HEADER MEMBRANE PROTEIN 12-JUL-19 6PS7 TITLE XFEL A2AR STRUCTURE BY LIGAND EXCHANGE FROM LUF5843 TO ZM241385. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE COMPND 3 RECEPTOR A2A; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: 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: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS GPCR, COMPLEX-LCP METHOD, SBDD, DRUG DESIGN, XFEL, LCP-SFX, LIGAND KEYWDS 2 EXCHANGE, LUF5843, ZM241385, A2AAR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.ISHCHENKO,B.STAUCH,G.W.HAN,A.BATYUK,A.SHIRIAEVA,C.LI,N.A.ZATSEPIN, AUTHOR 2 U.WEIERSTALL,W.LIU,E.NANGO,T.NAKANE,R.TANAKA,K.TONO,Y.JOTI,S.IWATA, AUTHOR 3 I.MORAES,C.GATI,C.CHEREZOV REVDAT 3 01-JAN-20 6PS7 1 REMARK REVDAT 2 25-DEC-19 6PS7 1 JRNL REVDAT 1 13-NOV-19 6PS7 0 JRNL AUTH A.ISHCHENKO,B.STAUCH,G.W.HAN,A.BATYUK,A.SHIRIAEVA,C.LI, JRNL AUTH 2 N.ZATSEPIN,U.WEIERSTALL,W.LIU,E.NANGO,T.NAKANE,R.TANAKA, JRNL AUTH 3 K.TONO,Y.JOTI,S.IWATA,I.MORAES,C.GATI,V.CHEREZOV JRNL TITL TOWARD G PROTEIN-COUPLED RECEPTOR STRUCTURE-BASED DRUG JRNL TITL 2 DESIGN USING X-RAY LASERS. JRNL REF IUCRJ V. 6 1106 2019 JRNL REFN ESSN 2052-2525 JRNL PMID 31709066 JRNL DOI 10.1107/S2052252519013137 REMARK 2 REMARK 2 RESOLUTION. 1.85 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.10_2155 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) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.49 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 45044 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.176 REMARK 3 R VALUE (WORKING SET) : 0.176 REMARK 3 FREE R VALUE : 0.201 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.740 REMARK 3 FREE R VALUE TEST SET COUNT : 1233 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 33.4940 - 3.8464 1.00 5125 145 0.1791 0.2032 REMARK 3 2 3.8464 - 3.0537 1.00 4931 139 0.1455 0.1882 REMARK 3 3 3.0537 - 2.6679 1.00 4868 138 0.1421 0.1622 REMARK 3 4 2.6679 - 2.4240 1.00 4848 136 0.1467 0.1816 REMARK 3 5 2.4240 - 2.2503 1.00 4822 137 0.1671 0.1971 REMARK 3 6 2.2503 - 2.1177 1.00 4820 135 0.1813 0.2037 REMARK 3 7 2.1177 - 2.0116 1.00 4791 135 0.2181 0.2135 REMARK 3 8 2.0116 - 1.9241 1.00 4802 136 0.3082 0.3239 REMARK 3 9 1.9241 - 1.8500 1.00 4804 132 0.4276 0.3905 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.520 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.86 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 : 0.009 3627 REMARK 3 ANGLE : 1.053 4899 REMARK 3 CHIRALITY : 0.058 565 REMARK 3 PLANARITY : 0.006 618 REMARK 3 DIHEDRAL : 16.583 2230 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' REMARK 3 ORIGIN FOR THE GROUP (A): 17.1140 198.4344 18.2995 REMARK 3 T TENSOR REMARK 3 T11: 0.2419 T22: 0.2377 REMARK 3 T33: 0.2264 T12: 0.0199 REMARK 3 T13: 0.0037 T23: -0.0064 REMARK 3 L TENSOR REMARK 3 L11: 0.8098 L22: 1.2972 REMARK 3 L33: 0.4519 L12: 0.0307 REMARK 3 L13: -0.1326 L23: -0.0019 REMARK 3 S TENSOR REMARK 3 S11: 0.0335 S12: 0.0044 S13: 0.1856 REMARK 3 S21: -0.0345 S22: 0.0129 S23: 0.1387 REMARK 3 S31: -0.1231 S32: -0.0100 S33: -0.0371 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 6PS7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-19. REMARK 100 THE DEPOSITION ID IS D_1000242948. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-DEC-17 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : CXI REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.33 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-2 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45163 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 33.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 118.0 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4EIY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM SODIUM THIOCYANATE, 100 MM SODIUM REMARK 280 CITRATE PH 4.8, AND 28% PEG 400, 2 MM OF TARGET LIGAND ZM241385, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.24000 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 71.24000 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 20.16000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.24500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 20.16000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.24500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.24000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 20.16000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.24500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.24000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 20.16000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.24500 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 ALA A -19 REMARK 465 LEU A -18 REMARK 465 SER A -17 REMARK 465 TYR A -16 REMARK 465 ILE A -15 REMARK 465 PHE A -14 REMARK 465 CYS A -13 REMARK 465 LEU A -12 REMARK 465 VAL A -11 REMARK 465 PHE A -10 REMARK 465 ALA A -9 REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 MET A 1058 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 HIS A 317 REMARK 465 HIS A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 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 ASP A -2 OD1 OD2 REMARK 470 ARG A 107 CZ NH1 NH2 REMARK 470 GLN A 148 CD OE1 NE2 REMARK 470 ARG A 199 NE CZ NH1 NH2 REMARK 470 LYS A1015 CD CE NZ REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 ASP A1021 CG OD1 OD2 REMARK 470 GLN A1025 CG CD OE1 NE2 REMARK 470 LYS A1027 CE NZ REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1077 CD CE NZ REMARK 470 GLU A1086 CG CD OE1 OE2 REMARK 470 GLN A1093 CG CD OE1 NE2 REMARK 470 LYS A1104 CD CE NZ REMARK 470 ARG A 222 NE CZ NH1 NH2 REMARK 470 LYS A 227 CE NZ REMARK 470 LYS A 301 CE NZ REMARK 470 VAL A 307 CG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -50.65 -122.03 REMARK 500 TYR A1101 -47.96 -130.46 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 OLC A 1208 REMARK 610 OLC A 1209 REMARK 610 OLC A 1210 REMARK 610 OLB A 1214 REMARK 610 OLA A 1215 REMARK 610 OLA A 1216 REMARK 610 OLA A 1217 REMARK 610 OLA A 1218 REMARK 610 OLA A 1219 REMARK 610 OLA A 1220 REMARK 610 OLA A 1221 REMARK 610 OLA A 1222 REMARK 610 OLA A 1223 REMARK 610 OLA A 1224 REMARK 610 OLA A 1225 REMARK 610 OLA A 1226 REMARK 610 OLA A 1227 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A1228 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 128.7 REMARK 620 3 HOH A1319 O 105.7 119.3 REMARK 620 4 HOH A1357 O 86.1 117.3 87.5 REMARK 620 5 HOH A1380 O 77.1 74.8 96.5 163.2 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZMA 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 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1223 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1224 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1226 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1227 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1228 DBREF 6PS7 A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 6PS7 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 6PS7 A 219 316 UNP P29274 AA2AR_HUMAN 219 316 SEQADV 6PS7 ALA A -19 UNP P29274 EXPRESSION TAG SEQADV 6PS7 LEU A -18 UNP P29274 EXPRESSION TAG SEQADV 6PS7 SER A -17 UNP P29274 EXPRESSION TAG SEQADV 6PS7 TYR A -16 UNP P29274 EXPRESSION TAG SEQADV 6PS7 ILE A -15 UNP P29274 EXPRESSION TAG SEQADV 6PS7 PHE A -14 UNP P29274 EXPRESSION TAG SEQADV 6PS7 CYS A -13 UNP P29274 EXPRESSION TAG SEQADV 6PS7 LEU A -12 UNP P29274 EXPRESSION TAG SEQADV 6PS7 VAL A -11 UNP P29274 EXPRESSION TAG SEQADV 6PS7 PHE A -10 UNP P29274 EXPRESSION TAG SEQADV 6PS7 ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 6PS7 ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 6PS7 TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 6PS7 LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 6PS7 ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 6PS7 ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 6PS7 ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 6PS7 ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 6PS7 GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 6PS7 ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 6PS7 PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 6PS7 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6PS7 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6PS7 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 6PS7 HIS A 317 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 318 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 6PS7 HIS A 326 UNP P29274 EXPRESSION TAG SEQRES 1 A 442 ALA LEU SER TYR ILE PHE CYS LEU VAL PHE ALA ASP TYR SEQRES 2 A 442 LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET GLY SER SEQRES 3 A 442 SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA VAL LEU SEQRES 4 A 442 ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA VAL TRP SEQRES 5 A 442 LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR PHE VAL SEQRES 6 A 442 VAL SER LEU ALA ALA ALA ASP ILE ALA VAL GLY VAL LEU SEQRES 7 A 442 ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY PHE CYS SEQRES 8 A 442 ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS PHE VAL SEQRES 9 A 442 LEU VAL LEU THR GLN SER SER ILE PHE SER LEU LEU ALA SEQRES 10 A 442 ILE ALA ILE ASP ARG TYR ILE ALA ILE ARG ILE PRO LEU SEQRES 11 A 442 ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA LYS GLY SEQRES 12 A 442 ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA ILE GLY SEQRES 13 A 442 LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY GLN PRO SEQRES 14 A 442 LYS GLU GLY LYS ASN HIS SER GLN GLY CYS GLY GLU GLY SEQRES 15 A 442 GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO MET ASN SEQRES 16 A 442 TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL LEU VAL SEQRES 17 A 442 PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG ILE PHE SEQRES 18 A 442 LEU ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU ASP ASN SEQRES 19 A 442 TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS SEQRES 20 A 442 ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS SEQRES 21 A 442 MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA THR PRO SEQRES 22 A 442 PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO GLU MET SEQRES 23 A 442 LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN SEQRES 24 A 442 ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL SEQRES 25 A 442 LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS THR THR SEQRES 26 A 442 ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG ALA ARG SEQRES 27 A 442 SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER LEU SEQRES 28 A 442 ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU PRO SEQRES 29 A 442 LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO ASP SEQRES 30 A 442 CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA ILE SEQRES 31 A 442 VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE ILE SEQRES 32 A 442 TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE ARG SEQRES 33 A 442 LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU PRO SEQRES 34 A 442 PHE LYS ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HET ZMA A1201 25 HET OLC A1202 17 HET OLC A1203 16 HET OLC A1204 18 HET OLC A1205 17 HET OLC A1206 17 HET OLC A1207 11 HET OLC A1208 11 HET OLC A1209 11 HET OLC A1210 17 HET CLR A1211 28 HET CLR A1212 28 HET CLR A1213 28 HET OLB A1214 17 HET OLA A1215 16 HET OLA A1216 9 HET OLA A1217 9 HET OLA A1218 12 HET OLA A1219 11 HET OLA A1220 13 HET OLA A1221 12 HET OLA A1222 11 HET OLA A1223 9 HET OLA A1224 8 HET OLA A1225 18 HET OLA A1226 12 HET OLA A1227 17 HET NA A1228 1 HETNAM ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3, HETNAM 2 ZMA 5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM CLR CHOLESTEROL HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETNAM NA SODIUM ION HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 ZMA C16 H15 N7 O2 FORMUL 3 OLC 9(C21 H40 O4) FORMUL 12 CLR 3(C27 H46 O) FORMUL 15 OLB C21 H40 O4 FORMUL 16 OLA 13(C18 H34 O2) FORMUL 29 NA NA 1+ FORMUL 30 HOH *105(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 SER A 67 1 10 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ILE A 108 VAL A 116 1 9 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLN A 157 1 8 HELIX 10 AB1 LEU A 167 VAL A 172 1 6 HELIX 11 AB2 PRO A 173 PHE A 180 1 8 HELIX 12 AB3 VAL A 186 ALA A 1020 1 43 HELIX 13 AB4 ASN A 1022 ALA A 1043 1 22 HELIX 14 AB5 ASP A 1060 GLU A 1081 1 22 HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11 HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9 HELIX 17 AB8 TYR A 1101 CYS A 259 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 VAL A 307 1 16 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.00 SSBOND 2 CYS A 74 CYS A 146 1555 1555 1.95 SSBOND 3 CYS A 77 CYS A 166 1555 1555 1.99 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.02 LINK OD1 ASP A 52 NA NA A1228 1555 1555 2.39 LINK OG SER A 91 NA NA A1228 1555 1555 2.49 LINK NA NA A1228 O HOH A1319 1555 1555 2.62 LINK NA NA A1228 O HOH A1357 1555 1555 2.35 LINK NA NA A1228 O HOH A1380 1555 1555 2.49 SITE 1 AC1 12 PHE A 168 GLU A 169 MET A 177 TRP A 246 SITE 2 AC1 12 LEU A 249 HIS A 250 ASN A 253 MET A 270 SITE 3 AC1 12 HOH A1321 HOH A1331 HOH A1348 HOH A1379 SITE 1 AC2 5 CYS A 28 VAL A 31 VAL A 46 OLC A1203 SITE 2 AC2 5 OLA A1223 SITE 1 AC3 5 TYR A 43 LYS A 122 ILE A 125 TRP A 129 SITE 2 AC3 5 OLC A1202 SITE 1 AC4 6 GLY A 5 SER A 6 LEU A 267 TYR A 271 SITE 2 AC4 6 OLA A1215 HOH A1318 SITE 1 AC5 3 CLR A1212 OLA A1227 HOH A1367 SITE 1 AC6 1 PHE A 258 SITE 1 AC7 1 OLA A1222 SITE 1 AC8 4 LEU A 190 LEU A 194 VAL A 239 CLR A1211 SITE 1 AC9 2 TYR A 179 OLB A1214 SITE 1 AD1 4 PHE A 258 OLC A1209 OLA A1227 HOH A1315 SITE 1 AD2 3 PHE A 255 SER A 263 OLC A1205 SITE 1 AD3 4 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 1 AD4 5 MET A 140 LEU A 141 TYR A 179 ALA A 184 SITE 2 AD4 5 OLC A1210 SITE 1 AD5 3 TYR A 290 OLC A1204 OLA A1221 SITE 1 AD6 3 PHE A 44 ALA A 97 HOH A1306 SITE 1 AD7 1 SER A 7 SITE 1 AD8 5 SER A 7 LEU A 22 TRP A 29 PHE A 286 SITE 2 AD8 5 HOH A1359 SITE 1 AD9 1 LEU A 244 SITE 1 AE1 1 OLA A1215 SITE 1 AE2 2 OLC A1208 OLA A1226 SITE 1 AE3 1 OLC A1202 SITE 1 AE4 2 TRP A 32 LYS A 233 SITE 1 AE5 3 THR A 65 PHE A 70 OLA A1222 SITE 1 AE6 4 THR A 65 CYS A 71 OLC A1205 CLR A1211 SITE 1 AE7 5 ASP A 52 SER A 91 HOH A1319 HOH A1357 SITE 2 AE7 5 HOH A1380 CRYST1 40.320 180.490 142.480 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.024802 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005540 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007019 0.00000 ATOM 1 N ASP A -2 23.465 151.966 3.175 1.00122.46 N ANISOU 1 N ASP A -2 16033 14464 16031 138 381 -1299 N ATOM 2 CA ASP A -2 23.152 152.885 2.043 1.00118.35 C ANISOU 2 CA ASP A -2 15588 14025 15356 104 342 -1359 C ATOM 3 C ASP A -2 22.580 154.202 2.574 1.00123.04 C ANISOU 3 C ASP A -2 16146 14723 15882 91 270 -1271 C ATOM 4 O ASP A -2 22.565 154.432 3.781 1.00130.35 O ANISOU 4 O ASP A -2 16993 15662 16872 111 261 -1170 O ATOM 5 CB ASP A -2 22.185 152.216 1.060 1.00105.70 C ANISOU 5 CB ASP A -2 14056 12374 13730 45 291 -1472 C ATOM 6 CG ASP A -2 22.888 151.269 0.103 1.00 97.91 C ANISOU 6 CG ASP A -2 13141 11311 12748 56 370 -1587 C ATOM 7 N GLY A -1 22.105 155.050 1.664 1.00114.19 N ANISOU 7 N GLY A -1 15085 13672 14630 58 217 -1310 N ATOM 8 CA GLY A -1 21.860 156.449 1.967 1.00 99.60 C ANISOU 8 CA GLY A -1 13215 11926 12703 56 169 -1234 C ATOM 9 C GLY A -1 23.040 157.293 1.521 1.00 86.98 C ANISOU 9 C GLY A -1 11646 10387 11014 92 236 -1227 C ATOM 10 O GLY A -1 24.188 156.839 1.584 1.00 87.05 O ANISOU 10 O GLY A -1 11647 10360 11067 134 328 -1235 O ATOM 11 N ALA A 0 22.774 158.507 1.053 1.00 76.00 N ANISOU 11 N ALA A 0 10290 9083 9505 76 193 -1211 N ATOM 12 CA ALA A 0 23.823 159.321 0.459 1.00 68.29 C ANISOU 12 CA ALA A 0 9354 8160 8435 102 258 -1212 C ATOM 13 C ALA A 0 24.994 159.473 1.433 1.00 63.00 C ANISOU 13 C ALA A 0 8605 7491 7841 154 335 -1138 C ATOM 14 O ALA A 0 24.776 159.677 2.634 1.00 65.44 O ANISOU 14 O ALA A 0 8834 7810 8222 165 304 -1054 O ATOM 15 CB ALA A 0 23.265 160.692 0.080 1.00 65.88 C ANISOU 15 CB ALA A 0 9078 7945 8009 78 191 -1179 C ATOM 16 N PRO A 1 26.238 159.375 0.968 1.00 55.66 N ANISOU 16 N PRO A 1 7695 6551 6902 188 435 -1167 N ATOM 17 CA PRO A 1 27.385 159.582 1.864 1.00 50.44 C ANISOU 17 CA PRO A 1 6954 5895 6318 237 499 -1097 C ATOM 18 C PRO A 1 27.255 160.893 2.621 1.00 45.50 C ANISOU 18 C PRO A 1 6278 5350 5660 237 450 -1002 C ATOM 19 O PRO A 1 26.987 161.944 2.015 1.00 42.11 O ANISOU 19 O PRO A 1 5896 4986 5120 214 425 -1001 O ATOM 20 CB PRO A 1 28.581 159.599 0.908 1.00 51.64 C ANISOU 20 CB PRO A 1 7151 6042 6428 261 607 -1153 C ATOM 21 CG PRO A 1 28.126 158.810 -0.282 1.00 54.25 C ANISOU 21 CG PRO A 1 7581 6327 6704 233 616 -1265 C ATOM 22 CD PRO A 1 26.660 159.045 -0.408 1.00 55.40 C ANISOU 22 CD PRO A 1 7761 6499 6790 181 496 -1269 C ATOM 23 N PRO A 2 27.418 160.869 3.950 1.00 47.11 N ANISOU 23 N PRO A 2 6393 5551 5957 261 435 -921 N ATOM 24 CA PRO A 2 27.218 162.102 4.742 1.00 45.05 C ANISOU 24 CA PRO A 2 6088 5364 5667 258 386 -836 C ATOM 25 C PRO A 2 28.101 163.269 4.339 1.00 37.47 C ANISOU 25 C PRO A 2 5136 4465 4635 269 429 -821 C ATOM 26 O PRO A 2 27.705 164.428 4.521 1.00 37.11 O ANISOU 26 O PRO A 2 5089 4484 4529 252 383 -777 O ATOM 27 CB PRO A 2 27.537 161.647 6.182 1.00 51.85 C ANISOU 27 CB PRO A 2 6860 6197 6643 290 384 -763 C ATOM 28 CG PRO A 2 27.244 160.181 6.200 1.00 54.57 C ANISOU 28 CG PRO A 2 7208 6453 7072 292 393 -802 C ATOM 29 CD PRO A 2 27.571 159.677 4.810 1.00 51.54 C ANISOU 29 CD PRO A 2 6898 6035 6648 286 449 -903 C ATOM 30 N ILE A 3 29.304 163.010 3.850 1.00 35.40 N ANISOU 30 N ILE A 3 4878 4182 4391 297 520 -853 N ATOM 31 CA ILE A 3 30.211 164.094 3.480 1.00 41.47 C ANISOU 31 CA ILE A 3 5649 5005 5105 306 572 -836 C ATOM 32 C ILE A 3 29.602 164.999 2.400 1.00 39.46 C ANISOU 32 C ILE A 3 5482 4800 4710 268 550 -864 C ATOM 33 O ILE A 3 30.000 166.166 2.266 1.00 36.78 O ANISOU 33 O ILE A 3 5144 4515 4315 265 565 -829 O ATOM 34 CB ILE A 3 31.564 163.523 3.007 1.00 50.88 C ANISOU 34 CB ILE A 3 6830 6154 6347 341 686 -877 C ATOM 35 CG1 ILE A 3 32.646 164.607 3.047 1.00 56.70 C ANISOU 35 CG1 ILE A 3 7529 6940 7074 356 740 -838 C ATOM 36 CG2 ILE A 3 31.427 162.943 1.593 1.00 53.58 C ANISOU 36 CG2 ILE A 3 7275 6466 6619 325 737 -976 C ATOM 37 CD1 ILE A 3 33.957 164.240 2.347 1.00 63.75 C ANISOU 37 CD1 ILE A 3 8419 7800 8002 386 864 -884 C ATOM 38 N MET A 4 28.683 164.477 1.578 1.00 38.38 N ANISOU 38 N MET A 4 5424 4643 4514 238 514 -927 N ATOM 39 CA MET A 4 28.112 165.315 0.513 1.00 36.73 C ANISOU 39 CA MET A 4 5305 4483 4166 204 485 -950 C ATOM 40 C MET A 4 27.272 166.427 1.109 1.00 34.58 C ANISOU 40 C MET A 4 5006 4268 3865 186 393 -878 C ATOM 41 O MET A 4 27.538 167.613 0.888 1.00 33.17 O ANISOU 41 O MET A 4 4841 4143 3620 183 402 -842 O ATOM 42 CB MET A 4 27.288 164.470 -0.471 1.00 36.22 C ANISOU 42 CB MET A 4 5330 4384 4047 175 453 -1037 C ATOM 43 CG MET A 4 28.144 163.515 -1.181 1.00 36.95 C ANISOU 43 CG MET A 4 5463 4422 4152 193 553 -1116 C ATOM 44 SD MET A 4 27.273 162.559 -2.444 1.00 42.71 S ANISOU 44 SD MET A 4 6312 5111 4803 155 521 -1232 S ATOM 45 CE MET A 4 27.070 163.781 -3.750 1.00 45.90 C ANISOU 45 CE MET A 4 6836 5592 5013 127 507 -1245 C ATOM 46 N GLY A 5 26.279 166.067 1.921 1.00 32.56 N ANISOU 46 N GLY A 5 4706 3999 3667 175 312 -854 N ATOM 47 CA GLY A 5 25.518 167.086 2.619 1.00 32.31 C ANISOU 47 CA GLY A 5 4636 4014 3624 162 237 -785 C ATOM 48 C GLY A 5 26.394 167.965 3.500 1.00 33.39 C ANISOU 48 C GLY A 5 4707 4186 3794 188 272 -714 C ATOM 49 O GLY A 5 26.188 169.180 3.590 1.00 32.61 O ANISOU 49 O GLY A 5 4607 4137 3645 179 243 -670 O ATOM 50 N ASER A 6 27.380 167.362 4.173 0.50 34.64 N ANISOU 50 N ASER A 6 4807 4313 4042 220 330 -703 N ATOM 51 N BSER A 6 27.392 167.362 4.150 0.50 34.66 N ANISOU 51 N BSER A 6 4810 4315 4043 219 331 -704 N ATOM 52 CA ASER A 6 28.254 168.134 5.057 0.50 32.79 C ANISOU 52 CA ASER A 6 4504 4109 3846 242 355 -640 C ATOM 53 CA BSER A 6 28.264 168.109 5.052 0.50 32.78 C ANISOU 53 CA BSER A 6 4503 4107 3846 242 356 -641 C ATOM 54 C ASER A 6 29.039 169.185 4.279 0.50 31.29 C ANISOU 54 C ASER A 6 4346 3959 3585 240 409 -641 C ATOM 55 C BSER A 6 29.097 169.146 4.302 0.50 31.34 C ANISOU 55 C BSER A 6 4349 3962 3596 241 412 -641 C ATOM 56 O ASER A 6 29.273 170.288 4.778 0.50 30.17 O ANISOU 56 O ASER A 6 4171 3858 3435 239 398 -588 O ATOM 57 O BSER A 6 29.411 170.206 4.849 0.50 30.15 O ANISOU 57 O BSER A 6 4160 3852 3444 243 405 -588 O ATOM 58 CB ASER A 6 29.224 167.209 5.800 0.50 34.65 C ANISOU 58 CB ASER A 6 4673 4300 4191 279 403 -632 C ATOM 59 CB BSER A 6 29.179 167.138 5.801 0.50 34.66 C ANISOU 59 CB BSER A 6 4675 4298 4194 279 401 -633 C ATOM 60 OG ASER A 6 28.575 166.515 6.852 0.50 34.61 O ANISOU 60 OG ASER A 6 4625 4268 4257 283 351 -601 O ATOM 61 OG BSER A 6 30.035 167.830 6.679 0.50 34.31 O ANISOU 61 OG BSER A 6 4563 4283 4192 299 414 -575 O ATOM 62 N SER A 7 29.463 168.859 3.060 1.00 31.81 N ANISOU 62 N SER A 7 4479 4008 3599 237 472 -702 N ATOM 63 CA ASER A 7 30.246 169.815 2.282 0.50 31.61 C ANISOU 63 CA ASER A 7 4488 4015 3506 234 537 -700 C ATOM 64 CA BSER A 7 30.244 169.813 2.280 0.50 31.61 C ANISOU 64 CA BSER A 7 4489 4016 3506 234 537 -701 C ATOM 65 C SER A 7 29.417 171.045 1.929 1.00 30.17 C ANISOU 65 C SER A 7 4355 3885 3225 205 476 -670 C ATOM 66 O SER A 7 29.931 172.166 1.937 1.00 28.43 O ANISOU 66 O SER A 7 4124 3698 2979 203 502 -629 O ATOM 67 CB ASER A 7 30.796 169.148 1.019 0.50 34.39 C ANISOU 67 CB ASER A 7 4914 4338 3814 237 624 -776 C ATOM 68 CB BSER A 7 30.779 169.138 1.016 0.50 34.38 C ANISOU 68 CB BSER A 7 4914 4337 3812 237 622 -776 C ATOM 69 OG ASER A 7 31.716 168.116 1.345 0.50 35.17 O ANISOU 69 OG ASER A 7 4960 4387 4018 270 692 -800 O ATOM 70 OG BSER A 7 29.720 168.669 0.201 0.50 37.01 O ANISOU 70 OG BSER A 7 5336 4661 4066 211 572 -829 O ATOM 71 N VAL A 8 28.128 170.859 1.628 1.00 29.91 N ANISOU 71 N VAL A 8 4370 3853 3140 182 393 -687 N ATOM 72 CA VAL A 8 27.259 172.008 1.353 1.00 30.30 C ANISOU 72 CA VAL A 8 4458 3948 3109 159 325 -652 C ATOM 73 C VAL A 8 27.118 172.878 2.590 1.00 30.08 C ANISOU 73 C VAL A 8 4347 3944 3137 164 285 -579 C ATOM 74 O VAL A 8 27.229 174.107 2.522 1.00 30.28 O ANISOU 74 O VAL A 8 4379 4004 3121 158 284 -538 O ATOM 75 CB VAL A 8 25.883 171.537 0.844 1.00 30.53 C ANISOU 75 CB VAL A 8 4540 3968 3091 134 235 -687 C ATOM 76 CG1 VAL A 8 24.959 172.730 0.621 1.00 32.57 C ANISOU 76 CG1 VAL A 8 4827 4270 3279 115 157 -644 C ATOM 77 CG2 VAL A 8 26.039 170.742 -0.449 1.00 29.52 C ANISOU 77 CG2 VAL A 8 4507 3818 2892 125 272 -766 C ATOM 78 N TYR A 9 26.822 172.253 3.735 1.00 29.03 N ANISOU 78 N TYR A 9 4143 3791 3095 174 251 -563 N ATOM 79 CA TYR A 9 26.625 172.983 4.983 1.00 26.87 C ANISOU 79 CA TYR A 9 3798 3540 2871 179 213 -500 C ATOM 80 C TYR A 9 27.855 173.816 5.340 1.00 26.50 C ANISOU 80 C TYR A 9 3712 3513 2842 193 271 -467 C ATOM 81 O TYR A 9 27.752 174.996 5.667 1.00 28.70 O ANISOU 81 O TYR A 9 3978 3824 3103 185 251 -424 O ATOM 82 CB TYR A 9 26.296 171.990 6.110 1.00 27.07 C ANISOU 82 CB TYR A 9 3761 3534 2988 191 185 -491 C ATOM 83 CG TYR A 9 26.397 172.602 7.487 1.00 26.70 C ANISOU 83 CG TYR A 9 3644 3508 2993 201 165 -431 C ATOM 84 CD1 TYR A 9 25.555 173.610 7.876 1.00 27.67 C ANISOU 84 CD1 TYR A 9 3762 3662 3091 187 112 -394 C ATOM 85 CD2 TYR A 9 27.331 172.138 8.412 1.00 27.26 C ANISOU 85 CD2 TYR A 9 3654 3564 3139 226 197 -411 C ATOM 86 CE1 TYR A 9 25.656 174.178 9.127 1.00 30.36 C ANISOU 86 CE1 TYR A 9 4045 4019 3470 195 98 -346 C ATOM 87 CE2 TYR A 9 27.415 172.688 9.646 1.00 28.80 C ANISOU 87 CE2 TYR A 9 3795 3780 3368 233 173 -360 C ATOM 88 CZ TYR A 9 26.587 173.715 9.994 1.00 31.33 C ANISOU 88 CZ TYR A 9 4118 4132 3654 216 127 -331 C ATOM 89 OH TYR A 9 26.701 174.266 11.222 1.00 32.55 O ANISOU 89 OH TYR A 9 4225 4305 3836 222 108 -287 O ATOM 90 N ILE A 10 29.035 173.212 5.271 1.00 24.89 N ANISOU 90 N ILE A 10 3486 3288 2684 212 345 -487 N ATOM 91 CA ILE A 10 30.275 173.884 5.669 1.00 26.89 C ANISOU 91 CA ILE A 10 3687 3555 2975 225 400 -459 C ATOM 92 C ILE A 10 30.589 175.039 4.740 1.00 26.77 C ANISOU 92 C ILE A 10 3721 3567 2883 208 439 -453 C ATOM 93 O ILE A 10 31.029 176.098 5.186 1.00 27.43 O ANISOU 93 O ILE A 10 3768 3673 2979 203 444 -413 O ATOM 94 CB ILE A 10 31.445 172.871 5.696 1.00 30.40 C ANISOU 94 CB ILE A 10 4092 3964 3495 253 472 -486 C ATOM 95 CG1 ILE A 10 31.263 171.917 6.880 1.00 32.23 C ANISOU 95 CG1 ILE A 10 4262 4170 3815 273 429 -470 C ATOM 96 CG2 ILE A 10 32.801 173.589 5.799 1.00 32.06 C ANISOU 96 CG2 ILE A 10 4252 4187 3743 262 538 -466 C ATOM 97 CD1 ILE A 10 32.272 170.723 6.875 1.00 34.85 C ANISOU 97 CD1 ILE A 10 4557 4455 4230 306 492 -498 C ATOM 98 N THR A 11 30.394 174.842 3.439 1.00 26.66 N ANISOU 98 N THR A 11 3794 3548 2788 197 468 -494 N ATOM 99 CA THR A 11 30.665 175.895 2.455 1.00 26.77 C ANISOU 99 CA THR A 11 3870 3586 2717 180 510 -485 C ATOM 100 C THR A 11 29.780 177.102 2.703 1.00 26.24 C ANISOU 100 C THR A 11 3813 3549 2607 162 436 -435 C ATOM 101 O THR A 11 30.236 178.246 2.626 1.00 27.89 O ANISOU 101 O THR A 11 4019 3776 2800 154 464 -399 O ATOM 102 CB THR A 11 30.425 175.356 1.043 1.00 30.25 C ANISOU 102 CB THR A 11 4416 4016 3062 171 540 -539 C ATOM 103 OG1 THR A 11 31.339 174.288 0.763 1.00 29.65 O ANISOU 103 OG1 THR A 11 4332 3906 3029 189 625 -589 O ATOM 104 CG2 THR A 11 30.621 176.445 -0.032 1.00 35.66 C ANISOU 104 CG2 THR A 11 5181 4726 3642 153 581 -523 C ATOM 105 N VAL A 12 28.498 176.858 3.005 1.00 25.83 N ANISOU 105 N VAL A 12 3769 3499 2545 156 343 -433 N ATOM 106 CA VAL A 12 27.572 177.942 3.268 1.00 27.37 C ANISOU 106 CA VAL A 12 3968 3718 2712 143 272 -388 C ATOM 107 C VAL A 12 27.927 178.646 4.569 1.00 26.43 C ANISOU 107 C VAL A 12 3764 3610 2669 150 266 -343 C ATOM 108 O VAL A 12 27.890 179.880 4.646 1.00 25.38 O ANISOU 108 O VAL A 12 3633 3494 2519 141 258 -305 O ATOM 109 CB VAL A 12 26.117 177.406 3.271 1.00 30.23 C ANISOU 109 CB VAL A 12 4349 4076 3060 136 178 -402 C ATOM 110 CG1 VAL A 12 25.161 178.429 3.850 1.00 32.69 C ANISOU 110 CG1 VAL A 12 4638 4406 3376 130 106 -353 C ATOM 111 CG2 VAL A 12 25.704 176.974 1.863 1.00 32.54 C ANISOU 111 CG2 VAL A 12 4739 4365 3258 123 170 -445 C ATOM 112 N GLU A 13 28.292 177.885 5.611 1.00 26.31 N ANISOU 112 N GLU A 13 3678 3581 2738 166 268 -347 N ATOM 113 CA GLU A 13 28.716 178.505 6.861 1.00 24.36 C ANISOU 113 CA GLU A 13 3357 3345 2556 171 260 -309 C ATOM 114 C GLU A 13 29.926 179.412 6.652 1.00 24.39 C ANISOU 114 C GLU A 13 3346 3357 2565 167 325 -295 C ATOM 115 O GLU A 13 29.982 180.515 7.206 1.00 24.77 O ANISOU 115 O GLU A 13 3368 3420 2624 158 310 -261 O ATOM 116 CB GLU A 13 29.056 177.433 7.915 1.00 24.73 C ANISOU 116 CB GLU A 13 3337 3373 2684 191 255 -315 C ATOM 117 CG GLU A 13 27.873 176.695 8.457 1.00 25.73 C ANISOU 117 CG GLU A 13 3462 3490 2824 193 191 -316 C ATOM 118 CD GLU A 13 27.212 177.433 9.617 1.00 26.60 C ANISOU 118 CD GLU A 13 3536 3618 2953 189 138 -275 C ATOM 119 OE1 GLU A 13 27.028 176.827 10.702 1.00 27.65 O ANISOU 119 OE1 GLU A 13 3627 3743 3137 200 115 -262 O ATOM 120 OE2 GLU A 13 26.885 178.620 9.461 1.00 26.74 O ANISOU 120 OE2 GLU A 13 3571 3656 2934 176 123 -255 O ATOM 121 N LEU A 14 30.903 178.976 5.850 1.00 24.90 N ANISOU 121 N LEU A 14 3425 3409 2627 172 403 -322 N ATOM 122 CA LEU A 14 32.103 179.787 5.661 1.00 25.70 C ANISOU 122 CA LEU A 14 3503 3515 2749 166 474 -309 C ATOM 123 C LEU A 14 31.800 181.047 4.864 1.00 25.93 C ANISOU 123 C LEU A 14 3594 3558 2701 143 