HEADER MEMBRANE PROTEIN 27-NOV-17 6BQH TITLE CRYSTAL STRUCTURE OF 5-HT2C IN COMPLEX WITH RITANSERIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5-HYDROXYTRYPTAMINE RECEPTOR 2C,SOLUBLE CYTOCHROME B562; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: 5-HTR2C,5-HYDROXYTRYPTAMINE RECEPTOR 1C,5-HT1C,SEROTONIN COMPND 5 RECEPTOR 2C,CYTOCHROME B-562; COMPND 6 ENGINEERED: 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: HTR2C, HTR1C, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS HUMAN 5-HT2C RECEPTOR, GPCR, RITANSERIN, SELECTIVITY, BRIL, LCP, KEYWDS 2 MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.PENG,J.D.MCCORVY,K.HARPSOE,K.LANSU,S.YUAN,P.POPOV,L.QU,M.PU,T.CHE, AUTHOR 2 L.F.NIKOLAJSE,X.P.HUANG,Y.WU,L.SHEN,W.E.BJORN-YOSHIMOTO,K.DING, AUTHOR 3 D.WACKER,G.W.HAN,J.CHENG,V.KATRITCH,A.A.JENSEN,M.A.HANSON,S.ZHAO, AUTHOR 4 D.E.GLORIAM,B.L.ROTH,R.C.STEVENS,Z.LIU REVDAT 2 21-FEB-18 6BQH 1 JRNL REVDAT 1 14-FEB-18 6BQH 0 JRNL AUTH Y.PENG,J.D.MCCORVY,K.HARPSOE,K.LANSU,S.YUAN,P.POPOV,L.QU, JRNL AUTH 2 M.PU,T.CHE,L.F.NIKOLAJSEN,X.P.HUANG,Y.WU,L.SHEN, JRNL AUTH 3 W.E.BJORN-YOSHIMOTO,K.DING,D.WACKER,G.W.HAN,J.CHENG, JRNL AUTH 4 V.KATRITCH,A.A.JENSEN,M.A.HANSON,S.ZHAO,D.E.GLORIAM, JRNL AUTH 5 B.L.ROTH,R.C.STEVENS,Z.J.LIU JRNL TITL 5-HT2C RECEPTOR STRUCTURES REVEAL THE STRUCTURAL BASIS OF JRNL TITL 2 GPCR POLYPHARMACOLOGY. JRNL REF CELL V. 172 719 2018 JRNL REFN ISSN 1097-4172 JRNL PMID 29398112 JRNL DOI 10.1016/J.CELL.2018.01.001 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (DEV_2289: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.53 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1 REMARK 3 NUMBER OF REFLECTIONS : 17052 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.254 REMARK 3 R VALUE (WORKING SET) : 0.253 REMARK 3 FREE R VALUE : 0.275 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020 REMARK 3 FREE R VALUE TEST SET COUNT : 856 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 48.5328 - 4.9049 0.98 2945 160 0.2520 0.2648 REMARK 3 2 4.9049 - 3.8937 0.98 2823 150 0.2235 0.2246 REMARK 3 3 3.8937 - 3.4017 0.96 2740 137 0.2359 0.2786 REMARK 3 4 3.4017 - 3.0907 0.92 2624 136 0.2919 0.3820 REMARK 3 5 3.0907 - 2.8692 0.91 2553 135 0.3241 0.3910 REMARK 3 6 2.8692 - 2.7001 0.89 2511 138 0.3798 0.4301 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.510 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.800 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 : 0.003 2863 REMARK 3 ANGLE : 0.600 3874 REMARK 3 CHIRALITY : 0.039 463 REMARK 3 PLANARITY : 0.004 466 REMARK 3 DIHEDRAL : 12.972 1706 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 40.4427 33.1211 40.8027 REMARK 3 T TENSOR REMARK 3 T11: 0.8265 T22: 0.8279 REMARK 3 T33: 0.8205 T12: -0.0672 REMARK 3 T13: -0.0406 T23: -0.0198 REMARK 3 L TENSOR REMARK 3 L11: 2.5809 L22: 1.3260 REMARK 3 L33: 1.6583 L12: -0.1185 REMARK 3 L13: -0.7173 L23: 0.4424 REMARK 3 S TENSOR REMARK 3 S11: -0.0695 S12: 0.4302 S13: -0.1584 REMARK 3 S21: -0.0728 S22: -0.0775 S23: 0.0665 REMARK 3 S31: 0.1606 S32: 0.0287 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 6BQH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-17. REMARK 100 THE DEPOSITION ID IS D_1000231265. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-NOV-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17076 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2 REMARK 200 DATA REDUNDANCY : 10.50 REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2 REMARK 200 DATA REDUNDANCY IN SHELL : 5.70 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: 4IB4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 6.0, 100MM REMARK 280 (NH4)2SO4, 30% PEG400, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z 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 REMARK 290 7555 -X+1/2,Y+1/2,-Z 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 0.00000 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 0.00000 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 44.15500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.52500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.15500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.52500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.15500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.52500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.15500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.52500 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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 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 MET A 14 REMARK 465 LYS A 15 REMARK 465 THR A 16 REMARK 465 ILE A 17 REMARK 465 ILE A 18 REMARK 465 ALA A 19 REMARK 465 LEU A 20 REMARK 465 SER A 21 REMARK 465 TYR A 22 REMARK 465 ILE A 23 REMARK 465 PHE A 24 REMARK 465 CYS A 25 REMARK 465 LEU A 26 REMARK 465 VAL A 27 REMARK 465 PHE A 28 REMARK 465 ALA A 29 REMARK 465 ASP A 30 REMARK 465 TYR A 31 REMARK 465 LYS A 32 REMARK 465 ASP A 33 REMARK 465 ASP A 34 REMARK 465 ASP A 35 REMARK 465 ASP A 36 REMARK 465 GLY A 37 REMARK 465 ALA A 38 REMARK 465 PRO A 39 REMARK 465 THR A 40 REMARK 465 SER A 41 REMARK 465 ASP A 42 REMARK 465 GLY A 43 REMARK 465 GLY A 44 REMARK 465 ARG A 45 REMARK 465 ASP A 1021 REMARK 465 ASN A 1022 REMARK 465 ALA A 1023 REMARK 465 ALA A 1024 REMARK 465 GLN A 1025 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 VAL A 1069 REMARK 465 GLY A 1070 REMARK 465 GLN A 1071 REMARK 465 ILE A 1072 REMARK 465 ASP A 1073 REMARK 465 ASP A 1074 REMARK 465 ALA A 1075 REMARK 465 LEU A 1076 REMARK 465 LYS A 1077 REMARK 465 LEU A 1078 REMARK 465 ALA A 1079 REMARK 465 ASN A 1080 REMARK 465 GLU A 1081 REMARK 465 GLY A 1082 REMARK 465 LYS A 1083 REMARK 465 VAL A 1084 REMARK 465 LYS A 1085 REMARK 465 GLU A 1086 REMARK 465 ALA A 1087 REMARK 465 GLN A 1088 REMARK 465 ALA A 1089 REMARK 465 ALA A 1090 REMARK 465 ALA A 1091 REMARK 465 GLU A 1092 REMARK 465 LYS A 388 REMARK 465 VAL A 389 REMARK 465 GLU A 390 REMARK 465 LYS A 391 REMARK 465 LYS A 392 REMARK 465 PRO A 393 REMARK 465 GLY A 394 REMARK 465 ARG A 395 REMARK 465 PRO A 396 REMARK 465 LEU A 397 REMARK 465 GLU A 398 REMARK 465 VAL A 399 REMARK 465 LEU A 400 REMARK 465 PHE A 401 REMARK 465 GLN A 402 REMARK 465 GLY A 403 REMARK 465 PRO A 404 REMARK 465 HIS A 405 REMARK 465 HIS A 406 REMARK 465 HIS A 407 REMARK 465 HIS A 408 REMARK 465 HIS A 409 REMARK 465 HIS A 410 REMARK 465 HIS A 411 REMARK 465 HIS A 412 REMARK 465 HIS A 413 REMARK 465 HIS 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 ASN A 158 CG OD1 ND2 REMARK 470 GLU A 161 CG CD OE1 OE2 REMARK 470 SER A 163 OG REMARK 470 ARG A 164 NE CZ NH1 NH2 REMARK 470 LYS A 170 CG CD CE NZ REMARK 470 ARG A 243 CG CD NE CZ NH1 NH2 REMARK 470 LEU A1003 CG CD1 CD2 REMARK 470 TRP A1007 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A1007 CZ3 CH2 REMARK 470 GLU A1008 CG CD OE1 OE2 REMARK 470 ASN A1013 CG OD1 ND2 REMARK 470 LEU A1014 CG CD1 CD2 REMARK 470 LYS A1015 CG CD CE NZ REMARK 470 VAL A1016 CG1 CG2 REMARK 470 ILE A1017 CG1 CG2 CD1 REMARK 470 GLU A1018 CG CD OE1 OE2 REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 VAL A1026 CG1 CG2 REMARK 470 ASP A1028 CG OD1 OD2 REMARK 470 LEU A1030 CG CD1 CD2 REMARK 470 GLN A1041 CG CD OE1 NE2 REMARK 470 MET A1058 CG SD CE REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 ASP A1060 CG OD1 OD2 REMARK 470 PHE A1061 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 HIS A1063 CG ND1 CD2 CE1 NE2 REMARK 470 PHE A1065 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A1068 CG CD1 CD2 REMARK 470 GLN A1093 CG CD OE1 NE2 REMARK 470 LEU A1094 CG CD1 CD2 REMARK 470 LYS A1095 CG CD CE NZ REMARK 470 THR A1096 OG1 CG2 REMARK 470 ARG A1098 CG CD NE CZ NH1 NH2 REMARK 470 GLN A1103 CG CD OE1 NE2 REMARK 470 LYS A1104 CG CD CE NZ REMARK 470 GLN A 301 CG CD OE1 NE2 REMARK 470 ARG A 307 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 336 CG CD1 CD2 REMARK 470 GLU A 338 CG CD OE1 OE2 REMARK 470 LYS A 339 CG CD CE NZ REMARK 470 SER A 340 OG REMARK 470 TYR A 387 CG CD1 CD2 CE1 CE2 CZ OH REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LYS A 47 75.55 52.98 REMARK 500 LYS A 83 7.92 -69.06 REMARK 500 THR A 205 -51.77 -128.76 REMARK 500 PHE A 223 -52.38 -136.39 REMARK 500 TYR A1101 -24.17 -147.90 REMARK 500 LYS A 339 -161.16 -112.38 REMARK 500 ARG A 384 -67.66 -100.45 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 1202 REMARK 610 OLC A 1203 REMARK 610 OLC A 1204 REMARK 610 OLC A 1205 REMARK 610 OLC A 1206 REMARK 610 OLC A 1207 REMARK 610 OLA A 1209 REMARK 610 OLA A 1210 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue E2J A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC 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 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1210 DBREF 6BQH A 40 245 UNP P28335 5HT2C_HUMAN 40 245 DBREF 6BQH A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 6BQH A 301 393 UNP P28335 5HT2C_HUMAN 301 393 SEQADV 6BQH MET A 14 UNP P28335 EXPRESSION TAG SEQADV 6BQH LYS A 15 UNP P28335 EXPRESSION TAG SEQADV 6BQH THR A 16 UNP P28335 EXPRESSION TAG SEQADV 6BQH ILE A 17 UNP P28335 EXPRESSION TAG SEQADV 6BQH ILE A 18 UNP P28335 EXPRESSION TAG SEQADV 6BQH ALA A 19 UNP P28335 EXPRESSION TAG SEQADV 6BQH LEU A 20 UNP P28335 EXPRESSION TAG SEQADV 6BQH SER A 21 UNP P28335 EXPRESSION TAG SEQADV 6BQH TYR A 22 UNP P28335 EXPRESSION TAG SEQADV 6BQH ILE A 23 UNP P28335 EXPRESSION TAG SEQADV 6BQH PHE A 24 UNP P28335 EXPRESSION TAG SEQADV 6BQH CYS A 25 UNP P28335 EXPRESSION TAG SEQADV 6BQH LEU A 26 UNP P28335 EXPRESSION TAG SEQADV 6BQH VAL A 27 UNP P28335 EXPRESSION TAG SEQADV 6BQH PHE A 28 UNP P28335 EXPRESSION TAG SEQADV 6BQH ALA A 29 UNP P28335 EXPRESSION TAG SEQADV 6BQH ASP A 30 UNP P28335 EXPRESSION TAG SEQADV 6BQH TYR A 31 UNP P28335 EXPRESSION TAG SEQADV 6BQH LYS A 32 UNP P28335 EXPRESSION TAG SEQADV 6BQH ASP A 33 UNP P28335 EXPRESSION TAG SEQADV 6BQH ASP A 34 UNP P28335 EXPRESSION TAG SEQADV 6BQH ASP A 35 UNP P28335 EXPRESSION TAG SEQADV 6BQH ASP A 36 UNP P28335 EXPRESSION TAG SEQADV 6BQH GLY A 37 UNP P28335 EXPRESSION TAG SEQADV 6BQH ALA A 38 UNP P28335 EXPRESSION TAG SEQADV 6BQH PRO A 39 UNP P28335 EXPRESSION TAG SEQADV 6BQH TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6BQH ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6BQH LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 6BQH ASN A 360 UNP P28335 CYS 360 CONFLICT SEQADV 6BQH GLY A 394 UNP P28335 EXPRESSION TAG SEQADV 6BQH ARG A 395 UNP P28335 EXPRESSION TAG SEQADV 6BQH PRO A 396 UNP P28335 EXPRESSION TAG SEQADV 6BQH LEU A 397 UNP P28335 EXPRESSION TAG SEQADV 6BQH GLU A 398 UNP P28335 EXPRESSION TAG SEQADV 6BQH VAL A 399 UNP P28335 EXPRESSION TAG SEQADV 6BQH LEU A 400 UNP P28335 EXPRESSION TAG SEQADV 6BQH PHE A 401 UNP P28335 EXPRESSION TAG SEQADV 6BQH GLN A 402 UNP P28335 EXPRESSION TAG SEQADV 6BQH GLY A 403 UNP P28335 EXPRESSION TAG SEQADV 6BQH PRO A 404 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 405 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 406 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 407 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 408 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 409 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 410 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 411 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 412 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 413 UNP P28335 EXPRESSION TAG SEQADV 6BQH HIS A 414 UNP P28335 EXPRESSION TAG SEQRES 1 A 452 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 452 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO SEQRES 3 A 452 THR SER ASP GLY GLY ARG PHE LYS PHE PRO ASP GLY VAL SEQRES 4 A 452 GLN ASN TRP PRO ALA LEU SER ILE VAL ILE ILE ILE ILE SEQRES 5 A 452 MET THR ILE GLY GLY ASN ILE LEU VAL ILE MET ALA VAL SEQRES 6 A 452 SER MET GLU LYS LYS LEU HIS ASN ALA THR ASN TYR PHE SEQRES 7 A 452 LEU MET SER LEU ALA ILE ALA ASP MET LEU VAL GLY LEU SEQRES 8 A 452 LEU VAL MET PRO LEU SER LEU LEU ALA ILE LEU TYR ASP SEQRES 9 A 452 TYR VAL TRP PRO LEU PRO ARG TYR LEU CYS PRO VAL TRP SEQRES 10 A 452 ILE SER LEU ASP VAL LEU PHE SER THR ALA SER ILE MET SEQRES 11 A 452 HIS LEU CYS ALA ILE SER LEU ASP ARG TYR VAL ALA ILE SEQRES 12 A 452 ARG ASN PRO ILE GLU HIS SER ARG PHE ASN SER ARG THR SEQRES 13 A 452 LYS ALA ILE MET LYS ILE ALA ILE VAL TRP ALA ILE SER SEQRES 14 A 452 ILE GLY VAL SER VAL PRO ILE PRO VAL ILE GLY LEU ARG SEQRES 15 A 452 ASP GLU GLU LYS VAL PHE VAL ASN ASN THR THR CYS VAL SEQRES 16 A 452 LEU ASN ASP PRO ASN PHE VAL LEU ILE GLY SER PHE VAL SEQRES 17 A 452 ALA PHE PHE ILE PRO LEU THR ILE MET VAL ILE THR TYR SEQRES 18 A 452 CYS LEU THR ILE TYR VAL LEU ARG ARG GLN ALA ALA ASP SEQRES 19 A 452 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 20 A 452 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 21 A 452 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 22 A 452 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 23 A 452 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 24 A 452 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 25 A 452 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 26 A 452 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 27 A 452 GLN ALA ILE ASN ASN GLU ARG LYS ALA SER LYS VAL LEU SEQRES 28 A 452 GLY ILE VAL PHE PHE VAL PHE LEU ILE MET TRP CYS PRO SEQRES 29 A 452 PHE PHE ILE THR ASN ILE LEU SER VAL LEU CYS GLU LYS SEQRES 30 A 452 SER CYS ASN GLN LYS LEU MET GLU LYS LEU LEU ASN VAL SEQRES 31 A 452 PHE VAL TRP ILE GLY TYR VAL ASN SER GLY ILE ASN PRO SEQRES 32 A 452 LEU VAL TYR THR LEU PHE ASN LYS ILE TYR ARG ARG ALA SEQRES 33 A 452 PHE SER ASN TYR LEU ARG CYS ASN TYR LYS VAL GLU LYS SEQRES 34 A 452 LYS PRO GLY ARG PRO LEU GLU VAL LEU PHE GLN GLY PRO SEQRES 35 A 452 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HET E2J A1201 34 HET OLC A1202 19 HET OLC A1203 13 HET OLC A1204 15 HET OLC A1205 12 HET OLC A1206 14 HET OLC A1207 7 HET PEG A1208 7 HET OLA A1209 16 HET OLA A1210 17 HETNAM E2J 6-(2-{4-[BIS(4-FLUOROPHENYL)METHYLIDENE]PIPERIDIN-1- HETNAM 2 E2J YL}ETHYL)-7-METHYL-5H-[1,3]THIAZOLO[3,2-A]PYRIMIDIN-5- HETNAM 3 E2J ONE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM OLA OLEIC ACID HETSYN E2J RITANSERIN HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 E2J C27 H25 F2 N3 O S FORMUL 3 OLC 6(C21 H40 O4) FORMUL 9 PEG C4 H10 O3 FORMUL 10 OLA 2(C18 H34 O2) FORMUL 12 HOH *4(H2 O) HELIX 1 AA1 TRP A 55 SER A 59 5 5 HELIX 2 AA2 ILE A 60 GLU A 81 1 22 HELIX 3 AA3 LYS A 82 HIS A 85 5 4 HELIX 4 AA4 ASN A 86 VAL A 106 1 21 HELIX 5 AA5 VAL A 106 TYR A 116 1 11 HELIX 6 AA6 TYR A 125 ALA A 155 1 31 HELIX 7 AA7 ASN A 166 VAL A 187 1 22 HELIX 8 AA8 VAL A 187 ASP A 196 1 10 HELIX 9 AA9 GLU A 197 LYS A 199 5 3 HELIX 10 AB1 ASP A 211 PHE A 223 1 13 HELIX 11 AB2 PHE A 223 ILE A 1017 1 40 HELIX 12 AB3 LYS A 1027 GLN A 1041 1 15 HELIX 13 AB4 LYS A 1059 ILE A 1067 1 9 HELIX 14 AB5 LEU A 1094 TYR A 1101 1 8 HELIX 15 AB6 TYR A 1101 LEU A 336 1 42 HELIX 16 AB7 ASN A 342 ASN A 372 1 31 HELIX 17 AB8 ASN A 372 ASN A 386 1 15 SHEET 1 AA1 2 PHE A 201 VAL A 202 0 SHEET 2 AA1 2 THR A 206 CYS A 207 -1 O THR A 206 N VAL A 202 SSBOND 1 CYS A 127 CYS A 207 1555 1555 2.03 SSBOND 2 CYS A 337 CYS A 341 1555 1555 2.04 CISPEP 1 PHE A 48 PRO A 49 0 -0.74 CISPEP 2 LYS A 1019 ALA A 1020 0 -0.97 SITE 1 AC1 17 TRP A 130 ASP A 134 VAL A 135 SER A 138 SITE 2 AC1 17 THR A 139 ILE A 142 VAL A 215 GLY A 218 SITE 3 AC1 17 SER A 219 PHE A 223 PHE A 320 PHE A 327 SITE 4 AC1 17 PHE A 328 ASN A 351 VAL A 354 TYR A 358 SITE 5 AC1 17 HOH A1301 SITE 1 AC2 4 TRP A 55 LEU A 349 PHE A 353 OLC A1203 SITE 1 AC3 3 LEU A 333 MET A 346 OLC A1202 SITE 1 AC4 4 MET A 76 TYR A 382 ASN A 386 TYR A 387 SITE 1 AC5 3 THR A 228 ILE A 229 ILE A 232 SITE 1 AC6 2 CYS A 146 VAL A 221 SITE 1 AC7 4 LEU A 370 PHE A 371 ARG A 376 ARG A 377 SITE 1 AC8 5 TYR A 90 MET A 93 ILE A 97 ILE A 172 SITE 2 AC8 5 TRP A 179 CRYST1 88.310 97.050 150.230 90.00 90.00 90.00 C 2 2 2 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 0.011324 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010304 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006656 0.00000 ATOM 1 N PHE A 46 23.369 44.902 64.915 1.00163.97 N ANISOU 1 N PHE A 46 20683 20138 21480 -1193 804 -1354 N ATOM 2 CA PHE A 46 23.866 45.470 63.665 1.00170.96 C ANISOU 2 CA PHE A 46 21531 20940 22487 -1136 668 -1294 C ATOM 3 C PHE A 46 23.827 46.992 63.734 1.00171.61 C ANISOU 3 C PHE A 46 21558 20947 22699 -1094 659 -1405 C ATOM 4 O PHE A 46 22.827 47.612 63.361 1.00179.44 O ANISOU 4 O PHE A 46 22442 21875 23860 -1047 687 -1463 O ATOM 5 CB PHE A 46 23.040 44.969 62.474 1.00174.24 C ANISOU 5 CB PHE A 46 21858 21319 23026 -1108 636 -1231 C ATOM 6 CG PHE A 46 23.702 45.173 61.131 1.00166.26 C ANISOU 6 CG PHE A 46 20837 20258 22077 -1056 494 -1127 C ATOM 7 CD1 PHE A 46 23.809 46.441 60.575 1.00164.50 C ANISOU 7 CD1 PHE A 46 20560 19956 21985 -991 431 -1144 C ATOM 8 CD2 PHE A 46 24.196 44.092 60.414 1.00149.88 C ANISOU 8 CD2 PHE A 46 18806 18208 19932 -1070 433 -1011 C ATOM 9 CE1 PHE A 46 24.410 46.628 59.341 1.00158.66 C ANISOU 9 CE1 PHE A 46 19815 19179 21290 -945 312 -1034 C ATOM 10 CE2 PHE A 46 24.796 44.274 59.177 1.00137.41 C ANISOU 10 CE2 PHE A 46 17215 16600 18394 -1024 311 -922 C ATOM 11 CZ PHE A 46 24.903 45.543 58.641 1.00146.95 C ANISOU 11 CZ PHE A 46 18372 17744 19717 -963 251 -927 C ATOM 12 N LYS A 47 24.924 47.583 64.200 1.00172.19 N ANISOU 12 N LYS A 47 21696 21025 22701 -1110 621 -1437 N ATOM 13 CA LYS A 47 25.029 49.027 64.392 1.00171.47 C ANISOU 13 CA LYS A 47 21568 20848 22734 -1088 627 -1559 C ATOM 14 C LYS A 47 23.864 49.539 65.246 1.00172.19 C ANISOU 14 C LYS A 47 21595 20935 22893 -1086 761 -1723 C ATOM 15 O LYS A 47 22.905 50.142 64.762 1.00170.10 O ANISOU 15 O LYS A 47 21230 20581 22820 -1025 787 -1761 O ATOM 16 CB LYS A 47 25.092 49.754 63.045 1.00162.75 C ANISOU 16 CB LYS A 47 20405 19611 21823 -1017 535 -1480 C ATOM 17 CG LYS A 47 25.389 51.241 63.158 1.00163.61 C ANISOU 17 CG LYS A 47 20490 19598 22076 -997 541 -1582 C ATOM 18 CD LYS A 47 25.143 51.955 61.838 1.00171.39 C ANISOU 18 CD LYS A 47 21409 20445 23268 -909 476 -1486 C ATOM 19 CE LYS A 47 25.219 53.466 62.012 1.00180.88 C ANISOU 19 CE LYS A 47 22583 21491 24653 -882 514 -1592 C ATOM 20 NZ LYS A 47 24.848 54.203 60.770 1.00182.72 N ANISOU 20 NZ LYS A 47 22751 21581 25095 -778 465 -1480 N ATOM 21 N PHE A 48 23.982 49.260 66.546 1.00177.06 N ANISOU 21 N PHE A 48 22271 21667 23337 -1148 847 -1817 N ATOM 22 CA PHE A 48 22.963 49.691 67.501 1.00181.40 C ANISOU 22 CA PHE A 48 22769 22240 23915 -1158 991 -1989 C ATOM 23 C PHE A 48 22.679 51.193 67.486 1.00179.86 C ANISOU 23 C PHE A 48 22498 21912 23927 -1112 1017 -2143 C ATOM 24 O PHE A 48 21.495 51.565 67.580 1.00177.92 O ANISOU 24 O PHE A 48 22157 21624 23820 -1072 1111 -2235 O ATOM 25 CB PHE A 48 23.362 49.226 68.909 1.00181.98 C ANISOU 25 CB PHE A 48 22933 22477 23734 -1232 1067 -2058 C ATOM 26 CG PHE A 48 23.249 47.738 69.111 1.00175.53 C ANISOU 26 CG PHE A 48 22179 21774 22740 -1268 1097 -1918 C ATOM 27 CD1 PHE A 48 22.099 47.062 68.735 1.00173.01 C ANISOU 27 CD1 PHE A 48 21798 21436 22503 -1263 1168 -1869 C ATOM 28 CD2 PHE A 48 24.294 47.012 69.666 1.00171.88 C ANISOU 28 CD2 PHE A 48 21833 21433 22041 -1305 1056 -1835 C ATOM 29 CE1 PHE A 48 21.988 45.694 68.915 1.00170.96 C ANISOU 29 CE1 PHE A 48 21599 21254 22104 -1306 1211 -1743 C ATOM 30 CE2 PHE A 48 24.188 45.641 69.846 1.00163.71 C ANISOU 30 CE2 PHE A 48 20863 20477 20862 -1330 1095 -1692 C ATOM 31 CZ PHE A 48 23.034 44.983 69.470 1.00166.91 C ANISOU 31 CZ PHE A 48 21214 20839 21363 -1336 1180 -1647 C ATOM 32 N PRO A 49 23.671 52.102 67.380 1.00181.73 N ANISOU 32 N PRO A 49 22765 22073 24210 -1115 949 -2184 N ATOM 33 CA PRO A 49 25.127 51.948 67.277 1.00182.09 C ANISOU 33 CA PRO A 49 22899 22157 24129 -1159 839 -2111 C ATOM 34 C PRO A 49 25.835 51.854 68.627 1.00185.98 C ANISOU 34 C PRO A 49 23465 22805 24394 -1239 875 -2235 C ATOM 35 O PRO A 49 27.054 51.699 68.653 1.00181.96 O ANISOU 35 O PRO A 49 23016 22355 23765 -1276 784 -2189 O ATOM 36 CB PRO A 49 25.549 53.217 66.540 1.00180.91 C ANISOU 36 CB PRO A 49 22712 21824 24201 -1122 785 -2134 C ATOM 37 CG PRO A 49 24.581 54.237 67.016 1.00181.23 C ANISOU 37 CG PRO A 49 22679 21768 24413 -1089 901 -2318 C ATOM 38 CD PRO A 49 23.269 53.511 67.205 1.00182.62 C ANISOU 38 CD PRO A 49 22801 22016 24569 -1060 986 -2311 C ATOM 39 N ASP A 50 25.082 51.939 69.722 1.00187.72 N ANISOU 39 N ASP A 50 23673 23106 24547 -1263 1006 -2392 N ATOM 40 CA ASP A 50 25.683 51.979 71.050 1.00179.85 C ANISOU 40 CA ASP A 50 22738 22275 23324 -1335 1044 -2533 C ATOM 41 C ASP A 50 26.465 50.701 71.338 1.00164.78 C ANISOU 41 C ASP A 50 20924 20545 21139 -1365 981 -2374 C ATOM 42 O ASP A 50 25.959 49.589 71.155 1.00167.93 O ANISOU 42 O ASP A 50 21347 20990 21470 -1351 1007 -2222 O ATOM 43 CB ASP A 50 24.601 52.191 72.108 1.00185.48 C ANISOU 43 CB ASP A 50 23417 23055 24003 -1349 1211 -2714 C ATOM 44 CG ASP A 50 24.140 53.636 72.191 1.00190.26 C ANISOU 44 CG ASP A 50 23940 23507 24843 -1328 1279 -2934 C ATOM 45 OD1 ASP A 50 24.454 54.417 71.266 1.00187.54 O ANISOU 45 OD1 ASP A 50 23560 22975 24723 -1289 1205 -2908 O ATOM 46 OD2 ASP A 50 23.462 53.990 73.179 1.00190.55 O ANISOU 46 OD2 ASP A 50 23951 23607 24843 -1347 1416 -3129 O ATOM 47 N GLY A 51 27.706 50.870 71.798 1.00137.97 N ANISOU 47 N GLY A 51 17578 17251 17595 -1407 901 -2414 N ATOM 48 CA GLY A 51 28.589 49.770 72.120 1.00119.53 C ANISOU 48 CA GLY A 51 15327 15090 14998 -1420 829 -2270 C ATOM 49 C GLY A 51 29.799 49.654 71.219 1.00105.66 C ANISOU 49 C GLY A 51 13582 13290 13272 -1408 673 -2137 C ATOM 50 O GLY A 51 30.759 48.958 71.581 1.00115.68 O ANISOU 50 O GLY A 51 14910 14715 14330 -1416 599 -2053 O ATOM 51 N VAL A 52 29.783 50.318 70.059 1.00 92.38 N ANISOU 51 N VAL A 52 11844 11411 11845 -1383 626 -2111 N ATOM 52 CA VAL A 52 30.866 50.192 69.089 1.00 87.79 C ANISOU 52 CA VAL A 52 11269 10782 11304 -1371 492 -1974 C ATOM 53 C VAL A 52 32.156 50.755 69.668 1.00 91.95 C ANISOU 53 C VAL A 52 11799 11406 11731 -1429 423 -2089 C ATOM 54 O VAL A 52 32.167 51.824 70.293 1.00 96.15 O ANISOU 54 O VAL A 52 12297 11921 12314 -1478 467 -2305 O ATOM 55 CB VAL A 52 30.490 50.899 67.776 1.00 93.51 C ANISOU 55 CB VAL A 52 11932 11282 12316 -1331 472 -1927 C ATOM 56 CG1 VAL A 52 30.016 52.296 68.068 1.00116.27 C ANISOU 56 CG1 VAL A 52 14757 14040 15381 -1346 547 -2130 C ATOM 57 CG2 VAL A 52 31.674 50.929 66.819 1.00105.52 C ANISOU 57 CG2 VAL A 52 13455 12760 13877 -1330 348 -1807 C ATOM 58 N GLN A 53 33.257 50.028 69.467 1.00 83.41 N ANISOU 58 N GLN A 53 10751 10429 10511 -1425 315 -1957 N ATOM 59 CA GLN A 53 34.541 50.380 70.053 1.00 79.88 C ANISOU 59 CA GLN A 53 10295 10116 9938 -1478 235 -2055 C ATOM 60 C GLN A 53 35.618 50.730 69.033 1.00 81.91 C ANISOU 60 C GLN A 53 10514 10287 10322 -1488 129 -1989 C ATOM 61 O GLN A 53 36.724 51.114 69.439 1.00 83.47 O ANISOU 61 O GLN A 53 10683 10588 10444 -1542 61 -2086 O ATOM 62 CB GLN A 53 35.047 49.235 70.943 1.00 80.69 C ANISOU 62 CB GLN A 53 10460 10470 9728 -1460 198 -1975 C ATOM 63 CG GLN A 53 35.033 49.547 72.429 1.00 98.57 C ANISOU 63 CG GLN A 53 12734 12930 11789 -1506 245 -2170 C ATOM 64 CD GLN A 53 36.132 48.817 73.192 1.00124.93 C ANISOU 64 CD GLN A 53 16103 16533 14830 -1496 150 -2116 C ATOM 65 OE1 GLN A 53 36.006 47.632 73.505 1.00133.25 O ANISOU 65 OE1 GLN A 53 17229 17702 15699 -1436 157 -1942 O ATOM 66 NE2 GLN A 53 37.217 49.526 73.494 1.00131.65 N ANISOU 66 NE2 GLN A 53 16896 17482 15643 -1552 62 -2265 N ATOM 67 N ASN A 54 35.343 50.611 67.730 1.00 79.50 N ANISOU 67 N ASN A 54 10199 9811 10196 -1442 114 -1833 N ATOM 68 CA ASN A 54 36.362 50.887 66.712 1.00 75.63 C ANISOU 68 CA ASN A 54 9676 9247 9814 -1452 25 -1752 C ATOM 69 C ASN A 54 35.659 51.521 65.507 1.00 81.18 C ANISOU 69 C ASN A 54 10350 9713 10783 -1421 59 -1690 C ATOM 70 O ASN A 54 35.284 50.835 64.551 1.00 73.55 O ANISOU 70 O ASN A 54 9398 8694 9854 -1358 40 -1513 O ATOM 71 CB ASN A 54 37.117 49.623 66.332 1.00 74.48 C ANISOU 71 CB ASN A 54 9564 9221 9515 -1406 -63 -1560 C ATOM 72 CG ASN A 54 38.244 49.886 65.346 1.00 78.08 C ANISOU 72 CG ASN A 54 9976 9627 10062 -1420 -149 -1488 C ATOM 73 OD1 ASN A 54 38.578 51.033 65.056 1.00 85.44 O ANISOU 73 OD1 ASN A 54 10857 10449 11156 -1477 -143 -1586 O ATOM 74 ND2 ASN A 54 38.843 48.814 64.831 1.00 87.75 N ANISOU 74 ND2 ASN A 54 11223 10927 11191 -1370 -217 -1317 N ATOM 75 N TRP A 55 35.504 52.845 65.563 1.00 86.68 N ANISOU 75 N TRP A 55 11003 10268 11663 -1463 110 -1841 N ATOM 76 CA TRP A 55 34.816 53.598 64.518 1.00 98.46 C ANISOU 76 CA TRP A 55 12466 11531 13415 -1422 149 -1786 C ATOM 77 C TRP A 55 35.651 53.782 63.250 1.00 98.68 C ANISOU 77 C TRP A 55 12477 11467 13550 -1418 79 -1636 C ATOM 78 O TRP A 55 35.093 53.703 62.149 1.00 97.93 O ANISOU 78 O TRP A 55 12378 11261 13570 -1348 76 -1483 O ATOM 79 CB TRP A 55 34.369 54.962 65.051 1.00 95.75 C ANISOU 79 CB TRP A 55 12087 11047 13247 -1459 240 -1996 C ATOM 80 CG TRP A 55 32.983 54.948 65.625 1.00 96.50 C ANISOU 80 CG TRP A 55 12180 11127 13358 -1414 337 -2077 C ATOM 81 CD1 TRP A 55 32.620 55.250 66.907 1.00 89.97 C ANISOU 81 CD1 TRP A 55 11352 10377 12457 -1456 415 -2293 C ATOM 82 CD2 TRP A 55 31.774 54.599 64.937 1.00 97.27 C ANISOU 82 CD2 TRP A 55 12266 11145 13547 -1320 368 -1952 C ATOM 83 NE1 TRP A 55 31.259 55.120 67.056 1.00 88.86 N ANISOU 83 NE1 TRP A 55 11199 10199 12364 -1394 501 -2306 N ATOM 84 CE2 TRP A 55 30.717 54.723 65.862 1.00 85.19 C ANISOU 84 CE2 TRP A 55 10723 9639 12006 -1312 471 -2100 C ATOM 85 CE3 TRP A 55 31.482 54.202 63.629 1.00106.53 C ANISOU 85 CE3 TRP A 55 13430 12244 14803 -1246 318 -1740 C ATOM 86 CZ2 TRP A 55 29.392 54.460 65.520 1.00 96.57 C ANISOU 86 CZ2 TRP A 55 12132 11028 13530 -1232 524 -2043 C ATOM 87 CZ3 TRP A 55 30.164 53.939 63.292 1.00112.44 C ANISOU 87 CZ3 TRP A 55 14148 12950 15623 -1167 361 -1688 C ATOM 88 CH2 TRP A 55 29.137 54.068 64.235 1.00111.29 C ANISOU 88 CH2 TRP A 55 13981 12826 15478 -1162 463 -1838 C ATOM 89 N PRO A 56 36.962 54.043 63.332 1.00 93.34 N ANISOU 89 N PRO A 56 11783 10842 12839 -1491 26 -1675 N ATOM 90 CA PRO A 56 37.751 54.118 62.090 1.00 89.48 C ANISOU 90 CA PRO A 56 11277 10282 12439 -1487 -29 -1518 C ATOM 91 C PRO A 56 37.755 52.826 61.293 1.00 81.66 C ANISOU 91 C PRO A 56 10317 9380 11330 -1412 -93 -1305 C ATOM 92 O PRO A 56 38.055 52.859 60.094 1.00 73.63 O ANISOU 92 O PRO A 56 9290 8288 10397 -1387 -122 -1158 O ATOM 93 CB PRO A 56 39.160 54.479 62.583 1.00103.49 C ANISOU 93 CB PRO A 56 13015 12145 14161 -1590 -72 -1632 C ATOM 94 CG PRO A 56 39.166 54.141 64.032 1.00109.26 C ANISOU 94 CG PRO A 56 13755 13062 14696 -1622 -74 -1799 C ATOM 95 CD PRO A 56 37.779 54.440 64.493 1.00105.23 C ANISOU 95 CD PRO A 56 13268 12466 14247 -1586 19 -1880 C ATOM 96 N ALA A 57 37.427 51.689 61.910 1.00 97.48 N ANISOU 96 N ALA A 57 12359 11536 13141 -1378 -107 -1286 N ATOM 97 CA ALA A 57 37.297 50.451 61.151 1.00 81.33 C ANISOU 97 CA ALA A 57 10344 9546 11010 -1308 -151 -1101 C ATOM 98 C ALA A 57 36.151 50.520 60.156 1.00 81.00 C ANISOU 98 C ALA A 57 10297 9370 11108 -1242 -118 -1004 C ATOM 99 O ALA A 57 36.165 49.786 59.161 1.00 95.50 O ANISOU 99 O ALA A 57 12143 11217 12927 -1194 -159 -852 O ATOM 100 CB ALA A 57 37.107 49.263 62.099 1.00 70.65 C ANISOU 100 CB ALA A 57 9040 8359 9444 -1288 -151 -1102 C ATOM 101 N LEU A 58 35.175 51.404 60.395 1.00 78.65 N ANISOU 101 N LEU A 58 9979 8954 10950 -1236 -48 -1096 N ATOM 102 CA LEU A 58 34.073 51.574 59.457 1.00 92.82 C ANISOU 102 CA LEU A 58 11751 10632 12885 -1162 -26 -1007 C ATOM 103 C LEU A 58 34.570 51.949 58.067 1.00100.00 C ANISOU 103 C LEU A 58 12642 11455 13899 -1136 -74 -861 C ATOM 104 O LEU A 58 33.851 51.746 57.081 1.00 99.98 O ANISOU 104 O LEU A 58 12622 11412 13952 -1064 -88 -743 O ATOM 105 CB LEU A 58 33.100 52.631 59.982 1.00 82.30 C ANISOU 105 CB LEU A 58 10387 9177 11706 -1154 59 -1141 C ATOM 106 CG LEU A 58 31.775 52.780 59.236 1.00 85.71 C ANISOU 106 CG LEU A 58 10779 9513 12274 -1063 84 -1072 C ATOM 107 CD1 LEU A 58 31.018 51.464 59.235 1.00 89.81 C ANISOU 107 CD1 LEU A 58 11305 10153 12665 -1031 77 -1018 C ATOM 108 CD2 LEU A 58 30.946 53.883 59.872 1.00 89.19 C ANISOU 108 CD2 LEU A 58 11183 9831 12875 -1051 175 -1222 C ATOM 109 N SER A 59 35.795 52.471 57.965 1.00 94.48 N ANISOU 109 N SER A 59 11939 10741 13218 -1196 -98 -867 N ATOM 110 CA SER A 59 36.337 52.861 56.669 1.00 87.80 C ANISOU 110 CA SER A 59 11078 9817 12464 -1180 -127 -722 C ATOM 111 C SER A 59 36.597 51.676 55.748 1.00 91.27 C ANISOU 111 C SER A 59 11532 10369 12776 -1136 -194 -566 C ATOM 112 O SER A 59 36.879 51.891 54.564 1.00100.63 O ANISOU 112 O SER A 59 12707 11511 14018 -1110 -216 -432 O ATOM 113 CB SER A 59 37.629 53.653 56.851 1.00 87.63 C ANISOU 113 CB SER A 59 11041 9762 12493 -1272 -124 -781 C ATOM 114 OG SER A 59 38.579 52.920 57.600 1.00 91.54 O ANISOU 114 OG SER A 59 11542 10427 12813 -1328 -170 -847 O ATOM 115 N ILE A 60 36.525 50.443 56.258 1.00 90.63 N ANISOU 115 N ILE A 60 11479 10429 12529 -1128 -219 -579 N ATOM 116 CA ILE A 60 36.611 49.246 55.425 1.00 86.02 C ANISOU 116 CA ILE A 60 10910 9935 11841 -1082 -268 -451 C ATOM 117 C ILE A 60 35.405 49.096 54.506 1.00 85.57 C ANISOU 117 C ILE A 60 10836 9831 11846 -1010 -265 -371 C ATOM 118 O ILE A 60 35.427 48.270 53.586 1.00 83.15 O ANISOU 118 O ILE A 60 10532 9585 11478 -973 -306 -271 O ATOM 119 CB ILE A 60 36.794 48.018 56.346 1.00 82.41 C ANISOU 119 CB ILE A 60 10492 9612 11210 -1091 -278 -492 C ATOM 120 CG1 ILE A 60 38.054 48.184 57.198 1.00 83.77 C ANISOU 120 CG1 ILE A 60 10665 9859 11303 -1151 -299 -564 C ATOM 121 CG2 ILE A 60 36.902 46.717 55.564 1.00 70.68 C ANISOU 121 CG2 ILE A 60 9026 8200 9630 -1047 -316 -378 C ATOM 122 CD1 ILE A 60 38.447 46.935 57.956 1.00 85.86 C ANISOU 122 CD1 ILE A 60 10969 10268 11385 -1140 -322 -560 C ATOM 123 N VAL A 61 34.356 49.895 54.719 1.00 92.82 N ANISOU 123 N VAL A 61 11728 10651 12890 -985 -220 -424 N ATOM 124 CA VAL A 61 33.201 49.873 53.826 1.00 96.70 C ANISOU 124 CA VAL A 61 12182 11109 13449 -907 -228 -350 C ATOM 125 C VAL A 61 33.621 50.135 52.385 1.00 99.01 C ANISOU 125 C VAL A 61 12460 11387 13773 -867 -277 -197 C ATOM 126 O VAL A 61 33.028 49.586 51.447 1.00101.68 O ANISOU 126 O VAL A 61 12775 11778 14080 -809 -315 -115 O ATOM 127 CB VAL A 61 32.145 50.888 54.308 1.00 96.34 C ANISOU 127 CB VAL A 61 12099 10948 13557 -877 -169 -432 C ATOM 128 CG1 VAL A 61 31.098 51.134 53.236 1.00 97.69 C ANISOU 128 CG1 VAL A 61 12214 11082 13823 -782 -190 -336 C ATOM 129 CG2 VAL A 61 31.481 50.383 55.577 1.00105.41 C ANISOU 129 CG2 VAL A 61 13255 12148 14647 -906 -115 -572 C ATOM 130 N ILE A 62 34.660 50.951 52.182 1.00 92.25 N ANISOU 130 N ILE A 62 11614 10467 12969 -904 -273 -162 N ATOM 131 CA ILE A 62 35.149 51.211 50.829 1.00 94.59 C ANISOU 131 CA ILE A 62 11902 10756 13280 -873 -305 -5 C ATOM 132 C ILE A 62 35.617 49.919 50.169 1.00 94.19 C ANISOU 132 C ILE A 62 11864 10857 13065 -868 -360 58 C ATOM 133 O ILE A 62 35.323 49.662 48.995 1.00 82.60 O ANISOU 133 O ILE A 62 10379 9437 11567 -811 -397 170 O ATOM 134 CB ILE A 62 36.267 52.270 50.858 1.00 92.20 C ANISOU 134 CB ILE A 62 11607 10357 13068 -936 -272 7 C ATOM 135 CG1 ILE A 62 35.746 53.566 51.484 1.00 97.11 C ANISOU 135 CG1 ILE A 62 12218 10804 13876 -940 -206 -70 C ATOM 136 CG2 ILE A 62 36.795 52.523 49.455 1.00 81.24 C ANISOU 136 CG2 ILE A 62 10216 8968 11685 -908 -291 184 C ATOM 137 CD1 ILE A 62 36.813 54.617 51.706 1.00107.75 C ANISOU 137 CD1 ILE A 62 13570 12038 15334 -1025 -158 -100 C ATOM 138 N ILE A 63 36.353 49.089 50.911 1.00 94.64 N ANISOU 138 N ILE A 63 11950 10998 13013 -923 -366 -14 N ATOM 139 CA ILE A 63 36.747 47.778 50.403 1.00 73.85 C ANISOU 139 CA ILE A 63 9330 8492 10238 -911 -406 30 C ATOM 140 C ILE A 63 35.520 46.971 50.002 1.00 76.53 C ANISOU 140 C ILE A 63 9658 8874 10546 -857 -421 35 C ATOM 141 O ILE A 63 35.497 46.337 48.941 1.00 74.21 O ANISOU 141 O ILE A 63 9353 8652 10190 -823 -456 105 O ATOM 142 CB ILE A 63 37.596 47.040 51.455 1.00 82.33 C ANISOU 142 CB ILE A 63 10435 9635 11212 -960 -405 -49 C ATOM 143 CG1 ILE A 63 38.924 47.773 51.672 1.00105.01 C ANISOU 143 CG1 ILE A 63 13296 12496 14107 -1018 -404 -57 C ATOM 144 CG2 ILE A 63 37.828 45.594 51.047 1.00 83.84 C ANISOU 144 CG2 ILE A 63 10646 9932 11278 -935 -433 -13 C ATOM 145 CD1 ILE A 63 39.803 47.165 52.750 1.00116.97 C ANISOU 145 CD1 ILE A 63 14824 14099 15518 -1057 -417 -135 C ATOM 146 N ILE A 64 34.473 47.009 50.829 1.00 71.94 N ANISOU 146 N ILE A 64 9069 8255 10008 -853 -389 -52 N ATOM 147 CA ILE A 64 33.269 46.228 50.566 1.00 73.84 C ANISOU 147 CA ILE A 64 9285 8539 10232 -817 -394 -70 C ATOM 148 C ILE A 64 32.568 46.726 49.308 1.00 73.18 C ANISOU 148 C ILE A 64 9144 8455 10206 -749 -432 15 C ATOM 149 O ILE A 64 32.139 45.930 48.465 1.00 73.94 O ANISOU 149 O ILE A 64 9214 8638 10242 -721 -470 41 O ATOM 150 CB ILE A 64 32.338 46.273 51.792 1.00 86.60 C ANISOU 150 CB ILE A 64 10897 10117 11891 -834 -336 -184 C ATOM 151 CG1 ILE A 64 33.048 45.697 53.023 1.00 78.62 C ANISOU 151 CG1 ILE A 64 9947 9135 10788 -893 -303 -252 C ATOM 152 CG2 ILE A 64 31.038 45.525 51.510 1.00 78.58 C ANISOU 152 CG2 ILE A 64 9837 9143 10877 -808 -332 -211 C ATOM 153 CD1 ILE A 64 32.248 45.810 54.308 1.00 67.93 C ANISOU 153 CD1 ILE A 64 8597 7757 9454 -917 -236 -363 C ATOM 154 N ILE A 65 32.453 48.048 49.160 1.00 75.13 N ANISOU 154 N ILE A 65 9369 8606 10570 -717 -424 59 N ATOM 155 CA ILE A 65 31.759 48.635 48.016 1.00 77.61 C ANISOU 155 CA ILE A 65 9629 8918 10941 -633 -462 162 C ATOM 156 C ILE A 65 32.461 48.273 46.713 1.00 80.58 C ANISOU 156 C ILE A 65 10013 9390 11215 -616 -514 282 C ATOM 157 O ILE A 65 31.813 47.949 45.709 1.00 72.05 O ANISOU 157 O ILE A 65 8886 8402 10088 -556 -566 336 O ATOM 158 CB ILE A 65 31.658 50.162 48.196 1.00 86.98 C ANISOU 158 CB ILE A 65 10806 9953 12289 -601 -426 198 C ATOM 159 CG1 ILE A 65 30.743 50.510 49.373 1.00 92.28 C ANISOU 159 CG1 ILE A 65 11455 10544 13064 -602 -371 65 C ATOM 160 CG2 ILE A 65 31.188 50.837 46.911 1.00 75.89 C ANISOU 160 CG2 ILE A 65 9358 8545 10932 -500 -468 351 C ATOM 161 CD1 ILE A 65 30.719 51.991 49.696 1.00 98.78 C ANISOU 161 CD1 ILE A 65 12274 11195 14063 -579 -320 69 C ATOM 162 N MET A 66 33.793 48.330 46.702 1.00 85.17 N ANISOU 162 N MET A 66 10642 9965 11755 -668 -501 317 N ATOM 163 CA MET A 66 34.535 48.038 45.485 1.00 91.53 C ANISOU 163 CA MET A 66 11452 10863 12462 -656 -536 427 C ATOM 164 C MET A 66 34.573 46.551 45.165 1.00 86.70 C ANISOU 164 C MET A 66 10842 10388 11710 -667 -567 376 C ATOM 165 O MET A 66 34.766 46.188 43.998 1.00 78.23 O ANISOU 165 O MET A 66 9757 9421 10548 -638 -603 446 O ATOM 166 CB MET A 66 35.956 48.586 45.595 1.00100.61 C ANISOU 166 CB MET A 66 12638 11964 13626 -714 -502 470 C ATOM 167 CG MET A 66 36.010 50.089 45.755 1.00 93.98 C ANISOU 167 CG MET A 66 11797 10970 12941 -713 -460 525 C ATOM 168 SD MET A 66 37.698 50.709 45.706 1.00 94.82 S ANISOU 168 SD MET A 66 11927 11029 13069 -798 -414 573 S ATOM 169 CE MET A 66 37.381 52.469 45.793 1.00115.61 C ANISOU 169 CE MET A 66 14559 13450 15919 -785 -353 636 C ATOM 170 N THR A 67 34.391 45.690 46.169 1.00 84.09 N ANISOU 170 N THR A 67 10532 10058 11361 -709 -546 255 N ATOM 171 CA THR A 67 34.335 44.254 45.916 1.00 79.35 C ANISOU 171 CA THR A 67 9938 9557 10656 -720 -560 202 C ATOM 172 C THR A 67 33.002 43.851 45.298 1.00 85.89 C ANISOU 172 C THR A 67 10707 10447 11480 -680 -592 173 C ATOM 173 O THR A 67 32.956 42.972 44.428 1.00 91.79 O ANISOU 173 O THR A 67 11438 11298 12140 -674 -622 163 O ATOM 174 CB THR A 67 34.581 43.482 47.213 1.00 88.67 C ANISOU 174 CB THR A 67 11164 10704 11821 -771 -517 105 C ATOM 175 OG1 THR A 67 35.961 43.596 47.584 1.00 63.80 O ANISOU 175 OG1 THR A 67 8054 7546 8640 -802 -506 129 O ATOM 176 CG2 THR A 67 34.213 42.009 47.053 1.00 63.75 C ANISOU 176 CG2 THR A 67 8015 7611 8596 -780 -513 44 C ATOM 177 N ILE A 68 31.910 44.489 45.721 1.00 83.07 N ANISOU 177 N ILE A 68 10308 10035 11220 -655 -586 147 N ATOM 178 CA ILE A 68 30.603 44.177 45.152 1.00 90.07 C ANISOU 178 CA ILE A 68 11116 10995 12112 -616 -622 112 C ATOM 179 C ILE A 68 30.478 44.762 43.751 1.00100.52 C ANISOU 179 C ILE A 68 12390 12403 13400 -539 -692 228 C ATOM 180 O ILE A 68 30.146 44.055 42.793 1.00106.65 O ANISOU 180 O ILE A 68 13122 13314 14086 -523 -742 214 O ATOM 181 CB ILE A 68 29.478 44.677 46.074 1.00 89.79 C ANISOU 181 CB ILE A 68 11037 10882 12196 -606 -588 43 C ATOM 182 CG1 ILE A 68 29.577 43.999 47.440 1.00 87.14 C ANISOU 182 CG1 ILE A 68 10755 10489 11865 -682 -513 -66 C ATOM 183 CG2 ILE A 68 28.117 44.418 45.445 1.00 81.99 C ANISOU 183 CG2 ILE A 68 9944 9985 11223 -561 -632 4 C ATOM 184 CD1 ILE A 68 28.465 44.376 48.389 1.00 88.69 C ANISOU 184 CD1 ILE A 68 10908 10625 12164 -682 -464 -150 C ATOM 185 N GLY A 69 30.752 46.061 43.611 1.00102.15 N ANISOU 185 N GLY A 69 12604 12534 13675 -492 -692 343 N ATOM 186 CA GLY A 69 30.584 46.710 42.320 1.00 89.38 C ANISOU 186 CA GLY A 69 10946 10991 12025 -406 -751 483 C ATOM 187 C GLY A 69 31.514 46.165 41.252 1.00 82.82 C ANISOU 187 C GLY A 69 10141 10284 11041 -418 -778 546 C ATOM 188 O GLY A 69 31.133 46.051 40.084 1.00 92.11 O ANISOU 188 O GLY A 69 11270 11605 12123 -359 -842 605 O ATOM 189 N GLY A 70 32.747 45.826 41.634 1.00 86.46 N ANISOU 189 N GLY A 70 10674 10707 11472 -490 -731 531 N ATOM 190 CA GLY A 70 33.685 45.285 40.662 1.00 67.86 C ANISOU 190 CA GLY A 70 8339 8468 8978 -502 -744 578 C ATOM 191 C GLY A 70 33.217 43.968 40.072 1.00 92.42 C ANISOU 191 C GLY A 70 11414 11729 11973 -507 -783 475 C ATOM 192 O GLY A 70 33.228 43.779 38.853 1.00 94.43 O ANISOU 192 O GLY A 70 11640 12132 12109 -471 -828 522 O ATOM 193 N ASN A 71 32.785 43.042 40.934 1.00 91.78 N ANISOU 193 N ASN A 71 11335 11611 11926 -557 -760 328 N ATOM 194 CA ASN A 71 32.302 41.754 40.448 1.00 79.81 C ANISOU 194 CA ASN A 71 9785 10209 10329 -577 -782 209 C ATOM 195 C ASN A 71 30.942 41.873 39.775 1.00 76.56 C ANISOU 195 C ASN A 71 9276 9906 9909 -527 -850 186 C ATOM 196 O ASN A 71 30.624 41.072 38.889 1.00 86.35 O ANISOU 196 O ASN A 71 10468 11292 11049 -530 -891 115 O ATOM 197 CB ASN A 71 32.238 40.745 41.590 1.00 77.94 C ANISOU 197 CB ASN A 71 9585 9883 10145 -647 -722 76 C ATOM 198 CG ASN A 71 33.605 40.235 41.984 1.00 83.43 C ANISOU 198 CG ASN A 71 10361 10532 10808 -684 -673 81 C ATOM 199 OD1 ASN A 71 34.219 39.455 41.257 1.00 96.83 O ANISOU 199 OD1 ASN A 71 12068 12308 12416 -690 -674 59 O ATOM 200 ND2 ASN A 71 34.091 40.670 43.142 1.00 77.58 N ANISOU 200 ND2 ASN A 71 9670 9672 10137 -706 -631 102 N ATOM 201 N ILE A 72 30.124 42.845 40.184 1.00 72.59 N ANISOU 201 N ILE A 72 8732 9339 9509 -480 -864 232 N ATOM 202 CA ILE A 72 28.876 43.114 39.471 1.00 82.16 C ANISOU 202 CA ILE A 72 9835 10670 10712 -410 -941 234 C ATOM 203 C ILE A 72 29.166 43.428 38.009 1.00 89.95 C ANISOU 203 C ILE A 72 10798 11822 11556 -340 -1012 354 C ATOM 204 O ILE A 72 28.497 42.925 37.099 1.00 88.73 O ANISOU 204 O ILE A 72 10562 11851 11301 -315 -1085 301 O ATOM 205 CB ILE A 72 28.101 44.259 40.147 1.00 84.88 C ANISOU 205 CB ILE A 72 10144 10901 11206 -351 -935 286 C ATOM 206 CG1 ILE A 72 27.367 43.754 41.390 1.00 69.75 C ANISOU 206 CG1 ILE A 72 8209 8893 9400 -414 -879 131 C ATOM 207 CG2 ILE A 72 27.128 44.903 39.167 1.00 72.03 C ANISOU 207 CG2 ILE A 72 8410 9403 9557 -237 -1028 367 C ATOM 208 CD1 ILE A 72 26.588 44.831 42.115 1.00 85.63 C ANISOU 208 CD1 ILE A 72 10180 10794 11562 -359 -860 156 C ATOM 209 N LEU A 73 30.182 44.262 37.767 1.00 89.33 N ANISOU 209 N LEU A 73 10790 11690 11463 -314 -989 515 N ATOM 210 CA LEU A 73 30.546 44.608 36.397 1.00 84.40 C ANISOU 210 CA LEU A 73 10155 11221 10691 -250 -1040 654 C ATOM 211 C LEU A 73 30.975 43.375 35.611 1.00 85.69 C ANISOU 211 C LEU A 73 10316 11554 10687 -299 -1054 550 C ATOM 212 O LEU A 73 30.661 43.248 34.421 1.00 81.40 O ANISOU 212 O LEU A 73 9717 11217 9994 -247 -1125 576 O ATOM 213 CB LEU A 73 31.652 45.662 36.401 1.00 78.08 C ANISOU 213 CB LEU A 73 9436 10305 9925 -238 -984 834 C ATOM 214 CG LEU A 73 31.294 47.011 37.034 1.00 82.98 C ANISOU 214 CG LEU A 73 10062 10746 10719 -185 -961 946 C ATOM 215 CD1 LEU A 73 32.533 47.880 37.188 1.00 74.05 C ANISOU 215 CD1 LEU A 73 9016 9476 9643 -213 -884 1080 C ATOM 216 CD2 LEU A 73 30.235 47.732 36.217 1.00 74.46 C ANISOU 216 CD2 LEU A 73 8906 9762 9625 -54 -1040 1068 C ATOM 217 N VAL A 74 31.684 42.449 36.262 1.00 70.85 N ANISOU 217 N VAL A 74 8494 9597 8827 -392 -988 428 N ATOM 218 CA VAL A 74 32.049 41.196 35.608 1.00 74.81 C ANISOU 218 CA VAL A 74 8993 10231 9199 -438 -988 303 C ATOM 219 C VAL A 74 30.801 40.403 35.240 1.00 84.43 C ANISOU 219 C VAL A 74 10115 11580 10383 -444 -1049 145 C ATOM 220 O VAL A 74 30.701 39.852 34.138 1.00100.85 O ANISOU 220 O VAL A 74 12148 13856 12313 -437 -1097 86 O ATOM 221 CB VAL A 74 32.993 40.377 36.506 1.00 75.49 C ANISOU 221 CB VAL A 74 9158 10182 9342 -520 -900 213 C ATOM 222 CG1 VAL A 74 33.245 39.007 35.896 1.00 91.72 C ANISOU 222 CG1 VAL A 74 11207 12347 11295 -563 -890 63 C ATOM 223 CG2 VAL A 74 34.297 41.116 36.707 1.00 80.56 C ANISOU 223 CG2 VAL A 74 9872 10738 9998 -519 -850 353 C ATOM 224 N ILE A 75 29.835 40.327 36.158 1.00 93.36 N ANISOU 224 N ILE A 75 11208 12614 11650 -465 -1043 60 N ATOM 225 CA ILE A 75 28.582 39.636 35.870 1.00 97.79 C ANISOU 225 CA ILE A 75 11660 13295 12202 -482 -1096 -99 C ATOM 226 C ILE A 75 27.876 40.289 34.692 1.00105.24 C ANISOU 226 C ILE A 75 12502 14453 13032 -384 -1211 -20 C ATOM 227 O ILE A 75 27.361 39.605 33.800 1.00105.74 O ANISOU 227 O ILE A 75 12480 14718 12978 -392 -1274 -139 O ATOM 228 CB ILE A 75 27.687 39.611 37.123 1.00 83.53 C ANISOU 228 CB ILE A 75 9827 11338 10571 -518 -1056 -180 C ATOM 229 CG1 ILE A 75 28.413 38.927 38.283 1.00 76.56 C ANISOU 229 CG1 ILE A 75 9051 10263 9775 -607 -945 -241 C ATOM 230 CG2 ILE A 75 26.371 38.906 36.827 1.00 73.96 C ANISOU 230 CG2 ILE A 75 8484 10252 9364 -547 -1104 -353 C ATOM 231 CD1 ILE A 75 