CA PRO A 377 10542 9771 9469 566 152 270 C ATOM 2643 C PRO A 377 -20.542 -22.318 -12.117 1.00 77.88 C ANISOU 2643 C PRO A 377 10548 9707 9335 636 163 130 C ATOM 2644 O PRO A 377 -20.953 -22.161 -13.266 1.00 78.53 O ANISOU 2644 O PRO A 377 10683 9871 9284 637 166 87 O ATOM 2645 CB PRO A 377 -19.463 -20.473 -10.796 1.00 76.34 C ANISOU 2645 CB PRO A 377 10193 9570 9243 604 242 338 C ATOM 2646 CG PRO A 377 -19.547 -20.096 -9.368 1.00 72.80 C ANISOU 2646 CG PRO A 377 9695 9054 8912 560 199 420 C ATOM 2647 CD PRO A 377 -20.265 -21.222 -8.690 1.00 71.66 C ANISOU 2647 CD PRO A 377 9610 8792 8826 541 117 374 C ATOM 2648 N LEU A 378 -19.893 -23.407 -11.719 1.00 77.21 N ANISOU 2648 N LEU A 378 10469 9529 9339 700 161 55 N ATOM 2649 CA LEU A 378 -19.608 -24.505 -12.637 1.00 77.00 C ANISOU 2649 CA LEU A 378 10506 9484 9266 782 168 -102 C ATOM 2650 C LEU A 378 -20.895 -25.143 -13.148 1.00 76.89 C ANISOU 2650 C LEU A 378 10590 9414 9209 735 63 -182 C ATOM 2651 O LEU A 378 -21.096 -25.272 -14.355 1.00 84.22 O ANISOU 2651 O LEU A 378 11580 10417 10002 764 69 -278 O ATOM 2652 CB LEU A 378 -18.740 -25.561 -11.952 1.00 81.50 C ANISOU 2652 CB LEU A 378 11057 9931 9979 859 160 -160 C ATOM 2653 CG LEU A 378 -18.362 -26.774 -12.807 1.00 78.23 C ANISOU 2653 CG LEU A 378 10702 9473 9550 962 162 -343 C ATOM 2654 CD1 LEU A 378 -17.502 -26.359 -13.994 1.00 80.92 C ANISOU 2654 CD1 LEU A 378 11014 9982 9749 1045 297 -411 C ATOM 2655 CD2 LEU A 378 -17.649 -27.818 -11.962 1.00 73.31 C ANISOU 2655 CD2 LEU A 378 10060 8692 9103 1032 121 -381 C ATOM 2656 N VAL A 379 -21.761 -25.545 -12.224 1.00 68.28 N ANISOU 2656 N VAL A 379 9513 8199 8232 659 -35 -142 N ATOM 2657 CA VAL A 379 -23.035 -26.154 -12.583 1.00 71.01 C ANISOU 2657 CA VAL A 379 9931 8478 8571 598 -145 -206 C ATOM 2658 C VAL A 379 -23.793 -25.270 -13.569 1.00 71.86 C ANISOU 2658 C VAL A 379 10057 8716 8530 558 -156 -196 C ATOM 2659 O VAL A 379 -24.370 -25.754 -14.544 1.00 65.56 O ANISOU 2659 O VAL A 379 9333 7924 7652 562 -219 -307 O ATOM 2660 CB VAL A 379 -23.904 -26.384 -11.334 1.00 72.62 C ANISOU 2660 CB VAL A 379 10116 8564 8912 497 -222 -116 C ATOM 2661 CG1 VAL A 379 -25.341 -26.690 -11.728 1.00 63.62 C ANISOU 2661 CG1 VAL A 379 9018 7386 7770 411 -328 -155 C ATOM 2662 CG2 VAL A 379 -23.323 -27.508 -10.484 1.00 71.74 C ANISOU 2662 CG2 VAL A 379 10018 8298 8942 530 -247 -133 C ATOM 2663 N TYR A 380 -23.782 -23.969 -13.304 1.00 70.52 N ANISOU 2663 N TYR A 380 9821 8643 8329 521 -106 -64 N ATOM 2664 CA TYR A 380 -24.468 -22.998 -14.146 1.00 69.16 C ANISOU 2664 CA TYR A 380 9660 8587 8032 483 -125 -24 C ATOM 2665 C TYR A 380 -23.872 -22.963 -15.549 1.00 71.94 C ANISOU 2665 C TYR A 380 10070 9060 8204 556 -69 -102 C ATOM 2666 O TYR A 380 -24.582 -23.138 -16.539 1.00 74.34 O ANISOU 2666 O TYR A 380 10448 9403 8393 548 -138 -174 O ATOM 2667 CB TYR A 380 -24.380 -21.609 -13.510 1.00 72.65 C ANISOU 2667 CB TYR A 380 10016 9089 8500 443 -80 132 C ATOM 2668 CG TYR A 380 -25.112 -20.524 -14.271 1.00 74.30 C ANISOU 2668 CG TYR A 380 10228 9395 8606 403 -115 195 C ATOM 2669 CD1 TYR A 380 -26.490 -20.568 -14.425 1.00 75.96 C ANISOU 2669 CD1 TYR A 380 10457 9576 8828 341 -232 181 C ATOM 2670 CD2 TYR A 380 -24.427 -19.447 -14.822 1.00 72.37 C ANISOU 2670 CD2 TYR A 380 9963 9267 8269 424 -37 279 C ATOM 2671 CE1 TYR A 380 -27.165 -19.580 -15.113 1.00 68.39 C ANISOU 2671 CE1 TYR A 380 9499 8697 7788 312 -282 241 C ATOM 2672 CE2 TYR A 380 -25.095 -18.453 -15.510 1.00 70.96 C ANISOU 2672 CE2 TYR A 380 9794 9163 8003 388 -84 352 C ATOM 2673 CZ TYR A 380 -26.463 -18.524 -15.651 1.00 74.10 C ANISOU 2673 CZ TYR A 380 10214 9526 8413 337 -212 330 C ATOM 2674 OH TYR A 380 -27.132 -17.538 -16.336 1.00 87.76 O ANISOU 2674 OH TYR A 380 11952 11323 10069 309 -276 406 O ATOM 2675 N THR A 381 -22.565 -22.733 -15.625 1.00 76.07 N ANISOU 2675 N THR A 381 10555 9649 8699 626 58 -87 N ATOM 2676 CA THR A 381 -21.876 -22.597 -16.907 1.00 79.08 C ANISOU 2676 CA THR A 381 10976 10173 8899 694 147 -144 C ATOM 2677 C THR A 381 -21.790 -23.905 -17.690 1.00 82.29 C ANISOU 2677 C THR A 381 11473 10553 9241 771 126 -344 C ATOM 2678 O THR A 381 -21.508 -23.892 -18.888 1.00 76.32 O ANISOU 2678 O THR A 381 10776 9924 8297 823 179 -419 O ATOM 2679 CB THR A 381 -20.446 -22.038 -16.731 1.00 76.89 C ANISOU 2679 CB THR A 381 10609 9974 8632 745 301 -75 C ATOM 2680 OG1 THR A 381 -19.673 -22.915 -15.900 1.00 86.31 O ANISOU 2680 OG1 THR A 381 11756 11058 9978 804 323 -137 O ATOM 2681 CG2 THR A 381 -20.485 -20.643 -16.124 1.00 74.38 C ANISOU 2681 CG2 THR A 381 10209 9689 8364 671 316 113 C ATOM 2682 N LEU A 382 -22.031 -25.030 -17.022 1.00 83.47 N ANISOU 2682 N LEU A 382 11638 10535 9541 778 46 -432 N ATOM 2683 CA LEU A 382 -21.994 -26.328 -17.690 1.00 81.23 C ANISOU 2683 CA LEU A 382 11442 10191 9230 852 4 -636 C ATOM 2684 C LEU A 382 -23.137 -26.475 -18.689 1.00 70.57 C ANISOU 2684 C LEU A 382 10194 8873 7745 813 -111 -720 C ATOM 2685 O LEU A 382 -23.158 -27.416 -19.478 1.00105.09 O ANISOU 2685 O LEU A 382 14655 13224 12052 875 -152 -906 O ATOM 2686 CB LEU A 382 -22.045 -27.465 -16.668 1.00 87.48 C ANISOU 2686 CB LEU A 382 12227 10771 10240 854 -74 -684 C ATOM 2687 CG LEU A 382 -20.704 -27.902 -16.073 1.00 89.86 C ANISOU 2687 CG LEU A 382 12465 11022 10655 949 17 -702 C ATOM 2688 CD1 LEU A 382 -20.916 -28.865 -14.912 1.00 84.24 C ANISOU 2688 CD1 LEU A 382 11752 10093 10163 925 -84 -695 C ATOM 2689 CD2 LEU A 382 -19.828 -28.541 -17.140 1.00 89.43 C ANISOU 2689 CD2 LEU A 382 12448 11028 10501 1085 93 -890 C ATOM 2690 N PHE A 383 -24.086 -25.546 -18.654 1.00 86.02 N ANISOU 2690 N PHE A 383 12138 10877 9668 715 -173 -593 N ATOM 2691 CA PHE A 383 -25.196 -25.565 -19.601 1.00 88.28 C ANISOU 2691 CA PHE A 383 12511 11203 9830 675 -298 -656 C ATOM 2692 C PHE A 383 -24.887 -24.759 -20.862 1.00 92.23 C ANISOU 2692 C PHE A 383 13064 11911 10070 712 -232 -642 C ATOM 2693 O PHE A 383 -25.729 -24.638 -21.752 1.00 96.51 O ANISOU 2693 O PHE A 383 13685 12512 10472 685 -337 -681 O ATOM 2694 CB PHE A 383 -26.471 -25.040 -18.942 1.00 77.97 C ANISOU 2694 CB PHE A 383 11156 9833 8636 555 -415 -535 C ATOM 2695 CG PHE A 383 -27.043 -25.971 -17.914 1.00 83.64 C ANISOU 2695 CG PHE A 383 11845 10358 9575 502 -501 -563 C ATOM 2696 CD1 PHE A 383 -26.638 -25.895 -16.593 1.00 92.03 C ANISOU 2696 CD1 PHE A 383 12822 11341 10803 481 -439 -457 C ATOM 2697 CD2 PHE A 383 -27.977 -26.928 -18.270 1.00 87.59 C ANISOU 2697 CD2 PHE A 383 12407 10758 10116 466 -649 -691 C ATOM 2698 CE1 PHE A 383 -27.158 -26.753 -15.643 1.00 93.92 C ANISOU 2698 CE1 PHE A 383 13043 11411 11230 423 -512 -463 C ATOM 2699 CE2 PHE A 383 -28.502 -27.789 -17.325 1.00 93.91 C ANISOU 2699 CE2 PHE A 383 13178 11377 11128 403 -724 -698 C ATOM 2700 CZ PHE A 383 -28.091 -27.701 -16.010 1.00 96.41 C ANISOU 2700 CZ PHE A 383 13414 11624 11594 380 -649 -576 C ATOM 2701 N ASN A 384 -23.677 -24.213 -20.935 1.00 86.38 N ANISOU 2701 N ASN A 384 12277 11280 9264 768 -61 -578 N ATOM 2702 CA ASN A 384 -23.240 -23.471 -22.111 1.00 85.09 C ANISOU 2702 CA ASN A 384 12160 11323 8847 799 30 -547 C ATOM 2703 C ASN A 384 -22.209 -24.278 -22.893 1.00 87.01 C ANISOU 2703 C ASN A 384 12452 11646 8962 920 148 -724 C ATOM 2704 O ASN A 384 -21.203 -24.714 -22.336 1.00 86.48 O ANISOU 2704 O ASN A 384 12314 11532 9014 986 256 -763 O ATOM 2705 CB ASN A 384 -22.649 -22.126 -21.692 1.00 81.58 C ANISOU 2705 CB ASN A 384 11614 10961 8421 761 145 -327 C ATOM 2706 CG ASN A 384 -22.222 -21.282 -22.876 1.00 86.50 C ANISOU 2706 CG ASN A 384 12282 11795 8789 773 241 -256 C ATOM 2707 OD1 ASN A 384 -21.149 -21.486 -23.444 1.00 88.91 O ANISOU 2707 OD1 ASN A 384 12589 12216 8978 849 395 -316 O ATOM 2708 ND2 ASN A 384 -23.058 -20.320 -23.248 1.00 88.70 N ANISOU 2708 ND2 ASN A 384 12591 12126 8983 698 152 -122 N ATOM 2709 N LYS A 385 -22.468 -24.479 -24.182 1.00 86.74 N ANISOU 2709 N LYS A 385 12540 11735 8683 956 122 -839 N ATOM 2710 CA LYS A 385 -21.596 -25.294 -25.023 1.00 89.25 C ANISOU 2710 CA LYS A 385 12918 12141 8854 1080 230 -1041 C ATOM 2711 C LYS A 385 -20.165 -24.765 -25.043 1.00 88.53 C ANISOU 2711 C LYS A 385 12730 12187 8719 1138 467 -965 C ATOM 2712 O LYS A 385 -19.210 -25.538 -24.970 1.00 80.60 O ANISOU 2712 O LYS A 385 11688 11166 7771 1244 574 -1106 O ATOM 2713 CB LYS A 385 -22.143 -25.360 -26.451 1.00 97.01 C ANISOU 2713 CB LYS A 385 14054 13271 9534 1098 168 -1151 C ATOM 2714 N THR A 386 -20.021 -23.448 -25.142 1.00 90.30 N ANISOU 2714 N THR A 386 12908 12541 8861 1068 542 -741 N ATOM 2715 CA THR A 386 -18.702 -22.833 -25.207 1.00 89.45 C ANISOU 2715 CA THR A 386 12698 12572 8716 1101 765 -644 C ATOM 2716 C THR A 386 -17.918 -23.109 -23.929 1.00 77.97 C ANISOU 2716 C THR A 386 11096 10974 7555 1128 820 -627 C ATOM 2717 O THR A 386 -16.795 -23.610 -23.981 1.00 80.39 O ANISOU 2717 O THR A 386 11338 11321 7887 1227 965 -727 O ATOM 2718 CB THR A 386 -18.801 -21.316 -25.424 1.00 79.07 C ANISOU 2718 CB THR A 386 11357 11382 7303 999 804 -381 C ATOM 2719 OG1 THR A 386 -19.795 -21.036 -26.417 1.00 87.73 O ANISOU 2719 OG1 THR A 386 12598 12568 8167 958 689 -371 O ATOM 2720 CG2 THR A 386 -17.463 -20.756 -25.878 1.00101.14 C ANISOU 2720 CG2 THR A 386 14072 14364 9992 1032 1045 -302 C ATOM 2721 N PHE A 387 -18.512 -22.779 -22.786 1.00 75.60 N ANISOU 2721 N PHE A 387 10741 10513 7470 1043 702 -504 N ATOM 2722 CA PHE A 387 -17.903 -23.073 -21.493 1.00 74.12 C ANISOU 2722 CA PHE A 387 10432 10177 7552 1060 720 -484 C ATOM 2723 C PHE A 387 -17.578 -24.557 -21.369 1.00 83.96 C ANISOU 2723 C PHE A 387 11702 11308 8891 1169 699 -710 C ATOM 2724 O PHE A 387 -16.458 -24.933 -21.027 1.00 75.47 O ANISOU 2724 O PHE A 387 10534 10220 7921 1253 807 -759 O ATOM 2725 CB PHE A 387 -18.844 -22.679 -20.355 1.00 84.33 C ANISOU 2725 CB PHE A 387 11698 11315 9027 955 571 -355 C ATOM 2726 CG PHE A 387 -18.747 -21.234 -19.948 1.00 90.06 C ANISOU 2726 CG PHE A 387 12340 12097 9782 869 610 -126 C ATOM 2727 CD1 PHE A 387 -17.715 -20.800 -19.132 1.00 88.58 C ANISOU 2727 CD1 PHE A 387 12021 11895 9741 876 708 -34 C ATOM 2728 CD2 PHE A 387 -19.698 -20.315 -20.361 1.00 92.10 C ANISOU 2728 CD2 PHE A 387 12649 12407 9937 783 532 -10 C ATOM 2729 CE1 PHE A 387 -17.625 -19.476 -18.748 1.00 81.73 C ANISOU 2729 CE1 PHE A 387 11077 11061 8915 795 730 164 C ATOM 2730 CE2 PHE A 387 -19.613 -18.990 -19.979 1.00 89.01 C ANISOU 2730 CE2 PHE A 387 12181 12045 9592 709 555 193 C ATOM 2731 CZ PHE A 387 -18.575 -18.571 -19.171 1.00 82.90 C ANISOU 2731 CZ PHE A 387 11280 11252 8965 713 655 276 C ATOM 2732 N ARG A 388 -18.573 -25.394 -21.647 1.00 87.87 N ANISOU 2732 N ARG A 388 12315 11709 9362 1167 549 -847 N ATOM 2733 CA ARG A 388 -18.443 -26.837 -21.477 1.00 86.12 C ANISOU 2733 CA ARG A 388 12129 11334 9257 1258 490 -1060 C ATOM 2734 C ARG A 388 -17.313 -27.405 -22.330 1.00 87.43 C ANISOU 2734 C ARG A 388 12293 11612 9312 1404 642 -1240 C ATOM 2735 O ARG A 388 -16.514 -28.210 -21.855 1.00 90.92 O ANISOU 2735 O ARG A 388 12674 11953 9918 1500 678 -1344 O ATOM 2736 CB ARG A 388 -19.766 -27.530 -21.818 1.00 87.70 C ANISOU 2736 CB ARG A 388 12461 11432 9430 1216 297 -1174 C ATOM 2737 CG ARG A 388 -19.805 -29.006 -21.458 1.00 96.82 C ANISOU 2737 CG ARG A 388 13652 12376 10757 1281 198 -1366 C ATOM 2738 CD ARG A 388 -21.214 -29.581 -21.559 1.00101.87 C ANISOU 2738 CD ARG A 388 14395 12884 11425 1203 -11 -1435 C ATOM 2739 NE ARG A 388 -21.805 -29.389 -22.884 1.00101.64 N ANISOU 2739 NE ARG A 388 14481 13002 11136 1202 -50 -1528 N ATOM 2740 CZ ARG A 388 -22.656 -28.417 -23.210 1.00 98.89 C ANISOU 2740 CZ ARG A 388 14155 12758 10660 1102 -104 -1392 C ATOM 2741 NH1 ARG A 388 -23.047 -27.518 -22.313 1.00 98.87 N ANISOU 2741 NH1 ARG A 388 14065 12730 10773 996 -118 -1167 N ATOM 2742 NH2 ARG A 388 -23.125 -28.344 -24.447 1.00 97.68 N ANISOU 2742 NH2 ARG A 388 14116 12735 10261 1113 -153 -1488 N ATOM 2743 N ASP A 389 -17.243 -26.984 -23.589 1.00 88.48 N ANISOU 2743 N ASP A 389 12493 11960 9166 1426 732 -1277 N ATOM 2744 CA ASP A 389 -16.175 -27.432 -24.474 1.00101.03 C ANISOU 2744 CA ASP A 389 14075 13694 10616 1565 904 -1450 C ATOM 