483 -284 C ATOM 124 O LEU A 14 32.339 182.126 5.158 1.00 28.84 O ANISOU 124 O LEU A 14 3932 3932 3093 131 503 -254 O ATOM 125 CB LEU A 14 33.208 178.967 4.987 1.00 27.58 C ANISOU 125 CB LEU A 14 3738 3732 3010 179 566 -345 C ATOM 126 CG LEU A 14 33.827 177.856 5.899 1.00 32.52 C ANISOU 126 CG LEU A 14 4281 4337 3738 206 567 -359 C ATOM 127 CD1 LEU A 14 34.813 177.014 5.092 1.00 37.13 C ANISOU 127 CD1 LEU A 14 4868 4894 4346 222 663 -400 C ATOM 128 CD2 LEU A 14 34.486 178.455 7.110 1.00 33.65 C ANISOU 128 CD2 LEU A 14 4332 4491 3961 209 545 -324 C ATOM 129 N ALA A 15 30.911 180.949 3.864 1.00 26.17 N ANISOU 129 N ALA A 15 3713 3590 2639 136 463 -295 N ATOM 130 CA ALA A 15 30.474 182.143 3.145 1.00 27.43 C ANISOU 130 CA ALA A 15 3937 3763 2723 118 455 -263 C ATOM 131 C ALA A 15 29.853 183.152 4.097 1.00 27.91 C ANISOU 131 C ALA A 15 3958 3832 2814 113 388 -220 C ATOM 132 O ALA A 15 30.125 184.364 4.016 1.00 27.02 O ANISOU 132 O ALA A 15 3849 3722 2696 100 408 -185 O ATOM 133 CB ALA A 15 29.476 181.745 2.052 1.00 28.17 C ANISOU 133 CB ALA A 15 4128 3859 2715 114 418 -282 C ATOM 134 N ILE A 16 29.000 182.679 5.003 1.00 27.98 N ANISOU 134 N ILE A 16 3929 3844 2858 122 313 -223 N ATOM 135 CA ILE A 16 28.353 183.591 5.951 1.00 26.87 C ANISOU 135 CA ILE A 16 3753 3710 2747 119 254 -189 C ATOM 136 C ILE A 16 29.379 184.234 6.871 1.00 26.71 C ANISOU 136 C ILE A 16 3664 3690 2797 115 288 -174 C ATOM 137 O ILE A 16 29.291 185.435 7.180 1.00 26.77 O ANISOU 137 O ILE A 16 3664 3698 2811 104 278 -144 O ATOM 138 CB ILE A 16 27.279 182.859 6.755 1.00 27.03 C ANISOU 138 CB ILE A 16 3746 3730 2794 129 181 -197 C ATOM 139 CG1 ILE A 16 26.126 182.440 5.839 1.00 30.03 C ANISOU 139 CG1 ILE A 16 4190 4109 3111 127 133 -209 C ATOM 140 CG2 ILE A 16 26.757 183.721 7.929 1.00 25.60 C ANISOU 140 CG2 ILE A 16 3518 3554 2654 128 137 -167 C ATOM 141 CD1 ILE A 16 25.176 181.488 6.497 1.00 32.74 C ANISOU 141 CD1 ILE A 16 4504 4446 3489 134 75 -225 C ATOM 142 N ALA A 17 30.348 183.451 7.330 1.00 26.20 N ANISOU 142 N ALA A 17 3546 3621 2788 125 323 -195 N ATOM 143 CA ALA A 17 31.392 183.970 8.215 1.00 26.63 C ANISOU 143 CA ALA A 17 3528 3676 2914 120 346 -185 C ATOM 144 C ALA A 17 32.154 185.119 7.577 1.00 27.33 C ANISOU 144 C ALA A 17 3630 3760 2996 100 406 -167 C ATOM 145 O ALA A 17 32.421 186.144 8.227 1.00 28.52 O ANISOU 145 O ALA A 17 3745 3910 3183 86 397 -148 O ATOM 146 CB ALA A 17 32.358 182.853 8.581 1.00 27.02 C ANISOU 146 CB ALA A 17 3523 3719 3025 138 376 -209 C ATOM 147 N VAL A 18 32.561 184.948 6.314 1.00 27.96 N ANISOU 147 N VAL A 18 3761 3832 3030 96 473 -176 N ATOM 148 CA VAL A 18 33.310 185.997 5.617 1.00 29.51 C ANISOU 148 CA VAL A 18 3975 4019 3217 75 544 -156 C ATOM 149 C VAL A 18 32.497 187.289 5.578 1.00 28.43 C ANISOU 149 C VAL A 18 3877 3882 3043 60 504 -117 C ATOM 150 O VAL A 18 33.005 188.391 5.844 1.00 29.70 O ANISOU 150 O VAL A 18 4011 4031 3241 41 527 -94 O ATOM 151 CB VAL A 18 33.697 185.534 4.195 1.00 33.94 C ANISOU 151 CB VAL A 18 4605 4575 3716 75 625 -171 C ATOM 152 CG1 VAL A 18 34.279 186.668 3.387 1.00 36.01 C ANISOU 152 CG1 VAL A 18 4903 4826 3952 52 700 -141 C ATOM 153 CG2 VAL A 18 34.716 184.399 4.252 1.00 36.07 C ANISOU 153 CG2 VAL A 18 4824 4836 4045 91 684 -210 C ATOM 154 N LEU A 19 31.226 187.180 5.191 1.00 26.04 N ANISOU 154 N LEU A 19 3638 3586 2670 68 445 -110 N ATOM 155 CA LEU A 19 30.396 188.373 5.036 1.00 26.55 C ANISOU 155 CA LEU A 19 3743 3646 2701 59 406 -70 C ATOM 156 C LEU A 19 30.075 189.002 6.373 1.00 26.98 C ANISOU 156 C LEU A 19 3733 3697 2821 58 353 -60 C ATOM 157 O LEU A 19 29.969 190.226 6.457 1.00 26.86 O ANISOU 157 O LEU A 19 3723 3667 2815 45 352 -30 O ATOM 158 CB LEU A 19 29.100 188.031 4.305 1.00 27.94 C ANISOU 158 CB LEU A 19 3992 3829 2795 70 346 -66 C ATOM 159 CG LEU A 19 29.293 187.552 2.866 1.00 31.60 C ANISOU 159 CG LEU A 19 4541 4296 3170 68 392 -76 C ATOM 160 CD1 LEU A 19 27.985 186.956 2.306 1.00 34.28 C ANISOU 160 CD1 LEU A 19 4942 4646 3438 78 314 -85 C ATOM 161 CD2 LEU A 19 29.824 188.659 1.958 1.00 32.19 C ANISOU 161 CD2 LEU A 19 4672 4359 3201 51 457 -36 C ATOM 162 N ALA A 20 29.907 188.199 7.423 1.00 27.45 N ANISOU 162 N ALA A 20 3737 3768 2925 71 311 -86 N ATOM 163 CA ALA A 20 29.649 188.758 8.748 1.00 26.60 C ANISOU 163 CA ALA A 20 3576 3660 2872 69 267 -81 C ATOM 164 C ALA A 20 30.838 189.562 9.233 1.00 26.86 C ANISOU 164 C ALA A 20 3559 3682 2964 50 308 -79 C ATOM 165 O ALA A 20 30.669 190.624 9.850 1.00 28.39 O ANISOU 165 O ALA A 20 3737 3865 3184 38 289 -66 O ATOM 166 CB ALA A 20 29.332 187.646 9.747 1.00 25.84 C ANISOU 166 CB ALA A 20 3437 3577 2803 87 223 -105 C ATOM 167 N ILE A 21 32.047 189.055 8.991 1.00 26.31 N ANISOU 167 N ILE A 21 3459 3614 2924 46 365 -95 N ATOM 168 CA ILE A 21 33.252 189.769 9.420 1.00 26.78 C ANISOU 168 CA ILE A 21 3460 3662 3053 24 403 -95 C ATOM 169 C ILE A 21 33.415 191.075 8.646 1.00 28.47 C ANISOU 169 C ILE A 21 3712 3853 3254 0 450 -65 C ATOM 170 O ILE A 21 33.595 192.143 9.234 1.00 29.96 O ANISOU 170 O ILE A 21 3873 4025 3484 -20 441 -57 O ATOM 171 CB ILE A 21 34.480 188.865 9.259 1.00 29.74 C ANISOU 171 CB ILE A 21 3787 4041 3473 29 456 -117 C ATOM 172 CG1 ILE A 21 34.398 187.732 10.290 1.00 29.99 C ANISOU 172 CG1 ILE A 21 3771 4090 3534 53 400 -139 C ATOM 173 CG2 ILE A 21 35.792 189.674 9.448 1.00 32.79 C ANISOU 173 CG2 ILE A 21 4111 4411 3936 2 506 -116 C ATOM 174 CD1 ILE A 21 35.355 186.552 9.984 1.00 32.34 C ANISOU 174 CD1 ILE A 21 4032 4387 3869 70 447 -161 C ATOM 175 N LEU A 22 33.344 191.009 7.315 1.00 28.49 N ANISOU 175 N LEU A 22 3783 3850 3194 0 500 -49 N ATOM 176 CA LEU A 22 33.595 192.177 6.496 1.00 29.23 C ANISOU 176 CA LEU A 22 3918 3918 3270 -23 555 -14 C ATOM 177 C LEU A 22 32.598 193.288 6.788 1.00 29.41 C ANISOU 177 C LEU A 22 3969 3925 3280 -26 501 16 C ATOM 178 O LEU A 22 32.982 194.437 6.998 1.00 30.37 O ANISOU 178 O LEU A 22 4074 4019 3446 -50 523 34 O ATOM 179 CB LEU A 22 33.536 191.800 5.016 1.00 30.97 C ANISOU 179 CB LEU A 22 4223 4140 3404 -18 611 -1 C ATOM 180 CG LEU A 22 34.672 190.946 4.488 1.00 36.43 C ANISOU 180 CG LEU A 22 4896 4836 4110 -18 695 -27 C ATOM 181 CD1 LEU A 22 34.429 190.530 3.025 1.00 38.35 C ANISOU 181 CD1 LEU A 22 5241 5083 4246 -12 744 -20 C ATOM 182 CD2 LEU A 22 35.971 191.708 4.643 1.00 40.32 C ANISOU 182 CD2 LEU A 22 5326 5305 4687 -47 771 -19 C ATOM 183 N GLY A 23 31.315 192.964 6.805 1.00 28.33 N ANISOU 183 N GLY A 23 3871 3801 3092 -4 432 20 N ATOM 184 CA GLY A 23 30.317 194.000 6.950 1.00 27.69 C ANISOU 184 CA GLY A 23 3818 3701 3002 -2 385 50 C ATOM 185 C GLY A 23 30.367 194.660 8.316 1.00 27.18 C ANISOU 185 C GLY A 23 3688 3624 3014 -11 355 35 C ATOM 186 O GLY A 23 30.150 195.867 8.439 1.00 28.70 O ANISOU 186 O GLY A 23 3889 3785 3229 -22 354 59 O ATOM 187 N ASN A 24 30.650 193.879 9.357 1.00 26.50 N ANISOU 187 N ASN A 24 3541 3561 2966 -5 329 -4 N ATOM 188 CA ASN A 24 30.668 194.418 10.698 1.00 26.80 C ANISOU 188 CA ASN A 24 3527 3592 3062 -14 295 -23 C ATOM 189 C ASN A 24 31.988 195.105 11.041 1.00 27.59 C ANISOU 189 C ASN A 24 3578 3675 3230 -46 338 -34 C ATOM 190 O ASN A 24 31.973 196.027 11.840 1.00 27.71 O ANISOU 190 O ASN A 24 3572 3670 3288 -61 320 -42 O ATOM 191 CB ASN A 24 30.292 193.320 11.686 1.00 26.89 C ANISOU 191 CB ASN A 24 3506 3636 3076 7 243 -53 C ATOM 192 CG ASN A 24 28.802 193.046 11.648 1.00 26.51 C ANISOU 192 CG ASN A 24 3495 3594 2985 31 194 -43 C ATOM 193 OD1 ASN A 24 28.006 193.886 12.086 1.00 26.75 O ANISOU 193 OD1 ASN A 24 3533 3606 3025 33 167 -34 O ATOM 194 ND2 ASN A 24 28.406 191.924 11.071 1.00 26.29 N ANISOU 194 ND2 ASN A 24 3489 3584 2915 49 184 -45 N ATOM 195 N VAL A 25 33.121 194.699 10.444 1.00 26.99 N ANISOU 195 N VAL A 25 3482 3602 3170 -57 397 -36 N ATOM 196 CA VAL A 25 34.325 195.525 10.520 1.00 29.19 C ANISOU 196 CA VAL A 25 3716 3855 3521 -92 447 -39 C ATOM 197 C VAL A 25 34.054 196.897 9.931 1.00 30.63 C ANISOU 197 C VAL A 25 3945 3995 3700 -112 477 -2 C ATOM 198 O VAL A 25 34.523 197.918 10.442 1.00 33.15 O ANISOU 198 O VAL A 25 4231 4282 4083 -141 485 -7 O ATOM 199 CB VAL A 25 35.486 194.819 9.807 1.00 31.91 C ANISOU 199 CB VAL A 25 4034 4207 3883 -98 517 -43 C ATOM 200 CG1 VAL A 25 36.606 195.773 9.533 1.00 33.72 C ANISOU 200 CG1 VAL A 25 4229 4402 4181 -137 586 -34 C ATOM 201 CG2 VAL A 25 35.967 193.652 10.696 1.00 33.57 C ANISOU 201 CG2 VAL A 25 4175 4449 4129 -82 479 -81 C ATOM 202 N LEU A 26 33.316 196.944 8.826 1.00 30.41 N ANISOU 202 N LEU A 26 3995 3962 3598 -97 493 36 N ATOM 203 CA LEU A 26 33.001 198.226 8.209 1.00 30.93 C ANISOU 203 CA LEU A 26 4111 3984 3657 -111 519 81 C ATOM 204 C LEU A 26 32.206 199.115 9.159 1.00 31.32 C ANISOU 204 C LEU A 26 4152 4009 3740 -109 461 76 C ATOM 205 O LEU A 26 32.456 200.321 9.241 1.00 31.97 O ANISOU 205 O LEU A 26 4232 4045 3871 -134 485 91 O ATOM 206 CB LEU A 26 32.234 197.990 6.909 1.00 34.68 C ANISOU 206 CB LEU A 26 4677 4464 4035 -89 527 124 C ATOM 207 CG LEU A 26 31.893 199.149 5.989 1.00 42.28 C ANISOU 207 CG LEU A 26 5710 5385 4970 -97 556 184 C ATOM 208 CD1 LEU A 26 33.139 199.829 5.494 1.00 46.22 C ANISOU 208 CD1 LEU A 26 6201 5851 5512 -134 653 204 C ATOM 209 CD2 LEU A 26 31.056 198.629 4.811 1.00 46.04 C ANISOU 209 CD2 LEU A 26 6276 5881 5336 -70 540 218 C ATOM 210 N VAL A 27 31.234 198.546 9.874 1.00 32.03 N ANISOU 210 N VAL A 27 4238 4126 3807 -81 390 55 N ATOM 211 CA VAL A 27 30.484 199.328 10.864 1.00 30.74 C ANISOU 211 CA VAL A 27 4062 3940 3676 -78 342 43 C ATOM 212 C VAL A 27 31.427 199.952 11.900 1.00 29.94 C ANISOU 212 C VAL A 27 3901 3821 3655 -112 351 4 C ATOM 213 O VAL A 27 31.315 201.139 12.244 1.00 30.96 O ANISOU 213 O VAL A 27 4032 3904 3828 -128 355 5 O ATOM 214 CB VAL A 27 29.415 198.453 11.537 1.00 30.76 C ANISOU 214 CB VAL A 27 4061 3978 3647 -45 276 21 C ATOM 215 CG1 VAL A 27 28.779 199.194 12.715 1.00 30.59 C ANISOU 215 CG1 VAL A 27 4021 3935 3664 -43 240 -2 C ATOM 216 CG2 VAL A 27 28.307 198.033 10.539 1.00 31.82 C ANISOU 216 CG2 VAL A 27 4254 4122 3714 -14 255 58 C ATOM 217 N CYS A 28 32.309 199.140 12.476 1.00 28.77 N ANISOU 217 N CYS A 28 3697 3706 3528 -121 347 -33 N ATOM 218 CA CYS A 28 33.203 199.621 13.520 1.00 31.83 C ANISOU 218 CA CYS A 28 4023 4083 3989 -153 338 -74 C ATOM 219 C CYS A 28 34.140 200.698 12.992 1.00 34.86 C ANISOU 219 C CYS A 28 4394 4417 4433 -194 400 -59 C ATOM 220 O CYS A 28 34.422 201.695 13.678 1.00 37.80 O ANISOU 220 O CYS A 28 4743 4754 4866 -223 393 -82 O ATOM 221 CB CYS A 28 34.017 198.454 14.079 1.00 31.84 C ANISOU 221 CB CYS A 28 3967 4130 4002 -150 319 -107 C ATOM 222 SG CYS A 28 33.011 197.274 14.960 1.00 33.65 S ANISOU 222 SG CYS A 28 4204 4408 4174 -109 246 -127 S ATOM 223 N TRP A 29 34.648 200.491 11.774 1.00 35.24 N ANISOU 223 N TRP A 29 4460 4462 4468 -198 466 -23 N ATOM 224 CA TRP A 29 35.541 201.451 11.134 1.00 36.61 C ANISOU 224 CA TRP A 29 4626 4587 4697 -237 540 0 C ATOM 225 C TRP A 29 34.847 202.797 10.931 1.00 33.14 C ANISOU 225 C TRP A 29 4237 4090 4265 -245 547 32 C ATOM 226 O TRP A 29 35.445 203.858 11.179 1.00 32.98 O ANISOU 226 O TRP A 29 4191 4019 4322 -285 574 26 O ATOM 227 CB TRP A 29 36.024 200.860 9.808 1.00 52.37 C ANISOU 227 CB TRP A 29 6649 6595 6655 -233 614 37 C ATOM 228 CG TRP A 29 37.178 201.543 9.150 1.00 81.20 C ANISOU 228 CG TRP A 29 10279 10206 10369 -274 706 58 C ATOM 229 CD1 TRP A 29 37.676 202.772 9.438 1.00 92.43 C ANISOU 229 CD1 TRP A 29 11672 11572 11875 -316 730 58 C ATOM 230 CD2 TRP A 29 37.982 201.024 8.079 1.00 99.77 C ANISOU 230 CD2 TRP A 29 12635 12564 12709 -280 794 79 C ATOM 231 NE1 TRP A 29 38.741 203.057 8.619 1.00 99.59 N ANISOU 231 NE1 TRP A 29 12561 12450 12827 -349 828 83 N ATOM 232 CE2 TRP A 29 38.949 202.000 7.775 1.00103.19 C ANISOU 232 CE2 TRP A 29 13039 12946 13224 -327 873 96 C ATOM 233 CE3 TRP A 29 37.978 199.828 7.350 1.00107.27 C ANISOU 233 CE3 TRP A 29 13613 13557 13589 -251 819 83 C ATOM 234 CZ2 TRP A 29 39.903 201.821 6.774 1.00106.69 C ANISOU 234 CZ2 TRP A 29 13478 13380 13681 -344 981 120 C ATOM 235 CZ3 TRP A 29 38.927 199.652 6.357 1.00108.35 C ANISOU 235 CZ3 TRP A 29 13749 13685 13735 -267 925 102 C ATOM 236 CH2 TRP A 29 39.875 200.643 6.079 1.00107.58 C ANISOU 236 CH2 TRP A 29 13620 13536 13718 -312 1007 122 C ATOM 237 N ALA A 30 33.574 202.768 10.511 1.00 31.50 N ANISOU 237 N ALA A 30 4098 3885 3985 -208 518 65 N ATOM 238 CA ALA A 30 32.818 203.994 10.285 1.00 33.96 C ANISOU 238 CA ALA A 30 4458 4139 4306 -207 520 102 C ATOM 239 C ALA A 30 32.652 204.801 11.575 1.00 34.96 C ANISOU 239 C ALA A 30 4548 4234 4501 -222 481 55 C ATOM 240 O ALA A 30 32.779 206.025 11.567 1.00 37.57 O ANISOU 240 O ALA A 30 4886 4499 4889 -246 509 67 O ATOM 241 CB ALA A 30 31.444 203.666 9.692 1.00 34.13 C ANISOU 241 CB ALA A 30 4548 4177 4245 -160 482 141 C ATOM 242 N VAL A 31 32.340 204.136 12.689 1.00 32.52 N ANISOU 242 N VAL A 31 4206 3967 4183 -207 419 2 N ATOM 243 CA VAL A 31 32.158 204.853 13.951 1.00 32.78 C ANISOU 243 CA VAL A 31 4215 3974 4266 -220 384 -49 C ATOM 244 C VAL A 31 33.492 205.432 14.412 1.00 34.22 C ANISOU 244 C VAL A 31 4341 4129 4532 -274 407 -86 C ATOM 245 O VAL A 31 33.557 206.527 14.968 1.00 34.65 O ANISOU 245 O VAL A 31 4390 4130 4647 -301 408 -111 O ATOM 246 CB VAL A 31 31.535 203.922 15.001 1.00 33.01 C ANISOU 246 CB VAL A 31 4230 4058 4254 -191 318 -93 C ATOM 247 CG1 VAL A 31 31.472 204.597 16.380 1.00 35.07 C ANISOU 247 CG1 VAL A 31 4471 4298 4557 -209 285 -154 C ATOM 248 CG2 VAL A 31 30.119 203.486 14.555 1.00 31.82 C ANISOU 248 CG2 VAL A 31 4128 3922 4038 -142 296 -57 C ATOM 249 N TRP A 32 34.568 204.688 14.204 1.00 36.11 N ANISOU 249 N TRP A 32 4535 4403 4782 -291 425 -93 N ATOM 250 CA TRP A 32 35.894 205.162 14.573 1.00 39.24 C ANISOU 250 CA TRP A 32 4865 4776 5267 -344 445 -126 C ATOM 251 C TRP A 32 36.280 206.410 13.791 1.00 42.16 C ANISOU 251 C TRP A 32 5250 5070 5699 -379 517 -89 C ATOM 252 O TRP A 32 36.876 207.343 14.344 1.00 42.04 O ANISOU 252 O TRP A 32 5199 5006 5769 -424 521 -123 O ATOM 253 CB TRP A 32 36.919 204.046 14.332 1.00 44.75 C ANISOU 253 CB TRP A 32 5508 5525 5971 -347 459 -131 C ATOM 254 CG TRP A 32 38.349 204.519 14.481 1.00 56.20 C ANISOU 254 CG TRP A 32 6882 6947 7526 -402 490 -155 C ATOM 255 CD1 TRP A 32 39.159 205.028 13.502 1.00 59.73 C ANISOU 255 CD1 TRP A 32 7315 7352 8029 -434 577 -119 C ATOM 256 CD2 TRP A 32 39.123 204.526 15.682 1.00 65.83 C ANISOU 256 CD2 TRP A 32 8026 8178 8810 -432 431 -219 C ATOM 257 NE1 TRP A 32 40.387 205.346 14.022 1.00 61.35 N ANISOU 257 NE1 TRP A 32 7432 7540 8340 -484 579 -159 N ATOM 258 CE2 TRP A 32 40.391 205.052 15.359 1.00 64.84 C ANISOU 258 CE2 TRP A 32 7834 8014 8788 -483 484 -222 C ATOM 259 CE3 TRP A 32 38.871 204.138 16.997 1.00 75.65 C ANISOU 259 CE3 TRP A 32 9254 9459 10031 -421 340 -274 C ATOM 260 CZ2 TRP A 32 41.396 205.200 16.300 1.00 71.37 C ANISOU 260 CZ2 TRP A 32 8576 8841 9702 -524 437 -279 C ATOM 261 CZ3 TRP A 32 39.875 204.287 17.934 1.00 81.37 C ANISOU 261 CZ3 TRP A 32 9903 10185 10829 -460 292 -329 C ATOM 262 CH2 TRP A 32 41.120 204.811 17.580 1.00 78.90 C ANISOU 262 CH2 TRP A 32 9520 9835 10624 -511 336 -333 C ATOM 263 N LEU A 33 35.940 206.443 12.505 1.00 45.29 N ANISOU 263 N LEU A 33 5703 5453 6052 -361 573 -19 N ATOM 264 CA LEU A 33 36.404 207.486 11.599 1.00 49.42 C ANISOU 264 CA LEU A 33 6246 5906 6624 -394 654 30 C ATOM 265 C LEU A 33 35.611 208.773 11.764 1.00 43.32 C ANISOU 265 C LEU A 33 5518 5063 5880 -396 648 44 C ATOM 266 O LEU A 33 36.169 209.866 11.653 1.00 43.87 O ANISOU 266 O LEU A 33 5577 5061 6032 -439 695 53 O ATOM 267 CB LEU A 33 36.287 206.999 10.154 1.00 60.32 C ANISOU 267 CB LEU A 33 7684 7303 7930 -371 714 101 C ATOM 268 CG LEU A 33 37.517 207.055 9.255 1.00 71.07 C ANISOU 268 CG LEU A 33 9025 8647 9332 -408 812 131 C ATOM 269 CD1 LEU A 33 38.633 206.199 9.828 1.00 74.17 C ANISOU 269 CD1 LEU A 33 9323 9085 9775 -428 807 74 C ATOM 270 CD2 LEU A 33 37.139 206.593 7.846 1.00 74.53 C ANISOU 270 CD2 LEU A 33 9545 9103 9669 -378 863 201 C ATOM 271 N ASN A 34 34.310 208.665 12.000 1.00 38.90 N ANISOU 271 N ASN A 34 5006 4516 5260 -349 594 50 N ATOM 272 CA ASN A 34 33.387 209.775 11.845 1.00 39.15 C ANISOU 272 CA ASN A 34 5091 4479 5306 -335 596 83 C ATOM 273 C ASN A 34 32.833 210.198 13.197 1.00 38.18 C ANISOU 273 C ASN A 34 4948 4339 5218 -332 538 15 C ATOM 274 O ASN A 34 31.969 209.517 13.762 1.00 36.51 O ANISOU 274 O ASN A 34 4745 4177 4952 -292 481 -10 O ATOM 275 CB ASN A 34 32.264 209.370 10.895 1.00 40.25 C ANISOU 275 CB ASN A 34 5301 4639 5353 -280 584 151 C ATOM 276 CG ASN A 34 31.333 210.515 10.573 1.00 44.44 C ANISOU 276 CG ASN A 34 5885 5095 5904 -261 587 200 C ATOM 277 OD1 ASN A 34 31.414 211.577 11.186 1.00 49.10 O ANISOU 277 OD1 ASN A 34 6462 5618 6578 -284 596 175 O ATOM 278 ND2 ASN A 34 30.419 210.294 9.633 1.00 43.18 N ANISOU 278 ND2 ASN A 34 5789 4947 5672 -217 574 268 N ATOM 279 N SER A 35 33.260 211.376 13.677 1.00 41.08 N ANISOU 279 N SER A 35 5298 4632 5678 -373 558 -14 N ATOM 280 CA ASER A 35 32.820 211.824 14.990 0.50 42.24 C ANISOU 280 CA ASER A 35 5432 4760 5857 -375 510 -88 C ATOM 281 CA BSER A 35 32.826 211.860 14.983 0.50 42.26 C ANISOU 281 CA BSER A 35 5434 4760 5861 -376 512 -88 C ATOM 282 C SER A 35 31.324 212.100 15.034 1.00 41.36 C ANISOU 282 C SER A 35 5373 4628 5713 -320 487 -66 C ATOM 283 O SER A 35 30.740 212.111 16.122 1.00 41.41 O ANISOU 283 O SER A 35 5374 4642 5716 -306 446 -127 O ATOM 284 CB ASER A 35 33.614 213.066 15.419 0.50 44.72 C ANISOU 284 CB ASER A 35 5719 4991 6282 -435 539 -127 C ATOM 285 CB BSER A 35 33.580 213.153 15.349 0.50 44.89 C ANISOU 285 CB BSER A 35 5745 5006 6307 -435 544 -121 C ATOM 286 OG ASER A 35 34.768 212.665 16.136 0.50 49.32 O ANISOU 286 OG ASER A 35 6234 5609 6896 -481 517 -193 O ATOM 287 OG BSER A 35 33.319 214.180 14.418 0.50 43.53 O ANISOU 287 OG BSER A 35 5617 4749 6176 -435 601 -50 O ATOM 288 N ASN A 36 30.674 212.292 13.888 1.00 39.43 N ANISOU 288 N ASN A 36 5179 4360 5442 -287 512 20 N ATOM 289 CA ASN A 36 29.219 212.411 13.915 1.00 40.13 C ANISOU 289 CA ASN A 36 5307 4439 5504 -230 480 42 C ATOM 290 C ASN A 36 28.543 211.086 14.255 1.00 36.69 C ANISOU 290 C ASN A 36 4864 4094 4982 -189 426 23 C ATOM 291 O ASN A 36 27.353 211.075 14.576 1.00 37.55 O ANISOU 291 O ASN A 36 4987 4201 5078 -145 395 21 O ATOM 292 CB ASN A 36 28.686 212.892 12.569 1.00 49.59 C ANISOU 292 CB ASN A 36 6561 5592 6689 -203 507 144 C ATOM 293 CG ASN A 36 28.930 214.363 12.334 1.00 62.88 C ANISOU 293 CG ASN A 36 8262 7166 8464 -229 557 172 C ATOM 294 OD1 ASN A 36 29.021 215.156 13.272 1.00 68.49 O ANISOU 294 OD1 ASN A 36 8950 7821 9252 -251 560 111 O ATOM 295 ND2 ASN A 36 29.037 214.737 11.066 1.00 67.41 N ANISOU 295 ND2 ASN A 36 8881 7705 9027 -227 597 265 N ATOM 296 N LEU A 37 29.261 209.974 14.163 1.00 35.31 N ANISOU 296 N LEU A 37 4663 3994 4757 -202 418 10 N ATOM 297 CA LEU A 37 28.694 208.691 14.541 1.00 34.75 C ANISOU 297 CA LEU A 37 4584 4006 4614 -167 369 -10 C ATOM 298 C LEU A 37 29.047 208.301 15.961 1.00 36.37 C ANISOU 298 C LEU A 37 4746 4246 4826 -184 336 -97 C ATOM 299 O LEU A 37 28.574 207.262 16.449 1.00 35.65 O ANISOU 299 O LEU A 37 4648 4219 4680 -158 297 -118 O ATOM 300 CB LEU A 37 29.181 207.622 13.563 1.00 33.33 C ANISOU 300 CB LEU A 37 4408 3885 4371 -164 378 30 C ATOM 301 CG LEU A 37 28.624 207.732 12.144 1.00 35.94 C ANISOU 301 CG LEU A 37 4795 4199 4660 -137 396 116 C ATOM 302 CD1 LEU A 37 29.278 206.722 11.218 1.00 37.07 C ANISOU 302 CD1 LEU A 37 4946 4397 4741 -141 416 143 C ATOM 303 CD2 LEU A 37 27.098 207.569 12.148 1.00 37.69 C ANISOU 303 CD2 LEU A 37 5044 4428 4850 -83 346 136 C ATOM 304 N GLN A 38 29.863 209.097 16.632 1.00 37.71 N ANISOU 304 N GLN A 38 4891 4375 5061 -230 349 -146 N ATOM 305 CA GLN A 38 30.329 208.768 17.973 1.00 40.55 C ANISOU 305 CA GLN A 38 5215 4769 5422 -252 312 -228 C ATOM 306 C GLN A 38 29.340 209.350 18.975 1.00 44.85 C ANISOU 306 C GLN A 38 5782 5283 5975 -233 294 -274 C ATOM 307 O GLN A 38 29.504 210.455 19.484 1.00 50.92 O ANISOU 307 O GLN A 38 6554 5987 6806 -261 309 -314 O ATOM 308 CB GLN A 38 31.748 209.289 18.183 1.00 40.05 C ANISOU 308 CB GLN A 38 5110 4681 5427 -314 327 -263 C ATOM 309 CG GLN A 38 32.777 208.549 17.335 1.00 39.31 C ANISOU 309 CG GLN A 38 4984 4626 5328 -330 348 -227 C ATOM 310 CD GLN A 38 34.140 209.184 17.312 1.00 41.86 C ANISOU 310 CD GLN A 38 5258 4910 5736 -392 376 -247 C ATOM 311 OE1 GLN A 38 34.475 210.010 18.166 1.00 47.50 O ANISOU 311 OE1 GLN A 38 5955 5582 6510 -429 361 -306 O ATOM 312 NE2 GLN A 38 34.933 208.815 16.329 1.00 38.64 N ANISOU 312 NE2 GLN A 38 4830 4514 5338 -405 420 -202 N ATOM 313 N ASN A 39 28.310 208.577 19.282 1.00 42.63 N ANISOU 313 N ASN A 39 5516 5048 5634 -187 268 -273 N ATOM 314 CA ASN A 39 27.342 208.926 20.305 1.00 41.30 C ANISOU 314 CA ASN A 39 5366 4862 5466 -166 258 -319 C ATOM 315 C ASN A 39 26.972 207.644 21.030 1.00 39.87 C ANISOU 315 C ASN A 39 5177 4761 5209 -142 220 -343 C ATOM 316 O ASN A 39 27.383 206.548 20.635 1.00 37.67 O ANISOU 316 O ASN A 39 4882 4546 4886 -138 201 -317 O ATOM 317 CB ASN A 39 26.114 209.615 19.696 1.00 42.33 C ANISOU 317 CB ASN A 39 5525 4933 5625 -125 282 -271 C ATOM 318 CG ASN A 39 25.495 208.805 18.567 1.00 47.94 C ANISOU 318 CG ASN A 39 6244 5681 6291 -84 273 -193 C ATOM 319 OD1 ASN A 39 25.075 207.663 18.763 1.00 46.28 O ANISOU 319 OD1 ASN A 39 6026 5538 6021 -60 244 -194 O ATOM 320 ND2 ASN A 39 25.448 209.382 17.379 1.00 55.44 N ANISOU 320 ND2 ASN A 39 7213 6585 7267 -79 295 -124 N ATOM 321 N VAL A 40 26.198 207.781 22.107 1.00 40.24 N ANISOU 321 N VAL A 40 5241 4805 5244 -126 215 -393 N ATOM 322 CA VAL A 40 25.928 206.634 22.979 1.00 38.52 C ANISOU 322 CA VAL A 40 5021 4660 4955 -110 185 -420 C ATOM 323 C VAL A 40 25.175 205.551 22.225 1.00 34.31 C ANISOU 323 C VAL A 40 4484 4171 4381 -67 177 -358 C ATOM 324 O VAL A 40 25.446 204.355 22.393 1.00 36.47 O ANISOU 324 O VAL A 40 4745 4512 4602 -63 150 -354 O ATOM 325 CB VAL A 40 25.147 207.073 24.232 1.00 43.53 C ANISOU 325 CB VAL A 40 5682 5275 5582 -99 195 -482 C ATOM 326 CG1 VAL A 40 24.489 205.871 24.914 1.00 43.36 C ANISOU 326 CG1 VAL A 40 5666 5321 5487 -70 179 -488 C ATOM 327 CG2 VAL A 40 26.066 207.789 25.177 1.00 47.88 C ANISOU 327 CG2 VAL A 40 6240 5806 6147 -147 185 -559 C ATOM 328 N THR A 41 24.188 205.943 21.422 1.00 31.60 N ANISOU 328 N THR A 41 4151 3789 4065 -34 197 -310 N ATOM 329 CA THR A 41 23.414 204.958 20.676 1.00 32.56 C ANISOU 329 CA THR A 41 4269 3950 4153 3 183 -254 C ATOM 330 C THR A 41 24.324 204.070 19.843 1.00 33.87 C ANISOU 330 C THR A 41 4423 4163 4283 -11 166 -221 C ATOM 331 O THR A 41 24.142 202.846 19.791 1.00 33.61 O ANISOU 331 O THR A 41 4381 4187 4201 5 144 -209 O ATOM 332 CB THR A 41 22.399 205.662 19.777 1.00 35.08 C ANISOU 332 CB THR A 41 4600 4214 4516 36 196 -202 C ATOM 333 OG1 THR A 41 21.779 206.720 20.512 1.00 35.85 O ANISOU 333 OG1 THR A 41 4705 4251 4666 44 222 -237 O ATOM 334 CG2 THR A 41 21.362 204.687 19.333 1.00 35.40 C ANISOU 334 CG2 THR A 41 4633 4291 4526 76 174 -163 C ATOM 335 N ASN A 42 25.339 204.653 19.223 1.00 33.68 N ANISOU 335 N ASN A 42 4397 4114 4287 -43 181 -208 N ATOM 336 CA ASN A 42 26.211 203.856 18.372 1.00 30.99 C ANISOU 336 CA ASN A 42 4044 3813 3918 -55 178 -177 C ATOM 337 C ASN A 42 27.294 203.104 19.133 1.00 30.18 C ANISOU 337 C ASN A 42 3911 3760 3797 -81 159 -220 C ATOM 338 O ASN A 42 27.940 202.231 18.535 1.00 30.60 O ANISOU 338 O ASN A 42 3948 3851 3826 -84 156 -199 O ATOM 339 CB ASN A 42 26.822 204.736 17.288 1.00 31.12 C ANISOU 339 CB ASN A 42 4071 3780 3972 -76 213 -136 C ATOM 340 CG ASN A 42 25.796 205.114 16.236 1.00 34.51 C ANISOU 340 CG ASN A 42 4535 4176 4400 -43 220 -73 C ATOM 341 OD1 ASN A 42 24.782 204.439 16.087 1.00 35.98 O ANISOU 341 OD1 ASN A 42 4729 4390 4551 -5 193 -54 O ATOM 342 ND2 ASN A 42 26.052 206.178 15.501 1.00 36.17 N ANISOU 342 ND2 ASN A 42 4766 4326 4651 -56 252 -36 N ATOM 343 N TYR A 43 27.497 203.368 20.424 1.00 30.94 N ANISOU 343 N TYR A 43 3999 3857 3899 -98 143 -280 N ATOM 344 CA TYR A 43 28.355 202.468 21.200 1.00 33.73 C ANISOU 344 CA TYR A 43 4326 4267 4225 -114 110 -315 C ATOM 345 C TYR A 43 27.696 201.098 21.348 1.00 29.50 C ANISOU 345 C TYR A 43 3792 3787 3628 -77 88 -298 C ATOM 346 O TYR A 43 28.369 200.058 21.296 1.00 29.51 O ANISOU 346 O TYR A 43 3770 3836 3607 -78 68 -292 O ATOM 347 CB TYR A 43 28.677 203.082 22.560 1.00 48.91 C ANISOU 347 CB TYR A 43 6249 6179 6157 -140 90 -383 C ATOM 348 CG TYR A 43 29.382 204.430 22.442 1.00 72.62 C ANISOU 348 CG TYR A 43 9244 9119 9228 -182 110 -406 C ATOM 349 CD1 TYR A 43 29.976 204.832 21.245 1.00 83.76 C ANISOU 349 CD1 TYR A 43 10641 10499 10686 -198 143 -363 C ATOM 350 CD2 TYR A 43 29.452 205.296 23.520 1.00 84.61 C ANISOU 350 CD2 TYR A 43 10776 10608 10766 -206 101 -471 C ATOM 351 CE1 TYR A 43 30.612 206.050 21.130 1.00 89.73 C ANISOU 351 CE1 TYR A 43 11388 11191 11512 -239 167 -380 C ATOM 352 CE2 TYR A 43 30.091 206.520 23.411 1.00 91.13 C ANISOU 352 CE2 TYR A 43 11594 11369 11662 -248 119 -495 C ATOM 353 CZ TYR A 43 30.666 206.889 22.214 1.00 93.02 C ANISOU 353 CZ TYR A 43 11813 11575 11954 -264 153 -446 C ATOM 354 OH TYR A 43 31.300 208.104 22.098 1.00 96.74 O ANISOU 354 OH TYR A 43 12275 11978 12504 -307 176 -466 O ATOM 355 N PHE A 44 26.381 201.085 21.488 1.00 26.40 N ANISOU 355 N PHE A 44 3424 3387 3219 -45 94 -289 N ATOM 356 CA PHE A 44 25.632 199.829 21.491 1.00 26.94 C ANISOU 356 CA PHE A 44 3494 3500 3242 -12 79 -267 C ATOM 357 C PHE A 44 25.633 199.189 20.120 1.00 26.02 C ANISOU 357 C PHE A 44 3374 3396 3118 1 82 -215 C ATOM 358 O PHE A 44 25.719 197.949 20.013 1.00 26.91 O ANISOU 358 O PHE A 44 3476 3552 3196 13 65 -203 O ATOM 359 CB PHE A 44 24.215 200.076 21.996 1.00 29.82 C ANISOU 359 CB PHE A 44 3878 3847 3606 16 90 -273 C ATOM 360 CG PHE A 44 24.183 200.444 23.461 1.00 32.29 C ANISOU 360 CG PHE A 44 4204 4158 3906 6 91 -330 C ATOM 361 CD1 PHE A 44 24.530 199.497 24.430 1.00 32.70 C ANISOU 361 CD1 PHE A 44 4256 4262 3907 3 66 -353 C ATOM 362 CD2 PHE A 44 23.833 201.699 23.858 1.00 34.96 C ANISOU 362 CD2 PHE A 44 4559 4444 4281 0 116 -361 C ATOM 363 CE1 PHE A 44 24.521 199.842 25.792 1.00 34.66 C ANISOU 363 CE1 PHE A 44 4527 4512 4129 -8 65 -407 C ATOM 364 CE2 PHE A 44 23.829 202.047 25.206 1.00 36.80 C ANISOU 364 CE2 PHE A 44 4812 4675 4493 -12 119 -421 C ATOM 365 CZ PHE A 44 24.184 201.110 26.159 1.00 35.29 C ANISOU 365 CZ PHE A 44 4627 4540 4241 -17 92 -444 C ATOM 366 N VAL A 45 25.587 200.008 19.056 1.00 27.24 N ANISOU 366 N VAL A 45 3541 3509 3300 -2 104 -182 N ATOM 367 CA VAL A 45 25.714 199.479 17.695 1.00 28.07 C ANISOU 367 CA VAL A 45 3653 3625 3387 7 110 -135 C ATOM 368 C VAL A 45 27.044 198.760 17.517 1.00 28.11 C ANISOU 368 C VAL A 45 3634 3664 3383 -15 113 -142 C ATOM 369 O VAL A 45 27.093 197.668 16.922 1.00 27.87 O ANISOU 369 O VAL A 45 3603 3667 3320 -1 108 -123 O ATOM 370 CB VAL A 45 25.517 200.608 16.659 1.00 29.85 C ANISOU 370 CB VAL A 45 3904 3798 3640 5 134 -96 C ATOM 371 CG1 VAL A 45 25.899 200.180 15.257 1.00 29.39 C ANISOU 371 CG1 VAL A 45 3863 3750 3553 5 147 -50 C ATOM 372 CG2 VAL A 45 24.080 201.048 16.641 1.00 30.32 C ANISOU 372 CG2 VAL A 45 3981 3829 3711 37 123 -78 C ATOM 373 N VAL A 46 28.142 199.349 18.023 1.00 26.92 N ANISOU 373 N VAL A 46 3460 3501 3267 -49 122 -171 N ATOM 374 CA VAL A 46 29.456 198.715 17.901 1.00 27.80 C ANISOU 374 CA VAL A 46 3536 3640 3386 -69 125 -179 C ATOM 375 C VAL A 46 29.526 197.443 18.736 1.00 26.32 C ANISOU 375 C VAL A 46 3329 3506 3168 -53 87 -200 C ATOM 376 O VAL A 46 30.114 196.447 18.324 1.00 28.18 O ANISOU 376 O VAL A 46 3544 3770 3394 -48 89 -189 O ATOM 377 CB VAL A 46 30.539 199.724 18.300 1.00 32.21 C ANISOU 377 CB VAL