27.695 39.038 39.610 1.00 84.58 C ANISOU 231 CD1 ILE A 75 10062 11126 10948 -640 -889 -290 C ATOM 232 N MET A 76 27.851 41.625 34.665 1.00105.27 N ANISOU 232 N MET A 76 12511 14418 13067 -286 -1238 180 N ATOM 233 CA MET A 76 27.245 42.340 33.546 1.00 89.34 C ANISOU 233 CA MET A 76 10406 12601 10937 -169 -1347 299 C ATOM 234 C MET A 76 27.981 42.062 32.243 1.00 96.43 C ANISOU 234 C MET A 76 11324 13704 11612 -154 -1380 346 C ATOM 235 O MET A 76 27.353 41.877 31.193 1.00 98.82 O ANISOU 235 O MET A 76 11529 14256 11760 -104 -1479 317 O ATOM 236 CB MET A 76 27.237 43.839 33.829 1.00 77.33 C ANISOU 236 CB MET A 76 8912 10953 9517 -66 -1344 525 C ATOM 237 CG MET A 76 26.318 44.269 34.948 1.00 79.59 C ANISOU 237 CG MET A 76 9154 11079 10009 -54 -1326 482 C ATOM 238 SD MET A 76 26.479 46.035 35.266 1.00101.27 S ANISOU 238 SD MET A 76 11948 13642 12890 62 -1301 737 S ATOM 239 CE MET A 76 25.116 46.317 36.386 1.00111.39 C ANISOU 239 CE MET A 76 13133 14805 14383 86 -1295 629 C ATOM 240 N ALA A 77 29.314 42.040 32.287 1.00 93.58 N ANISOU 240 N ALA A 77 11079 13254 11222 -195 -1298 413 N ATOM 241 CA ALA A 77 30.097 41.888 31.066 1.00 92.38 C ANISOU 241 CA ALA A 77 10949 13291 10858 -177 -1312 474 C ATOM 242 C ALA A 77 29.894 40.511 30.446 1.00 97.71 C ANISOU 242 C ALA A 77 11569 14152 11403 -243 -1339 240 C ATOM 243 O ALA A 77 29.606 40.395 29.249 1.00 99.07 O ANISOU 243 O ALA A 77 11675 14587 11379 -197 -1419 234 O ATOM 244 CB ALA A 77 31.576 42.137 31.357 1.00 76.02 C ANISOU 244 CB ALA A 77 9000 11073 8811 -217 -1207 578 C ATOM 245 N VAL A 78 30.037 39.452 31.246 1.00 92.64 N ANISOU 245 N VAL A 78 10954 13377 10868 -350 -1269 43 N ATOM 246 CA VAL A 78 29.871 38.104 30.717 1.00 97.38 C ANISOU 246 CA VAL A 78 11509 14113 11378 -423 -1275 -196 C ATOM 247 C VAL A 78 28.423 37.831 30.323 1.00104.38 C ANISOU 247 C VAL A 78 12251 15172 12236 -414 -1377 -333 C ATOM 248 O VAL A 78 28.164 36.976 29.470 1.00111.15 O ANISOU 248 O VAL A 78 13041 16230 12961 -451 -1417 -509 O ATOM 249 CB VAL A 78 30.389 37.075 31.741 1.00 94.23 C ANISOU 249 CB VAL A 78 11183 13496 11125 -529 -1163 -346 C ATOM 250 CG1 VAL A 78 30.349 35.663 31.169 1.00 99.22 C ANISOU 250 CG1 VAL A 78 11781 14235 11683 -606 -1146 -593 C ATOM 251 CG2 VAL A 78 31.810 37.433 32.169 1.00 74.07 C ANISOU 251 CG2 VAL A 78 8752 10792 8601 -527 -1076 -204 C ATOM 252 N SER A 79 27.464 38.556 30.902 1.00101.02 N ANISOU 252 N SER A 79 11767 14685 11933 -367 -1421 -268 N ATOM 253 CA SER A 79 26.065 38.358 30.540 1.00 94.21 C ANISOU 253 CA SER A 79 10746 13999 11051 -352 -1524 -397 C ATOM 254 C SER A 79 25.692 39.100 29.263 1.00109.21 C ANISOU 254 C SER A 79 12561 16188 12747 -225 -1657 -266 C ATOM 255 O SER A 79 24.854 38.616 28.495 1.00123.12 O ANISOU 255 O SER A 79 14188 18200 14392 -225 -1754 -414 O ATOM 256 CB SER A 79 25.154 38.801 31.691 1.00 97.86 C ANISOU 256 CB SER A 79 11165 14286 11730 -347 -1511 -391 C ATOM 257 OG SER A 79 25.380 38.019 32.859 1.00 99.84 O ANISOU 257 OG SER A 79 11486 14299 12149 -466 -1391 -522 O ATOM 258 N MET A 80 26.309 40.254 29.007 1.00109.14 N ANISOU 258 N MET A 80 12625 16155 12687 -119 -1660 10 N ATOM 259 CA MET A 80 25.936 41.105 27.881 1.00102.25 C ANISOU 259 CA MET A 80 11685 15534 11633 23 -1779 189 C ATOM 260 C MET A 80 26.852 40.962 26.672 1.00102.02 C ANISOU 260 C MET A 80 11705 15712 11344 39 -1784 253 C ATOM 261 O MET A 80 26.380 41.067 25.535 1.00125.76 O ANISOU 261 O MET A 80 14622 19028 14134 119 -1898 279 O ATOM 262 CB MET A 80 25.912 42.577 28.312 1.00 84.28 C ANISOU 262 CB MET A 80 9452 13096 9476 144 -1773 476 C ATOM 263 CG MET A 80 24.824 42.934 29.312 1.00 99.75 C ANISOU 263 CG MET A 80 11334 14907 11660 167 -1789 437 C ATOM 264 SD MET A 80 24.905 44.658 29.846 1.00109.70 S ANISOU 264 SD MET A 80 12658 15939 13083 305 -1759 755 S ATOM 265 CE MET A 80 23.421 44.779 30.841 1.00114.92 C ANISOU 265 CE MET A 80 13185 16510 13971 327 -1792 630 C ATOM 266 N GLU A 81 28.149 40.743 26.876 1.00 99.90 N ANISOU 266 N GLU A 81 11572 15301 11086 -29 -1664 281 N ATOM 267 CA GLU A 81 29.099 40.765 25.769 1.00114.63 C ANISOU 267 CA GLU A 81 13489 17349 12715 -6 -1650 374 C ATOM 268 C GLU A 81 29.106 39.418 25.054 1.00125.34 C ANISOU 268 C GLU A 81 14793 18921 13911 -92 -1666 93 C ATOM 269 O GLU A 81 29.322 38.376 25.683 1.00128.58 O ANISOU 269 O GLU A 81 15225 19189 14441 -211 -1590 -132 O ATOM 270 CB GLU A 81 30.497 41.123 26.269 1.00121.10 C ANISOU 270 CB GLU A 81 14457 17936 13620 -43 -1512 514 C ATOM 271 CG GLU A 81 30.585 42.498 26.928 1.00119.82 C ANISOU 271 CG GLU A 81 14352 17554 13620 29 -1484 781 C ATOM 272 CD GLU A 81 30.156 43.625 26.000 1.00120.57 C ANISOU 272 CD GLU A 81 14412 17820 13578 178 -1569 1039 C ATOM 273 OE1 GLU A 81 30.427 43.542 24.780 1.00119.41 O ANISOU 273 OE1 GLU A 81 14253 17941 13175 219 -1604 1097 O ATOM 274 OE2 GLU A 81 29.542 44.595 26.493 1.00115.90 O ANISOU 274 OE2 GLU A 81 13806 17096 13134 260 -1596 1189 O ATOM 275 N LYS A 82 28.878 39.445 23.737 1.00128.65 N ANISOU 275 N LYS A 82 15143 19684 14056 -27 -1759 109 N ATOM 276 CA LYS A 82 28.893 38.218 22.944 1.00125.84 C ANISOU 276 CA LYS A 82 14729 19560 13523 -107 -1775 -172 C ATOM 277 C LYS A 82 30.274 37.570 22.949 1.00123.16 C ANISOU 277 C LYS A 82 14506 19116 13171 -192 -1633 -238 C ATOM 278 O LYS A 82 30.403 36.358 23.161 1.00128.26 O ANISOU 278 O LYS A 82 15147 19710 13876 -305 -1576 -516 O ATOM 279 CB LYS A 82 28.452 38.517 21.511 1.00124.37 C ANISOU 279 CB LYS A 82 14451 19787 13016 -8 -1906 -113 C ATOM 280 CG LYS A 82 27.090 39.186 21.389 1.00133.20 C ANISOU 280 CG LYS A 82 15437 21051 14123 102 -2063 -34 C ATOM 281 CD LYS A 82 26.879 39.741 19.982 1.00138.98 C ANISOU 281 CD LYS A 82 16107 22182 14517 236 -2186 122 C ATOM 282 CE LYS A 82 27.083 38.679 18.905 1.00141.39 C ANISOU 282 CE LYS A 82 16360 22813 14547 165 -2210 -137 C ATOM 283 NZ LYS A 82 26.831 39.204 17.528 1.00143.85 N ANISOU 283 NZ LYS A 82 16606 23552 14498 299 -2338 12 N ATOM 284 N LYS A 83 31.323 38.364 22.727 1.00 98.52 N ANISOU 284 N LYS A 83 11489 15956 9989 -140 -1566 17 N ATOM 285 CA LYS A 83 32.680 37.835 22.609 1.00104.65 C ANISOU 285 CA LYS A 83 12358 16673 10731 -206 -1434 -29 C ATOM 286 C LYS A 83 33.208 37.299 23.942 1.00121.21 C ANISOU 286 C LYS A 83 14528 18414 13112 -298 -1321 -128 C ATOM 287 O LYS A 83 34.388 36.946 24.061 1.00122.33 O ANISOU 287 O LYS A 83 14748 18458 13274 -343 -1207 -143 O ATOM 288 CB LYS A 83 33.613 38.916 22.048 1.00102.15 C ANISOU 288 CB LYS A 83 12119 16407 10286 -129 -1387 283 C ATOM 289 CG LYS A 83 33.099 39.577 20.774 1.00105.84 C ANISOU 289 CG LYS A 83 12529 17220 10467 -17 -1496 440 C ATOM 290 CD LYS A 83 33.878 40.841 20.453 1.00112.12 C ANISOU 290 CD LYS A 83 13410 17990 11200 63 -1438 801 C ATOM 291 CE LYS A 83 33.385 41.464 19.159 1.00130.83 C ANISOU 291 CE LYS A 83 15731 20714 13267 186 -1541 980 C ATOM 292 NZ LYS A 83 34.045 42.764 18.848 1.00137.29 N ANISOU 292 NZ LYS A 83 16636 21489 14039 269 -1477 1362 N ATOM 293 N LEU A 84 32.341 37.232 24.952 1.00116.22 N ANISOU 293 N LEU A 84 13867 17600 12693 -323 -1351 -195 N ATOM 294 CA LEU A 84 32.695 36.688 26.256 1.00110.13 C ANISOU 294 CA LEU A 84 13158 16510 12175 -405 -1254 -289 C ATOM 295 C LEU A 84 31.887 35.442 26.600 1.00119.76 C ANISOU 295 C LEU A 84 14315 17702 13487 -494 -1261 -591 C ATOM 296 O LEU A 84 31.996 34.934 27.721 1.00121.71 O ANISOU 296 O LEU A 84 14609 17689 13945 -559 -1185 -671 O ATOM 297 CB LEU A 84 32.510 37.751 27.344 1.00119.68 C ANISOU 297 CB LEU A 84 14408 17483 13582 -368 -1249 -86 C ATOM 298 CG LEU A 84 33.487 38.927 27.369 1.00111.46 C ANISOU 298 CG LEU A 84 13451 16360 12538 -312 -1200 197 C ATOM 299 CD1 LEU A 84 33.135 39.896 28.494 1.00106.65 C ANISOU 299 CD1 LEU A 84 12869 15511 12143 -285 -1197 344 C ATOM 300 CD2 LEU A 84 34.925 38.438 27.509 1.00 80.18 C ANISOU 300 CD2 LEU A 84 9573 12306 8585 -369 -1080 170 C ATOM 301 N HIS A 85 31.082 34.937 25.667 1.00126.34 N ANISOU 301 N HIS A 85 15040 18798 14166 -503 -1347 -763 N ATOM 302 CA HIS A 85 30.223 33.778 25.909 1.00108.90 C ANISOU 302 CA HIS A 85 12754 16573 12049 -600 -1353 -1065 C ATOM 303 C HIS A 85 30.994 32.516 25.545 1.00113.99 C ANISOU 303 C HIS A 85 13435 17219 12657 -683 -1257 -1293 C ATOM 304 O HIS A 85 31.013 32.094 24.386 1.00118.84 O ANISOU 304 O HIS A 85 13994 18100 13061 -688 -1293 -1428 O ATOM 305 CB HIS A 85 28.926 33.904 25.120 1.00 94.26 C ANISOU 305 CB HIS A 85 10746 15008 10060 -572 -1500 -1152 C ATOM 306 CG HIS A 85 28.038 35.005 25.608 1.00111.11 C ANISOU 306 CG HIS A 85 12830 17110 12278 -490 -1586 -962 C ATOM 307 ND1 HIS A 85 27.059 35.581 24.826 1.00116.04 N ANISOU 307 ND1 HIS A 85 13324 18014 12751 -404 -1735 -917 N ATOM 308 CD2 HIS A 85 27.983 35.638 26.804 1.00111.76 C ANISOU 308 CD2 HIS A 85 12969 16915 12581 -473 -1542 -811 C ATOM 309 CE1 HIS A 85 26.441 36.520 25.520 1.00113.92 C ANISOU 309 CE1 HIS A 85 13036 17628 12622 -333 -1774 -743 C ATOM 310 NE2 HIS A 85 26.982 36.575 26.724 1.00109.19 N ANISOU 310 NE2 HIS A 85 12550 16689 12247 -379 -1655 -684 N ATOM 311 N ASN A 86 31.630 31.912 26.545 1.00114.73 N ANISOU 311 N ASN A 86 13621 17016 12954 -742 -1134 -1337 N ATOM 312 CA ASN A 86 32.403 30.687 26.381 1.00123.29 C ANISOU 312 CA ASN A 86 14750 18039 14055 -809 -1025 -1542 C ATOM 313 C ASN A 86 32.706 30.134 27.768 1.00139.83 C ANISOU 313 C ASN A 86 16931 19780 16420 -860 -913 -1559 C ATOM 314 O ASN A 86 32.577 30.834 28.777 1.00131.53 O ANISOU 314 O ASN A 86 15919 18554 15503 -835 -915 -1383 O ATOM 315 CB ASN A 86 33.690 30.931 25.590 1.00119.18 C ANISOU 315 CB ASN A 86 14286 17637 13358 -754 -982 -1440 C ATOM 316 CG ASN A 86 34.454 32.142 26.085 1.00123.93 C ANISOU 316 CG ASN A 86 14968 18132 13988 -678 -967 -1119 C ATOM 317 OD1 ASN A 86 35.279 32.045 26.994 1.00114.19 O ANISOU 317 OD1 ASN A 86 13820 16655 12913 -687 -874 -1053 O ATOM 318 ND2 ASN A 86 34.177 33.296 25.489 1.00130.07 N ANISOU 318 ND2 ASN A 86 15714 19092 14614 -602 -1058 -918 N ATOM 319 N ALA A 87 33.139 28.870 27.797 1.00160.22 N ANISOU 319 N ALA A 87 19543 22258 19074 -926 -811 -1771 N ATOM 320 CA ALA A 87 33.247 28.134 29.055 1.00153.43 C ANISOU 320 CA ALA A 87 18755 21075 18466 -978 -705 -1819 C ATOM 321 C ALA A 87 34.129 28.859 30.064 1.00148.14 C ANISOU 321 C ALA A 87 18189 20211 17888 -915 -664 -1559 C ATOM 322 O ALA A 87 33.754 29.012 31.233 1.00156.46 O ANISOU 322 O ALA A 87 19275 21063 19109 -931 -645 -1486 O ATOM 323 CB ALA A 87 33.781 26.726 28.792 1.00153.17 C ANISOU 323 CB ALA A 87 18749 20963 18484 -1033 -592 -2057 C ATOM 324 N THR A 88 35.308 29.316 29.633 1.00136.62 N ANISOU 324 N THR A 88 16773 18818 16317 -850 -646 -1427 N ATOM 325 CA THR A 88 36.243 29.936 30.569 1.00123.00 C ANISOU 325 CA THR A 88 15134 16919 14683 -802 -603 -1209 C ATOM 326 C THR A 88 35.658 31.201 31.187 1.00115.23 C ANISOU 326 C THR A 88 14143 15903 13734 -774 -678 -1008 C ATOM 327 O THR A 88 35.851 31.463 32.380 1.00100.42 O ANISOU 327 O THR A 88 12326 13823 12007 -772 -644 -904 O ATOM 328 CB THR A 88 37.567 30.243 29.868 1.00112.50 C ANISOU 328 CB THR A 88 13829 15696 13220 -748 -570 -1117 C ATOM 329 OG1 THR A 88 38.153 29.023 29.398 1.00104.02 O ANISOU 329 OG1 THR A 88 12761 14624 12137 -767 -486 -1315 O ATOM 330 CG2 THR A 88 38.537 30.925 30.827 1.00114.93 C ANISOU 330 CG2 THR A 88 14206 15839 13623 -708 -531 -906 C ATOM 331 N ASN A 89 34.930 31.992 30.399 1.00115.27 N ANISOU 331 N ASN A 89 14077 16115 13606 -747 -779 -954 N ATOM 332 CA ASN A 89 34.377 33.231 30.928 1.00122.56 C ANISOU 332 CA ASN A 89 14993 17002 14574 -707 -844 -762 C ATOM 333 C ASN A 89 33.082 33.021 31.702 1.00114.38 C ANISOU 333 C ASN A 89 13912 15868 13679 -750 -871 -851 C ATOM 334 O ASN A 89 32.721 33.879 32.516 1.00108.87 O ANISOU 334 O ASN A 89 13225 15062 13078 -726 -892 -714 O ATOM 335 CB ASN A 89 34.163 34.240 29.800 1.00128.52 C ANISOU 335 CB ASN A 89 15692 18003 15135 -639 -937 -630 C ATOM 336 CG ASN A 89 35.449 34.933 29.395 1.00123.43 C ANISOU 336 CG ASN A 89 15106 17395 14395 -590 -898 -445 C ATOM 337 OD1 ASN A 89 36.039 35.676 30.180 1.00121.39 O ANISOU 337 OD1 ASN A 89 14908 16974 14242 -573 -862 -277 O ATOM 338 ND2 ASN A 89 35.891 34.694 28.167 1.00124.50 N ANISOU 338 ND2 ASN A 89 15219 17753 14332 -575 -899 -484 N ATOM 339 N TYR A 90 32.372 31.913 31.468 1.00116.93 N ANISOU 339 N TYR A 90 14180 16225 14022 -820 -863 -1088 N ATOM 340 CA TYR A 90 31.286 31.544 32.370 1.00 94.27 C ANISOU 340 CA TYR A 90 11278 13221 11320 -881 -852 -1185 C ATOM 341 C TYR A 90 31.832 31.174 33.744 1.00 82.89 C ANISOU 341 C TYR A 90 9944 11492 10061 -908 -743 -1143 C ATOM 342 O TYR A 90 31.217 31.485 34.770 1.00 72.59 O ANISOU 342 O TYR A 90 8644 10052 8885 -923 -734 -1094 O ATOM 343 CB TYR A 90 30.468 30.391 31.782 1.00 77.48 C ANISOU 343 CB TYR A 90 9066 11188 9186 -966 -854 -1463 C ATOM 344 CG TYR A 90 29.577 30.775 30.614 1.00 92.39 C ANISOU 344 CG TYR A 90 10819 13378 10907 -945 -983 -1524 C ATOM 345 CD1 TYR A 90 28.564 31.715 30.766 1.00105.93 C ANISOU 345 CD1 TYR A 90 12451 15167 12630 -902 -1080 -1427 C ATOM 346 CD2 TYR A 90 29.730 30.177 29.368 1.00103.08 C ANISOU 346 CD2 TYR A 90 12122 14952 12091 -962 -1009 -1687 C ATOM 347 CE1 TYR A 90 27.741 32.065 29.704 1.00107.98 C ANISOU 347 CE1 TYR A 90 12579 15719 12729 -866 -1209 -1472 C ATOM 348 CE2 TYR A 90 28.915 30.520 28.298 1.00107.76 C ANISOU 348 CE2 TYR A 90 12586 15851 12507 -936 -1138 -1743 C ATOM 349 CZ TYR A 90 27.921 31.464 28.473 1.00111.25 C ANISOU 349 CZ TYR A 90 12944 16368 12958 -884 -1242 -1627 C ATOM 350 OH TYR A 90 27.105 31.807 27.415 1.00113.76 O ANISOU 350 OH TYR A 90 13125 17005 13093 -842 -1381 -1670 O ATOM 351 N PHE A 91 32.992 30.512 33.777 1.00 93.41 N ANISOU 351 N PHE A 91 11356 12739 11396 -908 -660 -1160 N ATOM 352 CA PHE A 91 33.667 30.244 35.043 1.00 95.97 C ANISOU 352 CA PHE A 91 11782 12818 11865 -909 -569 -1088 C ATOM 353 C PHE A 91 33.954 31.536 35.797 1.00104.61 C ANISOU 353 C PHE A 91 12911 13856 12978 -855 -601 -863 C ATOM 354 O PHE A 91 33.749 31.614 37.013 1.00103.48 O ANISOU 354 O PHE A 91 12812 13544 12962 -871 -564 -815 O ATOM 355 CB PHE A 91 34.966 29.478 34.788 1.00 94.14 C ANISOU 355 CB PHE A 91 11613 12545 11611 -890 -493 -1121 C ATOM 356 CG PHE A 91 34.804 27.986 34.760 1.00108.94 C ANISOU 356 CG PHE A 91 13499 14322 13572 -951 -406 -1334 C ATOM 357 CD1 PHE A 91 34.662 27.274 35.939 1.00116.89 C ANISOU 357 CD1 PHE A 91 14570 15091 14752 -984 -318 -1351 C ATOM 358 CD2 PHE A 91 34.808 27.293 33.560 1.00114.75 C ANISOU 358 CD2 PHE A 91 14184 15200 14216 -975 -403 -1518 C ATOM 359 CE1 PHE A 91 34.515 25.899 35.922 1.00121.32 C ANISOU 359 CE1 PHE A 91 15149 15534 15415 -1041 -223 -1536 C ATOM 360 CE2 PHE A 91 34.661 25.919 33.537 1.00122.39 C ANISOU 360 CE2 PHE A 91 15162 16055 15285 -1037 -311 -1729 C ATOM 361 CZ PHE A 91 34.515 25.221 34.720 1.00123.19 C ANISOU 361 CZ PHE A 91 15332 15894 15581 -1069 -217 -1732 C ATOM 362 N LEU A 92 34.423 32.565 35.085 1.00110.00 N ANISOU 362 N LEU A 92 13578 14680 13538 -795 -663 -727 N ATOM 363 CA LEU A 92 34.740 33.839 35.720 1.00 95.60 C ANISOU 363 CA LEU A 92 11785 12794 11745 -751 -685 -525 C ATOM 364 C LEU A 92 33.497 34.536 36.254 1.00 94.68 C ANISOU 364 C LEU A 92 11624 12649 11703 -754 -735 -494 C ATOM 365 O LEU A 92 33.569 35.223 37.280 1.00 94.12 O ANISOU 365 O LEU A 92 11592 12444 11726 -744 -718 -389 O ATOM 366 CB LEU A 92 35.465 34.745 34.726 1.00 87.74 C ANISOU 366 CB LEU A 92 10778 11951 10607 -695 -725 -388 C ATOM 367 CG LEU A 92 36.766 34.176 34.160 1.00 87.25 C ANISOU 367 CG LEU A 92 10751 11935 10466 -687 -668 -410 C ATOM 368 CD1 LEU A 92 37.424 35.185 33.237 1.00 97.00 C ANISOU 368 CD1 LEU A 92 11974 13319 11564 -639 -696 -255 C ATOM 369 CD2 LEU A 92 37.698 33.777 35.292 1.00 76.28 C ANISOU 369 CD2 LEU A 92 9433 10353 9195 -696 -591 -392 C ATOM 370 N MET A 93 32.358 34.384 35.573 1.00 93.98 N ANISOU 370 N MET A 93 11443 12694 11572 -765 -796 -593 N ATOM 371 CA MET A 93 31.121 34.985 36.061 1.00104.74 C ANISOU 371 CA MET A 93 12744 14038 13015 -761 -841 -580 C ATOM 372 C MET A 93 30.654 34.307 37.341 1.00101.54 C ANISOU 372 C MET A 93 12368 13442 12771 -830 -763 -672 C ATOM 373 O MET A 93 30.367 34.975 38.342 1.00 86.94 O ANISOU 373 O MET A 93 10538 11477 11020 -820 -749 -591 O ATOM 374 CB MET A 93 30.037 34.906 34.986 1.00106.01 C ANISOU 374 CB MET A 93 12780 14413 13084 -754 -932 -678 C ATOM 375 CG MET A 93 28.654 35.323 35.473 1.00 99.47 C ANISOU 375 CG MET A 93 11864 13577 12353 -754 -975 -703 C ATOM 376 SD MET A 93 27.395 35.059 34.213 1.00110.08 S ANISOU 376 SD MET A 93 13039 15202 13586 -751 -1090 -851 S ATOM 377 CE MET A 93 25.922 35.640 35.059 1.00119.64 C ANISOU 377 CE MET A 93 14148 16359 14952 -743 -1119 -857 C ATOM 378 N SER A 94 30.562 32.974 37.320 1.00 95.06 N ANISOU 378 N SER A 94 11553 12586 11981 -901 -703 -844 N ATOM 379 CA SER A 94 30.215 32.230 38.526 1.00 90.23 C ANISOU 379 CA SER A 94 10984 11782 11519 -968 -609 -914 C ATOM 380 C SER A 94 31.212 32.504 39.642 1.00 85.18 C ANISOU 380 C SER A 94 10460 10974 10930 -941 -548 -775 C ATOM 381 O SER A 94 30.843 32.535 40.821 1.00 81.37 O ANISOU 381 O SER A 94 10011 10357 10551 -967 -496 -754 O ATOM 382 CB SER A 94 30.147 30.734 38.220 1.00 91.57 C ANISOU 382 CB SER A 94 11155 11919 11718 -1044 -541 -1107 C ATOM 383 OG SER A 94 29.979 29.979 39.407 1.00 70.28 O ANISOU 383 OG SER A 94 8522 9016 9165 -1103 -431 -1142 O ATOM 384 N LEU A 95 32.483 32.710 39.287 1.00 80.85 N ANISOU 384 N LEU A 95 9966 10449 10303 -892 -553 -684 N ATOM 385 CA LEU A 95 33.464 33.149 40.272 1.00 69.95 C ANISOU 385 CA LEU A 95 8673 8948 8957 -861 -517 -550 C ATOM 386 C LEU A 95 33.114 34.532 40.806 1.00 76.29 C ANISOU 386 C LEU A 95 9460 9741 9786 -832 -562 -429 C ATOM 387 O LEU A 95 33.171 34.775 42.018 1.00 72.47 O ANISOU 387 O LEU A 95 9024 9132 9377 -841 -522 -383 O ATOM 388 CB LEU A 95 34.863 33.147 39.659 1.00 74.56 C ANISOU 388 CB LEU A 95 9292 9585 9453 -817 -517 -490 C ATOM 389 CG LEU A 95 35.993 33.609 40.584 1.00 87.92 C ANISOU 389 CG LEU A 95 11054 11181 11170 -786 -490 -363 C ATOM 390 CD1 LEU A 95 36.067 32.731 41.824 1.00 89.50 C ANISOU 390 CD1 LEU A 95 11322 11223 11463 -807 -414 -395 C ATOM 391 CD2 LEU A 95 37.323 33.616 39.850 1.00 96.78 C ANISOU 391 CD2 LEU A 95 12186 12379 12209 -747 -489 -316 C ATOM 392 N ALA A 96 32.745 35.455 39.913 1.00 81.26 N ANISOU 392 N ALA A 96 10022 10500 10353 -793 -641 -376 N ATOM 393 CA ALA A 96 32.350 36.788 40.352 1.00 81.00 C ANISOU 393 CA ALA A 96 9970 10441 10365 -758 -677 -264 C ATOM 394 C ALA A 96 31.096 36.750 41.214 1.00 79.13 C ANISOU 394 C ALA A 96 9698 10133 10237 -790 -659 -334 C ATOM 395 O ALA A 96 30.916 37.626 42.064 1.00 70.82 O ANISOU 395 O ALA A 96 8657 8996 9255 -775 -650 -267 O ATOM 396 CB ALA A 96 32.136 37.705 39.146 1.00 83.47 C ANISOU 396 CB ALA A 96 10218 10906 10591 -697 -762 -180 C ATOM 397 N ILE A 97 30.233 35.753 41.021 1.00 96.08 N ANISOU 397 N ILE A 97 11794 12310 12401 -840 -645 -480 N ATOM 398 CA ILE A 97 29.075 35.602 41.894 1.00 95.35 C ANISOU 398 CA ILE A 97 11664 12147 12419 -884 -607 -556 C ATOM 399 C ILE A 97 29.507 35.172 43.291 1.00 89.31 C ANISOU 399 C ILE A 97 11000 11210 11726 -925 -506 -546 C ATOM 400 O ILE A 97 28.924 35.614 44.288 1.00 87.60 O ANISOU 400 O ILE A 97 10781 10918 11586 -936 -472 -536 O ATOM 401 CB ILE A 97 28.061 34.621 41.274 1.00 99.99 C ANISOU 401 CB ILE A 97 12160 12816 13014 -943 -611 -727 C ATOM 402 CG1 ILE A 97 27.503 35.201 39.969 1.00104.68 C ANISOU 402 CG1 ILE A 97 12638 13613 13521 -889 -728 -729 C ATOM 403 CG2 ILE A 97 26.920 34.329 42.237 1.00 79.60 C ANISOU 403 CG2 ILE A 97 9538 10150 10557 -1006 -548 -815 C ATOM 404 CD1 ILE A 97 26.421 34.362 39.325 1.00 85.91 C ANISOU 404 CD1 ILE A 97 10144 11351 11145 -948 -751 -915 C ATOM 405 N ALA A 98 30.540 34.335 43.400 1.00 84.36 N ANISOU 405 N ALA A 98 10458 10527 11067 -938 -458 -544 N ATOM 406 CA ALA A 98 31.043 33.974 44.721 1.00 82.17 C ANISOU 406 CA ALA A 98 10278 10107 10837 -956 -374 -508 C ATOM 407 C ALA A 98 31.752 35.154 45.374 1.00 77.77 C ANISOU 407 C ALA A 98 9761 9524 10265 -909 -398 -381 C ATOM 408 O ALA A 98 31.537 35.444 46.556 1.00 77.00 O ANISOU 408 O ALA A 98 9696 9346 10214 -923 -354 -362 O ATOM 409 CB ALA A 98 31.973 32.765 44.625 1.00 65.59 C ANISOU 409 CB ALA A 98 8251 7956 8714 -964 -320 -532 C ATOM 410 N ASP A 99 32.595 35.857 44.613 1.00 84.75 N ANISOU 410 N ASP A 99 10639 10478 11083 -860 -460 -302 N ATOM 411 CA ASP A 99 33.326 36.987 45.179 1.00 87.42 C ANISOU 411 CA ASP A 99 11008 10785 11422 -830 -476 -195 C ATOM 412 C ASP A 99 32.406 38.157 45.493 1.00 77.17 C ANISOU 412 C ASP A 99 9660 9472 10188 -819 -499 -176 C ATOM 413 O ASP A 99 32.682 38.926 46.419 1.00 74.26 O ANISOU 413 O ASP A 99 9323 9036 9856 -818 -481 -134 O ATOM 414 CB ASP A 99 34.434 37.432 44.229 1.00 86.05 C ANISOU 414 CB ASP A 99 10834 10686 11176 -792 -522 -116 C ATOM 415 CG ASP A 99 35.464 36.352 43.998 1.00 95.91 C ANISOU 415 CG ASP A 99 12127 11944 12370 -791 -493 -136 C ATOM 416 OD1 ASP A 99 35.597 35.460 44.867 1.00 98.36 O ANISOU 416 OD1 ASP A 99 12490 12173 12708 -809 -436 -174 O ATOM 417 OD2 ASP A 99 36.141 36.396 42.949 1.00109.72 O ANISOU 417 OD2 ASP A 99 13858 13780 14050 -767 -520 -107 O ATOM 418 N MET A 100 31.321 38.321 44.736 1.00 83.55 N ANISOU 418 N MET A 100 10384 10349 11011 -807 -540 -212 N ATOM 419 CA MET A 100 30.349 39.343 45.100 1.00 80.50 C ANISOU 419 CA MET A 100 9943 9941 10704 -785 -554 -202 C ATOM 420 C MET A 100 29.622 38.973 46.384 1.00 79.60 C ANISOU 420 C MET A 100 9841 9740 10664 -834 -478 -283 C ATOM 421 O MET A 100 29.345 39.847 47.213 1.00 81.91 O ANISOU 421 O MET A 100 10133 9969 11019 -824 -457 -267 O ATOM 422 CB MET A 100 29.348 39.561 43.967 1.00 86.26 C ANISOU 422 CB MET A 100 10564 10786 11424 -747 -625 -219 C ATOM 423 CG MET A 100 28.352 40.671 44.246 1.00 91.65 C ANISOU 423 CG MET A 100 11176 11447 12197 -701 -645 -197 C ATOM 424 SD MET A 100 26.976 40.661 43.085 1.00 97.30 S ANISOU 424 SD MET A 100 11743 12322 12904 -655 -730 -243 S ATOM 425 CE MET A 100 26.202 39.101 43.502 1.00107.43 C ANISOU 425 CE MET A 100 12994 13612 14210 -759 -669 -433 C ATOM 426 N LEU A 101 29.324 37.685 46.575 1.00 89.88 N ANISOU 426 N LEU A 101 11156 11032 11962 -890 -426 -371 N ATOM 427 CA LEU A 101 28.666 37.237 47.796 1.00 97.52 C ANISOU 427 CA LEU A 101 12144 11918 12991 -944 -336 -435 C ATOM 428 C LEU A 101 29.605 37.207 48.993 1.00 92.57 C ANISOU 428 C LEU A 101 11626 11207 12338 -953 -280 -382 C ATOM 429 O LEU A 101 29.129 37.225 50.133 1.00 90.12 O ANISOU 429 O LEU A 101 11338 10841 12063 -983 -210 -409 O ATOM 430 CB LEU A 101 28.045 35.856 47.583 1.00 87.37 C ANISOU 430 CB LEU A 101 10840 10634 11724 -1009 -285 -539 C ATOM 431 CG LEU A 101 26.847 35.844 46.629 1.00 77.28 C ANISOU 431 CG LEU A 101 9429 9455 10481 -1017 -333 -629 C ATOM 432 CD1 LEU A 101 26.289 34.437 46.461 1.00 67.47 C ANISOU 432 CD1 LEU A 101 8165 8201 9270 -1102 -270 -756 C ATOM 433 CD2 LEU A 101 25.776 36.799 47.120 1.00 77.30 C ANISOU 433 CD2 LEU A 101 9347 9461 10561 -999 -335 -643 C ATOM 434 N VAL A 102 30.919 37.149 48.766 1.00 77.55 N ANISOU 434 N VAL A 102 9786 9311 10367 -926 -308 -312 N ATOM 435 CA VAL A 102 31.866 37.359 49.857 1.00 83.47 C ANISOU 435 CA VAL A 102 10619 10013 11085 -922 -280 -259 C ATOM 436 C VAL A 102 31.753 38.786 50.374 1.00 88.77 C ANISOU 436 C VAL A 102 11267 10670 11792 -906 -299 -239 C ATOM 437 O VAL A 102 31.616 39.024 51.581 1.00 74.41 O ANISOU 437 O VAL A 102 9481 8811 9982 -926 -249 -260 O ATOM 438 CB VAL A 102 33.301 37.040 49.400 1.00 77.38 C ANISOU 438 CB VAL A 102 9893 9268 10241 -892 -313 -196 C ATOM 439 CG1 VAL A 102 34.307 37.511 50.443 1.00 71.30 C ANISOU 439 CG1 VAL A 102 9179 8479 9435 -882 -308 -145 C ATOM 440 CG2 VAL A 102 33.463 35.559 49.143 1.00 82.84 C ANISOU 440 CG2 VAL A 102 10621 9944 10912 -903 -272 -225 C ATOM 441 N GLY A 103 31.804 39.759 49.462 1.00 72.95 N ANISOU 441 N GLY A 103 9209 8697 9810 -869 -366 -199 N ATOM 442 CA GLY A 103 31.689 41.146 49.869 1.00 75.22 C ANISOU 442 CA GLY A 103 9475 8946 10159 -852 -375 -181 C ATOM 443 C GLY A 103 30.307 41.507 50.359 1.00 74.31 C ANISOU 443 C GLY A 103 9305 8801 10128 -855 -339 -249 C ATOM 444 O GLY A 103 30.148 42.459 51.126 1.00 88.66 O ANISOU 444 O GLY A 103 11120 10564 12001 -852 -314 -267 O ATOM 445 N LEU A 104 29.295 40.755 49.939 1.00 78.48 N ANISOU 445 N LEU A 104 9780 9366 10672 -865 -331 -302 N ATOM 446 CA LEU A 104 27.916 41.060 50.292 1.00 84.04 C ANISOU 446 CA LEU A 104 10408 10060 11464 -866 -298 -374 C ATOM 447 C LEU A 104 27.468 40.381 51.582 1.00 84.31 C ANISOU 447 C LEU A 104 10479 10053 11501 -929 -195 -449 C ATOM 448 O LEU A 104 26.596 40.912 52.279 1.00 77.78 O ANISOU 448 O LEU A 104 9609 9201 10744 -932 -146 -506 O ATOM 449 CB LEU A 104 26.989 40.655 49.140 1.00 87.80 C ANISOU 449 CB LEU A 104 10783 10617 11959 -850 -347 -405 C ATOM 450 CG LEU A 104 25.515 41.073 49.167 1.00 92.37 C ANISOU 450 CG LEU A 104 11242 11216 12636 -831 -340 -473 C ATOM 451 CD1 LEU A 104 25.373 42.580 49.298 1.00 92.79 C ANISOU 451 CD1 LEU A 104 11263 11225 12767 -756 -365 -423 C ATOM 452 CD2 LEU A 104 24.820 40.580 47.910 1.00 82.45 C ANISOU 452 CD2 LEU A 104 9883 10075 11369 -816 -410 -505 C ATOM 453 N LEU A 105 28.055 39.234 51.929 1.00 84.48 N ANISOU 453 N LEU A 105 10582 10067 11451 -973 -153 -443 N ATOM 454 CA LEU A 105 27.580 38.435 53.054 1.00 87.74 C ANISOU 454 CA LEU A 105 11036 10444 11857 -1032 -45 -493 C ATOM 455 C LEU A 105 28.654 38.030 54.055 1.00 88.64 C ANISOU 455 C LEU A 105 11270 10532 11877 -1043 -5 -441 C ATOM 456 O LEU A 105 28.302 37.710 55.196 1.00 94.71 O ANISOU 456 O LEU A 105 12081 11279 12627 -1079 86 -464 O ATOM 457 CB LEU A 105 26.887 37.161 52.546 1.00 82.23 C ANISOU 457 CB LEU A 105 10308 9753 11183 -1080 -7 -545 C ATOM 458 CG LEU A 105 25.633 37.371 51.696 1.00 77.09 C ANISOU 458 CG LEU A 105 9519 9154 10619 -1081 -39 -622 C ATOM 459 CD1 LEU A 105 25.238 36.083 50.998 1.00 68.07 C ANISOU 459 CD1 LEU A 105 8347 8028 9489 -1137 -19 -684 C ATOM 460 CD2 LEU A 105 24.486 37.891 52.551 1.00 81.51 C ANISOU 460 CD2 LEU A 105 10013 9700 11257 -1100 32 -690 C ATOM 461 N VAL A 106 29.928 38.014 53.682 1.00 73.17 N ANISOU 461 N VAL A 106 9361 8587 9853 -1010 -68 -370 N ATOM 462 CA VAL A 106 31.004 37.637 54.594 1.00 76.45 C ANISOU 462 CA VAL A 106 9874 8999 10173 -1006 -46 -317 C ATOM 463 C VAL A 106 31.755 38.859 55.103 1.00 91.41 C ANISOU 463 C VAL A 106 11775 10914 12041 -985 -90 -305 C ATOM 464 O VAL A 106 31.961 39.012 56.307 1.00 85.26 O ANISOU 464 O VAL A 106 11043 10147 11206 -999 -50 -318 O ATOM 465 CB VAL A 106 31.959 36.633 53.910 1.00 85.97 C ANISOU 465 CB VAL A 106 11124 10211 11331 -984 -75 -258 C ATOM 466 CG1 VAL A 106 33.049 36.196 54.874 1.00 78.05 C ANISOU 466 CG1 VAL A 106 10210 9214 10229 -963 -58 -194 C ATOM 467 CG2 VAL A 106 31.184 35.428 53.399 1.00 93.82 C ANISOU 467 CG2 VAL A 106 12109 11170 12369 -1016 -21 -294 C ATOM 468 N MET A 107 32.167 39.743 54.192 1.00 97.51 N ANISOU 468 N MET A 107 12499 11696 12852 -957 -168 -284 N ATOM 469 CA MET A 107 32.856 40.966 54.598 1.00 87.30 C ANISOU 469 CA MET A 107 11204 10403 11562 -952 -201 -285 C ATOM 470 C MET A 107 32.052 41.843 55.555 1.00 78.70 C ANISOU 470 C MET A 107 10095 9283 10524 -971 -150 -366 C ATOM 471 O MET A 107 32.636 42.305 56.552 1.00 66.68 O ANISOU 471 O MET A 107 8606 7774 8954 -989 -137 -397 O ATOM 472 CB MET A 107 33.259 41.771 53.355 1.00 77.43 C ANISOU 472 CB MET A 107 9904 9149 10367 -922 -274 -238 C ATOM 473 CG MET A 107 34.465 41.234 52.598 1.00 84.20 C ANISOU 473 CG MET A 107 10783 10051 11158 -906 -323 -166 C ATOM 474 SD MET A 107 34.963 42.370 51.284 1.00 89.70 S ANISOU 474 SD MET A 107 11426 10747 11910 -880 -388 -99 S ATOM 475 CE MET A 107 36.404 41.536 50.632 1.00 84.27 C ANISOU 475 CE MET A 107 10765 10128 11128 -869 -422 -36 C ATOM 476 N PRO A 108 30.761 42.130 55.329 1.00 78.08 N ANISOU 476 N PRO A 108 9955 9173 10539 -968 -120 -413 N ATOM 477 CA PRO A 108 30.070 43.060 56.241 1.00 74.59 C ANISOU 477 CA PRO A 108 9487 8698 10157 -979 -66 -499 C ATOM 478 C PRO A 108 29.971 42.544 57.664 1.00 78.99 C ANISOU 478 C PRO A 108 10104 9286 10623 -1021 18 -552 C ATOM 479 O PRO A 108 30.127 43.325 58.612 1.00 72.47 O ANISOU 479 O PRO A 108 9289 8461 9784 -1036 46 -619 O ATOM 480 CB PRO A 108 28.681 43.221 55.600 1.00 72.07 C ANISOU 480 CB PRO A 108 9077 8356 9951 -955 -53 -530 C ATOM 481 CG PRO A 108 28.851 42.793 54.187 1.00 71.62 C ANISOU 481 CG PRO A 108 8991 8324 9898 -925 -130 -454 C ATOM 482 CD PRO A 108 29.882 41.713 54.221 1.00 76.49 C ANISOU 482 CD PRO A 108 9689 8975 10398 -949 -139 -403 C ATOM 483 N LEU A 109 29.716 41.247 57.843 1.00 85.19 N ANISOU 483 N LEU A 109 10928 10096 11344 -1041 64 -524 N ATOM 484 CA LEU A 109 29.618 40.691 59.185 1.00 85.81 C ANISOU 484 CA LEU A 109 11073 10209 11322 -1076 152 -547 C ATOM 485 C LEU A 109 30.980 40.490 59.835 1.00 89.44 C ANISOU 485 C LEU A 109 11614 10726 11642 -1067 118 -495 C ATOM 486 O LEU A 109 31.054 40.385 61.064 1.00 98.46 O ANISOU 486 O LEU A 109 12809 11922 12681 -1085 174 -518 O ATOM 487 CB LEU A 109 28.841 39.372 59.156 1.00 91.82 C ANISOU 487 CB LEU A 109 11850 10957 12080 -1104 230 -524 C ATOM 488 CG LEU A 109 27.326 39.467 59.387 1.00 86.94 C ANISOU 488 CG LEU A 109 11161 10319 11553 -1139 321 -611 C ATOM 489 CD1 LEU A 109 26.658 40.402 58.385 1.00 73.21 C ANISOU 489 CD1 LEU A 109 9304 8554 9957 -1107 261 -661 C ATOM 490 CD2 LEU A 109 26.686 38.084 59.344 1.00 85.88 C ANISOU 490 CD2 LEU A 109 11045 10165 11423 -1184 406 -589 C ATOM 491 N SER A 110 32.055 40.430 59.044 1.00 81.15 N ANISOU 491 N SER A 110 10570 9683 10579 -1037 27 -427 N ATOM 492 CA SER A 110 33.395 40.502 59.619 1.00 67.69 C ANISOU 492 CA SER A 110 8913 8047 8761 -1025 -22 -397 C ATOM 493 C SER A 110 33.694 41.910 60.112 1.00 80.16 C ANISOU 493 C SER A 110 10457 9640 10360 -1045 -46 -487 C ATOM 494 O SER A 110 34.233 42.097 61.210 1.00 81.39 O ANISOU 494 O SER A 110 10644 9873 10407 -1059 -40 -527 O ATOM 495 CB SER A 110 34.441 40.071 58.592 1.00 72.30 C ANISOU 495 CB SER A 110 9496 8635 9339 -989 -102 -310 C ATOM 496 OG SER A 110 35.745 40.419 59.037 1.00 72.50 O ANISOU 496 OG SER A 110 9533 8732 9281 -979 -162 -300 O ATOM 497 N LEU A 111 33.356 42.915 59.303 1.00 80.39 N ANISOU 497 N LEU A 111 10419 9596 10529 -1044 -71 -522 N ATOM 498 CA LEU A 111 33.571 44.300 59.702 1.00 77.02 C ANISOU 498 CA LEU A 111 9957 9146 10159 -1067 -78 -615 C ATOM 499 C LEU A 111 32.788 44.641 60.964 1.00 85.14 C ANISOU 499 C LEU A 111 10994 10193 11163 -1096 6 -732 C ATOM 500 O LEU A 111 33.305 45.324 61.857 1.00 68.53 O ANISOU 500 O LEU A 111 8896 8132 9009 -1127 9 -823 O ATOM 501 CB LEU A 111 33.181 45.235 58.558 1.00 70.43 C ANISOU 501 CB LEU A 111 9057 8209 9494 -1047 -105 -605 C ATOM 502 CG LEU A 111 33.169 46.724 58.896 1.00 80.00 C ANISOU 502 CG LEU A 111 10232 9350 10814 -1067 -89 -704 C ATOM 503 CD1 LEU A 111 34.534 47.155 59.410 1.00 77.86 C ANISOU 503 CD1 LEU A 111 9978 9127 10479 -1109 -127 -740 C ATOM 504 CD2 LEU A 111 32.754 47.537 57.679 1.00 77.60 C ANISOU 504 CD2 LEU A 111 9870 8936 10677 -1027 -111 -653 C ATOM 505 N LEU A 112 31.540 44.170 61.056 1.00 67.89 N ANISOU 505 N LEU A 112 8801 7986 9010 -1092 80 -743 N ATOM 506 CA LEU A 112 30.734 44.437 62.244 1.00 80.77 C ANISOU 506 CA LEU A 112 10435 9642 10612 -1121 177 -855 C ATOM 507 C LEU A 112 31.403 43.887 63.499 1.00 73.67 C ANISOU 507 C LEU A 112 9613 8867 9511 -1144 198 -861 C ATOM 508 O LEU A 112 31.396 44.537 64.551 1.00 77.29 O ANISOU 508 O LEU A 112 10075 9378 9912 -1173 239 -977 O ATOM 509 CB LEU A 112 29.333 43.846 62.072 1.00 69.02 C ANISOU 509 CB LEU A 112 8917 8121 9187 -1119 257 -854 C ATOM 510 CG LEU A 112 28.269 44.309 63.069 1.00 84.53 C ANISOU 510 CG LEU A 112 10854 10093 11171 -1143 370 -982 C ATOM 511 CD1 LEU A 112 28.078 45.819 62.997 1.00 73.81 C ANISOU 511 CD1 LEU A 112 9427 8662 9955 -1128 362 -1095 C ATOM 512 CD2 LEU A 112 26.950 43.587 62.834 1.00 95.28 C ANISOU 512 CD2 LEU A 112 12172 11433 12595 -1150 449 -974 C ATOM 513 N ALA A 113 31.997 42.694 63.404 1.00 80.00 N ANISOU 513 N ALA A 113 10475 9721 10200 -1126 172 -737 N ATOM 514 CA ALA A 113 32.722 42.138 64.542 1.00 69.87 C ANISOU 514 CA ALA A 113 9266 8568 8715 -1127 178 -712 C ATOM 515 C ALA A 113 33.918 43.006 64.910 1.00 74.61 C ANISOU 515 C ALA A 113 9849 9243 9256 -1135 93 -778 C ATOM 516 O ALA A 113 34.163 43.260 66.095 1.00 81.68 O ANISOU 516 O ALA A 113 10767 10254 10013 -1156 113 -856 O ATOM 517 CB ALA A 113 33.169 40.709 64.237 1.00 72.93 C ANISOU 517 CB ALA A 113 9717 8970 9024 -1088 163 -552 C ATOM 518 N ILE A 114 34.665 43.480 63.908 1.00 75.94 N ANISOU 518 N ILE A 114 9974 9357 9525 -1126 4 -755 N ATOM 519 CA ILE A 114 35.788 44.380 64.169 1.00 74.65 C ANISOU 519 CA ILE A 114 9777 9251 9337 -1151 -69 -832 C ATOM 520 C ILE A 114 35.309 45.642 64.877 1.00 84.81 C ANISOU 520 C ILE A 114 11026 10517 10679 -1204 -18 -1014 C ATOM 521 O ILE A 114 36.002 46.185 65.748 1.00 85.43 O ANISOU 521 O ILE A 114 11096 10697 10666 -1241 -42 -1123 O ATOM 522 CB ILE A 114 36.521 44.720 62.857 1.00 73.36 C ANISOU 522 CB ILE A 114 9567 9009 9299 -1141 -148 -772 C ATOM 523 CG1 ILE A 114 37.084 43.461 62.200 1.00 82.07 C ANISOU 523 CG1 ILE A 114 10701 10141 10339 -1088 -194 -614 C ATOM 524 CG2 ILE A 114 37.641 45.714 63.110 1.00 69.62 C ANISOU 524 CG2 ILE A 114 9046 8580 8826 -1185 -208 -865 C ATOM 525 CD1 ILE A 114 37.776 43.737 60.884 1.00 73.26 C ANISOU 525 CD1 ILE A 114 9539 8965 9330 -1078 -260 -554 C ATOM 526 N LEU A 115 34.115 46.127 64.520 1.00 70.84 N ANISOU 526 N LEU A 115 9228 8623 9065 -1205 51 -1059 N ATOM 527 CA LEU A 115 33.617 47.364 65.114 1.00 92.77 C ANISOU 527 CA LEU A 115 11966 11355 11927 -1245 109 -1236 C ATOM 528 C LEU A 115 33.381 47.221 66.612 1.00 84.70 C ANISOU 528 C LEU A 115 10980 10472 10729 -1274 176 -1347 C ATOM 529 O LEU A 115 33.479 48.207 67.351 1.00 80.17 O ANISOU 529 O LEU A 115 10381 9920 10161 -1319 202 -1522 O ATOM 530 CB LEU A 115 32.330 47.803 64.415 1.00 94.62 C ANISOU 530 CB LEU A 115 12153 11436 12361 -1219 169 -1245 C ATOM 531 CG LEU A 115 32.421 49.098 63.606 1.00 96.25 C ANISOU 531 CG LEU A 115 12298 11489 12783 -1217 146 -1287 C ATOM 532 CD1 LEU A 115 33.322 48.927 62.388 1.00 92.82 C ANISOU 532 CD1 LEU A 115 11859 11018 12388 -1197 49 -1142 C ATOM 533 CD2 LEU A 115 31.036 49.561 63.193 1.00 90.39 C ANISOU 533 CD2 LEU A 115 11505 10623 12217 -1176 213 -1312 C ATOM 534 N TYR A 116 33.077 46.013 67.082 1.00 80.19 N ANISOU 534 N TYR A 116 10471 9997 10000 -1252 213 -1251 N ATOM 535 CA TYR A 116 32.829 45.761 68.495 1.00 86.56 C ANISOU 535 CA TYR A 116 11323 10954 10613 -1274 286 -1325 C ATOM 536 C TYR A 116 33.995 45.038 69.165 1.00 86.35 C ANISOU 536 C TYR A 116 11353 11111 10345 -1259 214 -1251 C ATOM 537 O TYR A 116 33.797 44.304 70.136 1.00 80.21 O ANISOU 537 O TYR A 116 10638 10466 9371 -1249 270 -1213 O ATOM 538 CB TYR A 116 31.533 44.971 68.672 1.00 74.69 C ANISOU 538 CB TYR A 116 9849 9427 9105 -1263 405 -1270 C ATOM 539 CG TYR A 116 30.284 45.810 68.508 1.00 82.36 C ANISOU 539 CG TYR A 116 10751 10278 10264 -1279 495 -1397 C ATOM 540 CD1 TYR A 116 29.681 46.408 69.607 1.00 80.73 C ANISOU 540 CD1 TYR A 116 10534 10133 10007 -1313 597 -1566 C ATOM 541 CD2 TYR A 116 29.708 46.006 67.256 1.00 77.94 C ANISOU 541 CD2 TYR A 116 10131 9556 9926 -1251 478 -1350 C ATOM 542 CE1 TYR A 116 28.539 47.175 69.468 1.00 78.79 C ANISOU 542 CE1 TYR A 116 10216 9776 9944 -1315 683 -1686 C ATOM 543 CE2 TYR A 116 28.564 46.774 67.108 1.00 78.15 C ANISOU 543 CE2 TYR A 116 10084 9482 10128 -1247 554 -1457 C ATOM 544 CZ TYR A 116 27.986 47.355 68.220 1.00 75.84 C ANISOU 544 CZ TYR A 116 9778 9238 9799 -1277 659 -1626 C ATOM 545 OH TYR A 116 26.850 48.120 68.087 1.00 79.94 O ANISOU 545 OH TYR A 116 10215 9655 10503 -1262 738 -1737 O ATOM 546 N ASP A 117 35.215 45.250 68.662 1.00 74.66 N ANISOU 546 N ASP A 117 9844 9646 8877 -1253 95 -1224 N ATOM 547 CA ASP A 117 36.425 44.622 69.202 1.00 75.21 C ANISOU 547 CA ASP A 117 9944 9898 8734 -1225 8 -1154 C ATOM 548 C ASP A 117 36.281 43.104 69.259 1.00 84.98 C ANISOU 548 C ASP A 117 11266 11176 9848 -1157 32 -948 C ATOM 549 O ASP A 117 36.644 42.456 70.246 1.00 85.73 O ANISOU 549 O ASP A 117 11416 11440 9716 -1126 30 -894 O ATOM 550 CB ASP A 117 36.781 45.195 70.574 1.00 84.07 C ANISOU 550 CB ASP A 117 11060 11212 9671 -1266 6 -1320 C ATOM 551 CG ASP A 117 37.528 46.517 70.480 1.00103.45 C ANISOU 551 CG ASP A 117 13427 13657 12224 -1333 -59 -1506 C ATOM 552 OD1 ASP A 117 37.484 47.158 69.407 1.00107.76 O ANISOU 552 OD1 ASP A 117 13923 14015 13006 -1352 -70 -1516 O ATOM 553 OD2 ASP A 117 38.159 46.914 71.482 1.00113.04 O ANISOU 553 OD2 ASP A 117 14620 15054 13274 -1369 -97 -1643 O ATOM 554 N TYR A 118 35.728 42.541 68.186 1.00 83.38 N ANISOU 554 N TYR A 118 11071 10811 9797 -1133 58 -832 N ATOM 555 CA TYR A 118 35.563 41.100 67.999 1.00 90.09 C ANISOU 555 CA TYR A 118 11995 11646 10590 -1076 91 -643 C ATOM 556 C TYR A 118 34.652 40.468 69.046 1.00 74.32 C ANISOU 556 C TYR A 118 10071 9706 8462 -1082 217 -617 C ATOM 557 O TYR A 118 34.702 39.256 69.267 1.00 90.61 O ANISOU 557 O TYR A 118 12212 11792 10425 -1035 251 -456 O ATOM 558 CB TYR A 118 36.924 40.391 67.956 1.00 87.18 C ANISOU 558 CB TYR A 118 11648 11376 10100 -1010 -14 -517 C ATOM 559 CG TYR A 118 37.730 40.788 66.736 1.00 95.81 C ANISOU 559 CG TYR A 118 12671 12392 11338 -1004 -116 -514 C ATOM 560 CD1 TYR A 118 37.383 40.317 65.477 1.00100.27 C ANISOU 560 CD1 TYR A 118 13233 12803 12063 -987 -106 -428 C ATOM 561 CD2 TYR A 118 38.817 41.650 66.837 1.00 90.12 C ANISOU 561 CD2 TYR A 118 11884 11762 10595 -1025 -216 -605 C ATOM 562 CE1 TYR A 118 38.100 40.678 64.354 1.00104.59 C ANISOU 562 CE1 TYR A 118 13720 13294 12727 -982 -188 -419 C ATOM 563 CE2 TYR A 118 39.546 42.018 65.713 1.00 87.69 C ANISOU 563 CE2 TYR A 118 11511 11383 10423 -1027 -292 -594 C ATOM 564 CZ TYR A 118 39.179 41.527 64.475 1.00 88.05 C ANISOU 564 CZ TYR A 118 11564 11282 10611 -1002 -276 -494 C ATOM 565 OH TYR A 118 39.886 41.879 63.348 1.00 88.76 O ANISOU 565 OH TYR A 118 11593 11314 10818 -1004 -342 -476 O ATOM 566 N VAL A 119 33.805 41.264 69.691 1.00 75.10 N ANISOU 566 N VAL A 119 10146 9820 8569 -1138 299 -769 N ATOM 567 CA VAL A 119 32.750 40.737 70.548 1.00 82.26 C ANISOU 567 CA VAL A 119 11109 10760 9385 -1156 444 -755 C ATOM 568 C VAL A 119 31.477 40.662 69.717 1.00 89.89 C ANISOU 568 C VAL A 119 12037 11546 10572 -1184 532 -765 C ATOM 569 O VAL A 119 30.943 41.694 69.294 1.00 98.07 O ANISOU 569 O VAL A 119 12990 12499 11773 -1215 536 -905 O ATOM 570 CB VAL A 119 32.549 41.607 71.796 1.00 77.82 C ANISOU 570 CB VAL A 119 10536 10343 8688 -1199 493 -930 C ATOM 571 CG1 VAL A 119 31.426 41.052 72.651 1.00 83.50 C ANISOU 571 CG1 VAL A 119 11312 11103 9314 -1221 659 -911 C ATOM 572 CG2 VAL A 119 33.837 41.678 72.602 1.00 78.92 C ANISOU 572 CG2 VAL A 119 10698 10690 8596 -1172 390 -934 C ATOM 573 N TRP A 120 31.008 39.445 69.469 1.00 87.85 N ANISOU 573 N TRP A 120 11831 11225 10322 -1171 602 -617 N ATOM 574 CA TRP A 120 29.906 39.204 68.546 1.00 87.75 C ANISOU 574 CA TRP A 120 11771 11053 10517 -1198 667 -618 C ATOM 575 C TRP A 120 28.677 40.017 68.940 1.00 88.01 C ANISOU 575 C TRP A 120 11737 11071 10630 -1250 772 -778 C ATOM 576 O TRP A 120 28.113 39.794 70.023 1.00 76.32 O ANISOU 576 O TRP A 120 10296 9674 9027 -1280 896 -800 O ATOM 577 CB TRP A 120 29.574 37.714 68.509 1.00 74.49 C ANISOU 577 CB TRP A 120 10168 9325 8810 -1193 753 -455 C ATOM 578 CG TRP A 120 28.650 37.331 67.399 1.00 87.87 C ANISOU 578 CG TRP A 120 11804 10866 10717 -1222 792 -455 C ATOM 579 CD1 TRP A 120 27.377 36.857 67.520 1.00 80.80 C ANISOU 579 CD1 TRP A 120 10891 9914 9895 -1279 936 -473 C ATOM 580 CD2 TRP A 120 28.922 37.396 65.992 1.00 92.23 C ANISOU 580 CD2 TRP A 120 12297 11318 11427 -1200 685 -445 C ATOM 581 NE1 TRP A 120 26.839 36.618 66.277 1.00 77.26 N ANISOU 581 NE1 TRP A 120 10370 9345 9642 -1294 915 -485 N ATOM 582 CE2 TRP A 120 27.767 36.941 65.322 1.00 88.52 C ANISOU 582 CE2 TRP A 120 11774 10746 11113 -1243 762 -465 C ATOM 583 CE3 TRP A 120 30.028 37.793 65.234 1.00 81.75 C ANISOU 583 CE3 TRP A 120 10952 9991 10119 -1153 537 -425 C ATOM 584 CZ2 TRP A 120 27.687 36.872 63.933 1.00 87.83 C ANISOU 584 CZ2 TRP A 120 11619 10570 11181 -1233 685 -467 C ATOM 585 CZ3 TRP A 120 29.946 37.723 63.852 1.00 85.44 C ANISOU 585 CZ3 TRP A 120 11361 10361 10743 -1144 474 -416 C ATOM 586 CH2 TRP A 120 28.785 37.265 63.218 1.00 84.42 C ANISOU 586 CH2 TRP A 120 11183 10145 10749 -1181 544 -437 C ATOM 587 N PRO A 121 28.242 40.970 68.111 1.00 86.72 N ANISOU 587 N PRO A 121 11472 10810 10666 -1256 733 -888 N ATOM 588 CA PRO A 121 27.109 41.825 68.477 1.00 83.33 C ANISOU 588 CA PRO A 121 10968 10364 10331 -1289 830 -1048 C ATOM 589 C PRO A 121 25.750 41.299 68.045 1.00 85.69 C ANISOU 589 C PRO A 121 11212 10579 10767 -1315 935 -1042 C ATOM 590 O PRO A 121 24.730 41.808 68.527 1.00 99.82 O ANISOU 590 O PRO A 121 12941 12375 12612 -1341 1042 -1166 O ATOM 591 CB PRO A 121 27.438 43.132 67.743 1.00 83.52 C ANISOU 591 CB PRO A 121 10910 10313 10511 -1266 725 -1148 C ATOM 592 CG PRO A 121 28.130 42.671 66.497 1.00 90.32 C ANISOU 592 CG PRO A 121 11776 11104 11440 -1231 605 -1015 C ATOM 593 CD PRO A 121 28.881 41.403 66.855 1.00 95.57 C ANISOU 593 CD PRO A 121 12544 11845 11925 -1223 596 -867 C ATOM 594 N LEU A 122 25.708 40.310 67.167 1.00 94.32 N ANISOU 594 N LEU A 122 12314 11601 11921 -1310 912 -918 N ATOM 595 CA LEU A 122 24.462 39.746 66.668 1.00 89.75 C ANISOU 595 CA LEU A 122 11670 10950 11481 -1345 1002 -922 C ATOM 596 C LEU A 122 24.044 38.562 67.531 1.00 88.58 C ANISOU 596 C LEU A 122 11601 10838 11216 -1396 1153 -846 C ATOM 597 O LEU A 122 24.787 38.126 68.416 1.00 89.73 O ANISOU 597 O LEU A 122 11862 11065 11168 -1388 1172 -762 O ATOM 598 CB LEU A 122 24.643 39.352 65.201 1.00 91.97 C ANISOU 598 CB LEU A 122 11911 11138 11894 -1320 895 -852 C ATOM 599 CG LEU A 122 25.036 40.514 64.279 1.00 97.34 C ANISOU 599 CG LEU A 122 12517 11779 