2745 C ASP A 389 -14.825 -26.957 -23.953 1.00 98.57 C ANISOU 2745 C ASP A 389 13587 13445 10418 1605 1093 -1345 C ATOM 2746 O ASP A 389 -13.858 -27.718 -23.925 1.00105.50 O ANISOU 2746 O ASP A 389 14397 14304 11383 1735 1187 -1499 O ATOM 2747 CB ASP A 389 -16.394 -26.922 -25.900 1.00114.86 C ANISOU 2747 CB ASP A 389 15937 15693 12013 1561 973 -1472 C ATOM 2748 CG ASP A 389 -17.604 -27.550 -26.565 1.00121.43 C ANISOU 2748 CG ASP A 389 16946 16474 12717 1549 783 -1627 C ATOM 2749 OD1 ASP A 389 -18.088 -28.589 -26.067 1.00122.58 O ANISOU 2749 OD1 ASP A 389 17126 16399 13048 1571 627 -1769 O ATOM 2750 OD2 ASP A 389 -18.065 -27.009 -27.593 1.00121.98 O ANISOU 2750 OD2 ASP A 389 17120 16722 12503 1514 781 -1601 O ATOM 2751 N ALA A 390 -14.765 -25.694 -23.540 1.00 92.02 N ANISOU 2751 N ALA A 390 12677 12684 9604 1495 1139 -1090 N ATOM 2752 CA ALA A 390 -13.543 -25.132 -22.981 1.00 92.36 C ANISOU 2752 CA ALA A 390 12541 12777 9775 1510 1297 -970 C ATOM 2753 C ALA A 390 -13.071 -25.986 -21.812 1.00 97.75 C ANISOU 2753 C ALA A 390 13135 13246 10761 1576 1236 -1039 C ATOM 2754 O ALA A 390 -11.903 -26.371 -21.744 1.00 98.24 O ANISOU 2754 O ALA A 390 13082 13332 10911 1685 1361 -1121 O ATOM 2755 CB ALA A 390 -13.777 -23.700 -22.534 1.00 86.47 C ANISOU 2755 CB ALA A 390 11737 12073 9046 1366 1295 -689 C ATOM 2756 N PHE A 391 -13.988 -26.283 -20.895 1.00 97.58 N ANISOU 2756 N PHE A 391 13163 13018 10897 1508 1042 -1001 N ATOM 2757 CA PHE A 391 -13.678 -27.130 -19.750 1.00102.09 C ANISOU 2757 CA PHE A 391 13676 13373 11742 1557 957 -1047 C ATOM 2758 C PHE A 391 -13.091 -28.455 -20.220 1.00 79.48 C ANISOU 2758 C PHE A 391 10832 10459 8908 1719 983 -1307 C ATOM 2759 O PHE A 391 -12.024 -28.864 -19.767 1.00 94.09 O ANISOU 2759 O PHE A 391 12565 12263 10922 1818 1048 -1354 O ATOM 2760 CB PHE A 391 -14.933 -27.394 -18.912 1.00103.66 C ANISOU 2760 CB PHE A 391 13957 13375 12055 1456 747 -990 C ATOM 2761 CG PHE A 391 -15.536 -26.159 -18.303 1.00 73.19 C ANISOU 2761 CG PHE A 391 10068 9539 8201 1311 709 -754 C ATOM 2762 CD1 PHE A 391 -14.786 -25.006 -18.133 1.00 83.56 C ANISOU 2762 CD1 PHE A 391 11264 10977 9507 1279 832 -593 C ATOM 2763 CD2 PHE A 391 -16.858 -26.157 -17.895 1.00 72.63 C ANISOU 2763 CD2 PHE A 391 10079 9361 8157 1206 549 -701 C ATOM 2764 CE1 PHE A 391 -15.348 -23.873 -17.570 1.00 79.59 C ANISOU 2764 CE1 PHE A 391 10737 10480 9022 1154 786 -394 C ATOM 2765 CE2 PHE A 391 -17.424 -25.029 -17.332 1.00 89.17 C ANISOU 2765 CE2 PHE A 391 12140 11476 10265 1086 515 -504 C ATOM 2766 CZ PHE A 391 -16.669 -23.886 -17.169 1.00 69.48 C ANISOU 2766 CZ PHE A 391 9540 9096 7763 1064 630 -355 C ATOM 2767 N GLY A 392 -13.795 -29.118 -21.133 1.00 87.94 N ANISOU 2767 N GLY A 392 12049 11534 9829 1750 922 -1483 N ATOM 2768 CA GLY A 392 -13.356 -30.398 -21.660 1.00 83.26 C ANISOU 2768 CA GLY A 392 11495 10883 9256 1908 930 -1758 C ATOM 2769 C GLY A 392 -11.942 -30.343 -22.205 1.00107.17 C ANISOU 2769 C GLY A 392 14402 14083 12234 2044 1155 -1845 C ATOM 2770 O GLY A 392 -11.191 -31.315 -22.118 1.00 86.77 O ANISOU 2770 O GLY A 392 11769 11409 9792 2191 1176 -2027 O ATOM 2771 N ARG A 393 -11.580 -29.197 -22.771 1.00104.26 N ANISOU 2771 N ARG A 393 13979 13961 11674 1994 1324 -1711 N ATOM 2772 CA ARG A 393 -10.240 -28.994 -23.308 1.00105.82 C ANISOU 2772 CA ARG A 393 14040 14353 11813 2100 1565 -1762 C ATOM 2773 C ARG A 393 -9.245 -28.699 -22.189 1.00101.87 C ANISOU 2773 C ARG A 393 13338 13782 11586 2108 1611 -1628 C ATOM 2774 O ARG A 393 -8.071 -29.056 -22.282 1.00 87.95 O ANISOU 2774 O ARG A 393 11437 12070 9909 2238 1751 -1734 O ATOM 2775 CB ARG A 393 -10.246 -27.843 -24.315 1.00112.77 C ANISOU 2775 CB ARG A 393 14938 15519 12389 2023 1725 -1638 C ATOM 2776 CG ARG A 393 -10.944 -28.163 -25.630 1.00123.43 C ANISOU 2776 CG ARG A 393 16475 16997 13424 2050 1720 -1801 C ATOM 2777 CD ARG A 393 -11.607 -26.925 -26.211 1.00128.68 C ANISOU 2777 CD ARG A 393 17217 17838 13837 1901 1737 -1589 C ATOM 2778 NE ARG A 393 -10.707 -25.776 -26.219 1.00129.96 N ANISOU 2778 NE ARG A 393 17228 18180 13971 1847 1938 -1374 N ATOM 2779 CZ ARG A 393 -11.103 -24.514 -26.351 1.00136.54 C ANISOU 2779 CZ ARG A 393 18075 19117 14688 1700 1946 -1120 C ATOM 2780 NH1 ARG A 393 -12.391 -24.223 -26.482 1.00135.27 N ANISOU 2780 NH1 ARG A 393 18068 18904 14425 1600 1765 -1050 N ATOM 2781 NH2 ARG A 393 -10.208 -23.537 -26.345 1.00144.27 N ANISOU 2781 NH2 ARG A 393 18906 20240 15669 1652 2128 -933 N ATOM 2782 N TYR A 394 -9.721 -28.050 -21.131 1.00 95.89 N ANISOU 2782 N TYR A 394 12561 12909 10966 1972 1490 -1405 N ATOM 2783 CA TYR A 394 -8.862 -27.661 -20.016 1.00 89.68 C ANISOU 2783 CA TYR A 394 11595 12057 10423 1962 1508 -1263 C ATOM 2784 C TYR A 394 -8.520 -28.834 -19.099 1.00 90.01 C ANISOU 2784 C TYR A 394 11601 11859 10740 2068 1384 -1379 C ATOM 2785 O TYR A 394 -7.415 -28.905 -18.564 1.00 85.60 O ANISOU 2785 O TYR A 394 10877 11281 10367 2143 1443 -1371 O ATOM 2786 CB TYR A 394 -9.524 -26.550 -19.200 1.00 88.72 C ANISOU 2786 CB TYR A 394 11476 11898 10337 1786 1415 -999 C ATOM 2787 CG TYR A 394 -9.722 -25.256 -19.957 1.00 94.10 C ANISOU 2787 CG TYR A 394 12165 12795 10795 1677 1528 -845 C ATOM 2788 CD1 TYR A 394 -8.885 -24.901 -21.009 1.00 93.27 C ANISOU 2788 CD1 TYR A 394 11992 12922 10526 1726 1748 -874 C ATOM 2789 CD2 TYR A 394 -10.750 -24.388 -19.619 1.00 91.83 C ANISOU 2789 CD2 TYR A 394 11951 12477 10465 1526 1417 -664 C ATOM 2790 CE1 TYR A 394 -9.069 -23.717 -21.697 1.00 97.59 C ANISOU 2790 CE1 TYR A 394 12554 13657 10869 1618 1844 -709 C ATOM 2791 CE2 TYR A 394 -10.940 -23.208 -20.301 1.00 92.18 C ANISOU 2791 CE2 TYR A 394 12006 12696 10321 1430 1502 -513 C ATOM 2792 CZ TYR A 394 -10.101 -22.878 -21.340 1.00 96.00 C ANISOU 2792 CZ TYR A 394 12433 13401 10641 1471 1710 -527 C ATOM 2793 OH TYR A 394 -10.294 -21.698 -22.016 1.00 97.45 O ANISOU 2793 OH TYR A 394 12637 13752 10639 1366 1787 -354 O ATOM 2794 N ILE A 395 -9.463 -29.752 -18.916 1.00 98.84 N ANISOU 2794 N ILE A 395 12871 12789 11896 2070 1203 -1479 N ATOM 2795 CA