A 46 4067 4169 4001 -111 136 -208 C ATOM 378 CG1 VAL A 46 31.874 199.054 18.526 1.00 34.74 C ANISOU 378 CG1 VAL A 46 4336 4520 4342 -130 127 -226 C ATOM 379 CG2 VAL A 46 30.660 200.806 17.237 1.00 34.81 C ANISOU 379 CG2 VAL A 46 4416 4446 4365 -127 185 -175 C ATOM 380 N SER A 47 28.943 197.459 19.926 1.00 25.26 N ANISOU 380 N SER A 47 3201 3379 3017 -46 58 -229 N ATOM 381 CA SER A 47 28.922 196.246 20.750 1.00 27.21 C ANISOU 381 CA SER A 47 3436 3673 3228 -30 24 -240 C ATOM 382 C SER A 47 28.204 195.110 20.018 1.00 26.47 C ANISOU 382 C SER A 47 3355 3600 3104 2 28 -205 C ATOM 383 O SER A 47 28.651 193.960 20.035 1.00 26.45 O ANISOU 383 O SER A 47 3332 3628 3088 11 15 -200 O ATOM 384 CB SER A 47 28.245 196.543 22.090 1.00 30.28 C ANISOU 384 CB SER A 47 3845 4064 3596 -26 4 -272 C ATOM 385 OG SER A 47 28.310 195.402 22.935 1.00 30.37 O ANISOU 385 OG SER A 47 3851 4119 3570 -13 -28 -278 O ATOM 386 N LEU A 48 27.108 195.439 19.331 1.00 27.37 N ANISOU 386 N LEU A 48 3497 3692 3211 18 43 -182 N ATOM 387 CA LEU A 48 26.365 194.476 18.510 1.00 28.16 C ANISOU 387 CA LEU A 48 3609 3805 3284 44 41 -152 C ATOM 388 C LEU A 48 27.207 194.002 17.325 1.00 28.00 C ANISOU 388 C LEU A 48 3585 3792 3261 38 60 -133 C ATOM 389 O LEU A 48 27.239 192.805 17.000 1.00 28.70 O ANISOU 389 O LEU A 48 3670 3905 3330 52 54 -127 O ATOM 390 CB LEU A 48 25.067 195.143 18.047 1.00 29.95 C ANISOU 390 CB LEU A 48 3863 4002 3514 59 45 -132 C ATOM 391 CG LEU A 48 24.060 194.330 17.242 1.00 32.44 C ANISOU 391 CG LEU A 48 4192 4326 3808 84 32 -104 C ATOM 392 CD1 LEU A 48 23.651 193.081 18.024 1.00 32.69 C ANISOU 392 CD1 LEU A 48 4209 4389 3824 98 14 -116 C ATOM 393 CD2 LEU A 48 22.840 195.197 16.895 1.00 35.09 C ANISOU 393 CD2 LEU A 48 4544 4628 4161 99 29 -85 C ATOM 394 N ALA A 49 27.950 194.916 16.693 1.00 26.48 N ANISOU 394 N ALA A 49 3394 3575 3092 16 89 -126 N ATOM 395 CA ALA A 49 28.786 194.520 15.567 1.00 25.87 C ANISOU 395 CA ALA A 49 3316 3502 3011 10 120 -109 C ATOM 396 C ALA A 49 29.904 193.603 16.031 1.00 26.29 C ANISOU 396 C ALA A 49 3325 3584 3081 5 117 -130 C ATOM 397 O ALA A 49 30.279 192.646 15.335 1.00 25.93 O ANISOU 397 O ALA A 49 3277 3554 3023 15 134 -123 O ATOM 398 CB ALA A 49 29.348 195.785 14.884 1.00 25.41 C ANISOU 398 CB ALA A 49 3268 3407 2981 -16 160 -94 C ATOM 399 N ALA A 50 30.435 193.863 17.223 1.00 26.38 N ANISOU 399 N ALA A 50 3302 3601 3120 -9 93 -158 N ATOM 400 CA ALA A 50 31.505 193.018 17.758 1.00 26.50 C ANISOU 400 CA ALA A 50 3269 3642 3156 -11 78 -175 C ATOM 401 C ALA A 50 31.014 191.596 18.034 1.00 25.66 C ANISOU 401 C ALA A 50 3166 3565 3017 20 53 -170 C ATOM 402 O ALA A 50 31.734 190.620 17.797 1.00 26.10 O ANISOU 402 O ALA A 50 3195 3636 3087 29 59 -168 O ATOM 403 CB ALA A 50 32.057 193.655 19.033 1.00 27.42 C ANISOU 403 CB ALA A 50 3357 3760 3302 -33 44 -206 C ATOM 404 N ALA A 51 29.805 191.464 18.545 1.00 25.44 N ANISOU 404 N ALA A 51 3169 3542 2956 36 30 -167 N ATOM 405 CA ALA A 51 29.182 190.150 18.724 1.00 25.58 C ANISOU 405 CA ALA A 51 3194 3580 2947 63 12 -158 C ATOM 406 C ALA A 51 28.999 189.434 17.391 1.00 25.15 C ANISOU 406 C ALA A 51 3155 3521 2880 76 38 -142 C ATOM 407 O ALA A 51 29.215 188.216 17.308 1.00 26.85 O ANISOU 407 O ALA A 51 3359 3750 3095 91 35 -140 O ATOM 408 CB ALA A 51 27.849 190.308 19.437 1.00 26.24 C ANISOU 408 CB ALA A 51 3304 3662 3005 74 -6 -158 C ATOM 409 N ASP A 52 28.658 190.175 16.309 1.00 23.78 N ANISOU 409 N ASP A 52 3011 3327 2696 69 64 -129 N ATOM 410 CA ASP A 52 28.517 189.525 15.006 1.00 23.89 C ANISOU 410 CA ASP A 52 3050 3340 2685 78 86 -116 C ATOM 411 C ASP A 52 29.868 189.187 14.358 1.00 25.82 C ANISOU 411 C ASP A 52 3274 3586 2949 70 127 -121 C ATOM 412 O ASP A 52 29.978 188.182 13.679 1.00 25.87 O ANISOU 412 O ASP A 52 3290 3598 2942 83 142 -123 O ATOM 413 CB ASP A 52 27.667 190.394 14.108 1.00 24.82 C ANISOU 413 CB ASP A 52 3214 3439 2779 76 92 -96 C ATOM 414 CG ASP A 52 26.201 190.388 14.548 1.00 26.10 C ANISOU 414 CG ASP A 52 3390 3598 2929 91 53 -90 C ATOM 415 OD1 ASP A 52 25.795 189.401 15.204 1.00 26.42 O ANISOU 415 OD1 ASP A 52 3415 3653 2968 104 31 -100 O ATOM 416 OD2 ASP A 52 25.474 191.337 14.286 1.00 26.64 O ANISOU 416 OD2 ASP A 52 3479 3647 2995 91 47 -75 O ATOM 417 N ILE A 53 30.902 190.004 14.546 1.00 26.20 N ANISOU 417 N ILE A 53 3293 3627 3036 48 149 -126 N ATOM 418 CA ILE A 53 32.250 189.580 14.154 1.00 24.37 C ANISOU 418 CA ILE A 53 3023 3396 2839 42 188 -134 C ATOM 419 C ILE A 53 32.603 188.270 14.834 1.00 23.61 C ANISOU 419 C ILE A 53 2888 3319 2762 63 163 -147 C ATOM 420 O ILE A 53 33.157 187.352 14.205 1.00 24.35 O ANISOU 420 O ILE A 53 2971 3413 2866 75 194 -150 O ATOM 421 CB ILE A 53 33.282 190.696 14.464 1.00 26.18 C ANISOU 421 CB ILE A 53 3213 3612 3123 12 206 -140 C ATOM 422 CG1 ILE A 53 33.062 191.912 13.576 1.00 28.06 C ANISOU 422 CG1 ILE A 53 3492 3822 3348 -8 246 -120 C ATOM 423 CG2 ILE A 53 34.700 190.165 14.266 1.00 27.84 C ANISOU 423 CG2 ILE A 53 3365 3824 3389 7 242 -150 C ATOM 424 CD1 ILE A 53 33.813 193.189 14.032 1.00 30.26 C ANISOU 424 CD1 ILE A 53 3736 4078 3683 -43 256 -127 C ATOM 425 N ALA A 54 32.313 188.163 16.145 1.00 24.25 N ANISOU 425 N ALA A 54 2951 3414 2849 68 108 -152 N ATOM 426 CA ALA A 54 32.616 186.943 16.887 1.00 27.06 C ANISOU 426 CA ALA A 54 3275 3786 3220 90 78 -156 C ATOM 427 C ALA A 54 31.811 185.733 16.406 1.00 26.08 C ANISOU 427 C ALA A 54 3182 3662 3066 115 81 -150 C ATOM 428 O ALA A 54 32.279 184.590 16.543 1.00 25.41 O ANISOU 428 O ALA A 54 3072 3580 3004 135 79 -151 O ATOM 429 CB ALA A 54 32.373 187.169 18.383 1.00 28.39 C ANISOU 429 CB ALA A 54 3432 3969 3384 89 21 -160 C ATOM 430 N VAL A 55 30.598 185.936 15.894 1.00 26.16 N ANISOU 430 N VAL A 55 3243 3666 3031 116 81 -143 N ATOM 431 CA VAL A 55 29.882 184.827 15.247 1.00 25.81 C ANISOU 431 CA VAL A 55 3228 3618 2962 134 84 -143 C ATOM 432 C VAL A 55 30.704 184.273 14.082 1.00 25.79 C ANISOU 432 C VAL A 55 3226 3606 2967 137 134 -153 C ATOM 433 O VAL A 55 30.833 183.053 13.908 1.00 26.00 O ANISOU 433 O VAL A 55 3247 3628 3004 155 140 -161 O ATOM 434 CB VAL A 55 28.473 185.280 14.803 1.00 26.34 C ANISOU 434 CB VAL A 55 3343 3679 2987 131 69 -134 C ATOM 435 CG1 VAL A 55 27.814 184.278 13.843 1.00 28.89 C ANISOU 435 CG1 VAL A 55 3699 3994 3283 142 72 -139 C ATOM 436 CG2 VAL A 55 27.587 185.436 16.028 1.00 24.84 C ANISOU 436 CG2 VAL A 55 3147 3494 2796 135 30 -128 C ATOM 437 N GLY A 56 31.310 185.143 13.285 1.00 26.16 N ANISOU 437 N GLY A 56 3281 3647 3012 120 176 -152 N ATOM 438 CA GLY A 56 32.046 184.653 12.122 1.00 27.04 C ANISOU 438 CA GLY A 56 3401 3748 3123 123 236 -163 C ATOM 439 C GLY A 56 33.402 184.050 12.478 1.00 27.63 C ANISOU 439 C GLY A 56 3411 3822 3266 131 261 -174 C ATOM 440 O GLY A 56 33.837 183.068 11.870 1.00 28.30 O ANISOU 440 O GLY A 56 3494 3897 3363 147 299 -189 O ATOM 441 N VAL A 57 34.078 184.615 13.478 1.00 28.26 N ANISOU 441 N VAL A 57 3435 3909 3395 122 238 -169 N ATOM 442 CA VAL A 57 35.429 184.182 13.857 1.00 30.00 C ANISOU 442 CA VAL A 57 3580 4126 3691 129 252 -177 C ATOM 443 C VAL A 57 35.384 182.947 14.740 1.00 29.48 C ANISOU 443 C VAL A 57 3487 4067 3649 159 206 -175 C ATOM 444 O VAL A 57 36.266 182.087 14.652 1.00 30.66 O ANISOU 444 O VAL A 57 3591 4206 3854 179 228 -181 O ATOM 445 CB VAL A 57 36.183 185.331 14.555 1.00 34.30 C ANISOU 445 CB VAL A 57 4076 4676 4282 104 236 -174 C ATOM 446 CG1 VAL A 57 37.524 184.850 15.115 1.00 36.82 C ANISOU 446 CG1 VAL A 57 4307 4996 4688 112 231 -181 C ATOM 447 CG2 VAL A 57 36.426 186.457 13.577 1.00 37.73 C ANISOU 447 CG2 VAL A 57 4532 5096 4709 75 297 -172 C ATOM 448 N LEU A 58 34.383 182.845 15.624 1.00 27.94 N ANISOU 448 N LEU A 58 3316 3883 3417 164 145 -164 N ATOM 449 CA LEU A 58 34.356 181.772 16.619 1.00 27.51 C ANISOU 449 CA LEU A 58 3237 3833 3383 190 99 -155 C ATOM 450 C LEU A 58 33.107 180.912 16.533 1.00 26.46 C ANISOU 450 C LEU A 58 3155 3693 3207 205 87 -150 C ATOM 451 O LEU A 58 33.223 179.692 16.480 1.00 25.30 O ANISOU 451 O LEU A 58 2998 3530 3083 229 91 -149 O ATOM 452 CB LEU A 58 34.499 182.351 18.028 1.00 29.96 C ANISOU 452 CB LEU A 58 3522 4163 3699 182 36 -144 C ATOM 453 CG LEU A 58 35.860 182.955 18.392 1.00 34.86 C ANISOU 453 CG LEU A 58 4075 4789 4380 169 28 -150 C ATOM 454 CD1 LEU A 58 35.783 183.682 19.735 1.00 37.91 C ANISOU 454 CD1 LEU A 58 4456 5197 4751 155 -40 -147 C ATOM 455 CD2 LEU A 58 36.939 181.875 18.442 1.00 36.56 C ANISOU 455 CD2 LEU A 58 4228 4996 4667 197 30 -145 C ATOM 456 N ALA A 59 31.910 181.491 16.512 1.00 25.07 N ANISOU 456 N ALA A 59 3027 3523 2976 191 72 -147 N ATOM 457 CA ALA A 59 30.741 180.628 16.614 1.00 23.73 C ANISOU 457 CA ALA A 59 2891 3345 2781 203 53 -141 C ATOM 458 C ALA A 59 30.571 179.757 15.383 1.00 23.14 C ANISOU 458 C ALA A 59 2841 3249 2701 212 90 -158 C ATOM 459 O ALA A 59 30.094 178.617 15.509 1.00 22.31 O ANISOU 459 O ALA A 59 2744 3129 2605 227 80 -158 O ATOM 460 CB ALA A 59 29.469 181.435 16.881 1.00 23.47 C ANISOU 460 CB ALA A 59 2895 3320 2703 189 30 -134 C ATOM 461 N ILE A 60 30.925 180.246 14.190 1.00 23.26 N ANISOU 461 N ILE A 60 2876 3260 2700 200 134 -175 N ATOM 462 CA ILE A 60 30.735 179.416 13.013 1.00 23.27 C ANISOU 462 CA ILE A 60 2914 3242 2685 206 168 -197 C ATOM 463 C ILE A 60 31.761 178.293 12.985 1.00 24.45 C ANISOU 463 C ILE A 60 3026 3374 2891 229 199 -210 C ATOM 464 O ILE A 60 31.398 177.153 12.710 1.00 25.26 O ANISOU 464 O ILE A 60 3144 3453 2998 243 203 -224 O ATOM 465 CB ILE A 60 30.728 180.267 11.745 1.00 25.58 C ANISOU 465 CB ILE A 60 3252 3538 2930 188 206 -207 C ATOM 466 CG1 ILE A 60 29.342 180.936 11.642 1.00 27.22 C ANISOU 466 CG1 ILE A 60 3505 3754 3085 174 163 -196 C ATOM 467 CG2 ILE A 60 31.022 179.430 10.530 1.00 26.82 C ANISOU 467 CG2 ILE A 60 3441 3676 3072 195 256 -237 C ATOM 468 CD1 ILE A 60 29.200 182.002 10.538 1.00 28.46 C ANISOU 468 CD1 ILE A 60 3711 3914 3188 156 186 -192 C ATOM 469 N PRO A 61 33.042 178.542 13.242 1.00 25.08 N ANISOU 469 N PRO A 61 3051 3456 3021 234 223 -206 N ATOM 470 CA PRO A 61 33.956 177.402 13.341 1.00 25.48 C ANISOU 470 CA PRO A 61 3057 3484 3139 262 246 -214 C ATOM 471 C PRO A 61 33.526 176.413 14.420 1.00 24.49 C ANISOU 471 C PRO A 61 2916 3350 3039 284 193 -194 C ATOM 472 O PRO A 61 33.627 175.202 14.235 1.00 24.44 O ANISOU 472 O PRO A 61 2905 3313 3066 308 209 -203 O ATOM 473 CB PRO A 61 35.306 178.079 13.623 1.00 27.71 C ANISOU 473 CB PRO A 61 3274 3776 3478 260 264 -207 C ATOM 474 CG PRO A 61 35.188 179.385 12.939 1.00 28.23 C ANISOU 474 CG PRO A 61 3372 3857 3498 228 292 -212 C ATOM 475 CD PRO A 61 33.764 179.820 13.156 1.00 26.94 C ANISOU 475 CD PRO A 61 3267 3707 3263 214 243 -201 C ATOM 476 N PHE A 62 33.010 176.890 15.545 1.00 24.36 N ANISOU 476 N PHE A 62 2895 3356 3005 277 134 -166 N ATOM 477 CA PHE A 62 32.493 175.969 16.549 1.00 25.11 C ANISOU 477 CA PHE A 62 2986 3441 3112 296 90 -142 C ATOM 478 C PHE A 62 31.330 175.152 16.016 1.00 25.02 C ANISOU 478 C PHE A 62 3024 3407 3076 295 97 -154 C ATOM 479 O PHE A 62 31.224 173.958 16.312 1.00 24.88 O ANISOU 479 O PHE A 62 3001 3361 3093 316 92 -146 O ATOM 480 CB PHE A 62 32.047 176.737 17.777 1.00 24.51 C ANISOU 480 CB PHE A 62 2910 3395 3006 284 36 -115 C ATOM 481 CG PHE A 62 33.181 177.314 18.627 1.00 25.30 C ANISOU 481 CG PHE A 62 2958 3516 3137 286 8 -101 C ATOM 482 CD1 PHE A 62 34.523 177.040 18.394 1.00 27.51 C ANISOU 482 CD1 PHE A 62 3181 3787 3484 301 26 -106 C ATOM 483 CD2 PHE A 62 32.850 178.070 19.738 1.00 25.55 C ANISOU 483 CD2 PHE A 62 2996 3575 3135 273 -40 -84 C ATOM 484 CE1 PHE A 62 35.528 177.595 19.211 1.00 28.22 C ANISOU 484 CE1 PHE A 62 3217 3897 3609 300 -11 -94 C ATOM 485 CE2 PHE A 62 33.828 178.610 20.563 1.00 27.22 C ANISOU 485 CE2 PHE A 62 3165 3807 3370 271 -77 -76 C ATOM 486 CZ PHE A 62 35.176 178.354 20.299 1.00 28.13 C ANISOU 486 CZ PHE A 62 3218 3914 3555 284 -67 -80 C ATOM 487 N ALA A 63 30.402 175.790 15.291 1.00 23.45 N ANISOU 487 N ALA A 63 2873 3217 2821 271 102 -170 N ATOM 488 CA ALA A 63 29.249 175.065 14.740 1.00 23.71 C ANISOU 488 CA ALA A 63 2948 3227 2832 267 99 -186 C ATOM 489 C ALA A 63 29.689 174.006 13.739 1.00 24.68 C ANISOU 489 C ALA A 63 3082 3315 2979 279 142 -220 C ATOM 490 O ALA A 63 29.155 172.893 13.706 1.00 25.11 O ANISOU 490 O ALA A 63 3149 3338 3055 287 137 -229 O ATOM 491 CB ALA A 63 28.255 176.053 14.078 1.00 23.88 C ANISOU 491 CB ALA A 63 3015 3267 2793 240 89 -196 C ATOM 492 N ILE A 64 30.661 174.321 12.913 1.00 26.74 N ANISOU 492 N ILE A 64 3339 3578 3241 281 190 -242 N ATOM 493 CA ILE A 64 31.172 173.316 11.983 1.00 26.37 C ANISOU 493 CA ILE A 64 3304 3496 3219 295 241 -280 C ATOM 494 C ILE A 64 31.750 172.137 12.761 1.00 27.52 C ANISOU 494 C ILE A 64 3400 3609 3445 328 240 -266 C ATOM 495 O ILE A 64 31.474 170.973 12.459 1.00 27.21 O ANISOU 495 O ILE A 64 3377 3529 3431 339 253 -287 O ATOM 496 CB ILE A 64 32.200 173.966 11.048 1.00 27.01 C ANISOU 496 CB ILE A 64 3385 3587 3290 291 304 -301 C ATOM 497 CG1 ILE A 64 31.511 174.933 10.109 1.00 27.08 C ANISOU 497 CG1 ILE A 64 3458 3618 3212 261 307 -313 C ATOM 498 CG2 ILE A 64 33.033 172.906 10.272 1.00 28.48 C ANISOU 498 CG2 ILE A 64 3568 3734 3520 313 373 -340 C ATOM 499 CD1 ILE A 64 32.519 175.878 9.387 1.00 27.32 C ANISOU 499 CD1 ILE A 64 3488 3663 3229 252 369 -319 C ATOM 500 N THR A 65 32.524 172.433 13.811 1.00 28.72 N ANISOU 500 N THR A 65 3494 3777 3640 342 219 -229 N ATOM 501 CA THR A 65 33.149 171.392 14.632 1.00 28.99 C ANISOU 501 CA THR A 65 3479 3783 3753 377 208 -205 C ATOM 502 C THR A 65 32.111 170.470 15.258 1.00 28.18 C ANISOU 502 C THR A 65 3399 3655 3653 382 171 -185 C ATOM 503 O THR A 65 32.232 169.240 15.187 1.00 29.18 O ANISOU 503 O THR A 65 3519 3734 3833 405 187 -191 O ATOM 504 CB THR A 65 34.005 172.049 15.726 1.00 30.91 C ANISOU 504 CB THR A 65 3663 4057 4026 385 171 -165 C ATOM 505 OG1 THR A 65 35.014 172.824 15.110 1.00 30.50 O ANISOU 505 OG1 THR A 65 3580 4019 3987 379 212 -185 O ATOM 506 CG2 THR A 65 34.657 171.004 16.642 1.00 32.52 C ANISOU 506 CG2 THR A 65 3816 4234 4308 425 146 -131 C ATOM 507 N ILE A 66 31.077 171.030 15.890 1.00 25.88 N ANISOU 507 N ILE A 66 3131 3391 3310 360 126 -162 N ATOM 508 CA AILE A 66 30.108 170.212 16.601 0.50 27.08 C ANISOU 508 CA AILE A 66 3299 3520 3471 362 97 -136 C ATOM 509 CA BILE A 66 30.163 170.139 16.593 0.50 27.05 C ANISOU 509 CA BILE A 66 3294 3513 3471 364 98 -136 C ATOM 510 C ILE A 66 29.225 169.400 15.660 1.00 26.25 C ANISOU 510 C ILE A 66 3235 3375 3364 351 118 -175 C ATOM 511 O ILE A 66 28.618 168.418 16.103 1.00 26.77 O ANISOU 511 O ILE A 66 3305 3403 3462 356 107 -160 O ATOM 512 CB AILE A 66 29.247 171.092 17.534 0.50 28.21 C ANISOU 512 CB AILE A 66 3455 3702 3563 342 53 -103 C ATOM 513 CB BILE A 66 29.318 170.833 17.681 0.50 28.25 C ANISOU 513 CB BILE A 66 3455 3699 3579 348 52 -97 C ATOM 514 CG1AILE A 66 28.601 170.221 18.607 0.50 26.03 C ANISOU 514 CG1AILE A 66 3181 3403 3307 352 29 -61 C ATOM 515 CG1BILE A 66 28.312 171.826 17.101 0.50 29.15 C ANISOU 515 CG1BILE A 66 3606 3840 3630 314 48 -120 C ATOM 516 CG2AILE A 66 28.171 171.871 16.741 0.50 29.28 C ANISOU 516 CG2AILE A 66 3631 3854 3639 309 54 -133 C ATOM 517 CG2BILE A 66 30.222 171.526 18.670 0.50 33.22 C ANISOU 517 CG2BILE A 66 4048 4364 4209 359 24 -64 C ATOM 518 CD1AILE A 66 28.101 171.000 19.822 0.50 22.71 C ANISOU 518 CD1AILE A 66 2765 3020 2843 342 -6 -21 C ATOM 519 CD1BILE A 66 27.275 172.226 18.129 0.50 31.15 C ANISOU 519 CD1BILE A 66 3869 4111 3854 301 15 -87 C ATOM 520 N SER A 67 29.104 169.819 14.386 1.00 27.94 N ANISOU 520 N SER A 67 3482 3595 3538 332 144 -224 N ATOM 521 CA SER A 67 28.341 169.041 13.417 1.00 29.56 C ANISOU 521 CA SER A 67 3731 3764 3738 319 158 -269 C ATOM 522 C SER A 67 28.972 167.678 13.133 1.00 30.81 C ANISOU 522 C SER A 67 3879 3864 3965 345 196 -292 C ATOM 523 O SER A 67 28.284 166.797 12.610 1.00 29.48 O ANISOU 523 O SER A 67 3741 3652 3806 336 200 -326 O ATOM 524 CB SER A 67 28.191 169.815 12.089 1.00 29.01 C ANISOU 524 CB SER A 67 3707 3717 3599 295 176 -315 C ATOM 525 OG SER A 67 29.373 169.766 11.316 1.00 29.43 O ANISOU 525 OG SER A 67 3759 3764 3661 310 233 -345 O ATOM 526 N THR A 68 30.252 167.478 13.479 1.00 32.17 N ANISOU 526 N THR A 68 4005 4028 4190 378 222 -276 N ATOM 527 CA THR A 68 30.918 166.214 13.230 1.00 33.82 C ANISOU 527 CA THR A 68 4198 4176 4475 409 262 -296 C ATOM 528 C THR A 68 30.663 165.190 14.315 1.00 34.37 C ANISOU 528 C THR A 68 4245 4205 4611 430 234 -249 C ATOM 529 O THR A 68 30.930 164.008 14.105 1.00 35.81 O ANISOU 529 O THR A 68 4422 4324 4860 453 263 -266 O ATOM 530 CB THR A 68 32.429 166.423 13.106 1.00 34.05 C ANISOU 530 CB THR A 68 4178 4210 4548 439 304 -297 C ATOM 531 OG1 THR A 68 32.975 166.756 14.388 1.00 33.64 O ANISOU 531 OG1 THR A 68 4070 4183 4529 458 262 -232 O ATOM 532 CG2 THR A 68 32.733 167.540 12.099 1.00 33.41 C ANISOU 532 CG2 THR A 68 4122 4172 4402 416 340 -333 C ATOM 533 N GLY A 69 30.175 165.602 15.482 1.00 33.13 N ANISOU 533 N GLY A 69 4076 4078 4435 424 182 -190 N ATOM 534 CA GLY A 69 30.016 164.645 16.562 1.00 32.69 C ANISOU 534 CA GLY A 69 4002 3983 4435 446 160 -137 C ATOM 535 C GLY A 69 31.310 164.052 17.083 1.00 34.60 C ANISOU 535 C GLY A 69 4193 4199 4755 494 167 -104 C ATOM 536 O GLY A 69 31.306 162.937 17.625 1.00 34.87 O ANISOU 536 O GLY A 69 4218 4178 4855 519 164 -71 O ATOM 537 N PHE A 70 32.414 164.786 16.973 1.00 35.79 N ANISOU 537 N PHE A 70 4305 4386 4908 507 173 -108 N ATOM 538 CA PHE A 70 33.727 164.300 17.405 1.00 36.60 C ANISOU 538 CA PHE A 70 4346 4465 5094 554 175 -79 C ATOM 539 C PHE A 70 33.753 163.988 18.907 1.00 35.87 C ANISOU 539 C PHE A 70 4233 4375 5022 577 113 4 C ATOM 540 O PHE A 70 33.026 164.577 19.713 1.00 34.81 O ANISOU 540 O PHE A 70 4124 4283 4821 554 68 39 O ATOM 541 CB PHE A 70 34.812 165.355 17.058 1.00 35.84 C ANISOU 541 CB PHE A 70 4207 4416 4992 555 189 -97 C ATOM 542 CG PHE A 70 34.819 166.558 17.973 1.00 37.59 C ANISOU 542 CG PHE A 70 4418 4708 5157 537 129 -57 C ATOM 543 CD1 PHE A 70 33.742 167.408 18.059 1.00 35.69 C ANISOU 543 CD1 PHE A 70 4227 4509 4825 496 107 -61 C ATOM 544 CD2 PHE A 70 35.932 166.838 18.744 1.00 43.44 C ANISOU 544 CD2 PHE A 70 5094 5469 5943 563 93 -19 C ATOM 545 CE1 PHE A 70 33.754 168.497 18.909 1.00 39.24 C ANISOU 545 CE1 PHE A 70 4668 5016 5225 481 58 -30 C ATOM 546 CE2 PHE A 70 35.944 167.925 19.593 1.00 44.93 C ANISOU 546 CE2 PHE A 70 5277 5718 6077 543 36 10 C ATOM 547 CZ PHE A 70 34.868 168.748 19.677 1.00 42.79 C ANISOU 547 CZ PHE A 70 5060 5485 5712 503 22 3 C ATOM 548 N CYS A 71 34.623 163.063 19.300 1.00 36.86 N ANISOU 548 N CYS A 71 4313 4453 5238 625 110 36 N ATOM 549 CA CYS A 71 34.775 162.746 20.720 1.00 37.63 C ANISOU 549 CA CYS A 71 4394 4552 5351 651 46 121 C ATOM 550 C CYS A 71 35.431 163.904 21.451 1.00 36.49 C ANISOU 550 C CYS A 71 4217 4482 5166 648 -10 149 C ATOM 551 O CYS A 71 36.428 164.451 20.987 1.00 36.95 O ANISOU 551 O CYS A 71 4225 4560 5254 655 2 121 O ATOM 552 CB CYS A 71 35.621 161.462 20.897 1.00 40.71 C ANISOU 552 CB CYS A 71 4740 4869 5860 708 53 152 C ATOM 553 SG CYS A 71 34.869 160.017 20.109 1.00 43.47 S ANISOU 553 SG CYS A 71 5129 5119 6268 711 119 116 S ATOM 554 N ALA A 72 34.874 164.279 22.601 1.00 34.37 N ANISOU 554 N ALA A 72 3978 4252 4830 635 -69 203 N ATOM 555 CA ALA A 72 35.420 165.369 23.387 1.00 34.43 C ANISOU 555 CA ALA A 72 3964 4327 4791 628 -129 227 C ATOM 556 C ALA A 72 35.087 165.154 24.849 1.00 35.32 C ANISOU 556 C ALA A 72 4106 4454 4862 638 -195 305 C ATOM 557 O ALA A 72 34.070 164.543 25.181 1.00 32.36 O ANISOU 557 O ALA A 72 3783 4052 4462 631 -182 332 O ATOM 558 CB ALA A 72 34.841 166.726 22.946 1.00 34.27 C ANISOU 558 CB ALA A 72 3973 4365 4683 577 -115 178 C ATOM 559 N ALA A 73 35.910 165.726 25.725 1.00 38.98 N ANISOU 559 N ALA A 73 4538 4961 5311 650 -264 339 N ATOM 560 CA ALA A 73 35.507 165.849 27.114 1.00 40.52 C ANISOU 560 CA ALA A 73 4778 5187 5430 649 -328 403 C ATOM 561 C ALA A 73 34.228 166.676 27.204 1.00 36.94 C ANISOU 561 C ALA A 73 4392 4772 4871 598 -305 379 C ATOM 562 O ALA A 73 34.093 167.710 26.553 1.00 34.15 O ANISOU 562 O ALA A 73 4036 4454 4487 565 -282 321 O ATOM 563 CB ALA A 73 36.608 166.513 27.934 1.00 43.74 C ANISOU 563 CB ALA A 73 5143 5644 5830 661 -413 428 C ATOM 564 N CYS A 74 33.318 166.263 28.083 1.00 36.81 N ANISOU 564 N CYS A 74 4436 4749 4801 595 -312 430 N ATOM 565 CA CYS A 74 31.947 166.753 27.979 1.00 37.69 C ANISOU 565 CA CYS A 74 4604 4875 4841 552 -269 406 C ATOM 566 C CYS A 74 31.867 168.245 28.258 1.00 33.04 C ANISOU 566 C CYS A 74 4029 4357 4169 518 -292 374 C ATOM 567 O CYS A 74 31.130 168.963 27.577 1.00 32.81 O ANISOU 567 O CYS A 74 4013 4341 4111 484 -251 323 O ATOM 568 CB CYS A 74 31.030 165.943 28.905 1.00 43.24 C ANISOU 568 CB CYS A 74 5364 5551 5514 556 -261 471 C ATOM 569 SG CYS A 74 29.255 166.196 28.581 1.00 40.93 S ANISOU 569 SG CYS A 74 5124 5253 5176 507 -192 441 S ATOM 570 N HIS A 75 32.652 168.752 29.208 1.00 32.29 N ANISOU 570 N HIS A 75 3926 4304 4037 528 -360 402 N ATOM 571 CA HIS A 75 32.617 170.187 29.468 1.00 34.81 C ANISOU 571 CA HIS A 75 4258 4684 4283 495 -382 365 C ATOM 572 C HIS A 75 33.318 171.012 28.378 1.00 32.07 C ANISOU 572 C HIS A 75 3855 4351 3980 480 -368 299 C ATOM 573 O HIS A 75 32.966 172.170 28.169 1.00 32.12 O ANISOU 573 O HIS A 75 3875 4391 3939 445 -356 256 O ATOM 574 CB HIS A 75 33.210 170.465 30.841 1.00 43.35 C ANISOU 574 CB HIS A 75 5357 5806 5307 505 -464 409 C ATOM 575 CG HIS A 75 32.326 170.001 31.965 1.00 52.29 C ANISOU 575 CG HIS A 75 6567 6939 6363 508 -465 468 C ATOM 576 ND1 HIS A 75 32.230 168.676 32.339 1.00 56.28 N ANISOU 576 ND1 HIS A 75 7087 7398 6898 541 -464 536 N ATOM 577 CD2 HIS A 75 31.450 170.675 32.749 1.00 56.02 C ANISOU 577 CD2 HIS A 75 7108 7445 6733 480 -456 469 C ATOM 578 CE1 HIS A 75 31.358 168.558 33.325 1.00 57.74 C ANISOU 578 CE1 HIS A 75 7348 7591 6999 532 -454 580 C ATOM 579 NE2 HIS A 75 30.868 169.756 33.590 1.00 58.07 N ANISOU 579 NE2 HIS A 75 7423 7682 6959 496 -447 538 N ATOM 580 N GLY A 76 34.327 170.457 27.697 1.00 30.47 N ANISOU 580 N GLY A 76 3587 4119 3870 507 -366 292 N ATOM 581 CA GLY A 76 34.848 171.119 26.500 1.00 29.23 C ANISOU 581 CA GLY A 76 3384 3966 3757 491 -330 230 C ATOM 582 C GLY A 76 33.795 171.155 25.414 1.00 28.73 C ANISOU 582 C GLY A 76 3354 3883 3680 467 -254 188 C ATOM 583 O GLY A 76 33.629 172.165 24.717 1.00 27.97 O ANISOU 583 O GLY A 76 3260 3809 3560 437 -228 140 O ATOM 584 N CYS A 77 33.072 170.047 25.254 1.00 28.98 N ANISOU 584 N CYS A 77 3412 3869 3730 480 -223 206 N ATOM 585 CA CYS A 77 31.969 169.993 24.297 1.00 29.22 C ANISOU 585 CA CYS A 77 3477 3879 3747 456 -163 167 C ATOM 586 C CYS A 77 30.919 171.054 24.619 1.00 27.55 C ANISOU 586 C CYS A 77 3310 3706 3450 418 -164 156 C ATOM 587 O CYS A 77 30.446 171.757 23.723 1.00 26.01 O ANISOU 587 O CYS A 77 3124 3520 3237 392 -133 110 O ATOM 588 CB CYS A 77 31.350 168.588 24.299 1.00 29.79 C ANISOU 588 CB CYS A 77 3569 3894 3857 473 -140 194 C ATOM 589 SG CYS A 77 29.850 168.404 23.242 1.00 30.89 S ANISOU 589 SG CYS A 77 3750 4004 3983 439 -81 149 S ATOM 590 N LEU A 78 30.554 171.203 25.906 1.00 26.23 N ANISOU 590 N LEU A 78 3174 3562 3230 417 -199 199 N ATOM 591 CA LEU A 78 29.553 172.208 26.288 1.00 24.71 C ANISOU 591 CA LEU A 78 3023 3403 2962 385 -193 187 C ATOM 592 C LEU A 78 29.994 173.613 25.938 1.00 23.94 C ANISOU 592 C LEU A 78 2910 3345 2840 363 -202 143 C ATOM 593 O LEU A 78 29.178 174.466 25.555 1.00 26.60 O ANISOU 593 O LEU A 78 3269 3695 3144 335 -177 113 O ATOM 594 CB LEU A 78 29.271 172.148 27.789 1.00 28.23 C ANISOU 594 CB LEU A 78 3509 3868 3350 390 -225 239 C ATOM 595 CG LEU A 78 28.251 171.149 28.279 1.00 31.15 C ANISOU 595 CG LEU A 78 3916 4204 3715 395 -197 282 C ATOM 596 CD1 LEU A 78 28.290 171.236 29.805 1.00 31.14 C ANISOU 596 CD1 LEU A 78 3957 4230 3643 402 -233 334 C ATOM 597 CD2 LEU A 78 26.814 171.388 27.755 1.00 31.15 C ANISOU 597 CD2 LEU A 78 3939 4191 3706 365 -142 255 C ATOM 598 N PHE A 79 31.271 173.901 26.085 1.00 24.12 N ANISOU 598 N PHE A 79 2892 3386 2886 373 -239 142 N ATOM 599 CA PHE A 79 31.713 175.248 25.795 1.00 23.77 C ANISOU 599 CA PHE A 79 2832 3375 2826 349 -246 101 C ATOM 600 C PHE A 79 31.545 175.575 24.315 1.00 24.20 C ANISOU 600 C PHE A 79 2875 3413 2907 334 -192 56 C ATOM 601 O PHE A 79 31.040 176.644 23.939 1.00 25.87 O ANISOU 601 O PHE A 79 3105 3641 3084 306 -174 27 O ATOM 602 CB PHE A 79 33.168 175.423 26.215 1.00 27.93 C ANISOU 602 CB PHE A 79 3306 3918 3387 361 -298 108 C ATOM 603 CG PHE A 79 33.692 176.807 25.912 1.00 32.06 C ANISOU 603 CG PHE A 79 3807 4469 3905 332 -303 66 C ATOM 604 CD1 PHE A 79 33.456 177.851 26.801 1.00 33.10 C ANISOU 604 CD1 PHE A 79 3969 4636 3973 308 -338 58 C ATOM 605 CD2 PHE A 79 34.394 177.064 24.739 1.00 34.87 C ANISOU 605 CD2 PHE A 79 4116 4812 4321 327 -267 33 C ATOM 606 CE1 PHE A 79 33.924 179.118 26.524 1.00 33.63 C ANISOU 606 CE1 PHE A 79 4015 4719 4042 279 -340 19 C ATOM 607 CE2 PHE A 79 34.860 178.353 24.449 1.00 37.07 C ANISOU 607 CE2 PHE A 79 4375 5110 4599 297 -265 -1 C ATOM 608 CZ PHE A 79 34.624 179.366 25.326 1.00 36.03 C ANISOU 608 CZ PHE A 79 4270 5009 4412 273 -303 -9 C ATOM 609 N ILE A 80 31.927 174.653 23.433 1.00 25.78 N ANISOU 609 N ILE A 80 3050 3579 3167 353 -162 50 N ATOM 610 CA AILE A 80 31.738 174.810 21.989 0.50 26.02 C ANISOU 610 CA AILE A 80 3081 3593 3212 340 -109 8 C ATOM 611 CA BILE A 80 31.722 175.011 22.042 0.50 25.91 C ANISOU 611 CA BILE A 80 3069 3585 3192 336 -111 7 C ATOM 612 C ILE A 80 30.261 174.912 21.640 1.00 26.36 C ANISOU 612 C ILE A 80 3175 3629 3211 320 -86 -2 C ATOM 613 O ILE A 80 29.870 175.585 20.701 1.00 24.17 O ANISOU 613 O ILE A 80 2913 3355 2915 300 -60 -34 O ATOM 614 CB AILE A 80 32.402 173.624 21.265 0.50 30.81 C ANISOU 614 CB AILE A 80 3658 4159 3889 368 -80 3 C ATOM 615 CB BILE A 80 32.615 174.199 21.097 0.50 29.22 C ANISOU 615 CB BILE A 80 3451 3972 3680 358 -78 -9 C ATOM 616 CG1AILE A 80 33.924 173.797 21.310 0.50 30.84 C ANISOU 616 CG1AILE A 80 3599 4170 3949 383 -91 3 C ATOM 617 CG1BILE A 80 32.322 172.708 21.187 0.50 31.24 C ANISOU 617 CG1BILE A 80 3713 4185 3971 385 -71 12 C ATOM 618 CG2AILE A 80 31.863 173.462 19.824 0.50 29.95 C ANISOU 618 CG2AILE A 80 3575 4026 3779 356 -24 -39 C ATOM 619 CG2BILE A 80 34.088 174.551 21.372 0.50 30.34 C ANISOU 619 CG2BILE A 80 3530 4128 3869 369 -99 -6 C ATOM 620 CD1AILE A 80 34.686 172.671 20.658 0.50 36.10 C ANISOU 620 CD1AILE A 80 4228 4793 4695 415 -58 -3 C ATOM 621 CD1BILE A 80 33.037 171.924 20.067 0.50 33.38 C ANISOU 621 CD1BILE A 80 3957 4417 4309 404 -23 -16 C ATOM 622 N ALA A 81 29.423 174.166 22.351 1.00 25.01 N ANISOU 622 N ALA A 81 3028 3444 3029 327 -96 28 N ATOM 623 CA ALA A 81 27.998 174.160 22.024 1.00 24.58 C ANISOU 623 CA ALA A 81 3011 3378 2950 309 -75 18 C ATOM 624 C ALA A 81 27.318 175.456 22.472 1.00 24.73 C ANISOU 624 C ALA A 81 3051 3431 2914 285 -83 14 C ATOM 625 O ALA A 81 26.395 175.962 21.810 1.00 25.85 O ANISOU 625 O ALA A 81 3211 3571 3040 266 -66 -9 O ATOM 626 CB ALA A 81 27.349 172.958 22.713 1.00 24.35 C ANISOU 626 CB ALA A 81 2995 3318 2937 322 -75 55 C ATOM 627 N CYS A 82 27.733 175.991 23.603 1.00 25.26 N ANISOU 627 N CYS A 82 3118 3526 2952 286 -112 33 N ATOM 628 CA CYS A 82 27.031 177.113 24.239 1.00 25.40 C ANISOU 628 CA CYS A 82 3162 3570 2918 266 -116 29 C ATOM 629 C CYS A 82 27.624 178.477 23.943 1.00 24.73 C ANISOU 629 C CYS A 82 3066 3510 2820 249 -124 -2 C ATOM 630 O CYS A 82 26.970 179.476 24.220 1.00 23.93 O ANISOU 630 O CYS A 82 2986 3422 2685 232 -119 -14 O ATOM 631 CB CYS A 82 27.022 176.945 25.753 1.00 28.39 C ANISOU 631 CB CYS A 82 3561 3964 3260 274 -141 64 C ATOM 