12689 -1266 756 -902 C ATOM 600 CD1 LEU A 122 25.452 40.015 62.900 1.00 99.51 C ANISOU 600 CD1 LEU A 122 12778 11996 13037 -1239 647 -812 C ATOM 601 CD2 LEU A 122 23.905 41.534 64.164 1.00 88.15 C ANISOU 601 CD2 LEU A 122 11228 10585 11681 -1261 794 -1039 C ATOM 602 N PRO A 123 22.831 38.033 67.334 1.00 95.42 N ANISOU 602 N PRO A 123 12404 11652 12197 -1451 1269 -871 N ATOM 603 CA PRO A 123 22.429 36.830 68.076 1.00 77.11 C ANISOU 603 CA PRO A 123 10165 9343 9789 -1511 1430 -781 C ATOM 604 C PRO A 123 23.392 35.673 67.850 1.00 82.65 C ANISOU 604 C PRO A 123 10991 10005 10408 -1489 1388 -600 C ATOM 605 O PRO A 123 24.047 35.573 66.810 1.00 84.49 O ANISOU 605 O PRO A 123 11214 10178 10711 -1447 1253 -559 O ATOM 606 CB PRO A 123 21.040 36.517 67.513 1.00 77.49 C ANISOU 606 CB PRO A 123 10091 9319 10031 -1577 1526 -854 C ATOM 607 CG PRO A 123 20.512 37.829 67.090 1.00 77.12 C ANISOU 607 CG PRO A 123 9902 9281 10118 -1544 1462 -1013 C ATOM 608 CD PRO A 123 21.693 38.629 66.608 1.00106.34 C ANISOU 608 CD PRO A 123 13631 12984 13791 -1462 1277 -997 C ATOM 609 N ARG A 124 23.461 34.781 68.844 1.00 97.10 N ANISOU 609 N ARG A 124 12938 11869 12087 -1513 1516 -485 N ATOM 610 CA ARG A 124 24.480 33.734 68.834 1.00 93.12 C ANISOU 610 CA ARG A 124 12564 11335 11483 -1469 1482 -298 C ATOM 611 C ARG A 124 24.238 32.702 67.738 1.00 92.41 C ANISOU 611 C ARG A 124 12459 11088 11565 -1498 1493 -242 C ATOM 612 O ARG A 124 25.192 32.078 67.260 1.00 88.40 O ANISOU 612 O ARG A 124 12021 10530 11038 -1443 1410 -128 O ATOM 613 CB ARG A 124 24.549 33.048 70.199 1.00 89.63 C ANISOU 613 CB ARG A 124 12253 10968 10834 -1477 1626 -171 C ATOM 614 CG ARG A 124 24.650 34.007 71.376 1.00 82.45 C ANISOU 614 CG ARG A 124 11355 10238 9736 -1464 1638 -249 C ATOM 615 CD ARG A 124 25.408 33.389 72.542 1.00 93.12 C ANISOU 615 CD ARG A 124 12858 11707 10818 -1417 1681 -80 C ATOM 616 NE ARG A 124 26.826 33.224 72.235 1.00109.56 N ANISOU 616 NE ARG A 124 14998 13811 12819 -1319 1508 28 N ATOM 617 CZ ARG A 124 27.750 32.853 73.117 1.00109.26 C ANISOU 617 CZ ARG A 124 15072 13902 12540 -1246 1483 170 C ATOM 618 NH1 ARG A 124 27.411 32.605 74.375 1.00113.69 N ANISOU 618 NH1 ARG A 124 15712 14584 12899 -1261 1621 231 N ATOM 619 NH2 ARG A 124 29.015 32.733 72.739 1.00101.76 N ANISOU 619 NH2 ARG A 124 14149 12972 11544 -1154 1319 252 N ATOM 620 N TYR A 125 22.984 32.498 67.327 1.00 93.20 N ANISOU 620 N TYR A 125 12461 11115 11834 -1585 1596 -333 N ATOM 621 CA TYR A 125 22.727 31.570 66.231 1.00 87.38 C ANISOU 621 CA TYR A 125 11694 10241 11266 -1623 1599 -316 C ATOM 622 C TYR A 125 23.241 32.101 64.902 1.00 87.45 C ANISOU 622 C TYR A 125 11623 10233 11372 -1567 1403 -377 C ATOM 623 O TYR A 125 23.514 31.309 63.993 1.00 96.00 O ANISOU 623 O TYR A 125 12714 11222 12539 -1568 1366 -337 O ATOM 624 CB TYR A 125 21.229 31.256 66.128 1.00 90.08 C ANISOU 624 CB TYR A 125 11928 10531 11765 -1739 1753 -420 C ATOM 625 CG TYR A 125 20.362 32.374 65.577 1.00 90.48 C ANISOU 625 CG TYR A 125 11799 10635 11946 -1750 1692 -607 C ATOM 626 CD1 TYR A 125 20.106 32.477 64.212 1.00 84.16 C ANISOU 626 CD1 TYR A 125 10877 9791 11310 -1749 1579 -692 C ATOM 627 CD2 TYR A 125 19.776 33.307 66.423 1.00 93.32 C ANISOU 627 CD2 TYR A 125 12106 11092 12261 -1756 1754 -699 C ATOM 628 CE1 TYR A 125 19.308 33.486 63.706 1.00 77.86 C ANISOU 628 CE1 TYR A 125 9911 9045 10627 -1741 1520 -842 C ATOM 629 CE2 TYR A 125 18.968 34.318 65.926 1.00 95.27 C ANISOU 629 CE2 TYR A 125 12183 11373 12641 -1750 1704 -862 C ATOM 630 CZ TYR A 125 18.742 34.404 64.566 1.00 90.10 C ANISOU 630 CZ TYR A 125 11412 10674 12149 -1737 1584 -922 C ATOM 631 OH TYR A 125 17.945 35.412 64.066 1.00 87.50 O ANISOU 631 OH TYR A 125 10914 10384 11948 -1713 1529 -1064 O ATOM 632 N LEU A 126 23.380 33.422 64.772 1.00 98.32 N ANISOU 632 N LEU A 126 12924 11692 12741 -1519 1287 -472 N ATOM 633 CA LEU A 126 23.845 34.028 63.532 1.00 91.32 C ANISOU 633 CA LEU A 126 11962 10795 11939 -1465 1111 -516 C ATOM 634 C LEU A 126 25.343 33.846 63.312 1.00 90.23 C ANISOU 634 C LEU A 126 11922 10662 11697 -1386 990 -402 C ATOM 635 O LEU A 126 25.826 34.122 62.209 1.00 84.59 O ANISOU 635 O LEU A 126 11161 9931 11047 -1346 858 -415 O ATOM 636 CB LEU A 126 23.483 35.515 63.530 1.00 91.58 C ANISOU 636 CB LEU A 126 11890 10894 12012 -1438 1047 -642 C ATOM 637 CG LEU A 126 22.823 36.093 62.279 1.00 85.85 C ANISOU 637 CG LEU A 126 11013 10143 11460 -1429 961 -741 C ATOM 638 CD1 LEU A 126 21.666 35.221 61.826 1.00 72.96 C ANISOU 638 CD1 LEU A 126 9301 8464 9955 -1508 1055 -788 C ATOM 639 CD2 LEU A 126 22.346 37.514 62.545 1.00 92.36 C ANISOU 639 CD2 LEU A 126 11747 11016 12331 -1399 940 -853 C ATOM 640 N CYS A 127 26.077 33.382 64.331 1.00 83.67 N ANISOU 640 N CYS A 127 11220 9867 10703 -1359 1033 -287 N ATOM 641 CA CYS A 127 27.524 33.181 64.157 1.00 72.37 C ANISOU 641 CA CYS A 127 9867 8455 9175 -1276 916 -179 C ATOM 642 C CYS A 127 27.831 31.973 63.301 1.00 79.85 C ANISOU 642 C CYS A 127 10852 9291 10198 -1268 916 -97 C ATOM 643 O CYS A 127 28.580 32.125 62.301 1.00 83.39 O ANISOU 643 O CYS A 127 11270 9728 10686 -1220 786 -98 O ATOM 644 CB CYS A 127 28.194 33.107 65.536 1.00 82.97 C ANISOU 644 CB CYS A 127 11321 9897 10308 -1238 950 -86 C ATOM 645 SG CYS A 127 29.835 32.339 65.563 1.00 98.79 S ANISOU 645 SG CYS A 127 13434 11918 12183 -1133 857 90 S ATOM 646 N PRO A 128 27.335 30.757 63.566 1.00 81.23 N ANISOU 646 N PRO A 128 11089 9370 10403 -1314 1060 -28 N ATOM 647 CA PRO A 128 27.661 29.618 62.700 1.00 87.19 C ANISOU 647 CA PRO A 128 11877 10001 11251 -1306 1064 30 C ATOM 648 C PRO A 128 27.059 29.719 61.307 1.00 91.87 C ANISOU 648 C PRO A 128 12345 10543 12017 -1355 1011 -104 C ATOM 649 O PRO A 128 27.545 29.042 60.392 1.00 74.09 O ANISOU 649 O PRO A 128 10103 8219 9829 -1334 968 -88 O ATOM 650 CB PRO A 128 27.100 28.409 63.459 1.00 80.93 C ANISOU 650 CB PRO A 128 11178 9108 10465 -1361 1258 123 C ATOM 651 CG PRO A 128 26.899 28.885 64.857 1.00 75.94 C ANISOU 651 CG PRO A 128 10594 8583 9677 -1362 1331 164 C ATOM 652 CD PRO A 128 26.513 30.319 64.717 1.00 83.59 C ANISOU 652 CD PRO A 128 11442 9666 10654 -1375 1240 7 C ATOM 653 N VAL A 129 26.010 30.523 61.121 1.00 96.44 N ANISOU 653 N VAL A 129 12805 11166 12671 -1412 1014 -239 N ATOM 654 CA VAL A 129 25.507 30.785 59.776 1.00 96.16 C ANISOU 654 CA VAL A 129 12639 11123 12774 -1437 932 -360 C ATOM 655 C VAL A 129 26.538 31.566 58.973 1.00 89.63 C ANISOU 655 C VAL A 129 11791 10358 11908 -1348 752 -352 C ATOM 656 O VAL A 129 26.830 31.238 57.817 1.00 80.78 O ANISOU 656 O VAL A 129 10637 9212 10845 -1335 679 -373 O ATOM 657 CB VAL A 129 24.164 31.534 59.836 1.00 92.97 C ANISOU 657 CB VAL A 129 12103 10766 12454 -1498 971 -493 C ATOM 658 CG1 VAL A 129 23.654 31.815 58.430 1.00 71.29 C ANISOU 658 CG1 VAL A 129 9216 8037 9835 -1508 872 -606 C ATOM 659 CG2 VAL A 129 23.144 30.741 60.632 1.00 86.10 C ANISOU 659 CG2 VAL A 129 11246 9839 11628 -1598 1165 -505 C ATOM 660 N TRP A 130 27.106 32.614 59.575 1.00 84.11 N ANISOU 660 N TRP A 130 11108 9743 11109 -1293 686 -329 N ATOM 661 CA TRP A 130 28.099 33.416 58.871 1.00 68.39 C ANISOU 661 CA TRP A 130 9094 7804 9089 -1221 530 -319 C ATOM 662 C TRP A 130 29.374 32.619 58.624 1.00 71.07 C ANISOU 662 C TRP A 130 9522 8119 9364 -1165 487 -212 C ATOM 663 O TRP A 130 29.980 32.726 57.552 1.00 69.68 O ANISOU 663 O TRP A 130 9311 7950 9214 -1128 387 -216 O ATOM 664 CB TRP A 130 28.389 34.693 59.661 1.00 68.74 C ANISOU 664 CB TRP A 130 9133 7930 9057 -1191 488 -336 C ATOM 665 CG TRP A 130 29.598 35.459 59.198 1.00 79.82 C ANISOU 665 CG TRP A 130 10534 9380 10416 -1126 349 -308 C ATOM 666 CD1 TRP A 130 29.743 36.138 58.021 1.00 78.83 C ANISOU 666 CD1 TRP A 130 10330 9258 10365 -1103 246 -340 C ATOM 667 CD2 TRP A 130 30.823 35.642 59.918 1.00 84.37 C ANISOU 667 CD2 TRP A 130 11182 10015 10861 -1080 305 -241 C ATOM 668 NE1 TRP A 130 30.987 36.722 57.960 1.00 75.20 N ANISOU 668 NE1 TRP A 130 9891 8841 9840 -1055 152 -297 N ATOM 669 CE2 TRP A 130 31.669 36.434 59.114 1.00 85.61 C ANISOU 669 CE2 TRP A 130 11294 10198 11036 -1042 182 -246 C ATOM 670 CE3 TRP A 130 31.288 35.210 61.165 1.00 94.10 C ANISOU 670 CE3 TRP A 130 12507 11292 11955 -1066 357 -175 C ATOM 671 CZ2 TRP A 130 32.953 36.802 59.516 1.00 96.66 C ANISOU 671 CZ2 TRP A 130 12726 11664 12335 -1000 111 -204 C ATOM 672 CZ3 TRP A 130 32.563 35.576 61.563 1.00 99.24 C ANISOU 672 CZ3 TRP A 130 13190 12026 12492 -1013 272 -131 C ATOM 673 CH2 TRP A 130 33.381 36.363 60.741 1.00 97.61 C ANISOU 673 CH2 TRP A 130 12925 11840 12321 -986 151 -154 C ATOM 674 N ILE A 131 29.788 31.803 59.598 1.00 68.95 N ANISOU 674 N ILE A 131 9364 7825 9008 -1150 567 -111 N ATOM 675 CA ILE A 131 30.994 30.995 59.432 1.00 73.55 C ANISOU 675 CA ILE A 131 10027 8382 9537 -1079 533 -2 C ATOM 676 C ILE A 131 30.849 30.050 58.244 1.00 80.15 C ANISOU 676 C ILE A 131 10843 9117 10493 -1097 546 -29 C ATOM 677 O ILE A 131 31.797 29.845 57.475 1.00 88.69 O ANISOU 677 O ILE A 131 11927 10200 11572 -1039 465 -3 O ATOM 678 CB ILE A 131 31.308 30.235 60.734 1.00 85.70 C ANISOU 678 CB ILE A 131 11687 9909 10964 -1051 628 126 C ATOM 679 CG1 ILE A 131 31.599 31.231 61.859 1.00 90.93 C ANISOU 679 CG1 ILE A 131 12363 10706 11481 -1028 594 134 C ATOM 680 CG2 ILE A 131 32.474 29.272 60.531 1.00 70.43 C ANISOU 680 CG2 ILE A 131 9831 7930 8998 -964 603 247 C ATOM 681 CD1 ILE A 131 31.974 30.587 63.172 1.00 83.20 C ANISOU 681 CD1 ILE A 131 11501 9759 10353 -987 670 269 C ATOM 682 N SER A 132 29.659 29.472 58.065 1.00 85.65 N ANISOU 682 N SER A 132 11510 9734 11298 -1185 652 -97 N ATOM 683 CA SER A 132 29.437 28.574 56.934 1.00 87.22 C ANISOU 683 CA SER A 132 11679 9845 11616 -1218 669 -156 C ATOM 684 C SER A 132 29.371 29.339 55.617 1.00 79.81 C ANISOU 684 C SER A 132 10621 8982 10720 -1215 539 -263 C ATOM 685 O SER A 132 29.846 28.847 54.587 1.00 81.39 O ANISOU 685 O SER A 132 10809 9162 10953 -1195 493 -287 O ATOM 686 CB SER A 132 28.163 27.761 57.146 1.00 87.56 C ANISOU 686 CB SER A 132 11711 9788 11770 -1327 824 -216 C ATOM 687 OG SER A 132 27.051 28.609 57.345 1.00 95.87 O ANISOU 687 OG SER A 132 12665 10908 12852 -1390 834 -311 O ATOM 688 N LEU A 133 28.775 30.534 55.624 1.00 82.87 N ANISOU 688 N LEU A 133 10922 9460 11107 -1229 483 -325 N ATOM 689 CA LEU A 133 28.813 31.384 54.437 1.00 87.82 C ANISOU 689 CA LEU A 133 11446 10167 11756 -1205 353 -390 C ATOM 690 C LEU A 133 30.230 31.853 54.129 1.00 94.89 C ANISOU 690 C LEU A 133 12377 11112 12564 -1118 244 -312 C ATOM 691 O LEU A 133 30.581 32.037 52.958 1.00 86.75 O ANISOU 691 O LEU A 133 11294 10123 11543 -1093 157 -337 O ATOM 692 CB LEU A 133 27.882 32.586 54.609 1.00 79.33 C ANISOU 692 CB LEU A 133 10275 9157 10710 -1224 328 -455 C ATOM 693 CG LEU A 133 26.386 32.275 54.520 1.00 81.54 C ANISOU 693 CG LEU A 133 10465 9420 11097 -1308 407 -564 C ATOM 694 CD1 LEU A 133 25.560 33.539 54.680 1.00 73.52 C ANISOU 694 CD1 LEU A 133 9348 8473 10115 -1301 374 -622 C ATOM 695 CD2 LEU A 133 26.066 31.588 53.202 1.00 73.13 C ANISOU 695 CD2 LEU A 133 9329 8356 10102 -1339 375 -647 C ATOM 696 N ASP A 134 31.057 32.051 55.158 1.00 99.67 N ANISOU 696 N ASP A 134 13063 11729 13078 -1074 248 -220 N ATOM 697 CA ASP A 134 32.465 32.345 54.921 1.00 85.33 C ANISOU 697 CA ASP A 134 11274 9962 11186 -999 154 -151 C ATOM 698 C ASP A 134 33.153 31.170 54.238 1.00 70.96 C ANISOU 698 C ASP A 134 9494 8090 9379 -967 164 -120 C ATOM 699 O ASP A 134 33.851 31.341 53.233 1.00 73.64 O ANISOU 699 O ASP A 134 9796 8470 9713 -931 84 -127 O ATOM 700 CB ASP A 134 33.159 32.691 56.240 1.00 76.15 C ANISOU 700 CB ASP A 134 10179 8839 9916 -963 158 -74 C ATOM 701 CG ASP A 134 34.641 32.979 56.065 1.00 90.95 C ANISOU 701 CG ASP A 134 12064 10776 11716 -890 63 -12 C ATOM 702 OD1 ASP A 134 35.020 33.550 55.021 1.00 95.23 O ANISOU 702 OD1 ASP A 134 12543 11353 12288 -879 -20 -40 O ATOM 703 OD2 ASP A 134 35.427 32.635 56.974 1.00 82.06 O ANISOU 703 OD2 ASP A 134 11006 9675 10500 -843 71 68 O ATOM 704 N VAL A 135 32.945 29.961 54.762 1.00 67.06 N ANISOU 704 N VAL A 135 9075 7497 8907 -980 273 -86 N ATOM 705 CA VAL A 135 33.608 28.781 54.213 1.00 74.47 C ANISOU 705 CA VAL A 135 10059 8359 9875 -942 299 -58 C ATOM 706 C VAL A 135 33.105 28.487 52.803 1.00 90.13 C ANISOU 706 C VAL A 135 11967 10330 11949 -988 284 -179 C ATOM 707 O VAL A 135 33.889 28.181 51.899 1.00 87.02 O ANISOU 707 O VAL A 135 11562 9948 11553 -944 237 -190 O ATOM 708 CB VAL A 135 33.410 27.578 55.151 1.00 72.31 C ANISOU 708 CB VAL A 135 9891 7960 9623 -946 437 17 C ATOM 709 CG1 VAL A 135 33.656 26.270 54.407 1.00 71.35 C ANISOU 709 CG1 VAL A 135 9802 7716 9593 -936 496 0 C ATOM 710 CG2 VAL A 135 34.330 27.701 56.356 1.00 68.79 C ANISOU 710 CG2 VAL A 135 9526 7557 9052 -862 425 160 C ATOM 711 N LEU A 136 31.789 28.580 52.596 1.00 83.66 N ANISOU 711 N LEU A 136 11083 9500 11203 -1077 322 -281 N ATOM 712 CA LEU A 136 31.204 28.227 51.304 1.00 77.94 C ANISOU 712 CA LEU A 136 10276 8783 10555 -1128 307 -412 C ATOM 713 C LEU A 136 31.774 29.082 50.180 1.00 76.99 C ANISOU 713 C LEU A 136 10084 8792 10378 -1080 170 -432 C ATOM 714 O LEU A 136 32.274 28.558 49.177 1.00 86.59 O ANISOU 714 O LEU A 136 11287 10017 11595 -1061 146 -475 O ATOM 715 CB LEU A 136 29.683 28.374 51.364 1.00 93.41 C ANISOU 715 CB LEU A 136 12155 10743 12592 -1226 355 -516 C ATOM 716 CG LEU A 136 28.935 28.495 50.033 1.00 90.47 C ANISOU 716 CG LEU A 136 11656 10451 12268 -1272 293 -662 C ATOM 717 CD1 LEU A 136 29.076 27.232 49.193 1.00 86.57 C ANISOU 717 CD1 LEU A 136 11170 9890 11833 -1306 339 -751 C ATOM 718 CD2 LEU A 136 27.471 28.820 50.283 1.00 87.72 C ANISOU 718 CD2 LEU A 136 11213 10126 11991 -1353 329 -751 C ATOM 719 N PHE A 137 31.705 30.404 50.325 1.00 72.28 N ANISOU 719 N PHE A 137 9440 8288 9733 -1059 90 -402 N ATOM 720 CA PHE A 137 32.111 31.273 49.228 1.00 76.31 C ANISOU 720 CA PHE A 137 9881 8913 10200 -1021 -27 -410 C ATOM 721 C PHE A 137 33.625 31.309 49.058 1.00 85.80 C ANISOU 721 C PHE A 137 11132 10139 11329 -947 -72 -325 C ATOM 722 O PHE A 137 34.116 31.472 47.935 1.00 83.82 O ANISOU 722 O PHE A 137 10840 9963 11047 -920 -135 -340 O ATOM 723 CB PHE A 137 31.544 32.672 49.448 1.00 77.61 C ANISOU 723 CB PHE A 137 9984 9143 10361 -1020 -84 -398 C ATOM 724 CG PHE A 137 30.042 32.715 49.442 1.00 87.50 C ANISOU 724 CG PHE A 137 11159 10397 11689 -1081 -52 -492 C ATOM 725 CD1 PHE A 137 29.323 32.026 48.475 1.00 80.31 C ANISOU 725 CD1 PHE A 137 10179 9512 10823 -1126 -50 -600 C ATOM 726 CD2 PHE A 137 29.348 33.418 50.415 1.00 77.06 C ANISOU 726 CD2 PHE A 137 9824 9061 10396 -1098 -21 -487 C ATOM 727 CE1 PHE A 137 27.944 32.051 48.470 1.00 76.43 C ANISOU 727 CE1 PHE A 137 9597 9037 10406 -1185 -25 -697 C ATOM 728 CE2 PHE A 137 27.968 33.445 50.414 1.00 77.19 C ANISOU 728 CE2 PHE A 137 9754 9086 10490 -1151 13 -579 C ATOM 729 CZ PHE A 137 27.263 32.762 49.440 1.00 79.71 C ANISOU 729 CZ PHE A 137 9994 9435 10855 -1195 8 -681 C ATOM 730 N SER A 138 34.384 31.147 50.144 1.00 78.12 N ANISOU 730 N SER A 138 10240 9120 10322 -910 -40 -235 N ATOM 731 CA SER A 138 35.835 31.103 50.001 1.00 77.79 C ANISOU 731 CA SER A 138 10228 9110 10219 -837 -82 -163 C ATOM 732 C SER A 138 36.278 29.829 49.295 1.00 78.85 C ANISOU 732 C SER A 138 10386 9194 10380 -814 -41 -194 C ATOM 733 O SER A 138 37.165 29.868 48.434 1.00 95.17 O ANISOU 733 O SER A 138 12427 11321 12413 -771 -89 -193 O ATOM 734 CB SER A 138 36.507 31.232 51.366 1.00 91.14 C ANISOU 734 CB SER A 138 11985 10788 11857 -797 -69 -67 C ATOM 735 OG SER A 138 36.425 32.565 51.850 1.00 87.46 O ANISOU 735 OG SER A 138 11486 10386 11358 -811 -123 -54 O ATOM 736 N THR A 139 35.671 28.692 49.638 1.00 83.21 N ANISOU 736 N THR A 139 10987 9628 11001 -846 59 -227 N ATOM 737 CA THR A 139 35.980 27.457 48.924 1.00 91.30 C ANISOU 737 CA THR A 139 12033 10580 12077 -832 113 -281 C ATOM 738 C THR A 139 35.563 27.552 47.460 1.00 92.40 C ANISOU 738 C THR A 139 12084 10798 12226 -874 69 -411 C ATOM 739 O THR A 139 36.295 27.103 46.571 1.00 92.92 O ANISOU 739 O THR A 139 12139 10888 12279 -837 58 -449 O ATOM 740 CB THR A 139 35.301 26.263 49.603 1.00 79.60 C ANISOU 740 CB THR A 139 10622 8934 10689 -873 245 -293 C ATOM 741 OG1 THR A 139 35.549 26.307 51.013 1.00 76.05 O ANISOU 741 OG1 THR A 139 10252 8440 10202 -835 281 -159 O ATOM 742 CG2 THR A 139 35.843 24.955 49.051 1.00 75.42 C ANISOU 742 CG2 THR A 139 10133 8297 10227 -841 314 -331 C ATOM 743 N ALA A 140 34.399 28.152 47.187 1.00 79.47 N ANISOU 743 N ALA A 140 10375 9215 10603 -945 41 -483 N ATOM 744 CA ALA A 140 33.952 28.300 45.805 1.00 81.69 C ANISOU 744 CA ALA A 140 10564 9604 10871 -977 -15 -600 C ATOM 745 C ALA A 140 34.952 29.091 44.969 1.00 87.46 C ANISOU 745 C ALA A 140 11262 10467 11500 -911 -111 -549 C ATOM 746 O ALA A 140 35.061 28.866 43.758 1.00 94.08 O ANISOU 746 O ALA A 140 12052 11390 12304 -912 -140 -631 O ATOM 747 CB ALA A 140 32.579 28.968 45.763 1.00 74.12 C ANISOU 747 CB ALA A 140 9524 8701 9936 -1042 -45 -659 C ATOM 748 N SER A 141 35.690 30.013 45.589 1.00 78.33 N ANISOU 748 N SER A 141 10129 9338 10295 -861 -155 -423 N ATOM 749 CA SER A 141 36.701 30.768 44.856 1.00 86.02 C ANISOU 749 CA SER A 141 11072 10425 11186 -809 -229 -367 C ATOM 750 C SER A 141 37.828 29.857 44.381 1.00 94.99 C ANISOU 750 C SER A 141 12236 11552 12305 -759 -197 -379 C ATOM 751 O SER A 141 38.109 29.771 43.180 1.00 83.99 O ANISOU 751 O SER A 141 10797 10251 10864 -751 -221 -435 O ATOM 752 CB SER A 141 37.247 31.901 45.730 1.00 95.00 C ANISOU 752 CB SER A 141 12224 11575 12296 -781 -269 -248 C ATOM 753 OG SER A 141 36.267 32.911 45.929 1.00 89.16 O ANISOU 753 OG SER A 141 11445 10858 11575 -817 -303 -245 O ATOM 754 N ILE A 142 38.480 29.157 45.313 1.00 93.72 N ANISOU 754 N ILE A 142 12145 11286 12178 -718 -142 -326 N ATOM 755 CA ILE A 142 39.587 28.277 44.947 1.00 91.87 C ANISOU 755 CA ILE A 142 11933 11031 11943 -653 -107 -331 C ATOM 756 C ILE A 142 39.093 27.128 44.071 1.00 98.19 C ANISOU 756 C ILE A 142 12728 11782 12796 -684 -44 -475 C ATOM 757 O ILE A 142 39.799 26.674 43.162 1.00 93.31 O ANISOU 757 O ILE A 142 12090 11208 12158 -649 -35 -531 O ATOM 758 CB ILE A 142 40.310 27.772 46.213 1.00 88.18 C ANISOU 758 CB ILE A 142 11540 10464 11501 -587 -66 -229 C ATOM 759 CG1 ILE A 142 41.423 26.779 45.861 1.00 85.31 C ANISOU 759 CG1 ILE A 142 11192 10065 11156 -502 -24 -233 C ATOM 760 CG2 ILE A 142 39.328 27.140 47.183 1.00 93.50 C ANISOU 760 CG2 ILE A 142 12280 10999 12246 -627 10 -228 C ATOM 761 CD1 ILE A 142 42.634 27.407 45.206 1.00 79.94 C ANISOU 761 CD1 ILE A 142 10448 9523 10401 -450 -87 -204 C ATOM 762 N MET A 143 37.868 26.650 44.316 1.00 99.76 N ANISOU 762 N MET A 143 12939 11895 13069 -759 5 -551 N ATOM 763 CA MET A 143 37.330 25.565 43.498 1.00 92.57 C ANISOU 763 CA MET A 143 12015 10935 12222 -808 69 -714 C ATOM 764 C MET A 143 37.062 26.016 42.066 1.00 80.35 C ANISOU 764 C MET A 143 10373 9564 10593 -840 -3 -825 C ATOM 765 O MET A 143 37.116 25.196 41.142 1.00 76.88 O ANISOU 765 O MET A 143 9913 9134 10165 -855 33 -965 O ATOM 766 CB MET A 143 36.053 25.002 44.129 1.00 91.42 C ANISOU 766 CB MET A 143 11891 10661 12183 -896 144 -774 C ATOM 767 CG MET A 143 36.274 24.216 45.424 1.00100.35 C ANISOU 767 CG MET A 143 13129 11600 13400 -866 247 -676 C ATOM 768 SD MET A 143 37.277 22.727 45.233 1.00106.00 S ANISOU 768 SD MET A 143 13917 12159 14200 -792 352 -698 S ATOM 769 CE MET A 143 37.198 22.042 46.890 1.00101.01 C ANISOU 769 CE MET A 143 13410 11318 13653 -763 463 -544 C ATOM 770 N HIS A 144 36.781 27.304 41.857 1.00 78.15 N ANISOU 770 N HIS A 144 10038 9426 10229 -846 -100 -764 N ATOM 771 CA HIS A 144 36.623 27.811 40.497 1.00 78.41 C ANISOU 771 CA HIS A 144 9986 9644 10160 -856 -174 -832 C ATOM 772 C HIS A 144 37.967 27.901 39.786 1.00 90.24 C ANISOU 772 C HIS A 144 11484 11230 11572 -787 -187 -794 C ATOM 773 O HIS A 144 38.108 27.458 38.640 1.00 92.32 O ANISOU 773 O HIS A 144 11708 11590 11779 -791 -184 -909 O ATOM 774 CB HIS A 144 35.936 29.178 40.515 1.00 70.17 C ANISOU 774 CB HIS A 144 8890 8707 9066 -869 -265 -754 C ATOM 775 CG HIS A 144 34.443 29.105 40.558 1.00 79.37 C ANISOU 775 CG HIS A 144 10002 9872 10283 -941 -272 -851 C ATOM 776 ND1 HIS A 144 33.746 28.757 41.695 1.00 92.13 N ANISOU 776 ND1 HIS A 144 11654 11342 12011 -986 -209 -855 N ATOM 777 CD2 HIS A 144 33.513 29.333 39.602 1.00 90.72 C ANISOU 777 CD2 HIS A 144 11345 11452 11673 -976 -333 -948 C ATOM 778 CE1 HIS A 144 32.451 28.776 41.437 1.00 92.74 C ANISOU 778 CE1 HIS A 144 11654 11464 12119 -1051 -226 -958 C ATOM 779 NE2 HIS A 144 32.283 29.123 40.174 1.00 85.39 N ANISOU 779 NE2 HIS A 144 10640 10713 11093 -1043 -309 -1018 N ATOM 780 N LEU A 145 38.969 28.476 40.454 1.00 89.61 N ANISOU 780 N LEU A 145 11438 11130 11479 -727 -199 -645 N ATOM 781 CA LEU A 145 40.288 28.612 39.849 1.00 83.14 C ANISOU 781 CA LEU A 145 10605 10397 10586 -665 -205 -604 C ATOM 782 C LEU A 145 40.889 27.252 39.526 1.00 93.13 C ANISOU 782 C LEU A 145 11894 11594 11896 -631 -122 -710 C ATOM 783 O LEU A 145 41.502 27.069 38.467 1.00 85.18 O ANISOU 783 O LEU A 145 10849 10695 10820 -608 -115 -773 O ATOM 784 CB LEU A 145 41.206 29.391 40.785 1.00 66.69 C ANISOU 784 CB LEU A 145 8544 8292 8503 -618 -229 -444 C ATOM 785 CG LEU A 145 40.679 30.757 41.213 1.00 79.99 C ANISOU 785 CG LEU A 145 10211 10015 10166 -649 -297 -346 C ATOM 786 CD1 LEU A 145 41.651 31.416 42.170 1.00 77.78 C ANISOU 786 CD1 LEU A 145 9949 9710 9893 -613 -313 -220 C ATOM 787 CD2 LEU A 145 40.442 31.632 39.994 1.00 66.03 C ANISOU 787 CD2 LEU A 145 8379 8406 8305 -666 -355 -341 C ATOM 788 N CYS A 146 40.726 26.287 40.434 1.00 91.92 N ANISOU 788 N CYS A 146 11806 11258 11862 -625 -49 -726 N ATOM 789 CA CYS A 146 41.225 24.940 40.188 1.00 78.84 C ANISOU 789 CA CYS A 146 10180 9499 10278 -587 44 -825 C ATOM 790 C CYS A 146 40.482 24.277 39.035 1.00 96.29 C ANISOU 790 C CYS A 146 12351 11749 12488 -655 73 -1031 C ATOM 791 O CYS A 146 41.093 23.581 38.215 1.00 96.87 O ANISOU 791 O CYS A 146 12409 11845 12553 -625 121 -1141 O ATOM 792 CB CYS A 146 41.105 24.103 41.461 1.00 80.05 C ANISOU 792 CB CYS A 146 10420 9432 10563 -565 121 -772 C ATOM 793 SG CYS A 146 41.464 22.351 41.233 1.00105.77 S ANISOU 793 SG CYS A 146 13728 12505 13956 -524 258 -896 S ATOM 794 N ALA A 147 39.164 24.482 38.956 1.00 96.29 N ANISOU 794 N ALA A 147 12324 11769 12494 -748 45 -1100 N ATOM 795 CA ALA A 147 38.386 23.903 37.865 1.00 98.01 C ANISOU 795 CA ALA A 147 12485 12054 12699 -823 59 -1314 C ATOM 796 C ALA A 147 38.759 24.526 36.525 1.00 93.87 C ANISOU 796 C ALA A 147 11886 11777 12005 -807 -14 -1355 C ATOM 797 O ALA A 147 38.825 23.826 35.508 1.00 88.36 O ANISOU 797 O ALA A 147 11154 11146 11273 -825 20 -1532 O ATOM 798 CB ALA A 147 36.892 24.071 38.135 1.00 87.11 C ANISOU 798 CB ALA A 147 11074 10662 11362 -922 35 -1371 C ATOM 799 N ILE A 148 38.992 25.840 36.501 1.00 86.74 N ANISOU 799 N ILE A 148 10957 11011 10991 -777 -106 -1195 N ATOM 800 CA ILE A 148 39.443 26.495 35.276 1.00 83.89 C ANISOU 800 CA ILE A 148 10535 10880 10460 -754 -163 -1193 C ATOM 801 C ILE A 148 40.754 25.881 34.804 1.00 92.27 C ANISOU 801 C ILE A 148 11608 11950 11501 -691 -95 -1231 C ATOM 802 O ILE A 148 40.903 25.507 33.635 1.00 87.70 O ANISOU 802 O ILE A 148 10985 11509 10828 -698 -80 -1370 O ATOM 803 CB ILE A 148 39.584 28.011 35.496 1.00 90.32 C ANISOU 803 CB ILE A 148 11334 11788 11194 -728 -251 -987 C ATOM 804 CG1 ILE A 148 38.216 28.639 35.757 1.00 91.39 C ANISOU 804 CG1 ILE A 148 11440 11942 11342 -780 -320 -972 C ATOM 805 CG2 ILE A 148 40.252 28.661 34.298 1.00 71.27 C ANISOU 805 CG2 ILE A 148 8873 9593 8613 -696 -286 -950 C ATOM 806 CD1 ILE A 148 38.265 30.120 36.059 1.00 93.27 C ANISOU 806 CD1 ILE A 148 11670 12235 11535 -753 -394 -776 C ATOM 807 N SER A 149 41.720 25.759 35.718 1.00 86.29 N ANISOU 807 N SER A 149 10903 11058 10827 -626 -52 -1115 N ATOM 808 CA SER A 149 43.027 25.219 35.364 1.00 81.68 C ANISOU 808 CA SER A 149 10317 10479 10237 -551 13 -1137 C ATOM 809 C SER A 149 42.957 23.735 35.032 1.00 85.68 C ANISOU 809 C SER A 149 10842 10873 10838 -553 113 -1341 C ATOM 810 O SER A 149 43.732 23.250 34.200 1.00100.38 O ANISOU 810 O SER A 149 12677 12805 12659 -513 166 -1441 O ATOM 811 CB SER A 149 44.014 25.457 36.506 1.00 85.38 C ANISOU 811 CB SER A 149 10824 10840 10777 -475 21 -963 C ATOM 812 OG SER A 149 45.301 24.964 36.181 1.00 87.26 O ANISOU 812 OG SER A 149 11044 11095 11017 -393 79 -981 O ATOM 813 N LEU A 150 42.050 22.998 35.670 1.00 92.14 N ANISOU 813 N LEU A 150 11706 11510 11791 -602 154 -1410 N ATOM 814 CA LEU A 150 41.923 21.577 35.372 1.00 92.32 C ANISOU 814 CA LEU A 150 11752 11396 11931 -616 264 -1612 C ATOM 815 C LEU A 150 41.243 21.365 34.026 1.00 95.72 C ANISOU 815 C LEU A 150 12112 11993 12266 -698 252 -1841 C ATOM 816 O LEU A 150 41.689 20.546 33.216 1.00101.78 O ANISOU 816 O LEU A 150 12861 12775 13034 -684 325 -2017 O ATOM 817 CB LEU A 150 41.155 20.876 36.492 1.00 96.55 C ANISOU 817 CB LEU A 150 12359 11677 12648 -653 325 -1604 C ATOM 818 CG LEU A 150 41.391 19.376 36.648 1.00 98.33 C ANISOU 818 CG LEU A 150 12642 11666 13053 -629 468 -1728 C ATOM 819 CD1 LEU A 150 41.167 18.962 38.090 1.00104.42 C ANISOU 819 CD1 LEU A 150 13507 12186 13982 -609 525 -1587 C ATOM 820 CD2 LEU A 150 40.471 18.600 35.727 1.00103.81 C ANISOU 820 CD2 LEU A 150 13298 12363 13784 -741 518 -2006 C ATOM 821 N ASP A 151 40.156 22.098 33.767 1.00102.81 N ANISOU 821 N ASP A 151 12962 13027 13075 -780 159 -1849 N ATOM 822 CA ASP A 151 39.483 21.979 32.477 1.00 97.25 C ANISOU 822 CA ASP A 151 12178 12524 12250 -852 126 -2059 C ATOM 823 C ASP A 151 40.391 22.424 31.340 1.00105.81 C ANISOU 823 C ASP A 151 13214 13849 13140 -797 100 -2062 C ATOM 824 O ASP A 151 40.418 21.796 30.276 1.00112.11 O ANISOU 824 O ASP A 151 13968 14759 13867 -823 136 -2278 O ATOM 825 CB ASP A 151 38.193 22.795 32.473 1.00 97.73 C ANISOU 825 CB ASP A 151 12185 12703 12246 -926 17 -2032 C ATOM 826 CG ASP A 151 37.461 22.714 31.149 1.00117.62 C ANISOU 826 CG ASP A 151 14607 15463 14620 -994 -37 -2243 C ATOM 827 OD1 ASP A 151 36.566 21.851 31.020 1.00125.28 O ANISOU 827 OD1 ASP A 151 15546 16374 15679 -1086 1 -2463 O ATOM 828 OD2 ASP A 151 37.790 23.501 30.235 1.00118.12 O ANISOU 828 OD2 ASP A 151 14622 15781 14478 -956 -112 -2191 O ATOM 829 N ARG A 152 41.142 23.509 31.547 1.00106.06 N ANISOU 829 N ARG A 152 13251 13963 13083 -729 46 -1831 N ATOM 830 CA ARG A 152 42.075 23.970 30.525 1.00 98.53 C ANISOU 830 CA ARG A 152 12255 13230 11951 -680 38 -1809 C ATOM 831 C ARG A 152 43.149 22.925 30.252 1.00106.64 C ANISOU 831 C ARG A 152 13295 14184 13038 -624 158 -1934 C ATOM 832 O ARG A 152 43.569 22.743 29.103 1.00107.60 O ANISOU 832 O ARG A 152 13369 14489 13025 -617 186 -2062 O ATOM 833 CB ARG A 152 42.704 25.295 30.956 1.00 86.35 C ANISOU 833 CB ARG A 152 10719 11744 10347 -629 -24 -1535 C ATOM 834 CG ARG A 152 43.618 25.936 29.922 1.00100.76 C ANISOU 834 CG ARG A 152 12498 13802 11985 -591 -27 -1480 C ATOM 835 CD ARG A 152 44.057 27.315 30.395 1.00107.37 C ANISOU 835 CD ARG A 152 13339 14671 12784 -564 -86 -1213 C ATOM 836 NE ARG A 152 45.101 27.896 29.556 1.00110.50 N ANISOU 836 NE ARG A 152 13697 15253 13033 -530 -63 -1138 N ATOM 837 CZ ARG A 152 44.866 28.636 28.479 1.00115.66 C ANISOU 837 CZ ARG A 152 14311 16145 13489 -547 -106 -1100 C ATOM 838 NH1 ARG A 152 43.618 28.879 28.100 1.00128.88 N ANISOU 838 NH1 ARG A 152 15972 17911 15087 -590 -188 -1136 N ATOM 839 NH2 ARG A 152 45.877 29.129 27.775 1.00102.91 N ANISOU 839 NH2 ARG A 152 12666 14685 11749 -519 -65 -1020 N ATOM 840 N TYR A 153 43.598 22.222 31.294 1.00112.33 N ANISOU 840 N TYR A 153 14078 14644 13959 -576 233 -1898 N ATOM 841 CA TYR A 153 44.599 21.176 31.103 1.00116.34 C ANISOU 841 CA TYR A 153 14596 15056 14552 -505 352 -2011 C ATOM 842 C TYR A 153 44.007 19.969 30.390 1.00125.56 C ANISOU 842 C TYR A 153 15755 16179 15773 -565 431 -2312 C ATOM 843 O TYR A 153 44.628 19.413 29.477 1.00136.65 O ANISOU 843 O TYR A 153 17126 17668 17128 -537 502 -2478 O ATOM 844 CB TYR A 153 45.193 20.759 32.448 1.00116.75 C ANISOU 844 CB TYR A 153 14717 14842 14800 -422 402 -1871 C ATOM 845 CG TYR A 153 46.172 19.608 32.355 1.00116.70 C ANISOU 845 CG TYR A 153 14722 14703 14914 -330 528 -1977 C ATOM 846 CD1 TYR A 153 47.460 19.804 31.870 1.00122.79 C ANISOU 846 CD1 TYR A 153 15442 15600 15611 -239 554 -1944 C ATOM 847 CD2 TYR A 153 45.810 18.327 32.756 1.00109.25 C ANISOU 847 CD2 TYR A 153 13838 13501 14172 -330 631 -2106 C ATOM 848 CE1 TYR A 153 48.361 18.757 31.783 1.00120.99 C ANISOU 848 CE1 TYR A 153 15215 15252 15503 -141 672 -2044 C ATOM 849 CE2 TYR A 153 46.703 17.273 32.674 1.00115.48 C ANISOU 849 CE2 TYR A 153 14640 14149 15089 -231 752 -2198 C ATOM 850 CZ TYR A 153 47.977 17.494 32.187 1.00122.20 C ANISOU 850 CZ TYR A 153 15432 15138 15861 -130 769 -2169 C ATOM 851 OH TYR A 153 48.870 16.449 32.102 1.00122.77 O ANISOU 851 OH TYR A 153 15507 15072 16070 -19 892 -2263 O ATOM 852 N VAL A 154 42.809 19.544 30.796 1.00122.61 N ANISOU 852 N VAL A 154 15406 15674 15506 -654 427 -2398 N ATOM 853 CA VAL A 154 42.170 18.416 30.129 1.00117.17 C ANISOU 853 CA VAL A 154 14700 14939 14882 -733 504 -2705 C ATOM 854 C VAL A 154 41.793 18.780 28.696 1.00 98.23 C ANISOU 854 C VAL A 154 12207 12869 12245 -796 439 -2876 C ATOM 855 O VAL A 154 41.774 17.913 27.815 1.00 93.71 O ANISOU 855 O VAL A 154 11602 12340 11664 -832 511 -3151 O ATOM 856 CB VAL A 154 40.957 17.942 30.954 1.00111.43 C ANISOU 856 CB VAL A 154 14010 13997 14330 -827 519 -2747 C ATOM 857 CG1 VAL A 154 40.249 16.791 30.264 1.00114.92 C ANISOU 857 CG1 VAL A 154 14423 14385 14855 -930 603 -3084 C ATOM 858 CG2 VAL A 154 41.406 17.523 32.344 1.00104.92 C ANISOU 858 CG2 VAL A 154 13286 12860 13720 -752 594 -2568 C ATOM 859 N ALA A 155 41.511 20.058 28.429 1.00100.96 N ANISOU 859 N ALA A 155 12511 13455 12393 -804 307 -2716 N ATOM 860 CA ALA A 155 41.221 20.504 27.071 1.00 99.87 C ANISOU 860 CA ALA A 155 12288 13657 12000 -843 237 -2832 C ATOM 861 C ALA A 155 42.425 20.395 26.146 1.00117.53 C ANISOU 861 C ALA A 155 14503 16051 14103 -774 300 -2887 C ATOM 862 O ALA A 155 42.253 20.466 24.925 1.00129.97 O ANISOU 862 O ALA A 155 16012 17904 15467 -806 274 -3040 O ATOM 863 CB ALA A 155 40.716 21.949 27.088 1.00 98.73 C ANISOU 863 CB ALA A 155 12115 13703 11694 -845 89 -2602 C ATOM 864 N ILE A 156 43.625 20.225 26.693 1.00120.76 N ANISOU 864 N ILE A 156 14957 16307 14620 -677 382 -2770 N ATOM 865 CA ILE A 156 44.853 20.178 25.917 1.00121.29 C ANISOU 865 CA ILE A 156 14994 16516 14576 -604 451 -2801 C ATOM 866 C ILE A 156 45.397 18.754 25.820 1.00124.52 C ANISOU 866 C ILE A 156 15418 16742 15153 -570 603 -3040 C ATOM 867 O ILE A 156 45.762 18.295 24.738 1.00124.79 O ANISOU 867 O ILE A 156 15404 16933 15076 -570 669 -3254 O ATOM 868 CB ILE A 156 45.907 21.147 26.502 1.00123.98 C ANISOU 868 CB ILE A 156 15347 16858 14900 -514 429 -2494 C ATOM 869 CG1 ILE A 156 45.799 22.528 25.838 1.00124.36 C ANISOU 869 CG1 ILE A 156 15353 17205 14693 -535 324 -2329 C ATOM 870 CG2 ILE A 156 47.308 20.594 26.335 1.00129.04 C ANISOU 870 CG2 ILE A 156 15975 17462 15591 -416 549 -2534 C ATOM 871 CD1 ILE A 156 44.474 23.240 26.057 1.00121.44 C ANISOU 871 CD1 ILE A 156 14985 16879 14276 -607 195 -2248 C ATOM 872 N ARG A 157 45.457 18.040 26.944 1.00134.91 N ANISOU 872 N ARG A 157 16801 17722 16735 -535 667 -3004 N ATOM 873 CA ARG A 157 45.806 16.625 26.935 1.00144.73 C ANISOU 873 CA ARG A 157 18070 18741 18178 -503 818 -3227 C ATOM 874 C ARG A 157 44.539 15.814 26.705 1.00158.64 C ANISOU 874 C ARG A 157 19836 20417 20023 -632 841 -3492 C ATOM 875 O ARG A 157 43.561 15.958 27.446 1.00170.67 O ANISOU 875 O ARG A 157 21393 21822 21634 -702 784 -3417 O ATOM 876 CB ARG A 157 46.477 16.204 28.243 1.00137.96 C ANISOU 876 CB ARG A 157 17286 17563 17568 -394 881 -3048 C ATOM 877 CG ARG A 157 46.937 14.745 28.255 1.00145.68 C ANISOU 877 CG ARG A 157 18295 18285 18770 -334 1048 -3250 C ATOM 878 CD ARG A 157 48.214 14.544 27.434 1.00147.13 C ANISOU 878 CD ARG A 157 18420 18600 18883 -231 1129 -3339 C ATOM 879 NE ARG A 157 49.420 14.820 28.215 1.00151.36 N ANISOU 879 NE ARG A 157 18962 19060 19489 -79 1137 -3088 N ATOM 880 CZ ARG A 157 50.655 14.845 27.720 1.00155.94 C ANISOU 880 CZ ARG A 157 19478 19757 20013 27 1194 -3096 C ATOM 881 NH1 ARG A 157 50.869 14.617 26.430 1.00159.17 N ANISOU 881 NH1 ARG A 157 19822 20368 20286 -1 1256 -3338 N ATOM 882 NH2 ARG A 157 51.683 15.103 28.520 1.00151.20 N ANISOU 882 NH2 ARG A 157 18872 19089 19489 159 1189 -2868 N ATOM 883 N ASN A 158 44.566 14.961 25.682 1.00160.47 N ANISOU 883 N ASN A 158 20027 20713 20232 -667 929 -3814 N ATOM 884 CA ASN A 158 43.389 14.253 25.187 1.00161.82 C ANISOU 884 CA ASN A 158 20171 20876 20436 -810 946 -4121 C ATOM 885 C ASN A 158 42.316 15.242 24.742 1.00156.24 C ANISOU 885 C ASN A 158 19401 20467 19496 -913 778 -4089 C ATOM 886 O ASN A 158 41.236 15.298 25.348 1.00138.28 O ANISOU 886 O ASN A 158 17137 18089 17315 -999 723 -4063 O ATOM 887 CB ASN A 158 42.838 13.300 26.252 1.00162.80 C ANISOU 887 CB ASN A 158 20373 20595 20888 -846 1036 -4153 C ATOM 888 N PRO A 159 42.562 16.069 23.662 1.00162.27 N ANISOU 888 N PRO A 159 20093 21617 19945 -902 694 -4081 N ATOM 889 CA PRO A 159 41.542 16.953 23.123 1.00169.30 C ANISOU 889 CA PRO A 159 20916 22807 20603 -983 536 -4061 C ATOM 890 C PRO A 159 40.585 16.243 22.159 1.00175.29 C ANISOU 890 C PRO A 159 21595 23717 21289 -1111 534 -4443 C ATOM 891 O PRO A 159 40.398 16.651 21.014 1.00177.04 O ANISOU 891 O PRO A 159 21738 24307 21223 -1136 459 -4548 O ATOM 892 CB PRO A 159 42.366 18.032 22.402 1.00159.98 C ANISOU 892 CB PRO A 159 19705 21945 19136 -902 476 -3876 C ATOM 893 CG PRO A 159 43.542 17.281 21.903 1.00152.20 C ANISOU 893 CG PRO A 159 18722 20936 18171 -835 623 -4027 C ATOM 894 CD PRO A 159 43.848 16.221 22.942 1.00159.05 C ANISOU 894 CD PRO A 159 19664 21377 19392 -802 752 -4068 C ATOM 895 N ILE A 160 39.980 15.154 22.645 1.00178.74 N ANISOU 895 N ILE A 160 22053 23868 21991 -1194 621 -4654 N ATOM 896 CA ILE A 160 39.083 14.354 21.820 1.00181.20 C ANISOU 896 CA ILE A 160 22285 24283 22281 -1332 637 -5054 C ATOM 897 C ILE A 160 37.902 15.210 21.373 1.00183.84 C ANISOU 897 C ILE A 160 22523 24941 22388 -1413 450 -5042 C ATOM 898 O ILE A 160 37.555 16.213 22.010 1.00181.22 O ANISOU 898 O ILE A 160 22204 24628 22023 -1382 335 -4736 O ATOM 899 CB ILE A 160 38.616 13.103 22.588 1.00181.72 C ANISOU 899 CB ILE A 160 22399 23935 22712 -1414 775 -5239 C ATOM 900 CG1 ILE A 160 39.825 12.365 23.167 1.00176.39 C ANISOU 900 CG1 ILE A 160 21827 22921 22270 -1298 948 -5178 C ATOM 901 CG2 ILE A 160 37.831 12.148 21.687 1.00183.81 C ANISOU 901 CG2 ILE A 160 22575 24281 22983 -1567 820 -5702 C ATOM 902 CD1 ILE A 160 39.482 11.077 23.877 1.00175.00 C ANISOU 902 CD1 ILE A 160 21713 22316 22462 -1361 1108 -5346 C ATOM 903 N GLU A 161 37.303 14.823 20.244 1.00191.41 N ANISOU 903 N GLU A 161 23376 26168 23181 -1512 419 -5383 N ATOM 904 CA GLU A 161 36.130 15.511 19.723 1.00191.41 C ANISOU 904 CA GLU A 161 23263 26501 22962 -1587 239 -5414 C ATOM 905 C GLU A 161 35.030 15.547 20.773 1.00195.39 C ANISOU 905 C GLU A 161 23765 26783 23691 -1666 195 -5337 C ATOM 906 O GLU A 161 34.525 14.502 21.198 1.00201.13 O ANISOU 906 O GLU A 161 24495 27238 24687 -1776 301 -5569 O ATOM 907 CB GLU A 161 35.638 14.818 18.459 1.00188.10 C ANISOU 907 CB GLU A 161 22728 26360 22382 -1696 235 -5855 C ATOM 908 N HIS A 162 34.673 16.757 21.200 1.00192.69 N ANISOU 908 N HIS A 162 23418 26547 23249 -1611 51 -5008 N ATOM 909 CA HIS A 162 33.657 16.969 22.231 1.00184.13 C ANISOU 909 CA HIS A 162 22327 25278 22354 -1670 3 -4895 C ATOM 910 C HIS A 162 32.278 16.738 21.621 1.00176.33 C ANISOU 910 C HIS A 162 21186 24513 21297 -1810 -92 -5188 C ATOM 911 O HIS A 162 31.532 17.669 21.312 1.00177.06 O ANISOU 911 O HIS A 162 21186 24895 21195 -1799 -264 -5085 O ATOM 912 CB HIS A 162 33.781 18.372 22.807 1.00181.65 C ANISOU 912 CB HIS A 162 22052 25021 21947 -1557 -114 -4468 C ATOM 913 CG HIS A 162 34.181 19.403 21.793 1.00181.59 C ANISOU 913 CG HIS A 162 22002 25409 21587 -1465 -236 -4333 C ATOM 914 ND1 HIS A 162 35.476 19.541 21.336 1.00181.44 N ANISOU 914 ND1 HIS A 162 22044 25453 21443 -1367 -174 -4244 N ATOM 915 CD2 HIS A 162 33.456 20.346 21.146 1.00180.61 C ANISOU 915 CD2 HIS A 162 21779 25636 21209 -1451 -409 -4259 C ATOM 916 CE1 HIS A 162 35.532 20.523 20.454 1.00180.90 C ANISOU 916 CE1 HIS A 162 21923 25752 21057 -1306 -294 -4118 C ATOM 917 NE2 HIS A 162 34.319 21.029 20.321 1.00182.06 N ANISOU 917 NE2 HIS A 162 21977 26078 21118 -1349 -441 -4117 N ATOM 918 N SER A 163 31.933 15.463 21.461 1.00174.37 N ANISOU 918 N SER A 163 20906 24120 21226 -1943 24 -5563 N ATOM 919 CA SER A 163 30.740 15.042 20.736 1.00176.06 C ANISOU 919 CA SER A 163 20959 24559 21378 -2096 -46 -5923 C ATOM 920 C SER A 163 29.518 14.858 21.628 1.00180.91 C ANISOU 920 C SER A 163 21522 24978 22237 -2218 -52 -5953 C ATOM 921 O SER A 163 28.417 14.640 21.105 1.00184.43 O ANISOU 921 O SER A 163 21810 25630 22633 -2347 -131 -6229 O ATOM 922 CB SER A 163 31.017 13.728 19.987 1.00172.44 C ANISOU 922 CB SER A 163 20480 24060 20981 -2194 95 -6363 C ATOM 923 N ARG A 164 29.673 14.949 22.952 1.00175.33 N ANISOU 923 N ARG A 164 20934 23900 21782 -2181 28 -5682 N ATOM 924 CA ARG A 164 28.537 14.703 23.833 1.00164.99 C ANISOU 924 CA ARG A 164 19582 22391 20717 -2304 50 -5717 C ATOM 925 C ARG A 164 27.664 15.947 23.988 1.00169.89 C ANISOU 925 C ARG A 164 20106 23260 21185 -2268 -146 -5501 C ATOM 926 O ARG A 164 26.457 15.900 23.723 1.00168.88 O ANISOU 926 O ARG A 164 19819 23301 21048 -2386 -230 -5700 O ATOM 927 CB ARG A 164 29.021 14.196 25.197 1.00152.52 C ANISOU 927 CB ARG A 164 18170 20312 19467 -2284 230 -5532 C ATOM 928 CG ARG A 164 30.198 14.952 25.800 1.00145.51 C ANISOU 928 CG ARG A 164 17432 19327 18527 -2094 229 -5125 C ATOM 929 CD ARG A 164 30.519 14.431 27.196 1.00136.90 C ANISOU 929 CD ARG A 164 16491 17772 17752 -2081 392 -4952 C ATOM 930 N PHE A 165 28.254 17.071 24.400 1.00179.01 N ANISOU 930 N PHE A 165 21344 24444 22226 -2107 -221 -5104 N ATOM 931 CA PHE A 165 27.491 18.277 24.693 1.00184.75 C ANISOU 931 CA PHE A 165 22000 25345 22852 -2057 -385 -4867 C ATOM 932 C PHE A 165 28.244 19.509 24.206 1.00185.88 C ANISOU 932 C PHE A 165 22178 25740 22707 -1882 -510 -4569 C ATOM 933 O PHE A 165 29.456 19.476 23.978 1.00194.02 O ANISOU 933 O PHE A 165 23317 26734 23669 -1795 -446 -4480 O ATOM 934 CB PHE A 165 27.196 18.402 26.196 1.00182.82 C ANISOU 934 CB PHE A 165 21836 24748 22878 -2066 -311 -4649 C ATOM 935 CG PHE A 165 26.709 17.128 26.825 1.00185.60 C ANISOU 935 CG PHE A 165 22200 24773 23544 -2226 -139 -4884 C ATOM 936 CD1 PHE A 165 25.423 16.670 26.589 1.00187.19 C ANISOU 936 CD1 PHE A 165 22241 25064 23820 -2389 -162 -5174 C ATOM 937 CD2 PHE A 165 27.540 16.384 27.648 1.00183.52 C ANISOU 937 CD2 PHE A 165 22105 24116 23508 -2212 48 -4812 C ATOM 938 CE1 PHE A 165 24.974 15.493 27.162 1.00183.54 C ANISOU 938 CE1 PHE A 165 21790 24284 23662 -2549 13 -5390 C ATOM 939 CE2 PHE A 165 27.095 15.206 28.224 1.00181.48 C ANISOU 939 CE2 PHE A 165 21869 23539 23548 -2355 220 -5009 C ATOM 940 CZ PHE A 165 25.811 14.761 27.981 1.00180.24 C ANISOU 940 CZ PHE A 165 21556 23456 23473 -2531 209 -5299 C ATOM 941 N ASN A 166 27.502 20.604 24.051 1.00179.70 N ANISOU 941 N ASN A 166 21299 25212 21769 -1831 -682 -4414 N ATOM 942 CA ASN A 166 28.083 21.874 23.643 1.00170.10 C ANISOU 942 CA ASN A 166 20112 24218 20298 -1670 -800 -4105 C ATOM 943 C ASN A 166 28.904 22.471 24.787 1.00159.70 C ANISOU 943 C ASN A 166 18957 22604 19119 -1571 -730 -3748 C ATOM 944 O ASN A 166 28.814 22.048 25.942 1.00160.31 O ANISOU 944 O ASN A 166 19105 22343 19464 -1619 -624 -3716 O ATOM 945 CB ASN A 166 26.985 22.844 23.203 1.00169.17 C ANISOU 945 CB ASN A 166 19843 24430 20005 -1636 -998 -4037 C ATOM 946 CG ASN A 166 27.536 24.101 22.547 1.00161.63 C ANISOU 946 CG ASN A 166 18907 23743 18760 -1473 -1117 -3744 C ATOM 947 OD1 ASN A 166 28.554 24.059 21.855 1.00155.73 O ANISOU 947 OD1 ASN A 166 18227 23097 17847 -1419 -1082 -3725 O ATOM 948 ND2 ASN A 166 26.868 25.226 22.770 1.00159.46 N ANISOU 948 ND2 ASN A 166 18577 23576 18436 -1393 -1249 -3511 N ATOM 949 N SER A 167 29.716 23.476 24.451 1.00153.16 N ANISOU 949 N SER A 167 18184 21915 18096 -1436 -790 -3479 N ATOM 950 CA SER A 167 30.597 24.079 25.446 1.00140.08 C ANISOU 950 CA SER A 167 16669 20007 16548 -1345 -730 -3159 C ATOM 951 C SER A 167 29.807 24.838 26.507 1.00145.46 C ANISOU 951 C SER A 167 17342 20559 17366 -1333 -782 -2963 C ATOM 952 O SER A 167 30.167 24.810 27.690 1.00139.04 O ANISOU 952 O SER A 167 16634 19440 16755 -1326 -692 -2822 O ATOM 953 CB SER A 167 31.606 25.000 24.760 1.00129.07 C ANISOU 953 CB SER A 167 15319 18807 14914 -1220 -776 -2935 C ATOM 954 OG SER A 167 32.655 25.354 25.644 1.00127.91 O ANISOU 954 OG SER A 167 15306 18411 14883 -1151 -693 -2688 O ATOM 955 N ARG A 168 28.731 25.525 26.107 1.00171.26 N ANISOU 955 N ARG A 168 20481 24066 20523 -1325 -928 -2953 N ATOM 956 CA ARG A 168 27.924 26.268 27.071 1.00174.82 C ANISOU 956 CA ARG A 168 20910 24408 21106 -1308 -975 -2783 C ATOM 957 C ARG A 168 27.310 25.337 28.110 1.00168.25 C ANISOU 957 C ARG A 168 20083 23289 20556 -1433 -865 -2941 C ATOM 958 O ARG A 168 27.389 25.595 29.316 1.00167.79 O ANISOU 958 O ARG A 168 20109 22971 20673 -1419 -801 -2770 O ATOM 959 CB ARG A 168 26.824 27.055 26.355 1.00180.43 C ANISOU 959 CB ARG A 168 21460 25445 21650 -1271 -1152 -2777 C ATOM 960 CG ARG A 168 27.288 28.284 25.591 1.00181.28 C ANISOU 960 CG ARG A 168 21575 25798 21505 -1124 -1265 -2520 C ATOM 961 CD ARG A 168 26.089 29.147 25.214 1.00180.40 C ANISOU 961 CD ARG A 168 21313 25941 21290 -1067 -1434 -2460 C ATOM 962 NE ARG A 168 26.430 30.172 24.235 1.00181.46 N ANISOU 962 NE ARG A 168 21438 26357 21151 -930 -1545 -2249 N ATOM 963 CZ ARG A 168 26.414 29.976 22.922 1.00190.55 C ANISOU 963 CZ ARG A 168 22511 27854 22035 -917 -1625 -2373 C ATOM 964 NH1 ARG A 168 26.074 28.790 22.434 1.00193.82 N ANISOU 964 NH1 ARG A 