ILE A 395 -9.237 -30.902 -18.043 1.00 99.82 C ANISOU 2795 CA ILE A 395 12982 12662 12283 2158 1063 -1571 C ATOM 2796 C ILE A 395 -8.160 -31.825 -18.611 1.00101.41 C ANISOU 2796 C ILE A 395 13107 12876 12547 2362 1164 -1813 C ATOM 2797 O ILE A 395 -7.469 -32.512 -17.860 1.00108.83 O ANISOU 2797 O ILE A 395 13959 13656 13736 2459 1103 -1856 O ATOM 2798 CB ILE A 395 -10.536 -31.701 -17.790 1.00 97.76 C ANISOU 2798 CB ILE A 395 12902 12191 12050 2101 849 -1619 C ATOM 2799 CG1 ILE A 395 -11.128 -32.207 -19.107 1.00103.25 C ANISOU 2799 CG1 ILE A 395 13739 12957 12534 2146 862 -1829 C ATOM 2800 CG2 ILE A 395 -11.549 -30.846 -17.040 1.00 95.87 C ANISOU 2800 CG2 ILE A 395 12709 11922 11794 1911 747 -1382 C ATOM 2801 CD1 ILE A 395 -10.809 -33.652 -19.398 1.00113.39 C ANISOU 2801 CD1 ILE A 395 15063 14088 13930 2312 807 -2101 C ATOM 2802 N THR A 396 -8.015 -31.836 -19.934 1.00100.08 N ANISOU 2802 N THR A 396 12972 12903 12151 2431 1317 -1972 N ATOM 2803 CA THR A 396 -6.951 -32.604 -20.576 1.00 97.20 C ANISOU 2803 CA THR A 396 12520 12593 11819 2633 1450 -2217 C ATOM 2804 C THR A 396 -5.688 -31.755 -20.704 1.00 98.27 C ANISOU 2804 C THR A 396 12438 12948 11952 2663 1682 -2130 C ATOM 2805 O THR A 396 -4.699 -32.182 -21.295 1.00 93.45 O ANISOU 2805 O THR A 396 11717 12440 11352 2825 1840 -2312 O ATOM 2806 CB THR A 396 -7.365 -33.113 -21.973 1.00100.52 C ANISOU 2806 CB THR A 396 13085 13130 11979 2708 1511 -2462 C ATOM 2807 OG1 THR A 396 -7.442 -32.014 -22.890 1.00107.28 O ANISOU 2807 OG1 THR A 396 13951 14283 12528 2624 1688 -2367 O ATOM 2808 CG2 THR A 396 -8.709 -33.830 -21.909 1.00100.02 C ANISOU 2808 CG2 THR A 396 13234 12860 11909 2649 1275 -2532 C ATOM 2809 N CYS A 397 -5.737 -30.547 -20.151 1.00103.07 N ANISOU 2809 N CYS A 397 12979 13627 12556 2507 1700 -1855 N ATOM 2810 CA CYS A 397 -4.575 -29.665 -20.093 1.00105.26 C ANISOU 2810 CA CYS A 397 13037 14080 12878 2505 1890 -1735 C ATOM 2811 C CYS A 397 -4.070 -29.287 -21.486 1.00103.85 C ANISOU 2811 C CYS A 397 12818 14203 12437 2552 2155 -1821 C ATOM 2812 O CYS A 397 -2.948 -29.626 -21.862 1.00101.05 O ANISOU 2812 O CYS A 397 12304 13949 12140 2696 2323 -1959 O ATOM 2813 CB CYS A 397 -3.451 -30.324 -19.283 1.00106.19 C ANISOU 2813 CB CYS A 397 12971 14061 13313 2644 1866 -1804 C ATOM 2814 SG CYS A 397 -3.943 -30.892 -17.626 1.00112.88 S ANISOU 2814 SG CYS A 397 13873 14557 14459 2604 1555 -1704 S ATOM 2815 N ASN A 398 -4.903 -28.578 -22.244 1.00111.00 N ANISOU 2815 N ASN A 398 13864 15256 13053 2431 2191 -1734 N ATOM 2816 CA ASN A 398 -4.532 -28.116 -23.579 1.00122.23 C ANISOU 2816 CA ASN A 398 15275 16983 14184 2449 2437 -1778 C ATOM 2817 C ASN A 398 -4.419 -26.593 -23.635 1.00124.20 C ANISOU 2817 C ASN A 398 15450 17408 14332 2276 2549 -1482 C ATOM 2818 O ASN A 398 -3.379 -26.052 -24.011 1.00127.77 O ANISOU 2818 O ASN A 398 15726 18057 14762 2291 2775 -1429 O ATOM 2819 CB ASN A 398 -5.548 -28.602 -24.617 1.00128.66 C ANISOU 2819 CB ASN A 398 16330 17847 14709 2465 2390 -1941 C ATOM 2820 CG ASN A 398 -5.573 -30.114 -24.747 1.00134.14 C ANISOU 2820 CG ASN A 398 17095 18383 15489 2646 2301 -2261 C ATOM 2821 OD1 ASN A 398 -4.593 -30.793 -24.436 1.00131.99 O ANISOU 2821 OD1 ASN A 398 16674 18046 15430 2796 2356 -2401 O ATOM 2822 ND2 ASN A 398 -6.696 -30.649 -25.214 1.00138.46 N ANISOU 2822 ND2 ASN A 398 17866 18859 15885 2633 2152 -2384 N ATOM 2823 N TYR A 399 -5.497 -25.909 -23.265 1.00125.78 N ANISOU 2823 N TYR A 399 15778 17532 14481 2113 2390 -1292 N ATOM 2824 CA TYR A 399 -5.508 -24.448 -23.197 1.00131.03 C ANISOU 2824 CA TYR A 399 16386 18314 15086 1943 2452 -1003 C ATOM 2825 C TYR A 399 -5.283 -23.797 -24.561 1.00135.16 C ANISOU 2825 C TYR A 399 16927 19138 15288 1913 2678 -963 C ATOM 2826 O TYR A 399 -4.872 -22.638 -24.639 1.00135.00 O ANISOU 2826 O TYR A 399 16804 19250 15240 1799 2796 -738 O ATOM 2827 CB TYR A 399 -4.435 -23.949 -22.228 1.00122.79 C ANISOU 2827 CB TYR A 399 15102 17228 14327 1925 2499 -868 C ATOM 2828 CG TYR A 399 -4.336 -24.742 -20.947 1.00113.33 C ANISOU 2828 CG TYR A 399 13858 15763 13441 1992 2311 -935 C ATOM 2829 CD1 TYR A 399 -5.180 -24.480 -19.878 1.00103.20 C ANISOU 2829 CD1 TYR A 399 12652 14280 12279 1884 2088 -800 C ATOM 2830 CD2 TYR A 399 -3.391 -25.748 -20.806 1.00120.08 C ANISOU 2830 CD2 TYR A 399 14589 16567 14467 2166 2359 -1131 C ATOM 2831 CE1 TYR A 399 -5.088 -25.203 -18.707 1.00106.73 C ANISOU 2831 CE1 TYR A 399 13069 14496 12989 1938 1920 -845 C ATOM 2832 CE2 TYR A 399 -3.291 -26.474 -19.641 1.00119.58 C ANISOU 2832 CE2 TYR A 399 14492 16256 14685 2225 2176 -1175 C ATOM 2833 CZ TYR A 399 -4.140 -26.198 -18.594 1.00116.52 C ANISOU 2833 CZ TYR A 399 14196 15683 14394 2106 1958 -1024 C ATOM 2834 OH TYR A 399 -4.038 -26.925 -17.431 1.00122.92 O ANISOU 2834 OH TYR A 399 14984 16257 15463 2160 1778 -1053 O ATOM 2835 N ARG A 400 -5.555 -24.537 -25.630 1.00134.54 N ANISOU 2835 N ARG A 400 16986 19168 14966 2012 2734 -1178 N ATOM 2836 CA ARG A 400 -5.356 -24.028 -26.983 1.00133.97 C ANISOU 2836 CA ARG A 400 16954 19400 14550 1996 2953 -1159 C ATOM 2837 C ARG A 400 -6.694 -23.848 -27.692 1.00135.15 C ANISOU 2837 C ARG A 400 17361 19583 14408 1916 2824 -1137 C ATOM 2838 O ARG A 400 -6.804 -23.077 -28.646 1.00135.25 O ANISOU 2838 O ARG A 400 17437 19822 14129 1840 2945 -1017 O ATOM 2839 CB ARG A 400 -4.464 -24.980 -27.784 1.00132.28 C ANISOU 2839 CB ARG A 400 16679 19334 14246 2189 3155 -1443 C TER 2840 ARG A 400 HETATM 2841 C1 PLM A1201 -3.981 -32.524 -17.354 1.00104.12 C ANISOU 2841 C1 PLM A1201 12835 13183 13542 2767 1390 -1930 C HETATM 2842 O1 PLM A1201 -3.785 -33.314 -18.303 1.00103.97 O ANISOU 2842 O1 PLM A1201 12848 13201 13457 2911 1468 -2182 O HETATM 2843 C2 PLM A1201 -4.656 -33.076 -16.117 1.00100.46 C ANISOU 2843 C2 PLM A1201 12474 12428 13270 2709 1123 -1837 C HETATM 2844 C3 PLM A1201 -3.718 -33.012 -14.914 1.00105.67 C ANISOU 2844 C3 PLM A1201 12963 12982 14203 2742 1055 -1718 C HETATM 2845 C4 PLM A1201 -4.261 -33.843 -13.754 1.00108.07 C ANISOU 2845 C4 PLM A1201 13375 12985 14703 2724 