632 SG CYS A 82 26.015 175.525 26.249 1.00 31.46 S ANISOU 632 SG CYS A 82 3974 4321 3659 288 -120 108 S ATOM 633 N PHE A 83 28.829 178.561 23.397 1.00 23.99 N ANISOU 633 N PHE A 83 2938 3418 2758 253 -131 -15 N ATOM 634 CA PHE A 83 29.429 179.886 23.229 1.00 23.57 C ANISOU 634 CA PHE A 83 2873 3386 2698 234 -136 -41 C ATOM 635 C PHE A 83 28.527 180.806 22.409 1.00 23.06 C ANISOU 635 C PHE A 83 2832 3316 2614 213 -106 -64 C ATOM 636 O PHE A 83 28.406 181.994 22.728 1.00 24.89 O ANISOU 636 O PHE A 83 3073 3560 2822 195 -111 -77 O ATOM 637 CB PHE A 83 30.822 179.766 22.606 1.00 25.87 C ANISOU 637 CB PHE A 83 3116 3674 3040 240 -135 -51 C ATOM 638 CG PHE A 83 31.530 181.105 22.510 1.00 31.58 C ANISOU 638 CG PHE A 83 3820 4413 3765 216 -140 -75 C ATOM 639 CD1 PHE A 83 32.017 181.729 23.649 1.00 37.59 C ANISOU 639 CD1 PHE A 83 4573 5197 4512 207 -186 -74 C ATOM 640 CD2 PHE A 83 31.651 181.765 21.296 1.00 30.81 C ANISOU 640 CD2 PHE A 83 3719 4305 3681 200 -98 -98 C ATOM 641 CE1 PHE A 83 32.633 182.985 23.568 1.00 38.89 C ANISOU 641 CE1 PHE A 83 4718 5370 4686 180 -190 -100 C ATOM 642 CE2 PHE A 83 32.291 182.998 21.213 1.00 30.76 C ANISOU 642 CE2 PHE A 83 3696 4307 3685 176 -98 -116 C ATOM 643 CZ PHE A 83 32.758 183.616 22.345 1.00 33.64 C ANISOU 643 CZ PHE A 83 4046 4691 4045 164 -143 -119 C ATOM 644 N VAL A 84 27.851 180.278 21.370 1.00 22.41 N ANISOU 644 N VAL A 84 2761 3213 2542 216 -78 -68 N ATOM 645 CA VAL A 84 27.001 181.141 20.542 1.00 22.55 C ANISOU 645 CA VAL A 84 2802 3226 2542 199 -60 -85 C ATOM 646 C VAL A 84 25.888 181.772 21.377 1.00 22.48 C ANISOU 646 C VAL A 84 2814 3221 2505 192 -66 -79 C ATOM 647 O VAL A 84 25.432 182.882 21.091 1.00 23.90 O ANISOU 647 O VAL A 84 3005 3402 2673 178 -59 -90 O ATOM 648 CB VAL A 84 26.449 180.345 19.354 1.00 23.85 C ANISOU 648 CB VAL A 84 2977 3367 2717 204 -41 -92 C ATOM 649 CG1 VAL A 84 25.566 179.240 19.818 1.00 23.49 C ANISOU 649 CG1 VAL A 84 2939 3307 2680 214 -46 -76 C ATOM 650 CG2 VAL A 84 25.705 181.233 18.382 1.00 25.53 C ANISOU 650 CG2 VAL A 84 3214 3577 2910 189 -31 -105 C ATOM 651 N LEU A 85 25.461 181.107 22.446 1.00 22.33 N ANISOU 651 N LEU A 85 2802 3204 2477 201 -75 -59 N ATOM 652 CA LEU A 85 24.385 181.659 23.276 1.00 22.56 C ANISOU 652 CA LEU A 85 2853 3237 2481 195 -69 -54 C ATOM 653 C LEU A 85 24.852 182.880 24.040 1.00 23.41 C ANISOU 653 C LEU A 85 2968 3365 2562 184 -80 -69 C ATOM 654 O LEU A 85 24.041 183.750 24.410 1.00 24.47 O ANISOU 654 O LEU A 85 3119 3497 2679 176 -66 -78 O ATOM 655 CB LEU A 85 23.905 180.580 24.270 1.00 24.60 C ANISOU 655 CB LEU A 85 3122 3492 2733 207 -67 -25 C ATOM 656 CG LEU A 85 23.451 179.259 23.651 1.00 27.51 C ANISOU 656 CG LEU A 85 3483 3834 3137 216 -57 -12 C ATOM 657 CD1 LEU A 85 23.018 178.326 24.835 1.00 30.20 C ANISOU 657 CD1 LEU A 85 3837 4168 3470 226 -50 24 C ATOM 658 CD2 LEU A 85 22.347 179.479 22.652 1.00 27.41 C ANISOU 658 CD2 LEU A 85 3468 3802 3143 206 -42 -28 C ATOM 659 N VAL A 86 26.149 182.951 24.311 1.00 23.68 N ANISOU 659 N VAL A 86 2986 3415 2596 183 -105 -72 N ATOM 660 CA VAL A 86 26.708 184.161 24.936 1.00 23.14 C ANISOU 660 CA VAL A 86 2921 3362 2508 167 -121 -94 C ATOM 661 C VAL A 86 26.568 185.331 23.974 1.00 23.06 C ANISOU 661 C VAL A 86 2909 3339 2515 150 -100 -117 C ATOM 662 O VAL A 86 26.162 186.440 24.340 1.00 24.21 O ANISOU 662 O VAL A 86 3071 3482 2646 137 -93 -134 O ATOM 663 CB VAL A 86 28.186 183.944 25.298 1.00 23.85 C ANISOU 663 CB VAL A 86 2982 3469 2610 168 -159 -93 C ATOM 664 CG1 VAL A 86 28.789 185.267 25.809 1.00 24.46 C ANISOU 664 CG1 VAL A 86 3058 3558 2676 144 -179 -123 C ATOM 665 CG2 VAL A 86 28.401 182.848 26.324 1.00 23.93 C ANISOU 665 CG2 VAL A 86 2999 3492 2602 187 -188 -64 C ATOM 666 N LEU A 87 26.918 185.085 22.700 1.00 23.13 N ANISOU 666 N LEU A 87 2899 3337 2554 151 -87 -116 N ATOM 667 CA LEU A 87 26.883 186.133 21.682 1.00 23.78 C ANISOU 667 CA LEU A 87 2983 3404 2647 137 -66 -129 C ATOM 668 C LEU A 87 25.452 186.575 21.393 1.00 25.34 C ANISOU 668 C LEU A 87 3206 3586 2835 138 -51 -126 C ATOM 669 O LEU A 87 25.187 187.770 21.237 1.00 26.26 O ANISOU 669 O LEU A 87 3333 3692 2953 127 -42 -136 O ATOM 670 CB LEU A 87 27.565 185.642 20.413 1.00 24.01 C ANISOU 670 CB LEU A 87 2997 3427 2699 139 -50 -127 C ATOM 671 CG LEU A 87 29.008 185.190 20.556 1.00 26.04 C ANISOU 671 CG LEU A 87 3216 3693 2983 141 -58 -130 C ATOM 672 CD1 LEU A 87 29.525 184.753 19.179 1.00 28.21 C ANISOU 672 CD1 LEU A 87 3482 3956 3280 144 -25 -131 C ATOM 673 CD2 LEU A 87 29.867 186.288 21.145 1.00 26.09 C ANISOU 673 CD2 LEU A 87 3204 3708 3001 120 -73 -145 C ATOM 674 N ATHR A 88 24.513 185.638 21.373 0.50 24.61 N ANISOU 674 N ATHR A 88 3121 3490 2741 152 -49 -112 N ATOM 675 N BTHR A 88 24.512 185.626 21.301 0.50 24.62 N ANISOU 675 N BTHR A 88 3122 3491 2743 152 -49 -112 N ATOM 676 CA ATHR A 88 23.128 185.990 21.103 0.50 25.78 C ANISOU 676 CA ATHR A 88 3282 3622 2893 155 -39 -109 C ATOM 677 CA BTHR A 88 23.112 186.007 21.123 0.50 25.87 C ANISOU 677 CA BTHR A 88 3293 3633 2904 155 -39 -109 C ATOM 678 C ATHR A 88 22.499 186.719 22.291 0.50 23.25 C ANISOU 678 C ATHR A 88 2971 3301 2561 153 -31 -115 C ATOM 679 C BTHR A 88 22.638 186.848 22.295 0.50 23.76 C ANISOU 679 C BTHR A 88 3036 3366 2625 151 -31 -117 C ATOM 680 O ATHR A 88 21.624 187.576 22.096 0.50 24.16 O ANISOU 680 O ATHR A 88 3091 3399 2688 153 -19 -119 O ATOM 681 O BTHR A 88 21.985 187.881 22.106 0.50 24.19 O ANISOU 681 O BTHR A 88 3097 3404 2689 148 -20 -124 O ATOM 682 CB ATHR A 88 22.381 184.704 20.744 0.50 24.25 C ANISOU 682 CB ATHR A 88 3085 3421 2710 166 -41 -95 C ATOM 683 CB BTHR A 88 22.206 184.771 20.970 0.50 24.43 C ANISOU 683 CB BTHR A 88 3108 3443 2731 166 -39 -94 C ATOM 684 OG1ATHR A 88 23.139 183.989 19.746 0.50 26.55 O ANISOU 684 OG1ATHR A 88 3371 3711 3005 168 -45 -97 O ATOM 685 OG1BTHR A 88 22.320 183.920 22.134 0.50 29.72 O ANISOU 685 OG1BTHR A 88 3776 4123 3392 173 -40 -83 O ATOM 686 CG2ATHR A 88 21.017 184.968 20.242 0.50 24.40 C ANISOU 686 CG2ATHR A 88 3106 3421 2744 168 -39 -91 C ATOM 687 CG2BTHR A 88 22.592 183.970 19.746 0.50 24.97 C ANISOU 687 CG2BTHR A 88 3173 3505 2808 169 -45 -94 C ATOM 688 N GLN A 89 22.923 186.400 23.526 1.00 23.38 N ANISOU 688 N GLN A 89 2994 3336 2555 154 -36 -116 N ATOM 689 CA GLN A 89 22.445 187.131 24.690 1.00 23.39 C ANISOU 689 CA GLN A 89 3015 3338 2534 150 -23 -129 C ATOM 690 C GLN A 89 23.022 188.536 24.714 1.00 24.34 C ANISOU 690 C GLN A 89 3140 3454 2654 134 -26 -157 C ATOM 691 O GLN A 89 22.328 189.491 25.071 1.00 24.80 O ANISOU 691 O GLN A 89 3213 3496 2714 132 -5 -172 O ATOM 692 CB GLN A 89 22.797 186.401 25.974 1.00 23.55 C ANISOU 692 CB GLN A 89 3051 3381 2517 154 -33 -121 C ATOM 693 CG GLN A 89 21.943 186.880 27.158 1.00 25.92 C ANISOU 693 CG GLN A 89 3381 3680 2786 154 -5 -131 C ATOM 694 CD GLN A 89 20.483 186.542 26.905 1.00 28.58 C ANISOU 694 CD GLN A 89 3711 3994 3152 165 33 -115 C ATOM 695 OE1 GLN A 89 20.188 185.479 26.353 1.00 28.62 O ANISOU 695 OE1 GLN A 89 3699 3994 3182 173 30 -91 O ATOM 696 NE2 GLN A 89 19.572 187.454 27.243 1.00 31.10 N ANISOU 696 NE2 GLN A 89 4040 4298 3479 164 68 -132 N ATOM 697 N SER A 90 24.292 188.687 24.325 1.00 25.31 N ANISOU 697 N SER A 90 3248 3585 2783 123 -47 -163 N ATOM 698 CA SER A 90 24.874 190.019 24.230 1.00 26.50 C ANISOU 698 CA SER A 90 3399 3725 2945 103 -48 -189 C ATOM 699 C SER A 90 24.144 190.859 23.194 1.00 24.49 C ANISOU 699 C SER A 90 3147 3440 2719 103 -24 -185 C ATOM 700 O SER A 90 23.891 192.051 23.425 1.00 24.36 O ANISOU 700 O SER A 90 3142 3402 2712 94 -11 -203 O ATOM 701 CB SER A 90 26.370 189.930 23.900 1.00 29.06 C ANISOU 701 CB SER A 90 3697 4061 3284 90 -70 -193 C ATOM 702 OG SER A 90 26.903 191.234 23.758 1.00 29.41 O ANISOU 702 OG SER A 90 3738 4088 3348 67 -66 -217 O ATOM 703 N SER A 91 23.743 190.246 22.080 1.00 22.44 N ANISOU 703 N SER A 91 2881 3175 2472 115 -20 -160 N ATOM 704 CA SER A 91 22.983 190.966 21.062 1.00 22.66 C ANISOU 704 CA SER A 91 2914 3174 2520 118 -8 -150 C ATOM 705 C SER A 91 21.655 191.447 21.629 1.00 24.69 C ANISOU 705 C SER A 91 3179 3413 2789 130 6 -153 C ATOM 706 O SER A 91 21.242 192.586 21.387 1.00 25.44 O ANISOU 706 O SER A 91 3279 3480 2906 129 17 -156 O ATOM 707 CB SER A 91 22.740 190.077 19.836 1.00 22.19 C ANISOU 707 CB SER A 91 2852 3117 2461 128 -15 -127 C ATOM 708 OG SER A 91 23.981 189.728 19.201 1.00 24.49 O ANISOU 708 OG SER A 91 3138 3420 2748 119 -15 -127 O ATOM 709 N ILE A 92 20.961 190.585 22.376 1.00 25.65 N ANISOU 709 N ILE A 92 3298 3547 2900 141 10 -149 N ATOM 710 CA ILE A 92 19.693 190.964 22.987 1.00 26.27 C ANISOU 710 CA ILE A 92 3379 3608 2996 153 33 -153 C ATOM 711 C ILE A 92 19.861 192.171 23.915 1.00 27.00 C ANISOU 711 C ILE A 92 3489 3688 3083 144 54 -184 C ATOM 712 O ILE A 92 19.049 193.104 23.888 1.00 29.27 O ANISOU 712 O ILE A 92 3775 3943 3402 152 76 -191 O ATOM 713 CB ILE A 92 19.081 189.759 23.708 1.00 29.06 C ANISOU 713 CB ILE A 92 3728 3976 3339 162 43 -143 C ATOM 714 CG1 ILE A 92 18.522 188.803 22.659 1.00 34.73 C ANISOU 714 CG1 ILE A 92 4425 4690 4081 170 26 -118 C ATOM 715 CG2 ILE A 92 18.003 190.223 24.702 1.00 28.94 C ANISOU 715 CG2 ILE A 92 3718 3945 3334 170 83 -154 C ATOM 716 CD1 ILE A 92 18.302 187.438 23.143 1.00 38.88 C ANISOU 716 CD1 ILE A 92 4945 5228 4598 175 29 -104 C ATOM 717 N PHE A 93 20.884 192.157 24.769 1.00 26.22 N ANISOU 717 N PHE A 93 3405 3611 2946 129 45 -205 N ATOM 718 CA PHE A 93 21.119 193.294 25.670 1.00 26.68 C ANISOU 718 CA PHE A 93 3485 3657 2995 116 58 -244 C ATOM 719 C PHE A 93 21.427 194.576 24.910 1.00 26.14 C ANISOU 719 C PHE A 93 3413 3554 2965 105 60 -253 C ATOM 720 O PHE A 93 20.947 195.663 25.280 1.00 27.12 O ANISOU 720 O PHE A 93 3550 3646 3109 105 86 -277 O ATOM 721 CB PHE A 93 22.259 192.981 26.626 1.00 30.56 C ANISOU 721 CB PHE A 93 3992 4182 3438 100 32 -264 C ATOM 722 CG PHE A 93 21.884 191.977 27.727 1.00 36.57 C ANISOU 722 CG PHE A 93 4774 4971 4151 110 38 -257 C ATOM 723 CD1 PHE A 93 20.617 191.956 28.287 1.00 44.74 C ANISOU 723 CD1 PHE A 93 5824 5993 5183 125 82 -257 C ATOM 724 CD2 PHE A 93 22.811 191.071 28.181 1.00 33.56 C ANISOU 724 CD2 PHE A 93 4395 4625 3732 106 1 -247 C ATOM 725 CE1 PHE A 93 20.291 191.028 29.307 1.00 44.85 C ANISOU 725 CE1 PHE A 93 5861 6029 5149 132 96 -245 C ATOM 726 CE2 PHE A 93 22.501 190.147 29.201 1.00 34.21 C ANISOU 726 CE2 PHE A 93 4503 4730 3767 116 5 -233 C ATOM 727 CZ PHE A 93 21.249 190.131 29.755 1.00 38.95 C ANISOU 727 CZ PHE A 93 5124 5318 4357 128 55 -231 C ATOM 728 N SER A 94 22.243 194.485 23.863 1.00 25.67 N ANISOU 728 N SER A 94 3337 3497 2917 96 39 -235 N ATOM 729 CA SER A 94 22.524 195.669 23.045 1.00 28.45 C ANISOU 729 CA SER A 94 3689 3814 3306 85 46 -235 C ATOM 730 C SER A 94 21.258 196.208 22.400 1.00 28.70 C ANISOU 730 C SER A 94 3721 3810 3375 106 64 -214 C ATOM 731 O SER A 94 21.023 197.424 22.398 1.00 28.28 O ANISOU 731 O SER A 94 3676 3715 3355 104 82 -225 O ATOM 732 CB SER A 94 23.577 195.336 21.992 1.00 30.92 C ANISOU 732 CB SER A 94 3988 4138 3622 73 31 -214 C ATOM 733 OG SER A 94 24.818 195.085 22.634 1.00 30.80 O ANISOU 733 OG SER A 94 3963 4149 3592 52 13 -237 O ATOM 734 N LEU A 95 20.410 195.323 21.872 1.00 27.34 N ANISOU 734 N LEU A 95 3537 3648 3203 128 56 -184 N ATOM 735 CA LEU A 95 19.174 195.776 21.244 1.00 26.14 C ANISOU 735 CA LEU A 95 3377 3462 3091 150 62 -161 C ATOM 736 C LEU A 95 18.240 196.431 22.248 1.00 25.66 C ANISOU 736 C LEU A 95 3316 3375 3059 162 95 -184 C ATOM 737 O LEU A 95 17.580 197.444 21.940 1.00 27.89 O ANISOU 737 O LEU A 95 3595 3613 3390 175 107 -178 O ATOM 738 CB LEU A 95 18.477 194.607 20.541 1.00 25.95 C ANISOU 738 CB LEU A 95 3339 3457 3065 166 39 -130 C ATOM 739 CG LEU A 95 19.234 194.074 19.312 1.00 28.54 C ANISOU 739 CG LEU A 95 3673 3802 3368 157 12 -107 C ATOM 740 CD1 LEU A 95 18.621 192.742 18.867 1.00 31.45 C ANISOU 740 CD1 LEU A 95 4030 4192 3729 168 -10 -91 C ATOM 741 CD2 LEU A 95 19.210 195.081 18.174 1.00 27.53 C ANISOU 741 CD2 LEU A 95 3559 3643 3259 158 5 -82 C ATOM 742 N LEU A 96 18.162 195.871 23.455 1.00 24.80 N ANISOU 742 N LEU A 96 3212 3289 2920 160 112 -210 N ATOM 743 CA LEU A 96 17.307 196.451 24.476 1.00 26.69 C ANISOU 743 CA LEU A 96 3458 3504 3178 171 156 -237 C ATOM 744 C LEU A 96 17.817 197.810 24.930 1.00 27.08 C ANISOU 744 C LEU A 96 3530 3521 3236 157 174 -276 C ATOM 745 O LEU A 96 17.025 198.746 25.139 1.00 28.69 O ANISOU 745 O LEU A 96 3733 3680 3487 172 209 -290 O ATOM 746 CB LEU A 96 17.192 195.483 25.659 1.00 30.21 C ANISOU 746 CB LEU A 96 3916 3986 3577 170 174 -252 C ATOM 747 CG LEU A 96 16.373 195.929 26.867 1.00 35.07 C ANISOU 747 CG LEU A 96 4547 4583 4195 179 231 -284 C ATOM 748 CD1 LEU A 96 14.963 196.154 26.512 1.00 36.46 C ANISOU 748 CD1 LEU A 96 4688 4722 4442 207 261 -267 C ATOM 749 CD2 LEU A 96 16.475 194.872 27.964 1.00 35.97 C ANISOU 749 CD2 LEU A 96 4684 4738 4244 174 244 -290 C ATOM 750 N ALA A 97 19.128 197.956 25.044 1.00 28.03 N ANISOU 750 N ALA A 97 3668 3659 3323 129 152 -294 N ATOM 751 CA ALA A 97 19.690 199.226 25.454 1.00 29.16 C ANISOU 751 CA ALA A 97 3831 3769 3479 110 165 -335 C ATOM 752 C ALA A 97 19.405 200.299 24.411 1.00 28.74 C ANISOU 752 C ALA A 97 3768 3660 3492 117 172 -313 C ATOM 753 O ALA A 97 19.117 201.446 24.763 1.00 30.16 O ANISOU 753 O ALA A 97 3959 3790 3710 118 202 -341 O ATOM 754 CB ALA A 97 21.194 199.090 25.666 1.00 30.06 C ANISOU 754 CB ALA A 97 3954 3913 3556 75 131 -354 C ATOM 755 N ILE A 98 19.555 199.963 23.122 1.00 25.62 N ANISOU 755 N ILE A 98 3357 3271 3108 122 145 -263 N ATOM 756 CA ILE A 98 19.240 200.919 22.060 1.00 25.71 C ANISOU 756 CA ILE A 98 3364 3231 3173 132 147 -230 C ATOM 757 C ILE A 98 17.809 201.401 22.177 1.00 28.33 C ANISOU 757 C ILE A 98 3684 3521 3558 167 170 -224 C ATOM 758 O ILE A 98 17.532 202.601 22.048 1.00 30.02 O ANISOU 758 O ILE A 98 3902 3676 3827 174 191 -226 O ATOM 759 CB ILE A 98 19.512 200.304 20.681 1.00 27.66 C ANISOU 759 CB ILE A 98 3605 3499 3407 134 114 -177 C ATOM 760 CG1 ILE A 98 21.020 200.195 20.505 1.00 29.37 C ANISOU 760 CG1 ILE A 98 3829 3738 3593 99 106 -186 C ATOM 761 CG2 ILE A 98 18.945 201.193 19.591 1.00 31.60 C ANISOU 761 CG2 ILE A 98 4106 3947 3952 152 112 -133 C ATOM 762 CD1 ILE A 98 21.470 199.316 19.327 1.00 32.09 C ANISOU 762 CD1 ILE A 98 4171 4114 3907 98 83 -145 C ATOM 763 N ALA A 99 16.875 200.489 22.412 1.00 30.13 N ANISOU 763 N ALA A 99 3892 3774 3781 189 170 -214 N ATOM 764 CA ALA A 99 15.474 200.894 22.487 1.00 30.84 C ANISOU 764 CA ALA A 99 3959 3825 3936 224 193 -205 C ATOM 765 C ALA A 99 15.240 201.863 23.632 1.00 31.09 C ANISOU 765 C ALA A 99 4004 3815 3993 225 249 -258 C ATOM 766 O ALA A 99 14.519 202.859 23.488 1.00 32.13 O ANISOU 766 O ALA A 99 4125 3887 4197 248 272 -255 O ATOM 767 CB ALA A 99 14.591 199.667 22.645 1.00 29.56 C ANISOU 767 CB ALA A 99 3767 3697 3766 240 189 -191 C ATOM 768 N ILE A 100 15.801 201.554 24.798 1.00 31.17 N ANISOU 768 N ILE A 100 4040 3856 3946 203 269 -308 N ATOM 769 CA ILE A 100 15.620 202.413 25.961 1.00 31.51 C ANISOU 769 CA ILE A 100 4108 3866 3999 201 323 -368 C ATOM 770 C ILE A 100 16.293 203.753 25.730 1.00 31.13 C ANISOU 770 C ILE A 100 4079 3764 3985 184 325 -389 C ATOM 771 O ILE A 100 15.789 204.795 26.147 1.00 30.54 O ANISOU 771 O ILE A 100 4011 3629 3962 196 370 -420 O ATOM 772 CB ILE A 100 16.153 201.701 27.220 1.00 33.26 C ANISOU 772 CB ILE A 100 4363 4139 4134 179 334 -412 C ATOM 773 CG1 ILE A 100 15.252 200.504 27.563 1.00 36.36 C ANISOU 773 CG1 ILE A 100 4737 4568 4509 199 350 -391 C ATOM 774 CG2 ILE A 100 16.244 202.664 28.432 1.00 32.01 C ANISOU 774 CG2 ILE A 100 4247 3949 3965 167 382 -485 C ATOM 775 CD1 ILE A 100 15.873 199.541 28.544 1.00 41.57 C ANISOU 775 CD1 ILE A 100 5431 5287 5076 179 345 -411 C ATOM 776 N ASP A 101 17.454 203.746 25.079 1.00 28.31 N ANISOU 776 N ASP A 101 3729 3424 3604 156 283 -373 N ATOM 777 CA ASP A 101 18.151 204.994 24.773 1.00 28.73 C ANISOU 777 CA ASP A 101 3797 3423 3696 135 286 -386 C ATOM 778 C ASP A 101 17.262 205.927 23.953 1.00 32.91 C ANISOU 778 C ASP A 101 4310 3881 4314 167 302 -348 C ATOM 779 O ASP A 101 17.130 207.115 24.262 1.00 35.91 O ANISOU 779 O ASP A 101 4703 4193 4749 168 337 -378 O ATOM 780 CB ASP A 101 19.454 204.670 24.031 1.00 27.96 C ANISOU 780 CB ASP A 101 3699 3357 3567 102 243 -362 C ATOM 781 CG ASP A 101 20.186 205.914 23.578 1.00 31.55 C ANISOU 781 CG ASP A 101 4164 3753 4070 77 249 -366 C ATOM 782 OD1 ASP A 101 20.819 206.562 24.420 1.00 34.31 O ANISOU 782 OD1 ASP A 101 4532 4082 4420 47 262 -427 O ATOM 783 OD2 ASP A 101 20.110 206.257 22.387 1.00 32.33 O ANISOU 783 OD2 ASP A 101 4254 3822 4206 87 242 -309 O ATOM 784 N ARG A 102 16.638 205.402 22.899 1.00 33.49 N ANISOU 784 N ARG A 102 4356 3965 4402 195 274 -281 N ATOM 785 CA ARG A 102 15.777 206.216 22.047 1.00 35.07 C ANISOU 785 CA ARG A 102 4540 4102 4684 229 275 -234 C ATOM 786 C ARG A 102 14.506 206.635 22.777 1.00 34.75 C ANISOU 786 C ARG A 102 4478 4017 4707 266 321 -259 C ATOM 787 O ARG A 102 13.944 207.696 22.488 1.00 35.13 O ANISOU 787 O ARG A 102 4518 3992 4838 292 339 -245 O ATOM 788 CB ARG A 102 15.456 205.445 20.758 1.00 34.82 C ANISOU 788 CB ARG A 102 4489 4101 4639 247 222 -159 C ATOM 789 CG ARG A 102 16.664 205.153 19.872 1.00 34.31 C ANISOU 789 CG ARG A 102 4448 4069 4520 215 188 -130 C ATOM 790 CD ARG A 102 17.305 206.467 19.354 1.00 36.34 C ANISOU 790 CD ARG A 102 4728 4261 4817 200 202 -116 C ATOM 791 NE ARG A 102 18.205 207.079 20.337 1.00 37.54 N ANISOU 791 NE ARG A 102 4897 4395 4970 163 236 -182 N ATOM 792 CZ ARG A 102 18.536 208.368 20.359 1.00 37.33 C ANISOU 792 CZ ARG A 102 4887 4297 5000 151 264 -194 C ATOM 793 NH1 ARG A 102 18.030 209.215 19.472 1.00 38.27 N ANISOU 793 NH1 ARG A 102 5008 4352 5180 175 265 -138 N ATOM 794 NH2 ARG A 102 19.347 208.817 21.283 1.00 36.13 N ANISOU 794 NH2 ARG A 102 4749 4135 4845 113 287 -261 N ATOM 795 N TYR A 103 14.045 205.836 23.738 1.00 33.43 N ANISOU 795 N TYR A 103 4304 3891 4508 271 345 -295 N ATOM 796 CA TYR A 103 12.871 206.209 24.509 1.00 33.92 C ANISOU 796 CA TYR A 103 4345 3912 4630 304 403 -324 C ATOM 797 C TYR A 103 13.170 207.374 25.443 1.00 34.31 C ANISOU 797 C TYR A 103 4430 3905 4700 292 460 -394 C ATOM 798 O TYR A 103 12.384 208.335 25.538 1.00 34.79 O ANISOU 798 O TYR A 103 4477 3892 4850 323 503 -403 O ATOM 799 CB TYR A 103 12.366 204.994 25.286 1.00 35.94 C ANISOU 799 CB TYR A 103 4589 4227 4839 308 422 -340 C ATOM 800 CG TYR A 103 11.200 205.317 26.189 1.00 42.84 C ANISOU 800 CG TYR A 103 5444 5062 5771 339 497 -375 C ATOM 801 CD1 TYR A 103 9.943 205.568 25.664 1.00 46.44 C ANISOU 801 CD1 TYR A 103 5841 5472 6331 384 506 -337 C ATOM 802 CD2 TYR A 103 11.369 205.404 27.561 1.00 46.85 C ANISOU 802 CD2 TYR A 103 5993 5576 6230 323 560 -447 C ATOM 803 CE1 TYR A 103 8.881 205.891 26.482 1.00 49.34 C ANISOU 803 CE1 TYR A 103 6184 5799 6764 414 584 -370 C ATOM 804 CE2 TYR A 103 10.309 205.726 28.391 1.00 51.04 C ANISOU 804 CE2 TYR A 103 6511 6069 6813 351 642 -483 C ATOM 805 CZ TYR A 103 9.072 205.959 27.842 1.00 55.03 C ANISOU 805 CZ TYR A 103 6951 6527 7432 397 658 -444 C ATOM 806 OH TYR A 103 8.017 206.271 28.659 1.00 64.57 O ANISOU 806 OH TYR A 103 8138 7693 8701 427 747 -479 O ATOM 807 N ILE A 104 14.299 207.316 26.142 1.00 34.54 N ANISOU 807 N ILE A 104 4505 3966 4652 248 459 -446 N ATOM 808 CA ILE A 104 14.710 208.455 26.969 1.00 37.82 C ANISOU 808 CA ILE A 104 4959 4327 5082 228 503 -519 C ATOM 809 C ILE A 104 14.851 209.716 26.122 1.00 39.07 C ANISOU 809 C ILE A 104 5114 4403 5329 233 500 -495 C ATOM 810 O ILE A 104 14.447 210.812 26.533 1.00 38.96 O ANISOU 810 O ILE A 104 5108 4310 5384 247 551 -534 O ATOM 811 CB ILE A 104 16.024 208.118 27.684 1.00 37.69 C ANISOU 811 CB ILE A 104 4987 4364 4969 176 479 -570 C ATOM 812 CG1 ILE A 104 15.824 206.926 28.643 1.00 39.63 C ANISOU 812 CG1 ILE A 104 5247 4686 5127 174 488 -593 C ATOM 813 CG2 ILE A 104 16.582 209.371 28.417 1.00 36.36 C ANISOU 813 CG2 ILE A 104 4860 4135 4818 147 511 -649 C ATOM 814 CD1 ILE A 104 17.153 206.396 29.195 1.00 40.84 C ANISOU 814 CD1 ILE A 104 5435 4901 5182 127 444 -625 C ATOM 815 N ALA A 105 15.451 209.586 24.937 1.00 38.08 N ANISOU 815 N ALA A 105 4978 4290 5202 222 444 -430 N ATOM 816 CA ALA A 105 15.713 210.745 24.083 1.00 38.76 C ANISOU 816 CA ALA A 105 5066 4298 5361 222 440 -397 C ATOM 817 C ALA A 105 14.426 211.426 23.632 1.00 38.31 C ANISOU 817 C ALA A 105 4980 4169 5409 278 462 -357 C ATOM 818 O ALA A 105 14.391 212.658 23.520 1.00 39.28 O ANISOU 818 O ALA A 105 5112 4203 5611 285 490 -363 O ATOM 819 CB ALA A 105 16.558 210.327 22.867 1.00 41.36 C ANISOU 819 CB ALA A 105 5395 4664 5655 201 382 -329 C ATOM 820 N ILE A 106 13.360 210.668 23.386 1.00 38.29 N ANISOU 820 N ILE A 106 4937 4195 5416 319 450 -317 N ATOM 821 CA ILE A 106 12.107 211.270 22.946 1.00 43.34 C ANISOU 821 CA ILE A 106 5536 4765 6164 375 463 -276 C ATOM 822 C ILE A 106 11.216 211.720 24.103 1.00 43.54 C ANISOU 822 C ILE A 106 5549 4744 6249 402 541 -343 C ATOM 823 O ILE A 106 10.329 212.571 23.899 1.00 44.46 O ANISOU 823 O ILE A 106 5635 4779 6477 447 567 -324 O ATOM 824 CB ILE A 106 11.305 210.314 22.041 1.00 47.78 C ANISOU 824 CB ILE A 106 6052 5373 6727 407 406 -200 C ATOM 825 CG1 ILE A 106 10.303 211.119 21.191 1.00 50.34 C ANISOU 825 CG1 ILE A 106 6339 5620 7167 461 389 -135 C ATOM 826 CG2 ILE A 106 10.561 209.258 22.847 1.00 49.38 C ANISOU 826 CG2 ILE A 106 6225 5632 6907 419 428 -231 C ATOM 827 CD1 ILE A 106 10.057 210.534 19.838 1.00 50.65 C ANISOU 827 CD1 ILE A 106 6360 5694 7192 476 305 -44 C ATOM 828 N ARG A 107 11.417 211.174 25.299 1.00 42.51 N ANISOU 828 N ARG A 107 5442 4662 6049 378 581 -416 N ATOM 829 CA ARG A 107 10.585 211.466 26.457 1.00 47.22 C ANISOU 829 CA ARG A 107 6035 5223 6683 401 666 -484 C ATOM 830 C ARG A 107 11.139 212.625 27.278 1.00 46.20 C ANISOU 830 C ARG A 107 5959 5030 6567 378 722 -567 C ATOM 831 O ARG A 107 10.384 213.522 27.672 1.00 48.50 O ANISOU 831 O ARG A 107 6240 5237 6950 411 789 -600 O ATOM 832 CB ARG A 107 10.453 210.204 27.328 1.00 58.89 C ANISOU 832 CB ARG A 107 7519 6789 8069 388 683 -515 C ATOM 833 CG ARG A 107 9.152 210.108 28.096 1.00 72.41 C ANISOU 833 CG ARG A 107 9198 8478 9837 429 763 -542 C ATOM 834 CD ARG A 107 7.988 209.782 27.186 1.00 78.31 C ANISOU 834 CD ARG A 107 9862 9211 10679 478 738 -463 C ATOM 835 NE ARG A 107 6.747 209.666 27.940 1.00 79.64 N ANISOU 835 NE ARG A 107 9989 9357 10913 515 821 -489 N ATOM 836 N ILE A 108 12.443 212.641 27.543 1.00 45.57 N ANISOU 836 N ILE A 108 5931 4981 6403 322 695 -605 N ATOM 837 CA ILE A 108 13.026 213.713 28.348 1.00 47.89 C ANISOU 837 CA ILE A 108 6277 5215 6705 292 740 -693 C ATOM 838 C ILE A 108 14.274 214.224 27.639 1.00 44.01 C ANISOU 838 C ILE A 108 5804 4707 6209 248 685 -673 C ATOM 839 O ILE A 108 15.405 214.097 28.142 1.00 42.70 O ANISOU 839 O ILE A 108 5679 4581 5966 194 663 -724 O ATOM 840 CB ILE A 108 13.306 213.245 29.784 1.00 55.18 C ANISOU 840 CB ILE A 108 7251 6191 7525 262 776 -786 C ATOM 841 CG1 ILE A 108 14.056 211.920 29.787 1.00 60.71 C ANISOU 841 CG1 ILE A 108 7958 7005 8104 229 711 -763 C ATOM 842 CG2 ILE A 108 11.982 213.090 30.550 1.00 55.77 C ANISOU 842 CG2 ILE A 108 7310 6250 7628 308 859 -815 C ATOM 843 CD1 ILE A 108 14.512 211.491 31.168 1.00 66.93 C ANISOU 843 CD1 ILE A 108 8806 7847 8779 195 732 -848 C ATOM 844 N PRO A 109 14.106 214.851 26.478 1.00 44.20 N ANISOU 844 N PRO A 109 5801 4671 6321 271 664 -599 N ATOM 845 CA PRO A 109 15.276 215.228 25.675 1.00 45.94 C ANISOU 845 CA PRO A 109 6037 4881 6537 229 618 -566 C ATOM 846 C PRO A 109 16.180 216.250 26.338 1.00 48.04 C ANISOU 846 C PRO A 109 6346 5087 6818 181 645 -649 C ATOM 847 O PRO A 109 17.387 216.279 26.054 1.00 46.47 O ANISOU 847 O PRO A 109 6164 4909 6586 128 608 -648 O ATOM 848 CB PRO A 109 14.640 215.782 24.392 1.00 45.79 C ANISOU 848 CB PRO A 109 5986 4798 6615 274 602 -467 C ATOM 849 CG PRO A 109 13.278 216.153 24.771 1.00 45.69 C ANISOU 849 CG PRO A 109 5946 4729 6687 333 653 -478 C ATOM 850 CD PRO A 109 12.846 215.201 25.815 1.00 44.95 C ANISOU 850 CD PRO A 109 5849 4707 6524 336 679 -535 C ATOM 851 N LEU A 110 15.635 217.113 27.199 1.00 52.06 N ANISOU 851 N LEU A 110 6874 5521 7384 195 712 -723 N ATOM 852 CA LEU A 110 16.472 218.089 27.881 1.00 58.02 C ANISOU 852 CA LEU A 110 7674 6216 8155 146 737 -813 C ATOM 853 C LEU A 110 17.328 217.463 28.979 1.00 58.50 C ANISOU 853 C LEU A 110 7774 6358 8094 91 718 -900 C ATOM 854 O LEU A 110 18.359 218.034 29.342 1.00 59.48 O ANISOU 854 O LEU A 110 7930 6459 8211 34 706 -962 O ATOM 855 CB LEU A 110 15.586 219.197 28.453 1.00 64.17 C ANISOU 855 CB LEU A 110 8465 6885 9034 181 818 -870 C ATOM 856 CG LEU A 110 14.783 219.940 27.382 1.00 69.12 C ANISOU 856 CG LEU A 110 9051 7418 9794 237 831 -781 C ATOM 857 CD1 LEU A 110 13.614 220.693 27.995 1.00 72.73 C ANISOU 857 CD1 LEU A 110 9503 7784 10349 290 916 -829 C ATOM 858 CD2 LEU A 110 15.682 220.889 26.603 1.00 70.51 C ANISOU 858 CD2 LEU A 110 9239 7519 10032 202 810 -749 C ATOM 859 N ARG A 111 16.924 216.318 29.520 1.00 61.42 N ANISOU 859 N ARG A 111 8143 6820 8372 106 713 -906 N ATOM 860 CA ARG A 111 17.718 215.595 30.504 1.00 74.31 C ANISOU 860 CA ARG A 111 9814 8539 9881 60 684 -973 C ATOM 861 C ARG A 111 18.595 214.512 29.884 1.00 57.17 C ANISOU 861 C ARG A 111 7620 6464 7637 33 604 -910 C ATOM 862 O ARG A 111 19.454 213.951 30.581 1.00 49.05 O ANISOU 862 O ARG A 111 6618 5504 6516 -9 566 -956 O ATOM 863 CB ARG A 111 16.791 214.968 31.555 1.00107.91 C ANISOU 863 CB ARG A 111 14091 12836 14074 90 734 -1016 C ATOM 864 CG ARG A 111 16.099 215.991 32.458 1.00138.59 C ANISOU 864 CG ARG A 111 18013 16634 18009 106 823 -1106 C ATOM 865 CD ARG A 111 14.784 215.466 33.015 1.00161.73 C ANISOU 865 CD ARG A 111 20938 19583 20931 159 893 -1109 C ATOM 866 NE ARG A 111 13.738 216.485 32.983 1.00179.99 N ANISOU 866 NE ARG A 111 23233 21786 23369 207 976 -1125 N ATOM 867 CZ ARG A 111 13.185 216.953 31.867 1.00191.81 C ANISOU 867 CZ ARG A 111 24670 23219 24991 249 973 -1044 C ATOM 868 NH1 ARG A 111 12.236 217.877 31.929 1.00194.95 N ANISOU 868 NH1 ARG A 111 25051 23514 25508 295 1049 -1062 N ATOM 869 NH2 ARG A 111 13.590 216.507 30.685 1.00196.09 N ANISOU 869 NH2 ARG A 111 25171 23797 25538 245 893 -946 N ATOM 870 N TYR A 112 18.419 214.215 28.593 1.00 52.55 N ANISOU 870 N TYR A 112 6989 5884 7093 58 576 -807 N ATOM 871 CA TYR A 112 19.074 213.053 28.009 1.00 49.02 C ANISOU 871 CA TYR A 112 6520 5531 6575 42 512 -748 C ATOM 872 C TYR A 112 20.583 213.122 28.198 1.00 48.50 C ANISOU 872 C TYR A 112 6470 5489 6471 -23 467 -785 C ATOM 873 O TYR A 112 21.205 212.177 28.700 1.00 47.34 O ANISOU 873 O TYR A 112 6328 5426 6232 -47 426 -804 O ATOM 874 CB TYR A 112 18.700 212.935 26.531 1.00 47.41 C ANISOU 874 CB TYR A 112 6276 5315 6425 75 492 -639 C ATOM 875 CG TYR A 112 19.453 211.847 25.804 1.00 45.22 C ANISOU 875 CG TYR A 112 5979 5121 6082 56 432 -580 C ATOM 876 CD1 TYR A 112 19.004 210.524 25.799 1.00 44.43 C ANISOU 876 CD1 TYR A 112 5862 5103 5915 79 410 -549 C ATOM 877 CD2 TYR A 112 20.625 212.137 25.148 1.00 44.22 C ANISOU 877 CD2 TYR A 112 5851 4987 5965 14 404 -560 C ATOM 878 CE1 TYR A 112 19.718 209.530 25.135 1.00 42.88 C ANISOU 878 CE1 TYR A 112 5650 4978 5663 63 359 -501 C ATOM 879 CE2 TYR A 112 21.337 211.167 24.488 1.00 43.15 C ANISOU 879 CE2 TYR A 112 5697 4923 5775 -1 359 -512 C ATOM 880 CZ TYR A 112 20.870 209.856 24.482 1.00 42.16 C ANISOU 880 CZ TYR A 112 5558 4878 5583 25 336 -484 C ATOM 881 OH TYR A 112 21.580 208.894 23.838 1.00 40.20 O ANISOU 881 OH TYR A 112 5293 4695 5285 11 295 -441 O ATOM 882 N ASN A 113 21.188 214.250 27.843 1.00 51.99 N ANISOU 882 N ASN