168 22844 28369 22431 -1038 -1608 -2729 N ATOM 965 NH2 ARG A 168 26.740 30.961 22.097 1.00195.75 N ANISOU 965 NH2 ARG A 168 23175 28757 22445 -785 -1715 -2142 N ATOM 966 N THR A 169 26.687 24.246 27.658 1.00149.91 N ANISOU 966 N THR A 169 17669 21011 18278 -1560 -834 -3271 N ATOM 967 CA THR A 169 26.012 23.347 28.587 1.00135.46 C ANISOU 967 CA THR A 169 15834 18912 16722 -1692 -718 -3426 C ATOM 968 C THR A 169 26.994 22.471 29.358 1.00126.13 C ANISOU 968 C THR A 169 14822 17374 15727 -1715 -532 -3412 C ATOM 969 O THR A 169 26.728 22.126 30.518 1.00110.12 O ANISOU 969 O THR A 169 12852 15061 13926 -1767 -427 -3368 O ATOM 970 CB THR A 169 24.994 22.482 27.837 1.00135.91 C ANISOU 970 CB THR A 169 15727 19132 16782 -1834 -741 -3798 C ATOM 971 OG1 THR A 169 24.347 21.593 28.756 1.00141.70 O ANISOU 971 OG1 THR A 169 16458 19582 17799 -1975 -608 -3944 O ATOM 972 CG2 THR A 169 25.671 21.675 26.735 1.00134.05 C ANISOU 972 CG2 THR A 169 15496 19016 16420 -1863 -708 -4030 C ATOM 973 N LYS A 170 28.125 22.102 28.745 1.00125.91 N ANISOU 973 N LYS A 170 14871 17365 15605 -1668 -486 -3441 N ATOM 974 CA LYS A 170 29.144 21.359 29.477 1.00111.41 C ANISOU 974 CA LYS A 170 13192 15202 13939 -1657 -320 -3393 C ATOM 975 C LYS A 170 29.718 22.188 30.617 1.00106.47 C ANISOU 975 C LYS A 170 12683 14399 13371 -1554 -309 -3047 C ATOM 976 O LYS A 170 30.117 21.635 31.649 1.00101.09 O ANISOU 976 O LYS A 170 12113 13411 12884 -1562 -181 -2982 O ATOM 977 CB LYS A 170 30.257 20.913 28.528 1.00105.25 C ANISOU 977 CB LYS A 170 12451 14508 13030 -1612 -282 -3488 C ATOM 978 N ALA A 171 29.762 23.513 30.453 1.00109.99 N ANISOU 978 N ALA A 171 13104 15035 13652 -1457 -441 -2824 N ATOM 979 CA ALA A 171 30.224 24.375 31.534 1.00103.74 C ANISOU 979 CA ALA A 171 12410 14090 12918 -1371 -437 -2519 C ATOM 980 C ALA A 171 29.258 24.346 32.711 1.00111.69 C ANISOU 980 C ALA A 171 13410 14910 14117 -1435 -401 -2493 C ATOM 981 O ALA A 171 29.682 24.408 33.870 1.00118.34 O ANISOU 981 O ALA A 171 14360 15518 15085 -1408 -325 -2328 O ATOM 982 CB ALA A 171 30.408 25.801 31.021 1.00 94.84 C ANISOU 982 CB ALA A 171 11250 13200 11586 -1263 -577 -2306 C ATOM 983 N ILE A 172 27.957 24.232 32.431 1.00118.09 N ANISOU 983 N ILE A 172 14086 15835 14946 -1523 -453 -2661 N ATOM 984 CA ILE A 172 26.946 24.272 33.487 1.00111.42 C ANISOU 984 CA ILE A 172 13214 14845 14275 -1588 -418 -2645 C ATOM 985 C ILE A 172 27.139 23.123 34.470 1.00109.42 C ANISOU 985 C ILE A 172 13067 14260 14248 -1668 -236 -2702 C ATOM 986 O ILE A 172 27.003 23.301 35.686 1.00107.12 O ANISOU 986 O ILE A 172 12844 13773 14084 -1667 -172 -2555 O ATOM 987 CB ILE A 172 25.533 24.257 32.875 1.00107.78 C ANISOU 987 CB ILE A 172 12564 14594 13792 -1673 -505 -2850 C ATOM 988 CG1 ILE A 172 25.326 25.482 31.984 1.00110.38 C ANISOU 988 CG1 ILE A 172 12795 15251 13894 -1568 -691 -2746 C ATOM 989 CG2 ILE A 172 24.476 24.221 33.967 1.00 89.37 C ANISOU 989 CG2 ILE A 172 10193 12109 11654 -1752 -450 -2853 C ATOM 990 CD1 ILE A 172 25.392 26.793 32.734 1.00111.51 C ANISOU 990 CD1 ILE A 172 12981 15356 14032 -1456 -745 -2445 C ATOM 991 N MET A 173 27.446 21.926 33.964 1.00115.12 N ANISOU 991 N MET A 173 13806 14910 15023 -1736 -144 -2916 N ATOM 992 CA MET A 173 27.689 20.802 34.863 1.00115.75 C ANISOU 992 CA MET A 173 14000 14655 15327 -1798 40 -2952 C ATOM 993 C MET A 173 28.956 21.015 35.682 1.00116.97 C ANISOU 993 C MET A 173 14320 14630 15494 -1675 94 -2689 C ATOM 994 O MET A 173 28.987 20.704 36.878 1.00111.23 O ANISOU 994 O MET A 173 13688 13652 14920 -1684 202 -2575 O ATOM 995 CB MET A 173 27.768 19.497 34.072 1.00125.28 C ANISOU 995 CB MET A 173 15186 15816 16598 -1891 130 -3249 C ATOM 996 CG MET A 173 26.419 18.823 33.854 1.00153.92 C ANISOU 996 CG MET A 173 18680 19458 20344 -2065 163 -3533 C ATOM 997 SD MET A 173 25.792 17.952 35.313 1.00167.09 S ANISOU 997 SD MET A 173 20422 20737 22328 -2184 365 -3521 S ATOM 998 CE MET A 173 26.500 16.318 35.086 1.00162.90 C ANISOU 998 CE MET A 173 19993 19927 21974 -2245 562 -3722 C ATOM 999 N LYS A 174 30.009 21.552 35.058 1.00116.93 N ANISOU 999 N LYS A 174 14344 14763 15321 -1561 21 -2589 N ATOM 1000 CA LYS A 174 31.253 21.793 35.781 1.00105.45 C ANISOU 1000 CA LYS A 174 13026 13170 13872 -1445 61 -2353 C ATOM 1001 C LYS A 174 31.068 22.856 36.857 1.00102.19 C ANISOU 1001 C LYS A 174 12645 12724 13461 -1397 13 -2106 C ATOM 1002 O LYS A 174 31.662 22.764 37.938 1.00109.56 O ANISOU 1002 O LYS A 174 13689 13461 14477 -1349 85 -1944 O ATOM 1003 CB LYS A 174 32.355 22.193 34.801 1.00 90.94 C ANISOU 1003 CB LYS A 174 11189 11512 11851 -1347 -5 -2316 C ATOM 1004 CG LYS A 174 32.633 21.144 33.733 1.00 96.78 C ANISOU 1004 CG LYS A 174 11901 12292 12578 -1386 51 -2571 C ATOM 1005 CD LYS A 174 33.391 21.742 32.558 1.00106.90 C ANISOU 1005 CD LYS A 174 13144 13842 13630 -1308 -39 -2558 C ATOM 1006 CE LYS A 174 33.458 20.775 31.386 1.00111.46 C ANISOU 1006 CE LYS A 174 13670 14513 14166 -1362 4 -2851 C ATOM 1007 NZ LYS A 174 34.026 21.424 30.171 1.00115.92 N ANISOU 1007 NZ LYS A 174 14183 15386 14477 -1296 -89 -2843 N ATOM 1008 N ILE A 175 30.251 23.873 36.583 1.00 92.45 N ANISOU 1008 N ILE A 175 11309 11683 12133 -1402 -109 -2077 N ATOM 1009 CA ILE A 175 29.947 24.852 37.619 1.00106.17 C ANISOU 1009 CA ILE A 175 13068 13378 13895 -1367 -142 -1875 C ATOM 1010 C ILE A 175 29.109 24.214 38.722 1.00105.22 C ANISOU 1010 C ILE A 175 12970 13049 13960 -1459 -30 -1916 C ATOM 1011 O ILE A 175 29.206 24.604 39.892 1.00109.11 O ANISOU 1011 O ILE A 175 13536 13414 14508 -1429 6 -1747 O ATOM 1012 CB ILE A 175 29.254 26.080 36.998 1.00107.19 C ANISOU 1012 CB ILE A 175 13079 13757 13893 -1339 -293 -1837 C ATOM 1013 CG1 ILE A 175 30.149 26.711 35.928 1.00103.24 C ANISOU 1013 CG1 ILE A 175 12571 13453 13201 -1247 -386 -1768 C ATOM 1014 CG2 ILE A 175 28.914 27.108 38.065 1.00104.60 C ANISOU 1014 CG2 ILE A 175 12767 13371 13604 -1302 -318 -1648 C ATOM 1015 CD1 ILE A 175 29.505 27.868 35.198 1.00112.73 C ANISOU 1015 CD1 ILE A 175 13663 14905 14265 -1205 -532 -1716 C ATOM 1016 N ALA A 176 28.298 23.210 38.381 1.00 99.06 N ANISOU 1016 N ALA A 176 12127 12231 13279 -1578 36 -2146 N ATOM 1017 CA ALA A 176 27.481 22.552 39.395 1.00 97.26 C ANISOU 1017 CA ALA A 176 11918 11797 13238 -1679 162 -2188 C ATOM 1018 C ALA A 176 28.337 21.741 40.360 1.00 95.77 C ANISOU 1018 C ALA A 176 11894 11329 13164 -1653 310 -2079 C ATOM 1019 O ALA A 176 28.056 21.706 41.563 1.00 93.81 O ANISOU 1019 O ALA A 176 11710 10921 13011 -1671 393 -1964 O ATOM 1020 CB ALA A 176 26.428 21.665 38.731 1.00 79.70 C ANISOU 1020 CB ALA A 176 9576 9603 11105 -1827 202 -2477 C ATOM 1021 N ILE A 177 29.388 21.085 39.860 1.00 92.33 N ANISOU 1021 N ILE A 177 11527 10839 12715 -1603 347 -2109 N ATOM 1022 CA ILE A 177 30.216 20.283 40.755 1.00105.35 C ANISOU 1022 CA ILE A 177 13327 12225 14476 -1558 484 -1997 C ATOM 1023 C ILE A 177 31.066 21.172 41.661 1.00 99.31 C ANISOU 1023 C ILE A 177 12650 11456 13627 -1430 436 -1719 C ATOM 1024 O ILE A 177 31.352 20.799 42.804 1.00 97.89 O ANISOU 1024 O ILE A 177 12580 11083 13531 -1403 533 -1580 O ATOM 1025 CB ILE A 177 31.085 19.284 39.964 1.00110.72 C ANISOU 1025 CB ILE A 177 14046 12838 15185 -1532 545 -2122 C ATOM 1026 CG1 ILE A 177 32.265 19.991 39.288 1.00132.40 C ANISOU 1026 CG1 ILE A 177 16793 15762 17751 -1402 433 -2032 C ATOM 1027 CG2 ILE A 177 30.246 18.544 38.935 1.00101.60 C ANISOU 1027 CG2 ILE A 177 12784 11734 14086 -1665 572 -2430 C ATOM 1028 CD1 ILE A 177 33.352 19.050 38.819 1.00144.35 C ANISOU 1028 CD1 ILE A 177 18368 17176 19303 -1342 513 -2097 C ATOM 1029 N VAL A 178 31.472 22.357 41.196 1.00 85.64 N ANISOU 1029 N VAL A 178 10871 9938 11730 -1353 290 -1632 N ATOM 1030 CA VAL A 178 32.277 23.209 42.066 1.00101.40 C ANISOU 1030 CA VAL A 178 12941 11928 13659 -1248 250 -1392 C ATOM 1031 C VAL A 178 31.410 23.851 43.142 1.00107.75 C ANISOU 1031 C VAL A 178 13742 12702 14495 -1284 251 -1298 C ATOM 1032 O VAL A 178 31.902 24.164 44.232 1.00119.44 O ANISOU 1032 O VAL A 178 15307 14103 15971 -1226 272 -1124 O ATOM 1033 CB VAL A 178 33.056 24.265 41.258 1.00107.28 C ANISOU 1033 CB VAL A 178 13643 12885 14236 -1161 115 -1323 C ATOM 1034 CG1 VAL A 178 33.880 23.603 40.164 1.00110.08 C ANISOU 1034 CG1 VAL A 178 13992 13283 14550 -1130 126 -1431 C ATOM 1035 CG2 VAL A 178 32.126 25.315 40.678 1.00116.51 C ANISOU 1035 CG2 VAL A 178 14696 14254 15320 -1194 -2 -1356 C ATOM 1036 N TRP A 179 30.117 24.045 42.873 1.00107.91 N ANISOU 1036 N TRP A 179 13658 12797 14546 -1378 229 -1420 N ATOM 1037 CA TRP A 179 29.209 24.493 43.921 1.00103.56 C ANISOU 1037 CA TRP A 179 13099 12201 14050 -1422 258 -1357 C ATOM 1038 C TRP A 179 28.733 23.335 44.788 1.00100.22 C ANISOU 1038 C TRP A 179 12742 11554 13784 -1507 428 -1393 C ATOM 1039 O TRP A 179 28.506 23.522 45.988 1.00 95.43 O ANISOU 1039 O TRP A 179 12193 10855 13209 -1509 489 -1272 O ATOM 1040 CB TRP A 179 28.011 25.224 43.313 1.00 98.35 C ANISOU 1040 CB TRP A 179 12286 11720 13364 -1477 165 -1464 C ATOM 1041 CG TRP A 179 28.338 26.602 42.825 1.00100.64 C ANISOU 1041 CG TRP A 179 12528 12202 13511 -1383 13 -1363 C ATOM 1042 CD1 TRP A 179 28.493 26.998 41.529 1.00105.45 C ANISOU 1042 CD1 TRP A 179 13056 13001 14009 -1349 -101 -1420 C ATOM 1043 CD2 TRP A 179 28.559 27.768 43.629 1.00100.54 C ANISOU 1043 CD2 TRP A 179 12546 12200 13454 -1313 -32 -1186 C ATOM 1044 NE1 TRP A 179 28.792 28.337 41.474 1.00104.71 N ANISOU 1044 NE1 TRP A 179 12948 13023 13814 -1260 -208 -1272 N ATOM 1045 CE2 TRP A 179 28.839 28.834 42.750 1.00104.94 C ANISOU 1045 CE2 TRP A 179 13043 12938 13892 -1241 -167 -1137 C ATOM 1046 CE3 TRP A 179 28.544 28.015 45.006 1.00103.82 C ANISOU 1046 CE3 TRP A 179 13036 12495 13915 -1307 33 -1068 C ATOM 1047 CZ2 TRP A 179 29.104 30.127 43.202 1.00 89.33 C ANISOU 1047 CZ2 TRP A 179 11077 10999 11866 -1168 -231 -982 C ATOM 1048 CZ3 TRP A 179 28.808 29.300 45.453 1.00108.31 C ANISOU 1048 CZ3 TRP A 179 13611 13123 14421 -1236 -39 -933 C ATOM 1049 CH2 TRP A 179 29.084 30.338 44.553 1.00104.14 C ANISOU 1049 CH2 TRP A 179 13021 12750 13799 -1171 -166 -894 C ATOM 1050 N ALA A 180 28.583 22.141 44.205 1.00106.15 N ANISOU 1050 N ALA A 180 13488 12212 14635 -1580 513 -1559 N ATOM 1051 CA ALA A 180 28.200 20.974 44.993 1.00 99.63 C ANISOU 1051 CA ALA A 180 12736 11141 13977 -1663 695 -1582 C ATOM 1052 C ALA A 180 29.254 20.649 46.043 1.00 91.01 C ANISOU 1052 C ALA A 180 11810 9879 12890 -1562 772 -1367 C ATOM 1053 O ALA A 180 28.921 20.376 47.202 1.00 84.47 O ANISOU 1053 O ALA A 180 11057 8908 12131 -1588 884 -1261 O ATOM 1054 CB ALA A 180 27.964 19.772 44.078 1.00 83.90 C ANISOU 1054 CB ALA A 180 10708 9072 12100 -1756 773 -1814 C ATOM 1055 N ILE A 181 30.531 20.676 45.656 1.00 86.18 N ANISOU 1055 N ILE A 181 11252 9295 12199 -1442 715 -1296 N ATOM 1056 CA ILE A 181 31.600 20.452 46.622 1.00 86.58 C ANISOU 1056 CA ILE A 181 11440 9220 12236 -1326 764 -1087 C ATOM 1057 C ILE A 181 31.632 21.576 47.650 1.00 73.58 C ANISOU 1057 C ILE A 181 9814 7660 10483 -1276 698 -904 C ATOM 1058 O ILE A 181 31.820 21.332 48.847 1.00 85.77 O ANISOU 1058 O ILE A 181 11460 9085 12043 -1242 778 -750 O ATOM 1059 CB ILE A 181 32.954 20.306 45.904 1.00 94.62 C ANISOU 1059 CB ILE A 181 12482 10276 13191 -1209 708 -1070 C ATOM 1060 CG1 ILE A 181 32.920 19.143 44.912 1.00 99.19 C ANISOU 1060 CG1 ILE A 181 13045 10761 13884 -1260 789 -1272 C ATOM 1061 CG2 ILE A 181 34.073 20.091 46.914 1.00 85.91 C ANISOU 1061 CG2 ILE A 181 11503 9066 12072 -1078 745 -853 C ATOM 1062 CD1 ILE A 181 34.116 19.100 43.986 1.00 92.13 C ANISOU 1062 CD1 ILE A 181 12142 9949 12916 -1157 727 -1300 C ATOM 1063 N SER A 182 31.439 22.820 47.206 1.00 72.32 N ANISOU 1063 N SER A 182 9559 7707 10212 -1269 557 -920 N ATOM 1064 CA SER A 182 31.542 23.958 48.116 1.00 95.45 C ANISOU 1064 CA SER A 182 12502 10717 13046 -1220 493 -767 C ATOM 1065 C SER A 182 30.461 23.905 49.189 1.00 97.63 C ANISOU 1065 C SER A 182 12794 10914 13387 -1301 588 -747 C ATOM 1066 O SER A 182 30.742 24.097 50.378 1.00 90.79 O ANISOU 1066 O SER A 182 12011 10003 12481 -1258 625 -596 O ATOM 1067 CB SER A 182 31.465 25.265 47.328 1.00 83.19 C ANISOU 1067 CB SER A 182 10842 9376 11390 -1201 338 -798 C ATOM 1068 OG SER A 182 32.591 25.405 46.480 1.00 85.36 O ANISOU 1068 OG SER A 182 11115 9730 11587 -1120 259 -783 O ATOM 1069 N ILE A 183 29.215 23.648 48.784 1.00 99.34 N ANISOU 1069 N ILE A 183 12922 11128 13695 -1420 631 -904 N ATOM 1070 CA ILE A 183 28.137 23.444 49.750 1.00102.76 C ANISOU 1070 CA ILE A 183 13360 11475 14209 -1513 748 -903 C ATOM 1071 C ILE A 183 28.451 22.260 50.654 1.00103.81 C ANISOU 1071 C ILE A 183 13634 11387 14420 -1516 916 -806 C ATOM 1072 O ILE A 183 28.163 22.282 51.858 1.00 94.35 O ANISOU 1072 O ILE A 183 12503 10127 13219 -1527 1004 -690 O ATOM 1073 CB ILE A 183 26.796 23.248 49.017 1.00105.09 C ANISOU 1073 CB ILE A 183 13513 11811 14604 -1647 766 -1114 C ATOM 1074 CG1 ILE A 183 26.472 24.471 48.160 1.00102.51 C ANISOU 1074 CG1 ILE A 183 13048 11714 14189 -1621 593 -1181 C ATOM 1075 CG2 ILE A 183 25.674 22.970 50.009 1.00 75.13 C ANISOU 1075 CG2 ILE A 183 9715 7923 10908 -1754 907 -1122 C ATOM 1076 CD1 ILE A 183 25.319 24.256 47.212 1.00 74.27 C ANISOU 1076 CD1 ILE A 183 9315 8220 10685 -1729 576 -1398 C ATOM 1077 N GLY A 184 29.046 21.206 50.089 1.00 75.19 N ANISOU 1077 N GLY A 184 10060 7642 10867 -1500 968 -846 N ATOM 1078 CA GLY A 184 29.352 20.026 50.878 1.00 82.65 C ANISOU 1078 CA GLY A 184 11144 8355 11905 -1491 1134 -743 C ATOM 1079 C GLY A 184 30.356 20.290 51.983 1.00 90.82 C ANISOU 1079 C GLY A 184 12301 9381 12825 -1353 1122 -499 C ATOM 1080 O GLY A 184 30.297 19.663 53.044 1.00 88.89 O ANISOU 1080 O GLY A 184 12167 8989 12617 -1349 1257 -365 O ATOM 1081 N VAL A 185 31.283 21.220 51.759 1.00 92.58 N ANISOU 1081 N VAL A 185 12504 9769 12905 -1242 963 -437 N ATOM 1082 CA VAL A 185 32.275 21.523 52.784 1.00 84.54 C ANISOU 1082 CA VAL A 185 11582 8773 11768 -1115 935 -227 C ATOM 1083 C VAL A 185 31.688 22.440 53.852 1.00 84.93 C ANISOU 1083 C VAL A 185 11627 8914 11728 -1142 925 -153 C ATOM 1084 O VAL A 185 32.021 22.322 55.036 1.00 73.91 O ANISOU 1084 O VAL A 185 10330 7485 10266 -1086 977 12 O ATOM 1085 CB VAL A 185 33.535 22.126 52.136 1.00 81.28 C ANISOU 1085 CB VAL A 185 11137 8495 11249 -997 781 -203 C ATOM 1086 CG1 VAL A 185 34.582 22.452 53.191 1.00 76.33 C ANISOU 1086 CG1 VAL A 185 10589 7912 10499 -870 740 -4 C ATOM 1087 CG2 VAL A 185 34.094 21.161 51.113 1.00 78.59 C ANISOU 1087 CG2 VAL A 185 10799 8062 10997 -968 809 -287 C ATOM 1088 N SER A 186 30.798 23.355 53.462 1.00 83.73 N ANISOU 1088 N SER A 186 11359 8884 11569 -1223 861 -274 N ATOM 1089 CA SER A 186 30.276 24.349 54.392 1.00 83.08 C ANISOU 1089 CA SER A 186 11261 8900 11406 -1242 844 -226 C ATOM 1090 C SER A 186 29.040 23.885 55.152 1.00 97.44 C ANISOU 1090 C SER A 186 13092 10625 13306 -1354 1002 -246 C ATOM 1091 O SER A 186 28.738 24.449 56.209 1.00104.20 O ANISOU 1091 O SER A 186 13972 11532 14088 -1356 1030 -173 O ATOM 1092 CB SER A 186 29.952 25.648 53.648 1.00 83.71 C ANISOU 1092 CB SER A 186 11208 9153 11446 -1255 699 -331 C ATOM 1093 OG SER A 186 28.952 25.444 52.660 1.00 91.97 O ANISOU 1093 OG SER A 186 12146 10201 12597 -1352 707 -503 O ATOM 1094 N VAL A 187 28.332 22.872 54.661 1.00106.43 N ANISOU 1094 N VAL A 187 14212 11629 14596 -1453 1114 -351 N ATOM 1095 CA VAL A 187 27.070 22.454 55.272 1.00105.56 C ANISOU 1095 CA VAL A 187 14090 11434 14584 -1582 1273 -392 C ATOM 1096 C VAL A 187 27.239 21.746 56.621 1.00107.83 C ANISOU 1096 C VAL A 187 14531 11587 14851 -1564 1433 -205 C ATOM 1097 O VAL A 187 26.296 21.786 57.425 1.00114.66 O ANISOU 1097 O VAL A 187 15392 12438 15735 -1651 1550 -198 O ATOM 1098 CB VAL A 187 26.249 21.593 54.290 1.00 99.10 C ANISOU 1098 CB VAL A 187 13190 10520 13945 -1710 1346 -584 C ATOM 1099 CG1 VAL A 187 26.720 20.146 54.264 1.00 90.94 C ANISOU 1099 CG1 VAL A 187 12273 9258 13023 -1712 1483 -541 C ATOM 1100 CG2 VAL A 187 24.762 21.683 54.613 1.00 88.13 C ANISOU 1100 CG2 VAL A 187 11704 9135 12645 -1857 1447 -693 C ATOM 1101 N PRO A 188 28.369 21.098 56.953 1.00100.74 N ANISOU 1101 N PRO A 188 13767 10599 13911 -1450 1452 -44 N ATOM 1102 CA PRO A 188 28.490 20.566 58.323 1.00 91.53 C ANISOU 1102 CA PRO A 188 12745 9340 12693 -1418 1592 160 C ATOM 1103 C PRO A 188 28.616 21.648 59.381 1.00 93.91 C ANISOU 1103 C PRO A 188 13059 9821 12802 -1363 1528 261 C ATOM 1104 O PRO A 188 28.285 21.391 60.546 1.00 80.28 O ANISOU 1104 O PRO A 188 11420 8060 11023 -1379 1658 387 O ATOM 1105 CB PRO A 188 29.759 19.700 58.264 1.00 79.56 C ANISOU 1105 CB PRO A 188 11347 7708 11176 -1282 1593 301 C ATOM 1106 CG PRO A 188 29.980 19.430 56.826 1.00 83.19 C ANISOU 1106 CG PRO A 188 11726 8133 11750 -1297 1523 132 C ATOM 1107 CD PRO A 188 29.513 20.660 56.130 1.00 85.79 C ANISOU 1107 CD PRO A 188 11902 8666 12029 -1349 1372 -35 C ATOM 1108 N ILE A 189 29.061 22.845 59.012 1.00 97.18 N ANISOU 1108 N ILE A 189 13391 10421 13111 -1307 1342 204 N ATOM 1109 CA ILE A 189 29.442 23.883 59.969 1.00 96.91 C ANISOU 1109 CA ILE A 189 13374 10555 12891 -1239 1265 290 C ATOM 1110 C ILE A 189 28.251 24.407 60.768 1.00 93.27 C ANISOU 1110 C ILE A 189 12878 10149 12413 -1339 1355 245 C ATOM 1111 O ILE A 189 28.382 24.577 61.989 1.00 84.83 O ANISOU 1111 O ILE A 189 11888 9136 11206 -1304 1405 368 O ATOM 1112 CB ILE A 189 30.193 25.018 59.254 1.00 88.91 C ANISOU 1112 CB ILE A 189 12275 9701 11807 -1169 1057 223 C ATOM 1113 CG1 ILE A 189 31.589 24.531 58.861 1.00 93.09 C ANISOU 1113 CG1 ILE A 189 12862 10206 12304 -1045 981 315 C ATOM 1114 CG2 ILE A 189 30.291 26.250 60.138 1.00 73.17 C ANISOU 1114 CG2 ILE A 189 10265 7876 9658 -1141 987 247 C ATOM 1115 CD1 ILE A 189 32.100 25.105 57.569 1.00111.48 C ANISOU 1115 CD1 ILE A 189 15091 12609 14657 -1020 830 204 C ATOM 1116 N PRO A 190 27.084 24.682 60.170 1.00105.80 N ANISOU 1116 N PRO A 190 14340 11735 14122 -1457 1380 72 N ATOM 1117 CA PRO A 190 25.937 25.059 61.014 1.00102.03 C ANISOU 1117 CA PRO A 190 13827 11298 13639 -1549 1492 35 C ATOM 1118 C PRO A 190 25.552 23.978 62.005 1.00104.45 C ANISOU 1118 C PRO A 190 14252 11474 13960 -1601 1708 160 C ATOM 1119 O PRO A 190 25.096 24.298 63.108 1.00101.87 O ANISOU 1119 O PRO A 190 13955 11210 13539 -1625 1798 212 O ATOM 1120 CB PRO A 190 24.818 25.322 59.996 1.00 99.40 C ANISOU 1120 CB PRO A 190 13328 10974 13466 -1657 1475 -175 C ATOM 1121 CG PRO A 190 25.533 25.676 58.743 1.00102.22 C ANISOU 1121 CG PRO A 190 13626 11379 13836 -1591 1294 -241 C ATOM 1122 CD PRO A 190 26.751 24.799 58.738 1.00110.44 C ANISOU 1122 CD PRO A 190 14799 12323 14839 -1504 1293 -103 C ATOM 1123 N VAL A 191 25.732 22.706 61.644 1.00105.18 N ANISOU 1123 N VAL A 191 14416 11379 14169 -1618 1803 211 N ATOM 1124 CA VAL A 191 25.447 21.611 62.569 1.00 97.89 C ANISOU 1124 CA VAL A 191 13623 10302 13271 -1659 2022 359 C ATOM 1125 C VAL A 191 26.445 21.624 63.717 1.00 96.44 C ANISOU 1125 C VAL A 191 13589 10177 12876 -1519 2013 595 C ATOM 1126 O VAL A 191 26.062 21.691 64.892 1.00107.03 O ANISOU 1126 O VAL A 191 14994 11565 14107 -1538 2128 698 O ATOM 1127 CB VAL A 191 25.451 20.256 61.832 1.00 95.93 C ANISOU 1127 CB VAL A 191 13412 9814 13222 -1706 2126 347 C ATOM 1128 CG1 VAL A 191 25.422 19.105 62.823 1.00 95.69 C ANISOU 1128 CG1 VAL A 191 13547 9601 13210 -1714 2349 552 C ATOM 1129 CG2 VAL A 191 24.275 20.160 60.876 1.00 92.47 C ANISOU 1129 CG2 VAL A 191 12818 9332 12984 -1870 2166 103 C ATOM 1130 N ILE A 192 27.740 21.564 63.387 1.00 87.35 N ANISOU 1130 N ILE A 192 12488 9042 11658 -1376 1874 678 N ATOM 1131 CA ILE A 192 28.790 21.508 64.402 1.00 93.99 C ANISOU 1131 CA ILE A 192 13460 9955 12298 -1228 1845 901 C ATOM 1132 C ILE A 192 28.718 22.721 65.319 1.00 91.42 C ANISOU 1132 C ILE A 192 13106 9863 11766 -1212 1776 896 C ATOM 1133 O ILE A 192 28.831 22.606 66.544 1.00 86.92 O ANISOU 1133 O ILE A 192 12639 9356 11032 -1170 1854 1057 O ATOM 1134 CB ILE A 192 30.171 21.397 63.730 1.00 95.04 C ANISOU 1134 CB ILE A 192 13606 10094 12410 -1082 1684 946 C ATOM 1135 CG1 ILE A 192 30.219 20.184 62.801 1.00 90.83 C ANISOU 1135 CG1 ILE A 192 13098 9322 12090 -1099 1763 927 C ATOM 1136 CG2 ILE A 192 31.268 21.315 64.782 1.00104.84 C ANISOU 1136 CG2 ILE A 192 14965 11428 13443 -921 1643 1174 C ATOM 1137 CD1 ILE A 192 31.442 20.144 61.920 1.00 87.59 C ANISOU 1137 CD1 ILE A 192 12668 8924 11689 -975 1607 918 C ATOM 1138 N GLY A 193 28.513 23.902 64.737 1.00 90.16 N ANISOU 1138 N GLY A 193 12809 9837 11611 -1245 1636 710 N ATOM 1139 CA GLY A 193 28.518 25.124 65.525 1.00 91.49 C ANISOU 1139 CA GLY A 193 12943 10215 11603 -1227 1562 679 C ATOM 1140 C GLY A 193 27.322 25.258 66.448 1.00 96.55 C ANISOU 1140 C GLY A 193 13584 10884 12218 -1333 1728 656 C ATOM 1141 O GLY A 193 27.463 25.681 67.599 1.00 93.48 O ANISOU 1141 O GLY A 193 13250 10633 11634 -1298 1749 731 O ATOM 1142 N LEU A 194 26.128 24.917 65.957 1.00 95.81 N ANISOU 1142 N LEU A 194 13417 10674 12312 -1467 1848 540 N ATOM 1143 CA LEU A 194 24.923 25.064 66.771 1.00 82.21 C ANISOU 1143 CA LEU A 194 11673 8981 10584 -1577 2017 500 C ATOM 1144 C LEU A 194 24.807 23.952 67.809 1.00 98.87 C ANISOU 1144 C LEU A 194 13937 10997 12633 -1591 2227 704 C ATOM 1145 O LEU A 194 24.397 24.200 68.951 1.00107.80 O ANISOU 1145 O LEU A 194 15110 12228 13621 -1614 2336 759 O ATOM 1146 CB LEU A 194 23.684 25.099 65.875 1.00 91.75 C ANISOU 1146 CB LEU A 194 12728 10115 12019 -1716 2067 297 C ATOM 1147 CG LEU A 194 23.522 26.370 65.035 1.00 96.09 C ANISOU 1147 CG LEU A 194 13114 10785 12612 -1707 1884 101 C ATOM 1148 CD1 LEU A 194 22.370 26.209 64.061 1.00 89.00 C ANISOU 1148 CD1 LEU A 194 12065 9815 11936 -1828 1924 -80 C ATOM 1149 CD2 LEU A 194 23.309 27.582 65.936 1.00 91.51 C ANISOU 1149 CD2 LEU A 194 12501 10383 11887 -1687 1862 56 C ATOM 1150 N ARG A 195 25.177 22.721 67.439 1.00 93.37 N ANISOU 1150 N ARG A 195 13331 10105 12042 -1574 2295 823 N ATOM 1151 CA ARG A 195 25.129 21.624 68.403 1.00107.02 C ANISOU 1151 CA ARG A 195 15220 11719 13722 -1573 2502 1048 C ATOM 1152 C ARG A 195 26.093 21.864 69.557 1.00105.97 C ANISOU 1152 C ARG A 195 15213 11750 13300 -1425 2449 1253 C ATOM 1153 O ARG A 195 25.763 21.595 70.720 1.00 94.73 O ANISOU 1153 O ARG A 195 13887 10366 11741 -1438 2607 1398 O ATOM 1154 CB ARG A 195 25.446 20.290 67.723 1.00 95.12 C ANISOU 1154 CB ARG A 195 13787 9953 12401 -1566 2575 1133 C ATOM 1155 CG ARG A 195 25.250 19.098 68.649 1.00 91.71 C ANISOU 1155 CG ARG A 195 13521 9358 11965 -1580 2821 1370 C ATOM 1156 CD ARG A 195 26.031 17.864 68.218 1.00 92.70 C ANISOU 1156 CD ARG A 195 13763 9249 12211 -1496 2857 1520 C ATOM 1157 NE ARG A 195 25.665 16.708 69.034 1.00131.91 N ANISOU 1157 NE ARG A 195 18882 14022 17215 -1531 3122 1740 N ATOM 1158 CZ ARG A 195 26.284 15.531 69.007 1.00137.96 C ANISOU 1158 CZ ARG A 195 19787 14563 18068 -1445 3210 1936 C ATOM 1159 NH1 ARG A 195 25.865 14.544 69.789 1.00140.22 N ANISOU 1159 NH1 ARG A 195 20215 14669 18394 -1486 3467 2145 N ATOM 1160 NH2 ARG A 195 27.317 15.337 68.197 1.00147.26 N ANISOU 1160 NH2 ARG A 195 20963 15688 19299 -1318 3051 1928 N ATOM 1161 N ASP A 196 27.286 22.373 69.256 1.00 98.20 N ANISOU 1161 N ASP A 196 14222 10877 12213 -1285 2229 1263 N ATOM 1162 CA ASP A 196 28.320 22.641 70.254 1.00 93.91 C ANISOU 1162 CA ASP A 196 13773 10514 11393 -1136 2142 1434 C ATOM 1163 C ASP A 196 28.868 24.039 69.975 1.00 89.69 C ANISOU 1163 C ASP A 196 13122 10195 10762 -1092 1910 1268 C ATOM 1164 O ASP A 196 29.685 24.220 69.066 1.00 94.95 O ANISOU 1164 O ASP A 196 13737 10849 11492 -1024 1743 1216 O ATOM 1165 CB ASP A 196 29.417 21.582 70.195 1.00104.74 C ANISOU 1165 CB ASP A 196 15268 11771 12755 -991 2125 1658 C ATOM 1166 CG ASP A 196 30.270 21.554 71.445 1.00123.58 C ANISOU 1166 CG ASP A 196 17773 14333 14850 -843 2095 1885 C ATOM 1167 OD1 ASP A 196 30.342 22.584 72.144 1.00133.72 O ANISOU 1167 OD1 ASP A 196 19018 15865 15924 -835 2012 1822 O ATOM 1168 OD2 ASP A 196 30.873 20.497 71.727 1.00136.45 O ANISOU 1168 OD2 ASP A 196 19532 15852 16460 -731 2156 2123 O ATOM 1169 N GLU A 197 28.425 25.024 70.762 1.00 85.64 N ANISOU 1169 N GLU A 197 12568 9872 10101 -1133 1911 1181 N ATOM 1170 CA GLU A 197 28.722 26.424 70.476 1.00 95.94 C ANISOU 1170 CA GLU A 197 13750 11347 11357 -1122 1723 992 C ATOM 1171 C GLU A 197 30.181 26.792 70.708 1.00108.12 C ANISOU 1171 C GLU A 197 15321 13044 12717 -975 1533 1067 C ATOM 1172 O GLU A 197 30.609 27.858 70.250 1.00104.91 O ANISOU 1172 O GLU A 197 14812 12739 12310 -963 1366 915 O ATOM 1173 CB GLU A 197 27.821 27.337 71.314 1.00116.78 C ANISOU 1173 CB GLU A 197 16339 14132 13898 -1206 1797 869 C ATOM 1174 CG GLU A 197 26.334 27.160 71.025 1.00140.85 C ANISOU 1174 CG GLU A 197 19320 17056 17140 -1356 1969 755 C ATOM 1175 CD GLU A 197 25.528 28.435 71.225 1.00142.50 C ANISOU 1175 CD GLU A 197 19404 17394 17347 -1428 1961 539 C ATOM 1176 OE1 GLU A 197 25.734 29.129 72.245 1.00146.16 O ANISOU 1176 OE1 GLU A 197 19892 18044 17598 -1397 1950 529 O ATOM 1177 OE2 GLU A 197 24.691 28.744 70.349 1.00133.59 O ANISOU 1177 OE2 GLU A 197 18146 16182 16430 -1511 1963 373 O ATOM 1178 N GLU A 198 30.955 25.951 71.393 1.00111.97 N ANISOU 1178 N GLU A 198 15938 13551 13056 -863 1555 1297 N ATOM 1179 CA GLU A 198 32.355 26.274 71.630 1.00 99.32 C ANISOU 1179 CA GLU A 198 14343 12115 11278 -719 1368 1364 C ATOM 1180 C GLU A 198 33.223 25.995 70.413 1.00103.83 C ANISOU 1180 C GLU A 198 14871 12575 12006 -651 1235 1356 C ATOM 1181 O GLU A 198 34.352 26.492 70.342 1.00109.49 O ANISOU 1181 O GLU A 198 15547 13431 12625 -555 1058 1349 O ATOM 1182 CB GLU A 198 32.875 25.501 72.843 1.00102.59 C ANISOU 1182 CB GLU A 198 14903 12619 11458 -605 1430 1623 C ATOM 1183 CG GLU A 198 31.780 24.897 73.728 1.00127.48 C ANISOU 1183 CG GLU A 198 18154 15718 14562 -681 1670 1730 C ATOM 1184 CD GLU A 198 30.805 25.925 74.297 1.00145.39 C ANISOU 1184 CD GLU A 198 20357 18128 16756 -807 1730 1545 C ATOM 1185 OE1 GLU A 198 31.105 27.138 74.260 1.00156.28 O ANISOU 1185 OE1 GLU A 198 21634 19679 18068 -813 1577 1359 O ATOM 1186 OE2 GLU A 198 29.732 25.511 74.788 1.00150.62 O ANISOU 1186 OE2 GLU A 198 21069 18723 17438 -902 1940 1583 O ATOM 1187 N LYS A 199 32.715 25.222 69.452 1.00106.12 N ANISOU 1187 N LYS A 199 15159 12625 12536 -705 1321 1343 N ATOM 1188 CA LYS A 199 33.415 25.009 68.195 1.00 95.55 C ANISOU 1188 CA LYS A 199 13767 11183 11356 -658 1208 1300 C ATOM 1189 C LYS A 199 33.385 26.238 67.297 1.00 81.26 C ANISOU 1189 C LYS A 199 11807 9446 9621 -718 1062 1069 C ATOM 1190 O LYS A 199 34.087 26.259 66.280 1.00 87.44 O ANISOU 1190 O LYS A 199 12535 10191 10499 -674 947 1025 O ATOM 1191 CB LYS A 199 32.803 23.814 67.462 1.00 96.96 C ANISOU 1191 CB LYS A 199 13985 11090 11764 -712 1355 1331 C ATOM 1192 CG LYS A 199 32.689 22.556 68.309 1.00 91.21 C ANISOU 1192 CG LYS A 199 13413 10242 11000 -668 1535 1567 C ATOM 1193 CD LYS A 199 33.986 21.763 68.309 1.00 94.03 C ANISOU 1193 CD LYS A 199 13849 10563 11315 -489 1471 1761 C ATOM 1194 CE LYS A 199 33.760 20.354 68.833 1.00104.08 C ANISOU 1194 CE LYS A 199 15276 11633 12635 -453 1674 1991 C ATOM 1195 NZ LYS A 199 34.986 19.518 68.735 1.00105.16 N ANISOU 1195 NZ LYS A 199 15483 11703 12768 -265 1620 2179 N ATOM 1196 N VAL A 200 32.597 27.255 67.645 1.00 91.10 N ANISOU 1196 N VAL A 200 12989 10793 10833 -812 1072 927 N ATOM 1197 CA VAL A 200 32.478 28.449 66.816 1.00 89.36 C ANISOU 1197 CA VAL A 200 12632 10623 10698 -866 950 722 C ATOM 1198 C VAL A 200 32.550 29.713 67.665 1.00 82.83 C ANISOU 1198 C VAL A 200 11764 9998 9709 -875 885 633 C ATOM 1199 O VAL A 200 32.334 30.819 67.158 1.00 75.43 O ANISOU 1199 O VAL A 200 10720 9099 8841 -924 806 465 O ATOM 1200 CB VAL A 200 31.179 28.423 65.987 1.00 90.97 C ANISOU 1200 CB VAL A 200 12764 10688 11114 -990 1038 586 C ATOM 1201 CG1 VAL A 200 31.271 27.382 64.880 1.00 87.63 C ANISOU 1201 CG1 VAL A 200 12348 10082 10864 -987 1059 615 C ATOM 1202 CG2 VAL A 200 29.977 28.158 66.884 1.00 80.30 C ANISOU 1202 CG2 VAL A 200 11451 9315 9745 -1079 1224 595 C ATOM 1203 N PHE A 201 32.853 29.567 68.954 1.00 87.30 N ANISOU 1203 N PHE A 201 12415 10695 10061 -826 922 743 N ATOM 1204 CA PHE A 201 33.000 30.711 69.845 1.00 92.96 C ANISOU 1204 CA PHE A 201 13097 11620 10604 -834 863 647 C ATOM 1205 C PHE A 201 34.224 30.523 70.724 1.00 90.51 C ANISOU 1205 C PHE A 201 12850 11485 10054 -715 777 782 C ATOM 1206 O PHE A 201 34.367 29.490 71.384 1.00 91.30 O ANISOU 1206 O PHE A 201 13064 11582 10045 -649 858 979 O ATOM 1207 CB PHE A 201 31.756 30.915 70.722 1.00 79.78 C ANISOU 1207 CB PHE A 201 11447 9982 8885 -926 1024 592 C ATOM 1208 CG PHE A 201 30.762 31.876 70.144 1.00 90.31 C ANISOU 1208 CG PHE A 201 12661 11265 10386 -1032 1039 378 C ATOM 1209 CD1 PHE A 201 31.037 33.234 70.103 1.00 89.47 C ANISOU 1209 CD1 PHE A 201 12463 11267 10264 -1041 921 209 C ATOM 1210 CD2 PHE A 201 29.552 31.426 69.643 1.00 88.42 C ANISOU 1210 CD2 PHE A 201 12397 10868 10330 -1119 1172 343 C ATOM 1211 CE1 PHE A 201 30.128 34.124 69.568 1.00 76.77 C ANISOU 1211 CE1 PHE A 201 10747 9602 8819 -1119 935 28 C ATOM 1212 CE2 PHE A 201 28.638 32.312 69.109 1.00 77.49 C ANISOU 1212 CE2 PHE A 201 10892 9453 9099 -1198 1175 153 C ATOM 1213 CZ PHE A 201 28.926 33.663 69.072 1.00 76.66 C ANISOU 1213 CZ PHE A 201 10704 9448 8976 -1190 1057 5 C ATOM 1214 N VAL A 202 35.099 31.520 70.727 1.00 88.44 N ANISOU 1214 N VAL A 202 12512 11376 9718 -687 614 677 N ATOM 1215 CA VAL A 202 36.263 31.551 71.604 1.00 85.89 C ANISOU 1215 CA VAL A 202 12216 11267 9154 -583 510 761 C ATOM 1216 C VAL A 202 35.962 32.500 72.751 1.00 81.67 C ANISOU 1216 C VAL A 202 11666 10937 8429 -635 521 638 C ATOM 1217 O VAL A 202 35.379 33.572 72.547 1.00 80.74 O ANISOU 1217 O VAL A 202 11466 10811 8401 -734 523 431 O ATOM 1218 CB VAL A 202 37.531 31.975 70.838 1.00 79.44 C ANISOU 1218 CB VAL A 202 11309 10492 8383 -524 322 716 C ATOM 1219 CG1 VAL A 202 38.640 32.370 71.805 1.00 89.34 C ANISOU 1219 CG1 VAL A 202 12546 12013 9386 -447 197 728 C ATOM 1220 CG2 VAL A 202 37.995 30.847 69.938 1.00 85.49 C ANISOU 1220 CG2 VAL A 202 12109 11095 9280 -443 318 867 C ATOM 1221 N ASN A 203 36.323 32.089 73.966 1.00 83.83 N ANISOU 1221 N ASN A 203 12020 11393 8438 -563 538 766 N ATOM 1222 CA ASN A 203 36.108 32.885 75.173 1.00 99.11 C ANISOU 1222 CA ASN A 203 13951 13558 10148 -603 553 655 C ATOM 1223 C ASN A 203 34.649 33.294 75.336 1.00 98.30 C ANISOU 1223 C ASN A 203 13846 13373 10132 -731 719 525 C ATOM 1224 O ASN A 203 34.353 34.293 76.000 1.00 85.71 O ANISOU 1224 O ASN A 203 12205 11923 8437 -794 725 343 O ATOM 1225 CB ASN A 203 37.011 34.122 75.188 1.00104.56 C ANISOU 1225 CB ASN A 203 14523 14421 10783 -612 373 457 C ATOM 1226 CG ASN A 203 38.477 33.767 75.297 1.00 97.82 C ANISOU 1226 CG ASN A 203 13660 13716 9792 -483 210 574 C ATOM 1227 OD1 ASN A 203 38.845 32.807 75.975 1.00 97.93 O ANISOU 1227 OD1 ASN A 203 13765 13824 9620 -372 226 791 O ATOM 1228 ND2 ASN A 203 39.324 34.540 74.627 1.00 97.56 N ANISOU 1228 ND2 ASN A 203 13510 13706 9854 -493 57 438 N ATOM 1229 N ASN A 204 33.739 32.538 74.720 1.00118.26 N ANISOU 1229 N ASN A 204 16410 15669 12853 -773 856 602 N ATOM 1230 CA ASN A 204 32.295 32.742 74.790 1.00116.68 C ANISOU 1230 CA ASN A 204 16197 15374 12760 -890 1027 499 C ATOM 1231 C ASN A 204 31.850 34.059 74.153 1.00104.96 C ANISOU 1231 C ASN A 204 14578 13850 11452 -977 974 234 C ATOM 1232 O ASN A 204 30.676 34.432 74.267 1.00116.36 O ANISOU 1232 O ASN A 204 15986 15245 12980 -1067 1100 116 O ATOM 1233 CB ASN A 204 31.801 32.651 76.245 1.00123.44 C ANISOU 1233 CB ASN A 204 17133 16407 13360 -905 1162 540 C ATOM 1234 CG ASN A 204 30.294 32.539 76.352 1.00128.17 C ANISOU 1234 CG ASN A 204 17733 16894 14072 -1018 1373 485 C ATOM 1235 OD1 ASN A 204 29.711 31.504 76.031 1.00126.39 O ANISOU 1235 OD1 ASN A 204 17565 16493 13967 -1039 1504 625 O ATOM 1236 ND2 ASN A 204 29.655 33.608 76.815 1.00131.09 N ANISOU 1236 ND2 ASN A 204 18031 17365 14413 -1095 1413 269 N ATOM 1237 N THR A 205 32.744 34.771 73.467 1.00 91.00 N ANISOU 1237 N THR A 205 12729 12094 9752 -949 798 142 N ATOM 1238 CA THR A 205 32.385 36.084 72.941 1.00 84.72 C ANISOU 1238 CA THR A 205 11814 11261 9115 -1022 751 -93 C ATOM 1239 C THR A 205 32.704 36.233 71.460 1.00 79.90 C ANISOU 1239 C THR A 205 11131 10484 8744 -1015 647 -112 C ATOM 1240 O THR A 205 31.840 36.646 70.677 1.00 78.35 O ANISOU 1240 O THR A 205 10865 10147 8757 -1074 685 -213 O ATOM 1241 CB THR A 205 33.086 37.191 73.733 1.00 91.22 C ANISOU 1241 CB THR A 205 12595 12293 9770 -1022 655 -244 C ATOM 1242 OG1 THR A 205 34.473 36.866 73.896 1.00 90.99 O ANISOU 1242 OG1 THR A 205 12589 12391 9589 -934 515 -138 O ATOM 1243 CG2 THR A 205 32.434 37.370 75.096 1.00 97.13 C ANISOU 1243 CG2 THR A 205 13388 13202 10316 -1058 780 -303 C ATOM 1244 N THR A 206 33.936 35.927 71.064 1.00 83.71 N ANISOU 1244 N THR A 206 11620 10994 9192 -939 514 -19 N ATOM 1245 CA THR A 206 34.333 36.106 69.676 1.00 75.76 C ANISOU 1245 CA THR A 206 10544 9854 8389 -932 415 -39 C ATOM 1246 C THR A 206 33.910 34.907 68.839 1.00 79.16 C ANISOU 1246 C THR A 206 11016 10106 8954 -917 482 96 C ATOM 1247 O THR A 206 34.019 33.756 69.269 1.00 76.16 O ANISOU 1247 O THR A 206 10732 9720 8486 -868 546 262 O ATOM 1248 CB THR A 206 35.844 36.341 69.561 1.00 98.08 C ANISOU 1248 CB THR A 206 13341 12789 11134 -865 251 -18 C ATOM 1249 OG1 THR A 206 36.324 35.856 68.300 1.00 96.07 O ANISOU 1249 OG1 THR A 206 13064 12406 11031 -827 189 58 O ATOM 1250 CG2 THR A 206 36.596 35.667 70.693 1.00105.16 C ANISOU 1250 CG2 THR A 206 14317 13866 11775 -784 234 114 C ATOM 1251 N CYS A 207 33.419 35.195 67.639 1.00 77.34 N ANISOU 1251 N CYS A 207 10712 9731 8941 -959 469 20 N ATOM 1252 CA CYS A 207 32.903 34.193 66.709 1.00 87.83 C ANISOU 1252 CA CYS A 207 12058 10892 10423 -966 529 97 C ATOM 1253 C CYS A 207 34.000 33.841 65.707 1.00 87.92 C ANISOU 1253 C CYS A 207 12055 10863 10487 -899 411 163 C ATOM 1254 O CYS A 207 34.276 34.604 64.777 1.00 89.66 O ANISOU 1254 O CYS A 207 12191 11063 10812 -909 315 77 O ATOM 1255 CB CYS A 207 31.654 34.722 66.009 1.00101.05 C ANISOU 1255 CB CYS A 207 13647 12465 12284 -1048 581 -36 C ATOM 1256 SG CYS A 207 31.037 33.706 64.655 1.00 95.28 S ANISOU 1256 SG CYS A 207 12896 11550 11755 -1072 624 1 S ATOM 1257 N VAL A 208 34.624 32.678 65.901 1.00 81.96 N ANISOU 1257 N VAL A 208 11384 10094 9662 -826 426 324 N ATOM 1258 CA VAL A 208 35.604 32.143 64.961 1.00 98.56 C ANISOU 1258 CA VAL A 208 13479 12146 11824 -756 339 393 C ATOM 1259 C VAL A 208 35.494 30.626 64.974 1.00 98.16 C ANISOU 1259 C VAL A 208 13525 11975 11795 -713 441 547 C ATOM 1260 O VAL A 208 35.060 30.027 65.961 1.00 75.72 O ANISOU 1260 O VAL A 208 10771 9135 8863 -711 553 640 O ATOM 1261 CB VAL A 208 37.050 32.585 65.294 1.00 98.12 C ANISOU 1261 CB VAL A 208 13402 12248 11633 -675 199 420 C ATOM 1262 CG1 VAL A 208 37.361 33.940 64.672 1.00103.70 C ANISOU 1262 CG1 VAL A 208 13995 13000 12404 -719 89 268 C ATOM 1263 CG2 VAL A 208 37.260 32.615 66.801 1.00 85.59 C ANISOU 1263 CG2 VAL A 208 11874 10821 9825 -642 216 474 C ATOM 1264 N LEU A 209 35.895 30.004 63.868 1.00105.35 N ANISOU 1264 N LEU A 209 14422 12775 12830 -680 412 572 N ATOM 1265 CA LEU A 209 35.887 28.549 63.782 1.00106.49 C ANISOU 1265 CA LEU A 209 14657 12779 13025 -635 510 706 C ATOM 1266 C LEU A 209 36.929 27.981 64.739 1.00100.18 C ANISOU 1266 C LEU A 209 13940 12065 12058 -507 488 882 C ATOM 1267 O LEU A 209 38.105 28.352 64.679 1.00106.73 O ANISOU 1267 O LEU A 209 14729 13014 12811 -424 353 896 O ATOM 1268 CB LEU A 209 36.158 28.103 62.347 1.00113.96 C ANISOU 1268 CB LEU A 209 15558 13605 14135 -627 475 665 C ATOM 1269 CG LEU A 209 35.854 26.642 62.008 1.00117.94 C ANISOU 1269 CG LEU A 209 16139 13916 14757 -617 601 744 C ATOM 1270 CD1 LEU A 209 34.492 26.231 62.552 1.00113.82 C ANISOU 1270 CD1 LEU A 209 15665 13298 14282 -718 767 740 C ATOM 1271 CD2 LEU A 209 35.914 26.430 60.504 1.00107.87 C ANISOU 1271 CD2 LEU A 209 14796 12548 13644 -638 565 642 C ATOM 1272 N ASN A 210 36.497 27.085 65.626 1.00107.07 N ANISOU 1272 N ASN A 210 14925 12883 12873 -490 622 1021 N ATOM 1273 CA ASN A 210 37.339 26.620 66.722 1.00110.53 C ANISOU 1273 CA ASN A 210 15448 13430 13118 -363 606 1206 C ATOM 1274 C ASN A 210 37.306 25.099 66.850 1.00119.92 C ANISOU 1274 C ASN A 210 16759 14441 14363 -292 740 1401 C ATOM 1275 O ASN A 210 37.434 24.557 67.953 1.00131.23 O ANISOU 1275 O ASN A 210 18295 15921 15646 -218 803 1581 O ATOM 1276 CB ASN A 210 36.920 27.285 68.035 1.00112.65 C ANISOU 1276 CB ASN A 210 15741 13873 13187 -398 633 1201 C ATOM 1277 CG ASN A 210 37.989 27.198 69.100 1.00115.11 C ANISOU 1277 CG ASN A 210 16098 14384 13256 -263 552 1347 C ATOM 1278 OD1 ASN A 210 39.133 26.845 68.818 1.00116.92 O ANISOU 1278 OD1 ASN A 210 16313 14643 13470 -140 448 1429 O ATOM 1279 ND2 ASN A 210 37.622 27.519 70.336 1.00109.27 N ANISOU 1279 ND2 ASN A 210 15403 13796 12317 -280 599 1373 N ATOM 1280 N ASP A 211 37.137 24.395 65.732 1.00120.11 N ANISOU 1280 N ASP A 211 16776 14258 14602 -313 788 1369 N ATOM 1281 CA ASP A 211 37.177 22.936 65.722 1.00120.02 C ANISOU 1281 CA ASP A 211 16877 14042 14684 -247 918 1536 C ATOM 1282 C ASP A 211 38.482 22.490 65.077 1.00111.90 C ANISOU 1282 C ASP A 211 15828 12996 13695 -101 813 1593 C ATOM 1283 O ASP A 211 38.623 22.569 63.846 1.00110.26 O ANISOU 1283 O ASP A 211 15540 12715 13639 -133 763 1456 O ATOM 1284 CB ASP A 211 35.976 22.364 64.963 1.00127.07 C ANISOU 1284 CB ASP A 211 17774 14701 15805 -387 1071 1438 C ATOM 1285 CG ASP A 211 35.773 20.881 65.220 1.00132.15 C ANISOU 1285 CG ASP A 211 18550 15114 16547 -350 1253 1612 C ATOM 1286 OD1 ASP A 211 36.714 20.217 65.709 1.00131.88 O ANISOU 1286 OD1 ASP A 211 18600 15074 16436 -189 1243 1812 O ATOM 1287 OD2 ASP A 211 34.668 20.377 64.930 1.00132.85 O ANISOU 1287 OD2 ASP A 211 18656 15024 16798 -481 1410 1548 O ATOM 1288 N PRO A 212 39.463 22.020 65.853 1.00104.87 N ANISOU 1288 N PRO A 212 15000 12182 12665 67 775 1793 N ATOM 1289 CA PRO A 212 40.767 21.688 65.253 1.00104.67 C ANISOU 1289 CA PRO A 212 14931 12164 12673 216 663 1835 C ATOM 1290 C PRO A 212 40.702 20.573 64.222 1.00113.01 C ANISOU 1290 C PRO A 212 16019 12947 13972 230 765 1833 C ATOM 1291 O PRO A 212 41.388 20.653 63.195 1.00113.83 O ANISOU 1291 O PRO A 212 16037 13044 14169 265 676 1734 O ATOM 1292 CB PRO A 212 41.618 21.295 66.471 1.00 91.45 C ANISOU 1292 CB PRO A 212 13330 10623 10795 396 628 2074 C ATOM 1293 CG PRO A 212 40.953 21.969 67.630 1.00 91.65 C ANISOU 1293 CG PRO A 212 13387 10812 10622 321 650 2086 C ATOM 1294 CD PRO A 212 39.487 21.917 67.321 1.00 98.96 C ANISOU 1294 CD PRO A 212 14345 11560 11695 135 811 1977 C ATOM 1295 N ASN A 213 39.895 19.534 64.459 1.00109.51 N ANISOU 1295 N ASN A 213 15696 12277 13638 197 957 1929 N ATOM 1296 CA ASN A 213 39.791 18.448 63.488 1.00117.62 C ANISOU 1296 CA ASN A 213 16752 13027 14910 196 1067 1903 C ATOM 1297 C ASN A 213 39.212 18.944 62.168 1.00116.35 C ANISOU 1297 C ASN A 213 16479 12827 14903 38 1040 1631 C ATOM 1298 O ASN A 213 39.734 18.631 61.092 1.00120.38 O ANISOU 1298 O ASN A 213 16937 13260 15542 72 1005 1541 O ATOM 1299 CB ASN A 213 38.938 17.309 64.051 1.00129.48 C ANISOU 1299 CB ASN A 213 18401 14285 16510 163 1295 2046 C ATOM 1300 CG ASN A 213 39.763 16.259 64.773 1.00145.25 C ANISOU 1300 CG ASN A 213 20521 16195 18472 371 1349 2330 C ATOM 1301 OD1 ASN A 213 40.410 15.420 64.144 1.00154.69 O ANISOU 1301 OD1 ASN A 213 21732 17224 19819 478 1371 2364 O ATOM 1302 ND2 ASN A 213 39.741 16.297 66.100 1.00147.85 N ANISOU 1302 ND2 ASN A 213 20939 16641 18599 434 1374 2537 N ATOM 1303 N PHE A 214 38.126 19.717 62.231 1.00111.50 N ANISOU 1303 N PHE A 214 15822 12272 14271 -130 1058 1498 N ATOM 1304 CA PHE A 214 37.521 20.227 61.005 1.00113.99 C ANISOU 1304 CA PHE A 214 16025 12570 14715 -271 1025 1253 C ATOM 1305 C PHE A 214 38.456 21.194 60.291 1.00116.03 C ANISOU 1305 C PHE A 214 16163 13015 14908 -222 829 1152 C ATOM 1306 O PHE A 214 38.614 21.117 59.068 1.00118.11 O ANISOU 1306 O PHE A 214 16357 13229 15290 -245 795 1017 O ATOM 1307 CB PHE A 214 36.184 20.901 61.319 1.00115.76 C ANISOU 1307 CB PHE A 214 16221 12836 14926 -440 1080 1149 C ATOM 1308 CG PHE A 214 35.361 21.220 60.100 1.00116.99 C ANISOU 1308 CG PHE A 214 16270 12950 15232 -583 1073 917 C ATOM 1309 CD1 PHE A 214 35.571 22.393 59.388 1.00108.85 C ANISOU 1309 CD1 PHE A 214 15115 12086 14156 -607 913 774 C ATOM 1310 CD2 PHE A 214 34.374 20.348 59.667 1.00111.74 C ANISOU 1310 CD2 PHE A 214 15624 12080 14751 -696 1229 843 C ATOM 1311 CE1 PHE A 214 34.816 22.686 58.267 1.00 98.92 C ANISOU 1311 CE1 PHE A 214 13758 10808 13018 -723 899 578 C ATOM 1312 CE2 PHE A 214 33.615 20.637 58.548 1.00105.55 C ANISOU 1312 CE2 PHE A 214 14729 11287 14088 -822 1210 624 C ATOM 1313 CZ PHE A 214 33.837 21.807 57.847 1.00100.29 C ANISOU 1313 CZ PHE A 214 13944 10804 13359 -827 1040 500 C ATOM 1314 N VAL A 215 39.089 22.102 61.037 1.00118.77 N ANISOU 1314 N VAL A 215 16482 13581 15064 -160 705 1209 N ATOM 1315 CA VAL A 215 39.964 23.097 60.423 1.00115.00 C ANISOU 1315 CA VAL A 215 15886 13279 14529 -131 529 1112 C ATOM 1316 C VAL A 215 41.147 22.422 59.738 1.00113.06 C ANISOU 1316 C VAL A 215 15623 12989 14344 3 486 1154 C ATOM 1317 O VAL A 215 41.564 22.828 58.647 1.00101.95 O ANISOU 1317 O VAL A 215 14121 11624 12994 -12 406 1027 O ATOM 1318 CB VAL A 215 40.419 24.126 61.475 1.00113.19 C ANISOU 1318 CB VAL A 215 15632 13285 14091 -98 420 1159 C ATOM 1319 CG1 VAL A 215 41.565 24.977 60.937 1.00118.72 C ANISOU 1319 CG1 VAL A 215 16216 14151 14741 -47 250 1091 C ATOM 1320 CG2 VAL A 215 39.251 25.009 61.885 1.00106.06 C ANISOU 1320 CG2 VAL A 215 14713 12434 13152 -243 450 1060 C ATOM 1321 N LEU A 216 41.695 21.374 60.352 1.00119.45 N ANISOU 1321 N LEU A 216 16525 13715 15145 142 546 1336 N ATOM 1322 CA LEU A 216 42.844 20.676 59.786 1.00118.06 C ANISOU 1322 CA LEU A 216 16331 13491 15033 290 514 1385 C ATOM 1323 C LEU A 216 42.471 19.917 58.517 1.00112.37 C ANISOU 1323 C LEU A 216 15607 12558 14529 234 608 1259 C ATOM 1324 O LEU A 216 42.935 20.265 