791 -1663 C HETATM 2846 C5 PLM A1201 -3.446 -33.636 -12.479 1.00108.46 C ANISOU 2846 C5 PLM A1201 13279 12943 14987 2730 700 -1508 C HETATM 2847 C6 PLM A1201 -4.022 -34.430 -11.307 1.00110.81 C ANISOU 2847 C6 PLM A1201 13699 12953 15448 2698 441 -1426 C HETATM 2848 C7 PLM A1201 -3.388 -34.021 -9.978 1.00113.75 C ANISOU 2848 C7 PLM A1201 13958 13263 15997 2666 337 -1234 C HETATM 2849 C8 PLM A1201 -4.004 -34.776 -8.800 1.00112.19 C ANISOU 2849 C8 PLM A1201 13899 12800 15929 2620 87 -1129 C HETATM 2850 C9 PLM A1201 -3.607 -34.146 -7.466 1.00104.24 C ANISOU 2850 C9 PLM A1201 12817 11771 15020 2548 -17 -909 C HETATM 2851 CA PLM A1201 -4.162 -34.922 -6.273 1.00100.96 C ANISOU 2851 CA PLM A1201 12542 11103 14716 2503 -258 -792 C HETATM 2852 CB PLM A1201 -4.682 -33.966 -5.203 1.00101.70 C ANISOU 2852 CB PLM A1201 12678 11243 14719 2324 -322 -553 C HETATM 2853 CC PLM A1201 -4.643 -34.567 -3.799 1.00105.39 C ANISOU 2853 CC PLM A1201 13207 11503 15334 2314 -550 -411 C HETATM 2854 CD PLM A1201 -5.814 -35.506 -3.527 1.00104.67 C ANISOU 2854 CD PLM A1201 13326 11217 15225 2243 -680 -378 C HETATM 2855 CE PLM A1201 -6.453 -35.193 -2.177 1.00106.60 C ANISOU 2855 CE PLM A1201 13671 11413 15419 2089 -811 -145 C HETATM 2856 CF PLM A1201 -7.060 -36.441 -1.547 1.00109.83 C ANISOU 2856 CF PLM A1201 14241 11564 15925 2070 -996 -84 C HETATM 2857 CG PLM A1201 -7.902 -36.084 -0.342 1.00109.68 C ANISOU 2857 CG PLM A1201 14337 11534 15801 1895 -1086 144 C HETATM 2858 C1 ERM A1202 -23.207 -14.779 5.258 1.00 71.97 C HETATM 2859 N1 ERM A1202 -23.981 -13.841 5.853 1.00 73.37 N HETATM 2860 O1 ERM A1202 -21.345 -19.525 11.781 1.00 75.19 O HETATM 2861 C10 ERM A1202 -23.417 -14.936 9.772 1.00 62.58 C HETATM 2862 C11 ERM A1202 -24.263 -13.829 9.591 1.00 68.26 C HETATM 2863 C12 ERM A1202 -24.531 -13.360 8.274 1.00 65.04 C HETATM 2864 C13 ERM A1202 -23.956 -14.004 7.241 1.00 69.42 C HETATM 2865 C14 ERM A1202 -23.120 -15.104 7.428 1.00 70.11 C HETATM 2866 C15 ERM A1202 -21.108 -19.722 6.479 1.00 69.63 C HETATM 2867 C16 ERM A1202 -20.336 -19.066 11.301 1.00 68.00 C HETATM 2868 C17 ERM A1202 -19.079 -19.801 13.277 1.00 61.17 C HETATM 2869 C18 ERM A1202 -20.048 -19.195 14.262 1.00 61.71 C HETATM 2870 C19 ERM A1202 -21.989 -19.995 15.470 1.00 66.56 C HETATM 2871 N2 ERM A1202 -20.898 -18.702 7.541 1.00 61.07 N HETATM 2872 C2 ERM A1202 -22.648 -15.596 6.197 1.00 73.93 C HETATM 2873 O2 ERM A1202 -19.492 -21.169 13.213 1.00 61.15 O HETATM 2874 C20 ERM A1202 -22.348 -21.316 16.131 1.00 62.66 C HETATM 2875 C21 ERM A1202 -21.933 -23.737 16.400 1.00 65.76 C HETATM 2876 C22 ERM A1202 -21.723 -24.674 15.235 1.00 65.08 C HETATM 2877 C23 ERM A1202 -20.639 -23.987 14.353 1.00 58.06 C HETATM 2878 C24 ERM A1202 -20.578 -22.568 14.942 1.00 67.44 C HETATM 2879 C25 ERM A1202 -20.705 -21.456 13.916 1.00 68.53 C HETATM 2880 C26 ERM A1202 -17.640 -19.624 13.724 1.00 62.49 C HETATM 2881 C27 ERM A1202 -23.178 -19.432 14.749 1.00 71.41 C HETATM 2882 C28 ERM A1202 -24.012 -18.562 15.664 1.00 74.14 C HETATM 2883 C29 ERM A1202 -23.451 -17.439 16.275 1.00 83.38 C HETATM 2884 C3 ERM A1202 -21.729 -16.778 6.157 1.00 75.29 C HETATM 2885 N3 ERM A1202 -19.159 -19.150 11.962 1.00 66.47 N HETATM 2886 O3 ERM A1202 -20.043 -18.061 14.692 1.00 61.39 O HETATM 2887 C30 ERM A1202 -24.228 -16.640 17.113 1.00 85.53 C HETATM 2888 C31 ERM A1202 -25.568 -16.962 17.338 1.00 79.24 C HETATM 2889 C32 ERM A1202 -26.128 -18.082 16.726 1.00 81.29 C HETATM 2890 C33 ERM A1202 -25.351 -18.881 15.887 1.00 77.04 C HETATM 2891 C4 ERM A1202 -21.926 -17.607 7.478 1.00 63.65 C HETATM 2892 N4 ERM A1202 -20.899 -20.175 14.562 1.00 65.09 N HETATM 2893 O4 ERM A1202 -23.283 -21.359 16.938 1.00 64.25 O HETATM 2894 C5 ERM A1202 -20.849 -19.400 8.867 1.00 64.92 C HETATM 2895 N5 ERM A1202 -21.688 -22.417 15.850 1.00 62.08 N HETATM 2896 O5 ERM A1202 -21.747 -21.712 13.035 1.00 66.26 O HETATM 2897 C6 ERM A1202 -20.410 -18.391 9.896 1.00 56.44 C HETATM 2898 C7 ERM A1202 -21.287 -17.170 9.864 1.00 70.62 C HETATM 2899 C8 ERM A1202 -21.903 -16.787 8.751 1.00 68.91 C HETATM 2900 C9 ERM A1202 -22.826 -15.598 8.707 1.00 60.53 C HETATM 2901 C1 CLR A1203 -6.392 -26.571 -12.872 1.00 93.98 C HETATM 2902 C2 CLR A1203 -6.308 -26.498 -14.410 1.00 96.08 C HETATM 2903 C3 CLR A1203 -6.381 -27.845 -15.137 1.00 99.95 C HETATM 2904 C4 CLR A1203 -7.562 -28.659 -14.627 1.00 98.46 C HETATM 2905 C5 CLR A1203 -7.281 -28.927 -13.168 1.00 96.68 C HETATM 2906 C6 CLR A1203 -7.141 -30.158 -12.774 1.00 97.77 C HETATM 2907 C7 CLR A1203 -6.859 -30.552 -11.352 1.00 94.28 C HETATM 2908 C8 CLR A1203 -7.194 -29.416 -10.385 1.00 97.74 C HETATM 2909 C9 CLR A1203 -6.595 -28.109 -10.910 1.00 91.39 C HETATM 2910 C10 CLR A1203 -7.186 -27.743 -12.264 1.00 91.03 C HETATM 2911 C11 CLR A1203 -6.763 -26.954 -9.925 1.00 84.59 C HETATM 2912 C12 CLR A1203 -6.164 -27.278 -8.548 1.00 80.33 C HETATM 2913 C13 CLR A1203 -6.755 -28.595 -8.021 1.00 80.50 C HETATM 2914 C14 CLR A1203 -6.499 -29.719 -9.068 1.00 99.06 C HETATM 2915 C15 CLR A1203 -7.008 -30.964 -8.324 1.00 92.09 C HETATM 2916 C16 CLR A1203 -6.567 -30.713 -6.856 1.00 92.15 C HETATM 2917 C17 CLR A1203 -6.097 -29.243 -6.802 1.00 86.10 C HETATM 2918 C18 CLR A1203 -8.277 -28.504 -7.839 1.00 72.12 C HETATM 2919 C19 CLR A1203 -8.619 -27.257 -12.036 1.00 86.25 C HETATM 2920 C20 CLR A1203 -6.520 -28.699 -5.439 1.00 89.82 C HETATM 2921 C21 CLR A1203 -6.612 -27.179 -5.405 1.00 92.79 C HETATM 2922 C22 CLR A1203 -5.404 -29.058 -4.467 1.00 92.73 C HETATM 2923 C23 CLR A1203 -5.957 -29.269 -3.057 1.00 99.91 C HETATM 2924 C24 CLR A1203 -4.908 -29.994 -2.207 1.00103.78 C HETATM 2925 C25 CLR A1203 -5.131 -29.764 -0.709 1.00103.89 C HETATM 2926 C26 CLR A1203 -4.355 -30.818 0.084 1.00105.91 C HETATM 2927 C27 CLR A1203 -6.617 -29.869 -0.358 1.00105.79 C HETATM 2928 O1 CLR A1203 -6.552 -27.640 -16.541 1.00100.18 O HETATM 2929 C10 OLC A1204 -42.120 -19.640 -2.795 1.00106.38 C HETATM 2930 C9 OLC A1204 -42.063 -19.440 -4.166 1.00108.70 C HETATM 2931 C11 OLC A1204 -40.918 -19.320 -1.939 1.00105.06 C HETATM 2932 