A 113 6914 5852 6987 -53 474 -798 N ATOM 883 CA ASN A 113 22.641 214.313 27.830 1.00 59.92 C ANISOU 883 CA ASN A 113 7917 6875 7974 -117 429 -821 C ATOM 884 C ASN A 113 23.258 214.333 29.229 1.00 59.62 C ANISOU 884 C ASN A 113 7916 6864 7875 -160 412 -931 C ATOM 885 O ASN A 113 24.460 214.097 29.356 1.00 62.52 O ANISOU 885 O ASN A 113 8274 7269 8213 -211 361 -952 O ATOM 886 CB ASN A 113 23.084 215.530 27.030 1.00 67.76 C ANISOU 886 CB ASN A 113 8902 7770 9073 -139 448 -800 C ATOM 887 CG ASN A 113 22.924 215.322 25.538 1.00 71.99 C ANISOU 887 CG ASN A 113 9407 8304 9644 -112 442 -683 C ATOM 888 OD1 ASN A 113 23.473 214.378 24.967 1.00 70.14 O ANISOU 888 OD1 ASN A 113 9150 8144 9357 -120 403 -633 O ATOM 889 ND2 ASN A 113 22.152 216.188 24.903 1.00 76.41 N ANISOU 889 ND2 ASN A 113 9967 8776 10289 -76 481 -639 N ATOM 890 N GLY A 114 22.482 214.587 30.272 1.00 56.88 N ANISOU 890 N GLY A 114 7610 6498 7505 -142 453 -1001 N ATOM 891 CA GLY A 114 23.025 214.517 31.613 1.00 58.33 C ANISOU 891 CA GLY A 114 7839 6716 7609 -182 432 -1103 C ATOM 892 C GLY A 114 22.847 213.145 32.233 1.00 59.67 C ANISOU 892 C GLY A 114 8021 6995 7658 -166 404 -1095 C ATOM 893 O GLY A 114 23.550 212.766 33.177 1.00 65.52 O ANISOU 893 O GLY A 114 8793 7790 8312 -202 359 -1156 O ATOM 894 N LEU A 115 21.886 212.395 31.707 1.00 53.23 N ANISOU 894 N LEU A 115 7180 6208 6838 -112 428 -1020 N ATOM 895 CA LEU A 115 21.560 211.064 32.196 1.00 50.12 C ANISOU 895 CA LEU A 115 6793 5908 6342 -91 412 -1000 C ATOM 896 C LEU A 115 22.367 209.999 31.471 1.00 48.97 C ANISOU 896 C LEU A 115 6605 5837 6163 -102 343 -930 C ATOM 897 O LEU A 115 22.927 209.092 32.099 1.00 47.19 O ANISOU 897 O LEU A 115 6394 5689 5848 -120 297 -943 O ATOM 898 CB LEU A 115 20.069 210.804 31.988 1.00 49.85 C ANISOU 898 CB LEU A 115 6746 5861 6335 -28 476 -957 C ATOM 899 CG LEU A 115 19.327 209.629 32.603 1.00 56.85 C ANISOU 899 CG LEU A 115 7643 6818 7139 2 493 -944 C ATOM 900 CD1 LEU A 115 17.949 209.514 31.947 1.00 58.32 C ANISOU 900 CD1 LEU A 115 7789 6974 7396 60 545 -882 C ATOM 901 CD2 LEU A 115 20.075 208.328 32.459 1.00 62.40 C ANISOU 901 CD2 LEU A 115 8332 7615 7762 -14 422 -899 C ATOM 902 N VAL A 116 22.398 210.085 30.146 1.00 47.78 N ANISOU 902 N VAL A 116 6407 5663 6084 -90 338 -853 N ATOM 903 CA VAL A 116 22.997 209.066 29.301 1.00 44.44 C ANISOU 903 CA VAL A 116 5944 5304 5637 -93 287 -781 C ATOM 904 C VAL A 116 24.337 209.615 28.834 1.00 43.40 C ANISOU 904 C VAL A 116 5793 5151 5546 -144 252 -787 C ATOM 905 O VAL A 116 24.408 210.415 27.901 1.00 47.79 O ANISOU 905 O VAL A 116 6330 5643 6184 -147 272 -754 O ATOM 906 CB VAL A 116 22.079 208.715 28.130 1.00 44.00 C ANISOU 906 CB VAL A 116 5854 5240 5622 -45 307 -691 C ATOM 907 CG1 VAL A 116 22.609 207.507 27.399 1.00 46.04 C ANISOU 907 CG1 VAL A 116 6082 5572 5840 -46 260 -628 C ATOM 908 CG2 VAL A 116 20.671 208.445 28.628 1.00 41.31 C ANISOU 908 CG2 VAL A 116 5525 4899 5270 2 353 -694 C ATOM 909 N THR A 117 25.411 209.173 29.467 1.00 38.97 N ANISOU 909 N THR A 117 5233 4642 4932 -184 198 -826 N ATOM 910 CA THR A 117 26.747 209.638 29.139 1.00 40.25 C ANISOU 910 CA THR A 117 5367 4788 5139 -236 162 -839 C ATOM 911 C THR A 117 27.569 208.483 28.601 1.00 40.62 C ANISOU 911 C THR A 117 5370 4908 5154 -242 113 -785 C ATOM 912 O THR A 117 27.294 207.309 28.884 1.00 40.54 O ANISOU 912 O THR A 117 5363 4970 5071 -215 92 -763 O ATOM 913 CB THR A 117 27.461 210.215 30.359 1.00 44.14 C ANISOU 913 CB THR A 117 5889 5272 5611 -285 131 -940 C ATOM 914 OG1 THR A 117 27.662 209.167 31.302 1.00 44.23 O ANISOU 914 OG1 THR A 117 5919 5369 5519 -284 82 -963 O ATOM 915 CG2 THR A 117 26.659 211.325 31.005 1.00 48.77 C ANISOU 915 CG2 THR A 117 6526 5784 6222 -280 184 -1006 C ATOM 916 N GLY A 118 28.595 208.826 27.819 1.00 41.66 N ANISOU 916 N GLY A 118 5461 5018 5349 -277 101 -764 N ATOM 917 CA GLY A 118 29.457 207.794 27.273 1.00 42.64 C ANISOU 917 CA GLY A 118 5540 5205 5456 -283 64 -718 C ATOM 918 C GLY A 118 30.049 206.911 28.356 1.00 44.20 C ANISOU 918 C GLY A 118 5737 5477 5580 -295 -1 -759 C ATOM 919 O GLY A 118 30.178 205.695 28.183 1.00 43.63 O ANISOU 919 O GLY A 118 5645 5470 5462 -274 -27 -716 O ATOM 920 N THR A 119 30.398 207.510 29.498 1.00 44.61 N ANISOU 920 N THR A 119 5815 5517 5617 -330 -31 -842 N ATOM 921 CA THR A 119 31.008 206.754 30.586 1.00 44.67 C ANISOU 921 CA THR A 119 5829 5594 5550 -344 -104 -881 C ATOM 922 C THR A 119 30.028 205.774 31.201 1.00 40.82 C ANISOU 922 C THR A 119 5386 5161 4963 -297 -99 -865 C ATOM 923 O THR A 119 30.400 204.641 31.536 1.00 42.14 O ANISOU 923 O THR A 119 5543 5399 5071 -287 -148 -844 O ATOM 924 CB THR A 119 31.544 207.713 31.653 1.00 52.23 C ANISOU 924 CB THR A 119 6815 6522 6510 -395 -140 -979 C ATOM 925 OG1 THR A 119 32.776 208.273 31.194 1.00 57.77 O ANISOU 925 OG1 THR A 119 7457 7193 7302 -446 -168 -991 O ATOM 926 CG2 THR A 119 31.816 206.991 32.959 1.00 53.35 C ANISOU 926 CG2 THR A 119 6990 6733 6546 -399 -212 -1023 C ATOM 927 N ARG A 120 28.775 206.184 31.373 1.00 39.40 N ANISOU 927 N ARG A 120 5253 4947 4769 -267 -38 -874 N ATOM 928 CA ARG A 120 27.787 205.258 31.898 1.00 40.03 C ANISOU 928 CA ARG A 120 5370 5075 4766 -223 -21 -854 C ATOM 929 C ARG A 120 27.483 204.160 30.885 1.00 39.85 C ANISOU 929 C ARG A 120 5307 5087 4749 -185 -12 -764 C ATOM 930 O ARG A 120 27.336 202.991 31.262 1.00 40.12 O ANISOU 930 O ARG A 120 5347 5182 4714 -163 -34 -738 O ATOM 931 CB ARG A 120 26.533 206.018 32.288 1.00 39.96 C ANISOU 931 CB ARG A 120 5410 5014 4758 -200 50 -887 C ATOM 932 CG ARG A 120 26.804 207.021 33.389 1.00 41.85 C ANISOU 932 CG ARG A 120 5700 5220 4979 -237 44 -985 C ATOM 933 CD ARG A 120 25.572 207.825 33.765 1.00 42.95 C ANISOU 933 CD ARG A 120 5887 5301 5131 -213 125 -1023 C ATOM 934 NE ARG A 120 25.922 208.805 34.794 1.00 44.84 N ANISOU 934 NE ARG A 120 6180 5506 5353 -252 118 -1126 N ATOM 935 CZ ARG A 120 25.131 209.792 35.179 1.00 48.48 C ANISOU 935 CZ ARG A 120 6682 5897 5840 -244 187 -1182 C ATOM 936 NH1 ARG A 120 25.533 210.631 36.119 1.00 53.10 N ANISOU 936 NH1 ARG A 120 7320 6452 6403 -284 176 -1282 N ATOM 937 NH2 ARG A 120 23.939 209.932 34.620 1.00 47.69 N ANISOU 937 NH2 ARG A 120 6571 5757 5791 -195 263 -1138 N ATOM 938 N ALA A 121 27.417 204.511 29.593 1.00 37.95 N ANISOU 938 N ALA A 121 5027 4806 4585 -178 18 -715 N ATOM 939 CA ALA A 121 27.162 203.512 28.554 1.00 35.70 C ANISOU 939 CA ALA A 121 4710 4553 4304 -146 24 -635 C ATOM 940 C ALA A 121 28.248 202.437 28.516 1.00 36.05 C ANISOU 940 C ALA A 121 4719 4658 4321 -158 -32 -615 C ATOM 941 O ALA A 121 27.954 201.259 28.324 1.00 35.73 O ANISOU 941 O ALA A 121 4670 4663 4242 -128 -40 -570 O ATOM 942 CB ALA A 121 27.049 204.207 27.204 1.00 34.50 C ANISOU 942 CB ALA A 121 4532 4345 4231 -144 61 -592 C ATOM 943 N LYS A 122 29.510 202.828 28.647 1.00 37.40 N ANISOU 943 N LYS A 122 4862 4826 4521 -201 -72 -645 N ATOM 944 CA LYS A 122 30.611 201.859 28.656 1.00 41.65 C ANISOU 944 CA LYS A 122 5358 5419 5049 -211 -128 -628 C ATOM 945 C LYS A 122 30.496 200.893 29.837 1.00 39.13 C ANISOU 945 C LYS A 122 5069 5161 4640 -195 -174 -642 C ATOM 946 O LYS A 122 30.731 199.688 29.686 1.00 38.18 O ANISOU 946 O LYS A 122 4925 5087 4494 -174 -199 -599 O ATOM 947 CB LYS A 122 31.961 202.589 28.697 1.00 51.70 C ANISOU 947 CB LYS A 122 6591 6671 6383 -263 -164 -667 C ATOM 948 CG LYS A 122 32.456 203.028 27.329 1.00 65.53 C ANISOU 948 CG LYS A 122 8294 8382 8223 -277 -124 -628 C ATOM 949 CD LYS A 122 33.350 204.270 27.383 1.00 77.72 C ANISOU 949 CD LYS A 122 9814 9873 9844 -332 -129 -675 C ATOM 950 CE LYS A 122 33.426 204.950 26.011 1.00 83.89 C ANISOU 950 CE LYS A 122 10573 10596 10705 -340 -63 -631 C ATOM 951 NZ LYS A 122 33.813 206.391 26.118 1.00 87.50 N ANISOU 951 NZ LYS A 122 11029 10980 11237 -388 -48 -677 N ATOM 952 N GLY A 123 30.140 201.402 31.022 1.00 37.48 N ANISOU 952 N GLY A 123 4914 4948 4379 -206 -183 -701 N ATOM 953 CA GLY A 123 29.913 200.516 32.154 1.00 35.99 C ANISOU 953 CA GLY A 123 4768 4815 4093 -189 -218 -708 C ATOM 954 C GLY A 123 28.765 199.545 31.916 1.00 35.43 C ANISOU 954 C GLY A 123 4713 4764 3984 -140 -173 -652 C ATOM 955 O GLY A 123 28.854 198.366 32.269 1.00 35.73 O ANISOU 955 O GLY A 123 4753 4852 3970 -121 -203 -619 O ATOM 956 N ILE A 124 27.678 200.027 31.306 1.00 34.63 N ANISOU 956 N ILE A 124 4620 4620 3917 -120 -103 -638 N ATOM 957 CA ILE A 124 26.541 199.168 30.964 1.00 34.88 C ANISOU 957 CA ILE A 124 4657 4664 3931 -76 -60 -585 C ATOM 958 C ILE A 124 26.972 198.067 30.001 1.00 31.14 C ANISOU 958 C ILE A 124 4134 4220 3479 -62 -82 -522 C ATOM 959 O ILE A 124 26.581 196.906 30.151 1.00 32.45 O ANISOU 959 O ILE A 124 4304 4422 3604 -36 -85 -485 O ATOM 960 CB ILE A 124 25.394 200.004 30.357 1.00 40.59 C ANISOU 960 CB ILE A 124 5386 5331 4706 -59 9 -581 C ATOM 961 CG1 ILE A 124 24.848 201.039 31.358 1.00 46.60 C ANISOU 961 CG1 ILE A 124 6199 6057 5450 -67 43 -647 C ATOM 962 CG2 ILE A 124 24.251 199.110 29.872 1.00 42.88 C ANISOU 962 CG2 ILE A 124 5668 5632 4994 -17 44 -525 C ATOM 963 CD1 ILE A 124 23.959 200.491 32.403 1.00 51.66 C ANISOU 963 CD1 ILE A 124 6888 6723 6017 -45 71 -658 C ATOM 964 N ILE A 125 27.718 198.429 28.957 1.00 29.37 N ANISOU 964 N ILE A 125 3865 3976 3320 -78 -88 -508 N ATOM 965 CA ILE A 125 28.177 197.451 27.972 1.00 30.26 C ANISOU 965 CA ILE A 125 3932 4110 3454 -65 -99 -454 C ATOM 966 C ILE A 125 29.021 196.370 28.642 1.00 31.75 C ANISOU 966 C ILE A 125 4108 4352 3603 -65 -157 -449 C ATOM 967 O ILE A 125 28.818 195.175 28.410 1.00 31.06 O ANISOU 967 O ILE A 125 4011 4293 3496 -39 -159 -407 O ATOM 968 CB ILE A 125 28.945 198.162 26.848 1.00 32.02 C ANISOU 968 CB ILE A 125 4116 4300 3750 -88 -89 -446 C ATOM 969 CG1 ILE A 125 27.962 198.993 26.017 1.00 32.46 C ANISOU 969 CG1 ILE A 125 4187 4305 3841 -77 -34 -430 C ATOM 970 CG2 ILE A 125 29.701 197.132 25.970 1.00 31.90 C ANISOU 970 CG2 ILE A 125 4055 4312 3753 -80 -101 -402 C ATOM 971 CD1 ILE A 125 28.638 199.848 24.957 1.00 33.37 C ANISOU 971 CD1 ILE A 125 4276 4379 4023 -100 -14 -420 C ATOM 972 N ALA A 126 29.961 196.774 29.511 1.00 31.81 N ANISOU 972 N ALA A 126 4115 4371 3600 -96 -207 -492 N ATOM 973 CA ALA A 126 30.801 195.791 30.207 1.00 33.37 C ANISOU 973 CA ALA A 126 4299 4618 3762 -94 -273 -485 C ATOM 974 C ALA A 126 29.963 194.856 31.070 1.00 33.83 C ANISOU 974 C ALA A 126 4407 4709 3737 -63 -274 -466 C ATOM 975 O ALA A 126 30.193 193.640 31.087 1.00 34.84 O ANISOU 975 O ALA A 126 4519 4869 3848 -41 -299 -424 O ATOM 976 CB ALA A 126 31.854 196.512 31.042 1.00 35.25 C ANISOU 976 CB ALA A 126 4531 4860 4001 -134 -336 -540 C ATOM 977 N ILE A 127 28.977 195.399 31.791 1.00 34.01 N ANISOU 977 N ILE A 127 4490 4720 3711 -61 -240 -495 N ATOM 978 CA ILE A 127 28.112 194.576 32.631 1.00 34.26 C ANISOU 978 CA ILE A 127 4574 4779 3666 -35 -225 -476 C ATOM 979 C ILE A 127 27.296 193.591 31.800 1.00 33.16 C ANISOU 979 C ILE A 127 4414 4638 3548 0 -182 -416 C ATOM 980 O ILE A 127 27.084 192.441 32.210 1.00 33.61 O ANISOU 980 O ILE A 127 4484 4725 3563 22 -191 -379 O ATOM 981 CB ILE A 127 27.199 195.472 33.484 1.00 36.89 C ANISOU 981 CB ILE A 127 4971 5091 3953 -40 -182 -525 C ATOM 982 CG1 ILE A 127 28.026 196.102 34.612 1.00 41.33 C ANISOU 982 CG1 ILE A 127 5571 5669 4464 -73 -240 -586 C ATOM 983 CG2 ILE A 127 26.049 194.662 34.051 1.00 37.88 C ANISOU 983 CG2 ILE A 127 5141 5232 4018 -9 -136 -496 C ATOM 984 CD1 ILE A 127 27.353 197.337 35.239 1.00 46.56 C ANISOU 984 CD1 ILE A 127 6290 6295 5104 -88 -193 -652 C ATOM 985 N CYS A 128 26.739 194.054 30.689 1.00 30.86 N ANISOU 985 N CYS A 128 4097 4310 3318 5 -135 -406 N ATOM 986 CA CYS A 128 25.935 193.193 29.819 1.00 29.10 C ANISOU 986 CA CYS A 128 3854 4083 3118 34 -100 -355 C ATOM 987 C CYS A 128 26.760 192.043 29.232 1.00 27.17 C ANISOU 987 C CYS A 128 3569 3864 2892 43 -136 -315 C ATOM 988 O CYS A 128 26.257 190.918 29.081 1.00 28.16 O ANISOU 988 O CYS A 128 3692 4000 3007 67 -126 -276 O ATOM 989 CB CYS A 128 25.304 194.042 28.716 1.00 32.70 C ANISOU 989 CB CYS A 128 4294 4496 3636 36 -56 -354 C ATOM 990 SG CYS A 128 23.937 195.048 29.374 1.00 37.61 S ANISOU 990 SG CYS A 128 4958 5082 4249 42 2 -387 S ATOM 991 N TRP A 129 28.016 192.296 28.914 1.00 27.64 N ANISOU 991 N TRP A 129 3593 3927 2982 24 -174 -326 N ATOM 992 CA TRP A 129 28.888 191.232 28.400 1.00 31.20 C ANISOU 992 CA TRP A 129 3999 4397 3457 33 -203 -293 C ATOM 993 C TRP A 129 29.183 190.190 29.482 1.00 31.22 C ANISOU 993 C TRP A 129 4018 4437 3408 47 -248 -276 C ATOM 994 O TRP A 129 29.187 188.992 29.206 1.00 31.87 O ANISOU 994 O TRP A 129 4084 4530 3496 71 -251 -236 O ATOM 995 CB TRP A 129 30.194 191.816 27.852 1.00 32.88 C ANISOU 995 CB TRP A 129 4164 4603 3727 8 -227 -310 C ATOM 996 CG TRP A 129 30.117 192.200 26.399 1.00 31.67 C ANISOU 996 CG TRP A 129 3985 4418 3629 5 -180 -297 C ATOM 997 CD1 TRP A 129 29.997 193.460 25.886 1.00 33.84 C ANISOU 997 CD1 TRP A 129 4264 4659 3936 -16 -151 -318 C ATOM 998 CD2 TRP A 129 30.124 191.310 25.273 1.00 31.16 C ANISOU 998 CD2 TRP A 129 3897 4354 3590 25 -157 -260 C ATOM 999 NE1 TRP A 129 29.933 193.412 24.510 1.00 34.29 N ANISOU 999 NE1 TRP A 129 4303 4697 4030 -10 -112 -290 N ATOM 1000 CE2 TRP A 129 30.011 192.109 24.104 1.00 32.38 C ANISOU 1000 CE2 TRP A 129 4045 4476 3781 14 -116 -259 C ATOM 1001 CE3 TRP A 129 30.218 189.930 25.135 1.00 30.95 C ANISOU 1001 CE3 TRP A 129 3856 4346 3558 50 -167 -230 C ATOM 1002 CZ2 TRP A 129 30.005 191.567 22.815 1.00 32.97 C ANISOU 1002 CZ2 TRP A 129 4106 4543 3876 26 -85 -230 C ATOM 1003 CZ3 TRP A 129 30.191 189.388 23.832 1.00 30.91 C ANISOU 1003 CZ3 TRP A 129 3833 4329 3581 63 -133 -206 C ATOM 1004 CH2 TRP A 129 30.083 190.216 22.705 1.00 31.90 C ANISOU 1004 CH2 TRP A 129 3960 4428 3733 50 -94 -208 C ATOM 1005 N VAL A 130 29.401 190.622 30.727 1.00 29.00 N ANISOU 1005 N VAL A 130 3773 4173 3074 33 -284 -306 N ATOM 1006 CA VAL A 130 29.582 189.677 31.830 1.00 28.59 C ANISOU 1006 CA VAL A 130 3748 4156 2958 48 -329 -285 C ATOM 1007 C VAL A 130 28.323 188.856 32.041 1.00 27.34 C ANISOU 1007 C VAL A 130 3630 3997 2761 75 -280 -249 C ATOM 1008 O VAL A 130 28.385 187.627 32.164 1.00 30.15 O ANISOU 1008 O VAL A 130 3982 4367 3106 98 -294 -204 O ATOM 1009 CB VAL A 130 29.965 190.416 33.127 1.00 33.13 C ANISOU 1009 CB VAL A 130 4369 4750 3470 24 -376 -330 C ATOM 1010 CG1 VAL A 130 30.035 189.426 34.304 1.00 36.34 C ANISOU 1010 CG1 VAL A 130 4819 5194 3794 42 -421 -300 C ATOM 1011 CG2 VAL A 130 31.307 191.099 32.951 1.00 34.35 C ANISOU 1011 CG2 VAL A 130 4472 4904 3674 -6 -435 -363 C ATOM 1012 N LEU A 131 27.161 189.527 32.154 1.00 26.42 N ANISOU 1012 N LEU A 131 3551 3861 2627 72 -220 -269 N ATOM 1013 CA LEU A 131 25.921 188.780 32.291 1.00 27.82 C ANISOU 1013 CA LEU A 131 3754 4033 2783 96 -167 -236 C ATOM 1014 C LEU A 131 25.710 187.815 31.127 1.00 28.81 C ANISOU 1014 C LEU A 131 3833 4145 2968 115 -151 -193 C ATOM 1015 O LEU A 131 25.101 186.757 31.303 1.00 30.79 O ANISOU 1015 O LEU A 131 4094 4398 3206 134 -132 -154 O ATOM 1016 CB LEU A 131 24.748 189.727 32.387 1.00 30.96 C ANISOU 1016 CB LEU A 131 4180 4404 3178 91 -103 -266 C ATOM 1017 CG LEU A 131 24.715 190.595 33.665 1.00 37.47 C ANISOU 1017 CG LEU A 131 5067 5237 3933 75 -102 -314 C ATOM 1018 CD1 LEU A 131 23.601 191.647 33.531 1.00 39.64 C ANISOU 1018 CD1 LEU A 131 5355 5474 4231 74 -31 -347 C ATOM 1019 CD2 LEU A 131 24.430 189.713 34.849 1.00 40.95 C ANISOU 1019 CD2 LEU A 131 5564 5707 4289 87 -101 -289 C ATOM 1020 N SER A 132 26.092 188.215 29.915 1.00 27.93 N ANISOU 1020 N SER A 132 3675 4016 2920 108 -151 -201 N ATOM 1021 CA SER A 132 25.925 187.345 28.753 1.00 27.18 C ANISOU 1021 CA SER A 132 3544 3909 2875 124 -136 -168 C ATOM 1022 C SER A 132 26.719 186.048 28.934 1.00 28.02 C ANISOU 1022 C SER A 132 3633 4033 2979 139 -174 -134 C ATOM 1023 O SER A 132 26.226 184.956 28.615 1.00 28.59 O ANISOU 1023 O SER A 132 3700 4098 3064 158 -157 -101 O ATOM 1024 CB SER A 132 26.349 188.084 27.469 1.00 27.20 C ANISOU 1024 CB SER A 132 3510 3892 2933 112 -129 -183 C ATOM 1025 OG SER A 132 25.443 189.173 27.200 1.00 28.12 O ANISOU 1025 OG SER A 132 3642 3983 3059 104 -92 -204 O ATOM 1026 N PHE A 133 27.952 186.143 29.419 1.00 28.88 N ANISOU 1026 N PHE A 133 3729 4163 3082 131 -227 -143 N ATOM 1027 CA PHE A 133 28.735 184.926 29.654 1.00 29.48 C ANISOU 1027 CA PHE A 133 3785 4254 3164 151 -268 -107 C ATOM 1028 C PHE A 133 28.070 184.045 30.701 1.00 30.65 C ANISOU 1028 C PHE A 133 3980 4412 3253 168 -266 -73 C ATOM 1029 O PHE A 133 28.013 182.822 30.547 1.00 30.48 O ANISOU 1029 O PHE A 133 3949 4384 3249 191 -264 -32 O ATOM 1030 CB PHE A 133 30.163 185.282 30.057 1.00 29.89 C ANISOU 1030 CB PHE A 133 3807 4325 3224 139 -333 -124 C ATOM 1031 CG PHE A 133 31.081 185.454 28.897 1.00 31.96 C ANISOU 1031 CG PHE A 133 4005 4574 3564 132 -332 -134 C ATOM 1032 CD1 PHE A 133 31.795 184.366 28.400 1.00 34.29 C ANISOU 1032 CD1 PHE A 133 4255 4866 3908 154 -344 -105 C ATOM 1033 CD2 PHE A 133 31.228 186.667 28.291 1.00 31.62 C ANISOU 1033 CD2 PHE A 133 3948 4518 3549 106 -312 -171 C ATOM 1034 CE1 PHE A 133 32.648 184.514 27.305 1.00 35.10 C ANISOU 1034 CE1 PHE A 133 4299 4955 4083 149 -330 -116 C ATOM 1035 CE2 PHE A 133 32.068 186.818 27.211 1.00 32.07 C ANISOU 1035 CE2 PHE A 133 3949 4561 3674 99 -300 -177 C ATOM 1036 CZ PHE A 133 32.771 185.741 26.709 1.00 34.69 C ANISOU 1036 CZ PHE A 133 4237 4892 4051 120 -306 -151 C ATOM 1037 N ALA A 134 27.510 184.648 31.753 1.00 30.57 N ANISOU 1037 N ALA A 134 4025 4414 3176 158 -259 -89 N ATOM 1038 CA ALA A 134 26.926 183.840 32.824 1.00 32.02 C ANISOU 1038 CA ALA A 134 4261 4609 3296 173 -252 -53 C ATOM 1039 C ALA A 134 25.667 183.133 32.356 1.00 29.22 C ANISOU 1039 C ALA A 134 3909 4227 2966 186 -184 -24 C ATOM 1040 O ALA A 134 25.463 181.959 32.685 1.00 29.01 O ANISOU 1040 O ALA A 134 3894 4197 2931 205 -180 23 O ATOM 1041 CB ALA A 134 26.631 184.717 34.056 1.00 35.75 C ANISOU 1041 CB ALA A 134 4799 5100 3683 157 -251 -83 C ATOM 1042 N ILE A 135 24.827 183.816 31.567 1.00 28.30 N ANISOU 1042 N ILE A 135 3778 4088 2886 177 -135 -51 N ATOM 1043 CA ILE A 135 23.596 183.216 31.073 1.00 27.59 C ANISOU 1043 CA ILE A 135 3682 3972 2829 186 -78 -29 C ATOM 1044 C ILE A 135 23.897 182.137 30.031 1.00 27.95 C ANISOU 1044 C ILE A 135 3683 4001 2935 199 -90 -3 C ATOM 1045 O ILE A 135 23.327 181.049 30.067 1.00 28.56 O ANISOU 1045 O ILE A 135 3763 4063 3027 211 -68 33 O ATOM 1046 CB ILE A 135 22.659 184.291 30.484 1.00 28.80 C ANISOU 1046 CB ILE A 135 3828 4105 3012 175 -34 -64 C ATOM 1047 CG1 ILE A 135 22.015 185.110 31.580 1.00 35.56 C ANISOU 1047 CG1 ILE A 135 4731 4966 3814 168 1 -86 C ATOM 1048 CG2 ILE A 135 21.601 183.644 29.607 1.00 26.45 C ANISOU 1048 CG2 ILE A 135 3501 3778 2769 183 4 -44 C ATOM 1049 CD1 ILE A 135 21.404 186.440 31.086 1.00 38.30 C ANISOU 1049 CD1 ILE A 135 5068 5292 4192 158 32 -127 C ATOM 1050 N GLY A 136 24.725 182.451 29.030 1.00 27.78 N ANISOU 1050 N GLY A 136 3621 3977 2955 195 -115 -22 N ATOM 1051 CA GLY A 136 24.943 181.503 27.950 1.00 26.25 C ANISOU 1051 CA GLY A 136 3392 3766 2818 206 -115 -7 C ATOM 1052 C GLY A 136 25.712 180.277 28.364 1.00 25.43 C ANISOU 1052 C GLY A 136 3281 3665 2717 226 -146 30 C ATOM 1053 O GLY A 136 25.556 179.222 27.756 1.00 26.63 O ANISOU 1053 O GLY A 136 3416 3794 2910 238 -133 49 O ATOM 1054 N LEU A 137 26.543 180.386 29.398 1.00 23.33 N ANISOU 1054 N LEU A 137 3029 3425 2411 229 -189 38 N ATOM 1055 CA LEU A 137 27.355 179.256 29.839 1.00 23.05 C ANISOU 1055 CA LEU A 137 2984 3390 2382 251 -227 79 C ATOM 1056 C LEU A 137 26.812 178.598 31.098 1.00 25.36 C ANISOU 1056 C LEU A 137 3330 3688 2618 262 -225 122 C ATOM 1057 O LEU A 137 27.483 177.762 31.690 1.00 26.67 O ANISOU 1057 O LEU A 137 3498 3858 2777 282 -265 162 O ATOM 1058 CB LEU A 137 28.808 179.685 30.055 1.00 24.65 C ANISOU 1058 CB LEU A 137 3157 3617 2590 250 -290 66 C ATOM 1059 CG LEU A 137 29.561 180.245 28.850 1.00 27.70 C ANISOU 1059 CG LEU A 137 3489 3997 3039 240 -288 30 C ATOM 1060 CD1 LEU A 137 31.016 180.552 29.189 1.00 29.84 C ANISOU 1060 CD1 LEU A 137 3722 4289 3328 239 -351 22 C ATOM 1061 CD2 LEU A 137 29.478 179.271 27.660 1.00 29.07 C ANISOU 1061 CD2 LEU A 137 3630 4137 3276 256 -253 40 C ATOM 1062 N THR A 138 25.614 178.966 31.524 1.00 25.92 N ANISOU 1062 N THR A 138 3441 3757 2650 250 -177 118 N ATOM 1063 CA THR A 138 24.985 178.300 32.672 1.00 26.54 C ANISOU 1063 CA THR A 138 3573 3835 2674 259 -158 162 C ATOM 1064 C THR A 138 25.016 176.771 32.593 1.00 24.52 C ANISOU 1064 C THR A 138 3309 3552 2457 281 -156 219 C ATOM 1065 O THR A 138 25.219 176.141 33.641 1.00 25.64 O ANISOU 1065 O THR A 138 3491 3701 2551 295 -175 267 O ATOM 1066 CB THR A 138 23.551 178.854 32.814 1.00 29.46 C ANISOU 1066 CB THR A 138 3970 4195 3027 243 -86 145 C ATOM 1067 OG1 THR A 138 23.610 180.111 33.502 1.00 32.32 O ANISOU 1067 OG1 THR A 138 4368 4586 3326 227 -91 107 O ATOM 1068 CG2 THR A 138 22.624 177.920 33.560 1.00 29.73 C ANISOU 1068 CG2 THR A 138 4044 4213 3041 250 -37 195 C ATOM 1069 N PRO A 139 24.862 176.110 31.433 1.00 24.28 N ANISOU 1069 N PRO A 139 3232 3487 2508 287 -137 216 N ATOM 1070 CA PRO A 139 24.988 174.633 31.416 1.00 25.48 C ANISOU 1070 CA PRO A 139 3377 3605 2700 309 -137 267 C ATOM 1071 C PRO A 139 26.300 174.132 31.958 1.00 25.18 C ANISOU 1071 C PRO A 139 3334 3580 2654 334 -203 301 C ATOM 1072 O PRO A 139 26.349 173.031 32.517 1.00 26.00 O ANISOU 1072 O PRO A 139 3456 3662 2760 355 -208 359 O ATOM 1073 CB PRO A 139 24.824 174.289 29.925 1.00 25.20 C ANISOU 1073 CB PRO A 139 3290 3535 2749 306 -115 238 C ATOM 1074 CG PRO A 139 23.865 175.380 29.445 1.00 26.03 C ANISOU 1074 CG PRO A 139 3395 3648 2845 280 -80 191 C ATOM 1075 CD PRO A 139 24.368 176.617 30.154 1.00 25.52 C ANISOU 1075 CD PRO A 139 3352 3627 2716 272 -107 171 C ATOM 1076 N AMET A 140 27.373 174.919 31.862 0.50 27.01 N ANISOU 1076 N AMET A 140 3541 3843 2880 332 -255 270 N ATOM 1077 N BMET A 140 27.366 174.926 31.832 0.50 26.99 N ANISOU 1077 N BMET A 140 3537 3839 2878 332 -255 269 N ATOM 1078 CA AMET A 140 28.671 174.496 32.380 0.50 27.46 C ANISOU 1078 CA AMET A 140 3583 3913 2940 356 -328 301 C ATOM 1079 CA BMET A 140 28.663 174.540 32.374 0.50 27.51 C ANISOU 1079 CA BMET A 140 3589 3920 2945 355 -327 299 C ATOM 1080 C AMET A 140 28.736 174.513 33.902 0.50 27.42 C ANISOU 1080 C AMET A 140 3641 3938 2841 362 -367 343 C ATOM 1081 C BMET A 140 28.593 174.316 33.876 0.50 27.29 C ANISOU 1081 C BMET A 140 3626 3913 2828 364 -358 350 C ATOM 1082 O AMET A 140 29.720 174.029 34.478 0.50 28.51 O ANISOU 1082 O AMET A 140 3773 4085 2975 385 -436 381 O ATOM 1083 O BMET A 140 29.314 173.462 34.415 0.50 28.45 O ANISOU 1083 O BMET A 140 3774 4056 2980 392 -408 404 O ATOM 1084 CB AMET A 140 29.778 175.388 31.819 0.50 29.23 C ANISOU 1084 CB AMET A 140 3753 4160 3193 348 -370 253 C ATOM 1085 CB BMET A 140 29.708 175.619 32.062 0.50 29.71 C ANISOU 1085 CB BMET A 140 3827 4230 3233 343 -374 250 C ATOM 1086 CG AMET A 140 29.949 175.330 30.286 0.50 30.69 C ANISOU 1086 CG AMET A 140 3878 4316 3466 346 -334 216 C ATOM 1087 CG BMET A 140 29.994 175.864 30.561 0.50 30.23 C ANISOU 1087 CG BMET A 140 3830 4276 3381 336 -346 204 C ATOM 1088 SD AMET A 140 31.388 176.277 29.702 0.50 32.82 S ANISOU 1088 SD AMET A 140 4082 4608 3778 337 -376 170 S ATOM 1089 SD BMET A 140 30.910 174.565 29.727 0.50 35.85 S ANISOU 1089 SD BMET A 140 4479 4949 4194 371 -352 227 S ATOM 1090 CE AMET A 140 32.723 175.161 30.088 0.50 33.71 C ANISOU 1090 CE AMET A 140 4149 4712 3947 378 -440 217 C ATOM 1091 CE BMET A 140 32.413 174.416 30.687 0.50 36.97 C ANISOU 1091 CE BMET A 140 4591 5115 4340 395 -447 260 C ATOM 1092 N LEU A 141 27.736 175.066 34.570 1.00 28.96 N ANISOU 1092 N LEU A 141 3897 4148 2960 341 -327 336 N ATOM 1093 CA LEU A 141 27.679 175.011 36.028 1.00 30.94 C ANISOU 1093 CA LEU A 141 4224 4426 3108 346 -352 377 C ATOM 1094 C LEU A 141 26.954 173.783 36.540 1.00 31.31 C ANISOU 1094 C LEU A 141 4312 4440 3143 363 -310 449 C ATOM 1095 O LEU A 141 26.898 173.565 37.762 1.00 33.61 O ANISOU 1095 O LEU A 141 4675 4750 3345 370 -326 496 O ATOM 1096 CB LEU A 141 27.014 176.275 36.548 1.00 31.96 C ANISOU 1096 CB LEU A 141 4403 4585 3157 316 -322 329 C ATOM 1097 CG LEU A 141 27.648 177.599 36.082 1.00 36.36 C ANISOU 1097 CG LEU A 141 4923 5168 3725 294 -358 256 C ATOM 1098 CD1 LEU A 141 26.882 178.792 36.645 1.00 40.87 C ANISOU 1098 CD1 LEU A 141 5549 5759 4221 267 -319 209 C ATOM 1099 CD2 LEU A 141 29.090 177.686 36.500 1.00 37.47 C ANISOU 1099 CD2 LEU A 141 5044 5337 3854 303 -461 260 C ATOM 1100 N GLY A 142 26.465 172.929 35.646 1.00 29.14 N ANISOU 1100 N GLY A 142 3998 4116 2958 370 -260 461 N ATOM 1101 CA GLY A 142 25.870 171.678 36.090 1.00 30.68 C ANISOU 1101 CA GLY A 142 4226 4271 3159 385 -222 533 C ATOM 1102 C GLY A 142 24.530 171.367 35.451 1.00 30.45 C ANISOU 1102 C GLY A 142 4186 4200 3185 367 -129 521 C ATOM 1103 O GLY A 142 24.040 170.242 35.556 1.00 30.14 O ANISOU 1103 O GLY A 142 4157 4115 3180 376 -92 574 O ATOM 1104 N TRP A 143 23.917 172.332 34.786 1.00 29.16 N ANISOU 1104 N TRP A 143 4000 4047 3034 341 -94 456 N ATOM 1105 CA TRP A 143 22.635 172.077 34.130 1.00 27.40 C ANISOU 1105 CA TRP A 143 3758 3784 2870 323 -17 442 C ATOM 1106 C TRP A 143 22.915 171.518 32.730 1.00 25.53 C ANISOU 1106 C TRP A 143 3453 3511 2737 328 -27 417 C ATOM 1107 O TRP A 143 22.825 172.206 31.710 1.00 25.19 O ANISOU 1107 O TRP A 143 3370 3473 2727 314 -26 358 O ATOM 1108 CB TRP A 143 21.797 173.349 34.094 1.00 29.18 C ANISOU 1108 CB TRP A 143 3990 4034 3064 296 24 389 C ATOM 1109 CG TRP A 143 20.348 173.144 33.722 1.00 28.03 C ANISOU 1109 CG TRP A 143 3829 3850 2970 278 103 383 C ATOM 1110 CD1 TRP A 143 19.726 171.949 33.384 1.00 27.18 C ANISOU 1110 CD1 TRP A 143 3702 3690 2934 278 140 417 C ATOM 1111 CD2 TRP A 143 19.328 174.152 33.698 1.00 28.66 C ANISOU 1111 CD2 TRP A 143 3909 3939 3042 257 154 343 C ATOM 1112 NE1 TRP A 143 18.387 172.189 33.121 1.00 28.14 N ANISOU 1112 NE1 TRP A 143 3807 3791 3096 255 205 397 N ATOM 1113 CE2 TRP A 143 18.121 173.522 33.306 1.00 29.03 C ANISOU 1113 CE2 TRP A 143 3928 3940 3161 245 215 354 C ATOM 1114 CE3 TRP A 143 19.318 175.522 33.957 1.00 30.24 C ANISOU 1114 CE3 TRP A 143 4125 4176 3188 247 153 297 C ATOM 1115 CZ2 TRP A 143 16.925 174.223 33.162 1.00 28.99 C ANISOU 1115 CZ2 TRP A 143 3906 3928 3180 226 273 323 C ATOM 1116 CZ3 TRP A 143 18.113 176.223 33.821 1.00 29.11 C ANISOU 1116 CZ3 TRP A 143 3970 4023 3066 231 215 267 C ATOM 1117 CH2 TRP A 143 16.932 175.559 33.427 1.00 27.21 C ANISOU 1117 CH2 TRP A 143 3696 3739 2903 222 273 282 C ATOM 1118 N ASN A 144 23.287 170.233 32.692 1.00 26.78 N ANISOU 1118 N ASN A 144 3603 3629 2943 350 -37 464 N ATOM 1119 CA ASN A 144 23.734 169.630 31.449 1.00 27.88 C ANISOU 1119 CA ASN A 144 3686 3733 3174 359 -49 439 C ATOM 1120 C ASN A 144 23.478 168.126 31.507 1.00 29.52 C ANISOU 1120 C ASN A 144 3895 3877 3443 373 -25 493 C ATOM 1121 O ASN A 144 23.089 167.575 32.536 1.00 30.25 O ANISOU 1121 O ASN A 144 4033 3957 3504 378 -4 556 O ATOM 1122 CB ASN A 144 25.220 169.936 31.193 1.00 27.27 C ANISOU 1122 CB ASN A 144 3579 3683 3100 379 -117 423 C ATOM 1123 CG ASN A 144 26.133 169.344 32.251 1.00 29.42 C ANISOU 1123 CG ASN A 144 3873 3961 3343 411 -168 488 C ATOM 1124 OD1 ASN A 144 26.192 168.142 32.414 1.00 32.32 O ANISOU 1124 OD1 ASN A 144 4244 4283 3753 433 -163 540 O ATOM 1125 ND2 ASN A 144 26.880 170.206 32.962 1.00 28.89 N ANISOU 1125 ND2 ASN A 144 3821 3948 3206 413 -224 485 N ATOM 1126 N ASN A 145 23.695 167.457 30.376 1.00 29.69 N ANISOU 1126 N ASN A 145 3873 3857 3552 378 -23 466 N ATOM 1127 CA ASN A 145 23.448 166.021 30.281 1.00 31.71 