57.425 1.00111.19 O ANISOU 1324 O LEU A 216 15359 12461 14428 223 532 1121 O ATOM 1325 CB LEU A 216 43.451 19.727 60.823 1.00120.30 C ANISOU 1325 CB LEU A 216 16721 13729 15260 467 562 1630 C ATOM 1326 CG LEU A 216 44.336 20.393 61.885 1.00119.59 C ANISOU 1326 CG LEU A 216 16599 13902 14937 579 422 1750 C ATOM 1327 CD1 LEU A 216 44.532 19.488 63.095 1.00119.97 C ANISOU 1327 CD1 LEU A 216 16775 13909 14899 728 492 2011 C ATOM 1328 CD2 LEU A 216 45.680 20.789 61.286 1.00116.39 C ANISOU 1328 CD2 LEU A 216 16065 13647 14511 682 267 1699 C ATOM 1329 N ILE A 217 41.638 18.880 58.653 1.00 97.05 N ANISOU 1329 N ILE A 217 13773 10383 12719 193 780 1299 N ATOM 1330 CA ILE A 217 41.209 18.090 57.499 1.00 95.72 C ANISOU 1330 CA ILE A 217 13601 10005 12763 126 883 1158 C ATOM 1331 C ILE A 217 40.567 18.984 56.445 1.00102.05 C ANISOU 1331 C ILE A 217 14288 10897 13588 -37 818 920 C ATOM 1332 O ILE A 217 40.829 18.845 55.243 1.00104.23 O ANISOU 1332 O ILE A 217 14497 11150 13956 -49 796 775 O ATOM 1333 CB ILE A 217 40.247 16.973 57.947 1.00 98.69 C ANISOU 1333 CB ILE A 217 14105 10118 13274 70 1088 1227 C ATOM 1334 CG1 ILE A 217 40.945 15.996 58.907 1.00112.20 C ANISOU 1334 CG1 ILE A 217 15940 11717 14975 254 1162 1489 C ATOM 1335 CG2 ILE A 217 39.653 16.254 56.741 1.00 89.09 C ANISOU 1335 CG2 ILE A 217 12870 8700 12281 -37 1194 1033 C ATOM 1336 CD1 ILE A 217 41.975 15.095 58.251 1.00109.07 C ANISOU 1336 CD1 ILE A 217 15546 11192 14705 410 1175 1511 C ATOM 1337 N GLY A 218 39.727 19.925 56.882 1.00 94.45 N ANISOU 1337 N GLY A 218 13300 10050 12537 -155 787 879 N ATOM 1338 CA GLY A 218 39.054 20.803 55.941 1.00 82.40 C ANISOU 1338 CA GLY A 218 11666 8612 11032 -295 724 675 C ATOM 1339 C GLY A 218 40.009 21.669 55.141 1.00100.12 C ANISOU 1339 C GLY A 218 13801 11035 13207 -247 565 604 C ATOM 1340 O GLY A 218 39.783 21.918 53.956 1.00107.08 O ANISOU 1340 O GLY A 218 14603 11936 14148 -317 534 444 O ATOM 1341 N SER A 219 41.083 22.149 55.778 1.00109.27 N ANISOU 1341 N SER A 219 14949 12337 14233 -132 465 721 N ATOM 1342 CA SER A 219 42.053 22.972 55.061 1.00106.15 C ANISOU 1342 CA SER A 219 14445 12108 13779 -93 326 659 C ATOM 1343 C SER A 219 42.687 22.209 53.908 1.00 99.30 C ANISOU 1343 C SER A 219 13549 11162 13019 -35 347 593 C ATOM 1344 O SER A 219 42.968 22.795 52.857 1.00102.20 O ANISOU 1344 O SER A 219 13821 11625 13385 -69 276 475 O ATOM 1345 CB SER A 219 43.128 23.486 56.020 1.00109.93 C ANISOU 1345 CB SER A 219 14910 12749 14108 20 225 789 C ATOM 1346 OG SER A 219 42.657 24.612 56.755 1.00108.51 O ANISOU 1346 OG SER A 219 14713 12702 13816 -58 168 780 O ATOM 1347 N PHE A 220 42.903 20.905 54.076 1.00 95.14 N ANISOU 1347 N PHE A 220 13103 10457 12587 53 453 669 N ATOM 1348 CA PHE A 220 43.387 20.094 52.965 1.00102.99 C ANISOU 1348 CA PHE A 220 14075 11352 13705 100 497 581 C ATOM 1349 C PHE A 220 42.344 20.008 51.858 1.00103.26 C ANISOU 1349 C PHE A 220 14079 11316 13841 -53 552 379 C ATOM 1350 O PHE A 220 42.622 20.349 50.702 1.00104.04 O ANISOU 1350 O PHE A 220 14089 11502 13941 -79 497 243 O ATOM 1351 CB PHE A 220 43.767 18.698 53.460 1.00102.99 C ANISOU 1351 CB PHE A 220 14177 11147 13806 231 614 709 C ATOM 1352 CG PHE A 220 45.125 18.631 54.086 1.00111.69 C ANISOU 1352 CG PHE A 220 15271 12340 14827 424 541 874 C ATOM 1353 CD1 PHE A 220 45.299 18.937 55.423 1.00116.50 C ANISOU 1353 CD1 PHE A 220 15924 13040 15301 489 496 1055 C ATOM 1354 CD2 PHE A 220 46.231 18.276 53.333 1.00120.85 C ANISOU 1354 CD2 PHE A 220 16366 13515 16036 542 514 840 C ATOM 1355 CE1 PHE A 220 46.550 18.882 56.003 1.00118.96 C ANISOU 1355 CE1 PHE A 220 16211 13462 15526 670 415 1201 C ATOM 1356 CE2 PHE A 220 47.487 18.219 53.906 1.00122.95 C ANISOU 1356 CE2 PHE A 220 16604 13881 16231 725 440 986 C ATOM 1357 CZ PHE A 220 47.646 18.522 55.243 1.00121.35 C ANISOU 1357 CZ PHE A 220 16440 13776 15891 790 385 1167 C ATOM 1358 N VAL A 221 41.127 19.577 52.198 1.00 92.47 N ANISOU 1358 N VAL A 221 12777 9808 12551 -159 659 357 N ATOM 1359 CA VAL A 221 40.096 19.386 51.182 1.00 90.78 C ANISOU 1359 CA VAL A 221 12523 9529 12439 -306 714 156 C ATOM 1360 C VAL A 221 39.723 20.712 50.533 1.00 92.95 C ANISOU 1360 C VAL A 221 12687 10015 12615 -400 587 43 C ATOM 1361 O VAL A 221 39.588 20.802 49.307 1.00112.97 O ANISOU 1361 O VAL A 221 15147 12601 15176 -454 560 -119 O ATOM 1362 CB VAL A 221 38.863 18.695 51.792 1.00 95.27 C ANISOU 1362 CB VAL A 221 13173 9911 13114 -408 859 160 C ATOM 1363 CG1 VAL A 221 37.796 18.486 50.725 1.00 91.17 C ANISOU 1363 CG1 VAL A 221 12591 9345 12703 -565 907 -69 C ATOM 1364 CG2 VAL A 221 39.254 17.367 52.425 1.00 95.79 C ANISOU 1364 CG2 VAL A 221 13361 9746 13289 -307 999 296 C ATOM 1365 N ALA A 222 39.567 21.766 51.336 1.00 89.53 N ANISOU 1365 N ALA A 222 12242 9711 12064 -416 510 127 N ATOM 1366 CA ALA A 222 39.039 23.024 50.825 1.00 86.63 C ANISOU 1366 CA ALA A 222 11781 9509 11627 -508 409 33 C ATOM 1367 C ALA A 222 40.108 23.983 50.320 1.00 82.66 C ANISOU 1367 C ALA A 222 11199 9187 11019 -446 276 44 C ATOM 1368 O ALA A 222 39.768 24.945 49.623 1.00103.19 O ANISOU 1368 O ALA A 222 13720 11910 13579 -513 200 -38 O ATOM 1369 CB ALA A 222 38.206 23.727 51.902 1.00 84.50 C ANISOU 1369 CB ALA A 222 11531 9273 11303 -570 408 92 C ATOM 1370 N PHE A 223 41.382 23.765 50.638 1.00 80.49 N ANISOU 1370 N PHE A 223 10940 8936 10705 -320 249 147 N ATOM 1371 CA PHE A 223 42.383 24.721 50.180 1.00 91.81 C ANISOU 1371 CA PHE A 223 12288 10547 12049 -278 132 150 C ATOM 1372 C PHE A 223 43.634 24.048 49.628 1.00 96.28 C ANISOU 1372 C PHE A 223 12833 11110 12638 -162 136 159 C ATOM 1373 O PHE A 223 44.056 24.345 48.506 1.00 98.25 O ANISOU 1373 O PHE A 223 13006 11447 12876 -171 98 71 O ATOM 1374 CB PHE A 223 42.762 25.681 51.310 1.00 85.19 C ANISOU 1374 CB PHE A 223 11446 9821 11102 -254 54 261 C ATOM 1375 CG PHE A 223 43.673 26.788 50.872 1.00 88.85 C ANISOU 1375 CG PHE A 223 11813 10457 11488 -241 -57 252 C ATOM 1376 CD1 PHE A 223 43.166 27.898 50.214 1.00 88.95 C ANISOU 1376 CD1 PHE A 223 11762 10554 11480 -337 -110 175 C ATOM 1377 CD2 PHE A 223 45.036 26.715 51.104 1.00 83.37 C ANISOU 1377 CD2 PHE A 223 11088 9838 10751 -131 -103 324 C ATOM 1378 CE1 PHE A 223 44.003 28.916 49.800 1.00 81.65 C ANISOU 1378 CE1 PHE A 223 10755 9770 10499 -333 -195 176 C ATOM 1379 CE2 PHE A 223 45.876 27.728 50.694 1.00 78.70 C ANISOU 1379 CE2 PHE A 223 10401 9401 10103 -134 -192 308 C ATOM 1380 CZ PHE A 223 45.360 28.831 50.041 1.00 80.31 C ANISOU 1380 CZ PHE A 223 10552 9670 10292 -240 -232 237 C ATOM 1381 N PHE A 224 44.231 23.138 50.399 1.00 90.68 N ANISOU 1381 N PHE A 224 12189 10306 11958 -47 185 270 N ATOM 1382 CA PHE A 224 45.544 22.615 50.035 1.00 94.77 C ANISOU 1382 CA PHE A 224 12673 10842 12492 88 177 296 C ATOM 1383 C PHE A 224 45.486 21.688 48.824 1.00 87.17 C ANISOU 1383 C PHE A 224 11704 9772 11644 85 261 161 C ATOM 1384 O PHE A 224 46.375 21.738 47.967 1.00 74.56 O ANISOU 1384 O PHE A 224 10032 8259 10038 136 233 104 O ATOM 1385 CB PHE A 224 46.173 21.904 51.234 1.00 97.82 C ANISOU 1385 CB PHE A 224 13128 11162 12877 230 201 467 C ATOM 1386 CG PHE A 224 46.590 22.837 52.335 1.00 99.70 C ANISOU 1386 CG PHE A 224 13345 11561 12975 258 97 584 C ATOM 1387 CD1 PHE A 224 47.578 23.785 52.118 1.00 88.64 C ANISOU 1387 CD1 PHE A 224 11832 10358 11488 281 -19 572 C ATOM 1388 CD2 PHE A 224 46.001 22.765 53.588 1.00109.38 C ANISOU 1388 CD2 PHE A 224 14659 12747 14155 253 122 695 C ATOM 1389 CE1 PHE A 224 47.967 24.647 53.125 1.00 83.37 C ANISOU 1389 CE1 PHE A 224 11137 9842 10698 294 -113 652 C ATOM 1390 CE2 PHE A 224 46.388 23.625 54.601 1.00113.99 C ANISOU 1390 CE2 PHE A 224 15219 13495 14598 274 25 780 C ATOM 1391 CZ PHE A 224 47.373 24.568 54.370 1.00101.02 C ANISOU 1391 CZ PHE A 224 13460 12046 12878 292 -95 750 C ATOM 1392 N ILE A 225 44.467 20.840 48.726 1.00 86.99 N ANISOU 1392 N ILE A 225 11754 9569 11730 19 370 97 N ATOM 1393 CA ILE A 225 44.361 19.939 47.578 1.00 97.37 C ANISOU 1393 CA ILE A 225 13059 10779 13157 3 456 -62 C ATOM 1394 C ILE A 225 43.982 20.725 46.324 1.00100.02 C ANISOU 1394 C ILE A 225 13300 11271 13432 -110 394 -227 C ATOM 1395 O ILE A 225 44.648 20.562 45.290 1.00 93.57 O ANISOU 1395 O ILE A 225 12423 10516 12613 -75 392 -324 O ATOM 1396 CB ILE A 225 43.370 18.791 47.840 1.00 93.90 C ANISOU 1396 CB ILE A 225 12717 10093 12867 -50 600 -99 C ATOM 1397 CG1 ILE A 225 43.823 17.949 49.033 1.00 93.97 C ANISOU 1397 CG1 ILE A 225 12830 9940 12935 81 672 91 C ATOM 1398 CG2 ILE A 225 43.245 17.912 46.601 1.00 86.43 C ANISOU 1398 CG2 ILE A 225 11750 9050 12038 -83 686 -300 C ATOM 1399 CD1 ILE A 225 42.786 16.949 49.494 1.00 97.45 C ANISOU 1399 CD1 ILE A 225 13377 10130 13518 16 825 93 C ATOM 1400 N PRO A 226 42.944 21.576 46.341 1.00100.32 N ANISOU 1400 N PRO A 226 13318 11383 13415 -236 346 -261 N ATOM 1401 CA PRO A 226 42.637 22.346 45.122 1.00104.03 C ANISOU 1401 CA PRO A 226 13697 12015 13815 -322 280 -394 C ATOM 1402 C PRO A 226 43.763 23.268 44.695 1.00104.35 C ANISOU 1402 C PRO A 226 13660 12246 13743 -263 183 -346 C ATOM 1403 O PRO A 226 43.950 23.492 43.492 1.00106.81 O ANISOU 1403 O PRO A 226 13903 12670 14009 -287 162 -452 O ATOM 1404 CB PRO A 226 41.383 23.139 45.513 1.00 93.65 C ANISOU 1404 CB PRO A 226 12379 10735 12470 -438 242 -393 C ATOM 1405 CG PRO A 226 40.784 22.372 46.626 1.00 93.79 C ANISOU 1405 CG PRO A 226 12490 10566 12579 -446 334 -331 C ATOM 1406 CD PRO A 226 41.946 21.839 47.394 1.00 88.83 C ANISOU 1406 CD PRO A 226 11919 9871 11961 -305 358 -189 C ATOM 1407 N LEU A 227 44.519 23.814 45.649 1.00103.57 N ANISOU 1407 N LEU A 227 13565 12195 13593 -193 128 -195 N ATOM 1408 CA LEU A 227 45.660 24.651 45.299 1.00 92.60 C ANISOU 1408 CA LEU A 227 12093 10976 12115 -144 49 -154 C ATOM 1409 C LEU A 227 46.770 23.826 44.664 1.00 96.55 C ANISOU 1409 C LEU A 227 12562 11470 12651 -40 94 -193 C ATOM 1410 O LEU A 227 47.430 24.280 43.723 1.00106.85 O ANISOU 1410 O LEU A 227 13785 12914 13899 -37 65 -242 O ATOM 1411 CB LEU A 227 46.181 25.367 46.541 1.00103.59 C ANISOU 1411 CB LEU A 227 13487 12421 13451 -102 -19 -6 C ATOM 1412 CG LEU A 227 47.245 26.431 46.306 1.00 98.23 C ANISOU 1412 CG LEU A 227 12713 11921 12688 -84 -104 32 C ATOM 1413 CD1 LEU A 227 46.586 27.772 46.010 1.00 94.20 C ANISOU 1413 CD1 LEU A 227 12167 11508 12117 -200 -166 14 C ATOM 1414 CD2 LEU A 227 48.157 26.512 47.512 1.00 74.77 C ANISOU 1414 CD2 LEU A 227 9738 8981 9689 8 -147 155 C ATOM 1415 N THR A 228 46.997 22.614 45.174 1.00100.14 N ANISOU 1415 N THR A 228 13082 11761 13206 52 174 -166 N ATOM 1416 CA THR A 228 48.019 21.750 44.592 1.00 98.26 C ANISOU 1416 CA THR A 228 12814 11495 13024 165 230 -211 C ATOM 1417 C THR A 228 47.656 21.357 43.165 1.00 98.66 C ANISOU 1417 C THR A 228 12835 11552 13099 100 287 -405 C ATOM 1418 O THR A 228 48.530 21.264 42.294 1.00 86.97 O ANISOU 1418 O THR A 228 11283 10162 11598 152 298 -474 O ATOM 1419 CB THR A 228 48.205 20.506 45.457 1.00 94.89 C ANISOU 1419 CB THR A 228 12474 10862 12717 282 314 -131 C ATOM 1420 OG1 THR A 228 48.524 20.906 46.794 1.00 91.30 O ANISOU 1420 OG1 THR A 228 12045 10436 12210 344 252 53 O ATOM 1421 CG2 THR A 228 49.324 19.634 44.909 1.00100.62 C ANISOU 1421 CG2 THR A 228 13162 11551 13516 420 373 -171 C ATOM 1422 N ILE A 229 46.368 21.129 42.906 1.00 99.05 N ANISOU 1422 N ILE A 229 12928 11522 13184 -16 324 -506 N ATOM 1423 CA ILE A 229 45.940 20.768 41.559 1.00 91.38 C ANISOU 1423 CA ILE A 229 11921 10581 12218 -88 368 -709 C ATOM 1424 C ILE A 229 46.052 21.963 40.621 1.00 85.07 C ANISOU 1424 C ILE A 229 11029 10028 11263 -148 276 -742 C ATOM 1425 O ILE A 229 46.490 21.828 39.471 1.00 88.78 O ANISOU 1425 O ILE A 229 11441 10602 11688 -142 296 -861 O ATOM 1426 CB ILE A 229 44.510 20.202 41.588 1.00 95.08 C ANISOU 1426 CB ILE A 229 12447 10909 12771 -202 428 -816 C ATOM 1427 CG1 ILE A 229 44.474 18.926 42.429 1.00 99.04 C ANISOU 1427 CG1 ILE A 229 13047 11144 13441 -141 546 -778 C ATOM 1428 CG2 ILE A 229 44.007 19.946 40.177 1.00 76.77 C ANISOU 1428 CG2 ILE A 229 10073 8664 10431 -289 452 -1043 C ATOM 1429 CD1 ILE A 229 43.080 18.470 42.785 1.00 98.42 C ANISOU 1429 CD1 ILE A 229 13028 10911 13456 -260 610 -838 C ATOM 1430 N MET A 230 45.674 23.152 41.093 1.00 83.31 N ANISOU 1430 N MET A 230 10795 9902 10957 -204 182 -634 N ATOM 1431 CA MET A 230 45.716 24.321 40.220 1.00 89.56 C ANISOU 1431 CA MET A 230 11508 10906 11614 -260 104 -643 C ATOM 1432 C MET A 230 47.145 24.643 39.790 1.00 94.88 C ANISOU 1432 C MET A 230 12115 11709 12228 -181 93 -601 C ATOM 1433 O MET A 230 47.375 25.075 38.654 1.00 82.81 O ANISOU 1433 O MET A 230 10522 10338 10605 -209 81 -663 O ATOM 1434 CB MET A 230 45.074 25.527 40.911 1.00 92.05 C ANISOU 1434 CB MET A 230 11829 11267 11879 -324 18 -529 C ATOM 1435 CG MET A 230 45.987 26.264 41.875 1.00117.41 C ANISOU 1435 CG MET A 230 15031 14511 15069 -267 -34 -368 C ATOM 1436 SD MET A 230 45.313 27.848 42.390 1.00129.44 S ANISOU 1436 SD MET A 230 16542 16112 16528 -352 -128 -272 S ATOM 1437 CE MET A 230 44.548 28.337 40.856 1.00118.33 C ANISOU 1437 CE MET A 230 15083 14834 15043 -433 -150 -373 C ATOM 1438 N VAL A 231 48.123 24.406 40.669 1.00 91.53 N ANISOU 1438 N VAL A 231 11695 11228 11853 -79 99 -497 N ATOM 1439 CA VAL A 231 49.502 24.767 40.352 1.00 92.32 C ANISOU 1439 CA VAL A 231 11711 11459 11905 -7 85 -456 C ATOM 1440 C VAL A 231 50.098 23.778 39.358 1.00101.53 C ANISOU 1440 C VAL A 231 12846 12627 13103 56 174 -591 C ATOM 1441 O VAL A 231 50.742 24.168 38.376 1.00101.82 O ANISOU 1441 O VAL A 231 12804 12826 13059 52 179 -637 O ATOM 1442 CB VAL A 231 50.345 24.853 41.636 1.00 93.82 C ANISOU 1442 CB VAL A 231 11899 11616 12132 86 50 -310 C ATOM 1443 CG1 VAL A 231 51.814 25.029 41.289 1.00 72.13 C ANISOU 1443 CG1 VAL A 231 9048 9000 9359 168 48 -291 C ATOM 1444 CG2 VAL A 231 49.852 25.995 42.513 1.00 79.70 C ANISOU 1444 CG2 VAL A 231 10126 9862 10293 13 -37 -200 C ATOM 1445 N ILE A 232 49.896 22.482 39.602 1.00101.73 N ANISOU 1445 N ILE A 232 12934 12467 13252 113 255 -656 N ATOM 1446 CA ILE A 232 50.462 21.464 38.722 1.00 89.04 C ANISOU 1446 CA ILE A 232 11300 10833 11697 181 353 -801 C ATOM 1447 C ILE A 232 49.798 21.512 37.352 1.00 88.87 C ANISOU 1447 C ILE A 232 11254 10916 11595 75 376 -982 C ATOM 1448 O ILE A 232 50.474 21.492 36.317 1.00102.35 O ANISOU 1448 O ILE A 232 12891 12760 13237 96 410 -1076 O ATOM 1449 CB ILE A 232 50.333 20.071 39.362 1.00 90.37 C ANISOU 1449 CB ILE A 232 11552 10744 12039 265 445 -822 C ATOM 1450 CG1 ILE A 232 51.063 20.039 40.705 1.00 78.43 C ANISOU 1450 CG1 ILE A 232 10058 9162 10579 389 413 -625 C ATOM 1451 CG2 ILE A 232 50.879 19.006 38.426 1.00 95.30 C ANISOU 1451 CG2 ILE A 232 12150 11322 12738 334 557 -994 C ATOM 1452 CD1 ILE A 232 50.938 18.720 41.436 1.00 85.16 C ANISOU 1452 CD1 ILE A 232 11005 9753 11599 486 505 -599 C ATOM 1453 N THR A 233 48.466 21.580 37.322 1.00 98.60 N ANISOU 1453 N THR A 233 12538 12105 12821 -38 356 -1036 N ATOM 1454 CA THR A 233 47.767 21.622 36.041 1.00 98.08 C ANISOU 1454 CA THR A 233 12440 12163 12664 -135 363 -1212 C ATOM 1455 C THR A 233 48.134 22.875 35.255 1.00 85.02 C ANISOU 1455 C THR A 233 10707 10770 10826 -170 290 -1158 C ATOM 1456 O THR A 233 48.283 22.822 34.030 1.00 80.46 O ANISOU 1456 O THR A 233 10079 10346 10148 -191 316 -1287 O ATOM 1457 CB THR A 233 46.252 21.541 36.249 1.00 90.32 C ANISOU 1457 CB THR A 233 11508 11099 11712 -248 343 -1269 C ATOM 1458 OG1 THR A 233 45.829 22.565 37.157 1.00 87.02 O ANISOU 1458 OG1 THR A 233 11109 10693 11262 -281 251 -1090 O ATOM 1459 CG2 THR A 233 45.860 20.174 36.801 1.00 78.78 C ANISOU 1459 CG2 THR A 233 10122 9372 10439 -232 446 -1354 C ATOM 1460 N TYR A 234 48.300 24.008 35.940 1.00 83.29 N ANISOU 1460 N TYR A 234 10479 10604 10562 -177 205 -970 N ATOM 1461 CA TYR A 234 48.677 25.234 35.244 1.00 97.55 C ANISOU 1461 CA TYR A 234 12218 12631 12215 -212 150 -899 C ATOM 1462 C TYR A 234 50.062 25.110 34.619 1.00102.48 C ANISOU 1462 C TYR A 234 12770 13367 12801 -139 206 -918 C ATOM 1463 O TYR A 234 50.244 25.380 33.426 1.00100.61 O ANISOU 1463 O TYR A 234 12481 13309 12437 -167 226 -985 O ATOM 1464 CB TYR A 234 48.630 26.432 36.196 1.00 92.32 C ANISOU 1464 CB TYR A 234 11562 11971 11544 -236 63 -706 C ATOM 1465 CG TYR A 234 49.072 27.717 35.537 1.00 88.72 C ANISOU 1465 CG TYR A 234 11042 11710 10958 -273 21 -617 C ATOM 1466 CD1 TYR A 234 48.178 28.482 34.800 1.00 87.79 C ANISOU 1466 CD1 TYR A 234 10920 11705 10731 -353 -26 -613 C ATOM 1467 CD2 TYR A 234 50.389 28.156 35.635 1.00 87.64 C ANISOU 1467 CD2 TYR A 234 10843 11645 10811 -227 34 -532 C ATOM 1468 CE1 TYR A 234 48.577 29.650 34.185 1.00 96.41 C ANISOU 1468 CE1 TYR A 234 11964 12959 11710 -382 -51 -511 C ATOM 1469 CE2 TYR A 234 50.798 29.323 35.022 1.00 97.62 C ANISOU 1469 CE2 TYR A 234 12051 13072 11970 -272 14 -447 C ATOM 1470 CZ TYR A 234 49.888 30.065 34.297 1.00100.42 C ANISOU 1470 CZ TYR A 234 12418 13518 12220 -348 -23 -428 C ATOM 1471 OH TYR A 234 50.289 31.229 33.686 1.00 96.96 O ANISOU 1471 OH TYR A 234 11933 13224 11682 -388 -31 -321 O ATOM 1472 N CYS A 235 51.059 24.718 35.417 1.00 97.09 N ANISOU 1472 N CYS A 235 12076 12594 12221 -39 233 -854 N ATOM 1473 CA CYS A 235 52.418 24.602 34.898 1.00 98.47 C ANISOU 1473 CA CYS A 235 12164 12876 12374 37 288 -872 C ATOM 1474 C CYS A 235 52.502 23.543 33.804 1.00104.95 C ANISOU 1474 C CYS A 235 12971 13713 13191 65 389 -1078 C ATOM 1475 O CYS A 235 53.127 23.761 32.760 1.00 95.70 O ANISOU 1475 O CYS A 235 11726 12721 11913 63 432 -1138 O ATOM 1476 CB CYS A 235 53.392 24.286 36.035 1.00 95.59 C ANISOU 1476 CB CYS A 235 11781 12409 12129 153 288 -770 C ATOM 1477 SG CYS A 235 53.645 25.652 37.204 1.00 92.47 S ANISOU 1477 SG CYS A 235 11366 12056 11712 121 173 -554 S ATOM 1478 N LEU A 236 51.873 22.386 34.026 1.00106.43 N ANISOU 1478 N LEU A 236 13228 13712 13497 85 439 -1195 N ATOM 1479 CA LEU A 236 51.875 21.343 33.005 1.00107.26 C ANISOU 1479 CA LEU A 236 13324 13816 13614 100 542 -1422 C ATOM 1480 C LEU A 236 51.171 21.812 31.737 1.00112.96 C ANISOU 1480 C LEU A 236 14022 14742 14155 -14 524 -1538 C ATOM 1481 O LEU A 236 51.595 21.478 30.625 1.00121.54 O ANISOU 1481 O LEU A 236 15056 15962 15160 -5 594 -1691 O ATOM 1482 CB LEU A 236 51.223 20.071 33.546 1.00113.67 C ANISOU 1482 CB LEU A 236 14223 14361 14607 123 604 -1521 C ATOM 1483 CG LEU A 236 52.173 18.962 34.005 1.00115.21 C ANISOU 1483 CG LEU A 236 14421 14378 14977 275 701 -1540 C ATOM 1484 CD1 LEU A 236 53.313 19.513 34.853 1.00116.29 C ANISOU 1484 CD1 LEU A 236 14507 14551 15125 383 651 -1329 C ATOM 1485 CD2 LEU A 236 51.400 17.905 34.773 1.00117.79 C ANISOU 1485 CD2 LEU A 236 14853 14411 15489 286 753 -1573 C ATOM 1486 N THR A 237 50.094 22.591 31.882 1.00106.15 N ANISOU 1486 N THR A 237 13193 13918 13220 -115 430 -1468 N ATOM 1487 CA THR A 237 49.442 23.175 30.712 1.00 98.19 C ANISOU 1487 CA THR A 237 12154 13133 12021 -208 393 -1541 C ATOM 1488 C THR A 237 50.379 24.128 29.985 1.00100.45 C ANISOU 1488 C THR A 237 12366 13656 12145 -197 390 -1447 C ATOM 1489 O THR A 237 50.524 24.063 28.760 1.00113.02 O ANISOU 1489 O THR A 237 13913 15440 13590 -215 432 -1567 O ATOM 1490 CB THR A 237 48.168 23.913 31.120 1.00103.72 C ANISOU 1490 CB THR A 237 12895 13823 12692 -298 287 -1453 C ATOM 1491 OG1 THR A 237 47.240 22.989 31.701 1.00123.45 O ANISOU 1491 OG1 THR A 237 15455 16115 15338 -325 306 -1558 O ATOM 1492 CG2 THR A 237 47.531 24.583 29.910 1.00 99.65 C ANISOU 1492 CG2 THR A 237 12339 13558 11967 -374 236 -1501 C ATOM 1493 N ILE A 238 51.026 25.025 30.732 1.00101.76 N ANISOU 1493 N ILE A 238 12516 13816 12333 -173 346 -1236 N ATOM 1494 CA ILE A 238 51.897 26.016 30.119 1.00103.14 C ANISOU 1494 CA ILE A 238 12619 14197 12373 -179 352 -1129 C ATOM 1495 C ILE A 238 53.140 25.371 29.515 1.00104.55 C ANISOU 1495 C ILE A 238 12726 14449 12549 -103 463 -1232 C ATOM 1496 O ILE A 238 53.799 25.982 28.665 1.00 91.52 O ANISOU 1496 O ILE A 238 11010 13005 10760 -118 499 -1201 O ATOM 1497 CB ILE A 238 52.255 27.102 31.153 1.00103.19 C ANISOU 1497 CB ILE A 238 12620 14156 12431 -185 282 -902 C ATOM 1498 CG1 ILE A 238 52.219 28.487 30.504 1.00118.38 C ANISOU 1498 CG1 ILE A 238 14514 16268 14197 -258 245 -768 C ATOM 1499 CG2 ILE A 238 53.615 26.832 31.781 1.00 96.37 C ANISOU 1499 CG2 ILE A 238 11699 13240 11676 -95 329 -859 C ATOM 1500 CD1 ILE A 238 52.101 29.623 31.499 1.00121.00 C ANISOU 1500 CD1 ILE A 238 14862 16528 14585 -295 164 -572 C ATOM 1501 N TYR A 239 53.474 24.143 29.919 1.00113.07 N ANISOU 1501 N TYR A 239 13816 15363 13783 -17 529 -1352 N ATOM 1502 CA TYR A 239 54.589 23.434 29.299 1.00114.78 C ANISOU 1502 CA TYR A 239 13959 15640 14010 67 644 -1476 C ATOM 1503 C TYR A 239 54.184 22.840 27.956 1.00112.01 C ANISOU 1503 C TYR A 239 13604 15418 13538 30 714 -1707 C ATOM 1504 O TYR A 239 54.935 22.931 26.978 1.00114.52 O ANISOU 1504 O TYR A 239 13848 15932 13734 42 789 -1773 O ATOM 1505 CB TYR A 239 55.112 22.344 30.239 1.00118.29 C ANISOU 1505 CB TYR A 239 14418 15850 14678 189 691 -1508 C ATOM 1506 CG TYR A 239 55.792 21.184 29.535 1.00129.79 C ANISOU 1506 CG TYR A 239 15830 17297 16188 278 824 -1716 C ATOM 1507 CD1 TYR A 239 57.109 21.281 29.098 1.00137.84 C ANISOU 1507 CD1 TYR A 239 16738 18456 17179 352 896 -1720 C ATOM 1508 CD2 TYR A 239 55.119 19.986 29.320 1.00134.25 C ANISOU 1508 CD2 TYR A 239 16458 17707 16846 286 887 -1921 C ATOM 1509 CE1 TYR A 239 57.734 20.218 28.457 1.00136.18 C ANISOU 1509 CE1 TYR A 239 16481 18235 17025 441 1026 -1921 C ATOM 1510 CE2 TYR A 239 55.734 18.921 28.681 1.00137.02 C ANISOU 1510 CE2 TYR A 239 16770 18032 17261 369 1019 -2127 C ATOM 1511 CZ TYR A 239 57.041 19.041 28.252 1.00134.66 C ANISOU 1511 CZ TYR A 239 16361 17877 16927 452 1087 -2126 C ATOM 1512 OH TYR A 239 57.651 17.981 27.617 1.00135.95 O ANISOU 1512 OH TYR A 239 16479 18012 17162 542 1226 -2342 O ATOM 1513 N VAL A 240 53.000 22.225 27.894 1.00106.44 N ANISOU 1513 N VAL A 240 12969 14614 12860 -22 694 -1842 N ATOM 1514 CA VAL A 240 52.516 21.654 26.640 1.00104.70 C ANISOU 1514 CA VAL A 240 12738 14528 12516 -70 749 -2086 C ATOM 1515 C VAL A 240 52.312 22.751 25.602 1.00112.93 C ANISOU 1515 C VAL A 240 13743 15880 13287 -148 701 -2027 C ATOM 1516 O VAL A 240 52.730 22.623 24.444 1.00113.89 O ANISOU 1516 O VAL A 240 13810 16214 13250 -150 774 -2156 O ATOM 1517 CB VAL A 240 51.220 20.856 26.874 1.00 95.50 C ANISOU 1517 CB VAL A 240 11647 13193 11447 -127 728 -2238 C ATOM 1518 CG1 VAL A 240 50.730 20.251 25.571 1.00 88.00 C ANISOU 1518 CG1 VAL A 240 10672 12397 10365 -185 780 -2520 C ATOM 1519 CG2 VAL A 240 51.441 19.769 27.908 1.00105.18 C ANISOU 1519 CG2 VAL A 240 12921 14097 12944 -44 791 -2271 C ATOM 1520 N LEU A 241 51.671 23.852 26.007 1.00106.38 N ANISOU 1520 N LEU A 241 12941 15078 12399 -209 584 -1824 N ATOM 1521 CA LEU A 241 51.357 24.919 25.064 1.00102.99 C ANISOU 1521 CA LEU A 241 12488 14922 11722 -275 534 -1739 C ATOM 1522 C LEU A 241 52.612 25.518 24.448 1.00105.25 C ANISOU 1522 C LEU A 241 12703 15398 11888 -246 607 -1647 C ATOM 1523 O LEU A 241 52.590 25.930 23.283 1.00 99.60 O ANISOU 1523 O LEU A 241 11957 14943 10943 -281 626 -1668 O ATOM 1524 CB LEU A 241 50.536 26.006 25.753 1.00104.07 C ANISOU 1524 CB LEU A 241 12668 15012 11861 -326 405 -1520 C ATOM 1525 CG LEU A 241 49.118 25.627 26.165 1.00 94.48 C ANISOU 1525 CG LEU A 241 11509 13673 10715 -376 326 -1601 C ATOM 1526 CD1 LEU A 241 48.412 26.836 26.754 1.00 95.64 C ANISOU 1526 CD1 LEU A 241 11685 13805 10851 -417 209 -1376 C ATOM 1527 CD2 LEU A 241 48.351 25.068 24.975 1.00 98.14 C ANISOU 1527 CD2 LEU A 241 11953 14313 11022 -423 331 -1832 C ATOM 1528 N ARG A 242 53.710 25.575 25.205 1.00120.30 N ANISOU 1528 N ARG A 242 14576 17191 13940 -183 650 -1545 N ATOM 1529 CA ARG A 242 54.940 26.142 24.666 1.00123.54 C ANISOU 1529 CA ARG A 242 14904 17778 14257 -164 729 -1463 C ATOM 1530 C ARG A 242 55.599 25.191 23.675 1.00125.74 C ANISOU 1530 C ARG A 242 15125 18179 14471 -117 862 -1694 C ATOM 1531 O ARG A 242 56.110 25.626 22.637 1.00121.30 O ANISOU 1531 O ARG A 242 14507 17866 13715 -138 930 -1691 O ATOM 1532 CB ARG A 242 55.907 26.485 25.797 1.00127.92 C ANISOU 1532 CB ARG A 242 15422 18192 14991 -115 726 -1302 C ATOM 1533 CG ARG A 242 57.056 27.382 25.359 1.00140.20 C ANISOU 1533 CG ARG A 242 16885 19929 16457 -127 791 -1173 C ATOM 1534 CD ARG A 242 58.375 26.989 26.017 1.00148.70 C ANISOU 1534 CD ARG A 242 17873 20924 17703 -39 854 -1174 C ATOM 1535 NE ARG A 242 58.905 25.735 25.485 1.00151.16 N ANISOU 1535 NE ARG A 242 18140 21249 18045 49 967 -1401 N ATOM 1536 CZ ARG A 242 59.655 25.645 24.391 1.00151.23 C ANISOU 1536 CZ ARG A 242 18067 21468 17926 57 1088 -1494 C ATOM 1537 NH1 ARG A 242 60.091 24.462 23.980 1.00153.01 N ANISOU 1537 NH1 ARG A 242 18255 21681 18202 144 1193 -1718 N ATOM 1538 NH2 ARG A 242 59.963 26.737 23.704 1.00153.77 N ANISOU 1538 NH2 ARG A 242 18347 22005 18072 -22 1115 -1364 N ATOM 1539 N ARG A 243 55.604 23.889 23.983 1.00129.84 N ANISOU 1539 N ARG A 243 15657 18521 15154 -51 912 -1895 N ATOM 1540 CA ARG A 243 56.231 22.918 23.092 1.00130.59 C ANISOU 1540 CA ARG A 243 15697 18705 15216 2 1049 -2139 C ATOM 1541 C ARG A 243 55.517 22.859 21.747 1.00131.04 C ANISOU 1541 C ARG A 243 15761 19005 15022 -73 1063 -2306 C ATOM 1542 O ARG A 243 56.162 22.783 20.695 1.00140.63 O ANISOU 1542 O ARG A 243 16911 20445 16076 -65 1167 -2412 O ATOM 1543 CB ARG A 243 56.251 21.538 23.751 1.00127.04 C ANISOU 1543 CB ARG A 243 15275 17977 15019 88 1099 -2312 C ATOM 1544 N GLN A 244 54.183 22.904 21.759 1.00124.09 N ANISOU 1544 N GLN A 244 14952 18102 14096 -146 959 -2336 N ATOM 1545 CA GLN A 244 53.441 22.825 20.507 1.00121.52 C ANISOU 1545 CA GLN A 244 14624 18027 13522 -215 954 -2506 C ATOM 1546 C GLN A 244 53.508 24.131 19.726 1.00122.66 C ANISOU 1546 C GLN A 244 14744 18475 13387 -262 917 -2307 C ATOM 1547 O GLN A 244 53.514 24.109 18.490 1.00130.33 O ANISOU 1547 O GLN A 244 15682 19729 14109 -287 966 -2428 O ATOM 1548 CB GLN A 244 51.991 22.437 20.781 1.00121.94 C ANISOU 1548 CB GLN A 244 14741 17966 13624 -278 852 -2610 C ATOM 1549 CG GLN A 244 51.838 21.064 21.408 1.00129.15 C ANISOU 1549 CG GLN A 244 15685 18582 14804 -244 910 -2826 C ATOM 1550 CD GLN A 244 50.394 20.712 21.689 1.00135.21 C ANISOU 1550 CD GLN A 244 16507 19237 15628 -323 820 -2928 C ATOM 1551 OE1 GLN A 244 49.549 21.593 21.855 1.00133.36 O ANISOU 1551 OE1 GLN A 244 16294 19073 15304 -382 692 -2768 O ATOM 1552 NE2 GLN A 244 50.099 19.418 21.740 1.00140.61 N ANISOU 1552 NE2 GLN A 244 17208 19741 16475 -325 894 -3199 N ATOM 1553 N ALA A 245 53.560 25.271 20.419 1.00116.96 N ANISOU 1553 N ALA A 245 14041 17699 12700 -276 839 -2005 N ATOM 1554 CA ALA A 245 53.654 26.549 19.722 1.00109.66 C ANISOU 1554 CA ALA A 245 13102 17029 11537 -318 818 -1791 C ATOM 1555 C ALA A 245 55.039 26.749 19.119 1.00122.20 C ANISOU 1555 C ALA A 245 14612 18779 13038 -289 960 -1760 C ATOM 1556 O ALA A 245 55.167 27.276 18.008 1.00118.74 O ANISOU 1556 O ALA A 245 14150 18630 12335 -319 1004 -1721 O ATOM 1557 CB ALA A 245 53.312 27.694 20.674 1.00101.33 C ANISOU 1557 CB ALA A 245 12089 15839 10574 -344 706 -1493 C ATOM 1558 N ALA A1001 56.087 26.331 19.836 1.00127.18 N ANISOU 1558 N ALA A1001 15198 19239 13887 -228 1037 -1773 N ATOM 1559 CA ALA A1001 57.452 26.487 19.344 1.00127.69 C ANISOU 1559 CA ALA A1001 15170 19449 13900 -198 1179 -1753 C ATOM 1560 C ALA A1001 57.683 25.742 18.038 1.00129.85 C ANISOU 1560 C ALA A1001 15401 19960 13978 -186 1300 -2007 C ATOM 1561 O ALA A1001 58.619 26.078 17.302 1.00130.04 O ANISOU 1561 O ALA A1001 15352 20195 13864 -185 1420 -1977 O ATOM 1562 CB ALA A1001 58.452 26.012 20.403 1.00128.42 C ANISOU 1562 CB ALA A1001 15208 19309 14276 -118 1224 -1755 C ATOM 1563 N ASP A1002 56.860 24.734 17.742 1.00133.65 N ANISOU 1563 N ASP A1002 15920 20412 14447 -183 1279 -2268 N ATOM 1564 CA ASP A1002 56.965 24.035 16.468 1.00136.81 C ANISOU 1564 CA ASP A1002 16282 21054 14644 -182 1387 -2539 C ATOM 1565 C ASP A1002 56.772 25.003 15.306 1.00143.89 C ANISOU 1565 C ASP A1002 17175 22317 15181 -247 1385 -2419 C ATOM 1566 O ASP A1002 57.627 25.116 14.421 1.00149.26 O ANISOU 1566 O ASP A1002 17789 23236 15686 -239 1518 -2449 O ATOM 1567 CB ASP A1002 55.938 22.903 16.412 1.00134.03 C ANISOU 1567 CB ASP A1002 15978 20599 14349 -191 1345 -2833 C ATOM 1568 CG ASP A1002 56.252 21.880 15.333 1.00154.27 C ANISOU 1568 CG ASP A1002 18491 23328 16797 -173 1484 -3181 C ATOM 1569 OD1 ASP A1002 57.058 22.178 14.422 1.00162.11 O ANISOU 1569 OD1 ASP A1002 19420 24592 17583 -166 1595 -3184 O ATOM 1570 OD2 ASP A1002 55.684 20.771 15.395 1.00156.93 O ANISOU 1570 OD2 ASP A1002 18852 23521 17253 -171 1490 -3459 O ATOM 1571 N LEU A1003 55.648 25.723 15.301 1.00143.76 N ANISOU 1571 N LEU A1003 17224 22350 15046 -305 1237 -2272 N ATOM 1572 CA LEU A1003 55.380 26.691 14.242 1.00136.23 C ANISOU 1572 CA LEU A1003 16277 21736 13750 -352 1220 -2120 C ATOM 1573 C LEU A1003 56.152 27.989 14.452 1.00130.77 C ANISOU 1573 C LEU A1003 15572 21068 13047 -364 1254 -1766 C ATOM 1574 O LEU A1003 56.601 28.606 13.481 1.00131.05 O ANISOU 1574 O LEU A1003 15581 21387 12825 -385 1338 -1662 O ATOM 1575 CB LEU A1003 53.880 26.978 14.163 1.00133.60 C ANISOU 1575 CB LEU A1003 16008 21448 13306 -394 1046 -2089 C ATOM 1576 N GLU A1004 56.318 28.413 15.707 1.00131.71 N ANISOU 1576 N GLU A1004 15708 20895 13440 -358 1197 -1584 N ATOM 1577 CA GLU A1004 56.959 29.696 15.981 1.00133.03 C ANISOU 1577 CA GLU A1004 15864 21060 13622 -387 1220 -1258 C ATOM 1578 C GLU A1004 58.402 29.716 15.493 1.00142.17 C ANISOU 1578 C GLU A1004 16926 22353 14740 -377 1405 -1264 C ATOM 1579 O GLU A1004 58.824 30.659 14.814 1.00139.88 O ANISOU 1579 O GLU A1004 16619 22266 14264 -419 1478 -1068 O ATOM 1580 CB GLU A1004 56.895 30.005 17.476 1.00123.71 C ANISOU 1580 CB GLU A1004 14709 19541 12754 -383 1126 -1118 C ATOM 1581 CG GLU A1004 55.567 30.568 17.946 1.00119.44 C ANISOU 1581 CG GLU A1004 14258 18899 12226 -413 955 -987 C ATOM 1582 CD GLU A1004 55.516 30.702 19.451 1.00132.40 C ANISOU 1582 CD GLU A1004 15922 20210 14174 -405 874 -896 C ATOM 1583 OE1 GLU A1004 56.372 30.086 20.124 1.00134.57 O ANISOU 1583 OE1 GLU A1004 16149 20333 14650 -364 934 -984 O ATOM 1584 OE2 GLU A1004 54.628 31.418 19.962 1.00134.05 O ANISOU 1584 OE2 GLU A1004 16193 20321 14418 -434 752 -737 O ATOM 1585 N ASP A1005 59.179 28.684 15.835 1.00166.06 N ANISOU 1585 N ASP A1005 19884 25264 17945 -317 1490 -1481 N ATOM 1586 CA ASP A1005 60.581 28.649 15.428 1.00175.80 C ANISOU 1586 CA ASP A1005 21007 26621 19167 -299 1670 -1503 C ATOM 1587 C ASP A1005 60.731 28.633 13.911 1.00172.68 C ANISOU 1587 C ASP A1005 20589 26593 18429 -321 1791 -1591 C ATOM 1588 O ASP A1005 61.721 29.149 13.381 1.00176.69 O ANISOU 1588 O ASP A1005 21022 27274 18837 -343 1934 -1492 O ATOM 1589 CB ASP A1005 61.277 27.438 16.050 1.00189.76 C ANISOU 1589 CB ASP A1005 22707 28198 21194 -208 1729 -1738 C ATOM 1590 CG ASP A1005 61.458 27.577 17.552 1.00198.09 C ANISOU 1590 CG ASP A1005 23763 28933 22570 -179 1638 -1611 C ATOM 1591 OD1 ASP A1005 60.782 28.438 18.158 1.00192.59 O ANISOU 1591 OD1 ASP A1005 23138 28131 21905 -233 1508 -1395 O ATOM 1592 OD2 ASP A1005 62.274 26.822 18.125 1.00198.07 O ANISOU 1592 OD2 ASP A1005 23685 28790 22783 -96 1696 -1728 O ATOM 1593 N ASN A1006 59.768 28.048 13.196 1.00163.80 N ANISOU 1593 N ASN A1006 19519 25603 17114 -321 1739 -1782 N ATOM 1594 CA ASN A1006 59.795 28.111 11.739 1.00161.56 C ANISOU 1594 CA ASN A1006 19220 25703 16463 -345 1835 -1854 C ATOM 1595 C ASN A1006 59.316 29.469 11.235 1.00161.54 C ANISOU 1595 C ASN A1006 19277 25891 16211 -407 1780 -1527 C ATOM 1596 O ASN A1006 59.848 29.992 10.249 1.00160.70 O ANISOU 1596 O ASN A1006 19140 26074 15843 -434 1904 -1430 O ATOM 1597 CB ASN A1006 58.944 26.987 11.145 1.00159.26 C ANISOU 1597 CB ASN A1006 18954 25505 16051 -327 1797 -2199 C ATOM 1598 CG ASN A1006 59.443 25.609 11.536 1.00157.42 C ANISOU 1598 CG ASN A1006 18668 25079 16065 -260 1877 -2529 C ATOM 1599 OD1 ASN A1006 58.658 24.729 11.889 1.00155.68 O ANISOU 1599 OD1 ASN A1006 18489 24692 15971 -245 1795 -2744 O ATOM 1600 ND2 ASN A1006 60.755 25.416 11.477 1.00159.85 N ANISOU 1600 ND2 ASN A1006 18880 25403 16454 -218 2046 -2567 N ATOM 1601 N TRP A1007 58.315 30.055 11.902 1.00159.24 N ANISOU 1601 N TRP A1007 19069 25437 16000 -426 1603 -1348 N ATOM 1602 CA TRP A1007 57.845 31.382 11.518 1.00164.77 C ANISOU 1602 CA TRP A1007 19827 26276 16501 -470 1547 -1015 C ATOM 1603 C TRP A1007 58.827 32.469 11.934 1.00175.85 C ANISOU 1603 C TRP A1007 21202 27588 18023 -508 1639 -710 C ATOM 1604 O TRP A1007 58.879 33.531 11.301 1.00170.64 O ANISOU 1604 O TRP A1007 20568 27106 17162 -546 1682 -444 O ATOM 1605 CB TRP A1007 56.470 31.649 12.129 1.00162.32 C ANISOU 1605 CB TRP A1007 19604 25809 16262 -471 1334 -934 C ATOM 1606 N GLU A1008 59.605 32.231 12.995 1.00192.43 N ANISOU 1606 N GLU A1008 23246 29417 20451 -498 1670 -742 N ATOM 1607 CA GLU A1008 60.598 33.214 13.416 1.00186.26 C ANISOU 1607 CA GLU A1008 22416 28555 19799 -546 1762 -491 C ATOM 1608 C GLU A1008 61.766 33.271 12.439 1.00185.36 C ANISOU 1608 C GLU A1008 22211 28704 19514 -567 1979 -503 C ATOM 1609 O GLU A1008 62.258 34.360 12.116 1.00189.12 O ANISOU 1609 O GLU A1008 22677 29271 19910 -632 2072 -238 O ATOM 1610 CB GLU A1008 61.094 32.892 14.825 1.00181.33 C ANISOU 1610 CB GLU A1008 21744 27599 19554 -524 1722 -542 C ATOM 1611 N THR A1009 62.223 32.112 11.957 1.00183.81 N ANISOU 1611 N THR A1009 21946 28626 19268 -515 2074 -811 N ATOM 1612 CA THR A1009 63.347 32.088 11.025 1.00174.00 C ANISOU 1612 CA THR A1009 20606 27644 17863 -530 2293 -852 C ATOM 1613 C THR A1009 62.982 32.761 9.708 1.00166.46 C ANISOU 1613 C THR A1009 19707 27036 16505 -574 2349 -703 C ATOM 1614 O THR A1009 63.751 33.573 9.178 1.00172.98 O ANISOU 1614 O THR A1009 20493 28019 17213 -631 2503 -501 O ATOM 1615 CB THR A1009 63.803 30.648 10.780 1.00169.34 C ANISOU 1615 CB THR A1009 19936 27099 17308 -453 2377 -1238 C ATOM 1616 OG1 THR A1009 62.671 29.838 10.430 1.00170.31 O ANISOU 1616 OG1 THR A1009 20139 27268 17305 -416 2264 -1460 O ATOM 1617 CG2 THR A1009 64.473 30.079 12.021 1.00162.79 C ANISOU 1617 CG2 THR A1009 19027 25953 16871 -398 2364 -1338 C ATOM 1618 N LEU A1010 61.810 32.427 9.160 1.00158.22 N ANISOU 1618 N LEU A1010 18751 26125 15240 -548 2229 -799 N ATOM 1619 CA LEU A1010 61.374 33.041 7.911 1.00153.93 C ANISOU 1619 CA LEU A1010 18263 25934 14287 -573 2259 -652 C ATOM 1620 C LEU A1010 61.268 34.556 8.048 1.00160.76 C ANISOU 1620 C LEU A1010 19190 26755 15135 -630 2241 -214 C ATOM 1621 O LEU A1010 61.638 35.298 7.130 1.00155.84 O ANISOU 1621 O LEU A1010 18574 26387 14252 -667 2372 -7 O ATOM 1622 CB LEU A1010 60.039 32.438 7.478 1.00141.20 C ANISOU 1622 CB LEU A1010 16724 24445 12480 -534 2094 -834 C ATOM 1623 CG LEU A1010 59.388 33.055 6.245 1.00139.68 C ANISOU 1623 CG LEU A1010 16594 24630 11848 -542 2078 -679 C ATOM 1624 CD1 LEU A1010 59.116 31.982 5.202 1.00134.91 C ANISOU 1624 CD1 LEU A1010 15962 24346 10950 -512 2106 -1038 C ATOM 1625 CD2 LEU A1010 58.107 33.780 6.640 1.00136.64 C ANISOU 1625 CD2 LEU A1010 16311 24139 11468 -534 1859 -452 C ATOM 1626 N ASN A1011 60.779 35.031 9.197 1.00173.42 N ANISOU 1626 N ASN A1011 20843 28030 17021 -637 2092 -67 N ATOM 1627 CA ASN A1011 60.698 36.470 9.437 1.00180.06 C ANISOU 1627 CA ASN A1011 21741 28777 17897 -691 2081 334 C ATOM 1628 C ASN A1011 62.087 37.093 9.532 1.00178.19 C ANISOU 1628 C ASN A1011 21418 28507 17779 -763 2285 486 C ATOM 1629 O ASN A1011 62.360 38.125 8.908 1.00179.81 O ANISOU 1629 O ASN A1011 21648 28846 17824 -818 2397 775 O ATOM 1630 CB ASN A1011 59.898 36.746 10.711 1.00182.11 C ANISOU 1630 CB ASN A1011 22060 28682 18452 -683 1883 410 C ATOM 1631 CG ASN A1011 58.414 36.486 10.539 1.00183.98 C ANISOU 1631 CG ASN A1011 22386 28969 18548 -628 1684 352 C ATOM 1632 OD1 ASN A1011 57.985 35.908 9.541 1.00182.35 O ANISOU 1632 OD1 ASN A1011 22186 29053 18045 -593 1678 196 O ATOM 1633 ND2 ASN A1011 57.622 36.912 11.517 1.00182.64 N ANISOU 1633 ND2 ASN A1011 22275 28527 18592 -623 1520 465 N ATOM 1634 N ASP A1012 62.978 36.485 10.323 1.00175.72 N ANISOU 1634 N ASP A1012 21000 28013 17754 -764 2338 299 N ATOM 1635 CA ASP A1012 64.329 37.022 10.467 1.00172.53 C ANISOU 1635 CA ASP A1012 20487 27583 17484 -836 2526 412 C ATOM 1636 C ASP A1012 65.065 37.025 9.131 1.00180.07 C ANISOU 1636 C ASP A1012 21388 28899 18131 -861 2749 411 C ATOM 1637 O ASP A1012 65.716 38.013 8.770 1.00179.35 O ANISOU 1637 O ASP A1012 21274 28881 17987 -946 2904 667 O ATOM 1638 CB ASP A1012 65.112 36.220 11.509 1.00162.11 C ANISOU 1638 CB ASP A1012 19048 26042 16503 -807 2526 179 C ATOM 1639 CG ASP A1012 64.812 36.656 12.934 1.00158.57 C ANISOU 1639 CG ASP A1012 18627 25234 16389 -822 2369 283 C ATOM 1640 OD1 ASP A1012 65.375 37.682 13.375 1.00157.25 O ANISOU 1640 OD1 ASP A1012 18425 24953 16369 -909 2426 507 O ATOM 1641 OD2 ASP A1012 64.024 35.968 13.617 1.00158.34 O ANISOU 1641 OD2 ASP A1012 18650 25036 16478 -754 2196 132 O ATOM 1642 N ASN A1013 64.972 35.923 8.380 1.00187.00 N ANISOU 1642 N ASN A1013 22243 30004 18804 -794 2778 117 N ATOM 1643 CA ASN A1013 65.624 35.856 7.076 1.00195.55 C ANISOU 1643 CA ASN A1013 23277 31459 19566 -813 2992 89 C ATOM 1644 C ASN A1013 65.008 36.827 6.076 1.00210.03 C ANISOU 1644 C ASN A1013 25225 33540 21039 -846 3008 391 C ATOM 1645 O ASN A1013 65.615 37.095 5.034 1.00216.32 O ANISOU 1645 O ASN A1013 25989 34636 21565 -882 3206 468 O ATOM 1646 CB ASN A1013 65.567 34.430 6.528 1.00193.58 C ANISOU 1646 CB ASN A1013 22983 31386 19183 -731 3008 -322 C ATOM 1647 N LEU A1014 63.817 37.357 6.365 1.00217.06 N ANISOU 1647 N LEU A1014 26242 34317 21913 -828 2808 569 N ATOM 1648 CA LEU A1014 63.253 38.417 5.538 1.00220.66 C ANISOU 1648 CA LEU A1014 26807 34969 22067 -847 2815 912 C ATOM 1649 C LEU A1014 63.892 39.768 5.834 1.00224.09 C ANISOU 1649 C LEU A1014 27245 35249 22649 -942 2937 1295 C ATOM 1650 O LEU A1014 63.948 40.629 4.947 1.00231.77 O ANISOU 1650 O LEU A1014 28272 36429 23360 -975 3055 1586 O ATOM 1651 CB LEU A1014 61.738 38.497 5.743 1.00219.41 C ANISOU 1651 CB LEU A1014 26768 34745 21850 -782 2556 961 C ATOM 1652 N LYS A1015 64.375 39.972 7.065 1.00210.43 N ANISOU 1652 N LYS A1015 25458 33162 21334 -989 2916 1300 N ATOM 1653 CA LYS A1015 65.007 41.241 7.412 1.00199.41 C ANISOU 1653 CA LYS A1015 24054 31598 20114 -1095 3035 1630 C ATOM 1654 C LYS A1015 66.317 41.431 6.656 1.00223.92 C ANISOU 1654 C LYS A1015 27053 34918 23110 -1176 3324 1674 C ATOM 1655 O LYS A1015 66.635 42.544 6.219 1.00203.71 O ANISOU 1655 O LYS A1015 24526 32398 20476 -1260 3472 2005 O ATOM 1656 CB LYS A1015 65.240 41.312 8.922 1.00172.33 C ANISOU 1656 CB LYS A1015 20570 27765 17141 -1127 2937 1573 C ATOM 1657 N VAL A1016 67.090 40.353 6.488 1.00259.26 N ANISOU 1657 N VAL A1016 31398 39526 27583 -1152 3418 1344 N ATOM 1658 CA VAL A1016 68.362 40.449 5.780 1.00261.30 C ANISOU 1658 CA VAL A1016 31536 40002 27745 -1225 3701 1351 C ATOM 1659 C VAL A1016 68.142 40.751 4.302 1.00263.97 C ANISOU 1659 C VAL A1016 31952 40732 27611 -1223 3830 1510 C ATOM 1660 O VAL A1016 68.990 41.384 3.659 1.00272.90 O ANISOU 1660 O VAL A1016 33038 42021 28632 -1313 4074 1696 O ATOM 1661 CB VAL A1016 69.180 39.160 5.979 1.00263.22 C ANISOU 1661 CB VAL A1016 31616 40286 28108 -1176 3758 941 C ATOM 1662 N ILE A1017 67.016 40.308 3.735 1.00244.06 N ANISOU 1662 N ILE A1017 29544 38389 24798 -1125 3675 1439 N ATOM 1663 CA ILE A1017 66.661 40.710 2.379 1.00223.06 C ANISOU 1663 CA ILE A1017 26974 36109 21668 -1114 3763 1632 C ATOM 1664 C ILE A1017 66.307 42.186 2.293 1.00215.76 C ANISOU 1664 C ILE A1017 26171 35097 20711 -1167 3778 2122 C ATOM 1665 O ILE A1017 66.254 42.741 1.189 1.00210.11 O ANISOU 1665 O ILE A1017 25523 34679 19630 -1174 3903 2365 O ATOM 1666 CB ILE A1017 65.497 39.851 1.844 1.00213.03 C ANISOU 1666 CB ILE A1017 25782 35058 20103 -995 3569 1411 C ATOM 1667 N GLU A1018 66.067 42.836 3.435 1.00215.81 N ANISOU 1667 N GLU A1018 26207 34701 21089 -1201 3659 2273 N ATOM 1668 CA GLU A1018 65.840 44.274 3.500 1.00222.25 C ANISOU 1668 CA GLU A1018 27126 35362 21955 -1260 3693 2728 C ATOM 1669 C GLU A1018 66.986 45.006 4.193 1.00227.54 C ANISOU 1669 C GLU A1018 27702 35766 22989 -1405 3873 2855 C ATOM 1670 O GLU A1018 66.798 46.126 4.679 1.00221.33 O ANISOU 1670 O GLU A1018 26984 34715 22396 -1465 3865 3165 O ATOM 1671 CB GLU A1018 64.517 44.572 4.207 1.00213.39 C ANISOU 1671 CB GLU A1018 26126 33995 20956 -1184 3410 2823 C ATOM 1672 N LYS A1019 68.173 44.396 4.245 1.00236.00 N ANISOU 1672 N LYS A1019 28606 36902 24162 -1463 4039 2612 N ATOM 1673 CA LYS A1019 69.304 45.014 4.937 1.00230.30 C ANISOU 1673 CA LYS A1019 27762 35945 23795 -1605 4202 2689 C ATOM 1674 C LYS A1019 69.803 46.271 4.214 1.00229.28 C ANISOU 1674 C LYS A1019 27672 35891 23554 -1727 4456 3094 C ATOM 1675 O LYS A1019 69.900 47.339 4.831 1.00236.15 O ANISOU 1675 O LYS A1019 28569 36464 24692 -1826 4484 3348 O ATOM 1676 CB LYS A1019 70.431 43.991 5.145 1.00231.00 C ANISOU 1676 CB LYS A1019 27647 36110 24013 -1618 4307 2317 C ATOM 1677 N ALA A1020 70.134 46.192 2.915 1.00203.88 N ANISOU 1677 N ALA A1020 24460 33059 19946 -1728 4656 3163 N ATOM 1678 CA ALA A1020 70.100 45.007 2.055 1.00175.40 C ANISOU 1678 CA ALA A1020 20817 29835 15991 -1627 4664 2865 C ATOM 1679 C ALA A1020 71.381 44.901 1.231 1.00161.05 C ANISOU 1679 C ALA A1020 18864 28300 14027 -1716 4990 2825 C ATOM 1680 O ALA A1020 71.677 45.765 0.404 1.00157.39 O ANISOU 1680 O ALA A1020 18451 27996 13355 -1794 5207 3152 O ATOM 1681 CB ALA A1020 68.877 45.041 1.144 1.00169.33 C ANISOU 1681 CB ALA A1020 20227 29319 14791 -1510 4537 3008 C ATOM 1682 N VAL A1026 72.329 36.436 0.060 1.00195.69 N ANISOU 1682 N VAL A1026 22684 33673 17997 -1128 4864 104 N ATOM 1683 CA VAL A1026 70.907 36.544 -0.248 1.00192.30 C ANISOU 1683 CA VAL A1026 22447 33308 17311 -1074 4643 195 C ATOM 1684 C VAL A1026 70.383 35.222 -0.795 1.00187.30 C ANISOU 1684 C VAL A1026 21819 32884 16463 -966 4569 -226 C ATOM 1685 O VAL A1026 69.274 34.802 -0.468 1.00192.70 O ANISOU 1685 O VAL A1026 22601 