C8 OLC A1204 -40.716 -19.573 -4.927 1.00 70.19 C HETATM 2933 C24 OLC A1204 -35.038 -14.825 -13.746 1.00 96.54 C HETATM 2934 C12 OLC A1204 -39.918 -20.476 -1.973 1.00100.85 C HETATM 2935 C7 OLC A1204 -40.897 -19.202 -6.392 1.00 60.12 C HETATM 2936 C6 OLC A1204 -39.581 -19.561 -7.159 1.00 63.47 C HETATM 2937 C5 OLC A1204 -38.469 -18.547 -6.837 1.00 58.88 C HETATM 2938 C4 OLC A1204 -37.097 -19.133 -7.311 1.00 74.64 C HETATM 2939 C3 OLC A1204 -36.125 -17.970 -7.573 1.00 76.02 C HETATM 2940 C2 OLC A1204 -35.058 -18.400 -8.580 1.00 76.68 C HETATM 2941 C21 OLC A1204 -34.877 -15.829 -11.475 1.00 85.03 C HETATM 2942 C1 OLC A1204 -34.666 -17.162 -9.475 1.00 88.85 C HETATM 2943 C22 OLC A1204 -35.761 -15.641 -12.705 1.00 91.90 C HETATM 2944 O19 OLC A1204 -33.651 -16.521 -9.233 1.00 88.33 O HETATM 2945 O25 OLC A1204 -34.778 -15.612 -14.883 1.00 92.85 O HETATM 2946 O23 OLC A1204 -36.093 -16.897 -13.230 1.00 95.09 O HETATM 2947 O20 OLC A1204 -35.465 -16.825 -10.614 1.00 90.25 O HETATM 2948 C9 OLC A1205 -0.661 -29.786 -5.274 1.00 70.11 C HETATM 2949 C8 OLC A1205 -1.442 -30.296 -6.512 1.00 88.57 C HETATM 2950 C24 OLC A1205 0.349 -25.038 -17.887 1.00115.68 C HETATM 2951 C7 OLC A1205 -1.505 -29.216 -7.586 1.00 83.35 C HETATM 2952 C6 OLC A1205 -2.175 -29.816 -8.868 1.00 87.65 C HETATM 2953 C5 OLC A1205 -2.190 -28.784 -10.009 1.00 93.74 C HETATM 2954 C4 OLC A1205 -2.903 -29.412 -11.255 1.00101.78 C HETATM 2955 C3 OLC A1205 -3.145 -28.336 -12.329 1.00 99.12 C HETATM 2956 C2 OLC A1205 -1.878 -27.517 -12.568 1.00 97.86 C HETATM 2957 C21 OLC A1205 -0.961 -26.025 -16.033 1.00112.22 C HETATM 2958 C1 OLC A1205 -1.778 -27.222 -14.110 1.00121.00 C HETATM 2959 C22 OLC A1205 0.436 -25.646 -16.512 1.00118.61 C HETATM 2960 O19 OLC A1205 -2.322 -27.983 -14.902 1.00125.52 O HETATM 2961 O25 OLC A1205 1.336 -24.049 -18.034 1.00114.77 O HETATM 2962 O23 OLC A1205 1.004 -24.730 -15.619 1.00124.63 O HETATM 2963 O20 OLC A1205 -0.959 -26.152 -14.596 1.00115.02 O HETATM 2964 C1 PEG A1206 -26.005 -20.632 -18.573 1.00 94.48 C HETATM 2965 O1 PEG A1206 -26.960 -20.532 -19.528 1.00 97.86 O HETATM 2966 C2 PEG A1206 -24.720 -20.057 -19.080 1.00101.15 C HETATM 2967 O2 PEG A1206 -24.645 -18.668 -18.800 1.00100.42 O HETATM 2968 C3 PEG A1206 -23.726 -17.947 -19.651 1.00101.85 C HETATM 2969 C4 PEG A1206 -24.367 -17.660 -20.988 1.00104.84 C HETATM 2970 O4 PEG A1206 -23.434 -17.051 -21.838 1.00107.36 O HETATM 2971 C18 OLC A1207 -3.679 -22.580 5.762 1.00112.71 C HETATM 2972 C10 OLC A1207 -3.586 -25.292 -0.951 1.00108.23 C HETATM 2973 C9 OLC A1207 -3.200 -25.415 -2.271 1.00113.24 C HETATM 2974 C17 OLC A1207 -3.586 -21.074 5.515 1.00109.90 C HETATM 2975 C11 OLC A1207 -4.344 -24.071 -0.501 1.00108.04 C HETATM 2976 C8 OLC A1207 -2.906 -24.144 -3.108 1.00113.32 C HETATM 2977 C24 OLC A1207 -5.202 -17.291 -13.655 1.00134.88 C HETATM 2978 C16 OLC A1207 -4.684 -20.587 4.554 1.00103.36 C HETATM 2979 C12 OLC A1207 -4.070 -23.834 0.976 1.00109.23 C HETATM 2980 C7 OLC A1207 -3.055 -24.465 -4.586 1.00114.69 C HETATM 2981 C15 OLC A1207 -4.183 -20.610 3.104 1.00 99.30 C HETATM 2982 C13 OLC A1207 -3.996 -22.318 1.212 1.00112.27 C HETATM 2983 C6 OLC A1207 -3.066 -23.115 -5.371 1.00132.22 C HETATM 2984 C14 OLC A1207 -3.869 -22.093 2.719 1.00112.69 C HETATM 2985 C5 OLC A1207 -4.108 -23.182 -6.499 1.00130.84 C HETATM 2986 C4 OLC A1207 -4.493 -21.728 -6.934 1.00124.32 C HETATM 2987 C3 OLC A1207 -5.220 -21.787 -8.288 1.00122.26 C HETATM 2988 C2 OLC A1207 -5.395 -20.371 -8.827 1.00119.63 C HETATM 2989 C21 OLC A1207 -5.885 -18.382 -11.544 1.00143.52 C HETATM 2990 C1 OLC A1207 -5.463 -20.442 -10.398 1.00153.79 C HETATM 2991 C22 OLC A1207 -6.253 -18.152 -13.006 1.00139.14 C HETATM 2992 O19 OLC A1207 -4.460 -20.810 -11.002 1.00154.74 O HETATM 2993 O25 OLC A1207 -5.811 -16.451 -14.602 1.00130.24 O HETATM 2994 O23 OLC A1207 -6.313 -19.381 -13.673 1.00137.59 O HETATM 2995 O20 OLC A1207 -6.420 -19.648 -11.107 1.00150.14 O HETATM 2996 C10 OLC A1208 -26.037 -1.766 2.779 1.00106.23 C HETATM 2997 C9 OLC A1208 -26.557 -2.357 3.915 1.00105.16 C HETATM 2998 C11 OLC A1208 -24.570 -1.419 2.709 1.00 92.83 C HETATM 2999 C8 OLC A1208 -25.619 -2.756 5.083 1.00103.95 C HETATM 3000 C24 OLC A1208 -25.447 -5.023 18.151 1.00128.44 C HETATM 3001 C12 OLC A1208 -24.288 -0.624 1.435 1.00 80.62 C HETATM 3002 C7 OLC A1208 -26.468 -3.054 6.310 1.00111.11 C HETATM 3003 C6 OLC A1208 -25.555 -3.548 7.480 1.00100.41 C HETATM 3004 C5 OLC A1208 -26.356 -4.534 8.347 1.00 96.53 C HETATM 3005 C4 OLC A1208 -25.463 -5.075 9.513 1.00118.30 C HETATM 3006 C3 OLC A1208 -26.005 -4.567 10.864 1.00119.39 C HETATM 3007 C2 OLC A1208 -25.563 -5.513 11.982 1.00116.31 C HETATM 3008 C21 OLC A1208 -25.513 -4.610 15.697 1.00121.56 C HETATM 3009 C1 OLC A1208 -26.003 -4.933 13.381 1.00105.44 C HETATM 3010 C22 OLC A1208 -24.719 -5.218 16.848 1.00127.20 C HETATM 3011 O19 OLC A1208 -26.497 -3.814 13.441 1.00111.23 O HETATM 3012 O25 OLC A1208 -26.816 -5.275 17.961 1.00130.61 O HETATM 3013 O23 OLC A1208 -24.577 -6.592 16.625 1.00125.99 O HETATM 3014 O20 OLC A1208 -25.540 -5.539 14.592 1.00111.38 O HETATM 3015 C TRS A1209 -31.591 -8.376 21.657 1.00137.59 C HETATM 3016 C1 TRS A1209 -32.918 -7.753 22.079 1.00137.26 C HETATM 3017 C2 TRS A1209 -31.826 -9.726 20.976 1.00136.29 C HETATM 3018 C3 TRS A1209 -30.691 -8.556 22.876 1.00137.48 C HETATM 3019 N TRS A1209 -30.900 -7.457 20.748 1.00136.64 N HETATM 3020 O1 TRS A1209 -33.388 -8.366 23.260 1.00136.01 O HETATM 3021 O2 TRS A1209 -32.338 -9.603 19.665 1.00133.78 O HETATM 3022 O3 TRS A1209 -29.476 -9.162 22.492 1.00138.22 O HETATM 3023 C1 OLA A1210 -13.238 -8.743 -11.683 1.00 85.82 C HETATM 3024 C2 OLA A1210 -13.220 -9.549 -10.405 1.00 84.61 C HETATM 3025 C3 OLA A1210 -13.514 -8.636 -9.220 1.00 86.33 C HETATM 3026 C4 OLA A1210 -12.747 -9.071 -7.976 1.00 88.15 C HETATM 3027 C5 OLA A1210 -13.001 -8.101 -6.827 1.00 90.59 C HETATM 3028 C6 OLA A1210 -11.943 -8.231 -5.738 1.00 92.38 C HETATM 3029 C7 OLA A1210 -12.587 -8.573 -4.399 1.00 96.31 C HETATM 3030 C8 OLA A1210 -11.777 -8.018 -3.233 1.00 97.94 C HETATM 3031 C9 OLA A1210 -12.690 -7.790 -2.051 1.00101.44 C HETATM 3032 C10 OLA A1210 -12.320 -6.826 -1.003 1.00101.96 C HETATM 3033 C1 OLA A1211 -21.510 -35.852 11.906 1.00108.50 C HETATM 3034 O1 OLA A1211 -21.542 -35.915 13.154 1.00105.55 O HETATM 3035 O2 OLA A1211 -22.386 -36.452 11.245 1.00106.95 O HETATM 3036 C2 OLA A1211 -20.429 -35.066 11.202 1.00109.98 C HETATM 3037 C3 OLA A1211 -19.803 -34.045 12.148 1.00108.78 C HETATM 3038 C4 OLA A1211 -18.748 -33.203 11.434 1.00108.30 C HETATM 3039 C5 OLA A1211 -19.390 -32.090 10.612 1.00102.23 C HETATM 3040 C6 OLA A1211 -19.035 -32.219 9.134 1.00 96.69 C HETATM 3041 C7 OLA A1211 -20.082 -33.056 8.410 1.00 85.85 C HETATM 3042 C8 OLA A1211 -20.133 -32.738 6.922 1.00 77.36 C HETATM 3043 C9 OLA A1211 -21.453 -33.228 6.374 1.00 90.32 C HETATM 3044 C10 OLA A1211 -21.709 -33.245 4.926 1.00100.73 C HETATM 3045 C11 OLA A1211 -20.990 -32.286 4.007 1.00103.83 C HETATM 3046 C12 OLA A1211 -21.627 -32.340 2.623 1.00107.72 C HETATM 3047 C13 OLA A1211 -20.620 -32.741 1.552 1.00109.80 C HETATM 3048 C14 OLA A1211 -21.291 -33.610 0.495 1.00110.72 C HETATM 3049 C15 OLA A1211 -20.601 -33.470 -0.857 1.00110.08 C HETATM 3050 C16 OLA A1211 -21.539 -32.861 -1.895 1.00112.18 C HETATM 3051 C17 OLA A1211 -21.401 -33.553 -3.248 1.00113.74 C HETATM 3052 C18 OLA A1211 -20.939 -32.592 -4.338 1.00106.38 C HETATM 3053 C1 OLA A1212 -26.327 -0.467 11.438 1.00125.55 C HETATM 3054 O1 OLA A1212 -26.944 -0.674 12.506 1.00124.81 O HETATM 3055 O2 OLA A1212 -25.287 -1.118 11.204 1.00124.68 O HETATM 3056 C2 OLA A1212 -26.832 0.552 10.445 1.00121.67 C HETATM 3057 C3 OLA A1212 -27.798 -0.112 9.474 1.00117.73 C HETATM 3058 C4 OLA A1212 -28.364 0.895 8.480 1.00116.96 C HETATM 3059 C5 OLA A1212 -29.672 0.376 7.895 1.00119.72 C HETATM 3060 C6 OLA A1212 -29.446 -0.352 6.576 1.00123.60 C HETATM 3061 C7 OLA A1212 -30.468 0.078 5.531 1.00127.14 C HETATM 3062 C8 OLA A1212 -29.792 0.491 4.229 1.00128.73 C HETATM 3063 C9 OLA A1212 -30.000 1.963 3.957 1.00128.96 C HETATM 3064 C10 OLA A1212 -30.041 2.428 2.563 1.00126.60 C HETATM 3065 C11 OLA A1212 -29.345 1.624 1.491 1.00123.19 C HETATM 3066 C12 OLA A1212 -29.814 2.076 0.113 1.00117.31 C HETATM 3067 C13 OLA A1212 -29.068 3.326 -0.334 1.00108.39 C HETATM 3068 C14 OLA A1212 -28.912 3.357 -1.850 1.00105.49 C HETATM 3069 C15 OLA A1212 -29.776 4.440 -2.487 1.00104.68 C HETATM 3070 C16 OLA A1212 -31.101 3.882 -2.998 1.00105.95 C HETATM 3071 C17 OLA A1212 -31.661 4.753 -4.117 1.00101.83 C HETATM 3072 CA1 DGA A1213 -45.394 -4.971 -13.729 1.00143.81 C HETATM 3073 CA2 DGA A1213 -44.033 -4.871 -13.049 1.00137.39 C HETATM 3074 CA3 DGA A1213 -43.737 -3.416 -12.684 1.00129.70 C HETATM 3075 CA4 DGA A1213 -42.275 -3.285 -12.227 1.00123.20 C HETATM 3076 CA5 DGA A1213 -42.225 -3.079 -10.699 1.00116.84 C HETATM 3077 OA1 DGA A1213 -45.527 -4.578 -14.876 1.00147.06 O HETATM 3078 CB1 DGA A1213 -47.013 -9.281 -11.667 1.00128.90 C HETATM 3079 CB2 DGA A1213 -47.050 -9.439 -10.150 1.00118.25 C HETATM 3080 CB3 DGA A1213 -45.638 -9.654 -9.606 1.00111.77 C HETATM 3081 CB4 DGA A1213 -45.600 -9.257 -8.125 1.00108.72 C HETATM 3082 CB5 DGA A1213 -45.541 -10.517 -7.261 1.00116.13 C HETATM 3083 CB6 DGA A1213 -45.512 -10.126 -5.773 1.00126.15 C HETATM 3084 CB7 DGA A1213 -44.399 -10.893 -5.084 1.00135.12 C HETATM 3085 CB8 DGA A1213 -44.606 -10.859 -3.568 1.00141.95 C HETATM 3086 CB9 DGA A1213 -43.321 -10.398 -2.891 1.00139.99 C HETATM 3087 CAB DGA A1213 -42.896 -11.426 -1.828 1.00133.97 C HETATM 3088 CBB DGA A1213 -41.630 -10.940 -1.145 1.00126.57 C HETATM 3089 CCB DGA A1213 -41.792 -11.052 0.377 1.00121.30 C HETATM 3090 CDB DGA A1213 -42.765 -9.964 0.848 1.00118.33 C HETATM 3091 OB1 DGA A1213 -47.362 -10.209 -12.379 1.00130.79 O HETATM 3092 OG1 DGA A1213 -46.415 -5.726 -13.129 1.00145.02 O HETATM 3093 CG1 DGA A1213 -47.188 -6.475 -14.040 1.00146.48 C HETATM 3094 CG2 DGA A1213 -47.629 -7.764 -13.386 1.00143.83 C HETATM 3095 OG2 DGA A1213 -46.848 -7.997 -12.229 1.00138.23 O HETATM 3096 CG3 DGA A1213 -49.084 -7.656 -12.998 1.00143.21 C HETATM 3097 OXT DGA A1213 -49.889 -7.797 -14.140 1.00140.86 O HETATM 3098 CA1 DGA A1214 -49.374 -17.837 -12.200 1.00131.16 C HETATM 3099 CA2 DGA A1214 -50.629 -18.018 -11.350 1.00127.90 C HETATM 3100 CA3 DGA A1214 -50.331 -17.657 -9.893 1.00125.04 C HETATM 3101 CA4 DGA A1214 -49.203 -18.536 -9.333 1.00121.52 C HETATM 3102 CA5 DGA A1214 -48.822 -18.040 -7.922 1.00117.16 C HETATM 3103 CA6 DGA A1214 -49.305 -19.031 -6.853 1.00115.02 C HETATM 3104 CA7 DGA A1214 -49.033 -18.436 -5.475 1.00111.08 C HETATM 3105 CA8 DGA A1214 -50.318 -17.858 -4.900 1.00104.10 C HETATM 3106 OA1 DGA A1214 -48.573 -18.750 -12.302 1.00132.93 O HETATM 3107 CB1 DGA A1214 -49.411 -13.905 -10.087 1.00141.93 C HETATM 3108 CB2 DGA A1214 -49.074 -14.145 -8.618 1.00137.09 C HETATM 3109 CB3 DGA A1214 -47.830 -13.346 -8.233 1.00130.76 C HETATM 3110 CB4 DGA A1214 -47.664 -13.366 -6.706 1.00124.43 C HETATM 3111 OB1 DGA A1214 -50.494 -14.275 -10.511 1.00146.61 O HETATM 3112 OG1 DGA A1214 -49.093 -16.592 -12.787 1.00128.90 O HETATM 3113 CG1 DGA A1214 -48.233 -15.791 -12.007 1.00128.54 C HETATM 3114 CG2 DGA A1214 -48.505 -14.321 -12.237 1.00130.76 C HETATM 3115 OG2 DGA A1214 -48.374 -13.632 -11.005 1.00139.04 O HETATM 3116 CG3 DGA A1214 -47.505 -13.780 -13.232 1.00118.95 C HETATM 3117 OXT DGA A1214 -48.153 -12.945 -14.156 1.00112.06 O HETATM 3118 O HOH A1301 -26.536 -23.873 -7.780 1.00 66.77 O HETATM 3119 O HOH A1302 -17.300 -19.869 9.827 1.00 96.48 O HETATM 3120 O HOH A1303 -13.874 -10.958 28.301 1.00 92.23 O HETATM 3121 O HOH A1304 -40.628 -3.760 -15.281 1.00 96.70 O HETATM 3122 O HOH A1305 -3.491 -23.428 -11.527 1.00 95.19 O HETATM 3123 O HOH A1306 -18.573 -40.134 12.373 1.00 95.71 O HETATM 3124 O HOH A1307 -21.898 -19.001 -5.666 1.00 67.81 O CONECT 611 1196 CONECT 1196 611 CONECT 2437 2457 CONECT 2457 2437 CONECT 2814 2841 CONECT 2841 2814 2842 2843 CONECT 2842 2841 CONECT 2843 2841 2844 CONECT 2844 2843 2845 CONECT 2845 2844 2846 CONECT 2846 2845 2847 CONECT 