C ANISOU 1127 CA ASN A 145 4125 4042 3880 389 3 506 C ATOM 1128 C ASN A 145 24.744 165.215 30.340 1.00 31.60 C ANISOU 1128 C ASN A 145 4096 4006 3904 431 -42 540 C ATOM 1129 O ASN A 145 24.740 164.043 29.956 1.00 34.18 O ANISOU 1129 O ASN A 145 4409 4267 4311 443 -23 557 O ATOM 1130 CB ASN A 145 22.688 165.673 28.990 1.00 35.76 C ANISOU 1130 CB ASN A 145 4603 4510 4472 366 39 450 C ATOM 1131 CG ASN A 145 21.249 166.180 28.972 1.00 40.30 C ANISOU 1131 CG ASN A 145 5186 5090 5036 328 85 430 C ATOM 1132 OD1 ASN A 145 20.618 166.369 30.002 1.00 40.39 O ANISOU 1132 OD1 ASN A 145 5231 5113 5001 319 114 471 O ATOM 1133 ND2 ASN A 145 20.720 166.364 27.770 1.00 43.50 N ANISOU 1133 ND2 ASN A 145 5559 5482 5487 305 94 367 N ATOM 1134 N CYS A 146 25.840 165.811 30.837 1.00 29.76 N ANISOU 1134 N CYS A 146 3863 3823 3622 452 -100 549 N ATOM 1135 CA CYS A 146 27.109 165.087 30.912 1.00 33.89 C ANISOU 1135 CA CYS A 146 4360 4326 4191 494 -148 583 C ATOM 1136 C CYS A 146 27.015 163.882 31.838 1.00 39.47 C ANISOU 1136 C CYS A 146 5102 4985 4910 520 -146 674 C ATOM 1137 O CYS A 146 27.795 162.924 31.695 1.00 40.87 O ANISOU 1137 O CYS A 146 5253 5117 5160 557 -167 705 O ATOM 1138 CB CYS A 146 28.229 166.035 31.366 1.00 34.70 C ANISOU 1138 CB CYS A 146 4452 4494 4239 507 -218 577 C ATOM 1139 SG CYS A 146 28.673 167.260 30.101 1.00 36.17 S ANISOU 1139 SG CYS A 146 4584 4719 4440 485 -221 477 S ATOM 1140 N GLY A 147 26.085 163.899 32.793 1.00 43.85 N ANISOU 1140 N GLY A 147 5716 5547 5400 503 -116 720 N ATOM 1141 CA GLY A 147 25.958 162.752 33.679 1.00 47.02 C ANISOU 1141 CA GLY A 147 6157 5899 5808 525 -107 813 C ATOM 1142 C GLY A 147 25.128 161.627 33.114 1.00 47.94 C ANISOU 1142 C GLY A 147 6263 5930 6020 515 -40 821 C ATOM 1143 O GLY A 147 24.988 160.584 33.754 1.00 47.75 O ANISOU 1143 O GLY A 147 6270 5853 6020 532 -24 900 O ATOM 1144 N GLN A 148 24.582 161.802 31.916 1.00 47.31 N ANISOU 1144 N GLN A 148 6143 5834 5999 486 -3 740 N ATOM 1145 CA GLN A 148 23.734 160.797 31.280 1.00 47.32 C ANISOU 1145 CA GLN A 148 6130 5754 6094 469 55 732 C ATOM 1146 C GLN A 148 24.185 160.589 29.843 1.00 45.32 C ANISOU 1146 C GLN A 148 5822 5473 5925 472 49 654 C ATOM 1147 O GLN A 148 23.441 160.862 28.900 1.00 46.67 O ANISOU 1147 O GLN A 148 5972 5638 6121 437 78 583 O ATOM 1148 CB GLN A 148 22.269 161.221 31.353 1.00 51.71 C ANISOU 1148 CB GLN A 148 6703 6317 6627 421 115 714 C ATOM 1149 CG GLN A 148 21.787 161.433 32.781 1.00 59.46 C ANISOU 1149 CG GLN A 148 7746 7325 7521 417 137 788 C ATOM 1150 N PRO A 149 25.413 160.104 29.640 1.00 45.38 N ANISOU 1150 N PRO A 149 5803 5461 5977 514 10 663 N ATOM 1151 CA PRO A 149 25.949 160.010 28.280 1.00 45.59 C ANISOU 1151 CA PRO A 149 5782 5468 6073 519 11 584 C ATOM 1152 C PRO A 149 25.199 158.977 27.454 1.00 47.31 C ANISOU 1152 C PRO A 149 5993 5600 6384 501 62 553 C ATOM 1153 O PRO A 149 24.553 158.071 27.973 1.00 49.35 O ANISOU 1153 O PRO A 149 6273 5798 6679 496 93 606 O ATOM 1154 CB PRO A 149 27.411 159.592 28.489 1.00 45.68 C ANISOU 1154 CB PRO A 149 5766 5469 6120 574 -35 618 C ATOM 1155 CG PRO A 149 27.431 158.877 29.813 1.00 46.68 C ANISOU 1155 CG PRO A 149 5930 5570 6235 600 -51 726 C ATOM 1156 CD PRO A 149 26.349 159.572 30.648 1.00 46.99 C ANISOU 1156 CD PRO A 149 6022 5658 6175 562 -33 751 C ATOM 1157 N LYS A 150 25.272 159.154 26.141 1.00 44.81 N ANISOU 1157 N LYS A 150 5647 5278 6100 487 72 463 N ATOM 1158 CA LYS A 150 24.734 158.186 25.187 1.00 41.35 C ANISOU 1158 CA LYS A 150 5202 4760 5751 470 112 416 C ATOM 1159 C LYS A 150 25.832 157.164 24.949 1.00 42.18 C ANISOU 1159 C LYS A 150 5285 4800 5940 518 111 427 C ATOM 1160 O LYS A 150 26.726 157.365 24.128 1.00 41.67 O ANISOU 1160 O LYS A 150 5193 4746 5893 537 104 372 O ATOM 1161 CB LYS A 150 24.327 158.863 23.890 1.00 41.44 C ANISOU 1161 CB LYS A 150 5202 4799 5747 434 119 315 C ATOM 1162 CG LYS A 150 23.198 159.876 24.008 1.00 49.30 C ANISOU 1162 CG LYS A 150 6210 5850 6673 390 119 300 C ATOM 1163 CD LYS A 150 21.865 159.228 24.253 1.00 62.39 C ANISOU 1163 CD LYS A 150 7878 7455 8372 355 152 318 C ATOM 1164 CE LYS A 150 20.738 160.258 24.390 1.00 71.78 C ANISOU 1164 CE LYS A 150 9071 8698 9504 314 155 304 C ATOM 1165 NZ LYS A 150 20.319 160.832 23.082 1.00 76.29 N ANISOU 1165 NZ LYS A 150 9627 9289 10071 284 143 213 N ATOM 1166 N GLU A 151 25.798 156.071 25.694 1.00 48.59 N ANISOU 1166 N GLU A 151 6109 5543 6809 540 122 502 N ATOM 1167 CA GLU A 151 26.915 155.136 25.607 1.00 62.75 C ANISOU 1167 CA GLU A 151 7880 7275 8689 594 117 524 C ATOM 1168 C GLU A 151 26.917 154.354 24.300 1.00 54.32 C ANISOU 1168 C GLU A 151 6795 6130 7715 588 158 440 C ATOM 1169 O GLU A 151 27.987 153.913 23.858 1.00 50.29 O ANISOU 1169 O GLU A 151 6254 5586 7267 631 158 422 O ATOM 1170 CB GLU A 151 26.920 154.201 26.815 1.00 88.66 C ANISOU 1170 CB GLU A 151 11183 10500 12002 623 114 638 C ATOM 1171 CG GLU A 151 27.316 154.900 28.128 1.00109.81 C ANISOU 1171 CG GLU A 151 13883 13256 14586 644 62 724 C ATOM 1172 CD GLU A 151 28.738 155.489 28.131 1.00124.18 C ANISOU 1172 CD GLU A 151 15663 15130 16388 688 4 719 C ATOM 1173 OE1 GLU A 151 29.391 155.555 27.067 1.00127.34 O ANISOU 1173 OE1 GLU A 151 16020 15524 16840 698 11 643 O ATOM 1174 OE2 GLU A 151 29.210 155.891 29.215 1.00129.82 O ANISOU 1174 OE2 GLU A 151 16392 15896 17037 710 -50 791 O ATOM 1175 N GLY A 152 25.766 154.215 23.644 1.00 52.24 N ANISOU 1175 N GLY A 152 6546 5840 7461 536 190 382 N ATOM 1176 CA GLY A 152 25.753 153.621 22.317 1.00 53.82 C ANISOU 1176 CA GLY A 152 6739 5979 7731 525 222 286 C ATOM 1177 C GLY A 152 26.502 154.460 21.297 1.00 54.32 C ANISOU 1177 C GLY A 152 6785 6102 7752 531 214 203 C ATOM 1178 O GLY A 152 27.314 153.946 20.512 1.00 59.05 O ANISOU 1178 O GLY A 152 7368 6656 8411 559 236 154 O ATOM 1179 N LYS A 153 26.222 155.763 21.279 1.00 49.75 N ANISOU 1179 N LYS A 153 6211 5620 7072 504 188 186 N ATOM 1180 CA LYS A 153 26.955 156.674 20.410 1.00 50.14 C ANISOU 1180 CA LYS A 153 6246 5731 7073 508 182 120 C ATOM 1181 C LYS A 153 28.430 156.732 20.788 1.00 48.33 C ANISOU 1181 C LYS A 153 5981 5515 6865 565 169 156 C ATOM 1182 O LYS A 153 29.310 156.733 19.912 1.00 46.58 O ANISOU 1182 O LYS A 153 5739 5287 6673 586 190 100 O ATOM 1183 CB LYS A 153 26.339 158.071 20.482 1.00 58.69 C ANISOU 1183 CB LYS A 153 7341 6909 8050 471 156 109 C ATOM 1184 CG LYS A 153 25.385 158.376 19.364 1.00 71.90 C ANISOU 1184 CG LYS A 153 9035 8588 9696 421 166 26 C ATOM 1185 CD LYS A 153 24.823 159.777 19.479 1.00 82.46 C ANISOU 1185 CD LYS A 153 10379 10014 10937 391 139 23 C ATOM 1186 CE LYS A 153 23.317 159.752 19.596 1.00 90.70 C ANISOU 1186 CE LYS A 153 11438 11048 11976 344 136 22 C ATOM 1187 NZ LYS A 153 22.712 161.084 19.352 1.00 95.35 N ANISOU 1187 NZ LYS A 153 12033 11713 12484 314 114 -2 N ATOM 1188 N AASN A 154 28.729 156.746 22.086 0.50 48.84 N ANISOU 1188 N AASN A 154 6039 5597 6921 592 134 251 N ATOM 1189 N BASN A 154 28.711 156.858 22.088 0.50 48.77 N ANISOU 1189 N BASN A 154 6031 5597 6904 590 132 250 N ATOM 1190 CA AASN A 154 30.106 156.951 22.509 0.50 48.75 C ANISOU 1190 CA AASN A 154 5988 5610 6925 643 105 288 C ATOM 1191 CA BASN A 154 30.082 156.871 22.580 0.50 48.78 C ANISOU 1191 CA BASN A 154 5992 5609 6932 645 105 294 C ATOM 1192 C AASN A 154 30.976 155.709 22.268 0.50 48.16 C ANISOU 1192 C AASN A 154 5882 5444 6972 695 129 295 C ATOM 1193 C BASN A 154 30.868 155.721 21.969 0.50 48.28 C ANISOU 1193 C BASN A 154 5900 5456 6987 687 140 272 C ATOM 1194 O AASN A 154 32.194 155.851 22.116 0.50 47.58 O ANISOU 1194 O AASN A 154 5763 5382 6934 735 121 291 O ATOM 1195 O BASN A 154 31.854 155.920 21.253 0.50 46.93 O ANISOU 1195 O BASN A 154 5693 5292 6846 710 155 224 O ATOM 1196 CB AASN A 154 30.137 157.388 23.982 0.50 49.59 C ANISOU 1196 CB AASN A 154 6103 5768 6973 654 51 385 C ATOM 1197 CB BASN A 154 30.063 156.782 24.113 0.50 51.50 C ANISOU 1197 CB BASN A 154 6348 5968 7251 664 59 405 C ATOM 1198 CG AASN A 154 29.377 158.735 24.249 0.50 41.23 C ANISOU 1198 CG AASN A 154 5071 4801 5794 607 31 373 C ATOM 1199 CG BASN A 154 31.426 156.479 24.717 0.50 58.46 C ANISOU 1199 CG BASN A 154 7188 6841 8183 727 21 465 C ATOM 1200 OD1AASN A 154 28.904 159.422 23.335 0.50 30.09 O ANISOU 1200 OD1AASN A 154 3666 3421 4346 570 51 298 O ATOM 1201 OD1BASN A 154 32.416 157.113 24.396 0.50 59.09 O ANISOU 1201 OD1BASN A 154 7226 6965 8262 745 2 436 O ATOM 1202 ND2AASN A 154 29.260 159.084 25.523 0.50 46.77 N ANISOU 1202 ND2AASN A 154 5792 5542 6435 611 -8 450 N ATOM 1203 ND2BASN A 154 31.471 155.499 25.614 0.50 70.13 N ANISOU 1203 ND2BASN A 154 8676 8261 9709 760 6 553 N ATOM 1204 N HIS A 155 30.389 154.502 22.193 1.00 49.43 N ANISOU 1204 N HIS A 155 6064 5511 7206 694 162 302 N ATOM 1205 CA HIS A 155 31.150 153.319 21.798 1.00 53.13 C ANISOU 1205 CA HIS A 155 6506 5883 7798 741 195 294 C ATOM 1206 C HIS A 155 31.202 153.148 20.287 1.00 52.63 C ANISOU 1206 C HIS A 155 6443 5786 7766 725 252 175 C ATOM 1207 O HIS A 155 32.205 152.651 19.760 1.00 51.84 O ANISOU 1207 O HIS A 155 6309 5640 7749 768 283 145 O ATOM 1208 CB HIS A 155 30.553 152.075 22.448 1.00 59.74 C ANISOU 1208 CB HIS A 155 7366 6625 8706 748 206 360 C ATOM 1209 CG HIS A 155 30.748 152.034 23.932 1.00 67.35 C ANISOU 1209 CG HIS A 155 8333 7606 9651 778 155 486 C ATOM 1210 ND1 HIS A 155 29.707 151.877 24.819 1.00 69.61 N ANISOU 1210 ND1 HIS A 155 8664 7888 9896 749 148 553 N ATOM 1211 CD2 HIS A 155 31.866 152.162 24.685 1.00 72.96 C ANISOU 1211 CD2 HIS A 155 9008 8341 10370 834 105 556 C ATOM 1212 CE1 HIS A 155 30.175 151.898 26.054 1.00 73.38 C ANISOU 1212 CE1 HIS A 155 9143 8387 10349 786 100 660 C ATOM 1213 NE2 HIS A 155 31.483 152.070 26.001 1.00 75.25 N ANISOU 1213 NE2 HIS A 155 9332 8644 10616 837 66 664 N ATOM 1214 N SER A 156 30.161 153.557 19.565 1.00 55.34 N ANISOU 1214 N SER A 156 6825 6153 8047 665 267 105 N ATOM 1215 CA SER A 156 30.203 153.417 18.115 1.00 63.96 C ANISOU 1215 CA SER A 156 7930 7219 9153 648 317 -9 C ATOM 1216 C SER A 156 31.206 154.383 17.502 1.00 67.30 C ANISOU 1216 C SER A 156 8327 7712 9533 663 324 -53 C ATOM 1217 O SER A 156 31.842 154.057 16.494 1.00 72.75 O ANISOU 1217 O SER A 156 9010 8365 10265 679 376 -127 O ATOM 1218 CB SER A 156 28.810 153.629 17.517 1.00 68.85 C ANISOU 1218 CB SER A 156 8597 7848 9713 580 318 -69 C ATOM 1219 OG SER A 156 28.517 155.004 17.358 1.00 73.50 O ANISOU 1219 OG SER A 156 9196 8543 10189 547 289 -86 O ATOM 1220 N GLN A 157 31.371 155.563 18.099 1.00 64.44 N ANISOU 1220 N GLN A 157 7950 7445 9087 657 279 -11 N ATOM 1221 CA GLN A 157 32.383 156.507 17.645 1.00 66.82 C ANISOU 1221 CA GLN A 157 8219 7811 9358 671 285 -41 C ATOM 1222 C GLN A 157 33.762 156.170 18.190 1.00 59.54 C ANISOU 1222 C GLN A 157 7232 6868 8521 735 279 9 C ATOM 1223 O GLN A 157 34.761 156.687 17.676 1.00 60.82 O ANISOU 1223 O GLN A 157 7356 7059 8694 753 301 -24 O ATOM 1224 CB GLN A 157 32.010 157.928 18.068 1.00 85.83 C ANISOU 1224 CB GLN A 157 10637 10325 11652 636 238 -20 C ATOM 1225 CG GLN A 157 30.630 158.371 17.625 1.00109.55 C ANISOU 1225 CG GLN A 157 13695 13354 14575 576 234 -60 C ATOM 1226 CD GLN A 157 30.537 158.593 16.134 1.00129.42 C ANISOU 1226 CD GLN A 157 16240 15872 17062 550 278 -162 C ATOM 1227 OE1 GLN A 157 31.278 159.396 15.569 1.00134.74 O ANISOU 1227 OE1 GLN A 157 16900 16592 17701 554 294 -194 O ATOM 1228 NE2 GLN A 157 29.619 157.882 15.484 1.00136.98 N ANISOU 1228 NE2 GLN A 157 17238 16775 18032 522 296 -212 N ATOM 1229 N GLY A 158 33.835 155.355 19.237 1.00 54.06 N ANISOU 1229 N GLY A 158 6524 6126 7890 769 248 94 N ATOM 1230 CA GLY A 158 35.114 154.984 19.803 1.00 51.49 C ANISOU 1230 CA GLY A 158 6133 5778 7653 834 231 150 C ATOM 1231 C GLY A 158 35.709 155.994 20.752 1.00 50.04 C ANISOU 1231 C GLY A 158 5914 5682 7417 845 159 214 C ATOM 1232 O GLY A 158 36.928 156.033 20.910 1.00 54.29 O ANISOU 1232 O GLY A 158 6385 6222 8020 891 145 234 O ATOM 1233 N CYS A 159 34.892 156.815 21.401 1.00 47.41 N ANISOU 1233 N CYS A 159 5620 5420 6973 803 113 244 N ATOM 1234 CA CYS A 159 35.467 157.812 22.302 1.00 50.93 C ANISOU 1234 CA CYS A 159 6038 5949 7364 810 44 297 C ATOM 1235 C CYS A 159 36.109 157.158 23.531 1.00 56.93 C ANISOU 1235 C CYS A 159 6768 6682 8180 864 -17 399 C ATOM 1236 O CYS A 159 35.726 156.075 23.959 1.00 54.03 O ANISOU 1236 O CYS A 159 6424 6244 7861 884 -13 450 O ATOM 1237 CB CYS A 159 34.398 158.798 22.755 1.00 48.13 C ANISOU 1237 CB CYS A 159 5738 5669 6880 755 15 304 C ATOM 1238 SG CYS A 159 33.426 159.460 21.382 1.00 43.66 S ANISOU 1238 SG CYS A 159 5215 5126 6247 692 74 197 S ATOM 1239 N GLY A 160 37.069 157.872 24.128 1.00 63.70 N ANISOU 1239 N GLY A 160 7576 7598 9027 885 -79 433 N ATOM 1240 CA GLY A 160 37.757 157.413 25.322 1.00 70.20 C ANISOU 1240 CA GLY A 160 8371 8411 9891 936 -155 533 C ATOM 1241 C GLY A 160 36.974 157.685 26.591 1.00 72.12 C ANISOU 1241 C GLY A 160 8679 8698 10025 915 -217 609 C ATOM 1242 O GLY A 160 35.746 157.835 26.572 1.00 73.82 O ANISOU 1242 O GLY A 160 8963 8923 10163 868 -186 595 O ATOM 1243 N GLU A 161 37.699 157.771 27.712 1.00 70.36 N ANISOU 1243 N GLU A 161 8434 8503 9796 950 -306 690 N ATOM 1244 CA GLU A 161 37.097 157.886 29.036 1.00 75.84 C ANISOU 1244 CA GLU A 161 9195 9232 10388 940 -367 774 C ATOM 1245 C GLU A 161 36.845 159.348 29.379 1.00 64.91 C ANISOU 1245 C GLU A 161 7836 7953 8874 891 -403 746 C ATOM 1246 O GLU A 161 37.708 160.208 29.168 1.00 57.77 O ANISOU 1246 O GLU A 161 6875 7100 7974 890 -437 708 O ATOM 1247 CB GLU A 161 38.002 157.249 30.099 1.00105.81 C ANISOU 1247 CB GLU A 161 12965 13008 14232 1002 -454 878 C ATOM 1248 CG GLU A 161 39.231 158.083 30.486 1.00129.35 C ANISOU 1248 CG GLU A 161 15878 16056 17212 1022 -545 883 C ATOM 1249 CD GLU A 161 39.012 158.944 31.725 1.00142.77 C ANISOU 1249 CD GLU A 161 17634 17843 18769 998 -633 932 C ATOM 1250 OE1 GLU A 161 37.954 158.812 32.377 1.00147.61 O ANISOU 1250 OE1 GLU A 161 18339 18461 19286 974 -621 974 O ATOM 1251 OE2 GLU A 161 39.908 159.754 32.050 1.00145.39 O ANISOU 1251 OE2 GLU A 161 17917 18236 19088 1002 -710 926 O ATOM 1252 N GLY A 162 35.667 159.623 29.936 1.00 68.21 N ANISOU 1252 N GLY A 162 8336 8398 9183 851 -393 765 N ATOM 1253 CA GLY A 162 35.222 160.988 30.136 1.00 68.02 C ANISOU 1253 CA GLY A 162 8343 8463 9039 801 -407 726 C ATOM 1254 C GLY A 162 34.738 161.685 28.883 1.00 60.63 C ANISOU 1254 C GLY A 162 7397 7542 8097 756 -337 623 C ATOM 1255 O GLY A 162 34.275 162.833 28.972 1.00 54.48 O ANISOU 1255 O GLY A 162 6646 6830 7225 713 -341 589 O ATOM 1256 N GLN A 163 34.800 161.025 27.731 1.00 59.43 N ANISOU 1256 N GLN A 163 7215 7329 8039 764 -272 574 N ATOM 1257 CA GLN A 163 34.477 161.638 26.450 1.00 52.86 C ANISOU 1257 CA GLN A 163 6375 6509 7202 727 -210 477 C ATOM 1258 C GLN A 163 33.086 161.233 25.993 1.00 46.14 C ANISOU 1258 C GLN A 163 5580 5622 6329 691 -149 452 C ATOM 1259 O GLN A 163 32.638 160.107 26.218 1.00 44.64 O ANISOU 1259 O GLN A 163 5411 5365 6184 706 -129 492 O ATOM 1260 CB GLN A 163 35.476 161.241 25.365 1.00 48.96 C ANISOU 1260 CB GLN A 163 5814 5974 6817 756 -174 427 C ATOM 1261 CG GLN A 163 36.870 161.727 25.580 1.00 45.71 C ANISOU 1261 CG GLN A 163 5329 5594 6444 785 -224 436 C ATOM 1262 CD GLN A 163 37.723 161.518 24.356 1.00 47.29 C ANISOU 1262 CD GLN A 163 5465 5759 6744 804 -166 372 C ATOM 1263 OE1 GLN A 163 37.484 160.600 23.563 1.00 46.50 O ANISOU 1263 OE1 GLN A 163 5373 5589 6706 815 -100 341 O ATOM 1264 NE2 GLN A 163 38.715 162.371 24.184 1.00 51.26 N ANISOU 1264 NE2 GLN A 163 5907 6307 7264 805 -185 347 N ATOM 1265 N VAL A 164 32.418 162.165 25.323 1.00 40.85 N ANISOU 1265 N VAL A 164 4929 4994 5598 644 -120 387 N ATOM 1266 CA VAL A 164 31.133 161.912 24.694 1.00 37.59 C ANISOU 1266 CA VAL A 164 4558 4552 5172 606 -67 348 C ATOM 1267 C VAL A 164 31.287 162.251 23.222 1.00 34.43 C ANISOU 1267 C VAL A 164 4140 4151 4791 589 -23 257 C ATOM 1268 O VAL A 164 32.156 163.030 22.830 1.00 34.00 O ANISOU 1268 O VAL A 164 4050 4137 4730 594 -31 225 O ATOM 1269 CB VAL A 164 30.009 162.758 25.311 1.00 40.13 C ANISOU 1269 CB VAL A 164 4928 4927 5393 564 -76 361 C ATOM 1270 CG1 VAL A 164 29.845 162.447 26.774 1.00 40.14 C ANISOU 1270 CG1 VAL A 164 4958 4931 5361 579 -112 451 C ATOM 1271 CG2 VAL A 164 30.311 164.236 25.134 1.00 41.49 C ANISOU 1271 CG2 VAL A 164 5089 5178 5496 542 -98 320 C ATOM 1272 N ALA A 165 30.414 161.695 22.406 1.00 33.83 N ANISOU 1272 N ALA A 165 4090 4029 4736 567 23 213 N ATOM 1273 CA ALA A 165 30.233 162.227 21.065 1.00 34.61 C ANISOU 1273 CA ALA A 165 4193 4142 4816 538 58 126 C ATOM 1274 C ALA A 165 29.576 163.602 21.182 1.00 34.26 C ANISOU 1274 C ALA A 165 4171 4174 4673 498 38 114 C ATOM 1275 O ALA A 165 28.479 163.727 21.737 1.00 34.40 O ANISOU 1275 O ALA A 165 4220 4200 4650 472 29 139 O ATOM 1276 CB ALA A 165 29.394 161.259 20.231 1.00 35.19 C ANISOU 1276 CB ALA A 165 4294 4146 4930 521 100 83 C ATOM 1277 N CYS A 166 30.255 164.644 20.694 1.00 32.93 N ANISOU 1277 N CYS A 166 3984 4057 4472 493 35 80 N ATOM 1278 CA CYS A 166 29.830 166.012 20.959 1.00 30.93 C ANISOU 1278 CA CYS A 166 3745 3874 4134 462 12 77 C ATOM 1279 C CYS A 166 28.751 166.407 19.964 1.00 31.27 C ANISOU 1279 C CYS A 166 3822 3920 4138 422 36 22 C ATOM 1280 O CYS A 166 29.054 166.822 18.840 1.00 31.60 O ANISOU 1280 O CYS A 166 3864 3970 4170 412 60 -33 O ATOM 1281 CB CYS A 166 31.005 166.976 20.864 1.00 30.60 C ANISOU 1281 CB CYS A 166 3667 3878 4081 470 -2 65 C ATOM 1282 SG CYS A 166 30.553 168.610 21.388 1.00 31.36 S ANISOU 1282 SG CYS A 166 3781 4051 4084 435 -34 68 S ATOM 1283 N LEU A 167 27.496 166.244 20.373 1.00 32.15 N ANISOU 1283 N LEU A 167 3963 4023 4229 399 30 39 N ATOM 1284 CA LEU A 167 26.330 166.618 19.603 1.00 31.04 C ANISOU 1284 CA LEU A 167 3850 3888 4058 361 40 -4 C ATOM 1285 C LEU A 167 25.442 167.478 20.484 1.00 28.03 C ANISOU 1285 C LEU A 167 3480 3547 3621 340 19 29 C ATOM 1286 O LEU A 167 25.164 167.106 21.623 1.00 27.53 O ANISOU 1286 O LEU A 167 3420 3476 3563 348 12 83 O ATOM 1287 CB LEU A 167 25.577 165.375 19.154 1.00 32.17 C ANISOU 1287 CB LEU A 167 4006 3964 4255 353 60 -21 C ATOM 1288 CG LEU A 167 26.394 164.513 18.192 1.00 35.78 C ANISOU 1288 CG LEU A 167 4457 4373 4764 373 89 -64 C ATOM 1289 CD1 LEU A 167 25.846 163.139 18.101 1.00 38.01 C ANISOU 1289 CD1 LEU A 167 4749 4579 5115 372 106 -67 C ATOM 1290 CD2 LEU A 167 26.425 165.182 16.813 1.00 36.73 C ANISOU 1290 CD2 LEU A 167 4596 4517 4843 353 102 -135 C ATOM 1291 N PHE A 168 24.954 168.582 19.932 1.00 26.12 N ANISOU 1291 N PHE A 168 3249 3344 3331 315 14 -5 N ATOM 1292 CA PHE A 168 24.274 169.605 20.725 1.00 25.47 C ANISOU 1292 CA PHE A 168 3175 3305 3199 298 -1 19 C ATOM 1293 C PHE A 168 23.180 168.999 21.603 1.00 25.96 C ANISOU 1293 C PHE A 168 3246 3341 3276 290 6 58 C ATOM 1294 O PHE A 168 23.122 169.244 22.818 1.00 25.95 O ANISOU 1294 O PHE A 168 3251 3360 3248 296 2 104 O ATOM 1295 CB PHE A 168 23.692 170.678 19.790 1.00 25.03 C ANISOU 1295 CB PHE A 168 3129 3276 3104 272 -4 -25 C ATOM 1296 CG PHE A 168 23.114 171.856 20.514 1.00 24.70 C ANISOU 1296 CG PHE A 168 3092 3276 3017 259 -15 -7 C ATOM 1297 CD1 PHE A 168 21.796 171.855 20.971 1.00 25.08 C ANISOU 1297 CD1 PHE A 168 3146 3316 3069 242 -10 7 C ATOM 1298 CD2 PHE A 168 23.903 172.963 20.788 1.00 24.69 C ANISOU 1298 CD2 PHE A 168 3088 3318 2976 263 -26 -6 C ATOM 1299 CE1 PHE A 168 21.288 172.943 21.653 1.00 26.54 C ANISOU 1299 CE1 PHE A 168 3335 3534 3216 233 -12 20 C ATOM 1300 CE2 PHE A 168 23.379 174.073 21.471 1.00 26.33 C ANISOU 1300 CE2 PHE A 168 3302 3558 3142 251 -33 4 C ATOM 1301 CZ PHE A 168 22.051 174.036 21.911 1.00 27.07 C ANISOU 1301 CZ PHE A 168 3405 3642 3239 238 -23 17 C ATOM 1302 N GLU A 169 22.261 168.248 20.990 1.00 26.45 N ANISOU 1302 N GLU A 169 3310 3359 3379 272 19 37 N ATOM 1303 CA GLU A 169 21.073 167.824 21.727 1.00 26.98 C ANISOU 1303 CA GLU A 169 3380 3402 3467 257 33 70 C ATOM 1304 C GLU A 169 21.371 166.714 22.704 1.00 28.24 C ANISOU 1304 C GLU A 169 3544 3524 3662 277 47 126 C ATOM 1305 O GLU A 169 20.517 166.400 23.538 1.00 27.44 O ANISOU 1305 O GLU A 169 3448 3405 3571 267 67 166 O ATOM 1306 CB GLU A 169 19.944 167.361 20.803 1.00 27.39 C ANISOU 1306 CB GLU A 169 3427 3416 3564 227 37 30 C ATOM 1307 CG GLU A 169 19.347 168.565 19.990 1.00 28.85 C ANISOU 1307 CG GLU A 169 3610 3640 3710 205 16 -13 C ATOM 1308 CD GLU A 169 18.031 168.293 19.289 1.00 28.38 C ANISOU 1308 CD GLU A 169 3541 3552 3691 174 7 -44 C ATOM 1309 OE1 GLU A 169 17.461 167.207 19.465 1.00 27.86 O ANISOU 1309 OE1 GLU A 169 3465 3433 3687 163 21 -35 O ATOM 1310 OE2 GLU A 169 17.551 169.188 18.559 1.00 27.45 O ANISOU 1310 OE2 GLU A 169 3422 3460 3546 159 -17 -75 O ATOM 1311 N ASP A 170 22.557 166.128 22.637 1.00 29.47 N ANISOU 1311 N ASP A 170 3694 3664 3838 307 41 134 N ATOM 1312 CA ASP A 170 22.934 165.131 23.618 1.00 29.14 C ANISOU 1312 CA ASP A 170 3657 3586 3827 333 47 196 C ATOM 1313 C ASP A 170 23.490 165.732 24.896 1.00 29.96 C ANISOU 1313 C ASP A 170 3773 3739 3871 352 26 252 C ATOM 1314 O ASP A 170 23.435 165.070 25.939 1.00 32.93 O ANISOU 1314 O ASP A 170 4166 4094 4252 366 31 316 O ATOM 1315 CB ASP A 170 23.985 164.181 23.022 1.00 30.31 C ANISOU 1315 CB ASP A 170 3790 3690 4035 362 48 183 C ATOM 1316 CG ASP A 170 23.408 163.245 21.937 1.00 34.48 C ANISOU 1316 CG ASP A 170 4316 4153 4630 345 72 134 C ATOM 1317 OD1 ASP A 170 22.187 163.239 21.693 1.00 34.54 O ANISOU 1317 OD1 ASP A 170 4331 4147 4644 310 82 115 O ATOM 1318 OD2 ASP A 170 24.191 162.490 21.332 1.00 37.38 O ANISOU 1318 OD2 ASP A 170 4674 4479 5048 367 81 111 O ATOM 1319 N VAL A 171 24.066 166.933 24.843 1.00 27.66 N ANISOU 1319 N VAL A 171 3476 3509 3523 352 2 229 N ATOM 1320 CA VAL A 171 24.722 167.507 26.012 1.00 26.52 C ANISOU 1320 CA VAL A 171 3345 3411 3323 369 -28 273 C ATOM 1321 C VAL A 171 23.979 168.701 26.617 1.00 25.74 C ANISOU 1321 C VAL A 171 3268 3361 3150 344 -25 271 C ATOM 1322 O VAL A 171 24.105 168.924 27.828 1.00 28.12 O ANISOU 1322 O VAL A 171 3597 3689 3399 352 -38 316 O ATOM 1323 CB VAL A 171 26.185 167.890 25.713 1.00 30.60 C ANISOU 1323 CB VAL A 171 3833 3954 3841 392 -63 256 C ATOM 1324 CG1 VAL A 171 26.955 166.639 25.372 1.00 34.51 C ANISOU 1324 CG1 VAL A 171 4304 4395 4412 424 -61 269 C ATOM 1325 CG2 VAL A 171 26.286 168.901 24.605 1.00 32.69 C ANISOU 1325 CG2 VAL A 171 4081 4248 4093 372 -59 189 C ATOM 1326 N VAL A 172 23.256 169.488 25.824 1.00 23.91 N ANISOU 1326 N VAL A 172 3030 3144 2911 317 -11 220 N ATOM 1327 CA VAL A 172 22.546 170.678 26.300 1.00 25.82 C ANISOU 1327 CA VAL A 172 3288 3426 3095 297 -4 212 C ATOM 1328 C VAL A 172 21.102 170.269 26.572 1.00 27.26 C ANISOU 1328 C VAL A 172 3480 3579 3298 277 38 228 C ATOM 1329 O VAL A 172 20.431 169.805 25.645 1.00 27.93 O ANISOU 1329 O VAL A 172 3546 3629 3438 262 52 201 O ATOM 1330 CB VAL A 172 22.579 171.846 25.302 1.00 27.70 C ANISOU 1330 CB VAL A 172 3511 3694 3320 281 -13 154 C ATOM 1331 CG1 VAL A 172 21.838 173.054 25.942 1.00 30.46 C ANISOU 1331 CG1 VAL A 172 3878 4079 3616 264 -3 151 C ATOM 1332 CG2 VAL A 172 24.008 172.243 24.959 1.00 28.26 C ANISOU 1332 CG2 VAL A 172 3566 3790 3382 296 -45 137 C ATOM 1333 N PRO A 173 20.586 170.419 27.796 1.00 28.30 N ANISOU 1333 N PRO A 173 3641 3723 3389 275 60 270 N ATOM 1334 CA PRO A 173 19.209 169.964 28.077 1.00 27.28 C ANISOU 1334 CA PRO A 173 3514 3559 3292 255 110 288 C ATOM 1335 C PRO A 173 18.185 170.836 27.382 1.00 25.05 C ANISOU 1335 C PRO A 173 3208 3285 3026 230 125 241 C ATOM 1336 O PRO A 173 18.346 172.055 27.286 1.00 25.35 O ANISOU 1336 O PRO A 173 3248 3365 3020 228 110 211 O ATOM 1337 CB PRO A 173 19.085 170.095 29.594 1.00 29.03 C ANISOU 1337 CB PRO A 173 3781 3800 3449 261 134 342 C ATOM 1338 CG PRO A 173 20.435 170.349 30.090 1.00 30.59 C ANISOU 1338 CG PRO A 173 3999 4035 3588 286 85 356 C ATOM 1339 CD PRO A 173 21.206 171.009 28.990 1.00 30.29 C ANISOU 1339 CD PRO A 173 3928 4019 3564 287 43 299 C ATOM 1340 N MET A 174 17.121 170.207 26.878 1.00 24.44 N ANISOU 1340 N MET A 174 3106 3164 3018 210 150 234 N ATOM 1341 CA AMET A 174 16.100 170.991 26.194 0.50 25.68 C ANISOU 1341 CA AMET A 174 3233 3325 3199 188 155 192 C ATOM 1342 CA BMET A 174 16.079 170.979 26.201 0.50 25.72 C ANISOU 1342 CA BMET A 174 3238 3330 3206 188 156 193 C ATOM 1343 C MET A 174 15.294 171.831 27.168 1.00 24.26 C ANISOU 1343 C MET A 174 3062 3166 2989 182 197 208 C ATOM 1344 O MET A 174 14.785 172.895 26.781 1.00 25.17 O ANISOU 1344 O MET A 174 3160 3302 3102 173 193 174 O ATOM 1345 CB AMET A 174 15.198 170.067 25.371 0.50 27.33 C ANISOU 1345 CB AMET A 174 3407 3479 3497 167 161 177 C ATOM 1346 CB BMET A 174 15.134 170.050 25.439 0.50 27.29 C ANISOU 1346 CB BMET A 174 3402 3473 3493 167 165 179 C ATOM 1347 CG AMET A 174 14.519 170.745 24.216 0.50 32.44 C ANISOU 1347 CG AMET A 174 4022 4132 4172 150 134 124 C ATOM 1348 CG BMET A 174 15.727 169.509 24.172 0.50 31.07 C ANISOU 1348 CG BMET A 174 3871 3933 4000 168 122 140 C ATOM 1349 SD AMET A 174 15.632 171.533 23.034 0.50 35.27 S ANISOU 1349 SD AMET A 174 4391 4529 4481 162 76 75 S ATOM 1350 SD BMET A 174 16.059 170.815 22.972 0.50 33.28 S ANISOU 1350 SD BMET A 174 4145 4259 4240 167 74 80 S ATOM 1351 CE AMET A 174 16.284 170.129 22.125 0.50 36.08 C ANISOU 1351 CE AMET A 174 4496 4588 4625 164 56 56 C ATOM 1352 CE BMET A 174 14.480 170.859 22.225 0.50 34.99 C ANISOU 1352 CE BMET A 174 4323 4449 4524 136 70 52 C ATOM 1353 N ASN A 175 15.171 171.398 28.430 1.00 24.97 N ANISOU 1353 N ASN A 175 3183 3250 3054 186 241 260 N ATOM 1354 CA ASN A 175 14.429 172.253 29.347 1.00 26.09 C ANISOU 1354 CA ASN A 175 3340 3413 3160 181 290 268 C ATOM 1355 C ASN A 175 15.164 173.573 29.574 1.00 26.10 C ANISOU 1355 C ASN A 175 3366 3469 3080 192 262 242 C ATOM 1356 O ASN A 175 14.525 174.627 29.620 1.00 27.18 O ANISOU 1356 O ASN A 175 3495 3622 3212 185 283 215 O ATOM 1357 CB ASN A 175 14.086 171.564 30.674 1.00 27.90 C ANISOU 1357 CB ASN A 175 3608 3626 3369 181 352 330 C ATOM 1358 CG ASN A 175 15.247 170.848 31.331 1.00 32.05 C ANISOU 1358 CG ASN A 175 4181 4158 3839 203 327 376 C ATOM 1359 OD1 ASN A 175 16.417 171.159 31.087 1.00 32.93 O ANISOU 1359 OD1 ASN A 175 4303 4300 3908 220 265 360 O ATOM 1360 ND2 ASN A 175 14.916 169.870 32.209 1.00 34.85 N ANISOU 1360 ND2 ASN A 175 4565 4480 4197 203 375 438 N ATOM 1361 N TYR A 176 16.503 173.550 29.638 1.00 24.91 N ANISOU 1361 N TYR A 176 3241 3345 2878 209 212 245 N ATOM 1362 CA TYR A 176 17.279 174.801 29.629 1.00 24.47 C ANISOU 1362 CA TYR A 176 3200 3337 2763 215 176 211 C ATOM 1363 C TYR A 176 16.993 175.623 28.365 1.00 23.90 C ANISOU 1363 C TYR A 176 3086 3265 2729 206 156 159 C ATOM 1364 O TYR A 176 16.784 176.849 28.438 1.00 24.60 O ANISOU 1364 O TYR A 176 3177 3376 2793 201 161 131 O ATOM 1365 CB TYR A 176 18.792 174.490 29.752 1.00 24.38 C ANISOU 1365 CB TYR A 176 3206 3346 2713 234 121 224 C ATOM 1366 CG TYR A 176 19.636 175.714 29.447 1.00 26.24 C ANISOU 1366 CG TYR A 176 3439 3621 2911 235 80 182 C ATOM 1367 CD1 TYR A 176 20.038 175.985 28.153 1.00 28.04 C ANISOU 1367 CD1 TYR A 176 3630 3846 3177 232 50 144 C ATOM 1368 CD2 TYR A 176 19.943 176.645 30.448 1.00 27.04 C ANISOU 1368 CD2 TYR A 176 3578 3759 2937 235 76 178 C ATOM 1369 CE1 TYR A 176 20.756 177.121 27.841 1.00 30.24 C ANISOU 1369 CE1 TYR A 176 3906 4155 3429 230 21 109 C ATOM 1370 CE2 TYR A 176 20.684 177.797 30.160 1.00 29.40 C ANISOU 1370 CE2 TYR A 176 3872 4088 3212 231 40 137 C ATOM 1371 CZ TYR A 176 21.057 178.030 28.842 1.00 32.12 C ANISOU 1371 CZ TYR A 176 4174 4426 3604 228 16 105 C ATOM 1372 OH TYR A 176 21.773 179.136 28.519 1.00 36.56 O ANISOU 1372 OH TYR A 176 4730 5011 4149 222 -12 69 O ATOM 1373 N MET A 177 16.982 