33458 17159 -896 4320 -334 O ATOM 1686 CB VAL A1026 70.638 37.685 -1.240 1.00201.07 C ANISOU 1686 CB VAL A1026 23676 34688 18035 -1139 4745 603 C ATOM 1687 N LYS A1027 71.185 34.569 -1.639 1.00200.31 N ANISOU 1687 N LYS A1027 23354 34836 17918 -957 4794 -475 N ATOM 1688 CA LYS A1027 70.817 33.249 -2.138 1.00192.74 C ANISOU 1688 CA LYS A1027 22381 34060 16792 -861 4752 -923 C ATOM 1689 C LYS A1027 70.843 32.207 -1.029 1.00194.34 C ANISOU 1689 C LYS A1027 22511 33898 17432 -782 4616 -1258 C ATOM 1690 O LYS A1027 70.198 31.162 -1.156 1.00183.49 O ANISOU 1690 O LYS A1027 21164 32552 16002 -701 4502 -1601 O ATOM 1691 CB LYS A1027 71.752 32.844 -3.279 1.00152.85 C ANISOU 1691 CB LYS A1027 17217 29411 11447 -873 5049 -1110 C ATOM 1692 CG LYS A1027 71.070 32.074 -4.395 1.00155.42 C ANISOU 1692 CG LYS A1027 17601 30124 11326 -814 5031 -1392 C ATOM 1693 CD LYS A1027 71.856 32.193 -5.690 1.00171.88 C ANISOU 1693 CD LYS A1027 19623 32679 13005 -857 5335 -1400 C ATOM 1694 CE LYS A1027 71.023 31.797 -6.899 1.00175.37 C ANISOU 1694 CE LYS A1027 20158 33566 12908 -819 5297 -1560 C ATOM 1695 NZ LYS A1027 71.689 32.195 -8.173 1.00167.50 N ANISOU 1695 NZ LYS A1027 19132 33050 11460 -872 5585 -1454 N ATOM 1696 N ASP A1028 71.576 32.472 0.053 1.00205.34 N ANISOU 1696 N ASP A1028 23810 34954 19257 -805 4630 -1165 N ATOM 1697 CA ASP A1028 71.527 31.667 1.265 1.00209.37 C ANISOU 1697 CA ASP A1028 24272 35080 20202 -727 4472 -1394 C ATOM 1698 C ASP A1028 70.413 32.096 2.209 1.00212.34 C ANISOU 1698 C ASP A1028 24789 35139 20751 -725 4184 -1204 C ATOM 1699 O ASP A1028 69.950 31.274 3.011 1.00210.62 O ANISOU 1699 O ASP A1028 24582 34660 20782 -647 4013 -1426 O ATOM 1700 CB ASP A1028 72.873 31.735 2.005 1.00210.94 C ANISOU 1700 CB ASP A1028 24284 35091 20771 -744 4614 -1392 C ATOM 1701 N ALA A1029 69.983 33.361 2.143 1.00214.05 N ANISOU 1701 N ALA A1029 25111 35365 20852 -806 4137 -797 N ATOM 1702 CA ALA A1029 68.873 33.801 2.980 1.00208.65 C ANISOU 1702 CA ALA A1029 24563 34401 20315 -800 3870 -620 C ATOM 1703 C ALA A1029 67.523 33.537 2.325 1.00211.40 C ANISOU 1703 C ALA A1029 25054 34931 20336 -753 3706 -680 C ATOM 1704 O ALA A1029 66.513 33.410 3.026 1.00210.62 O ANISOU 1704 O ALA A1029 25044 34605 20377 -716 3468 -690 O ATOM 1705 CB ALA A1029 69.016 35.283 3.309 1.00203.46 C ANISOU 1705 CB ALA A1029 23948 33623 19733 -901 3890 -164 C ATOM 1706 N LEU A1030 67.486 33.459 0.991 1.00212.94 N ANISOU 1706 N LEU A1030 25267 35550 20091 -755 3829 -725 N ATOM 1707 CA LEU A1030 66.255 33.095 0.295 1.00205.68 C ANISOU 1707 CA LEU A1030 24457 34855 18835 -707 3675 -836 C ATOM 1708 C LEU A1030 65.921 31.623 0.515 1.00204.04 C ANISOU 1708 C LEU A1030 24211 34573 18742 -630 3584 -1321 C ATOM 1709 O LEU A1030 64.776 31.276 0.829 1.00218.65 O ANISOU 1709 O LEU A1030 26144 36317 20616 -593 3358 -1417 O ATOM 1710 CB LEU A1030 66.384 33.402 -1.198 1.00208.65 C ANISOU 1710 CB LEU A1030 24853 35733 18690 -730 3841 -758 C ATOM 1711 N THR A1031 66.911 30.740 0.355 1.00186.54 N ANISOU 1711 N THR A1031 21863 32402 16611 -606 3768 -1635 N ATOM 1712 CA THR A1031 66.715 29.335 0.699 1.00173.42 C ANISOU 1712 CA THR A1031 20159 30596 15137 -529 3704 -2088 C ATOM 1713 C THR A1031 66.550 29.128 2.201 1.00174.66 C ANISOU 1713 C THR A1031 20318 30257 15788 -496 3538 -2081 C ATOM 1714 O THR A1031 66.040 28.082 2.618 1.00175.40 O ANISOU 1714 O THR A1031 20421 30177 16047 -435 3427 -2390 O ATOM 1715 CB THR A1031 67.886 28.499 0.181 1.00163.71 C ANISOU 1715 CB THR A1031 18782 29520 13901 -499 3957 -2404 C ATOM 1716 OG1 THR A1031 69.111 29.017 0.718 1.00166.85 O ANISOU 1716 OG1 THR A1031 19068 29772 14556 -525 4108 -2220 O ATOM 1717 CG2 THR A1031 67.948 28.544 -1.342 1.00157.71 C ANISOU 1717 CG2 THR A1031 18024 29276 12621 -526 4116 -2471 C ATOM 1718 N LYS A1032 66.978 30.096 3.019 1.00169.74 N ANISOU 1718 N LYS A1032 19686 29406 15401 -540 3527 -1740 N ATOM 1719 CA LYS A1032 66.735 30.033 4.458 1.00160.30 C ANISOU 1719 CA LYS A1032 18505 27765 14637 -515 3354 -1696 C ATOM 1720 C LYS A1032 65.249 30.134 4.787 1.00156.93 C ANISOU 1720 C LYS A1032 18225 27222 14180 -508 3093 -1637 C ATOM 1721 O LYS A1032 64.803 29.588 5.805 1.00142.01 O ANISOU 1721 O LYS A1032 16356 25008 12594 -465 2941 -1752 O ATOM 1722 CB LYS A1032 67.505 31.150 5.167 1.00153.74 C ANISOU 1722 CB LYS A1032 17629 26760 14025 -579 3405 -1345 C ATOM 1723 CG LYS A1032 68.775 30.709 5.881 1.00148.38 C ANISOU 1723 CG LYS A1032 16787 25898 13691 -549 3526 -1472 C ATOM 1724 CD LYS A1032 68.466 30.203 7.280 1.00143.68 C ANISOU 1724 CD LYS A1032 16200 24893 13498 -486 3339 -1555 C ATOM 1725 CE LYS A1032 69.739 29.909 8.057 1.00137.87 C ANISOU 1725 CE LYS A1032 15297 23985 13103 -449 3440 -1628 C ATOM 1726 NZ LYS A1032 69.451 29.566 9.478 1.00123.37 N ANISOU 1726 NZ LYS A1032 13476 21758 11641 -390 3252 -1650 N ATOM 1727 N MET A1033 64.472 30.828 3.947 1.00170.37 N ANISOU 1727 N MET A1033 20025 29190 15518 -545 3042 -1450 N ATOM 1728 CA MET A1033 63.042 30.985 4.196 1.00173.41 C ANISOU 1728 CA MET A1033 20534 29498 15857 -535 2795 -1384 C ATOM 1729 C MET A1033 62.223 29.826 3.634 1.00165.60 C ANISOU 1729 C MET A1033 19562 28663 14695 -490 2717 -1773 C ATOM 1730 O MET A1033 61.161 29.507 4.181 1.00171.91 O ANISOU 1730 O MET A1033 20426 29285 15608 -471 2513 -1851 O ATOM 1731 CB MET A1033 62.548 32.314 3.614 1.00179.25 C ANISOU 1731 CB MET A1033 21366 30437 16305 -580 2761 -979 C ATOM 1732 CG MET A1033 62.868 33.535 4.477 1.00176.84 C ANISOU 1732 CG MET A1033 21082 29861 16247 -630 2750 -578 C ATOM 1733 SD MET A1033 62.238 35.105 3.841 1.00176.20 S ANISOU 1733 SD MET A1033 21122 29962 15863 -670 2714 -84 S ATOM 1734 CE MET A1033 63.290 35.344 2.411 1.00175.72 C ANISOU 1734 CE MET A1033 21005 30346 15416 -709 3008 -24 C ATOM 1735 N ARG A1034 62.689 29.183 2.558 1.00152.78 N ANISOU 1735 N ARG A1034 17878 27368 12805 -480 2879 -2032 N ATOM 1736 CA ARG A1034 61.964 28.028 2.037 1.00143.86 C ANISOU 1736 CA ARG A1034 16754 26375 11532 -448 2817 -2444 C ATOM 1737 C ARG A1034 62.121 26.818 2.948 1.00140.48 C ANISOU 1737 C ARG A1034 16277 25587 11514 -399 2799 -2783 C ATOM 1738 O ARG A1034 61.202 25.998 3.051 1.00129.42 O ANISOU 1738 O ARG A1034 14911 24114 10150 -384 2669 -3052 O ATOM 1739 CB ARG A1034 62.426 27.694 0.614 1.00145.80 C ANISOU 1739 CB ARG A1034 16947 27085 11364 -454 3005 -2642 C ATOM 1740 CG ARG A1034 63.829 27.114 0.517 1.00137.03 C ANISOU 1740 CG ARG A1034 15710 25969 10386 -433 3258 -2839 C ATOM 1741 CD ARG A1034 64.083 26.435 -0.822 1.00141.78 C ANISOU 1741 CD ARG A1034 16260 27001 10609 -428 3423 -3165 C ATOM 1742 NE ARG A1034 63.989 27.355 -1.954 1.00159.30 N ANISOU 1742 NE ARG A1034 18519 29668 12338 -473 3482 -2916 N ATOM 1743 CZ ARG A1034 63.044 27.299 -2.887 1.00168.47 C ANISOU 1743 CZ ARG A1034 19743 31185 13083 -481 3387 -3002 C ATOM 1744 NH1 ARG A1034 63.039 28.175 -3.883 1.00172.04 N ANISOU 1744 NH1 ARG A1034 20233 32044 13090 -509 3451 -2736 N ATOM 1745 NH2 ARG A1034 62.109 26.360 -2.833 1.00166.36 N ANISOU 1745 NH2 ARG A1034 19494 30874 12841 -461 3233 -3354 N ATOM 1746 N ALA A1035 63.270 26.690 3.617 1.00138.69 N ANISOU 1746 N ALA A1035 15964 25131 11599 -373 2930 -2770 N ATOM 1747 CA ALA A1035 63.435 25.611 4.584 1.00136.76 C ANISOU 1747 CA ALA A1035 15680 24518 11765 -310 2905 -3035 C ATOM 1748 C ALA A1035 62.587 25.857 5.824 1.00141.07 C ANISOU 1748 C ALA A1035 16310 24692 12598 -311 2679 -2870 C ATOM 1749 O ALA A1035 62.088 24.908 6.442 1.00138.25 O ANISOU 1749 O ALA A1035 15972 24080 12476 -271 2591 -3110 O ATOM 1750 CB ALA A1035 64.909 25.459 4.957 1.00127.27 C ANISOU 1750 CB ALA A1035 14351 23201 10805 -269 3097 -3045 C ATOM 1751 N ALA A1036 62.421 27.127 6.201 1.00146.08 N ANISOU 1751 N ALA A1036 16996 25284 13223 -358 2596 -2463 N ATOM 1752 CA ALA A1036 61.556 27.481 7.320 1.00150.14 C ANISOU 1752 CA ALA A1036 17595 25479 13975 -364 2383 -2290 C ATOM 1753 C ALA A1036 60.129 27.014 7.066 1.00159.92 C ANISOU 1753 C ALA A1036 18916 26768 15079 -369 2211 -2457 C ATOM 1754 O ALA A1036 59.564 26.240 7.846 1.00163.63 O ANISOU 1754 O ALA A1036 19410 26960 15803 -343 2104 -2637 O ATOM 1755 CB ALA A1036 61.591 28.994 7.557 1.00143.58 C ANISOU 1755 CB ALA A1036 16806 24645 13104 -419 2343 -1835 C ATOM 1756 N ALA A1037 59.538 27.465 5.956 1.00163.10 N ANISOU 1756 N ALA A1037 19357 27539 15076 -403 2187 -2403 N ATOM 1757 CA ALA A1037 58.187 27.034 5.614 1.00155.87 C ANISOU 1757 CA ALA A1037 18498 26725 14001 -412 2021 -2579 C ATOM 1758 C ALA A1037 58.127 25.538 5.333 1.00163.00 C ANISOU 1758 C ALA A1037 19354 27629 14948 -390 2075 -3072 C ATOM 1759 O ALA A1037 57.062 24.926 5.473 1.00168.48 O ANISOU 1759 O ALA A1037 20082 28254 15678 -401 1935 -3278 O ATOM 1760 CB ALA A1037 57.669 27.820 4.410 1.00143.31 C ANISOU 1760 CB ALA A1037 16942 25573 11935 -438 1992 -2418 C ATOM 1761 N LEU A1038 59.251 24.934 4.931 1.00161.47 N ANISOU 1761 N LEU A1038 19078 27509 14764 -362 2284 -3273 N ATOM 1762 CA LEU A1038 59.267 23.497 4.671 1.00158.08 C ANISOU 1762 CA LEU A1038 18603 27053 14406 -335 2358 -3752 C ATOM 1763 C LEU A1038 58.934 22.708 5.931 1.00156.10 C ANISOU 1763 C LEU A1038 18375 26331 14606 -303 2269 -3881 C ATOM 1764 O LEU A1038 58.180 21.728 5.879 1.00150.24 O ANISOU 1764 O LEU A1038 17648 25521 13916 -312 2214 -4211 O ATOM 1765 CB LEU A1038 60.633 23.085 4.116 1.00157.70 C ANISOU 1765 CB LEU A1038 18455 27138 14327 -298 2610 -3908 C ATOM 1766 CG LEU A1038 60.774 21.736 3.412 1.00154.48 C ANISOU 1766 CG LEU A1038 17990 26839 13867 -273 2737 -4414 C ATOM 1767 CD1 LEU A1038 61.833 21.823 2.322 1.00146.12 C ANISOU 1767 CD1 LEU A1038 16847 26146 12528 -266 2967 -4481 C ATOM 1768 CD2 LEU A1038 61.120 20.635 4.405 1.00159.40 C ANISOU 1768 CD2 LEU A1038 18583 27019 14962 -204 2775 -4645 C ATOM 1769 N ASP A1039 59.486 23.123 7.073 1.00158.54 N ANISOU 1769 N ASP A1039 18683 26315 15239 -271 2257 -3627 N ATOM 1770 CA ASP A1039 59.194 22.470 8.342 1.00164.87 C ANISOU 1770 CA ASP A1039 19514 26673 16457 -234 2170 -3696 C ATOM 1771 C ASP A1039 57.917 22.991 8.987 1.00163.72 C ANISOU 1771 C ASP A1039 19463 26387 16356 -281 1944 -3511 C ATOM 1772 O ASP A1039 57.311 22.277 9.796 1.00163.42 O ANISOU 1772 O ASP A1039 19462 26046 16585 -270 1860 -3647 O ATOM 1773 CB ASP A1039 60.365 22.654 9.310 1.00170.40 C ANISOU 1773 CB ASP A1039 20162 27109 17475 -171 2251 -3518 C ATOM 1774 CG ASP A1039 61.710 22.406 8.657 1.00179.92 C ANISOU 1774 CG ASP A1039 21255 28489 18617 -127 2477 -3631 C ATOM 1775 OD1 ASP A1039 61.741 21.804 7.563 1.00177.68 O ANISOU 1775 OD1 ASP A1039 20939 28468 18102 -131 2585 -3919 O ATOM 1776 OD2 ASP A1039 62.736 22.815 9.243 1.00178.57 O ANISOU 1776 OD2 ASP A1039 21020 28202 18627 -90 2547 -3442 O ATOM 1777 N ALA A1040 57.500 24.217 8.657 1.00158.59 N ANISOU 1777 N ALA A1040 18852 25944 15459 -328 1854 -3199 N ATOM 1778 CA ALA A1040 56.268 24.756 9.220 1.00153.71 C ANISOU 1778 CA ALA A1040 18315 25212 14874 -364 1642 -3024 C ATOM 1779 C ALA A1040 55.051 24.007 8.692 1.00165.53 C ANISOU 1779 C ALA A1040 19832 26828 16234 -399 1543 -3326 C ATOM 1780 O ALA A1040 54.141 23.666 9.456 1.00161.89 O ANISOU 1780 O ALA A1040 19413 26121 15977 -414 1410 -3383 O ATOM 1781 CB ALA A1040 56.159 26.247 8.907 1.00143.94 C ANISOU 1781 CB ALA A1040 17110 24175 13404 -394 1587 -2620 C ATOM 1782 N GLN A1041 55.022 23.734 7.384 1.00169.27 N ANISOU 1782 N GLN A1041 20269 27688 16357 -417 1609 -3533 N ATOM 1783 CA GLN A1041 53.905 23.040 6.751 1.00168.40 C ANISOU 1783 CA GLN A1041 20160 27749 16076 -460 1518 -3850 C ATOM 1784 C GLN A1041 53.786 21.584 7.184 1.00166.79 C ANISOU 1784 C GLN A1041 19938 27267 16168 -459 1565 -4262 C ATOM 1785 O GLN A1041 52.845 20.905 6.755 1.00161.33 O ANISOU 1785 O GLN A1041 19239 26672 15387 -509 1495 -4564 O ATOM 1786 CB GLN A1041 54.040 23.119 5.229 1.00170.28 C ANISOU 1786 CB GLN A1041 20356 28496 15847 -476 1592 -3974 C ATOM 1787 N LYS A1042 54.702 21.092 8.017 1.00168.78 N ANISOU 1787 N LYS A1042 20179 27178 16771 -403 1680 -4280 N ATOM 1788 CA LYS A1042 54.641 19.739 8.552 1.00157.01 C ANISOU 1788 CA LYS A1042 18684 25366 15607 -386 1735 -4622 C ATOM 1789 C LYS A1042 53.945 19.667 9.908 1.00148.18 C ANISOU 1789 C LYS A1042 17630 23833 14841 -391 1601 -4499 C ATOM 1790 O LYS A1042 53.972 18.607 10.546 1.00136.31 O ANISOU 1790 O LYS A1042 16134 22001 13656 -366 1654 -4717 O ATOM 1791 CB LYS A1042 56.053 19.152 8.664 1.00150.14 C ANISOU 1791 CB LYS A1042 17757 24366 14921 -302 1944 -4724 C ATOM 1792 CG LYS A1042 56.836 19.131 7.357 1.00139.52 C ANISOU 1792 CG LYS A1042 16340 23418 13252 -294 2107 -4872 C ATOM 1793 CD LYS A1042 57.214 17.712 6.944 1.00145.75 C ANISOU 1793 CD LYS A1042 17078 24150 14149 -263 2272 -5345 C ATOM 1794 CE LYS A1042 55.981 16.861 6.669 1.00153.28 C ANISOU 1794 CE LYS A1042 18060 25094 15085 -338 2189 -5699 C ATOM 1795 NZ LYS A1042 56.318 15.523 6.100 1.00154.51 N ANISOU 1795 NZ LYS A1042 18165 25233 15310 -321 2363 -6188 N ATOM 1796 N ALA A1043 53.332 20.762 10.363 1.00160.19 N ANISOU 1796 N ALA A1043 19197 25355 16312 -417 1440 -4154 N ATOM 1797 CA ALA A1043 52.611 20.782 11.630 1.00177.59 C ANISOU 1797 CA ALA A1043 21461 27197 18819 -427 1311 -4027 C ATOM 1798 C ALA A1043 51.708 22.008 11.670 1.00178.19 C ANISOU 1798 C ALA A1043 21573 27413 18717 -470 1129 -3721 C ATOM 1799 O ALA A1043 52.128 23.104 11.290 1.00183.87 O ANISOU 1799 O ALA A1043 22289 28344 19228 -458 1126 -3436 O ATOM 1800 CB ALA A1043 53.572 20.787 12.829 1.00174.45 C ANISOU 1800 CB ALA A1043 21076 26440 18767 -351 1375 -3841 C ATOM 1801 N THR A1044 50.471 21.813 12.126 1.00173.70 N ANISOU 1801 N THR A1044 21037 26719 18243 -520 987 -3780 N ATOM 1802 CA THR A1044 49.530 22.922 12.296 1.00162.44 C ANISOU 1802 CA THR A1044 19640 25381 16698 -549 808 -3497 C ATOM 1803 C THR A1044 48.726 22.786 13.587 1.00155.72 C ANISOU 1803 C THR A1044 18836 24162 16167 -568 701 -3437 C ATOM 1804 O THR A1044 49.201 22.230 14.579 1.00149.25 O ANISOU 1804 O THR A1044 18044 22991 15673 -538 768 -3455 O ATOM 1805 CB THR A1044 48.546 23.029 11.108 1.00174.77 C ANISOU 1805 CB THR A1044 21166 27345 17894 -600 710 -3638 C ATOM 1806 OG1 THR A1044 47.945 21.752 10.862 1.00181.06 O ANISOU 1806 OG1 THR A1044 21929 28112 18752 -655 723 -4070 O ATOM 1807 CG2 THR A1044 49.259 23.514 9.849 1.00180.96 C ANISOU 1807 CG2 THR A1044 21916 28540 18301 -577 792 -3589 C ATOM 1808 N MET A1058 41.850 23.329 7.493 1.00146.80 N ANISOU 1808 N MET A1058 17327 25404 13046 -842 -142 -4319 N ATOM 1809 CA MET A1058 43.108 22.721 7.914 1.00153.29 C ANISOU 1809 CA MET A1058 18206 25931 14106 -834 69 -4390 C ATOM 1810 C MET A1058 43.969 22.366 6.708 1.00169.91 C ANISOU 1810 C MET A1058 20283 28369 15908 -823 204 -4583 C ATOM 1811 O MET A1058 45.195 22.461 6.758 1.00166.16 O ANISOU 1811 O MET A1058 19851 27805 15479 -774 365 -4468 O ATOM 1812 CB MET A1058 42.847 21.472 8.759 1.00152.19 C ANISOU 1812 CB MET A1058 18066 25388 14371 -908 128 -4718 C ATOM 1813 N LYS A1059 43.311 21.951 5.622 1.00193.75 N ANISOU 1813 N LYS A1059 23219 31786 18611 -872 140 -4891 N ATOM 1814 CA LYS A1059 44.035 21.619 4.399 1.00203.24 C ANISOU 1814 CA LYS A1059 24387 33355 19480 -866 262 -5099 C ATOM 1815 C LYS A1059 44.541 22.867 3.687 1.00200.20 C ANISOU 1815 C LYS A1059 24028 33320 18717 -781 253 -4701 C ATOM 1816 O LYS A1059 45.533 22.798 2.951 1.00196.81 O ANISOU 1816 O LYS A1059 23602 33092 18087 -755 409 -4743 O ATOM 1817 CB LYS A1059 43.141 20.804 3.464 1.00211.49 C ANISOU 1817 CB LYS A1059 25329 34738 20289 -952 188 -5566 C ATOM 1818 N ASP A1060 43.875 24.008 3.886 1.00190.99 N ANISOU 1818 N ASP A1060 22881 32229 17458 -734 83 -4315 N ATOM 1819 CA ASP A1060 44.339 25.266 3.314 1.00179.38 C ANISOU 1819 CA ASP A1060 21451 31035 15672 -649 83 -3888 C ATOM 1820 C ASP A1060 45.611 25.776 3.979 1.00185.73 C ANISOU 1820 C ASP A1060 22337 31530 16701 -605 248 -3576 C ATOM 1821 O ASP A1060 46.234 26.705 3.453 1.00187.86 O ANISOU 1821 O ASP A1060 22641 32010 16729 -549 304 -3255 O ATOM 1822 CB ASP A1060 43.243 26.329 3.413 1.00165.44 C ANISOU 1822 CB ASP A1060 19683 29387 13788 -602 -141 -3560 C ATOM 1823 N PHE A1061 46.014 25.197 5.111 1.00186.97 N ANISOU 1823 N PHE A1061 22524 31206 17309 -629 329 -3658 N ATOM 1824 CA PHE A1061 47.243 25.635 5.763 1.00185.34 C ANISOU 1824 CA PHE A1061 22378 30723 17320 -588 478 -3389 C ATOM 1825 C PHE A1061 48.467 24.935 5.180 1.00186.00 C ANISOU 1825 C PHE A1061 22437 30892 17341 -588 699 -3616 C ATOM 1826 O PHE A1061 49.502 25.571 4.952 1.00189.24 O ANISOU 1826 O PHE A1061 22868 31374 17662 -549 825 -3373 O ATOM 1827 CB PHE A1061 47.156 25.391 7.269 1.00180.94 C ANISOU 1827 CB PHE A1061 21861 29633 17257 -600 459 -3346 C ATOM 1828 N ARG A1062 48.367 23.624 4.936 1.00174.95 N ANISOU 1828 N ARG A1062 20990 29482 16003 -635 758 -4088 N ATOM 1829 CA ARG A1062 49.511 22.865 4.435 1.00160.96 C ANISOU 1829 CA ARG A1062 19188 27760 14209 -627 977 -4339 C ATOM 1830 C ARG A1062 50.006 23.424 3.105 1.00169.60 C ANISOU 1830 C ARG A1062 20258 29358 14823 -605 1049 -4258 C ATOM 1831 O ARG A1062 51.200 23.701 2.938 1.00160.09 O ANISOU 1831 O ARG A1062 19059 28176 13594 -569 1221 -4122 O ATOM 1832 CB ARG A1062 49.135 21.388 4.297 1.00146.06 C ANISOU 1832 CB ARG A1062 17252 25800 12444 -685 1015 -4879 C ATOM 1833 N HIS A1063 49.095 23.603 2.145 1.00192.46 N ANISOU 1833 N HIS A1063 23123 32678 17327 -627 920 -4335 N ATOM 1834 CA HIS A1063 49.452 24.177 0.854 1.00197.93 C ANISOU 1834 CA HIS A1063 23799 33884 17520 -601 974 -4233 C ATOM 1835 C HIS A1063 49.628 25.689 0.911 1.00209.19 C ANISOU 1835 C HIS A1063 25287 35382 18813 -544 930 -3662 C ATOM 1836 O HIS A1063 50.226 26.262 -0.009 1.00210.74 O ANISOU 1836 O HIS A1063 25486 35929 18655 -516 1028 -3497 O ATOM 1837 CB HIS A1063 48.388 23.828 -0.191 1.00191.56 C ANISOU 1837 CB HIS A1063 22932 33530 16323 -637 838 -4519 C ATOM 1838 N GLY A1064 49.122 26.341 1.963 1.00208.39 N ANISOU 1838 N GLY A1064 25235 34954 18989 -528 797 -3362 N ATOM 1839 CA GLY A1064 49.195 27.792 2.034 1.00203.61 C ANISOU 1839 CA GLY A1064 24690 34393 18279 -476 752 -2830 C ATOM 1840 C GLY A1064 50.617 28.317 2.037 1.00201.96 C ANISOU 1840 C GLY A1064 24509 34123 18105 -457 965 -2586 C ATOM 1841 O GLY A1064 50.901 29.372 1.464 1.00210.93 O ANISOU 1841 O GLY A1064 25678 35493 18973 -425 998 -2230 O ATOM 1842 N PHE A1065 51.531 27.589 2.684 1.00181.23 N ANISOU 1842 N PHE A1065 21866 31180 15813 -476 1117 -2769 N ATOM 1843 CA PHE A1065 52.934 27.983 2.666 1.00166.25 C ANISOU 1843 CA PHE A1065 19969 29240 13959 -463 1329 -2587 C ATOM 1844 C PHE A1065 53.594 27.641 1.336 1.00173.10 C ANISOU 1844 C PHE A1065 20788 30543 14439 -466 1497 -2774 C ATOM 1845 O PHE A1065 54.506 28.352 0.897 1.00170.49 O ANISOU 1845 O PHE A1065 20463 30362 13954 -456 1647 -2522 O ATOM 1846 CB PHE A1065 53.680 27.310 3.822 1.00124.34 C ANISOU 1846 CB PHE A1065 14645 23463 9137 -467 1422 -2719 C ATOM 1847 N ASP A1066 53.132 26.576 0.671 1.00189.77 N ANISOU 1847 N ASP A1066 22851 32869 16386 -486 1481 -3218 N ATOM 1848 CA ASP A1066 53.790 26.063 -0.527 1.00205.52 C ANISOU 1848 CA ASP A1066 24791 35254 18044 -493 1655 -3476 C ATOM 1849 C ASP A1066 53.715 27.018 -1.715 1.00215.94 C ANISOU 1849 C ASP A1066 26129 37086 18832 -475 1658 -3209 C ATOM 1850 O ASP A1066 54.408 26.787 -2.713 1.00225.46 O ANISOU 1850 O ASP A1066 27297 38635 19734 -479 1829 -3347 O ATOM 1851 CB ASP A1066 53.191 24.707 -0.913 1.00211.34 C ANISOU 1851 CB ASP A1066 25471 36084 18744 -527 1621 -4036 C ATOM 1852 CG ASP A1066 54.158 23.849 -1.715 1.00215.19 C ANISOU 1852 CG ASP A1066 25893 36771 19098 -534 1855 -4397 C ATOM 1853 OD1 ASP A1066 54.929 23.084 -1.097 1.00210.45 O ANISOU 1853 OD1 ASP A1066 25265 35833 18865 -525 1995 -4594 O ATOM 1854 OD2 ASP A1066 54.148 23.938 -2.962 1.00219.19 O ANISOU 1854 OD2 ASP A1066 26374 37778 19129 -540 1900 -4481 O ATOM 1855 N ILE A1067 52.905 28.072 -1.641 1.00211.76 N ANISOU 1855 N ILE A1067 25658 36619 18181 -451 1481 -2828 N ATOM 1856 CA ILE A1067 52.839 29.031 -2.739 1.00207.33 C ANISOU 1856 CA ILE A1067 25125 36528 17122 -419 1485 -2525 C ATOM 1857 C ILE A1067 53.764 30.225 -2.517 1.00199.00 C ANISOU 1857 C ILE A1067 24125 35360 16124 -403 1622 -2024 C ATOM 1858 O ILE A1067 54.199 30.854 -3.488 1.00208.76 O ANISOU 1858 O ILE A1067 25378 36966 16975 -388 1734 -1810 O ATOM 1859 CB ILE A1067 51.387 29.493 -2.961 1.00209.36 C ANISOU 1859 CB ILE A1067 25405 36981 17160 -386 1215 -2401 C ATOM 1860 CG1 ILE A1067 50.821 30.155 -1.698 1.00200.49 C ANISOU 1860 CG1 ILE A1067 24335 35407 16434 -369 1059 -2099 C ATOM 1861 CG2 ILE A1067 50.518 28.322 -3.393 1.00215.81 C ANISOU 1861 CG2 ILE A1067 26148 37998 17850 -418 1098 -2923 C ATOM 1862 CD1 ILE A1067 50.863 31.674 -1.722 1.00196.80 C ANISOU 1862 CD1 ILE A1067 23946 34970 15858 -316 1039 -1511 C ATOM 1863 N LEU A1068 54.071 30.552 -1.265 1.00179.00 N ANISOU 1863 N LEU A1068 21619 32331 14059 -411 1620 -1836 N ATOM 1864 CA LEU A1068 54.903 31.708 -0.945 1.00167.62 C ANISOU 1864 CA LEU A1068 20224 30742 12721 -411 1741 -1375 C ATOM 1865 C LEU A1068 56.321 31.540 -1.482 1.00172.74 C ANISOU 1865 C LEU A1068 20823 31527 13285 -438 2024 -1432 C ATOM 1866 O LEU A1068 56.640 32.013 -2.575 1.00181.74 O ANISOU 1866 O LEU A1068 21971 33069 14012 -434 2137 -1284 O ATOM 1867 CB LEU A1068 54.939 31.938 0.568 1.00160.26 C ANISOU 1867 CB LEU A1068 19314 29251 12325 -422 1675 -1240 C ATOM 1868 N GLN A1093 57.496 41.236 -1.808 1.00177.04 N ANISOU 1868 N GLN A1093 21893 31819 13554 -442 2400 2188 N ATOM 1869 CA GLN A1093 56.337 40.471 -2.256 1.00179.06 C ANISOU 1869 CA GLN A1093 22144 32349 13542 -355 2172 1926 C ATOM 1870 C GLN A1093 55.944 39.410 -1.232 1.00185.11 C ANISOU 1870 C GLN A1093 22845 32821 14665 -365 2011 1496 C ATOM 1871 O GLN A1093 54.758 39.180 -0.989 1.00173.79 O ANISOU 1871 O GLN A1093 21428 31370 13236 -303 1767 1403 O ATOM 1872 CB GLN A1093 56.617 39.810 -3.608 1.00175.08 C ANISOU 1872 CB GLN A1093 21599 32387 12534 -343 2284 1716 C ATOM 1873 N LEU A1094 56.952 38.771 -0.632 1.00198.42 N ANISOU 1873 N LEU A1094 24455 34280 16656 -441 2152 1244 N ATOM 1874 CA LEU A1094 56.691 37.670 0.289 1.00196.98 C ANISOU 1874 CA LEU A1094 24213 33831 16801 -448 2029 829 C ATOM 1875 C LEU A1094 55.865 38.124 1.488 1.00203.02 C ANISOU 1875 C LEU A1094 25027 34185 17927 -429 1823 971 C ATOM 1876 O LEU A1094 54.997 37.386 1.968 1.00208.45 O ANISOU 1876 O LEU A1094 25699 34771 18731 -400 1633 704 O ATOM 1877 CB LEU A1094 58.013 37.047 0.746 1.00193.80 C ANISOU 1877 CB LEU A1094 23719 33243 16671 -517 2230 602 C ATOM 1878 N LYS A1095 56.111 39.342 1.978 1.00207.15 N ANISOU 1878 N LYS A1095 25607 34469 18633 -450 1868 1385 N ATOM 1879 CA LYS A1095 55.433 39.817 3.181 1.00204.40 C ANISOU 1879 CA LYS A1095 25300 33710 18652 -438 1697 1514 C ATOM 1880 C LYS A1095 53.917 39.848 3.029 1.00220.34 C ANISOU 1880 C LYS A1095 27365 35839 20516 -349 1441 1530 C ATOM 1881 O LYS A1095 53.205 39.854 4.041 1.00210.36 O ANISOU 1881 O LYS A1095 26113 34263 19550 -334 1274 1499 O ATOM 1882 CB LYS A1095 55.946 41.211 3.561 1.00193.76 C ANISOU 1882 CB LYS A1095 24009 32129 17480 -478 1806 1966 C ATOM 1883 N THR A1096 53.405 39.868 1.795 1.00248.96 N ANISOU 1883 N THR A1096 31006 39912 23674 -287 1406 1572 N ATOM 1884 CA THR A1096 51.957 39.887 1.603 1.00251.00 C ANISOU 1884 CA THR A1096 31287 40312 23768 -196 1154 1577 C ATOM 1885 C THR A1096 51.332 38.532 1.924 1.00252.25 C ANISOU 1885 C THR A1096 31373 40464 24008 -202 1006 1078 C ATOM 1886 O THR A1096 50.225 38.469 2.471 1.00255.24 O ANISOU 1886 O THR A1096 31753 40713 24514 -162 793 1031 O ATOM 1887 CB THR A1096 51.619 40.306 0.173 1.00252.76 C ANISOU 1887 CB THR A1096 31540 41048 23447 -122 1154 1771 C ATOM 1888 N THR A1097 52.022 37.436 1.592 1.00217.45 N ANISOU 1888 N THR A1097 26898 36183 19541 -254 1126 700 N ATOM 1889 CA THR A1097 51.496 36.113 1.918 1.00181.76 C ANISOU 1889 CA THR A1097 22312 31617 15131 -269 1012 218 C ATOM 1890 C THR A1097 51.483 35.879 3.425 1.00180.79 C ANISOU 1890 C THR A1097 22187 30968 15539 -304 958 137 C ATOM 1891 O THR A1097 50.582 35.211 3.946 1.00178.38 O ANISOU 1891 O THR A1097 21858 30540 15377 -298 792 -107 O ATOM 1892 CB THR A1097 52.318 35.033 1.217 1.00156.23 C ANISOU 1892 CB THR A1097 19010 28616 11733 -310 1178 -159 C ATOM 1893 OG1 THR A1097 52.514 35.391 -0.157 1.00159.25 O ANISOU 1893 OG1 THR A1097 19401 29487 11618 -283 1265 -34 O ATOM 1894 CG2 THR A1097 51.595 33.699 1.279 1.00138.84 C ANISOU 1894 CG2 THR A1097 16746 26446 9560 -320 1053 -653 C ATOM 1895 N ARG A1098 52.476 36.421 4.139 1.00178.96 N ANISOU 1895 N ARG A1098 21974 30429 15594 -345 1100 336 N ATOM 1896 CA ARG A1098 52.520 36.270 5.591 1.00177.28 C ANISOU 1896 CA ARG A1098 21759 29733 15864 -375 1050 284 C ATOM 1897 C ARG A1098 51.298 36.898 6.251 1.00184.53 C ANISOU 1897 C ARG A1098 22728 30471 16913 -335 837 469 C ATOM 1898 O ARG A1098 50.722 36.324 7.182 1.00185.65 O ANISOU 1898 O ARG A1098 22857 30352 17331 -341 715 273 O ATOM 1899 CB ARG A1098 53.808 36.885 6.142 1.00171.90 C ANISOU 1899 CB ARG A1098 21079 28811 15425 -427 1236 492 C ATOM 1900 N ASN A1099 50.886 38.078 5.783 1.00189.77 N ANISOU 1900 N ASN A1099 23450 31265 17387 -287 796 852 N ATOM 1901 CA ASN A1099 49.688 38.703 6.328 1.00190.99 C ANISOU 1901 CA ASN A1099 23646 31273 17650 -233 595 1030 C ATOM 1902 C ASN A1099 48.410 38.047 5.813 1.00191.59 C ANISOU 1902 C ASN A1099 23683 31615 17497 -180 397 801 C ATOM 1903 O ASN A1099 47.360 38.178 6.452 1.00188.18 O ANISOU 1903 O ASN A1099 23254 31024 17221 -147 218 814 O ATOM 1904 CB ASN A1099 49.691 40.199 6.003 1.00189.24 C ANISOU 1904 CB ASN A1099 23497 31082 17322 -188 627 1528 C ATOM 1905 CG ASN A1099 48.558 40.952 6.684 1.00182.05 C ANISOU 1905 CG ASN A1099 22627 29962 16580 -126 440 1738 C ATOM 1906 OD1 ASN A1099 48.084 40.559 7.750 1.00184.05 O ANISOU 1906 OD1 ASN A1099 22862 29919 17148 -145 333 1567 O ATOM 1907 ND2 ASN A1099 48.123 42.045 6.067 1.00176.76 N ANISOU 1907 ND2 ASN A1099 22013 29446 15702 -46 407 2117 N ATOM 1908 N ALA A1100 48.485 37.322 4.692 1.00196.51 N ANISOU 1908 N ALA A1100 24262 32643 17761 -177 430 571 N ATOM 1909 CA ALA A1100 47.295 36.776 4.047 1.00189.96 C ANISOU 1909 CA ALA A1100 23384 32130 16661 -131 245 358 C ATOM 1910 C ALA A1100 46.717 35.575 4.788 1.00191.21 C ANISOU 1910 C ALA A1100 23483 32093 17074 -179 142 -74 C ATOM 1911 O ALA A1100 45.492 35.423 4.842 1.00193.59 O ANISOU 1911 O ALA A1100 23752 32462 17343 -147 -56 -165 O ATOM 1912 CB ALA A1100 47.613 36.386 2.602 1.00187.59 C ANISOU 1912 CB ALA A1100 23052 32340 15882 -122 325 231 C ATOM 1913 N TYR A1101 47.561 34.707 5.349 1.00190.66 N ANISOU 1913 N TYR A1101 23395 31787 17261 -251 274 -340 N ATOM 1914 CA TYR A1101 47.044 33.492 5.969 1.00185.94 C ANISOU 1914 CA TYR A1101 22746 31012 16891 -296 197 -754 C ATOM 1915 C TYR A1101 47.870 33.023 7.160 1.00185.76 C ANISOU 1915 C TYR A1101 22735 30538 17308 -348 309 -853 C ATOM 1916 O TYR A1101 47.353 32.312 8.029 1.00177.91 O ANISOU 1916 O TYR A1101 21725 29278 16595 -375 231 -1073 O ATOM 1917 CB TYR A1101 46.947 32.374 4.931 1.00181.85 C ANISOU 1917 CB TYR A1101 22159 30856 16080 -319 216 -1164 C ATOM 1918 CG TYR A1101 45.824 32.588 3.943 1.00178.73 C ANISOU 1918 CG TYR A1101 21729 30891 15288 -272 46 -1162 C ATOM 1919 CD1 TYR A1101 44.509 32.296 4.287 1.00176.08 C ANISOU 1919 CD1 TYR A1101 21349 30524 15028 -270 -161 -1308 C ATOM 1920 CD2 TYR A1101 46.075 33.098 2.674 1.00186.26 C ANISOU 1920 CD2 TYR A1101 22687 32295 15786 -226 91 -1005 C ATOM 1921 CE1 TYR A1101 43.472 32.498 3.389 1.00187.67 C ANISOU 1921 CE1 TYR A1101 22767 32408 16132 -220 -330 -1311 C ATOM 1922 CE2 TYR A1101 45.047 33.304 1.770 1.00192.34 C ANISOU 1922 CE2 TYR A1101 23419 33486 16174 -170 -78 -992 C ATOM 1923 CZ TYR A1101 43.746 33.002 2.131 1.00194.72 C ANISOU 1923 CZ TYR A1101 23665 33757 16562 -165 -294 -1151 C ATOM 1924 OH TYR A1101 42.715 33.202 1.237 1.00196.96 O ANISOU 1924 OH TYR A1101 23893 34480 16465 -103 -475 -1146 O ATOM 1925 N ILE A1102 49.148 33.401 7.211 1.00192.31 N ANISOU 1925 N ILE A1102 23586 31287 18195 -361 492 -692 N ATOM 1926 CA ILE A1102 49.983 33.007 8.340 1.00191.86 C ANISOU 1926 CA ILE A1102 23528 30827 18542 -398 591 -768 C ATOM 1927 C ILE A1102 49.485 33.661 9.626 1.00191.56 C ANISOU 1927 C ILE A1102 23536 30411 18838 -394 479 -552 C ATOM 1928 O ILE A1102 49.471 33.035 10.694 1.00194.57 O ANISOU 1928 O ILE A1102 23911 30465 19551 -417 459 -713 O ATOM 1929 CB ILE A1102 51.461 33.341 8.053 1.00191.47 C ANISOU 1929 CB ILE A1102 23473 30813 18466 -414 809 -637 C ATOM 1930 CG1 ILE A1102 52.069 32.335 7.067 1.00188.21 C ANISOU 1930 CG1 ILE A1102 22999 30683 17827 -424 944 -963 C ATOM 1931 CG2 ILE A1102 52.272 33.372 9.336 1.00190.94 C ANISOU 1931 CG2 ILE A1102 23406 30323 18819 -439 880 -584 C ATOM 1932 CD1 ILE A1102 51.806 32.641 5.603 1.00185.82 C ANISOU 1932 CD1 ILE A1102 22695 30874 17036 -403 951 -912 C ATOM 1933 N GLN A1103 49.036 34.917 9.542 1.00176.94 N ANISOU 1933 N GLN A1103 21731 28600 16899 -361 406 -185 N ATOM 1934 CA GLN A1103 48.571 35.627 10.729 1.00157.80 C ANISOU 1934 CA GLN A1103 19349 25825 14781 -356 309 25 C ATOM 1935 C GLN A1103 47.309 35.013 11.324 1.00151.29 C ANISOU 1935 C GLN A1103 18508 24883 14091 -350 131 -182 C ATOM 1936 O GLN A1103 46.962 35.330 12.467 1.00152.48 O ANISOU 1936 O GLN A1103 18686 24709 14541 -356 63 -90 O ATOM 1937 CB GLN A1103 48.324 37.100 10.399 1.00151.05 C ANISOU 1937 CB GLN A1103 18548 25052 13794 -312 279 455 C ATOM 1938 N LYS A1104 46.613 34.148 10.578 1.00150.49 N ANISOU 1938 N LYS A1104 18359 25045 13776 -347 58 -468 N ATOM 1939 CA LYS A1104 45.431 33.483 11.121 1.00147.69 C ANISOU 1939 CA LYS A1104 17976 24581 13561 -359 -96 -695 C ATOM 1940 C LYS A1104 45.797 32.582 12.295 1.00148.50 C ANISOU 1940 C LYS A1104 18080 24299 14044 -410 -41 -915 C ATOM 1941 O LYS A1104 45.080 32.536 13.302 1.00132.18 O ANISOU 1941 O LYS A1104 16024 21967 12232 -421 -138 -924 O ATOM 1942 CB LYS A1104 44.733 32.679 10.024 1.00145.90 C ANISOU 1942 CB LYS A1104 17683 24729 13025 -362 -166 -994 C ATOM 1943 N TYR A1105 46.908 31.853 12.179 1.00157.45 N ANISOU 1943 N TYR A1105 19201 25405 15218 -436 119 -1088 N ATOM 1944 CA TYR A1105 47.420 31.044 13.278 1.00156.86 C ANISOU 1944 CA TYR A1105 19131 24969 15501 -464 187 -1255 C ATOM 1945 C TYR A1105 48.379 31.816 14.174 1.00145.78 C ANISOU 1945 C TYR A1105 17765 23299 14325 -458 266 -980 C ATOM 1946 O TYR A1105 48.468 31.517 15.371 1.00128.65 O ANISOU 1946 O TYR A1105 15613 20794 12475 -469 259 -1013 O ATOM 1947 CB TYR A1105 48.130 29.800 12.735 1.00160.25 C ANISOU 1947 CB TYR A1105 19517 25487 15883 -481 319 -1601 C ATOM 1948 CG TYR A1105 47.212 28.653 12.374 1.00155.36 C ANISOU 1948 CG TYR A1105 18858 24958 15212 -512 253 -1979 C ATOM 1949 CD1 TYR A1105 46.455 28.680 11.209 1.00159.63 C ANISOU 1949 CD1 TYR A1105 19360 25886 15405 -516 173 -2073 C ATOM 1950 CD2 TYR A1105 47.120 27.533 13.192 1.00146.89 C ANISOU 1950 CD2 TYR A1105 17783 23589 14440 -540 277 -2244 C ATOM 1951 CE1 TYR A1105 45.620 27.628 10.875 1.00159.09 C ANISOU 1951 CE1 TYR A1105 19243 25908 15296 -558 114 -2445 C ATOM 1952 CE2 TYR A1105 46.292 26.478 12.868 1.00150.56 C ANISOU 1952 CE2 TYR A1105 18209 24114 14881 -583 232 -2601 C ATOM 1953 CZ TYR A1105 45.543 26.529 11.709 1.00153.32 C ANISOU 1953 CZ TYR A1105 18511 24854 14890 -599 150 -2713 C ATOM 1954 OH TYR A1105 44.715 25.478 11.382 1.00143.74 O ANISOU 1954 OH TYR A1105 17247 23710 13659 -656 106 -3093 O ATOM 1955 N LEU A1106 49.098 32.797 13.618 1.00154.51 N ANISOU 1955 N LEU A1106 18882 24555 15270 -445 344 -714 N ATOM 1956 CA LEU A1106 50.037 33.584 14.414 1.00160.01 C ANISOU 1956 CA LEU A1106 19601 25017 16179 -454 426 -463 C ATOM 1957 C LEU A1106 49.326 34.292 15.562 1.00147.12 C ANISOU 1957 C LEU A1106 18014 23100 14784 -454 303 -275 C ATOM 1958 O LEU A1106 49.782 34.251 16.711 1.00127.71 O ANISOU 1958 O LEU A1106 15564 20338 12622 -470 326 -259 O ATOM 1959 CB LEU A1106 50.759 34.596 13.522 1.00162.10 C ANISOU 1959 CB LEU A1106 19870 25508 16211 -451 529 -196 C ATOM 1960 CG LEU A1106 51.513 35.723 14.235 1.00159.30 C ANISOU 1960 CG LEU A1106 19540 24938 16048 -473 595 118 C ATOM 1961 CD1 LEU A1106 52.745 35.195 14.963 1.00161.56 C ANISOU 1961 CD1 LEU A1106 19781 25021 16581 -500 719 2 C ATOM 1962 CD2 LEU A1106 51.885 36.834 13.259 1.00154.18 C ANISOU 1962 CD2 LEU A1106 18910 24523 15146 -473 677 416 C ATOM 1963 N GLN A 301 48.206 34.955 15.265 1.00142.29 N ANISOU 1963 N GLN A 301 17427 22596 14042 -429 171 -135 N ATOM 1964 CA GLN A 301 47.427 35.581 16.326 1.00134.66 C ANISOU 1964 CA GLN A 301 16496 21369 13299 -423 54 16 C ATOM 1965 C GLN A 301 46.774 34.538 17.223 1.00127.95 C ANISOU 1965 C GLN A 301 15636 20311 12669 -441 -21 -252 C ATOM 1966 O GLN A 301 46.581 34.786 18.419 1.00118.15 O ANISOU 1966 O GLN A 301 14422 18775 11695 -451 -62 -182 O ATOM 1967 CB GLN A 301 46.369 36.510 15.728 1.00124.28 C ANISOU 1967 CB GLN A 301 15199 20236 11787 -377 -67 226 C ATOM 1968 N ALA A 302 46.438 33.369 16.668 1.00123.57 N ANISOU 1968 N ALA A 302 15042 19901 12007 -450 -31 -564 N ATOM 1969 CA ALA A 302 45.773 32.332 17.451 1.00116.09 C ANISOU 1969 CA ALA A 302 14086 18754 11270 -476 -88 -823 C ATOM 1970 C ALA A 302 46.656 31.856 18.599 1.00118.76 C ANISOU 1970 C ALA A 302 14444 18764 11914 -490 3 -869 C ATOM 1971 O ALA A 302 46.194 31.718 19.738 1.00121.64 O ANISOU 1971 O ALA A 302 14833 18859 12524 -501 -52 -876 O ATOM 1972 CB ALA A 302 45.386 31.163 16.545 1.00115.18 C ANISOU 1972 CB ALA A 302 13921 18860 10983 -494 -88 -1164 C ATOM 1973 N ILE A 303 47.934 31.596 18.316 1.00121.58 N ANISOU 1973 N ILE A 303 14785 19156 12254 -484 144 -900 N ATOM 1974 CA ILE A 303 48.855 31.158 19.360 1.00105.85 C ANISOU 1974 CA ILE A 303 12797 16882 10537 -482 226 -934 C ATOM 1975 C ILE A 303 49.107 32.279 20.358 1.00115.09 C ANISOU 1975 C ILE A 303 14001 17851 11878 -485 200 -643 C ATOM 1976 O ILE A 303 49.118 32.053 21.574 1.00119.12 O ANISOU 1976 O ILE A 303 14531 18086 12643 -486 178 -652 O ATOM 1977 CB ILE A 303 50.166 30.646 18.736 1.00106.29 C ANISOU 1977 CB ILE A 303 12810 17054 10523 -467 383 -1039 C ATOM 1978 CG1 ILE A 303 49.963 29.248 18.146 1.00108.34 C ANISOU 1978 CG1 ILE A 303 13040 17398 10725 -465 421 -1396 C ATOM 1979 CG2 ILE A 303 51.291 30.646 19.764 1.00 99.34 C ANISOU 1979 CG2 ILE A 303 11919 15927 9897 -452 461 -967 C ATOM 1980 CD1 ILE A 303 51.235 28.604 17.642 1.00 93.36 C ANISOU 1980 CD1 ILE A 303 11094 15579 8800 -440 584 -1537 C ATOM 1981 N ASN A 304 49.311 33.505 19.866 1.00121.78 N ANISOU 1981 N ASN A 304 14855 18831 12586 -487 207 -384 N ATOM 1982 CA ASN A 304 49.494 34.638 20.767 1.00126.50 C ANISOU 1982 CA ASN A 304 15481 19234 13348 -500 186 -119 C ATOM 1983 C ASN A 304 48.279 34.825 21.668 1.00124.75 C ANISOU 1983 C ASN A 304 15300 18828 13272 -500 49 -93 C ATOM 1984 O ASN A 304 48.420 35.191 22.840 1.00127.32 O ANISOU 1984 O ASN A 304 15646 18905 13824 -512 32 -4 O ATOM 1985 CB ASN A 304 49.775 35.909 19.966 1.00134.56 C ANISOU 1985 CB ASN A 304 16509 20428 14188 -505 224 154 C ATOM 1986 CG ASN A 304 51.148 35.898 19.319 1.00148.98 C ANISOU 1986 CG ASN A 304 18294 22390 15923 -519 383 169 C ATOM 1987 OD1 ASN A 304 51.869 34.902 19.383 1.00149.53 O ANISOU 1987 OD1 ASN A 304 18320 22447 16047 -514 460 -41 O ATOM 1988 ND2 ASN A 304 51.514 37.008 18.687 1.00157.28 N ANISOU 1988 ND2 ASN A 304 19353 23567 16839 -533 442 421 N ATOM 1989 N ASN A 305 47.077 34.570 21.139 1.00119.69 N ANISOU 1989 N ASN A 305 14659 18318 12499 -488 -50 -182 N ATOM 1990 CA ASN A 305 45.874 34.614 21.965 1.00109.41 C ANISOU 1990 CA ASN A 305 13379 16853 11337 -490 -173 -193 C ATOM 1991 C ASN A 305 45.953 33.602 23.100 1.00106.02 C ANISOU 1991 C ASN A 305 12959 16166 11158 -508 -158 -380 C ATOM 1992 O ASN A 305 45.637 33.918 24.253 1.00 95.72 O ANISOU 1992 O ASN A 305 11684 14629 10055 -516 -203 -303 O ATOM 1993 CB ASN A 305 44.633 34.352 21.110 1.00104.14 C ANISOU 1993 CB ASN A 305 12686 16406 10477 -477 -275 -300 C ATOM 1994 CG ASN A 305 44.254 35.540 20.256 1.00110.16 C ANISOU 1994 CG ASN A 305 13450 17383 11024 -439 -328 -56 C ATOM 1995 OD1 ASN A 305 44.647 36.671 20.539 1.00112.83 O ANISOU 1995 OD1 ASN A 305 13821 17634 11416 -428 -304 213 O ATOM 1996 ND2 ASN A 305 43.480 35.292 19.205 1.00114.03 N ANISOU 1996 ND2 ASN A 305 13901 18155 11269 -418 -399 -148 N ATOM 1997 N GLU A 306 46.363 32.370 22.785 1.00100.67 N ANISOU 1997 N GLU A 306 12258 15523 10468 -511 -90 -626 N ATOM 1998 CA GLU A 306 46.490 31.352 23.821 1.00 94.32 C ANISOU 1998 CA GLU A 306 11469 14467 9900 -516 -63 -788 C ATOM 1999 C GLU A 306 47.554 31.732 24.839 1.00 94.56 C ANISOU 1999 C GLU A 306 11514 14298 10116 -503 -7 -645 C ATOM 2000 O GLU A 306 47.424 31.407 26.025 1.00 95.71 O ANISOU 2000 O GLU A 306 11689 14205 10473 -502 -26 -663 O ATOM 2001 CB GLU A 306 46.813 29.999 23.188 1.00101.59 C ANISOU 2001 CB GLU A 306 12361 15462 10776 -512 16 -1073 C ATOM 2002 CG GLU A 306 46.422 28.807 24.045 1.00120.68 C ANISOU 2002 CG GLU A 306 14801 17642 13412 -520 23 -1275 C ATOM 2003 CD GLU A 306 44.926 28.740 24.297 1.00141.86 C ANISOU 2003 CD GLU A 306 17494 20285 16123 -561 -87 -1333 C ATOM 2004 OE1 GLU A 306 44.518 28.717 25.478 1.00143.01 O ANISOU 2004 OE1 GLU A 306 17677 20190 16471 -570 -120 -1284 O ATOM 2005 OE2 GLU A 306 44.155 28.720 23.313 1.00149.48 O ANISOU 2005 OE2 GLU A 306 18422 21475 16899 -584 -141 -1431 O ATOM 2006 N ARG A 307 48.605 32.427 24.395 1.00103.04 N ANISOU 2006 N ARG A 307 12564 15478 11107 -496 64 -502 N ATOM 2007 CA ARG A 307 49.637 32.888 25.316 1.00101.10 C ANISOU 2007 CA ARG A 307 12314 15071 11028 -494 111 -369 C ATOM 2008 C ARG A 307 49.113 33.994 26.224 1.00102.15 C ANISOU 2008 C ARG A 307 12485 15056 11272 -517 29 -168 C ATOM 2009 O ARG A 307 49.438 34.031 27.416 1.00 97.18 O ANISOU 2009 O ARG A 307 11866 14223 10836 -518 22 -135 O ATOM 2010 CB ARG A 307 50.861 33.367 24.534 1.00 90.53 C ANISOU 2010 CB ARG A 307 10927 13897 9572 -495 218 -280 C ATOM 2011 N LYS A 308 48.302 34.905 25.680 1.00103.76 N ANISOU 2011 N LYS A 308 12706 15365 11353 -529 -33 -33 N ATOM 2012 CA LYS A 308 47.750 35.973 26.505 1.00116.97 C ANISOU 2012 CA LYS A 308 14414 16889 13141 -545 -104 148 C ATOM 2013 C LYS A 308 46.763 35.433 27.534 1.00112.77 C ANISOU 2013 C LYS A 308 13912 16173 12763 -544 -186 42 C ATOM 2014 O LYS A 308 46.621 36.014 28.616 1.00112.34 O ANISOU 2014 O LYS A 308 13882 15935 12867 -557 -219 138 O ATOM 2015 CB LYS A 308 47.087 37.033 25.622 1.00133.31 C ANISOU 2015 CB LYS A 308 16493 19114 15046 -538 -148 324 C ATOM 2016 CG LYS A 308 48.051 37.742 24.672 1.00138.31 C ANISOU 2016 CG LYS A 308 17107 19912 15532 -545 -54 477 C ATOM 2017 CD LYS A 308 47.304 38.571 23.631 1.00137.14 C ANISOU 2017 CD LYS A 308 16973 19953 15180 -520 -99 639 C ATOM 2018 CE LYS A 308 48.249 39.096 22.558 1.00135.40 C ANISOU 2018 CE LYS A 308 16738 19926 14780 -527 11 777 C ATOM 2019 NZ LYS A 308 47.527 39.851 21.496 1.00130.11 N ANISOU 2019 NZ LYS A 308 16088 19461 13887 -487 -32 950 N ATOM 2020 N ALA A 309 46.083 34.325 27.225 1.00104.16 N ANISOU 2020 N ALA A 309 12817 15129 11631 -536 -210 -163 N ATOM 2021 CA ALA A 309 45.166 33.736 28.195 1.00101.19 C ANISOU 2021 CA ALA A 309 12467 14574 11408 -545 -267 -269 C ATOM 2022 C ALA A 309 45.925 33.060 29.330 1.00102.34 C ANISOU 2022 C ALA A 309 12631 14510 11744 -539 -214 -327 C ATOM 2023 O ALA A 309 45.550 33.196 30.500 1.00100.56 O ANISOU 2023 O ALA A 309 12437 14098 11672 -548 -250 -288 O ATOM 2024 CB ALA A 309 44.228 32.745 27.503 1.00 86.78 C ANISOU 2024 CB ALA A 309 10624 12856 9494 -553 -298 -483 C ATOM 2025 N SER A 310 46.997 32.330 29.005 1.00101.37 N ANISOU 2025 N SER A 310 12484 14425 11606 -516 -126 -419 N ATOM 2026 CA SER A 310 47.830 31.738 30.048 1.00109.50 C ANISOU 2026 CA SER A 310 13522 15276 12808 -489 -79 -449 C ATOM 2027 C SER A 310 48.456 32.803 30.937 1.00103.71 C ANISOU 2027 C SER A 310 12787 14454 12163 -497 -92 -258 C ATOM 2028 O SER A 310 48.728 32.548 32.116 1.00111.56 O ANISOU 2028 O SER A 310 13799 15280 13309 -481 -97 -252 O ATOM 2029 CB SER A 310 48.926 30.868 29.428 1.00118.59 C ANISOU 2029 CB SER A 310 14632 16505 13923 -450 21 -571 C ATOM 2030 OG SER A 310 48.389 29.728 28.784 1.00124.95 O ANISOU 2030 OG SER A 310 15442 17351 14684 -445 44 -786 O ATOM 2031 N LYS A 311 48.706 33.993 30.389 1.00 97.82 N ANISOU 2031 N LYS A 311 12021 13822 11326 -523 -93 -102 N ATOM 2032 CA LYS A 311 49.266 35.075 31.189 1.00100.43 C ANISOU 2032 CA LYS A 311 12345 14063 11751 -548 -98 65 C ATOM 2033 C LYS A 311 48.263 35.553 32.232 1.00110.17 C ANISOU 2033 C LYS A 311 13628 15138 13095 -567 -181 118 C ATOM 2034 O LYS A 311 48.593 35.676 33.418 1.00106.32 O ANISOU 2034 O LYS A 311 13148 14506 12743 -571 -192 144 O ATOM 2035 CB LYS A 311 49.695 36.223 30.272 1.00 92.66 C ANISOU 2035 CB LYS A 311 11334 13223 10651 -578 -63 220 C ATOM 2036 CG LYS A 311 50.442 37.365 30.953 1.00 92.60 C ANISOU 2036 CG LYS A 311 11306 13129 10747 -620 -44 377 C ATOM 2037 CD LYS A 311 50.901 38.372 29.903 1.00119.91 C ANISOU 2037 CD LYS A 311 14741 16729 14090 -653 17 529 C ATOM 2038 CE LYS A 311 51.599 39.579 30.506 1.00127.44 C ANISOU 2038 CE LYS A 311 15672 17587 15161 -712 48 679 C ATOM 2039 NZ LYS A 311 51.989 40.552 29.443 1.00120.27 N ANISOU 2039 NZ LYS A 311 14750 16801 14146 -749 125 842 N ATOM 2040 N VAL A 312 47.022 35.807 31.807 1.00105.65 N ANISOU 2040 N VAL A 312 13082 14603 12458 -575 -241 127 N ATOM 2041 CA VAL A 312 45.998 36.316 32.719 1.00 83.65 C ANISOU 2041 CA VAL A 312 10333 11679 9773 -591 -313 175 C ATOM 2042 C VAL A 312 45.693 35.295 33.808 1.00 88.92 C ANISOU 2042 C VAL A 312 11029 12192 10566 -582 -323 48 C ATOM 2043 O VAL A 312 45.640 35.627 34.998 1.00 87.07 O ANISOU 2043 O VAL A 312 10819 11812 10453 -593 -344 94 O ATOM 2044 CB VAL A 312 44.726 36.693 31.940 1.00 89.22 C ANISOU 2044 CB VAL A 312 11041 12482 10378 -588 -376 198 C ATOM 2045 CG1 VAL A 312 43.643 37.171 32.892 1.00 87.03 C ANISOU 2045 CG1 VAL A 312 10790 12062 10215 -598 -443 232 C ATOM 2046 CG2 VAL A 312 45.041 37.751 30.896 1.00102.81 C ANISOU 2046 