2847 2846 2848 CONECT 2848 2847 2849 CONECT 2849 2848 2850 CONECT 2850 2849 2851 CONECT 2851 2850 2852 CONECT 2852 2851 2853 CONECT 2853 2852 2854 CONECT 2854 2853 2855 CONECT 2855 2854 2856 CONECT 2856 2855 2857 CONECT 2857 2856 CONECT 2858 2859 2872 CONECT 2859 2858 2864 CONECT 2860 2867 CONECT 2861 2862 2900 CONECT 2862 2861 2863 CONECT 2863 2862 2864 CONECT 2864 2859 2863 2865 CONECT 2865 2864 2872 2900 CONECT 2866 2871 CONECT 2867 2860 2885 2897 CONECT 2868 2869 2873 2880 2885 CONECT 2869 2868 2886 2892 CONECT 2870 2874 2881 2892 CONECT 2871 2866 2891 2894 CONECT 2872 2858 2865 2884 CONECT 2873 2868 2879 CONECT 2874 2870 2893 2895 CONECT 2875 2876 2895 CONECT 2876 2875 2877 CONECT 2877 2876 2878 CONECT 2878 2877 2879 2895 CONECT 2879 2873 2878 2892 2896 CONECT 2880 2868 CONECT 2881 2870 2882 CONECT 2882 2881 2883 2890 CONECT 2883 2882 2887 CONECT 2884 2872 2891 CONECT 2885 2867 2868 CONECT 2886 2869 CONECT 2887 2883 2888 CONECT 2888 2887 2889 CONECT 2889 2888 2890 CONECT 2890 2882 2889 CONECT 2891 2871 2884 2899 CONECT 2892 2869 2870 2879 CONECT 2893 2874 CONECT 2894 2871 2897 CONECT 2895 2874 2875 2878 CONECT 2896 2879 CONECT 2897 2867 2894 2898 CONECT 2898 2897 2899 CONECT 2899 2891 2898 2900 CONECT 2900 2861 2865 2899 CONECT 2901 2902 2910 CONECT 2902 2901 2903 CONECT 2903 2902 2904 2928 CONECT 2904 2903 2905 CONECT 2905 2904 2906 2910 CONECT 2906 2905 2907 CONECT 2907 2906 2908 CONECT 2908 2907 2909 2914 CONECT 2909 2908 2910 2911 CONECT 2910 2901 2905 2909 2919 CONECT 2911 2909 2912 CONECT 2912 2911 2913 CONECT 2913 2912 2914 2917 2918 CONECT 2914 2908 2913 2915 CONECT 2915 2914 2916 CONECT 2916 2915 2917 CONECT 2917 2913 2916 2920 CONECT 2918 2913 CONECT 2919 2910 CONECT 2920 2917 2921 2922 CONECT 2921 2920 CONECT 2922 2920 2923 CONECT 2923 2922 2924 CONECT 2924 2923 2925 CONECT 2925 2924 2926 2927 CONECT 2926 2925 CONECT 2927 2925 CONECT 2928 2903 CONECT 2929 2930 2931 CONECT 2930 2929 2932 CONECT 2931 2929 2934 CONECT 2932 2930 2935 CONECT 2933 2943 2945 CONECT 2934 2931 CONECT 2935 2932 2936 CONECT 2936 2935 2937 CONECT 2937 2936 2938 CONECT 2938 2937 2939 CONECT 2939 2938 2940 CONECT 2940 2939 2942 CONECT 2941 2943 2947 CONECT 2942 2940 2944 2947 CONECT 2943 2933 2941 2946 CONECT 2944 2942 CONECT 2945 2933 CONECT 2946 2943 CONECT 2947 2941 2942 CONECT 2948 2949 CONECT 2949 2948 2951 CONECT 2950 2959 2961 CONECT 2951 2949 2952 CONECT 2952 2951 2953 CONECT 2953 2952 2954 CONECT 2954 2953 2955 CONECT 2955 2954 2956 CONECT 2956 2955 2958 CONECT 2957 2959 2963 CONECT 2958 2956 2960 2963 CONECT 2959 2950 2957 2962 CONECT 2960 2958 CONECT 2961 2950 CONECT 2962 2959 CONECT 2963 2957 2958 CONECT 2964 2965 2966 CONECT 2965 2964 CONECT 2966 2964 2967 CONECT 2967 2966 2968 CONECT 2968 2967 2969 CONECT 2969 2968 2970 CONECT 2970 2969 CONECT 2971 2974 CONECT 2972 2973 2975 CONECT 2973 2972 2976 CONECT 2974 2971 2978 CONECT 2975 2972 2979 CONECT 2976 2973 2980 CONECT 2977 2991 2993 CONECT 2978 2974 2981 CONECT 2979 2975 2982 CONECT 2980 2976 2983 CONECT 2981 2978 2984 CONECT 2982 2979 2984 CONECT 2983 2980 2985 CONECT 2984 2981 2982 CONECT 2985 2983 2986 CONECT 2986 2985 2987 CONECT 2987 2986 2988 CONECT 2988 2987 2990 CONECT 2989 2991 2995 CONECT 2990 2988 2992 2995 CONECT 2991 2977 2989 2994 CONECT 2992 2990 CONECT 2993 2977 CONECT 2994 2991 CONECT 2995 2989 2990 CONECT 2996 2997 2998 CONECT 2997 2996 2999 CONECT 2998 2996 3001 CONECT 2999 2997 3002 CONECT 3000 3010 3012 CONECT 3001 2998 CONECT 3002 2999 3003 CONECT 3003 3002 3004 CONECT 3004 3003 3005 CONECT 3005 3004 3006 CONECT 3006 3005 3007 CONECT 3007 3006 3009 CONECT 3008 3010 3014 CONECT 3009 3007 3011 3014 CONECT 3010 3000 3008 3013 CONECT 3011 3009 CONECT 3012 3000 CONECT 3013 3010 CONECT 3014 3008 3009 CONECT 3015 3016 3017 3018 3019 CONECT 3016 3015 3020 CONECT 3017 3015 3021 CONECT 3018 3015 3022 CONECT 3019 3015 CONECT 3020 3016 CONECT 3021 3017 CONECT 3022 3018 CONECT 3023 3024 CONECT 3024 3023 3025 CONECT 3025 3024 3026 CONECT 3026 3025 3027 CONECT 3027 3026 3028 CONECT 3028 3027 3029 CONECT 3029 3028 3030 CONECT 3030 3029 3031 CONECT 3031 3030 3032 CONECT 3032 3031 CONECT 3033 3034 3035 3036 CONECT 3034 3033 CONECT 3035 3033 CONECT 3036 3033 3037 CONECT 3037 3036 3038 CONECT 3038 3037 3039 CONECT 3039 3038 3040 CONECT 3040 3039 3041 CONECT 3041 3040 3042 CONECT 3042 3041 3043 CONECT 3043 3042 3044 CONECT 3044 3043 3045 CONECT 3045 3044 3046 CONECT 3046 3045 3047 CONECT 3047 3046 3048 CONECT 3048 3047 3049 CONECT 3049 3048 3050 CONECT 3050 3049 3051 CONECT 3051 3050 3052 CONECT 3052 3051 CONECT 3053 3054 3055 3056 CONECT 3054 3053 CONECT 3055 3053 CONECT 3056 3053 3057 CONECT 3057 3056 3058 CONECT 3058 3057 3059 CONECT 3059 3058 3060 CONECT 3060 3059 3061 CONECT 3061 3060 3062 CONECT 3062 3061 3063 CONECT 3063 3062 3064 CONECT 3064 3063 3065 CONECT 3065 3064 3066 CONECT 3066 3065 3067 CONECT 3067 3066 3068 CONECT 3068 3067 3069 CONECT 3069 3068 3070 CONECT 3070 3069 3071 CONECT 3071 3070 CONECT 3072 3073 3077 3092 CONECT 3073 3072 3074 CONECT 3074 3073 3075 CONECT 3075 3074 3076 CONECT 3076 3075 CONECT 3077 3072 CONECT 3078 3079 3091 3095 CONECT 3079 3078 3080 CONECT 3080 3079 3081 CONECT 3081 3080 3082 CONECT 3082 3081 3083 CONECT 3083 3082 3084 CONECT 3084 3083 3085 CONECT 3085 3084 3086 CONECT 3086 3085 3087 CONECT 3087 3086 3088 CONECT 3088 3087 3089 CONECT 3089 3088 3090 CONECT 3090 3089 CONECT 3091 3078 CONECT 3092 3072 3093 CONECT 3093 3092 3094 CONECT 3094 3093 3095 3096 CONECT 3095 3078 3094 CONECT 3096 3094 3097 CONECT 3097 3096 CONECT 3098 3099 3106 3112 CONECT 3099 3098 3100 CONECT 3100 3099 3101 CONECT 3101 3100 3102 CONECT 3102 3101 3103 CONECT 3103 3102 3104 CONECT 3104 3103 3105 CONECT 3105 3104 CONECT 3106 3098 CONECT 3107 3108 3111 3115 CONECT 3108 3107 3109 CONECT 3109 3108 3110 CONECT 3110 3109 CONECT 3111 3107 CONECT 3112 3098 3113 CONECT 3113 3112 3114 CONECT 3114 3113 3115 3116 CONECT 3115 3107 3114 CONECT 3116 3114 3117 CONECT 3117 3116 MASTER 437 0 14 16 0 0 17 6 3121 1 282 34 END