174.977 27.172 1.00 24.12 N ANISOU 1373 N MET A 177 3081 3267 2818 202 132 144 N ATOM 1374 CA MET A 177 16.850 175.752 25.935 1.00 23.15 C ANISOU 1374 CA MET A 177 2929 3149 2716 194 104 99 C ATOM 1375 C MET A 177 15.476 176.365 25.812 1.00 22.91 C ANISOU 1375 C MET A 177 2875 3107 2722 181 131 86 C ATOM 1376 O MET A 177 15.330 177.452 25.240 1.00 25.48 O ANISOU 1376 O MET A 177 3190 3447 3044 179 115 56 O ATOM 1377 CB MET A 177 17.117 174.880 24.708 1.00 22.14 C ANISOU 1377 CB MET A 177 2782 2997 2635 192 74 83 C ATOM 1378 CG MET A 177 18.562 174.441 24.499 1.00 23.00 C ANISOU 1378 CG MET A 177 2903 3114 2721 208 45 84 C ATOM 1379 SD MET A 177 19.707 175.823 24.422 1.00 24.88 S ANISOU 1379 SD MET A 177 3152 3401 2900 215 17 60 S ATOM 1380 CE MET A 177 19.113 176.697 23.008 1.00 27.31 C ANISOU 1380 CE MET A 177 3443 3708 3226 201 5 17 C ATOM 1381 N VAL A 178 14.443 175.673 26.318 1.00 22.58 N ANISOU 1381 N VAL A 178 2820 3036 2724 172 174 110 N ATOM 1382 CA VAL A 178 13.086 176.153 26.118 1.00 22.92 C ANISOU 1382 CA VAL A 178 2825 3062 2822 160 200 98 C ATOM 1383 C VAL A 178 12.680 177.125 27.215 1.00 23.94 C ANISOU 1383 C VAL A 178 2971 3208 2916 165 251 104 C ATOM 1384 O VAL A 178 12.269 178.264 26.927 1.00 24.44 O ANISOU 1384 O VAL A 178 3019 3281 2988 166 248 77 O ATOM 1385 CB VAL A 178 12.113 174.963 26.013 1.00 26.75 C ANISOU 1385 CB VAL A 178 3276 3500 3388 144 224 115 C ATOM 1386 CG1 VAL A 178 10.681 175.442 26.017 1.00 29.64 C ANISOU 1386 CG1 VAL A 178 3594 3846 3820 133 257 108 C ATOM 1387 CG2 VAL A 178 12.378 174.220 24.679 1.00 26.84 C ANISOU 1387 CG2 VAL A 178 3268 3491 3438 137 167 92 C ATOM 1388 N TYR A 179 12.771 176.697 28.479 1.00 24.91 N ANISOU 1388 N TYR A 179 3131 3333 2999 168 299 138 N ATOM 1389 CA TYR A 179 12.270 177.552 29.554 1.00 26.56 C ANISOU 1389 CA TYR A 179 3363 3556 3174 171 358 139 C ATOM 1390 C TYR A 179 13.229 178.703 29.846 1.00 27.66 C ANISOU 1390 C TYR A 179 3543 3737 3230 181 331 114 C ATOM 1391 O TYR A 179 12.817 179.850 30.014 1.00 29.47 O ANISOU 1391 O TYR A 179 3771 3974 3454 183 353 87 O ATOM 1392 CB TYR A 179 12.101 176.746 30.815 1.00 26.25 C ANISOU 1392 CB TYR A 179 3362 3508 3103 170 420 186 C ATOM 1393 CG TYR A 179 10.957 175.720 30.766 1.00 30.65 C ANISOU 1393 CG TYR A 179 3878 4017 3751 155 470 213 C ATOM 1394 CD1 TYR A 179 9.716 176.062 30.270 1.00 33.84 C ANISOU 1394 CD1 TYR A 179 4218 4394 4245 144 497 193 C ATOM 1395 CD2 TYR A 179 11.125 174.447 31.261 1.00 33.31 C ANISOU 1395 CD2 TYR A 179 4237 4332 4086 152 490 261 C ATOM 1396 CE1 TYR A 179 8.685 175.168 30.249 1.00 36.01 C ANISOU 1396 CE1 TYR A 179 4448 4623 4610 127 541 216 C ATOM 1397 CE2 TYR A 179 10.076 173.529 31.256 1.00 36.25 C ANISOU 1397 CE2 TYR A 179 4570 4654 4548 134 541 287 C ATOM 1398 CZ TYR A 179 8.871 173.895 30.749 1.00 37.51 C ANISOU 1398 CZ TYR A 179 4663 4790 4799 120 566 262 C ATOM 1399 OH TYR A 179 7.821 173.012 30.717 1.00 39.61 O ANISOU 1399 OH TYR A 179 4880 5004 5165 99 614 283 O ATOM 1400 N PHE A 180 14.524 178.410 29.934 1.00 26.69 N ANISOU 1400 N PHE A 180 3454 3639 3050 189 283 121 N ATOM 1401 CA PHE A 180 15.481 179.388 30.436 1.00 27.66 C ANISOU 1401 CA PHE A 180 3617 3799 3092 195 259 101 C ATOM 1402 C PHE A 180 15.978 180.278 29.296 1.00 27.86 C ANISOU 1402 C PHE A 180 3615 3834 3136 194 207 61 C ATOM 1403 O PHE A 180 15.859 181.512 29.355 1.00 29.51 O ANISOU 1403 O PHE A 180 3829 4052 3332 192 214 29 O ATOM 1404 CB PHE A 180 16.638 178.670 31.101 1.00 28.32 C ANISOU 1404 CB PHE A 180 3743 3903 3114 203 227 131 C ATOM 1405 CG PHE A 180 17.530 179.572 31.928 1.00 29.96 C ANISOU 1405 CG PHE A 180 3998 4151 3235 206 204 114 C ATOM 1406 CD1 PHE A 180 18.629 180.196 31.335 1.00 29.95 C ANISOU 1406 CD1 PHE A 180 3986 4171 3224 206 142 84 C ATOM 1407 CD2 PHE A 180 17.303 179.754 33.280 1.00 33.25 C ANISOU 1407 CD2 PHE A 180 4473 4583 3579 206 244 126 C ATOM 1408 CE1 PHE A 180 19.476 180.988 32.083 1.00 31.88 C ANISOU 1408 CE1 PHE A 180 4267 4447 3397 205 114 65 C ATOM 1409 CE2 PHE A 180 18.148 180.547 34.049 1.00 33.94 C ANISOU 1409 CE2 PHE A 180 4607 4705 3581 205 214 105 C ATOM 1410 CZ PHE A 180 19.234 181.169 33.452 1.00 32.11 C ANISOU 1410 CZ PHE A 180 4357 4493 3350 204 145 73 C ATOM 1411 N ASN A 181 16.525 179.670 28.243 1.00 25.42 N ANISOU 1411 N ASN A 181 3281 3518 2859 195 161 61 N ATOM 1412 CA ASN A 181 17.054 180.469 27.150 1.00 24.16 C ANISOU 1412 CA ASN A 181 3103 3367 2709 193 118 28 C ATOM 1413 C ASN A 181 15.916 181.136 26.352 1.00 23.98 C ANISOU 1413 C ASN A 181 3046 3324 2742 188 130 9 C ATOM 1414 O ASN A 181 15.869 182.369 26.240 1.00 25.98 O ANISOU 1414 O ASN A 181 3301 3584 2988 188 129 -15 O ATOM 1415 CB ASN A 181 17.959 179.631 26.249 1.00 25.95 C ANISOU 1415 CB ASN A 181 3317 3592 2950 196 75 31 C ATOM 1416 CG ASN A 181 18.740 180.507 25.276 1.00 27.75 C ANISOU 1416 CG ASN A 181 3538 3834 3173 194 39 1 C ATOM 1417 OD1 ASN A 181 18.337 180.706 24.149 1.00 28.13 O ANISOU 1417 OD1 ASN A 181 3566 3868 3254 190 28 -15 O ATOM 1418 ND2 ASN A 181 19.877 181.019 25.720 1.00 28.15 N ANISOU 1418 ND2 ASN A 181 3605 3909 3179 196 20 -6 N ATOM 1419 N PHE A 182 14.979 180.351 25.804 1.00 23.25 N ANISOU 1419 N PHE A 182 2921 3203 2711 183 136 19 N ATOM 1420 CA PHE A 182 13.954 180.922 24.927 1.00 23.44 C ANISOU 1420 CA PHE A 182 2905 3207 2792 180 130 3 C ATOM 1421 C PHE A 182 12.971 181.797 25.705 1.00 24.74 C ANISOU 1421 C PHE A 182 3061 3364 2974 183 181 -1 C ATOM 1422 O PHE A 182 12.887 183.007 25.463 1.00 26.56 O ANISOU 1422 O PHE A 182 3289 3598 3205 188 175 -21 O ATOM 1423 CB PHE A 182 13.211 179.820 24.158 1.00 24.74 C ANISOU 1423 CB PHE A 182 3034 3343 3022 171 116 10 C ATOM 1424 CG PHE A 182 12.161 180.331 23.207 1.00 27.13 C ANISOU 1424 CG PHE A 182 3294 3627 3386 167 93 -5 C ATOM 1425 CD1 PHE A 182 12.315 181.555 22.531 1.00 26.27 C ANISOU 1425 CD1 PHE A 182 3188 3530 3265 174 64 -23 C ATOM 1426 CD2 PHE A 182 10.994 179.612 22.991 1.00 31.34 C ANISOU 1426 CD2 PHE A 182 3783 4129 3996 156 99 2 C ATOM 1427 CE1 PHE A 182 11.335 182.010 21.662 1.00 28.20 C ANISOU 1427 CE1 PHE A 182 3394 3756 3564 174 35 -30 C ATOM 1428 CE2 PHE A 182 10.025 180.060 22.101 1.00 33.15 C ANISOU 1428 CE2 PHE A 182 3968 4342 4286 154 66 -11 C ATOM 1429 CZ PHE A 182 10.203 181.274 21.443 1.00 32.00 C ANISOU 1429 CZ PHE A 182 3829 4210 4121 164 31 -24 C ATOM 1430 N PHE A 183 12.205 181.212 26.639 1.00 25.75 N ANISOU 1430 N PHE A 183 3185 3478 3122 180 237 20 N ATOM 1431 CA PHE A 183 11.143 181.981 27.275 1.00 27.73 C ANISOU 1431 CA PHE A 183 3418 3714 3402 184 296 14 C ATOM 1432 C PHE A 183 11.707 183.150 28.088 1.00 27.40 C ANISOU 1432 C PHE A 183 3423 3695 3292 192 317 -6 C ATOM 1433 O PHE A 183 11.303 184.305 27.896 1.00 29.72 O ANISOU 1433 O PHE A 183 3702 3980 3609 199 325 -29 O ATOM 1434 CB PHE A 183 10.262 181.096 28.180 1.00 28.24 C ANISOU 1434 CB PHE A 183 3474 3758 3498 178 366 42 C ATOM 1435 CG PHE A 183 9.350 180.114 27.435 1.00 31.96 C ANISOU 1435 CG PHE A 183 3884 4194 4065 166 356 55 C ATOM 1436 CD1 PHE A 183 9.179 180.162 26.070 1.00 32.98 C ANISOU 1436 CD1 PHE A 183 3972 4314 4244 163 287 38 C ATOM 1437 CD2 PHE A 183 8.691 179.107 28.133 1.00 36.03 C ANISOU 1437 CD2 PHE A 183 4389 4685 4615 155 414 85 C ATOM 1438 CE1 PHE A 183 8.343 179.259 25.407 1.00 34.45 C ANISOU 1438 CE1 PHE A 183 4105 4468 4517 148 270 45 C ATOM 1439 CE2 PHE A 183 7.866 178.201 27.469 1.00 38.19 C ANISOU 1439 CE2 PHE A 183 4603 4922 4984 140 403 94 C ATOM 1440 CZ PHE A 183 7.700 178.292 26.097 1.00 35.75 C ANISOU 1440 CZ PHE A 183 4252 4606 4726 136 327 70 C ATOM 1441 N ALA A 184 12.629 182.880 29.011 1.00 25.86 N ANISOU 1441 N ALA A 184 3284 3526 3015 191 324 2 N ATOM 1442 CA ALA A 184 13.032 183.934 29.940 1.00 27.31 C ANISOU 1442 CA ALA A 184 3515 3729 3132 194 349 -22 C ATOM 1443 C ALA A 184 14.059 184.879 29.333 1.00 27.16 C ANISOU 1443 C ALA A 184 3506 3727 3086 194 290 -51 C ATOM 1444 O ALA A 184 13.981 186.101 29.544 1.00 27.50 O ANISOU 1444 O ALA A 184 3561 3767 3123 196 306 -82 O ATOM 1445 CB ALA A 184 13.579 183.306 31.228 1.00 28.94 C ANISOU 1445 CB ALA A 184 3783 3958 3255 192 372 -1 C ATOM 1446 N CYS A 185 15.058 184.354 28.617 1.00 25.91 N ANISOU 1446 N CYS A 185 3345 3583 2915 191 228 -43 N ATOM 1447 CA CYS A 185 16.158 185.189 28.160 1.00 25.23 C ANISOU 1447 CA CYS A 185 3271 3514 2801 188 181 -68 C ATOM 1448 C CYS A 185 15.987 185.785 26.769 1.00 26.15 C ANISOU 1448 C CYS A 185 3351 3614 2971 188 151 -79 C ATOM 1449 O CYS A 185 16.704 186.731 26.449 1.00 28.01 O ANISOU 1449 O CYS A 185 3596 3856 3192 184 128 -100 O ATOM 1450 CB CYS A 185 17.469 184.413 28.171 1.00 27.56 C ANISOU 1450 CB CYS A 185 3582 3834 3055 185 135 -54 C ATOM 1451 SG CYS A 185 17.929 184.030 29.912 1.00 32.11 S ANISOU 1451 SG CYS A 185 4217 4437 3548 186 153 -41 S ATOM 1452 N VAL A 186 15.099 185.257 25.931 1.00 26.61 N ANISOU 1452 N VAL A 186 3371 3651 3089 191 147 -65 N ATOM 1453 CA VAL A 186 14.929 185.795 24.580 1.00 27.18 C ANISOU 1453 CA VAL A 186 3418 3710 3201 192 111 -71 C ATOM 1454 C VAL A 186 13.545 186.399 24.389 1.00 26.60 C ANISOU 1454 C VAL A 186 3308 3606 3191 200 132 -72 C ATOM 1455 O VAL A 186 13.402 187.571 24.006 1.00 25.97 O ANISOU 1455 O VAL A 186 3225 3514 3129 206 127 -84 O ATOM 1456 CB VAL A 186 15.204 184.693 23.544 1.00 27.46 C ANISOU 1456 CB VAL A 186 3440 3747 3248 188 70 -59 C ATOM 1457 CG1 VAL A 186 14.854 185.159 22.128 1.00 27.98 C ANISOU 1457 CG1 VAL A 186 3486 3799 3346 189 32 -62 C ATOM 1458 CG2 VAL A 186 16.687 184.285 23.609 1.00 27.36 C ANISOU 1458 CG2 VAL A 186 3454 3759 3182 184 49 -60 C ATOM 1459 N LEU A 187 12.517 185.603 24.614 1.00 27.47 N ANISOU 1459 N LEU A 187 3389 3701 3347 201 157 -58 N ATOM 1460 CA LEU A 187 11.171 186.064 24.333 1.00 28.46 C ANISOU 1460 CA LEU A 187 3466 3795 3551 210 171 -56 C ATOM 1461 C LEU A 187 10.764 187.211 25.251 1.00 28.01 C ANISOU 1461 C LEU A 187 3416 3727 3500 220 228 -72 C ATOM 1462 O LEU A 187 10.188 188.196 24.788 1.00 28.42 O ANISOU 1462 O LEU A 187 3442 3756 3602 233 223 -79 O ATOM 1463 CB LEU A 187 10.211 184.888 24.444 1.00 32.82 C ANISOU 1463 CB LEU A 187 3980 4332 4160 204 189 -38 C ATOM 1464 CG LEU A 187 8.782 185.049 23.988 1.00 41.10 C ANISOU 1464 CG LEU A 187 4961 5347 5307 209 190 -34 C ATOM 1465 CD1 LEU A 187 8.750 185.541 22.549 1.00 42.98 C ANISOU 1465 CD1 LEU A 187 5182 5580 5568 213 112 -37 C ATOM 1466 CD2 LEU A 187 8.055 183.710 24.114 1.00 45.49 C ANISOU 1466 CD2 LEU A 187 5481 5887 5916 196 205 -17 C ATOM 1467 N VAL A 188 11.053 187.141 26.546 1.00 27.80 N ANISOU 1467 N VAL A 188 3427 3713 3422 218 283 -80 N ATOM 1468 CA VAL A 188 10.656 188.228 27.445 1.00 29.93 C ANISOU 1468 CA VAL A 188 3710 3969 3692 227 344 -103 C ATOM 1469 C VAL A 188 11.335 189.539 27.037 1.00 29.63 C ANISOU 1469 C VAL A 188 3693 3929 3636 230 314 -128 C ATOM 1470 O VAL A 188 10.637 190.548 26.878 1.00 27.68 O ANISOU 1470 O VAL A 188 3421 3650 3445 244 334 -140 O ATOM 1471 CB VAL A 188 10.875 187.846 28.892 1.00 31.65 C ANISOU 1471 CB VAL A 188 3978 4204 3843 221 404 -107 C ATOM 1472 CG1 VAL A 188 10.862 189.096 29.814 1.00 31.25 C ANISOU 1472 CG1 VAL A 188 3964 4146 3762 227 457 -144 C ATOM 1473 CG2 VAL A 188 9.762 186.885 29.324 1.00 34.43 C ANISOU 1473 CG2 VAL A 188 4298 4540 4244 221 460 -82 C ATOM 1474 N PRO A 189 12.646 189.577 26.807 1.00 30.18 N ANISOU 1474 N PRO A 189 3800 4026 3642 219 267 -134 N ATOM 1475 CA PRO A 189 13.238 190.825 26.302 1.00 29.37 C ANISOU 1475 CA PRO A 189 3709 3913 3537 219 241 -154 C ATOM 1476 C PRO A 189 12.691 191.291 24.957 1.00 28.21 C ANISOU 1476 C PRO A 189 3522 3740 3457 230 204 -138 C ATOM 1477 O PRO A 189 12.579 192.504 24.735 1.00 30.62 O ANISOU 1477 O PRO A 189 3827 4018 3790 238 209 -150 O ATOM 1478 CB PRO A 189 14.733 190.479 26.221 1.00 30.87 C ANISOU 1478 CB PRO A 189 3934 4139 3657 202 198 -156 C ATOM 1479 CG PRO A 189 14.933 189.442 27.230 1.00 31.28 C ANISOU 1479 CG PRO A 189 4008 4216 3659 197 217 -149 C ATOM 1480 CD PRO A 189 13.677 188.605 27.228 1.00 30.28 C ANISOU 1480 CD PRO A 189 3848 4075 3584 206 247 -125 C ATOM 1481 N LEU A 190 12.404 190.387 24.008 1.00 27.25 N ANISOU 1481 N LEU A 190 3371 3623 3360 229 163 -111 N ATOM 1482 CA LEU A 190 11.859 190.832 22.723 1.00 27.62 C ANISOU 1482 CA LEU A 190 3386 3647 3461 240 118 -94 C ATOM 1483 C LEU A 190 10.503 191.504 22.905 1.00 28.00 C ANISOU 1483 C LEU A 190 3390 3655 3592 261 149 -93 C ATOM 1484 O LEU A 190 10.199 192.512 22.248 1.00 27.53 O ANISOU 1484 O LEU A 190 3318 3569 3574 275 128 -86 O ATOM 1485 CB LEU A 190 11.736 189.645 21.753 1.00 28.97 C ANISOU 1485 CB LEU A 190 3539 3831 3637 233 67 -73 C ATOM 1486 CG LEU A 190 13.029 189.104 21.136 1.00 33.55 C ANISOU 1486 CG LEU A 190 4155 4440 4150 218 29 -72 C ATOM 1487 CD1 LEU A 190 12.658 187.886 20.294 1.00 34.81 C ANISOU 1487 CD1 LEU A 190 4296 4605 4326 213 -11 -59 C ATOM 1488 CD2 LEU A 190 13.756 190.154 20.290 1.00 36.64 C ANISOU 1488 CD2 LEU A 190 4572 4828 4521 218 2 -71 C ATOM 1489 N LEU A 191 9.684 190.993 23.828 1.00 29.15 N ANISOU 1489 N LEU A 191 3512 3796 3769 264 203 -96 N ATOM 1490 CA LEU A 191 8.392 191.620 24.100 1.00 32.28 C ANISOU 1490 CA LEU A 191 3858 4151 4254 285 245 -98 C ATOM 1491 C LEU A 191 8.550 192.960 24.799 1.00 34.53 C ANISOU 1491 C LEU A 191 4170 4414 4535 297 295 -126 C ATOM 1492 O LEU A 191 7.793 193.906 24.525 1.00 36.13 O ANISOU 1492 O LEU A 191 4337 4575 4814 319 303 -125 O ATOM 1493 CB LEU A 191 7.539 190.683 24.940 1.00 33.47 C ANISOU 1493 CB LEU A 191 3978 4300 4438 283 302 -95 C ATOM 1494 CG LEU A 191 7.159 189.359 24.271 1.00 37.80 C ANISOU 1494 CG LEU A 191 4490 4858 5014 270 258 -69 C ATOM 1495 CD1 LEU A 191 6.418 188.480 25.277 1.00 39.74 C ANISOU 1495 CD1 LEU A 191 4712 5098 5290 264 331 -65 C ATOM 1496 CD2 LEU A 191 6.284 189.607 23.067 1.00 41.65 C ANISOU 1496 CD2 LEU A 191 4915 5320 5590 283 195 -52 C ATOM 1497 N LEU A 192 9.527 193.075 25.693 1.00 32.69 N ANISOU 1497 N LEU A 192 3998 4204 4218 282 325 -153 N ATOM 1498 CA LEU A 192 9.814 194.373 26.304 1.00 32.79 C ANISOU 1498 CA LEU A 192 4044 4194 4220 287 365 -188 C ATOM 1499 C LEU A 192 10.231 195.396 25.261 1.00 31.36 C ANISOU 1499 C LEU A 192 3863 3991 4061 292 313 -181 C ATOM 1500 O LEU A 192 9.816 196.562 25.317 1.00 30.97 O ANISOU 1500 O LEU A 192 3805 3897 4064 310 339 -195 O ATOM 1501 CB LEU A 192 10.914 194.246 27.347 1.00 35.02 C ANISOU 1501 CB LEU A 192 4395 4512 4401 265 385 -218 C ATOM 1502 CG LEU A 192 10.621 193.431 28.599 1.00 39.28 C ANISOU 1502 CG LEU A 192 4955 5072 4898 260 447 -226 C ATOM 1503 CD1 LEU A 192 11.905 193.321 29.448 1.00 41.23 C ANISOU 1503 CD1 LEU A 192 5274 5358 5034 237 439 -251 C ATOM 1504 CD2 LEU A 192 9.513 194.079 29.397 1.00 41.54 C ANISOU 1504 CD2 LEU A 192 5228 5320 5236 278 535 -250 C ATOM 1505 N MET A 193 11.072 194.985 24.322 1.00 30.23 N ANISOU 1505 N MET A 193 3734 3875 3878 278 245 -160 N ATOM 1506 CA MET A 193 11.497 195.862 23.236 1.00 29.16 C ANISOU 1506 CA MET A 193 3604 3720 3757 281 198 -145 C ATOM 1507 C MET A 193 10.321 196.314 22.394 1.00 32.00 C ANISOU 1507 C MET A 193 3913 4039 4208 309 177 -115 C ATOM 1508 O MET A 193 10.258 197.479 21.987 1.00 35.50 O ANISOU 1508 O MET A 193 4357 4442 4689 323 172 -110 O ATOM 1509 CB MET A 193 12.502 195.148 22.322 1.00 30.61 C ANISOU 1509 CB MET A 193 3808 3941 3882 261 137 -124 C ATOM 1510 CG MET A 193 13.853 195.077 22.904 1.00 33.42 C ANISOU 1510 CG MET A 193 4209 4327 4162 236 144 -150 C ATOM 1511 SD MET A 193 14.947 194.200 21.767 1.00 37.33 S ANISOU 1511 SD MET A 193 4718 4860 4606 218 84 -125 S ATOM 1512 CE MET A 193 15.550 192.818 22.754 1.00 39.61 C ANISOU 1512 CE MET A 193 5019 5196 4835 203 95 -139 C ATOM 1513 N LEU A 194 9.411 195.387 22.075 1.00 34.06 N ANISOU 1513 N LEU A 194 4127 4307 4508 317 157 -93 N ATOM 1514 CA LEU A 194 8.201 195.739 21.343 1.00 38.48 C ANISOU 1514 CA LEU A 194 4629 4829 5164 345 129 -64 C ATOM 1515 C LEU A 194 7.421 196.815 22.080 1.00 34.27 C ANISOU 1515 C LEU A 194 4069 4245 4708 371 193 -82 C ATOM 1516 O LEU A 194 6.961 197.797 21.478 1.00 33.56 O ANISOU 1516 O LEU A 194 3956 4111 4683 396 171 -63 O ATOM 1517 CB LEU A 194 7.339 194.491 21.126 1.00 44.66 C ANISOU 1517 CB LEU A 194 5360 5628 5982 343 106 -48 C ATOM 1518 CG LEU A 194 5.913 194.706 20.568 1.00 50.05 C ANISOU 1518 CG LEU A 194 5965 6272 6781 371 78 -22 C ATOM 1519 CD1 LEU A 194 5.952 195.351 19.187 1.00 54.39 C ANISOU 1519 CD1 LEU A 194 6518 6806 7340 384 -9 13 C ATOM 1520 CD2 LEU A 194 5.134 193.395 20.501 1.00 49.09 C ANISOU 1520 CD2 LEU A 194 5791 6165 6697 361 61 -14 C ATOM 1521 N GLY A 195 7.268 196.656 23.385 1.00 30.04 N ANISOU 1521 N GLY A 195 3539 3712 4164 367 274 -117 N ATOM 1522 CA GLY A 195 6.543 197.645 24.155 1.00 29.62 C ANISOU 1522 CA GLY A 195 3465 3608 4180 392 348 -142 C ATOM 1523 C GLY A 195 7.243 198.984 24.219 1.00 30.86 C ANISOU 1523 C GLY A 195 3669 3735 4323 394 360 -164 C ATOM 1524 O GLY A 195 6.593 200.034 24.148 1.00 34.28 O ANISOU 1524 O GLY A 195 4074 4110 4842 424 383 -165 O ATOM 1525 N VAL A 196 8.575 198.979 24.343 1.00 30.19 N ANISOU 1525 N VAL A 196 3651 3683 4139 364 344 -182 N ATOM 1526 CA VAL A 196 9.314 200.237 24.334 1.00 31.79 C ANISOU 1526 CA VAL A 196 3894 3852 4331 360 350 -203 C ATOM 1527 C VAL A 196 9.132 200.962 22.998 1.00 32.61 C ANISOU 1527 C VAL A 196 3977 3919 4495 379 290 -156 C ATOM 1528 O VAL A 196 8.852 202.166 22.966 1.00 33.40 O ANISOU 1528 O VAL A 196 4073 3960 4660 400 312 -161 O ATOM 1529 CB VAL A 196 10.801 200.006 24.658 1.00 32.90 C ANISOU 1529 CB VAL A 196 4099 4037 4363 321 335 -228 C ATOM 1530 CG1 VAL A 196 11.598 201.289 24.516 1.00 32.44 C ANISOU 1530 CG1 VAL A 196 4078 3943 4306 312 335 -247 C ATOM 1531 CG2 VAL A 196 10.934 199.508 26.104 1.00 36.06 C ANISOU 1531 CG2 VAL A 196 4530 4467 4704 306 395 -275 C ATOM 1532 N TYR A 197 9.312 200.259 21.872 1.00 31.15 N ANISOU 1532 N TYR A 197 3784 3767 4286 373 214 -110 N ATOM 1533 CA TYR A 197 9.095 200.900 20.569 1.00 32.40 C ANISOU 1533 CA TYR A 197 3930 3891 4488 392 153 -60 C ATOM 1534 C TYR A 197 7.673 201.426 20.432 1.00 34.00 C ANISOU 1534 C TYR A 197 4069 4041 4811 436 157 -39 C ATOM 1535 O TYR A 197 7.468 202.527 19.913 1.00 34.69 O ANISOU 1535 O TYR A 197 4152 4073 4955 459 144 -15 O ATOM 1536 CB TYR A 197 9.451 199.957 19.408 1.00 32.70 C ANISOU 1536 CB TYR A 197 3977 3977 4471 378 74 -20 C ATOM 1537 CG TYR A 197 10.950 199.993 19.188 1.00 32.05 C ANISOU 1537 CG TYR A 197 3957 3922 4296 344 66 -28 C ATOM 1538 CD1 TYR A 197 11.573 201.147 18.727 1.00 33.90 C ANISOU 1538 CD1 TYR A 197 4225 4121 4534 342 64 -15 C ATOM 1539 CD2 TYR A 197 11.745 198.897 19.500 1.00 28.87 C ANISOU 1539 CD2 TYR A 197 3576 3578 3815 314 66 -48 C ATOM 1540 CE1 TYR A 197 12.949 201.210 18.563 1.00 35.04 C ANISOU 1540 CE1 TYR A 197 4419 4287 4608 308 65 -25 C ATOM 1541 CE2 TYR A 197 13.134 198.947 19.341 1.00 28.79 C ANISOU 1541 CE2 TYR A 197 3614 3591 3734 285 62 -57 C ATOM 1542 CZ TYR A 197 13.726 200.110 18.879 1.00 32.66 C ANISOU 1542 CZ TYR A 197 4132 4046 4232 280 63 -47 C ATOM 1543 OH TYR A 197 15.086 200.188 18.725 1.00 34.22 O ANISOU 1543 OH TYR A 197 4367 4262 4373 249 64 -56 O ATOM 1544 N ALEU A 198 6.680 200.663 20.886 0.50 34.90 N ANISOU 1544 N ALEU A 198 4127 4164 4970 447 177 -45 N ATOM 1545 N BLEU A 198 6.679 200.657 20.873 0.50 34.90 N ANISOU 1545 N BLEU A 198 4126 4164 4969 447 176 -45 N ATOM 1546 CA ALEU A 198 5.308 201.170 20.866 0.50 36.16 C ANISOU 1546 CA ALEU A 198 4212 4268 5258 490 190 -29 C ATOM 1547 CA BLEU A 198 5.307 201.163 20.874 0.50 36.17 C ANISOU 1547 CA BLEU A 198 4214 4270 5259 490 190 -30 C ATOM 1548 C ALEU A 198 5.193 202.477 21.640 0.50 35.27 C ANISOU 1548 C ALEU A 198 4107 4093 5202 510 268 -63 C ATOM 1549 C BLEU A 198 5.225 202.491 21.620 0.50 35.17 C ANISOU 1549 C BLEU A 198 4096 4080 5187 510 266 -62 C ATOM 1550 O ALEU A 198 4.521 203.415 21.189 0.50 36.81 O ANISOU 1550 O ALEU A 198 4265 4225 5495 548 256 -36 O ATOM 1551 O BLEU A 198 4.621 203.455 21.133 0.50 36.75 O ANISOU 1551 O BLEU A 198 4264 4219 5481 546 252 -35 O ATOM 1552 CB ALEU A 198 4.339 200.131 21.430 0.50 36.43 C ANISOU 1552 CB ALEU A 198 4185 4321 5336 492 219 -39 C ATOM 1553 CB BLEU A 198 4.357 200.137 21.493 0.50 36.40 C ANISOU 1553 CB BLEU A 198 4183 4318 5331 492 224 -42 C ATOM 1554 CG ALEU A 198 4.052 198.912 20.553 0.50 35.81 C ANISOU 1554 CG ALEU A 198 4076 4286 5246 480 136 -4 C ATOM 1555 CG BLEU A 198 2.873 200.516 21.557 0.50 38.77 C ANISOU 1555 CG BLEU A 198 4390 4562 5779 535 245 -29 C ATOM 1556 CD1ALEU A 198 3.110 197.958 21.266 0.50 34.58 C ANISOU 1556 CD1ALEU A 198 3857 4139 5144 479 182 -18 C ATOM 1557 CD1BLEU A 198 2.230 200.437 20.188 0.50 39.55 C ANISOU 1557 CD1BLEU A 198 4436 4651 5939 555 134 31 C ATOM 1558 CD2ALEU A 198 3.486 199.289 19.192 0.50 37.37 C ANISOU 1558 CD2ALEU A 198 4237 4458 5504 506 37 51 C ATOM 1559 CD2BLEU A 198 2.137 199.625 22.547 0.50 39.86 C ANISOU 1559 CD2BLEU A 198 4482 4714 5949 529 319 -56 C ATOM 1560 N ARG A 199 5.857 202.567 22.798 1.00 36.48 N ANISOU 1560 N ARG A 199 4310 4257 5292 487 345 -121 N ATOM 1561 CA ARG A 199 5.823 203.800 23.586 1.00 38.31 C ANISOU 1561 CA ARG A 199 4561 4429 5568 502 422 -165 C ATOM 1562 C ARG A 199 6.527 204.957 22.878 1.00 34.84 C ANISOU 1562 C ARG A 199 4159 3947 5132 503 387 -148 C ATOM 1563 O ARG A 199 6.099 206.117 22.989 1.00 35.37 O ANISOU 1563 O ARG A 199 4213 3939 5287 533 423 -155 O ATOM 1564 CB ARG A 199 6.452 203.557 24.956 1.00 43.70 C ANISOU 1564 CB ARG A 199 5299 5141 6164 471 500 -234 C ATOM 1565 CG ARG A 199 5.600 202.691 25.881 1.00 48.85 C ANISOU 1565 CG ARG A 199 5918 5814 6829 476 566 -255 C ATOM 1566 CD ARG A 199 6.205 202.585 27.278 1.00 52.07 C ANISOU 1566 CD ARG A 199 6393 6246 7144 449 644 -321 C ATOM 1567 N ILE A 200 7.583 204.670 22.124 1.00 31.48 N ANISOU 1567 N ILE A 200 3778 3562 4621 472 321 -122 N ATOM 1568 CA ILE A 200 8.269 205.716 21.367 1.00 32.11 C ANISOU 1568 CA ILE A 200 3895 3602 4705 470 291 -98 C ATOM 1569 C ILE A 200 7.331 206.312 20.323 1.00 34.54 C ANISOU 1569 C ILE A 200 4155 3854 5114 515 242 -32 C ATOM 1570 O ILE A 200 7.191 207.538 20.201 1.00 34.59 O ANISOU 1570 O ILE A 200 4163 3786 5192 539 260 -24 O ATOM 1571 CB ILE A 200 9.539 205.141 20.720 1.00 32.74 C ANISOU 1571 CB ILE A 200 4025 3740 4674 428 236 -80 C ATOM 1572 CG1 ILE A 200 10.606 204.859 21.763 1.00 32.47 C ANISOU 1572 CG1 ILE A 200 4039 3745 4553 385 279 -144 C ATOM 1573 CG2 ILE A 200 10.090 206.121 19.675 1.00 33.47 C ANISOU 1573 CG2 ILE A 200 4147 3790 4778 429 198 -35 C ATOM 1574 CD1 ILE A 200 11.752 204.030 21.224 1.00 31.53 C ANISOU 1574 CD1 ILE A 200 3954 3692 4335 348 230 -129 C ATOM 1575 N PHE A 201 6.676 205.450 19.544 1.00 36.11 N ANISOU 1575 N PHE A 201 4311 4087 5321 528 174 16 N ATOM 1576 CA PHE A 201 5.794 205.948 18.493 1.00 38.43 C ANISOU 1576 CA PHE A 201 4562 4336 5705 571 110 84 C ATOM 1577 C PHE A 201 4.596 206.689 19.071 1.00 37.51 C ANISOU 1577 C PHE A 201 4378 4146 5729 619 162 73 C ATOM 1578 O PHE A 201 4.150 207.687 18.492 1.00 38.01 O ANISOU 1578 O PHE A 201 4422 4141 5878 658 138 116 O ATOM 1579 CB PHE A 201 5.358 204.791 17.592 1.00 41.43 C ANISOU 1579 CB PHE A 201 4912 4771 6059 570 21 128 C ATOM 1580 CG PHE A 201 6.510 204.152 16.849 1.00 43.15 C ANISOU 1580 CG PHE A 201 5198 5051 6146 529 -30 144 C ATOM 1581 CD1 PHE A 201 7.372 204.933 16.097 1.00 44.57 C ANISOU 1581 CD1 PHE A 201 5438 5211 6284 520 -53 176 C ATOM 1582 CD2 PHE A 201 6.735 202.802 16.922 1.00 42.55 C ANISOU 1582 CD2 PHE A 201 5123 5046 5997 499 -47 126 C ATOM 1583 CE1 PHE A 201 8.456 204.371 15.411 1.00 42.85 C ANISOU 1583 CE1 PHE A 201 5282 5048 5952 483 -88 189 C ATOM 1584 CE2 PHE A 201 7.834 202.212 16.234 1.00 41.33 C ANISOU 1584 CE2 PHE A 201 5030 4945 5728 464 -87 137 C ATOM 1585 CZ PHE A 201 8.685 203.018 15.488 1.00 40.96 C ANISOU 1585 CZ PHE A 201 5042 4879 5641 456 -104 168 C ATOM 1586 N LEU A 202 4.083 206.241 20.220 1.00 36.89 N ANISOU 1586 N LEU A 202 4265 4077 5676 620 239 17 N ATOM 1587 CA LEU A 202 2.966 206.934 20.866 1.00 39.85 C ANISOU 1587 CA LEU A 202 4575 4381 6187 665 308 -2 C ATOM 1588 C LEU A 202 3.386 208.297 21.386 1.00 36.97 C ANISOU 1588 C LEU A 202 4252 3943 5852 674 377 -38 C ATOM 1589 O LEU A 202 2.626 209.269 21.276 1.00 35.87 O ANISOU 1589 O LEU A 202 4068 3722 5838 721 394 -21 O ATOM 1590 CB LEU A 202 2.413 206.087 22.008 1.00 47.99 C ANISOU 1590 CB LEU A 202 5570 5442 7223 658 387 -55 C ATOM 1591 CG LEU A 202 1.623 204.842 21.603 1.00 60.20 C ANISOU 1591 CG LEU A 202 7047 7035 8790 659 334 -22 C ATOM 1592 CD1 LEU A 202 1.431 203.910 22.800 1.00 66.49 C ANISOU 1592 CD1 LEU A 202 7837 7872 9555 636 422 -75 C ATOM 1593 CD2 LEU A 202 0.268 205.226 21.012 1.00 65.04 C ANISOU 1593 CD2 LEU A 202 7558 7591 9563 713 297 25 C ATOM 1594 N ALA A 203 4.575 208.398 21.979 1.00 36.41 N ANISOU 1594 N ALA A 203 4262 3897 5675 629 416 -89 N ATOM 1595 CA ALA A 203 5.044 209.703 22.445 1.00 39.22 C ANISOU 1595 CA ALA A 203 4662 4181 6058 630 476 -129 C ATOM 1596 C ALA A 203 5.224 210.668 21.282 1.00 41.95 C ANISOU 1596 C ALA A 203 5016 4468 6453 650 413 -62 C ATOM 1597 O ALA A 203 4.830 211.836 21.364 1.00 44.09 O ANISOU 1597 O ALA A 203 5275 4648 6829 685 450 -64 O ATOM 1598 CB ALA A 203 6.357 209.561 23.216 1.00 37.99 C ANISOU 1598 CB ALA A 203 4590 4069 5776 573 511 -195 C ATOM 1599 N ALA A 204 5.827 210.202 20.191 1.00 41.34 N ANISOU 1599 N ALA A 204 4966 4439 6301 629 322 -2 N ATOM 1600 CA ALA A 204 6.005 211.059 19.032 1.00 41.21 C ANISOU 1600 CA ALA A 204 4967 4372 6319 647 262 70 C ATOM 1601 C ALA A 204 4.658 211.539 18.508 1.00 46.28 C ANISOU 1601 C ALA A 204 5534 4950 7101 713 230 128 C ATOM 1602 O ALA A 204 4.474 212.735 18.252 1.00 42.83 O ANISOU 1602 O ALA A 204 5097 4423 6753 745 240 155 O ATOM 1603 CB ALA A 204 6.802 210.317 17.946 1.00 38.72 C ANISOU 1603 CB ALA A 204 4694 4129 5890 613 175 124 C ATOM 1604 N AARG A 205 3.695 210.626 18.379 0.50 51.44 N ANISOU 1604 N AARG A 205 6118 5643 7784 733 193 146 N ATOM 1605 N BARG A 205 3.703 210.625 18.337 0.50 51.44 N ANISOU 1605 N BARG A 205 6119 5643 7783 733 190 148 N ATOM 1606 CA AARG A 205 2.378 210.984 17.860 0.50 55.18 C ANISOU 1606 CA AARG A 205 6507 6060 8398 796 151 202 C ATOM 1607 CA BARG A 205 2.381 211.022 17.860 0.50 55.20 C ANISOU 1607 CA BARG A 205 6510 6060 8402 797 152 202 C ATOM 1608 C AARG A 205 1.665 211.972 18.782 0.50 54.59 C ANISOU 1608 C AARG A 205 6387 5892 8462 838 250 159 C ATOM 1609 C BARG A 205 1.759 212.059 18.787 0.50 54.64 C ANISOU 1609 C BARG A 205 6401 5895 8464 836 253 158 C ATOM 1610 O AARG A 205 0.955 212.867 18.310 0.50 56.03 O ANISOU 1610 O AARG A 205 6526 5993 8771 893 227 209 O ATOM 1611 O BARG A 205 1.198 213.063 18.331 0.50 56.01 O ANISOU 1611 O BARG A 205 6544 5983 8756 887 236 205 O ATOM 1612 CB AARG A 205 1.551 209.709 17.657 0.50 58.95 C ANISOU 1612 CB AARG A 205 6916 6603 8879 800 97 217 C ATOM 1613 CB BARG A 205 1.467 209.800 17.736 0.50 59.04 C ANISOU 1613 CB BARG A 205 6922 6606 8906 805 105 214 C ATOM 1614 CG AARG A 205 0.117 209.922 17.199 0.50 61.44 C ANISOU 1614 CG AARG A 205 7126 6868 9349 862 47 269 C ATOM 1615 CG BARG A 205 0.136 210.091 17.046 0.50 61.47 C ANISOU 1615 CG BARG A 205 7134 6862 9358 867 37 280 C ATOM 1616 CD AARG A 205 -0.455 208.658 16.555 0.50 61.15 C ANISOU 1616 CD AARG A 205 7040 6903 9293 855 -48 303 C ATOM 1617 CD BARG A 205 -0.814 208.901 17.092 0.50 62.14 C ANISOU 1617 CD BARG A 205 7133 6999 9479 870 4 279 C ATOM 1618 NE AARG A 205 -0.203 208.625 15.116 0.50 56.03 N ANISOU 1618 NE AARG A 205 6427 6274 8586 855 -180 384 N ATOM 1619 NE BARG A 205 -1.497 208.782 18.377 0.50 60.60 N ANISOU 1619 NE BARG A 205 6875 