CG2 VAL A 312 12744 14351 11970 -586 -361 358 C ATOM 2047 N LEU A 313 45.477 34.037 33.413 1.00 92.56 N ANISOU 2047 N LEU A 313 11492 12682 10997 -564 -302 -114 N ATOM 2048 CA LEU A 313 45.128 33.006 34.387 1.00 85.05 C ANISOU 2048 CA LEU A 313 10576 11570 10168 -556 -296 -224 C ATOM 2049 C LEU A 313 46.230 32.825 35.424 1.00 87.93 C ANISOU 2049 C LEU A 313 10948 11822 10638 -527 -261 -185 C ATOM 2050 O LEU A 313 45.948 32.706 36.622 1.00 92.87 O ANISOU 2050 O LEU A 313 11612 12303 11373 -527 -279 -170 O ATOM 2051 CB LEU A 313 44.830 31.689 33.671 1.00 84.83 C ANISOU 2051 CB LEU A 313 10545 11585 10102 -546 -260 -412 C ATOM 2052 CG LEU A 313 43.516 31.689 32.889 1.00 97.12 C ANISOU 2052 CG LEU A 313 12088 13242 11573 -580 -312 -487 C ATOM 2053 CD1 LEU A 313 43.438 30.508 31.931 1.00 84.81 C ANISOU 2053 CD1 LEU A 313 10507 11770 9945 -581 -269 -690 C ATOM 2054 CD2 LEU A 313 42.339 31.681 33.853 1.00 97.91 C ANISOU 2054 CD2 LEU A 313 12218 13199 11786 -610 -358 -497 C ATOM 2055 N GLY A 314 47.491 32.821 34.986 1.00 78.20 N ANISOU 2055 N GLY A 314 9672 10672 9368 -501 -210 -166 N ATOM 2056 CA GLY A 314 48.587 32.687 35.932 1.00 81.58 C ANISOU 2056 CA GLY A 314 10086 11023 9889 -466 -187 -130 C ATOM 2057 C GLY A 314 48.614 33.798 36.965 1.00 82.00 C ANISOU 2057 C GLY A 314 10144 11005 10006 -500 -236 -3 C ATOM 2058 O GLY A 314 48.876 33.556 38.146 1.00 88.97 O ANISOU 2058 O GLY A 314 11043 11783 10979 -478 -250 5 O ATOM 2059 N ILE A 315 48.340 35.031 36.537 1.00 84.41 N ANISOU 2059 N ILE A 315 10438 11368 10265 -551 -260 96 N ATOM 2060 CA ILE A 315 48.313 36.149 37.475 1.00 86.76 C ANISOU 2060 CA ILE A 315 10741 11587 10637 -591 -297 199 C ATOM 2061 C ILE A 315 47.154 35.993 38.452 1.00 86.42 C ANISOU 2061 C ILE A 315 10758 11414 10663 -597 -346 172 C ATOM 2062 O ILE A 315 47.317 36.166 39.664 1.00 93.44 O ANISOU 2062 O ILE A 315 11661 12211 11633 -601 -366 189 O ATOM 2063 CB ILE A 315 48.240 37.486 36.718 1.00 80.23 C ANISOU 2063 CB ILE A 315 9894 10828 9761 -639 -297 318 C ATOM 2064 CG1 ILE A 315 49.512 37.700 35.901 1.00 88.04 C ANISOU 2064 CG1 ILE A 315 10819 11939 10691 -646 -231 357 C ATOM 2065 CG2 ILE A 315 48.032 38.634 37.689 1.00 75.13 C ANISOU 2065 CG2 ILE A 315 9260 10073 9212 -685 -330 402 C ATOM 2066 CD1 ILE A 315 49.411 38.830 34.912 1.00 97.13 C ANISOU 2066 CD1 ILE A 315 11961 13173 11770 -685 -210 483 C ATOM 2067 N VAL A 316 45.968 35.660 37.939 1.00 75.61 N ANISOU 2067 N VAL A 316 9419 10052 9258 -599 -365 121 N ATOM 2068 CA VAL A 316 44.818 35.430 38.810 1.00 78.26 C ANISOU 2068 CA VAL A 316 9802 10273 9663 -609 -399 83 C ATOM 2069 C VAL A 316 45.100 34.290 39.780 1.00 81.07 C ANISOU 2069 C VAL A 316 10190 10527 10085 -577 -373 14 C ATOM 2070 O VAL A 316 44.772 34.370 40.971 1.00 79.81 O ANISOU 2070 O VAL A 316 10065 10263 9994 -584 -388 31 O ATOM 2071 CB VAL A 316 43.558 35.159 37.967 1.00 80.60 C ANISOU 2071 CB VAL A 316 10101 10619 9905 -619 -421 21 C ATOM 2072 CG1 VAL A 316 42.473 34.530 38.822 1.00 65.84 C ANISOU 2072 CG1 VAL A 316 8270 8631 8114 -632 -431 -56 C ATOM 2073 CG2 VAL A 316 43.063 36.452 37.329 1.00 66.59 C ANISOU 2073 CG2 VAL A 316 8302 8917 8081 -637 -462 125 C ATOM 2074 N PHE A 317 45.729 33.219 39.292 1.00 82.56 N ANISOU 2074 N PHE A 317 10370 10746 10253 -534 -327 -60 N ATOM 2075 CA PHE A 317 45.985 32.058 40.139 1.00 79.87 C ANISOU 2075 CA PHE A 317 10067 10297 9984 -487 -294 -112 C ATOM 2076 C PHE A 317 46.981 32.389 41.242 1.00 78.03 C ANISOU 2076 C PHE A 317 9823 10033 9791 -457 -307 -30 C ATOM 2077 O PHE A 317 46.706 32.171 42.427 1.00 85.13 O ANISOU 2077 O PHE A 317 10768 10833 10745 -446 -318 -10 O ATOM 2078 CB PHE A 317 46.499 30.891 39.294 1.00 70.08 C ANISOU 2078 CB PHE A 317 8813 9090 8725 -439 -234 -213 C ATOM 2079 CG PHE A 317 45.497 30.363 38.304 1.00 85.92 C ANISOU 2079 CG PHE A 317 10827 11127 10692 -472 -220 -329 C ATOM 2080 CD1 PHE A 317 44.155 30.704 38.394 1.00 82.63 C ANISOU 2080 CD1 PHE A 317 10430 10686 10279 -530 -261 -342 C ATOM 2081 CD2 PHE A 317 45.903 29.522 37.281 1.00 94.23 C ANISOU 2081 CD2 PHE A 317 11855 12245 11703 -446 -167 -441 C ATOM 2082 CE1 PHE A 317 43.240 30.214 37.483 1.00 82.70 C ANISOU 2082 CE1 PHE A 317 10428 10747 10248 -563 -258 -464 C ATOM 2083 CE2 PHE A 317 44.993 29.030 36.365 1.00 92.95 C ANISOU 2083 CE2 PHE A 317 11691 12131 11496 -483 -159 -572 C ATOM 2084 CZ PHE A 317 43.659 29.377 36.465 1.00 90.57 C ANISOU 2084 CZ PHE A 317 11402 11816 11194 -544 -209 -583 C ATOM 2085 N PHE A 318 48.144 32.923 40.870 1.00 91.05 N ANISOU 2085 N PHE A 318 11407 11781 11408 -447 -304 14 N ATOM 2086 CA PHE A 318 49.225 33.109 41.827 1.00 97.06 C ANISOU 2086 CA PHE A 318 12134 12541 12203 -414 -319 67 C ATOM 2087 C PHE A 318 49.033 34.326 42.721 1.00 95.50 C ANISOU 2087 C PHE A 318 11936 12322 12027 -474 -370 136 C ATOM 2088 O PHE A 318 49.599 34.359 43.818 1.00100.61 O ANISOU 2088 O PHE A 318 12572 12953 12702 -451 -396 160 O ATOM 2089 CB PHE A 318 50.565 33.193 41.091 1.00113.77 C ANISOU 2089 CB PHE A 318 14163 14777 14289 -389 -288 71 C ATOM 2090 CG PHE A 318 51.060 31.861 40.601 1.00133.01 C ANISOU 2090 CG PHE A 318 16590 17219 16728 -304 -232 -6 C ATOM 2091 CD1 PHE A 318 50.598 31.329 39.407 1.00127.54 C ANISOU 2091 CD1 PHE A 318 15911 16558 15990 -308 -187 -87 C ATOM 2092 CD2 PHE A 318 51.971 31.130 41.346 1.00137.63 C ANISOU 2092 CD2 PHE A 318 17152 17779 17364 -213 -225 -3 C ATOM 2093 CE1 PHE A 318 51.044 30.099 38.961 1.00131.73 C ANISOU 2093 CE1 PHE A 318 16434 17080 16537 -232 -125 -178 C ATOM 2094 CE2 PHE A 318 52.422 29.900 40.904 1.00133.04 C ANISOU 2094 CE2 PHE A 318 16563 17181 16805 -123 -165 -74 C ATOM 2095 CZ PHE A 318 51.957 29.384 39.710 1.00133.34 C ANISOU 2095 CZ PHE A 318 16618 17235 16810 -137 -109 -170 C ATOM 2096 N VAL A 319 48.254 35.323 42.298 1.00 76.72 N ANISOU 2096 N VAL A 319 9565 9947 9636 -544 -387 165 N ATOM 2097 CA VAL A 319 47.912 36.390 43.232 1.00 73.99 C ANISOU 2097 CA VAL A 319 9230 9551 9331 -597 -426 210 C ATOM 2098 C VAL A 319 46.951 35.867 44.290 1.00 82.74 C ANISOU 2098 C VAL A 319 10410 10556 10471 -584 -441 180 C ATOM 2099 O VAL A 319 47.092 36.172 45.480 1.00 83.54 O ANISOU 2099 O VAL A 319 10521 10624 10597 -591 -466 194 O ATOM 2100 CB VAL A 319 47.344 37.612 42.489 1.00 80.25 C ANISOU 2100 CB VAL A 319 10013 10359 10120 -660 -432 261 C ATOM 2101 CG1 VAL A 319 46.714 38.584 43.473 1.00 64.42 C ANISOU 2101 CG1 VAL A 319 8031 8269 8175 -707 -463 283 C ATOM 2102 CG2 VAL A 319 48.448 38.307 41.713 1.00 65.52 C ANISOU 2102 CG2 VAL A 319 8077 8585 8233 -685 -406 314 C ATOM 2103 N PHE A 320 45.976 35.052 43.879 1.00 89.14 N ANISOU 2103 N PHE A 320 11267 11324 11278 -571 -421 132 N ATOM 2104 CA PHE A 320 45.124 34.368 44.847 1.00 86.16 C ANISOU 2104 CA PHE A 320 10956 10844 10936 -562 -414 102 C ATOM 2105 C PHE A 320 45.959 33.538 45.814 1.00 82.84 C ANISOU 2105 C PHE A 320 10554 10398 10523 -496 -402 116 C ATOM 2106 O PHE A 320 45.756 33.592 47.032 1.00 84.32 O ANISOU 2106 O PHE A 320 10779 10538 10722 -495 -415 139 O ATOM 2107 CB PHE A 320 44.104 33.488 44.122 1.00 81.34 C ANISOU 2107 CB PHE A 320 10376 10199 10330 -565 -382 30 C ATOM 2108 CG PHE A 320 43.182 32.735 45.044 1.00 83.52 C ANISOU 2108 CG PHE A 320 10718 10362 10655 -568 -355 -1 C ATOM 2109 CD1 PHE A 320 42.004 33.313 45.488 1.00 97.56 C ANISOU 2109 CD1 PHE A 320 12511 12098 12458 -621 -368 -6 C ATOM 2110 CD2 PHE A 320 43.489 31.450 45.461 1.00 88.27 C ANISOU 2110 CD2 PHE A 320 11364 10891 11283 -515 -305 -20 C ATOM 2111 CE1 PHE A 320 41.150 32.627 46.334 1.00100.27 C ANISOU 2111 CE1 PHE A 320 12911 12342 12846 -633 -329 -34 C ATOM 2112 CE2 PHE A 320 42.641 30.759 46.309 1.00103.85 C ANISOU 2112 CE2 PHE A 320 13404 12751 13305 -524 -264 -34 C ATOM 2113 CZ PHE A 320 41.470 31.349 46.744 1.00108.86 C ANISOU 2113 CZ PHE A 320 14049 13356 13956 -589 -273 -43 C ATOM 2114 N LEU A 321 46.910 32.765 45.284 1.00 80.38 N ANISOU 2114 N LEU A 321 10215 10125 10201 -434 -378 104 N ATOM 2115 CA LEU A 321 47.783 31.967 46.141 1.00 83.51 C ANISOU 2115 CA LEU A 321 10618 10504 10606 -349 -372 131 C ATOM 2116 C LEU A 321 48.579 32.851 47.095 1.00 84.82 C ANISOU 2116 C LEU A 321 10738 10739 10751 -353 -428 185 C ATOM 2117 O LEU A 321 48.705 32.537 48.283 1.00 80.85 O ANISOU 2117 O LEU A 321 10267 10213 10240 -311 -446 220 O ATOM 2118 CB LEU A 321 48.718 31.110 45.281 1.00 85.59 C ANISOU 2118 CB LEU A 321 10841 10806 10872 -275 -333 101 C ATOM 2119 CG LEU A 321 49.764 30.205 45.949 1.00 95.50 C ANISOU 2119 CG LEU A 321 12085 12054 12145 -159 -324 134 C ATOM 2120 CD1 LEU A 321 49.937 28.923 45.151 1.00 99.67 C ANISOU 2120 CD1 LEU A 321 12627 12529 12714 -87 -252 73 C ATOM 2121 CD2 LEU A 321 51.109 30.914 46.089 1.00 88.66 C ANISOU 2121 CD2 LEU A 321 11113 11323 11250 -139 -370 170 C ATOM 2122 N ILE A 322 49.106 33.973 46.597 1.00 87.21 N ANISOU 2122 N ILE A 322 10966 11128 11041 -410 -454 192 N ATOM 2123 CA ILE A 322 49.977 34.814 47.414 1.00 91.49 C ANISOU 2123 CA ILE A 322 11445 11742 11573 -428 -503 217 C ATOM 2124 C ILE A 322 49.180 35.548 48.488 1.00 84.66 C ANISOU 2124 C ILE A 322 10625 10830 10711 -486 -534 219 C ATOM 2125 O ILE A 322 49.646 35.710 49.623 1.00 79.10 O ANISOU 2125 O ILE A 322 9906 10165 9984 -472 -574 226 O ATOM 2126 CB ILE A 322 50.765 35.786 46.516 1.00 99.46 C ANISOU 2126 CB ILE A 322 12361 12841 12588 -485 -500 220 C ATOM 2127 CG1 ILE A 322 51.889 35.041 45.797 1.00112.95 C ANISOU 2127 CG1 ILE A 322 14002 14630 14285 -414 -472 212 C ATOM 2128 CG2 ILE A 322 51.323 36.948 47.322 1.00 77.67 C ANISOU 2128 CG2 ILE A 322 9540 10129 9841 -549 -544 224 C ATOM 2129 CD1 ILE A 322 52.765 34.232 46.725 1.00123.95 C ANISOU 2129 CD1 ILE A 322 15365 16058 15673 -313 -499 220 C ATOM 2130 N MET A 323 47.964 35.993 48.158 1.00 79.44 N ANISOU 2130 N MET A 323 10014 10097 10074 -547 -517 206 N ATOM 2131 CA MET A 323 47.174 36.775 49.104 1.00 83.81 C ANISOU 2131 CA MET A 323 10601 10603 10640 -604 -536 196 C ATOM 2132 C MET A 323 46.509 35.924 50.179 1.00 82.72 C ANISOU 2132 C MET A 323 10543 10407 10481 -564 -525 196 C ATOM 2133 O MET A 323 46.069 36.470 51.197 1.00 78.48 O ANISOU 2133 O MET A 323 10028 9855 9935 -599 -539 183 O ATOM 2134 CB MET A 323 46.118 37.590 48.357 1.00 76.74 C ANISOU 2134 CB MET A 323 9718 9655 9786 -669 -523 189 C ATOM 2135 CG MET A 323 46.720 38.627 47.421 1.00 77.73 C ANISOU 2135 CG MET A 323 9775 9828 9932 -715 -526 215 C ATOM 2136 SD MET A 323 45.529 39.827 46.797 1.00 92.98 S ANISOU 2136 SD MET A 323 11717 11694 11916 -778 -519 234 S ATOM 2137 CE MET A 323 45.342 40.882 48.233 1.00 88.92 C ANISOU 2137 CE MET A 323 11208 11122 11455 -833 -536 200 C ATOM 2138 N TRP A 324 46.425 34.610 49.988 1.00 82.63 N ANISOU 2138 N TRP A 324 10576 10357 10465 -495 -490 207 N ATOM 2139 CA TRP A 324 45.886 33.726 51.013 1.00 84.39 C ANISOU 2139 CA TRP A 324 10879 10514 10672 -454 -463 227 C ATOM 2140 C TRP A 324 46.966 33.005 51.806 1.00 92.42 C ANISOU 2140 C TRP A 324 11894 11582 11641 -357 -481 282 C ATOM 2141 O TRP A 324 46.662 32.443 52.864 1.00 96.51 O ANISOU 2141 O TRP A 324 12478 12067 12125 -318 -466 323 O ATOM 2142 CB TRP A 324 44.936 32.692 50.391 1.00 66.19 C ANISOU 2142 CB TRP A 324 8634 8103 8412 -447 -396 205 C ATOM 2143 CG TRP A 324 43.519 33.172 50.297 1.00 68.88 C ANISOU 2143 CG TRP A 324 9000 8385 8786 -529 -377 162 C ATOM 2144 CD1 TRP A 324 42.829 33.480 49.161 1.00 64.36 C ANISOU 2144 CD1 TRP A 324 8401 7807 8248 -577 -372 113 C ATOM 2145 CD2 TRP A 324 42.619 33.406 51.389 1.00 74.37 C ANISOU 2145 CD2 TRP A 324 9743 9035 9477 -565 -359 162 C ATOM 2146 NE1 TRP A 324 41.553 33.887 49.477 1.00 74.16 N ANISOU 2146 NE1 TRP A 324 9661 8998 9517 -636 -359 84 N ATOM 2147 CE2 TRP A 324 41.400 33.850 50.838 1.00 75.41 C ANISOU 2147 CE2 TRP A 324 9867 9128 9659 -633 -344 108 C ATOM 2148 CE3 TRP A 324 42.726 33.280 52.778 1.00 74.74 C ANISOU 2148 CE3 TRP A 324 9836 9087 9475 -543 -355 202 C ATOM 2149 CZ2 TRP A 324 40.297 34.172 51.628 1.00 74.63 C ANISOU 2149 CZ2 TRP A 324 9797 8984 9576 -680 -317 86 C ATOM 2150 CZ3 TRP A 324 41.629 33.600 53.561 1.00 73.06 C ANISOU 2150 CZ3 TRP A 324 9662 8834 9265 -596 -323 181 C ATOM 2151 CH2 TRP A 324 40.432 34.041 52.984 1.00 79.19 C ANISOU 2151 CH2 TRP A 324 10423 9561 10106 -665 -301 120 C ATOM 2152 N CYS A 325 48.210 33.013 51.329 1.00 79.35 N ANISOU 2152 N CYS A 325 10159 10014 9978 -312 -512 289 N ATOM 2153 CA CYS A 325 49.282 32.319 52.038 1.00 85.97 C ANISOU 2153 CA CYS A 325 10976 10916 10774 -201 -539 344 C ATOM 2154 C CYS A 325 49.504 32.833 53.455 1.00 93.34 C ANISOU 2154 C CYS A 325 11904 11932 11629 -201 -598 368 C ATOM 2155 O CYS A 325 49.572 32.001 54.377 1.00 97.67 O ANISOU 2155 O CYS A 325 12507 12476 12127 -111 -596 436 O ATOM 2156 CB CYS A 325 50.573 32.385 51.215 1.00 97.58 C ANISOU 2156 CB CYS A 325 12337 12483 12258 -163 -561 332 C ATOM 2157 SG CYS A 325 50.753 31.019 50.041 1.00112.03 S ANISOU 2157 SG CYS A 325 14184 14236 14147 -74 -486 326 S ATOM 2158 N PRO A 326 49.626 34.145 53.715 1.00 97.25 N ANISOU 2158 N PRO A 326 12339 12504 12107 -294 -647 315 N ATOM 2159 CA PRO A 326 49.944 34.569 55.093 1.00 94.38 C ANISOU 2159 CA PRO A 326 11960 12244 11656 -291 -707 315 C ATOM 2160 C PRO A 326 48.933 34.077 56.112 1.00 94.00 C ANISOU 2160 C PRO A 326 12029 12135 11554 -274 -674 353 C ATOM 2161 O PRO A 326 49.322 33.613 57.192 1.00 77.98 O ANISOU 2161 O PRO A 326 10017 10185 9427 -195 -706 409 O ATOM 2162 CB PRO A 326 49.963 36.103 54.995 1.00 87.11 C ANISOU 2162 CB PRO A 326 10970 11364 10764 -421 -736 226 C ATOM 2163 CG PRO A 326 50.172 36.396 53.550 1.00 89.86 C ANISOU 2163 CG PRO A 326 11269 11674 11201 -460 -708 212 C ATOM 2164 CD PRO A 326 49.450 35.308 52.825 1.00 86.07 C ANISOU 2164 CD PRO A 326 10871 11081 10752 -406 -644 254 C ATOM 2165 N PHE A 327 47.640 34.150 55.784 1.00 81.72 N ANISOU 2165 N PHE A 327 10547 10449 10054 -341 -608 330 N ATOM 2166 CA PHE A 327 46.616 33.586 56.656 1.00 74.32 C ANISOU 2166 CA PHE A 327 9717 9442 9079 -332 -555 366 C ATOM 2167 C PHE A 327 46.822 32.087 56.842 1.00 84.61 C ANISOU 2167 C PHE A 327 11088 10693 10365 -210 -513 471 C ATOM 2168 O PHE A 327 46.848 31.587 57.974 1.00 91.61 O ANISOU 2168 O PHE A 327 12032 11615 11162 -147 -510 546 O ATOM 2169 CB PHE A 327 45.228 33.879 56.083 1.00 72.61 C ANISOU 2169 CB PHE A 327 9544 9099 8947 -424 -490 313 C ATOM 2170 CG PHE A 327 44.112 33.142 56.775 1.00 96.96 C ANISOU 2170 CG PHE A 327 12732 12092 12017 -422 -411 347 C ATOM 2171 CD1 PHE A 327 43.537 33.647 57.931 1.00 96.52 C ANISOU 2171 CD1 PHE A 327 12709 12072 11893 -463 -402 330 C ATOM 2172 CD2 PHE A 327 43.626 31.949 56.258 1.00 97.61 C ANISOU 2172 CD2 PHE A 327 12875 12051 12162 -388 -336 385 C ATOM 2173 CE1 PHE A 327 42.507 32.971 58.565 1.00 87.64 C ANISOU 2173 CE1 PHE A 327 11676 10868 10755 -468 -315 366 C ATOM 2174 CE2 PHE A 327 42.601 31.270 56.886 1.00 91.91 C ANISOU 2174 CE2 PHE A 327 12244 11236 11442 -399 -249 416 C ATOM 2175 CZ PHE A 327 42.039 31.781 58.041 1.00 88.39 C ANISOU 2175 CZ PHE A 327 11830 10833 10921 -439 -237 414 C ATOM 2176 N PHE A 328 46.981 31.349 55.740 1.00 76.29 N ANISOU 2176 N PHE A 328 10031 9556 9398 -172 -476 479 N ATOM 2177 CA PHE A 328 47.032 29.894 55.847 1.00 77.61 C ANISOU 2177 CA PHE A 328 10274 9631 9585 -63 -415 568 C ATOM 2178 C PHE A 328 48.347 29.424 56.453 1.00 93.66 C ANISOU 2178 C PHE A 328 12270 11771 11546 75 -473 657 C ATOM 2179 O PHE A 328 48.366 28.455 57.220 1.00108.17 O ANISOU 2179 O PHE A 328 14185 13568 13348 177 -438 768 O ATOM 2180 CB PHE A 328 46.795 29.248 54.485 1.00 89.89 C ANISOU 2180 CB PHE A 328 11832 11066 11258 -69 -352 523 C ATOM 2181 CG PHE A 328 45.348 28.939 54.215 1.00 89.67 C ANISOU 2181 CG PHE A 328 11881 10894 11298 -153 -265 481 C ATOM 2182 CD1 PHE A 328 44.768 27.784 54.718 1.00 85.89 C ANISOU 2182 CD1 PHE A 328 11504 10280 10850 -114 -173 543 C ATOM 2183 CD2 PHE A 328 44.567 29.802 53.465 1.00 87.50 C ANISOU 2183 CD2 PHE A 328 11569 10617 11061 -268 -271 383 C ATOM 2184 CE1 PHE A 328 43.439 27.494 54.478 1.00 83.73 C ANISOU 2184 CE1 PHE A 328 11284 9879 10649 -203 -88 490 C ATOM 2185 CE2 PHE A 328 43.237 29.518 53.221 1.00105.11 C ANISOU 2185 CE2 PHE A 328 13848 12734 13354 -342 -199 335 C ATOM 2186 CZ PHE A 328 42.671 28.360 53.728 1.00 93.72 C ANISOU 2186 CZ PHE A 328 12498 11164 11946 -317 -107 379 C ATOM 2187 N ILE A 329 49.457 30.092 56.126 1.00 92.35 N ANISOU 2187 N ILE A 329 11982 11746 11361 85 -557 617 N ATOM 2188 CA ILE A 329 50.729 29.771 56.773 1.00 86.62 C ANISOU 2188 CA ILE A 329 11194 11158 10558 215 -630 689 C ATOM 2189 C ILE A 329 50.613 29.994 58.273 1.00 97.43 C ANISOU 2189 C ILE A 329 12600 12631 11788 234 -675 744 C ATOM 2190 O ILE A 329 50.836 29.079 59.073 1.00111.09 O ANISOU 2190 O ILE A 329 14388 14370 13452 364 -670 869 O ATOM 2191 CB ILE A 329 51.884 30.598 56.175 1.00 95.80 C ANISOU 2191 CB ILE A 329 12201 12468 11731 193 -708 614 C ATOM 2192 CG1 ILE A 329 52.186 30.155 54.750 1.00 93.24 C ANISOU 2192 CG1 ILE A 329 11841 12067 11520 210 -657 582 C ATOM 2193 CG2 ILE A 329 53.135 30.478 57.034 1.00 98.76 C ANISOU 2193 CG2 ILE A 329 12487 13026 12009 310 -803 669 C ATOM 2194 CD1 ILE A 329 53.428 30.791 54.148 1.00 90.87 C ANISOU 2194 CD1 ILE A 329 11384 11912 11231 204 -716 526 C ATOM 2195 N THR A 330 50.232 31.215 58.670 1.00 98.13 N ANISOU 2195 N THR A 330 12660 12795 11828 106 -714 653 N ATOM 2196 CA THR A 330 50.116 31.545 60.088 1.00 92.92 C ANISOU 2196 CA THR A 330 12026 12259 11020 109 -757 675 C ATOM 2197 C THR A 330 49.158 30.600 60.802 1.00 89.23 C ANISOU 2197 C THR A 330 11710 11682 10511 157 -669 787 C ATOM 2198 O THR A 330 49.379 30.239 61.963 1.00 87.24 O ANISOU 2198 O THR A 330 11495 11533 10118 243 -696 881 O ATOM 2199 CB THR A 330 49.659 32.997 60.255 1.00 89.60 C ANISOU 2199 CB THR A 330 11563 11889 10591 -51 -783 534 C ATOM 2200 OG1 THR A 330 50.578 33.872 59.585 1.00 96.40 O ANISOU 2200 OG1 THR A 330 12287 12837 11505 -104 -850 440 O ATOM 2201 CG2 THR A 330 49.589 33.374 61.728 1.00 77.76 C ANISOU 2201 CG2 THR A 330 10082 10538 8927 -54 -828 530 C ATOM 2202 N ASN A 331 48.096 30.174 60.115 1.00102.92 N ANISOU 2202 N ASN A 331 13527 13214 12363 102 -561 779 N ATOM 2203 CA ASN A 331 47.137 29.257 60.723 1.00108.71 C ANISOU 2203 CA ASN A 331 14400 13823 13082 129 -457 878 C ATOM 2204 C ASN A 331 47.744 27.872 60.925 1.00126.31 C ANISOU 2204 C ASN A 331 16683 16001 15306 299 -428 1040 C ATOM 2205 O ASN A 331 47.674 27.306 62.023 1.00129.02 O ANISOU 2205 O ASN A 331 17108 16374 15540 381 -406 1172 O ATOM 2206 CB ASN A 331 45.878 29.167 59.864 1.00 99.31 C ANISOU 2206 CB ASN A 331 13261 12439 12033 17 -352 808 C ATOM 2207 CG ASN A 331 44.616 29.362 60.669 1.00108.75 C ANISOU 2207 CG ASN A 331 14540 13593 13188 -68 -279 801 C ATOM 2208 OD1 ASN A 331 44.272 28.536 61.512 1.00117.15 O ANISOU 2208 OD1 ASN A 331 15703 14613 14194 -13 -207 917 O ATOM 2209 ND2 ASN A 331 43.913 30.460 60.412 1.00104.36 N ANISOU 2209 ND2 ASN A 331 13940 13046 12664 -198 -287 670 N ATOM 2210 N ILE A 332 48.337 27.301 59.872 1.00131.96 N ANISOU 2210 N ILE A 332 17358 16639 16141 360 -420 1036 N ATOM 2211 CA ILE A 332 48.946 25.984 60.009 1.00136.94 C ANISOU 2211 CA ILE A 332 18036 17202 16794 534 -386 1184 C ATOM 2212 C ILE A 332 50.230 26.046 60.829 1.00141.51 C ANISOU 2212 C ILE A 332 18539 17995 17231 678 -506 1274 C ATOM 2213 O ILE A 332 50.681 25.017 61.345 1.00152.95 O ANISOU 2213 O ILE A 332 20041 19422 18654 845 -489 1436 O ATOM 2214 CB ILE A 332 49.209 25.351 58.630 1.00135.58 C ANISOU 2214 CB ILE A 332 17835 16885 16793 560 -335 1133 C ATOM 2215 CG1 ILE A 332 50.355 26.072 57.913 1.00123.04 C ANISOU 2215 CG1 ILE A 332 16090 15454 15207 568 -442 1042 C ATOM 2216 CG2 ILE A 332 47.931 25.352 57.792 1.00132.25 C ANISOU 2216 CG2 ILE A 332 17470 16286 16494 411 -233 1025 C ATOM 2217 CD1 ILE A 332 50.709 25.479 56.566 1.00105.03 C ANISOU 2217 CD1 ILE A 332 13771 13064 13073 599 -392 985 C ATOM 2218 N LEU A 333 50.835 27.231 60.963 1.00129.24 N ANISOU 2218 N LEU A 333 16859 16652 15593 618 -627 1171 N ATOM 2219 CA LEU A 333 51.965 27.405 61.869 1.00111.01 C ANISOU 2219 CA LEU A 333 14464 14583 13131 733 -753 1231 C ATOM 2220 C LEU A 333 51.516 27.530 63.319 1.00104.87 C ANISOU 2220 C LEU A 333 13764 13916 12166 742 -769 1309 C ATOM 2221 O LEU A 333 52.334 27.341 64.228 1.00105.42 O ANISOU 2221 O LEU A 333 13795 14178 12084 874 -861 1405 O ATOM 2222 CB LEU A 333 52.782 28.638 61.463 1.00100.06 C ANISOU 2222 CB LEU A 333 12904 13378 11737 647 -867 1072 C ATOM 2223 CG LEU A 333 54.271 28.706 61.829 1.00107.04 C ANISOU 2223 CG LEU A 333 13638 14498 12535 771 -1000 1095 C ATOM 2224 CD1 LEU A 333 55.054 27.598 61.136 1.00109.05 C ANISOU 2224 CD1 LEU A 333 13863 14677 12893 939 -977 1187 C ATOM 2225 CD2 LEU A 333 54.865 30.074 61.490 1.00 92.88 C ANISOU 2225 CD2 LEU A 333 11681 12862 10746 635 -1089 914 C ATOM 2226 N SER A 334 50.232 27.822 63.548 1.00 88.30 N ANISOU 2226 N SER A 334 11768 11714 10069 609 -682 1268 N ATOM 2227 CA SER A 334 49.697 27.994 64.892 1.00 94.14 C ANISOU 2227 CA SER A 334 12585 12559 10627 599 -677 1325 C ATOM 2228 C SER A 334 49.326 26.672 65.557 1.00124.93 C ANISOU 2228 C SER A 334 16635 16350 14482 730 -579 1545 C ATOM 2229 O SER A 334 49.192 26.630 66.786 1.00129.81 O ANISOU 2229 O SER A 334 17311 17101 14908 775 -590 1641 O ATOM 2230 CB SER A 334 48.476 28.917 64.846 1.00 92.51 C ANISOU 2230 CB SER A 334 12410 12288 10450 401 -617 1178 C ATOM 2231 OG SER A 334 47.827 28.993 66.104 1.00105.83 O ANISOU 2231 OG SER A 334 14184 14056 11971 385 -583 1228 O ATOM 2232 N VAL A 335 49.159 25.596 64.785 1.00135.32 N ANISOU 2232 N VAL A 335 18018 17430 15969 791 -476 1626 N ATOM 2233 CA VAL A 335 48.872 24.285 65.361 1.00137.64 C ANISOU 2233 CA VAL A 335 18458 17587 16251 921 -368 1846 C ATOM 2234 C VAL A 335 50.093 23.366 65.372 1.00127.30 C ANISOU 2234 C VAL A 335 17120 16306 14944 1150 -420 2006 C ATOM 2235 O VAL A 335 50.130 22.416 66.169 1.00117.98 O ANISOU 2235 O VAL A 335 16046 15089 13693 1298 -368 2226 O ATOM 2236 CB VAL A 335 47.691 23.608 64.631 1.00133.33 C ANISOU 2236 CB VAL A 335 18024 16727 15906 827 -189 1830 C ATOM 2237 CG1 VAL A 335 46.464 24.525 64.634 1.00137.87 C ANISOU 2237 CG1 VAL A 335 18613 17289 16483 614 -142 1675 C ATOM 2238 CG2 VAL A 335 48.081 23.211 63.212 1.00109.69 C ANISOU 2238 CG2 VAL A 335 14972 13579 13127 840 -173 1748 C ATOM 2239 N LEU A 336 51.094 23.627 64.526 1.00148.87 N ANISOU 2239 N LEU A 336 19707 19103 17754 1187 -515 1910 N ATOM 2240 CA LEU A 336 52.343 22.874 64.587 1.00161.92 C ANISOU 2240 CA LEU A 336 21301 20821 19399 1414 -582 2046 C ATOM 2241 C LEU A 336 53.043 23.044 65.930 1.00175.67 C ANISOU 2241 C LEU A 336 23008 22852 20888 1546 -710 2174 C ATOM 2242 O LEU A 336 53.809 22.161 66.341 1.00176.72 O ANISOU 2242 O LEU A 336 23145 23019 20980 1769 -738 2366 O ATOM 2243 CB LEU A 336 53.269 23.299 63.441 1.00154.45 C ANISOU 2243 CB LEU A 336 20186 19927 18572 1403 -661 1890 C ATOM 2244 N CYS A 337 52.790 24.153 66.624 1.00179.19 N ANISOU 2244 N CYS A 337 23414 23509 21161 1418 -788 2069 N ATOM 2245 CA CYS A 337 53.220 24.345 68.008 1.00177.13 C ANISOU 2245 CA CYS A 337 23138 23534 20628 1516 -897 2173 C ATOM 2246 C CYS A 337 51.979 24.612 68.855 1.00169.43 C ANISOU 2246 C CYS A 337 22303 22542 19530 1392 -807 2186 C ATOM 2247 O CYS A 337 51.430 25.718 68.833 1.00158.69 O ANISOU 2247 O CYS A 337 20906 21242 18148 1197 -820 1987 O ATOM 2248 CB CYS A 337 54.233 25.483 68.135 1.00175.96 C ANISOU 2248 CB CYS A 337 22783 23704 20368 1480 -1086 2004 C ATOM 2249 SG CYS A 337 53.777 27.051 67.312 1.00169.08 S ANISOU 2249 SG CYS A 337 21814 22824 19605 1185 -1098 1677 S ATOM 2250 N GLU A 338 51.531 23.599 69.598 1.00177.99 N ANISOU 2250 N GLU A 338 23548 23536 20542 1508 -706 2423 N ATOM 2251 CA GLU A 338 50.370 23.781 70.464 1.00183.24 C ANISOU 2251 CA GLU A 338 24347 24197 21080 1399 -606 2452 C ATOM 2252 C GLU A 338 50.663 24.811 71.547 1.00186.92 C ANISOU 2252 C GLU A 338 24735 25027 21261 1365 -746 2369 C ATOM 2253 O GLU A 338 49.912 25.780 71.723 1.00187.25 O ANISOU 2253 O GLU A 338 24771 25114 21261 1173 -726 2187 O ATOM 2254 CB GLU A 338 49.960 22.443 71.078 1.00183.04 C ANISOU 2254 CB GLU A 338 24506 24014 21026 1545 -465 2748 C ATOM 2255 N LYS A 339 51.759 24.615 72.282 1.00187.67 N ANISOU 2255 N LYS A 339 24760 25388 21157 1553 -889 2492 N ATOM 2256 CA LYS A 339 52.276 25.625 73.197 1.00184.77 C ANISOU 2256 CA LYS A 339 24277 25403 20526 1526 -1054 2375 C ATOM 2257 C LYS A 339 53.613 26.150 72.682 1.00188.93 C ANISOU 2257 C LYS A 339 24583 26113 21089 1569 -1238 2239 C ATOM 2258 O LYS A 339 53.921 26.006 71.495 1.00213.61 O ANISOU 2258 O LYS A 339 27648 29051 24463 1557 -1220 2177 O ATOM 2259 CB LYS A 339 52.404 25.054 74.611 1.00184.79 C ANISOU 2259 CB LYS A 339 24367 25626 20221 1697 -1080 2616 C ATOM 2260 N SER A 340 54.404 26.775 73.551 1.00173.04 N ANISOU 2260 N SER A 340 22443 24474 18831 1610 -1412 2178 N ATOM 2261 CA SER A 340 55.698 27.374 73.225 1.00167.58 C ANISOU 2261 CA SER A 340 21520 24007 18147 1635 -1595 2029 C ATOM 2262 C SER A 340 55.606 28.473 72.174 1.00161.85 C ANISOU 2262 C SER A 340 20683 23175 17635 1403 -1590 1734 C ATOM 2263 O SER A 340 56.644 28.999 71.737 1.00159.64 O ANISOU 2263 O SER A 340 20209 23040 17407 1396 -1717 1597 O ATOM 2264 CB SER A 340 56.715 26.320 72.769 1.00161.40 C ANISOU 2264 CB SER A 340 20681 23187 17457 1877 -1642 2220 C ATOM 2265 N CYS A 341 54.402 28.849 71.760 1.00148.53 N ANISOU 2265 N CYS A 341 19109 21249 16076 1216 -1446 1636 N ATOM 2266 CA CYS A 341 54.212 29.855 70.731 1.00140.21 C ANISOU 2266 CA CYS A 341 17971 20072 15231 1008 -1427 1387 C ATOM 2267 C CYS A 341 53.314 30.969 71.252 1.00118.61 C ANISOU 2267 C CYS A 341 15265 17383 12419 803 -1394 1198 C ATOM 2268 O CYS A 341 52.420 30.739 72.072 1.00108.38 O ANISOU 2268 O CYS A 341 14110 16079 10989 796 -1313 1277 O ATOM 2269 CB CYS A 341 53.613 29.240 69.453 1.00160.62 C ANISOU 2269 CB CYS A 341 20645 22287 18095 982 -1279 1435 C ATOM 2270 SG CYS A 341 54.820 28.489 68.311 1.00173.49 S ANISOU 2270 SG CYS A 341 22164 23844 19913 1136 -1323 1504 S ATOM 2271 N ASN A 342 53.569 32.187 70.774 1.00112.65 N ANISOU 2271 N ASN A 342 14374 16671 11756 636 -1450 948 N ATOM 2272 CA ASN A 342 52.746 33.329 71.150 1.00101.20 C ANISOU 2272 CA ASN A 342 12939 15236 10276 438 -1412 745 C ATOM 2273 C ASN A 342 51.397 33.241 70.449 1.00 97.82 C ANISOU 2273 C ASN A 342 12652 14479 10037 333 -1238 750 C ATOM 2274 O ASN A 342 51.238 33.744 69.333 1.00 88.34 O ANISOU 2274 O ASN A 342 11407 13097 9059 223 -1202 638 O ATOM 2275 CB ASN A 342 53.447 34.648 70.809 1.00 86.90 C ANISOU 2275 CB ASN A 342 10942 13542 8534 293 -1511 484 C ATOM 2276 CG ASN A 342 52.843 35.839 71.535 1.00105.84 C ANISOU 2276 CG ASN A 342 13335 16032 10847 120 -1502 267 C ATOM 2277 OD1 ASN A 342 51.639 35.881 71.796 1.00103.70 O ANISOU 2277 OD1 ASN A 342 13201 15629 10571 56 -1383 271 O ATOM 2278 ND2 ASN A 342 53.682 36.813 71.870 1.00106.72 N ANISOU 2278 ND2 ASN A 342 13281 16372 10898 42 -1624 64 N ATOM 2279 N GLN A 343 50.421 32.602 71.097 1.00100.73 N ANISOU 2279 N GLN A 343 13183 14778 10311 367 -1130 884 N ATOM 2280 CA GLN A 343 49.098 32.471 70.497 1.00 90.46 C ANISOU 2280 CA GLN A 343 12004 13182 9183 267 -965 884 C ATOM 2281 C GLN A 343 48.420 33.827 70.358 1.00 82.47 C ANISOU 2281 C GLN A 343 10949 12140 8246 65 -939 638 C ATOM 2282 O GLN A 343 47.721 34.081 69.370 1.00 80.47 O ANISOU 2282 O GLN A 343 10712 11654 8209 -33 -856 572 O ATOM 2283 CB GLN A 343 48.237 31.522 71.331 1.00 96.37 C ANISOU 2283 CB GLN A 343 12926 13885 9807 338 -847 1075 C ATOM 2284 CG GLN A 343 47.544 30.444 70.516 1.00103.64 C ANISOU 2284 CG GLN A 343 13964 14493 10922 372 -703 1224 C ATOM 2285 CD GLN A 343 48.523 29.468 69.893 1.00104.58 C ANISOU 2285 CD GLN A 343 14057 14557 11122 535 -749 1376 C ATOM 2286 OE1 GLN A 343 48.675 29.415 68.672 1.00 99.85 O ANISOU 2286 OE1 GLN A 343 13410 13789 10739 507 -738 1322 O ATOM 2287 NE2 GLN A 343 49.192 28.685 70.731 1.00116.70 N ANISOU 2287 NE2 GLN A 343 15623 16241 12478 716 -799 1570 N ATOM 2288 N LYS A 344 48.616 34.710 71.341 1.00 83.72 N ANISOU 2288 N LYS A 344 11049 12535 8226 7 -1010 496 N ATOM 2289 CA LYS A 344 48.033 36.046 71.271 1.00 82.75 C ANISOU 2289 CA LYS A 344 10879 12380 8183 -177 -984 252 C ATOM 2290 C LYS A 344 48.540 36.815 70.060 1.00 81.11 C ANISOU 2290 C LYS A 344 10549 12063 8206 -264 -1029 117 C ATOM 2291 O LYS A 344 47.784 37.581 69.452 1.00 79.58 O ANISOU 2291 O LYS A 344 10358 11695 8186 -394 -957 -8 O ATOM 2292 CB LYS A 344 48.338 36.813 72.557 1.00 84.75 C ANISOU 2292 CB LYS A 344 11077 12927 8197 -216 -1062 107 C ATOM 2293 CG LYS A 344 47.506 38.072 72.751 1.00 84.21 C ANISOU 2293 CG LYS A 344 10996 12815 8187 -394 -1000 -135 C ATOM 2294 CD LYS A 344 48.038 38.906 73.907 1.00100.42 C ANISOU 2294 CD LYS A 344 12963 15174 10020 -441 -1096 -320 C ATOM 2295 CE LYS A 344 48.227 38.065 75.169 1.00119.72 C ANISOU 2295 CE LYS A 344 15473 17879 12138 -306 -1132 -169 C ATOM 2296 NZ LYS A 344 46.938 37.635 75.792 1.00114.61 N ANISOU 2296 NZ LYS A 344 14986 17162 11398 -307 -979 -82 N ATOM 2297 N LEU A 345 49.811 36.623 69.693 1.00 86.02 N ANISOU 2297 N LEU A 345 11061 12788 8834 -188 -1143 148 N ATOM 2298 CA LEU A 345 50.346 37.271 68.498 1.00 80.15 C ANISOU 2298 CA LEU A 345 10204 11944 8307 -266 -1172 43 C ATOM 2299 C LEU A 345 49.735 36.690 67.230 1.00 90.12 C ANISOU 2299 C LEU A 345 11541 12921 9781 -257 -1069 146 C ATOM 2300 O LEU A 345 49.413 37.434 66.294 1.00 82.87 O ANISOU 2300 O LEU A 345 10590 11848 9050 -371 -1030 43 O ATOM 2301 CB LEU A 345 51.869 37.138 68.458 1.00 87.64 C ANISOU 2301 CB LEU A 345 11005 13091 9202 -183 -1311 53 C ATOM 2302 CG LEU A 345 52.541 37.675 67.190 1.00 90.21 C ANISOU 2302 CG LEU A 345 11209 13323 9742 -252 -1331 -30 C ATOM 2303 CD1 LEU A 345 52.263 39.161 67.028 1.00 87.79 C ANISOU 2303 CD1 LEU A 345 10841 12972 9544 -449 -1313 -257 C ATOM 2304 CD2 LEU A 345 54.040 37.405 67.195 1.00 81.51 C ANISOU 2304 CD2 LEU A 345 9956 12431 8585 -156 -1460 -8 C ATOM 2305 N MET A 346 49.578 35.364 67.179 1.00 87.19 N ANISOU 2305 N MET A 346 11268 12477 9383 -121 -1025 349 N ATOM 2306 CA MET A 346 49.023 34.713 65.996 1.00 82.71 C ANISOU 2306 CA MET A 346 10767 11652 9008 -111 -928 432 C ATOM 2307 C MET A 346 47.653 35.277 65.651 1.00 90.11 C ANISOU 2307 C MET A 346 11771 12405 10062 -247 -819 344 C ATOM 2308 O MET A 346 47.366 35.581 64.488 1.00 73.66 O ANISOU 2308 O MET A 346 9665 10161 8162 -314 -783 294 O ATOM 2309 CB MET A 346 48.927 33.205 66.225 1.00 97.77 C ANISOU 2309 CB MET A 346 12786 13501 10862 45 -877 651 C ATOM 2310 CG MET A 346 50.227 32.525 66.612 1.00105.78 C ANISOU 2310 CG MET A 346 13741 14690 11761 213 -981 768 C ATOM 2311 SD MET A 346 51.227 32.039 65.195 1.00121.25 S ANISOU 2311 SD MET A 346 15605 16558 13904 287 -1011 799 S ATOM 2312 CE MET A 346 52.276 33.481 64.988 1.00117.72 C ANISOU 2312 CE MET A 346 14955 16307 13465 180 -1142 592 C ATOM 2313 N GLU A 347 46.789 35.416 66.659 1.00103.01 N ANISOU 2313 N GLU A 347 13483 14073 11582 -283 -765 326 N ATOM 2314 CA GLU A 347 45.443 35.918 66.412 1.00 96.95 C ANISOU 2314 CA GLU A 347 12771 13143 10924 -400 -658 243 C ATOM 2315 C GLU A 347 45.476 37.340 65.872 1.00 92.13 C ANISOU 2315 C GLU A 347 12060 12510 10437 -529 -691 52 C ATOM 2316 O GLU A 347 44.721 37.679 64.953 1.00 95.33 O ANISOU 2316 O GLU A 347 12471 12736 11016 -598 -629 10 O ATOM 2317 CB GLU A 347 44.614 35.852 67.692 1.00 97.32 C ANISOU 2317 CB GLU A 347 12905 13262 10811 -413 -592 248 C ATOM 2318 CG GLU A 347 43.156 36.213 67.483 1.00107.06 C ANISOU 2318 CG GLU A 347 14192 14327 12159 -517 -469 175 C ATOM 2319 CD GLU A 347 42.578 36.989 68.646 1.00129.32 C ANISOU 2319 CD GLU A 347 17023 17263 14849 -588 -437 54 C ATOM 2320 OE1 GLU A 347 43.308 37.213 69.634 1.00133.16 O ANISOU 2320 OE1 GLU A 347 17483 17972 15141 -558 -513 25 O ATOM 2321 OE2 GLU A 347 41.394 37.380 68.568 1.00138.93 O ANISOU 2321 OE2 GLU A 347 18269 18361 16158 -671 -337 -22 O ATOM 2322 N LYS A 348 46.351 38.185 66.425 1.00 86.48 N ANISOU 2322 N LYS A 348 11247 11975 9637 -562 -787 -65 N ATOM 2323 CA LYS A 348 46.443 39.565 65.960 1.00 84.28 C ANISOU 2323 CA LYS A 348 10875 11660 9490 -689 -807 -245 C ATOM 2324 C LYS A 348 46.939 39.636 64.520 1.00 97.02 C ANISOU 2324 C LYS A 348 12425 13150 11287 -697 -823 -218 C ATOM 2325 O LYS A 348 46.441 40.444 63.726 1.00 99.16 O ANISOU 2325 O LYS A 348 12678 13276 11724 -787 -780 -293 O ATOM 2326 CB LYS A 348 47.351 40.368 66.889 1.00 80.78 C ANISOU 2326 CB LYS A 348 10332 11442 8918 -729 -903 -387 C ATOM 2327 CG LYS A 348 46.849 40.435 68.320 1.00 78.99 C ANISOU 2327 CG LYS A 348 10161 11361 8491 -733 -886 -440 C ATOM 2328 CD LYS A 348 45.469 41.068 68.383 1.00 98.36 C ANISOU 2328 CD LYS A 348 12678 13660 11034 -829 -769 -536 C ATOM 2329 CE LYS A 348 44.843 40.900 69.759 1.00117.25 C ANISOU 2329 CE LYS A 348 15144 16187 13217 -819 -725 -558 C ATOM 2330 NZ LYS A 348 45.737 41.411 70.837 1.00127.94 N ANISOU 2330 NZ LYS A 348 16422 17816 14374 -833 -826 -686 N ATOM 2331 N LEU A 349 47.920 38.803 64.164 1.00 73.09 N ANISOU 2331 N LEU A 349 9362 10182 8227 -596 -880 -107 N ATOM 2332 CA LEU A 349 48.351 38.724 62.771 1.00 81.84 C ANISOU 2332 CA LEU A 349 10420 11180 9494 -594 -880 -71 C ATOM 2333 C LEU A 349 47.226 38.222 61.876 1.00 87.59 C ANISOU 2333 C LEU A 349 11242 11694 10343 -594 -781 -1 C ATOM 2334 O LEU A 349 47.021 38.736 60.769 1.00 69.42 O ANISOU 2334 O LEU A 349 8910 9274 8191 -655 -755 -34 O ATOM 2335 CB LEU A 349 49.566 37.807 62.644 1.00 79.82 C ANISOU 2335 CB LEU A 349 10114 11037 9178 -469 -950 33 C ATOM 2336 CG LEU A 349 50.922 38.346 63.087 1.00 84.96 C ANISOU 2336 CG LEU A 349 10621 11902 9756 -473 -1063 -46 C ATOM 2337 CD1 LEU A 349 51.909 37.202 63.213 1.00 88.03 C ANISOU 2337 CD1 LEU A 349 10980 12412 10056 -311 -1126 86 C ATOM 2338 CD2 LEU A 349 51.415 39.374 62.087 1.00 91.51 C ANISOU 2338 CD2 LEU A 349 11341 12682 10747 -585 -1069 -153 C ATOM 2339 N LEU A 350 46.487 37.212 62.339 1.00 87.63 N ANISOU 2339 N LEU A 350 11358 11655 10284 -528 -721 99 N ATOM 2340 CA LEU A 350 45.420 36.642 61.527 1.00 80.35 C ANISOU 2340 CA LEU A 350 10513 10541 9476 -533 -627 152 C ATOM 2341 C LEU A 350 44.263 37.614 61.336 1.00 82.91 C ANISOU 2341 C LEU A 350 10845 10763 9895 -647 -572 46 C ATOM 2342 O LEU A 350 43.545 37.519 60.333 1.00 67.66 O ANISOU 2342 O LEU A 350 8929 8690 8090 -672 -521 54 O ATOM 2343 CB LEU A 350 44.923 35.341 62.154 1.00 82.52 C ANISOU 2343 CB LEU A 350 10901 10785 9669 -448 -564 279 C ATOM 2344 CG LEU A 350 45.853 34.142 61.975 1.00 83.00 C ANISOU 2344 CG LEU A 350 10971 10870 9697 -314 -591 414 C ATOM 2345 CD1 LEU A 350 45.299 32.920 62.685 1.00 75.60 C ANISOU 2345 CD1 LEU A 350 10156 9880 8688 -235 -512 549 C ATOM 2346 CD2 LEU A 350 46.067 33.857 60.497 1.00 82.55 C ANISOU 2346 CD2 LEU A 350 10877 10695 9792 -309 -580 417 C ATOM 2347 N ASN A 351 44.057 38.542 62.277 1.00 73.39 N ANISOU 2347 N ASN A 351 9623 9631 8629 -710 -580 -59 N ATOM 2348 CA ASN A 351 43.013 39.547 62.085 1.00 79.65 C ANISOU 2348 CA ASN A 351 10412 10321 9532 -807 -527 -166 C ATOM 2349 C ASN A 351 43.286 40.380 60.840 1.00 86.79 C ANISOU 2349 C ASN A 351 11240 11141 10595 -857 -551 -207 C ATOM 2350 O ASN A 351 42.359 40.730 60.099 1.00 77.24 O ANISOU 2350 O ASN A 351 10039 9798 9510 -894 -501 -222 O ATOM 2351 CB ASN A 351 42.902 40.450 63.314 1.00 79.91 C ANISOU 2351 CB ASN A 351 10431 10455 9478 -866 -532 -293 C ATOM 2352 CG ASN A 351 42.595 39.682 64.583 1.00 77.30 C ANISOU 2352 CG ASN A 351 10179 10227 8964 -817 -500 -245 C ATOM 2353 OD1 ASN A 351 42.978 40.093 65.679 1.00 84.12 O ANISOU 2353 OD1 ASN A 351 11026 11248 9687 -831 -536 -321 O ATOM 2354 ND2 ASN A 351 41.913 38.554 64.441 1.00 82.04 N ANISOU 2354 ND2 ASN A 351 10865 10745 9562 -764 -430 -121 N ATOM 2355 N VAL A 352 44.557 40.697 60.592 1.00 85.53 N ANISOU 2355 N VAL A 352 11002 11066 10430 -856 -626 -220 N ATOM 2356 CA VAL A 352 44.938 41.451 59.403 1.00 76.20 C ANISOU 2356 CA VAL A 352 9750 9813 9389 -904 -639 -239 C ATOM 2357 C VAL A 352 45.077 40.529 58.199 1.00 80.61 C ANISOU 2357 C VAL A 352 10321 10315 9992 -841 -631 -125 C ATOM 2358 O VAL A 352 44.730 40.905 57.072 1.00 80.15 O ANISOU 2358 O VAL A 352 10248 10156 10048 -869 -607 -114 O ATOM 2359 CB VAL A 352 46.239 42.228 59.679 1.00 69.20 C ANISOU 2359 CB VAL A 352 8762 9044 8485 -948 -709 -317 C ATOM 2360 CG1 VAL A 352 46.684 42.994 58.445 1.00 71.64 C ANISOU 2360 CG1 VAL A 352 9002 9276 8941 -1003 -707 -320 C ATOM 2361 CG2 VAL A 352 46.052 43.167 60.856 1.00 75.33 C ANISOU 2361 CG2 VAL A 352 9524 9877 9221 -1021 -712 -459 C ATOM 2362 N PHE A 353 45.580 39.309 58.416 1.00 78.15 N ANISOU 2362 N PHE A 353 10037 10067 9588 -749 -648 -39 N ATOM 2363 CA PHE A 353 45.846 38.409 57.298 1.00 77.91 C ANISOU 2363 CA PHE A 353 10011 9989 9602 -687 -638 47 C ATOM 2364 C PHE A 353 44.564 37.929 56.629 1.00 73.62 C ANISOU 2364 C PHE A 353 9537 9305 9129 -691 -565 74 C ATOM 2365 O PHE A 353 44.567 37.643 55.426 1.00 76.60 O ANISOU 2365 O PHE A 353 9902 9629 9575 -680 -552 102 O ATOM 2366 CB PHE A 353 46.681 37.220 57.769 1.00 85.33 C ANISOU 2366 CB PHE A 353 10964 11016 10441 -576 -666 130 C ATOM 2367 CG PHE A 353 48.120 37.563 58.052 1.00 88.08 C ANISOU 2367 CG PHE A 353 11211 11520 10737 -557 -750 109 C ATOM 2368 CD1 PHE A 353 48.707 38.679 57.479 1.00 88.80 C ANISOU 2368 CD1 PHE A 353 11203 11635 10901 -640 -778 34 C ATOM 2369 CD2 PHE A 353 48.886 36.766 58.889 1.00 77.71 C ANISOU 2369 CD2 PHE A 353 9894 10329 9304 -455 -797 170 C ATOM 2370 CE1 PHE A 353 50.031 38.994 57.736 1.00 90.46 C ANISOU 2370 CE1 PHE A 353 11303 11994 11074 -636 -850 0 C ATOM 2371 CE2 PHE A 353 50.208 37.077 59.151 1.00 77.33 C ANISOU 2371 CE2 PHE A 353 9731 10444 9206 -435 -882 141 C ATOM 2372 CZ PHE A 353 50.781 38.192 58.574 1.00 80.03 C ANISOU 2372 CZ PHE A 353 9965 10813 9629 -533 -908 46 C ATOM 2373 N VAL A 354 43.462 37.838 57.375 1.00 70.42 N ANISOU 2373 N VAL A 354 9199 8854 8705 -710 -516 57 N ATOM 2374 CA VAL A 354 42.215 37.391 56.765 1.00 74.34 C ANISOU 2374 CA VAL A 354 9743 9228 9275 -723 -448 67 C ATOM 2375 C VAL A 354 41.696 38.431 55.776 1.00 86.46 C ANISOU 2375 C VAL A 354 11227 10703 10922 -786 -451 15 C ATOM 2376 O VAL A 354 41.106 38.080 54.746 1.00 63.78 O ANISOU 2376 O VAL A 354 8356 7763 8113 -783 -427 31 O ATOM 2377 CB VAL A 354 41.171 37.053 57.849 1.00 67.35 C ANISOU 2377 CB VAL A 354 8930 8316 8344 -735 -384 59 C ATOM 2378 CG1 VAL A 354 40.714 38.307 58.587 1.00 65.62 C ANISOU 2378 CG1 VAL A 354 8687 8119 8125 -803 -384 -36 C ATOM 2379 CG2 VAL A 354 39.990 36.312 57.238 1.00 65.39 C ANISOU 2379 CG2 VAL A 354 8722 7951 8172 -744 -310 72 C ATOM 2380 N TRP A 355 41.924 39.718 56.045 1.00 78.81 N ANISOU 2380 N TRP A 355 10210 9756 9978 -840 -479 -46 N ATOM 2381 CA TRP A 355 41.466 40.749 55.123 1.00 79.53 C ANISOU 2381 CA TRP A 355 10258 9777 10183 -886 -476 -72 C ATOM 2382 C TRP A 355 42.367 40.886 53.905 1.00 88.31 C ANISOU 2382 C TRP A 355 11318 10907 11328 -877 -509 -24 C ATOM 2383 O TRP A 355 41.903 41.352 52.860 1.00 89.31 O ANISOU 2383 O TRP A 355 11424 10979 11531 -891 -501 -5 O ATOM 2384 CB TRP A 355 41.333 42.085 55.856 1.00 64.58 C ANISOU 2384 CB TRP A 355 8337 7872 8329 -948 -475 -158 C ATOM 2385 CG TRP A 355 40.023 42.183 56.568 1.00 87.07 C ANISOU 2385 CG TRP A 355 11224 10667 11191 -964 -421 -211 C ATOM 2386 CD1 TRP A 355 39.774 41.890 57.879 1.00 73.48 C ANISOU 2386 CD1 TRP A 355 9544 8995 9380 -966 -395 -254 C ATOM 2387 CD2 TRP A 355 38.769 42.567 55.996 1.00 79.65 C ANISOU 2387 CD2 TRP A 355 10277 9630 10354 -972 -383 -222 C ATOM 2388 NE1 TRP A 355 38.442 42.082 58.159 1.00 80.35 N ANISOU 2388 NE1 TRP A 355 10433 9798 10298 -985 -333 -300 N ATOM 2389 CE2 TRP A 355 37.804 42.499 57.020 1.00 83.75 C ANISOU 2389 CE2 TRP A 355 10828 10138 10854 -986 -329 -284 C ATOM 2390 CE3 TRP A 355 38.370 42.972 54.718 1.00 70.41 C ANISOU 2390 CE3 TRP A 355 9072 8397 9284 -964 -391 -183 C ATOM 2391 CZ2 TRP A 355 36.465 42.819 56.806 1.00 84.98 C ANISOU 2391 CZ2 TRP A 355 10971 10216 11101 -992 -283 -317 C ATOM 2392 CZ3 TRP A 355 37.042 43.290 54.507 1.00 77.60 C ANISOU 2392 CZ3 TRP A 355 9971 9238 10276 -962 -357 -207 C ATOM 2393 CH2 TRP A 355 36.105 43.212 55.546 1.00 74.86 C ANISOU 2393 CH2 TRP A 355 9645 8875 9922 -977 -303 -279 C ATOM 2394 N ILE A 356 43.635 40.484 54.007 1.00 85.84 N ANISOU 2394 N ILE A 356 10979 10681 10954 -849 -546 1 N ATOM 2395 CA ILE A 356 44.460 40.359 52.810 1.00 81.51 C ANISOU 2395 CA ILE A 356 10384 10160 10427 -832 -562 49 C ATOM 2396 C ILE A 356 43.876 39.299 51.884 1.00 77.20 C ANISOU 2396 C ILE A 356 9875 9575 9881 -783 -534 93 C ATOM 2397 O ILE A 356 43.820 39.481 50.662 1.00 68.87 O ANISOU 2397 O ILE A 356 8795 8510 8864 -789 -529 117 O ATOM 2398 CB ILE A 356 45.918 40.046 53.195 1.00 72.33 C ANISOU 2398 CB ILE A 356 9173 9109 9201 -803 -603 57 C ATOM 2399 CG1 ILE A 356 46.454 41.131 54.129 1.00 70.94 C ANISOU 2399 CG1 ILE A 356 8947 8983 9023 -867 -635 -14 C ATOM 2400 CG2 ILE A 356 46.791 39.941 51.952 1.00 65.02 C ANISOU 2400 CG2 ILE A 356 8190 8217 8299 -788 -607 99 C ATOM 2401 CD1 ILE A 356 47.813 40.827 54.715 1.00 66.10 C ANISOU 2401 CD1 ILE A 356 8272 8508 8335 -837 -689 -23 C ATOM 2402 N GLY A 357 43.409 38.186 52.452 1.00 63.51 N ANISOU 2402 N GLY A 357 8204 7822 8104 -740 -509 100 N ATOM 2403 CA GLY A 357 42.727 37.189 51.643 1.00 66.92 C ANISOU 2403 CA GLY A 357 8670 8202 8554 -711 -472 114 C ATOM 2404 C GLY A 357 41.381 37.669 51.131 1.00 75.98 C ANISOU 2404 C GLY A 357 9819 9286 9764 -756 -451 83 C ATOM 2405 O GLY A 357 40.994 37.366 49.999 1.00 81.54 O ANISOU 2405 O GLY A 357 10509 9981 10491 -750 -445 83 O ATOM 2406 N TYR A 358 40.652 38.431 51.951 1.00 72.77 N ANISOU 2406 N TYR A 358 9421 8847 9381 -795 -442 49 N ATOM 2407 CA TYR A 358 39.332 38.906 51.543 1.00 75.46 C ANISOU 2407 CA TYR A 358 9750 9132 9790 -825 -424 18 C ATOM 2408 C TYR A 358 39.427 39.879 50.375 1.00 86.79 C ANISOU 2408 C TYR A 358 11128 10574 11272 -834 -457 43 C ATOM 2409 O TYR A 358 38.637 39.806 49.426 1.00 89.44 O ANISOU 2409 O TYR A 358 11445 10902 11636 -827 -458 46 O ATOM 2410 CB TYR A 358 38.615 39.555 52.726 1.00 67.50 C ANISOU 2410 CB TYR A 358 8757 8089 8801 -859 -399 -31 C ATOM 2411 CG TYR A 358 37.950 38.547 53.628 1.00 78.23 C ANISOU 2411 CG TYR A 358 10174 9427 10123 -855 -344 -48 C ATOM 2412 CD1 TYR A 358 37.673 37.264 53.174 1.00 66.87 C ANISOU 2412 CD1 TYR A 358 8765 7966 8678 -833 -312 -29 C ATOM 2413 CD2 TYR A 358 37.600 38.872 54.933 1.00 84.64 C ANISOU 2413 CD2 TYR A 358 11012 10238 10908 -877 -312 -86 C ATOM 2414 CE1 TYR A 358 37.066 36.336 53.990 1.00 70.56 C ANISOU 2414 CE1 TYR A 358 9290 8395 9125 -836 -245 -33 C ATOM 2415 CE2 TYR A 358 36.989 37.944 55.759 1.00 80.05 C ANISOU 2415 CE2 TYR A 358 10490 9641 10286 -876 -247 -86 C ATOM 2416 CZ TYR A 358 36.726 36.677 55.277 1.00 74.26 C ANISOU 2416 CZ TYR A 358 9788 8869 9559 -857 -211 -51 C ATOM 2417 OH TYR A 358 36.122 35.736 56.074 1.00 87.94 O ANISOU 2417 OH TYR A 358 11582 10565 11265 -863 -131 -39 O ATOM 2418 N VAL A 359 40.389 40.804 50.429 1.00 85.35 N ANISOU 2418 N VAL A 359 10917 10414 11100 -852 -481 63 N ATOM 2419 CA VAL A 359 40.552 41.801 49.370 1.00 74.47 C ANISOU 2419 CA VAL A 359 9493 9031 9771 -864 -498 108 C ATOM 2420 C VAL A 359 40.720 41.142 48.005 1.00 75.05 C ANISOU 2420 C VAL A 359 9553 9159 9804 -831 -507 155 C ATOM 2421 O VAL A 359 40.373 41.730 46.971 1.00 69.39 O ANISOU 2421 O VAL A 359 8808 8447 9110 -826 -517 200 O ATOM 2422 CB VAL A 359 41.735 42.732 49.718 1.00 78.42 C ANISOU 2422 CB VAL A 359 9962 9542 10291 -902 -508 114 C ATOM 2423 CG1 VAL A 359 42.215 43.514 48.510 1.00 75.84 C ANISOU 2423 CG1 VAL A 359 9594 9220 10002 -913 -510 186 C ATOM 2424 CG2 VAL A 359 41.325 43.687 50.832 1.00 63.71 C ANISOU 2424 CG2 VAL A 359 8102 7615 8488 -945 -495 50 C ATOM 2425 N ASN A 360 41.209 39.900 47.977 1.00 85.72 N ANISOU 2425 N ASN A 360 10924 10553 11092 -801 -501 143 N ATOM 2426 CA ASN A 360 41.345 39.179 46.714 1.00 80.08 C ANISOU 2426 CA ASN A 360 10197 9894 10336 -771 -502 159 C ATOM 2427 C ASN A 360 40.011 39.035 45.986 1.00 73.19 C ANISOU 2427 C ASN A 360 9319 9014 9477 -768 -504 138 C ATOM 2428 O ASN A 360 39.986 38.917 44.755 1.00 81.83 O ANISOU 2428 O ASN A 360 10385 10172 10533 -753 -516 155 O ATOM 2429 CB ASN A 360 41.959 37.803 46.961 1.00 77.53 C ANISOU 2429 CB ASN A 360 9901 9590 9967 -734 -483 135 C ATOM 2430 CG ASN A 360 42.179 37.035 45.686 1.00 85.77 C ANISOU 2430 CG ASN A 360 10929 10688 10971 -706 -474 127 C ATOM 2431 OD1 ASN A 360 41.303 36.296 45.235 1.00 91.19 O ANISOU 2431 OD1 ASN A 360 11630 11360 11657 -702 -458 78 O ATOM 2432 ND2 ASN A 360 43.347 37.215 45.082 1.00 79.50 N ANISOU 2432 ND2 ASN A 360 10097 9965 10144 -692 -478 162 N ATOM 2433 N SER A 361 38.894 39.046 46.718 1.00 70.17 N ANISOU 2433 N SER A 361 8954 8570 9139 -783 -492 95 N ATOM 2434 CA SER A 361 37.590 38.992 46.065 1.00 76.43 C ANISOU 2434 CA SER A 361 9719 9368 9953 -782 -501 65 C ATOM 2435 C SER A 361 37.305 40.235 45.233 1.00 82.46 C ANISOU 2435 C SER A 361 10436 10158 10738 -770 -538 129 C ATOM 2436 O SER A 361 36.372 40.220 44.423 1.00 97.22 O ANISOU 2436 O SER A 361 12267 12071 12603 -752 -562 120 O ATOM 2437 CB SER A 361 36.479 38.802 47.099 1.00 82.53 C ANISOU 2437 CB SER A 361 10508 10071 10778 -804 -470 3 C ATOM 2438 OG SER A 361 36.588 37.544 47.737 1.00 93.04 O ANISOU 2438 OG SER A 361 11889 11373 12089 -811 -425 -39 O ATOM 2439 N GLY A 362 38.074 41.305 45.413 1.00 73.18 N ANISOU 2439 N GLY A 362 9259 8958 9590 -777 -541 193 N ATOM 2440 CA GLY A 362 37.901 42.494 44.603 1.00 82.85 C ANISOU 2440 CA GLY A 362 10449 10187 10845 -761 -562 278 C ATOM 2441 C GLY A 362 38.965 42.648 43.535 1.00 92.56 C ANISOU 2441 C GLY A 362 11666 11493 12011 -753 -567 360 C ATOM 2442 O GLY A 362 38.818 43.463 42.619 1.00 93.83 O ANISOU 2442 O GLY A 362 11802 11677 12170 -731 -580 452 O ATOM 2443 N ILE A 363 40.034 41.853 43.629 1.00 88.90 N ANISOU 2443 N ILE A 363 11216 11071 11491 -766 -551 334 N ATOM 2444 CA ILE A 363 41.184 42.051 42.751 1.00100.02 C ANISOU 2444 CA ILE A 363 12605 12552 12847 -767 -540 403 C ATOM 2445 C ILE A 363 40.897 41.538 41.343 1.00 98.55 C ANISOU 2445 C ILE A 363 12400 12481 12563 -731 -555 422 C ATOM 2446 O ILE A 363 41.302 42.161 40.353 1.00104.15 O ANISOU 2446 O ILE A 363 13089 13254 13231 -723 -550 516 O ATOM 2447 CB ILE A 363 42.434 41.389 43.359 1.00104.33 C ANISOU 2447 CB ILE A 363 13155 13113 13371 -781 -520 362 C ATOM 2448 CG1 ILE A 363 42.814 42.089 44.663 1.00100.41 C ANISOU 2448 CG1 ILE A 363 12664 12536 12951 -821 -515 346 C ATOM 2449 CG2 ILE A 363 43.604 41.441 42.385 1.00 85.70 C ANISOU 2449 CG2 ILE A 363 10763 10846 10955 -781 -500 418 C ATOM 2450 CD1 ILE A 363 43.173 43.550 44.477 1.00 80.93 C ANISOU 2450 CD1 ILE A 363 10170 10025 10553 -862 -501 417 C ATOM 2451 N ASN A 364 40.197 40.408 41.226 1.00 83.97 N ANISOU 2451 N ASN A 364 10559 10668 10677 -714 -567 331 N ATOM 2452 CA ASN A 364 39.977 39.778 39.924 1.00 95.44 C ANISOU 2452 CA ASN A 364 11988 12247 12026 -688 -580 312 C ATOM 2453 C ASN A 364 39.367 40.707 38.875 1.00 85.29 C ANISOU 2453 C ASN A 364 10670 11038 10698 -660 -617 407 C ATOM 2454 O ASN A 364 39.894 40.754 37.755 1.00 90.43 O ANISOU 2454 O ASN A 364 11303 11808 11246 -644 -613 461 O ATOM 2455 CB ASN A 364 39.117 38.519 40.101 1.00112.99 C ANISOU 2455 CB ASN A 364 14217 14466 14246 -689 -583 179 C ATOM 2456 CG ASN A 364 39.827 37.436 40.879 1.00104.64 C ANISOU 2456 CG ASN A 364 13199 13349 13212 -698 -539 107 C ATOM 2457 OD1 ASN A 364 40.695 36.746 40.347 1.00 97.75 O ANISOU 2457 OD1 ASN A 364 12325 12532 12283 -683 -514 83 O ATOM 2458 ND2 ASN A 364 39.459 37.277 42.146 1.00102.88 N ANISOU 2458 ND2 ASN A 364 13009 13013 13067 -715 -524 77 N ATOM 2459 N PRO A 365 38.284 41.448 39.148 1.00 82.51 N ANISOU 2459 N PRO A 365 10305 10633 10412 -645 -649 437 N ATOM 2460 CA PRO A 365 37.774 42.363 38.110 1.00 90.80 C ANISOU 2460 CA PRO A 365 11322 11761 11418 -598 -687 554 C ATOM 2461 C PRO A 365 38.783 43.417 37.689 1.00 86.15 C ANISOU 2461 C PRO A 365 10747 11162 10825 -599 -653 708 C ATOM 2462 O PRO A 365 38.759 43.856 36.532 1.00 84.80 O ANISOU 2462 O PRO A 365 10557 11099 10561 -559 -668 818 O ATOM 2463 CB PRO A 365 36.533 42.990 38.766 1.00 98.26 C ANISOU 2463 CB PRO A 365 12249 12613 12472 -577 -716 552 C ATOM 2464 CG PRO A 365 36.691 42.748 40.222 1.00100.59 C ANISOU 2464 CG PRO A 365 12579 12766 12873 -627 -677 465 C ATOM 2465 CD PRO A 365 37.423 41.455 40.342 1.00 86.94 C ANISOU 2465 CD PRO A 365 10876 11076 11083 -660 -651 369 C ATOM 2466 N LEU A 366 39.677 43.832 38.589 1.00 84.27 N ANISOU 2466 N LEU A 366 10534 10803 10679 -647 -605 718 N ATOM 2467 CA LEU A 366 40.744 44.746 38.198 1.00 80.45 C ANISOU 2467 CA LEU A 366 10056 10308 10205 -668 -557 845 C ATOM 2468 C LEU A 366 41.709 44.079 37.226 1.00 91.59 C ANISOU 2468 C LEU A 366 11454 11867 11479 -672 -532 853 C ATOM 2469 O LEU A 366 42.147 44.700 36.251 1.00 90.29 O ANISOU 2469 O LEU A 366 11282 11771 11253 -663 -505 983 O ATOM 2470 CB LEU A 366 41.496 45.240 39.433 1.00 76.79 C ANISOU 2470 CB LEU A 366 9606 9701 9870 -731 -516 817 C ATOM 2471 CG LEU A 366 42.676 46.171 39.144 1.00 92.86 C ANISOU 2471 CG LEU A 366 11633 11710 11940 -776 -456 925 C ATOM 2472 CD1 LEU A 366 42.178 47.578 38.840 1.00102.80 C ANISOU 2472 CD1 LEU A 366 12901 12871 13287 -761 -438 1067 C ATOM 2473 CD2 LEU A 366 43.674 46.176 40.293 1.00 78.28 C ANISOU 2473 CD2 LEU A 366 9779 9789 10174 -847 -426 842 C ATOM 2474 N VAL A 367 42.045 42.811 37.475 1.00 95.05 N ANISOU 2474 N VAL A 367 11892 12352 11872 -682 -531 719 N ATOM 2475 CA VAL A 367 42.994 42.106 36.619 1.00 98.57 C ANISOU 2475 CA VAL A 367 12321 12931 12201 -681 -498 702 C ATOM 2476 C VAL A 367 42.443 41.966 35.206 1.00102.15 C ANISOU 2476 C VAL A 367 12758 13549 12505 -637 -522 739 C ATOM 2477 O VAL A 367 43.169 42.159 34.222 1.00105.98 O ANISOU 2477 O VAL A 367 13229 14150 12888 -635 -484 816 O ATOM 2478 CB VAL A 367 43.343 40.737 37.228 1.00 93.67 C ANISOU 2478 CB VAL A 367 11707 12303 11582 -685 -490 547 C ATOM 2479 CG1 VAL A 367 44.359 40.017 36.354 1.00 95.74 C ANISOU 2479 CG1 VAL A 367 11945 12694 11738 -676 -447 518 C ATOM 2480 CG2 VAL A 367 43.865 40.910 38.647 1.00 72.54 C ANISOU 2480 CG2 VAL A 367 9043 9491 9028 -718 -477 522 C ATOM 2481 N TYR A 368 41.155 41.624 35.081 1.00 96.49 N ANISOU 2481 N TYR A 368 12035 12861 11766 -605 -584 680 N ATOM 2482 CA TYR A 368 40.545 41.508 33.759 1.00 87.95 C ANISOU 2482 CA TYR A 368 10926 11962 10530 -560 -624 704 C ATOM 2483 C TYR A 368 40.654 42.817 32.990 1.00 92.36 C ANISOU 2483 C TYR A 368 11483 12565 11042 -529 -618 914 C ATOM 2484 O TYR A 368 40.939 42.819 31.786 1.00 89.87 O ANISOU 2484 O TYR A 368 11155 12425 10567 -504 -609 979 O ATOM 2485 CB TYR A 368 39.075 41.102 33.879 1.00 86.40 C ANISOU 2485 CB TYR A 368 10705 11781 10344 -535 -699 609 C ATOM 2486 CG TYR A 368 38.804 39.881 34.730 1.00 98.10 C ANISOU 2486 CG TYR A 368 12193 13185 11894 -571 -693 417 C ATOM 2487 CD1 TYR A 368 39.757 38.879 34.880 1.00100.57 C ANISOU 2487 CD1 TYR A 368 12527 13491 12195 -599 -638 319 C ATOM 2488 CD2 TYR A 368 37.583 39.729 35.380 1.00 97.28 C ANISOU 2488 CD2 TYR A 368 12075 13012 11875 -572 -735 343 C ATOM 2489 CE1 TYR A 368 39.503 37.764 35.661 1.00101.23 C ANISOU 2489 CE1 TYR A 368 12626 13486 12351 -624 -623 166 C ATOM 2490 CE2 TYR A 368 37.321 38.620 36.160 1.00 92.17 C ANISOU 2490 CE2 TYR A 368 11441 12285 11295 -611 -714 184 C ATOM 2491 CZ TYR A 368 38.283 37.639 36.298 1.00 94.79 C ANISOU 2491 CZ TYR A 368 11804 12598 11616 -635 -657 104 C ATOM 2492 OH TYR A 368 38.023 36.532 37.076 1.00 93.44 O ANISOU 2492 OH TYR A 368 11654 12330 11518 -665 -626 -33 O ATOM 2493 N THR A 369 40.426 43.941 33.675 1.00 87.57 N ANISOU 2493 N THR A 369 10894 11800 10578 -529 -615 1024 N ATOM 2494 CA THR A 369 40.453 45.245 33.021 1.00 85.38 C ANISOU 2494 CA THR A 369 10626 11525 10291 -494 -599 1239 C ATOM 2495 C THR A 369 41.829 45.547 32.442 1.00 91.82 C ANISOU 2495 C THR A 369 11452 12386 11048 -534 -510 1339 C ATOM 2496 O THR A 369 41.941 46.081 31.332 1.00 93.96 O ANISOU 2496 O THR A 369 11724 12775 11201 -498 -492 1497 O ATOM 2497 CB THR A 369 40.050 46.330 34.018 1.00 86.85 C ANISOU 2497 CB THR A 369 10830 11493 10676 -497 -593 1306 C ATOM 2498 OG1 THR A 369 38.936 45.876 34.796 1.00 95.40 O ANISOU 2498 OG1 THR A 369 11897 12521 11829 -480 -656 1173 O ATOM 2499 CG2 THR A 369 39.661 47.601 33.293 1.00105.82 C ANISOU 2499 CG2 THR A 369 13240 13887 13081 -433 -592 1528 C ATOM 2500 N LEU A 370 42.887 45.208 33.181 1.00 93.32 N ANISOU 2500 N LEU A 370 11645 12497 11317 -605 -453 1253 N ATOM 2501 CA LEU A 370 44.240 45.537 32.745 1.00 92.16 C ANISOU 2501 CA LEU A 370 11491 12384 11141 -654 -360 1336 C ATOM 2502 C LEU A 370 44.665 44.703 31.544 1.00 95.77 C ANISOU 2502 C LEU A 370 11928 13069 11392 -633 -342 1308 C ATOM 2503 O LEU A 370 45.422 45.179 30.691 1.00106.46 O ANISOU 2503 O LEU A 370 13277 14512 12664 -646 -270 1435 O ATOM 2504 CB LEU A 370 45.225 45.334 33.896 1.00 89.23 C ANISOU 2504 CB LEU A 370 11109 11890 10905 -727 -318 1232 C ATOM 2505 CG LEU A 370 45.179 46.332 35.052 1.00 87.78 C ANISOU 2505 CG LEU A 370 10938 11493 10920 -772 -309 1261 C ATOM 2506 CD1 LEU A 370 45.963 45.801 36.236 1.00 79.22 C ANISOU 2506 CD1 LEU A 370 9835 10341 9926 -828 -300 1115 C ATOM 2507 CD2 LEU A 370 45.739 47.668 34.607 1.00102.82 C ANISOU 2507 CD2 LEU A 370 12847 13336 12884 -810 -229 1445 C ATOM 2508 N PHE A 371 44.189 43.462 31.456 1.00 93.14 N ANISOU 2508 N PHE A 371 11581 12830 10977 -606 -395 1136 N ATOM 2509 CA PHE A 371 44.719 42.501 30.499 1.00 92.72 C ANISOU 2509 CA PHE A 371 11504 12974 10751 -597 -366 1053 C ATOM 2510 C PHE A 371 43.720 42.091 29.423 1.00103.90 C ANISOU 2510 C PHE A 371 12909 14584 11983 -538 -432 1027 C ATOM 2511 O PHE A 371 43.999 41.156 28.665 1.00120.11 O ANISOU 2511 O PHE A 371 14940 16804 13891 -532 -416 912 O ATOM 2512 CB PHE A 371 45.222 41.260 31.237 1.00 83.66 C ANISOU 2512 CB PHE A 371 10344 11778 9664 -620 -354 849 C ATOM 2513 CG PHE A 371 46.456 41.501 32.055 1.00 94.15 C ANISOU 2513 CG PHE A 371 11662 12992 11120 -671 -287 862 C ATOM 2514 CD1 PHE A 371 47.709 41.214 31.539 1.00103.91 C ANISOU 2514 CD1 PHE A 371 12860 14325 12294 -689 -206 853 C ATOM 2515 CD2 PHE A 371 46.364 42.017 33.337 1.00 96.83 C ANISOU 2515 CD2 PHE A 371 12017 13140 11635 -701 -307 872 C ATOM 2516 CE1 PHE A 371 48.849 41.435 32.288 1.00 90.13 C ANISOU 2516 CE1 PHE A 371 11085 12494 10666 -735 -152 855 C ATOM 2517 CE2 PHE A 371 47.501 42.242 34.090 1.00 91.29 C ANISOU 2517 CE2 PHE A 371 11291 12357 11038 -749 -257 869 C ATOM 2518 CZ PHE A 371 48.744 41.951 33.564 1.00 86.93 C ANISOU 2518 CZ PHE A 371 10692 11908 10429 -766 -183 862 C ATOM 2519 N ASN A 372 42.574 42.759 29.322 1.00 75.48 N ANISOU 2519 N ASN A 372 9316 10977 8386 -492 -507 1120 N ATOM 2520 CA ASN A 372 41.595 42.375 28.312 1.00 97.60 C ANISOU 2520 CA ASN A 372 12090 13989 11005 -433 -585 1086 C ATOM 2521 C ASN A 372 40.784 43.591 27.900 1.00 99.01 C ANISOU 2521 C ASN A 372 12273 14188 11160 -365 -636 1301 C ATOM 2522 O ASN A 372 40.112 44.203 28.737 1.00 99.33 O ANISOU 2522 O ASN A 372 12322 14053 11366 -351 -673 1345 O ATOM 2523 CB ASN A 372 40.681 41.265 28.830 1.00108.22 C ANISOU 2523 CB ASN A 372 13410 15315 12393 -438 -655 855 C ATOM 2524 CG ASN A 372 39.917 40.583 27.718 1.00111.10 C ANISOU 2524 CG ASN A 372 13728 15930 12554 -401 -723 753 C ATOM 2525 OD1 ASN A 372 38.850 41.038 27.314 1.00 94.57 O ANISOU 2525 OD1 ASN A 372 11605 13928 10400 -346 -810 817 O ATOM 2526 ND2 ASN A 372 40.464 39.484 27.214 1.00122.10 N ANISOU 2526 ND2 ASN A 372 15108 17442 13842 -430 -683 585 N ATOM 2527 N LYS A 373 40.836 43.925 26.607 1.00101.88 N ANISOU 2527 N LYS A 373 12630 14769 11313 -316 -635 1435 N ATOM 2528 CA LYS A 373 40.131 45.098 26.104 1.00104.80 C ANISOU 2528 CA LYS A 373 13006 15170 11643 -232 -680 1673 C ATOM 2529 C LYS A 373 38.616 44.935 26.147 1.00111.38 C ANISOU 2529 C LYS A 373 13791 16062 12466 -161 -815 1607 C ATOM 2530 O LYS A 373 37.902 45.943 26.156 1.00107.18 O ANISOU 2530 O LYS A 373 13261 15475 11989 -84 -860 1786 O ATOM 2531 CB LYS A 373 40.579 45.407 24.673 1.00107.14 C ANISOU 2531 CB LYS A 373 13308 15714 11685 -192 -643 1839 C ATOM 2532 CG LYS A 373 40.475 44.219 23.726 1.00124.23 C ANISOU 2532 CG LYS A 373 15427 18174 13599 -186 -683 1654 C ATOM 2533 CD LYS A 373 40.778 44.604 22.280 1.00138.72 C ANISOU 2533 CD LYS A 373 17268 20286 15153 -133 -655 1831 C ATOM 2534 CE LYS A 373 39.612 45.343 21.627 1.00140.37 C ANISOU 2534 CE LYS A 373 17459 20636 15239 -12 -768 2015 C ATOM 2535 NZ LYS A 373 38.355 44.536 21.614 1.00126.65 N ANISOU 2535 NZ LYS A 373 15647 19030 13445 25 -917 1801 N ATOM 2536 N ILE A 374 38.109 43.701 26.171 1.00109.98 N ANISOU 2536 N ILE A 374 13566 15988 12234 -184 -876 1352 N ATOM 2537 CA ILE A 374 36.662 43.500 26.191 1.00111.15 C ANISOU 2537 CA ILE A 374 13650 16208 12375 -128 -1002 1268 C ATOM 2538 C ILE A 374 36.091 43.883 27.552 1.00106.75 C ANISOU 2538 C ILE A 374 13098 15375 12086 -140 -1013 1250 C ATOM 2539 O ILE A 374 35.094 44.609 27.643 1.00 80.40 O ANISOU 2539 O ILE A 374 9729 12015 8802 -63 -1085 1350 O ATOM 2540 CB ILE A 374 36.313 42.049 25.818 1.00114.86 C ANISOU 2540 CB ILE A 374 14061 16856 12722 -168 -1047 983 C ATOM 2541 CG1 ILE A 374 37.131 41.597 24.606 1.00113.80 C ANISOU 2541 CG1 ILE A 374 13932 16969 12340 -176 -1004 967 C ATOM 2542 CG2 ILE A 374 34.823 41.918 25.539 1.00111.46 C ANISOU 2542 CG2 ILE A 374 13542 16569 12237 -109 -1182 910 C ATOM 2543 CD1 ILE A 374 37.024 40.114 24.317 1.00111.33 C ANISOU 2543 CD1 ILE A 374 13573 16789 11938 -233 -1016 660 C ATOM 2544 N TYR A 375 36.714 43.397 28.629 1.00104.05 N ANISOU 2544 N TYR A 375 12794 14830 11908 -229 -942 1123 N ATOM 2545 CA TYR A 375 36.284 43.781 29.971 1.00107.24 C ANISOU 2545 CA TYR A 375 13212 14981 12553 -247 -939 1105 C ATOM 2546 C TYR A 375 36.507 45.267 30.215 1.00107.36 C ANISOU 2546 C TYR A 375 13267 14841 12682 -209 -902 1347 C ATOM 2547 O TYR A 375 35.622 45.959 30.732 1.00 93.35 O ANISOU 2547 O TYR A 375 11477 12956 11038 -160 -942 1402 O ATOM 2548 CB TYR A 375 37.027 42.958 31.022 1.00107.31 C ANISOU 2548 CB TYR A 375 13257 14831 12684 -344 -869 938 C ATOM 2549 CG TYR A 375 36.523 41.546 31.180 1.00 99.54 C ANISOU 2549 CG TYR A 375 12238 13906 11676 -382 -898 690 C ATOM 2550 CD1 TYR A 375 35.400 41.272 31.952 1.00 80.52 C ANISOU 2550 CD1 TYR A 375 9796 11414 9383 -388 -945 578 C ATOM 2551 CD2 TYR A 375 37.175 40.484 30.566 1.00104.41 C ANISOU 2551 CD2 TYR A 375 12854 14649 12167 -417 -866 563 C ATOM 2552 CE1 TYR A 375 34.938 39.980 32.106 1.00 91.08 C ANISOU 2552 CE1 TYR A 375 11104 12786 10717 -435 -956 354 C ATOM 2553 CE2 TYR A 375 36.722 39.187 30.713 1.00109.91 C ANISOU 2553 CE2 TYR A 375 13523 15372 12865 -457 -879 331 C ATOM 2554 CZ TYR A 375 35.602 38.940 31.484 1.00106.67 C ANISOU 2554 CZ TYR A 375 13084 14869 12577 -471 -922 232 C ATOM 2555 OH TYR A 375 35.146 37.650 31.633 1.00105.78 O ANISOU 2555 OH TYR A 375 12945 14764 12481 -522 -919 5 O ATOM 2556 N ARG A 376 37.692 45.770 29.856 1.00105.29 N ANISOU 2556 N ARG A 376 13055 14563 12388 -235 -815 1485 N ATOM 2557 CA ARG A 376 38.004 47.179 30.078 1.00 90.25 C ANISOU 2557 CA ARG A 376 11192 12487 10610 -216 -758 1708 C ATOM 2558 C ARG A 376 37.023 48.085 29.345 1.00 94.66 C ANISOU 2558 C ARG A 376 11730 13118 11117 -93 -824 1905 C ATOM 2559 O ARG A 376 36.571 49.097 29.895 1.00 85.85 O ANISOU 2559 O ARG A 376 10628 11816 10176 -52 -819 2018 O ATOM 2560 CB ARG A 376 39.442 47.470 29.642 1.00 84.05 C ANISOU 2560 CB ARG A 376 10449 11709 9777 -274 -647 1817 C ATOM 2561 CG ARG A 376 39.872 48.917 29.843 1.00 90.75 C ANISOU 2561 CG ARG A 376 11342 12365 10773 -276 -567 2041 C ATOM 2562 CD ARG A 376 41.378 49.104 29.674 1.00102.27 C ANISOU 2562 CD ARG A 376 12829 13800 12229 -366 -443 2099 C ATOM 2563 NE ARG A 376 41.844 48.782 28.327 1.00111.34 N ANISOU 2563 NE ARG A 376 13972 15198 13133 -345 -418 2180 N ATOM 2564 CZ ARG A 376 42.549 47.698 28.019 1.00113.77 C ANISOU 2564 CZ ARG A 376 14257 15659 13310 -393 -397 2028 C ATOM 2565 NH1 ARG A 376 42.879 46.827 28.965 1.00 91.24 N ANISOU 2565 NH1 ARG A 376 11388 12725 10554 -458 -400 1805 N ATOM 2566 NH2 ARG A 376 42.930 47.487 26.765 1.00125.47 N ANISOU 2566 NH2 ARG A 376 15735 17377 14563 -370 -367 2102 N ATOM 2567 N ARG A 377 36.667 47.730 28.108 1.00 97.34 N ANISOU 2567 N ARG A 377 12034 13733 11217 -27 -888 1942 N ATOM 2568 CA ARG A 377 35.745 48.559 27.338 1.00102.65 C ANISOU 2568 CA ARG A 377 12680 14510 11813 109 -963 2145 C ATOM 2569 C ARG A 377 34.331 48.481 27.901 1.00 90.21 C ANISOU 2569 C ARG A 377 11034 12902 10340 171 -1072 2043 C ATOM 2570 O ARG A 377 33.636 49.499 27.990 1.00 88.62 O ANISOU 2570 O ARG A 377 10823 12608 10240 272 -1101 2210 O ATOM 2571 CB ARG A 377 35.770 48.137 25.869 1.00113.00 C ANISOU 2571 CB ARG A 377 13964 16161 12810 162 -1009 2195 C ATOM 2572 CG ARG A 377 35.685 49.286 24.882 1.00118.95 C ANISOU 2572 CG ARG A 377 14742 17002 13453 280 -1008 2523 C ATOM 2573 CD ARG A 377 36.399 48.943 23.579 1.00134.47 C ANISOU 2573 CD ARG A 377 16720 19252 15119 279 -977 2591 C ATOM 2574 NE ARG A 377 37.825 48.699 23.789 1.00142.18 N ANISOU 2574 NE ARG A 377 17755 20135 16132 150 -834 2546 N ATOM 2575 CZ ARG A 377 38.705 48.496 22.812 1.00139.25 C ANISOU 2575 CZ ARG A 377 17405 19958 15545 126 -764 2609 C ATOM 2576 NH1 ARG A 377 38.310 48.506 21.545 1.00134.55 N ANISOU 2576 NH1 ARG A 377 16787 19671 14663 221 -824 2721 N ATOM 2577 NH2 ARG A 377 39.983 48.284 23.103 1.00136.08 N ANISOU 2577 NH2 ARG A 377 17040 19458 15206 10 -633 2555 N ATOM 2578 N ALA A 378 33.888 47.281 28.287 1.00 98.68 N ANISOU 2578 N ALA A 378 12054 14042 11399 114 -1124 1771 N ATOM 2579 CA ALA A 378 32.561 47.137 28.876 1.00 97.72 C ANISOU 2579 CA ALA A 378 11855 13890 11384 155 -1213 1654 C ATOM 2580 C ALA A 378 32.488 47.776 30.257 1.00 96.74 C ANISOU 2580 C ALA A 378 11766 13448 11543 126 -1154 1653 C ATOM 2581 O ALA A 378 31.444 48.328 30.625 1.00 87.53 O ANISOU 2581 O ALA A 378 10549 12216 10494 204 -1206 1684 O ATOM 2582 CB ALA A 378 32.171 45.660 28.954 1.00 80.59 C ANISOU 2582 CB ALA A 378 9625 11854 9141 81 -1261 1359 C ATOM 2583 N PHE A 379 33.578 47.716 31.029 1.00 96.34 N ANISOU 2583 N PHE A 379 11793 13212 11601 19 -1047 1611 N ATOM 2584 CA PHE A 379 33.574 48.315 32.361 1.00 87.44 C ANISOU 2584 CA PHE A 379 10698 11801 10725 -17 -989 1592 C ATOM 2585 C PHE A 379 33.392 49.826 32.282 1.00 95.70 C ANISOU 2585 C PHE A 379 11765 12707 11889 72 -966 1832 C ATOM 2586 O PHE A 379 32.592 50.406 33.026 1.00 83.72 O ANISOU 2586 O PHE A 379 10225 11038 10547 116 -977 1825 O ATOM 2587 CB PHE A 379 34.863 47.970 33.106 1.00 84.49 C ANISOU 2587 CB PHE A 379 10392 11293 10416 -144 -889 1508 C ATOM 2588 CG PHE A 379 34.876 46.588 33.696 1.00 91.06 C ANISOU 2588 CG PHE A 379 11210 12159 11228 -226 -898 1259 C ATOM 2589 CD1 PHE A 379 33.895 45.664 33.371 1.00 87.00 C ANISOU 2589 CD1 PHE A 379 10630 11803 10624 -204 -979 1119 C ATOM 2590 CD2 PHE A 379 35.868 46.218 34.591 1.00 99.26 C ANISOU 2590 CD2 PHE A 379 12299 13068 12345 -324 -822 1167 C ATOM 2591 CE1 PHE A 379 33.911 44.394 33.920 1.00 84.01 C ANISOU 2591 CE1 PHE A 379 10245 11427 10247 -283 -970 899 C ATOM 2592 CE2 PHE A 379 35.889 44.950 35.145 1.00 97.39 C ANISOU 2592 CE2 PHE A 379 12057 12848 12097 -386 -823 962 C ATOM 2593 CZ PHE A 379 34.909 44.037 34.809 1.00 88.79 C ANISOU 2593 CZ PHE A 379 10913 11890 10931 -368 -890 832 C ATOM 2594 N SER A 380 34.128 50.483 31.380 1.00104.65 N ANISOU 2594 N SER A 380 12945 13883 12935 101 -922 2048 N ATOM 2595 CA SER A 380 34.003 51.931 31.239 1.00103.17 C ANISOU 2595 CA SER A 380 12789 13542 12870 188 -883 2299 C ATOM 2596 C SER A 380 32.615 52.331 30.754 1.00 94.81 C ANISOU 2596 C SER A 380 11657 12579 11786 350 -992 2395 C ATOM 2597 O SER A 380 32.108 53.394 31.130 1.00 93.21 O ANISOU 2597 O SER A 380 11458 12188 11768 431 -975 2518 O ATOM 2598 CB SER A 380 35.072 52.464 30.284 1.00101.24 C ANISOU 2598 CB SER A 380 12608 13342 12518 181 -804 2521 C ATOM 2599 OG SER A 380 34.812 52.069 28.950 1.00111.34 O ANISOU 2599 OG SER A 380 13854 14923 13525 262 -879 2609 O ATOM 2600 N ASN A 381 31.980 51.493 29.929 1.00 87.76 N ANISOU 2600 N ASN A 381 10691 11979 10674 403 -1105 2330 N ATOM 2601 CA ASN A 381 30.643 51.809 29.441 1.00100.56 C ANISOU 2601 CA ASN A 381 12220 13730 12257 561 -1225 2407 C ATOM 2602 C ASN A 381 29.582 51.592 30.518 1.00109.46 C ANISOU 2602 C ASN A 381 13272 14749 13568 563 -1269 2212 C ATOM 2603 O ASN A 381 28.616 52.360 30.598 1.00107.89 O ANISOU 2603 O ASN A 381 13017 14498 13478 693 -1316 2310 O ATOM 2604 CB ASN A 381 30.324 50.980 28.193 1.00116.06 C ANISOU 2604 CB ASN A 381 14116 16068 13915 607 -1336 2379 C ATOM 2605 CG ASN A 381 31.169 51.377 26.991 1.00122.09 C ANISOU 2605 CG ASN A 381 14944 16972 14474 644 -1300 2618 C ATOM 2606 OD1 ASN A 381 32.254 51.942 27.137 1.00130.14 O ANISOU 2606 OD1 ASN A 381 16064 17816 15569 582 -1173 2745 O ATOM 2607 ND2 ASN A 381 30.672 51.081 25.795 1.00123.82 N ANISOU 2607 ND2 ASN A 381 15097 17521 14426 740 -1410 2674 N ATOM 2608 N TYR A 382 29.735 50.559 31.355 1.00112.55 N ANISOU 2608 N TYR A 382 13659 15105 13999 426 -1247 1943 N ATOM 2609 CA TYR A 382 28.769 50.358 32.432 1.00112.89 C ANISOU 2609 CA TYR A 382 13637 15039 14216 415 -1267 1763 C ATOM 2610 C TYR A 382 28.890 51.455 33.481 1.00118.16 C ANISOU 2610 C TYR A 382 14360 15389 15149 419 -1175 1831 C ATOM 2611 O TYR A 382 27.881 51.906 34.037 1.00115.27 O ANISOU 2611 O TYR A 382 13929 14933 14934 492 -1198 1805 O ATOM 2612 CB TYR A 382 28.952 48.983 33.079 1.00 99.63 C ANISOU 2612 CB TYR A 382 11954 13388 12514 267 -1251 1481 C ATOM 2613 CG TYR A 382 28.870 47.807 32.130 1.00 98.21 C ANISOU 2613 CG TYR A 382 11722 13496 12099 242 -1326 1367 C ATOM 2614 CD1 TYR A 382 28.168 47.893 30.935 1.00 93.73 C ANISOU 2614 CD1 TYR A 382 11068 13186 11358 357 -1439 1453 C ATOM 2615 CD2 TYR A 382 29.501 46.607 32.434 1.00106.55 C ANISOU 2615 CD2 TYR A 382 12813 14567 13106 106 -1282 1170 C ATOM 2616 CE1 TYR A 382 28.100 46.818 30.067 1.00 87.80 C ANISOU 2616 CE1 TYR A 382 10264 12707 10387 324 -1505 1322 C ATOM 2617 CE2 TYR A 382 29.438 45.527 31.572 1.00108.05 C ANISOU 2617 CE2 TYR A 382 12956 15002 13097 78 -1338 1046 C ATOM 2618 CZ TYR A 382 28.735 45.638 30.391 1.00101.70 C ANISOU 2618 CZ TYR A 382 12063 14458 12119 180 -1449 1111 C ATOM 2619 OH TYR A 382 28.669 44.566 29.529 1.00114.07 O ANISOU 2619 OH TYR A 382 13578 16279 13483 144 -1504 962 O ATOM 2620 N LEU A 383 30.118 51.901 33.762 1.00112.96 N ANISOU 2620 N LEU A 383 13810 14560 14550 339 -1065 1906 N ATOM 2621 CA LEU A 383 30.319 52.990 34.712 1.00108.25 C ANISOU 2621 CA LEU A 383 13266 13661 14203 330 -970 1959 C ATOM 2622 C LEU A 383 29.742 54.307 34.205 1.00115.94 C ANISOU 2622 C LEU A 383 14227 14554 15271 493 -978 2206 C ATOM 2623 O LEU A 383 29.332 55.150 35.015 1.00107.54 O ANISOU 2623 O LEU A 383 13162 13260 14437 528 -930 2208 O ATOM 2624 CB LEU A 383 31.809 53.151 35.014 1.00 95.34 C ANISOU 2624 CB LEU A 383 11735 11892 12599 200 -856 1979 C ATOM 2625 CG LEU A 383 32.489 51.993 35.755 1.00 90.82 C ANISOU 2625 CG LEU A 383 11183 11342 11982 47 -830 1745 C ATOM 2626 CD1 LEU A 383 33.996 52.122 35.657 1.00 79.61 C ANISOU 2626 CD1 LEU A 383 9842 9868 10539 -54 -740 1802 C ATOM 2627 CD2 LEU A 383 32.048 51.953 37.206 1.00 96.57 C ANISOU 2627 CD2 LEU A 383 11901 11899 12891 -5 -802 1560 C ATOM 2628 N ARG A 384 29.702 54.502 32.883 1.00124.84 N ANISOU 2628 N ARG A 384 15344 15866 16223 598 -1035 2414 N ATOM 2629 CA ARG A 384 29.233 55.761 32.317 1.00129.65 C ANISOU 2629 CA ARG A 384 15952 16401 16910 768 -1039 2689 C ATOM 2630 C ARG A 384 27.791 55.661 31.825 1.00136.87 C ANISOU 2630 C ARG A 384 16737 17510 17757 938 -1182 2708 C ATOM 2631 O ARG A 384 26.889 56.280 32.401 1.00136.54 O ANISOU 2631 O ARG A 384 16640 17327 17912 1034 -1192 2704 O ATOM 2632 CB ARG A 384 30.159 56.212 31.181 1.00130.43 C ANISOU 2632 CB ARG A 384 16130 16564 16863 789 -995 2954 C ATOM 2633 CG ARG A 384 31.569 56.587 31.627 1.00135.39 C ANISOU 2633 CG ARG A 384 16873 16972 17598 637 -840 2975 C ATOM 2634 CD ARG A 384 32.414 57.139 30.477 1.00143.12 C ANISOU 2634 CD ARG A 384 17923 18005 18449 663 -780 3260 C ATOM 2635 NE ARG A 384 32.787 56.123 29.494 1.00147.68 N ANISOU 2635 NE ARG A 384 18486 18914 18713 635 -841 3236 N ATOM 2636 CZ ARG A 384 32.180 55.947 28.323 1.00145.64 C ANISOU 2636 CZ ARG A 384 18179 18939 18218 770 -948 3370 C ATOM 2637 NH1 ARG A 384 31.160 56.720 27.975 1.00139.59 N ANISOU 2637 NH1 ARG A 384 17372 18173 17494 956 -1015 3555 N ATOM 2638 NH2 ARG A 384 32.596 54.996 27.497 1.00148.04 N ANISOU 2638 NH2 ARG A 384 18471 19535 18242 725 -989 3312 N ATOM 2639 N CYS A 385 27.560 54.878 30.769 1.00145.45 N ANISOU 2639 N CYS A 385 17764 18930 18568 975 -1295 2712 N ATOM 2640 CA CYS A 385 26.257 54.851 30.109 1.00144.31 C ANISOU 2640 CA CYS A 385 17486 19016 18329 1147 -1444 2757 C ATOM 2641 C CYS A 385 25.148 54.272 30.983 1.00139.48 C ANISOU 2641 C CYS A 385 16752 18411 17833 1132 -1504 2490 C ATOM 2642 O CYS A 385 23.970 54.432 30.641 1.00140.79 O ANISOU 2642 O CYS A 385 16788 18719 17987 1283 -1617 2519 O ATOM 2643 CB CYS A 385 26.348 54.063 28.799 1.00134.87 C ANISOU 2643 CB CYS A 385 16253 18199 16794 1165 -1548 2783 C ATOM 2644 SG CYS A 385 25.889 52.320 28.933 1.00123.72 S ANISOU 2644 SG CYS A 385 14732 17045 15229 1034 -1641 2400 S ATOM 2645 N ASN A 386 25.484 53.611 32.089 1.00143.09 N ANISOU 2645 N ASN A 386 17241 18730 18397 960 -1429 2238 N ATOM 2646 CA ASN A 386 24.496 53.112 33.039 1.00142.04 C ANISOU 2646 CA ASN A 386 17007 18570 18394 930 -1454 1993 C ATOM 2647 C ASN A 386 24.545 53.851 34.369 1.00142.22 C ANISOU 2647 C ASN A 386 17080 18251 18705 897 -1336 1949 C ATOM 2648 O ASN A 386 23.525 54.381 34.820 1.00135.42 O ANISOU 2648 O ASN A 386 16131 17313 18007 1000 -1354 1934 O ATOM 2649 CB ASN A 386 24.684 51.600 33.264 1.00132.39 C ANISOU 2649 CB ASN A 386 15768 17491 17043 760 -1468 1718 C ATOM 2650 CG ASN A 386 24.180 50.758 32.090 1.00117.61 C ANISOU 2650 CG ASN A 386 13791 15978 14916 799 -1604 1675 C ATOM 2651 OD1 ASN A 386 23.214 51.120 31.415 1.00112.34 O ANISOU 2651 OD1 ASN A 386 13007 15480 14197 954 -1716 1766 O ATOM 2652 ND2 ASN A 386 24.835 49.625 31.851 1.00101.61 N ANISOU 2652 ND2 ASN A 386 11802 14075 12731 662 -1595 1528 N ATOM 2653 N TYR A 387 25.711 53.917 35.008 1.00162.96 N ANISOU 2653 N TYR A 387 19837 20681 21398 757 -1215 1920 N ATOM 2654 CA TYR A 387 25.853 54.645 36.268 1.00163.10 C ANISOU 2654 CA TYR A 387 19908 20388 21676 714 -1100 1864 C ATOM 2655 C TYR A 387 25.969 56.146 36.025 1.00163.90 C ANISOU 2655 C TYR A 387 20055 20285 21934 839 -1046 2117 C ATOM 2656 O TYR A 387 26.814 56.596 35.251 1.00162.13 O ANISOU 2656 O TYR A 387 19913 20051 21638 850 -1016 2323 O ATOM 2657 CB TYR A 387 27.073 54.148 37.049 1.00161.38 C ANISOU 2657 CB TYR A 387 19798 20056 21461 519 -1001 1729 C TER 2658 TYR A 387 HETATM 2659 C10 E2J A1201 39.372 36.092 61.609 1.00 95.03 C HETATM 2660 N11 E2J A1201 38.390 36.423 60.816 1.00 94.94 N HETATM 2661 C12 E2J A1201 37.658 33.183 59.160 1.00 77.25 C HETATM 2662 C13 E2J A1201 38.532 33.077 57.911 1.00 79.34 C HETATM 2663 C15 E2J A1201 38.440 32.363 55.619 1.00 94.24 C HETATM 2664 C26 E2J A1201 38.982 29.200 52.965 1.00101.64 C HETATM 2665 C28 E2J A1201 38.951 28.514 50.657 1.00 97.96 C HETATM 2666 C31 E2J A1201 39.995 30.113 52.664 1.00 97.85 C HETATM 2667 C33 E2J A1201 37.583 29.742 56.557 1.00 88.58 C HETATM 2668 C34 E2J A1201 38.358 30.749 57.408 1.00 77.26 C HETATM 2669 C19 E2J A1201 38.551 27.657 54.936 1.00 80.80 C HETATM 2670 C18 E2J A1201 38.463 29.023 54.352 1.00 95.96 C HETATM 2671 C21 E2J A1201 39.743 25.984 56.183 1.00 93.61 C HETATM 2672 C01 E2J A1201 36.683 35.965 59.133 1.00 71.62 C HETATM 2673 C02 E2J A1201 37.816 35.532 60.025 1.00 71.62 C HETATM 2674 C03 E2J A1201 38.274 34.229 60.050 1.00 77.66 C HETATM 2675 C04 E2J A1201 39.327 33.877 60.895 1.00 75.94 C HETATM 2676 O05 E2J A1201 39.731 32.723 60.911 1.00 71.62 O HETATM 2677 N06 E2J A1201 39.895 34.829 61.701 1.00 89.09 N HETATM 2678 C07 E2J A1201 40.931 34.664 62.592 1.00 90.99 C HETATM 2679 C08 E2J A1201 41.387 35.688 63.316 1.00 83.02 C HETATM 2680 S09 E2J A1201 40.338 37.028 62.769 1.00 94.43 S HETATM 2681 N14 E2J A1201 37.959 32.097 56.983 1.00 94.64 N1+ HETATM 2682 C16 E2J A1201 37.717 31.434 54.636 1.00 88.78 C HETATM 2683 C17 E2J A1201 37.932 30.008 55.107 1.00 91.37 C HETATM 2684 C20 E2J A1201 39.683 27.256 55.651 1.00 83.87 C HETATM 2685 C22 E2J A1201 38.687 25.101 56.003 1.00 93.90 C HETATM 2686 C23 E2J A1201 37.565 25.491 55.290 1.00 85.64 C HETATM 2687 C24 E2J A1201 37.496 26.761 54.755 1.00 81.86 C HETATM 2688 F25 E2J A1201 38.747 23.857 56.524 1.00 91.40 F HETATM 2689 C27 E2J A1201 38.475 28.393 51.947 1.00101.35 C HETATM 2690 C29 E2J A1201 39.944 29.434 50.364 1.00 99.24 C HETATM 2691 C30 E2J A1201 40.463 30.233 51.371 1.00 99.41 C HETATM 2692 F32 E2J A1201 40.405 29.550 49.099 1.00 94.85 F HETATM 2693 C10 OLC A1202 34.290 56.280 56.305 1.00 95.75 C HETATM 2694 C9 OLC A1202 34.054 55.905 57.551 1.00 98.25 C HETATM 2695 C11 OLC A1202 35.511 56.979 55.794 1.00 99.71 C HETATM 2696 C8 OLC A1202 34.953 56.092 58.739 1.00103.23 C HETATM 2697 C24 OLC A1202 30.921 57.819 69.728 1.00138.57 C HETATM 2698 C12 OLC A1202 35.441 57.256 54.291 1.00 90.76 C HETATM 2699 C7 OLC A1202 34.161 56.352 60.025 1.00 99.85 C HETATM 2700 C6 OLC A1202 33.423 57.680 60.022 1.00 90.13 C HETATM 2701 C5 OLC A1202 32.251 57.783 60.988 1.00 86.45 C HETATM 2702 C4 OLC A1202 32.591 57.795 62.470 1.00 94.02 C HETATM 2703 C3 OLC A1202 31.390 58.156 63.340 1.00 90.49 C HETATM 2704 C2 OLC A1202 31.706 58.243 64.829 1.00 93.99 C HETATM 2705 C21 OLC A1202 29.582 58.768 67.817 1.00118.91 C HETATM 2706 C1 OLC A1202 30.551 58.751 65.646 1.00121.03 C HETATM 2707 C22 OLC A1202 29.627 57.767 68.949 1.00130.27 C HETATM 2708 O19 OLC A1202 29.674 59.456 65.229 1.00138.73 O HETATM 2709 O25 OLC A1202 31.064 59.067 70.398 1.00140.74 O HETATM 2710 O23 OLC A1202 28.519 57.971 69.831 1.00136.42 O HETATM 2711 O20 OLC A1202 30.620 58.326 66.911 1.00127.62 O HETATM 2712 C24 OLC A1203 32.450 62.829 63.498 1.00116.76 C HETATM 2713 C6 OLC A1203 33.603 61.901 52.519 1.00 95.57 C HETATM 2714 C5 OLC A1203 33.717 61.240 53.884 1.00104.91 C HETATM 2715 C4 OLC A1203 33.899 62.211 55.044 1.00 98.57 C HETATM 2716 C3 OLC A1203 33.865 61.543 56.411 1.00 86.32 C HETATM 2717 C2 OLC A1203 33.787 62.527 57.571 1.00 95.23 C HETATM 2718 C21 OLC A1203 32.618 62.236 61.065 1.00122.80 C HETATM 2719 C1 OLC A1203 33.201 61.895 58.801 1.00115.98 C HETATM 2720 C22 OLC A1203 32.883 63.279 62.122 1.00125.81 C HETATM 2721 O19 OLC A1203 32.735 60.788 58.843 1.00122.80 O HETATM 2722 O25 OLC A1203 32.767 63.803 64.483 1.00109.03 O HETATM 2723 O23 OLC A1203 34.277 63.597 62.127 1.00129.14 O HETATM 2724 O20 OLC A1203 33.241 62.719 59.852 1.00115.51 O HETATM 2725 C8 OLC A1204 26.907 49.754 49.378 1.00 90.97 C HETATM 2726 C24 OLC A1204 26.165 50.721 36.610 1.00103.98 C HETATM 2727 C7 OLC A1204 26.666 48.411 48.692 1.00 90.38 C HETATM 2728 C6 OLC A1204 27.269 48.309 47.300 1.00 93.61 C HETATM 2729 C5 OLC A1204 26.723 49.321 46.302 1.00101.88 C HETATM 2730 C4 OLC A1204 27.272 49.141 44.896 1.00103.47 C HETATM 2731 C3 OLC A1204 26.617 50.020 43.843 1.00 92.70 C HETATM 2732 C2 OLC A1204 27.049 49.656 42.429 1.00 92.56 C HETATM 2733 C21 OLC A1204 26.452 51.099 39.079 1.00114.00 C HETATM 2734 C1 OLC A1204 26.397 50.506 41.378 1.00112.32 C HETATM 2735 C22 OLC A1204 26.232 50.087 37.979 1.00113.53 C HETATM 2736 O19 OLC A1204 25.485 51.262 41.573 1.00127.57 O HETATM 2737 O25 OLC A1204 26.124 49.732 35.591 1.00101.08 O HETATM 2738 O23 OLC A1204 27.275 49.109 38.012 1.00116.65 O HETATM 2739 O20 OLC A1204 26.963 50.319 40.184 1.00116.53 O HETATM 2740 C24 OLC A1205 21.221 42.423 32.770 1.00125.73 C HETATM 2741 C5 OLC A1205 22.950 41.597 42.459 1.00103.23 C HETATM 2742 C4 OLC A1205 23.107 41.061 41.046 1.00101.14 C HETATM 2743 C3 OLC A1205 22.594 42.004 39.968 1.00117.82 C HETATM 2744 C2 OLC A1205 22.731 41.443 38.558 1.00123.38 C HETATM 2745 C21 OLC A1205 21.883 42.696 35.182 1.00127.43 C HETATM 2746 C1 OLC A1205 22.238 42.397 37.509 1.00127.18 C HETATM 2747 C22 OLC A1205 21.809 41.764 33.996 1.00128.93 C HETATM 2748 O19 OLC A1205 21.806 43.497 37.733 1.00125.13 O HETATM 2749 O25 OLC A1205 21.070 41.488 31.709 1.00123.97 O HETATM 2750 O23 OLC A1205 23.115 41.265 33.699 1.00133.49 O HETATM 2751 O20 OLC A1205 22.336 41.873 36.283 1.00127.77 O HETATM 2752 C24 OLC A1206 46.894 16.333 37.398 1.00116.31 C HETATM 2753 C7 OLC A1206 47.041 15.709 48.576 1.00129.03 C HETATM 2754 C6 OLC A1206 47.764 16.824 47.836 1.00120.77 C HETATM 2755 C5 OLC A1206 47.161 17.159 46.481 1.00117.06 C HETATM 2756 C4 OLC A1206 46.941 15.946 45.593 1.00120.20 C HETATM 2757 C3 OLC A1206 46.487 16.262 44.176 1.00123.96 C HETATM 2758 C2 OLC A1206 47.624 16.684 43.252 1.00129.29 C HETATM 2759 C21 OLC A1206 46.366 16.057 39.842 1.00129.34 C HETATM 2760 C1 OLC A1206 47.533 16.004 41.917 1.00132.03 C HETATM 2761 C22 OLC A1206 47.444 16.249 38.803 1.00123.00 C HETATM 2762 O19 OLC A1206 48.020 14.936 41.660 1.00127.70 O HETATM 2763 O25 OLC A1206 45.937 15.309 37.160 1.00111.30 O HETATM 2764 O23 OLC A1206 48.212 17.417 39.102 1.00124.34 O HETATM 2765 O20 OLC A1206 46.805 16.718 41.053 1.00138.46 O HETATM 2766 C9 OLC A1207 39.483 18.572 46.730 1.00105.63 C HETATM 2767 C8 OLC A1207 38.493 18.681 45.615 1.00103.32 C HETATM 2768 C7 OLC A1207 39.131 19.103 44.292 1.00103.86 C HETATM 2769 C6 OLC A1207 38.119 19.461 43.213 1.00102.91 C HETATM 2770 C5 OLC A1207 38.728 20.048 41.949 1.00 93.74 C HETATM 2771 C4 OLC A1207 37.712 20.669 40.999 1.00 89.22 C HETATM 2772 C3 OLC A1207 36.693 19.692 40.436 1.00 92.95 C HETATM 2773 C1 PEG A1208 41.593 50.874 24.713 1.00103.15 C HETATM 2774 O1 PEG A1208 42.329 49.775 25.174 1.00101.78 O HETATM 2775 C2 PEG A1208 42.364 52.160 24.996 1.00119.00 C HETATM 2776 O2 PEG A1208 42.624 52.263 26.369 1.00131.00 O HETATM 2777 C3 PEG A1208 41.848 53.222 27.032 1.00128.13 C HETATM 2778 C4 PEG A1208 41.080 52.544 28.164 1.00122.79 C HETATM 2779 O4 PEG A1208 40.328 53.492 28.872 1.00112.28 O HETATM 2780 C1 OLA A1209 21.916 35.690 35.168 1.00122.27 C HETATM 2781 O1 OLA A1209 21.986 36.135 33.991 1.00117.99 O HETATM 2782 O2 OLA A1209 22.146 34.472 35.394 1.00128.11 O HETATM 2783 C2 OLA A1209 21.557 36.626 36.322 1.00116.37 C HETATM 2784 C3 OLA A1209 22.597 36.503 37.434 1.00113.17 C HETATM 2785 C4 OLA A1209 22.069 35.601 38.549 1.00115.12 C HETATM 2786 C5 OLA A1209 22.821 35.932 39.837 1.00116.86 C HETATM 2787 C6 OLA A1209 22.315 35.071 40.993 1.00114.18 C HETATM 2788 C7 OLA A1209 22.877 35.639 42.295 1.00114.87 C HETATM 2789 C8 OLA A1209 22.165 35.025 43.500 1.00111.59 C HETATM 2790 C9 OLA A1209 22.116 36.076 44.608 1.00118.69 C HETATM 2791 C10 OLA A1209 22.273 35.756 45.878 1.00123.73 C HETATM 2792 C11 OLA A1209 22.512 34.312 46.322 1.00112.72 C HETATM 2793 C12 OLA A1209 22.500 34.254 47.851 1.00 97.64 C HETATM 2794 C13 OLA A1209 23.197 32.982 48.332 1.00 90.31 C HETATM 2795 C14 OLA A1209 22.981 32.812 49.834 1.00 78.67 C HETATM 2796 C1 OLA A1210 25.950 30.977 33.268 1.00125.75 C HETATM 2797 O1 OLA A1210 26.027 30.243 32.247 1.00124.02 O HETATM 2798 O2 OLA A1210 26.239 32.200 33.190 1.00123.85 O HETATM 2799 C2 OLA A1210 25.502 30.379 34.600 1.00123.07 C HETATM 2800 C3 OLA A1210 26.646 30.438 35.609 1.00114.10 C HETATM 2801 C4 OLA A1210 26.132 30.003 36.980 1.00109.58 C HETATM 2802 C5 OLA A1210 25.593 31.220 37.728 1.00104.22 C HETATM 2803 C6 OLA A1210 24.926 30.766 39.024 1.00104.22 C HETATM 2804 C7 OLA A1210 25.987 30.415 40.067 1.00101.51 C HETATM 2805 C8 OLA A1210 25.441 30.738 41.459 1.00 98.00 C HETATM 2806 C9 OLA A1210 25.326 29.459 42.285 1.00103.01 C HETATM 2807 C10 OLA A1210 25.066 29.510 43.578 1.00113.82 C HETATM 2808 C11 OLA A1210 24.873 30.847 44.296 1.00115.55 C HETATM 2809 C12 OLA A1210 24.356 30.591 45.713 1.00113.69 C HETATM 2810 C13 OLA A1210 25.456 29.973 46.577 1.00118.26 C HETATM 2811 C14 OLA A1210 25.000 28.620 47.125 1.00128.33 C HETATM 2812 C15 OLA A1210 23.915 28.809 48.185 1.00128.30 C HETATM 2813 O HOH A1301 39.131 30.477 60.822 1.00 71.62 O HETATM 2814 O HOH A1302 46.410 36.289 54.266 1.00 71.62 O HETATM 2815 O HOH A1303 33.054 37.987 67.298 1.00 71.62 O HETATM 2816 O HOH A1304 43.198 27.020 58.357 1.00 74.76 O CONECT 645 1256 CONECT 1256 645 CONECT 2249 2270 CONECT 2270 2249 CONECT 2659 2660 2677 2680 CONECT 2660 2659 2673 CONECT 2661 2662 2674 CONECT 2662 2661 2681 CONECT 2663 2681 2682 CONECT 2664 2666 2670 2689 CONECT 2665 2689 2690 CONECT 2666 2664 2691 CONECT 2667 2668 2683 CONECT 2668 2667 2681 CONECT 2669 2670 2684 2687 CONECT 2670 2664 2669 2683 CONECT 2671 2684 2685 CONECT 2672 2673 CONECT 2673 2660 2672 2674 CONECT 2674 2661 2673 2675 CONECT 2675 2674 2676 2677 CONECT 2676 2675 CONECT 2677 2659 2675 2678 CONECT 2678 2677 2679 CONECT 2679 2678 2680 CONECT 2680 2659 2679 CONECT 2681 2662 2663 2668 CONECT 2682 2663 2683 CONECT 2683 2667 2670 2682 CONECT 2684 2669 2671 CONECT 2685 2671 2686 2688 CONECT 2686 2685 2687 CONECT 2687 2669 2686 CONECT 2688 2685 CONECT 2689 2664 2665 CONECT 2690 2665 2691 2692 CONECT 2691 2666 2690 CONECT 2692 2690 CONECT 2693 2694 2695 CONECT 2694 2693 2696 CONECT 2695 2693 2698 CONECT 2696 2694 2699 CONECT 2697 2707 2709 CONECT 2698 2695 CONECT 2699 2696 2700 CONECT 2700 2699 2701 CONECT 2701 2700 2702 CONECT 2702 2701 2703 CONECT 2703 2702 2704 CONECT 2704 2703 2706 CONECT 2705 2707 2711 CONECT 2706 2704 2708 2711 CONECT 2707 2697 2705 2710 CONECT 2708 2706 CONECT 2709 2697 CONECT 2710 2707 CONECT 2711 2705 2706 CONECT 2712 2720 2722 CONECT 2713 2714 CONECT 2714 2713 2715 CONECT 2715 2714 2716 CONECT 2716 2715 2717 CONECT 2717 2716 2719 CONECT 2718 2720 2724 CONECT 2719 2717 2721 2724 CONECT 2720 2712 2718 2723 CONECT 2721 2719 CONECT 2722 2712 CONECT 2723 2720 CONECT 2724 2718 2719 CONECT 2725 2727 CONECT 2726 2735 2737 CONECT 2727 2725 2728 CONECT 2728 2727 2729 CONECT 2729 2728 2730 CONECT 2730 2729 2731 CONECT 2731 2730 2732 CONECT 2732 2731 2734 CONECT 2733 2735 2739 CONECT 2734 2732 2736 2739 CONECT 2735 2726 2733 2738 CONECT 2736 2734 CONECT 2737 2726 CONECT 2738 2735 CONECT 2739 2733 2734 CONECT 2740 2747 2749 CONECT 2741 2742 CONECT 2742 2741 2743 CONECT 2743 2742 2744 CONECT 2744 2743 2746 CONECT 2745 2747 2751 CONECT 2746 2744 2748 2751 CONECT 2747 2740 2745 2750 CONECT 2748 2746 CONECT 2749 2740 CONECT 2750 2747 CONECT 2751 2745 2746 CONECT 2752 2761 2763 CONECT 2753 2754 CONECT 2754 2753 2755 CONECT 2755 2754 2756 CONECT 2756 2755 2757 CONECT 2757 2756 2758 CONECT 2758 2757 2760 CONECT 2759 2761 2765 CONECT 2760 2758 2762 2765 CONECT 2761 2752 2759 2764 CONECT 2762 2760 CONECT 2763 2752 CONECT 2764 2761 CONECT 2765 2759 2760 CONECT 2766 2767 CONECT 2767 2766 2768 CONECT 2768 2767 2769 CONECT 2769 2768 2770 CONECT 2770 2769 2771 CONECT 2771 2770 2772 CONECT 2772 2771 CONECT 2773 2774 2775 CONECT 2774 2773 CONECT 2775 2773 2776 CONECT 2776 2775 2777 CONECT 2777 2776 2778 CONECT 2778 2777 2779 CONECT 2779 2778 CONECT 2780 2781 2782 2783 CONECT 2781 2780 CONECT 2782 2780 CONECT 2783 2780 2784 CONECT 2784 2783 2785 CONECT 2785 2784 2786 CONECT 2786 2785 2787 CONECT 2787 2786 2788 CONECT 2788 2787 2789 CONECT 2789 2788 2790 CONECT 2790 2789 2791 CONECT 2791 2790 2792 CONECT 2792 2791 2793 CONECT 2793 2792 2794 CONECT 2794 2793 2795 CONECT 2795 2794 CONECT 2796 2797 2798 2799 CONECT 2797 2796 CONECT 2798 2796 CONECT 2799 2796 2800 CONECT 2800 2799 2801 CONECT 2801 2800 2802 CONECT 2802 2801 2803 CONECT 2803 2802 2804 CONECT 2804 2803 2805 CONECT 2805 2804 2806 CONECT 2806 2805 2807 CONECT 2807 2806 2808 CONECT 2808 2807 2809 CONECT 2809 2808 2810 CONECT 2810 2809 2811 CONECT 2811 2810 2812 CONECT 2812 2811 MASTER 453 0 10 17 2 0 13 6 2815 1 158 35 END