6783 9369 882 121 211 N ATOM 1620 CZ AARG A 205 -0.958 209.236 14.210 0.50 50.96 C ANISOU 1620 CZ AARG A 205 5743 5582 8038 906 -268 460 C ATOM 1621 CZ BARG A 205 -2.334 207.799 18.689 0.50 58.83 C ANISOU 1621 CZ BARG A 205 6570 6591 9189 881 127 197 C ATOM 1622 NH1AARG A 205 -2.023 209.934 14.580 0.50 48.52 N ANISOU 1622 NH1AARG A 205 5343 5194 7898 962 -239 466 N ATOM 1623 NH1BARG A 205 -2.598 206.839 17.808 0.50 57.77 N ANISOU 1623 NH1BARG A 205 6408 6514 9027 869 14 242 N ATOM 1624 NH2AARG A 205 -0.647 209.154 12.926 0.50 50.07 N ANISOU 1624 NH2AARG A 205 5681 5495 7849 901 -386 531 N ATOM 1625 NH2BARG A 205 -2.906 207.772 19.882 0.50 58.84 N ANISOU 1625 NH2BARG A 205 6523 6569 9264 891 248 137 N ATOM 1626 N ARG A 206 1.854 211.836 20.099 1.00 54.19 N ANISOU 1626 N ARG A 206 6350 5851 8389 816 360 67 N ATOM 1627 CA ARG A 206 1.240 212.763 21.045 1.00 57.79 C ANISOU 1627 CA ARG A 206 6775 6219 8966 852 468 14 C ATOM 1628 C ARG A 206 1.912 214.129 21.000 1.00 49.60 C ANISOU 1628 C ARG A 206 5797 5097 7950 854 497 7 C ATOM 1629 O ARG A 206 1.246 215.169 21.148 1.00 49.45 O ANISOU 1629 O ARG A 206 5741 4977 8071 905 541 7 O ATOM 1630 CB ARG A 206 1.309 212.194 22.462 1.00 78.62 C ANISOU 1630 CB ARG A 206 9426 8895 11551 823 577 -83 C ATOM 1631 CG ARG A 206 0.610 213.043 23.513 1.00110.01 C ANISOU 1631 CG ARG A 206 13371 12784 15642 860 702 -148 C ATOM 1632 CD ARG A 206 -0.902 213.053 23.307 1.00140.24 C ANISOU 1632 CD ARG A 206 17079 16567 19640 925 705 -110 C ATOM 1633 NE ARG A 206 -1.565 214.114 24.060 1.00165.47 N ANISOU 1633 NE ARG A 206 20243 19657 22973 971 817 -158 N ATOM 1634 CZ ARG A 206 -2.784 214.572 23.792 1.00185.57 C ANISOU 1634 CZ ARG A 206 22683 22127 25697 1039 822 -121 C ATOM 1635 NH1 ARG A 206 -3.307 215.540 24.531 1.00194.36 N ANISOU 1635 NH1 ARG A 206 23773 23142 26932 1080 936 -173 N ATOM 1636 NH2 ARG A 206 -3.482 214.070 22.781 1.00191.08 N ANISOU 1636 NH2 ARG A 206 23298 22845 26458 1066 711 -33 N ATOM 1637 N GLN A 207 3.229 214.157 20.822 1.00 45.43 N ANISOU 1637 N GLN A 207 5359 4604 7296 800 477 -2 N ATOM 1638 CA GLN A 207 3.916 215.447 20.751 1.00 44.40 C ANISOU 1638 CA GLN A 207 5287 4392 7193 795 504 -8 C ATOM 1639 C GLN A 207 3.582 216.188 19.460 1.00 44.82 C ANISOU 1639 C GLN A 207 5322 4380 7330 839 424 98 C ATOM 1640 O GLN A 207 3.431 217.419 19.464 1.00 44.12 O ANISOU 1640 O GLN A 207 5234 4183 7345 871 459 104 O ATOM 1641 CB GLN A 207 5.423 215.235 20.892 1.00 45.14 C ANISOU 1641 CB GLN A 207 5473 4542 7139 723 502 -45 C ATOM 1642 CG GLN A 207 5.797 214.728 22.274 1.00 48.11 C ANISOU 1642 CG GLN A 207 5875 4965 7438 683 584 -152 C ATOM 1643 CD GLN A 207 7.293 214.511 22.463 1.00 50.48 C ANISOU 1643 CD GLN A 207 6257 5320 7602 612 576 -190 C ATOM 1644 OE1 GLN A 207 8.116 215.153 21.813 1.00 51.23 O ANISOU 1644 OE1 GLN A 207 6394 5385 7685 591 545 -159 O ATOM 1645 NE2 GLN A 207 7.647 213.606 23.370 1.00 50.72 N ANISOU 1645 NE2 GLN A 207 6308 5429 7533 575 605 -255 N ATOM 1646 N LEU A 208 3.474 215.467 18.342 1.00 47.18 N ANISOU 1646 N LEU A 208 5607 4738 7580 841 314 182 N ATOM 1647 CA LEU A 208 3.107 216.111 17.082 1.00 49.87 C ANISOU 1647 CA LEU A 208 5937 5023 7987 885 228 289 C ATOM 1648 C LEU A 208 1.703 216.707 17.154 1.00 51.57 C ANISOU 1648 C LEU A 208 6057 5152 8383 962 236 315 C ATOM 1649 O LEU A 208 1.469 217.827 16.683 1.00 53.47 O ANISOU 1649 O LEU A 208 6296 5295 8726 1005 225 368 O ATOM 1650 CB LEU A 208 3.209 215.102 15.938 1.00 49.59 C ANISOU 1650 CB LEU A 208 5911 5079 7853 870 109 364 C ATOM 1651 CG LEU A 208 4.643 214.786 15.483 1.00 53.12 C ANISOU 1651 CG LEU A 208 6455 5588 8140 804 88 369 C ATOM 1652 CD1 LEU A 208 4.724 213.469 14.725 1.00 56.78 C ANISOU 1652 CD1 LEU A 208 6924 6160 8492 781 -2 404 C ATOM 1653 CD2 LEU A 208 5.162 215.938 14.613 1.00 53.86 C ANISOU 1653 CD2 LEU A 208 6606 5606 8252 812 65 441 C ATOM 1654 N ALA A1001 0.763 215.977 17.760 1.00 48.77 N ANISOU 1654 N ALA A1001 5622 4829 8079 982 260 277 N ATOM 1655 CA ALA A1001 -0.613 216.449 17.878 1.00 47.92 C ANISOU 1655 CA ALA A1001 5409 4643 8155 1056 274 297 C ATOM 1656 C ALA A1001 -0.690 217.675 18.772 1.00 50.36 C ANISOU 1656 C ALA A1001 5721 4840 8573 1081 395 236 C ATOM 1657 O ALA A1001 -1.466 218.600 18.512 1.00 53.30 O ANISOU 1657 O ALA A1001 6038 5109 9103 1147 394 279 O ATOM 1658 CB ALA A1001 -1.500 215.323 18.426 1.00 46.42 C ANISOU 1658 CB ALA A1001 5134 4516 7989 1060 290 261 C ATOM 1659 N ASP A1002 0.111 217.703 19.833 1.00 50.22 N ANISOU 1659 N ASP A1002 5770 4837 8475 1032 498 135 N ATOM 1660 CA ASP A1002 0.130 218.868 20.700 1.00 53.58 C ANISOU 1660 CA ASP A1002 6212 5157 8990 1049 614 66 C ATOM 1661 C ASP A1002 0.670 220.083 19.955 1.00 56.03 C ANISOU 1661 C ASP A1002 6572 5375 9340 1060 582 123 C ATOM 1662 O ASP A1002 0.069 221.160 19.989 1.00 57.72 O ANISOU 1662 O ASP A1002 6751 5471 9709 1117 620 135 O ATOM 1663 CB ASP A1002 0.965 218.575 21.940 1.00 58.04 C ANISOU 1663 CB ASP A1002 6848 5768 9438 985 713 -53 C ATOM 1664 CG ASP A1002 0.277 217.622 22.879 1.00 70.18 C ANISOU 1664 CG ASP A1002 8334 7364 10966 986 777 -116 C ATOM 1665 OD1 ASP A1002 -0.809 217.132 22.516 1.00 76.35 O ANISOU 1665 OD1 ASP A1002 9021 8155 11834 1030 741 -65 O ATOM 1666 OD2 ASP A1002 0.818 217.357 23.973 1.00 75.44 O ANISOU 1666 OD2 ASP A1002 9057 8067 11541 941 862 -212 O ATOM 1667 N LEU A1003 1.794 219.920 19.259 1.00 57.49 N ANISOU 1667 N LEU A1003 6839 5611 9394 1007 516 162 N ATOM 1668 CA LEU A1003 2.308 220.986 18.408 1.00 60.74 C ANISOU 1668 CA LEU A1003 7299 5941 9837 1015 479 233 C ATOM 1669 C LEU A1003 1.207 221.549 17.524 1.00 54.72 C ANISOU 1669 C LEU A1003 6466 5101 9225 1097 412 338 C ATOM 1670 O LEU A1003 1.005 222.766 17.453 1.00 53.42 O ANISOU 1670 O LEU A1003 6299 4812 9186 1138 444 360 O ATOM 1671 CB LEU A1003 3.453 220.446 17.543 1.00 73.43 C ANISOU 1671 CB LEU A1003 8984 7634 11281 954 398 283 C ATOM 1672 CG LEU A1003 4.905 220.882 17.767 1.00 87.15 C ANISOU 1672 CG LEU A1003 10820 9367 12928 885 442 238 C ATOM 1673 CD1 LEU A1003 5.211 221.301 19.203 1.00 93.93 C ANISOU 1673 CD1 LEU A1003 11697 10189 13805 858 563 106 C ATOM 1674 CD2 LEU A1003 5.833 219.744 17.346 1.00 89.93 C ANISOU 1674 CD2 LEU A1003 11218 9848 13102 821 383 249 C ATOM 1675 N GLU A1004 0.496 220.665 16.825 1.00 54.06 N ANISOU 1675 N GLU A1004 6324 5086 9131 1122 313 406 N ATOM 1676 CA GLU A1004 -0.550 221.093 15.904 1.00 60.67 C ANISOU 1676 CA GLU A1004 7090 5861 10101 1199 226 515 C ATOM 1677 C GLU A1004 -1.681 221.777 16.648 1.00 59.60 C ANISOU 1677 C GLU A1004 6859 5621 10165 1269 306 479 C ATOM 1678 O GLU A1004 -2.251 222.766 16.165 1.00 60.67 O ANISOU 1678 O GLU A1004 6960 5647 10446 1334 282 548 O ATOM 1679 CB GLU A1004 -1.060 219.880 15.116 1.00 69.31 C ANISOU 1679 CB GLU A1004 8140 7060 11134 1201 102 576 C ATOM 1680 CG GLU A1004 -2.225 220.150 14.169 1.00 80.38 C ANISOU 1680 CG GLU A1004 9459 8414 12668 1280 -8 687 C ATOM 1681 CD GLU A1004 -1.894 221.163 13.079 1.00 87.04 C ANISOU 1681 CD GLU A1004 10362 9183 13526 1305 -79 797 C ATOM 1682 OE1 GLU A1004 -2.698 222.098 12.880 1.00 88.78 O ANISOU 1682 OE1 GLU A1004 10526 9293 13915 1379 -91 852 O ATOM 1683 OE2 GLU A1004 -0.835 221.029 12.425 1.00 88.62 O ANISOU 1683 OE2 GLU A1004 10667 9432 13574 1253 -119 832 O ATOM 1684 N ASP A1005 -2.014 221.278 17.836 1.00 57.62 N ANISOU 1684 N ASP A1005 6567 5398 9927 1257 406 372 N ATOM 1685 CA ASP A1005 -3.098 221.890 18.586 1.00 59.94 C ANISOU 1685 CA ASP A1005 6769 5593 10410 1323 498 330 C ATOM 1686 C ASP A1005 -2.752 223.322 18.964 1.00 59.61 C ANISOU 1686 C ASP A1005 6774 5418 10457 1341 587 299 C ATOM 1687 O ASP A1005 -3.578 224.229 18.816 1.00 61.75 O ANISOU 1687 O ASP A1005 6980 5572 10912 1416 600 337 O ATOM 1688 CB ASP A1005 -3.412 221.059 19.825 1.00 65.92 C ANISOU 1688 CB ASP A1005 7492 6412 11142 1299 602 218 C ATOM 1689 CG ASP A1005 -4.294 219.858 19.520 1.00 77.76 C ANISOU 1689 CG ASP A1005 8897 7997 12651 1313 530 255 C ATOM 1690 OD1 ASP A1005 -5.052 219.891 18.523 1.00 82.73 O ANISOU 1690 OD1 ASP A1005 9453 8608 13374 1365 417 357 O ATOM 1691 OD2 ASP A1005 -4.234 218.876 20.289 1.00 82.76 O ANISOU 1691 OD2 ASP A1005 9529 8716 13199 1270 584 182 O ATOM 1692 N ASN A1006 -1.526 223.556 19.431 1.00 58.19 N ANISOU 1692 N ASN A1006 6704 5250 10156 1272 646 230 N ATOM 1693 CA ASN A1006 -1.145 224.918 19.776 1.00 58.93 C ANISOU 1693 CA ASN A1006 6845 5213 10333 1282 728 195 C ATOM 1694 C ASN A1006 -1.185 225.825 18.553 1.00 55.81 C ANISOU 1694 C ASN A1006 6456 4728 10022 1326 640 325 C ATOM 1695 O ASN A1006 -1.620 226.975 18.645 1.00 54.99 O ANISOU 1695 O ASN A1006 6328 4485 10081 1382 689 333 O ATOM 1696 CB ASN A1006 0.240 224.925 20.413 1.00 62.48 C ANISOU 1696 CB ASN A1006 7409 5700 10630 1193 788 103 C ATOM 1697 CG ASN A1006 0.211 224.461 21.847 1.00 66.79 C ANISOU 1697 CG ASN A1006 7959 6287 11131 1162 906 -38 C ATOM 1698 OD1 ASN A1006 -0.783 224.658 22.548 1.00 68.31 O ANISOU 1698 OD1 ASN A1006 8082 6426 11448 1214 989 -87 O ATOM 1699 ND2 ASN A1006 1.304 223.861 22.302 1.00 68.92 N ANISOU 1699 ND2 ASN A1006 8310 6651 11226 1080 916 -104 N ATOM 1700 N TRP A1007 -0.742 225.315 17.402 1.00 55.70 N ANISOU 1700 N TRP A1007 6478 4790 9897 1303 512 427 N ATOM 1701 CA TRP A1007 -0.679 226.121 16.189 1.00 62.80 C ANISOU 1701 CA TRP A1007 7401 5614 10848 1338 423 558 C ATOM 1702 C TRP A1007 -2.059 226.607 15.777 1.00 70.35 C ANISOU 1702 C TRP A1007 8249 6481 12001 1441 379 637 C ATOM 1703 O TRP A1007 -2.262 227.801 15.518 1.00 74.65 O ANISOU 1703 O TRP A1007 8802 6927 12635 1470 387 677 O ATOM 1704 CB TRP A1007 -0.040 225.304 15.066 1.00 61.57 C ANISOU 1704 CB TRP A1007 7301 5572 10519 1294 297 646 C ATOM 1705 CG TRP A1007 -0.068 225.970 13.728 1.00 63.15 C ANISOU 1705 CG TRP A1007 7529 5713 10752 1332 194 793 C ATOM 1706 CD1 TRP A1007 -0.793 225.586 12.644 1.00 65.18 C ANISOU 1706 CD1 TRP A1007 7745 6002 11018 1379 57 911 C ATOM 1707 CD2 TRP A1007 0.667 227.134 13.327 1.00 63.62 C ANISOU 1707 CD2 TRP A1007 7669 5669 10836 1325 217 841 C ATOM 1708 NE1 TRP A1007 -0.559 226.439 11.592 1.00 65.72 N ANISOU 1708 NE1 TRP A1007 7869 5997 11106 1404 -8 1033 N ATOM 1709 CE2 TRP A1007 0.336 227.395 11.988 1.00 64.69 C ANISOU 1709 CE2 TRP A1007 7812 5779 10987 1371 93 994 C ATOM 1710 CE3 TRP A1007 1.568 227.982 13.975 1.00 66.09 C ANISOU 1710 CE3 TRP A1007 8048 5904 11158 1282 328 768 C ATOM 1711 CZ2 TRP A1007 0.873 228.466 11.285 1.00 67.32 C ANISOU 1711 CZ2 TRP A1007 8219 6013 11346 1377 85 1083 C ATOM 1712 CZ3 TRP A1007 2.105 229.033 13.277 1.00 68.76 C ANISOU 1712 CZ3 TRP A1007 8453 6142 11530 1285 320 850 C ATOM 1713 CH2 TRP A1007 1.758 229.269 11.944 1.00 69.57 C ANISOU 1713 CH2 TRP A1007 8563 6221 11648 1332 203 1009 C ATOM 1714 N GLU A1008 -3.026 225.693 15.692 1.00 69.52 N ANISOU 1714 N GLU A1008 8048 6448 11918 1471 321 653 N ATOM 1715 CA GLU A1008 -4.353 226.108 15.265 1.00 75.96 C ANISOU 1715 CA GLU A1008 8770 7241 12851 1531 261 715 C ATOM 1716 C GLU A1008 -5.106 226.838 16.368 1.00 65.77 C ANISOU 1716 C GLU A1008 7420 5883 11687 1553 391 620 C ATOM 1717 O GLU A1008 -6.036 227.597 16.064 1.00 57.56 O ANISOU 1717 O GLU A1008 6319 4786 10765 1604 365 669 O ATOM 1718 CB GLU A1008 -5.156 224.906 14.756 1.00100.32 C ANISOU 1718 CB GLU A1008 11772 10430 15917 1547 148 763 C ATOM 1719 CG GLU A1008 -5.498 223.870 15.794 1.00117.27 C ANISOU 1719 CG GLU A1008 13856 12646 18057 1527 226 657 C ATOM 1720 CD GLU A1008 -6.094 222.615 15.176 1.00123.21 C ANISOU 1720 CD GLU A1008 14539 13502 18772 1531 103 709 C ATOM 1721 OE1 GLU A1008 -7.112 222.117 15.702 1.00123.96 O ANISOU 1721 OE1 GLU A1008 14531 13629 18939 1544 131 665 O ATOM 1722 OE2 GLU A1008 -5.549 222.135 14.157 1.00123.58 O ANISOU 1722 OE2 GLU A1008 14638 13599 18719 1518 -19 793 O ATOM 1723 N THR A1009 -4.710 226.662 17.631 1.00 67.17 N ANISOU 1723 N THR A1009 7619 6064 11840 1516 530 487 N ATOM 1724 CA THR A1009 -5.267 227.492 18.694 1.00 66.08 C ANISOU 1724 CA THR A1009 7448 5853 11805 1530 663 393 C ATOM 1725 C THR A1009 -4.882 228.957 18.500 1.00 63.92 C ANISOU 1725 C THR A1009 7234 5462 11591 1540 691 413 C ATOM 1726 O THR A1009 -5.715 229.860 18.672 1.00 59.36 O ANISOU 1726 O THR A1009 6603 4809 11141 1582 726 414 O ATOM 1727 CB THR A1009 -4.801 226.968 20.053 1.00 63.04 C ANISOU 1727 CB THR A1009 7096 5505 11351 1481 800 246 C ATOM 1728 OG1 THR A1009 -5.512 225.765 20.348 1.00 65.55 O ANISOU 1728 OG1 THR A1009 7335 5917 11655 1485 793 226 O ATOM 1729 CG2 THR A1009 -5.067 227.955 21.159 1.00 59.92 C ANISOU 1729 CG2 THR A1009 6706 5029 11032 1483 944 142 C ATOM 1730 N LEU A1010 -3.623 229.210 18.142 1.00 67.08 N ANISOU 1730 N LEU A1010 7742 5841 11904 1499 677 430 N ATOM 1731 CA LEU A1010 -3.214 230.560 17.789 1.00 70.79 C ANISOU 1731 CA LEU A1010 8270 6200 12426 1504 688 467 C ATOM 1732 C LEU A1010 -4.057 231.087 16.641 1.00 66.92 C ANISOU 1732 C LEU A1010 7728 5675 12023 1568 573 607 C ATOM 1733 O LEU A1010 -4.657 232.159 16.736 1.00 70.77 O ANISOU 1733 O LEU A1010 8185 6072 12632 1606 608 613 O ATOM 1734 CB LEU A1010 -1.731 230.590 17.405 1.00 77.59 C ANISOU 1734 CB LEU A1010 9250 7057 13175 1446 674 483 C ATOM 1735 CG LEU A1010 -0.665 230.395 18.486 1.00 83.92 C ANISOU 1735 CG LEU A1010 10126 7867 13895 1376 788 345 C ATOM 1736 CD1 LEU A1010 0.707 230.659 17.883 1.00 88.23 C ANISOU 1736 CD1 LEU A1010 10779 8386 14360 1324 761 387 C ATOM 1737 CD2 LEU A1010 -0.899 231.302 19.695 1.00 85.57 C ANISOU 1737 CD2 LEU A1010 10333 8001 14180 1371 924 219 C ATOM 1738 N ASN A1011 -4.112 230.338 15.541 1.00 63.36 N ANISOU 1738 N ASN A1011 7271 5296 11507 1579 433 719 N ATOM 1739 CA ASN A1011 -4.770 230.851 14.348 1.00 73.38 C ANISOU 1739 CA ASN A1011 8513 6536 12833 1633 311 858 C ATOM 1740 C ASN A1011 -6.271 231.003 14.558 1.00 70.73 C ANISOU 1740 C ASN A1011 8051 6188 12637 1693 305 857 C ATOM 1741 O ASN A1011 -6.852 232.025 14.174 1.00 69.49 O ANISOU 1741 O ASN A1011 7869 5948 12588 1741 285 915 O ATOM 1742 CB ASN A1011 -4.472 229.940 13.166 1.00 91.41 C ANISOU 1742 CB ASN A1011 10827 8909 14996 1625 162 968 C ATOM 1743 CG ASN A1011 -3.017 229.969 12.774 1.00110.80 C ANISOU 1743 CG ASN A1011 13410 11361 17328 1570 161 994 C ATOM 1744 OD1 ASN A1011 -2.295 230.913 13.096 1.00117.08 O ANISOU 1744 OD1 ASN A1011 14272 12069 18143 1546 247 962 O ATOM 1745 ND2 ASN A1011 -2.572 228.935 12.077 1.00119.56 N ANISOU 1745 ND2 ASN A1011 14552 12565 18310 1546 67 1051 N ATOM 1746 N ASP A1012 -6.920 230.007 15.163 1.00 69.97 N ANISOU 1746 N ASP A1012 7870 6168 12545 1692 326 793 N ATOM 1747 CA ASP A1012 -8.359 230.119 15.387 1.00 72.36 C ANISOU 1747 CA ASP A1012 8047 6459 12988 1744 327 791 C ATOM 1748 C ASP A1012 -8.693 231.366 16.196 1.00 71.44 C ANISOU 1748 C ASP A1012 7915 6228 13003 1766 456 725 C ATOM 1749 O ASP A1012 -9.579 232.146 15.823 1.00 73.05 O ANISOU 1749 O ASP A1012 8056 6366 13333 1822 424 784 O ATOM 1750 CB ASP A1012 -8.886 228.872 16.087 1.00 76.57 C ANISOU 1750 CB ASP A1012 8503 7088 13504 1726 359 716 C ATOM 1751 CG ASP A1012 -8.829 227.645 15.202 1.00 80.89 C ANISOU 1751 CG ASP A1012 9041 7746 13948 1714 216 789 C ATOM 1752 OD1 ASP A1012 -8.697 227.809 13.970 1.00 80.77 O ANISOU 1752 OD1 ASP A1012 9059 7733 13896 1731 79 908 O ATOM 1753 OD2 ASP A1012 -8.918 226.522 15.737 1.00 83.87 O ANISOU 1753 OD2 ASP A1012 9383 8207 14278 1685 242 727 O ATOM 1754 N ASN A1013 -8.002 231.564 17.322 1.00 70.21 N ANISOU 1754 N ASN A1013 7815 6046 12815 1723 601 601 N ATOM 1755 CA ASN A1013 -8.334 232.682 18.198 1.00 71.06 C ANISOU 1755 CA ASN A1013 7910 6051 13039 1739 732 524 C ATOM 1756 C ASN A1013 -8.045 234.021 17.536 1.00 71.15 C ANISOU 1756 C ASN A1013 7972 5950 13110 1764 704 597 C ATOM 1757 O ASN A1013 -8.701 235.025 17.848 1.00 69.29 O ANISOU 1757 O ASN A1013 7695 5623 13011 1803 763 582 O ATOM 1758 CB ASN A1013 -7.583 232.556 19.518 1.00 69.75 C ANISOU 1758 CB ASN A1013 7808 5890 12803 1681 883 372 C ATOM 1759 CG ASN A1013 -8.256 231.601 20.459 1.00 70.10 C ANISOU 1759 CG ASN A1013 7781 6010 12843 1672 954 284 C ATOM 1760 OD1 ASN A1013 -9.309 231.919 21.009 1.00 69.57 O ANISOU 1760 OD1 ASN A1013 7631 5908 12895 1706 1021 250 O ATOM 1761 ND2 ASN A1013 -7.672 230.418 20.641 1.00 71.42 N ANISOU 1761 ND2 ASN A1013 7981 6278 12878 1627 943 251 N ATOM 1762 N LEU A1014 -7.083 234.055 16.617 1.00 73.01 N ANISOU 1762 N LEU A1014 8298 6192 13250 1742 617 679 N ATOM 1763 CA LEU A1014 -6.877 235.254 15.818 1.00 77.12 C ANISOU 1763 CA LEU A1014 8866 6614 13824 1768 574 772 C ATOM 1764 C LEU A1014 -8.132 235.598 15.026 1.00 76.90 C ANISOU 1764 C LEU A1014 8745 6561 13915 1844 476 880 C ATOM 1765 O LEU A1014 -8.569 236.757 14.998 1.00 72.63 O ANISOU 1765 O LEU A1014 8185 5913 13498 1886 504 902 O ATOM 1766 CB LEU A1014 -5.683 235.054 14.885 1.00 80.84 C ANISOU 1766 CB LEU A1014 9447 7110 14158 1729 491 853 C ATOM 1767 CG LEU A1014 -4.398 235.786 15.258 1.00 83.44 C ANISOU 1767 CG LEU A1014 9890 7370 14444 1672 581 798 C ATOM 1768 CD1 LEU A1014 -3.256 235.290 14.396 1.00 83.92 C ANISOU 1768 CD1 LEU A1014 10048 7480 14359 1626 503 872 C ATOM 1769 CD2 LEU A1014 -4.576 237.284 15.094 1.00 85.77 C ANISOU 1769 CD2 LEU A1014 10198 7530 14861 1705 612 832 C ATOM 1770 N LYS A1015 -8.732 234.595 14.382 1.00 80.24 N ANISOU 1770 N LYS A1015 9107 7079 14302 1863 357 947 N ATOM 1771 CA LYS A1015 -9.950 234.835 13.618 1.00 82.81 C ANISOU 1771 CA LYS A1015 9339 7390 14736 1932 252 1047 C ATOM 1772 C LYS A1015 -11.075 235.325 14.523 1.00 80.48 C ANISOU 1772 C LYS A1015 8932 7035 14612 1972 352 974 C ATOM 1773 O LYS A1015 -11.831 236.230 14.149 1.00 85.59 O ANISOU 1773 O LYS A1015 9529 7601 15390 2030 324 1035 O ATOM 1774 CB LYS A1015 -10.360 233.563 12.877 1.00 84.04 C ANISOU 1774 CB LYS A1015 9450 7669 14815 1934 111 1112 C ATOM 1775 CG LYS A1015 -9.530 233.272 11.628 1.00 85.03 C ANISOU 1775 CG LYS A1015 9675 7840 14792 1916 -24 1225 C ATOM 1776 N VAL A1016 -11.194 234.749 15.721 1.00 73.87 N ANISOU 1776 N VAL A1016 8058 6236 13774 1941 472 845 N ATOM 1777 CA VAL A1016 -12.208 235.196 16.676 1.00 75.06 C ANISOU 1777 CA VAL A1016 8112 6331 14078 1971 587 766 C ATOM 1778 C VAL A1016 -12.068 236.693 16.935 1.00 75.46 C ANISOU 1778 C VAL A1016 8199 6244 14230 1994 671 750 C ATOM 1779 O VAL A1016 -13.049 237.449 16.880 1.00 74.41 O ANISOU 1779 O VAL A1016 7984 6034 14254 2052 677 780 O ATOM 1780 CB VAL A1016 -12.096 234.381 17.980 1.00 78.22 C ANISOU 1780 CB VAL A1016 8502 6791 14427 1922 720 623 C ATOM 1781 CG1 VAL A1016 -12.724 235.126 19.151 1.00 78.44 C ANISOU 1781 CG1 VAL A1016 8481 6737 14583 1938 881 519 C ATOM 1782 CG2 VAL A1016 -12.760 233.019 17.808 1.00 83.26 C ANISOU 1782 CG2 VAL A1016 9055 7546 15036 1920 648 640 C ATOM 1783 N ILE A1017 -10.844 237.138 17.239 1.00 76.21 N ANISOU 1783 N ILE A1017 8414 6302 14240 1946 738 701 N ATOM 1784 CA ILE A1017 -10.592 238.559 17.466 1.00 73.89 C ANISOU 1784 CA ILE A1017 8165 5876 14033 1959 815 683 C ATOM 1785 C ILE A1017 -10.974 239.373 16.237 1.00 70.87 C ANISOU 1785 C ILE A1017 7771 5425 13732 2019 696 832 C ATOM 1786 O ILE A1017 -11.529 240.466 16.351 1.00 68.23 O ANISOU 1786 O ILE A1017 7400 4982 13541 2065 740 839 O ATOM 1787 CB ILE A1017 -9.115 238.785 17.842 1.00 70.57 C ANISOU 1787 CB ILE A1017 7881 5439 13493 1889 883 615 C ATOM 1788 CG1 ILE A1017 -8.792 238.147 19.195 1.00 66.31 C ANISOU 1788 CG1 ILE A1017 7357 4952 12884 1833 1015 456 C ATOM 1789 CG2 ILE A1017 -8.784 240.281 17.866 1.00 72.40 C ANISOU 1789 CG2 ILE A1017 8166 5531 13811 1900 941 616 C ATOM 1790 CD1 ILE A1017 -7.296 237.974 19.437 1.00 63.48 C ANISOU 1790 CD1 ILE A1017 7127 4616 12376 1756 1047 398 C ATOM 1791 N GLU A1018 -10.652 238.868 15.046 1.00 72.24 N ANISOU 1791 N GLU A1018 7981 5660 13808 2020 545 952 N ATOM 1792 CA GLU A1018 -10.915 239.622 13.828 1.00 79.64 C ANISOU 1792 CA GLU A1018 8926 6538 14797 2073 426 1099 C ATOM 1793 C GLU A1018 -12.411 239.758 13.557 1.00 87.53 C ANISOU 1793 C GLU A1018 9789 7519 15947 2149 368 1154 C ATOM 1794 O GLU A1018 -12.842 240.745 12.952 1.00 86.92 O ANISOU 1794 O GLU A1018 9699 7352 15974 2205 322 1241 O ATOM 1795 CB GLU A1018 -10.202 238.961 12.650 1.00 82.80 C ANISOU 1795 CB GLU A1018 9405 7017 15037 2050 282 1209 C ATOM 1796 CG GLU A1018 -8.681 239.050 12.747 1.00 87.60 C ANISOU 1796 CG GLU A1018 10151 7619 15512 1980 334 1178 C ATOM 1797 CD GLU A1018 -7.961 238.415 11.566 1.00 92.12 C ANISOU 1797 CD GLU A1018 10808 8267 15926 1956 199 1290 C ATOM 1798 OE1 GLU A1018 -6.758 238.692 11.386 1.00 95.12 O ANISOU 1798 OE1 GLU A1018 11303 8623 16215 1906 225 1297 O ATOM 1799 OE2 GLU A1018 -8.592 237.633 10.825 1.00 92.15 O ANISOU 1799 OE2 GLU A1018 10762 8355 15894 1984 71 1367 O ATOM 1800 N LYS A1019 -13.219 238.800 14.009 1.00 95.33 N ANISOU 1800 N LYS A1019 10675 8589 16958 2152 371 1105 N ATOM 1801 CA LYS A1019 -14.660 238.845 13.803 1.00101.06 C ANISOU 1801 CA LYS A1019 11262 9303 17834 2217 319 1149 C ATOM 1802 C LYS A1019 -15.422 239.340 15.027 1.00 96.17 C ANISOU 1802 C LYS A1019 10554 8613 17372 2235 478 1038 C ATOM 1803 O LYS A1019 -16.656 239.341 15.008 1.00102.74 O ANISOU 1803 O LYS A1019 11261 9434 18344 2285 455 1060 O ATOM 1804 CB LYS A1019 -15.179 237.456 13.413 1.00104.12 C ANISOU 1804 CB LYS A1019 11581 9823 18158 2209 209 1178 C ATOM 1805 N ALA A1020 -14.730 239.768 16.079 1.00 85.98 N ANISOU 1805 N ALA A1020 9329 7276 16064 2194 636 918 N ATOM 1806 CA ALA A1020 -15.404 240.078 17.328 1.00 86.81 C ANISOU 1806 CA ALA A1020 9361 7331 16291 2202 796 799 C ATOM 1807 C ALA A1020 -16.015 241.479 17.295 1.00 89.64 C ANISOU 1807 C ALA A1020 9679 7547 16831 2264 835 827 C ATOM 1808 O ALA A1020 -15.679 242.330 16.462 1.00 80.17 O ANISOU 1808 O ALA A1020 8533 6277 15649 2291 763 921 O ATOM 1809 CB ALA A1020 -14.440 239.968 18.505 1.00 92.93 C ANISOU 1809 CB ALA A1020 10227 8115 16967 2132 949 652 C ATOM 1810 N ASP A1021 -16.925 241.715 18.238 1.00103.01 N ANISOU 1810 N ASP A1021 11279 9197 18662 2287 955 743 N ATOM 1811 CA ASP A1021 -17.540 243.025 18.394 1.00109.33 C ANISOU 1811 CA ASP A1021 12035 9859 19646 2344 1017 750 C ATOM 1812 C ASP A1021 -17.679 243.388 19.867 1.00107.01 C ANISOU 1812 C ASP A1021 11733 9514 19413 2324 1221 592 C ATOM 1813 O ASP A1021 -18.549 244.187 20.231 1.00112.47 O ANISOU 1813 O ASP A1021 12346 10109 20279 2373 1294 575 O ATOM 1814 CB ASP A1021 -18.904 243.069 17.701 1.00111.50 C ANISOU 1814 CB ASP A1021 12168 10118 20078 2420 916 853 C ATOM 1815 N ASN A1022 -16.829 242.824 20.723 1.00 98.93 N ANISOU 1815 N ASN A1022 10793 8551 18244 2251 1315 476 N ATOM 1816 CA ASN A1022 -16.923 243.053 22.157 1.00 95.44 C ANISOU 1816 CA ASN A1022 10357 8075 17831 2225 1506 321 C ATOM 1817 C ASN A1022 -15.552 242.895 22.803 1.00 89.98 C ANISOU 1817 C ASN A1022 9811 7416 16964 2146 1579 218 C ATOM 1818 O ASN A1022 -14.755 242.032 22.412 1.00 87.36 O ANISOU 1818 O ASN A1022 9541 7181 16471 2101 1500 242 O ATOM 1819 CB ASN A1022 -17.914 242.087 22.815 1.00 94.32 C ANISOU 1819 CB ASN A1022 10106 8007 17723 2226 1561 269 C ATOM 1820 CG ASN A1022 -17.684 241.953 24.304 1.00 95.31 C ANISOU 1820 CG ASN A1022 10277 8140 17794 2176 1748 102 C ATOM 1821 OD1 ASN A1022 -16.981 241.051 24.755 1.00 96.87 O ANISOU 1821 OD1 ASN A1022 10544 8436 17827 2113 1771 38 O ATOM 1822 ND2 ASN A1022 -18.262 242.862 25.075 1.00 95.79 N ANISOU 1822 ND2 ASN A1022 10306 8099 17992 2203 1883 32 N ATOM 1823 N ALA A1023 -15.314 243.712 23.836 1.00 88.31 N ANISOU 1823 N ALA A1023 9648 7122 16783 2128 1734 99 N ATOM 1824 CA ALA A1023 -14.005 243.760 24.481 1.00 89.17 C ANISOU 1824 CA ALA A1023 9898 7243 16741 2053 1805 -5 C ATOM 1825 C ALA A1023 -13.643 242.421 25.115 1.00 93.20 C ANISOU 1825 C ALA A1023 10437 7889 17087 1992 1833 -83 C ATOM 1826 O ALA A1023 -12.488 241.984 25.037 1.00 91.14 O ANISOU 1826 O ALA A1023 10279 7686 16665 1933 1800 -102 O ATOM 1827 CB ALA A1023 -13.980 244.871 25.531 1.00 91.41 C ANISOU 1827 CB ALA A1023 10219 7414 17100 2048 1966 -126 C ATOM 1828 N ALA A1024 -14.607 241.753 25.747 1.00 97.79 N ANISOU 1828 N ALA A1024 10929 8520 17708 2004 1895 -128 N ATOM 1829 CA ALA A1024 -14.317 240.497 26.422 1.00 97.03 C ANISOU 1829 CA ALA A1024 10860 8547 17461 1948 1933 -204 C ATOM 1830 C ALA A1024 -14.351 239.301 25.485 1.00 88.59 C ANISOU 1830 C ALA A1024 9749 7592 16319 1947 1784 -100 C ATOM 1831 O ALA A1024 -13.910 238.218 25.879 1.00 92.52 O ANISOU 1831 O ALA A1024 10284 8196 16674 1896 1793 -149 O ATOM 1832 CB ALA A1024 -15.295 240.275 27.577 1.00 99.10 C ANISOU 1832 CB ALA A1024 11054 8813 17786 1955 2079 -302 C ATOM 1833 N GLN A1025 -14.871 239.463 24.267 1.00 78.33 N ANISOU 1833 N GLN A1025 8377 6274 15112 2002 1644 41 N ATOM 1834 CA GLN A1025 -14.668 238.447 23.243 1.00 76.51 C ANISOU 1834 CA GLN A1025 8135 6145 14792 1996 1485 144 C ATOM 1835 C GLN A1025 -13.252 238.510 22.684 1.00 82.60 C ANISOU 1835 C GLN A1025 9037 6931 15418 1953 1415 172 C ATOM 1836 O GLN A1025 -12.703 237.484 22.269 1.00 79.87 O ANISOU 1836 O GLN A1025 8722 6687 14937 1918 1332 203 O ATOM 1837 CB GLN A1025 -15.693 238.610 22.121 1.00 79.00 C ANISOU 1837 CB GLN A1025 8336 6437 15245 2067 1352 285 C ATOM 1838 N VAL A1026 -12.649 239.699 22.674 1.00 89.00 N ANISOU 1838 N VAL A1026 9923 7637 16258 1952 1451 162 N ATOM 1839 CA VAL A1026 -11.242 239.828 22.311 1.00 84.54 C ANISOU 1839 CA VAL A1026 9487 7076 15560 1902 1411 170 C ATOM 1840 C VAL A1026 -10.352 239.357 23.451 1.00 75.82 C ANISOU 1840 C VAL A1026 8472 6022 14315 1826 1523 24 C ATOM 1841 O VAL A1026 -9.379 238.620 23.237 1.00 63.60 O ANISOU 1841 O VAL A1026 6999 4552 12616 1775 1473 25 O ATOM 1842 CB VAL A1026 -10.931 241.287 21.922 1.00 88.84 C ANISOU 1842 CB VAL A1026 10078 7485 16193 1925 1415 209 C ATOM 1843 CG1 VAL A1026 -9.424 241.538 21.880 1.00 88.73 C ANISOU 1843 CG1 VAL A1026 10204 7460 16050 1859 1419 180 C ATOM 1844 CG2 VAL A1026 -11.563 241.620 20.582 1.00 90.15 C ANISOU 1844 CG2 VAL A1026 10180 7617 16454 1993 1272 374 C ATOM 1845 N LYS A1027 -10.659 239.797 24.674 1.00 84.00 N ANISOU 1845 N LYS A1027 9506 7012 15397 1818 1675 -103 N ATOM 1846 CA LYS A1027 -9.823 239.449 25.815 1.00 87.41 C ANISOU 1846 CA LYS A1027 10033 7487 15692 1746 1783 -247 C ATOM 1847 C LYS A1027 -9.807 237.947 26.039 1.00 83.49 C ANISOU 1847 C LYS A1027 9523 7130 15070 1715 1762 -266 C ATOM 1848 O LYS A1027 -8.747 237.352 26.285 1.00 82.32 O ANISOU 1848 O LYS A1027 9465 7047 14763 1652 1760 -317 O ATOM 1849 CB LYS A1027 -10.308 240.184 27.065 1.00 89.14 C ANISOU 1849 CB LYS A1027 10249 7634 15987 1749 1947 -374 C ATOM 1850 CG LYS A1027 -10.161 239.390 28.362 1.00 88.01 C ANISOU 1850 CG LYS A1027 10146 7571 15723 1697 2061 -513 C ATOM 1851 CD LYS A1027 -10.192 240.313 29.579 1.00 89.08 C ANISOU 1851 CD LYS A1027 10330 7624 15891 1682 2218 -650 C ATOM 1852 N ASP A1028 -10.964 237.303 25.927 1.00 80.78 N ANISOU 1852 N ASP A1028 9063 6833 14798 1756 1742 -223 N ATOM 1853 CA ASP A1028 -11.003 235.869 26.174 1.00 81.66 C ANISOU 1853 CA ASP A1028 9157 7073 14798 1726 1729 -243 C ATOM 1854 C ASP A1028 -10.198 235.107 25.131 1.00 75.15 C ANISOU 1854 C ASP A1028 8370 6324 13859 1705 1582 -152 C ATOM 1855 O ASP A1028 -9.564 234.091 25.445 1.00 76.21 O ANISOU 1855 O ASP A1028 8553 6554 13848 1655 1584 -197 O ATOM 1856 CB ASP A1028 -12.448 235.389 26.193 1.00 94.19 C ANISOU 1856 CB ASP A1028 10603 8684 16501 1774 1732 -208 C ATOM 1857 CG ASP A1028 -12.567 233.948 26.601 1.00105.83 C ANISOU 1857 CG ASP A1028 12056 10283 17871 1740 1741 -241 C ATOM 1858 OD1 ASP A1028 -12.513 233.676 27.819 1.00110.59 O ANISOU 1858 OD1 ASP A1028 12696 10911 18412 1704 1875 -360 O ATOM 1859 OD2 ASP A1028 -12.699 233.086 25.707 1.00109.53 O ANISOU 1859 OD2 ASP A1028 12476 10825 18315 1749 1612 -146 O ATOM 1860 N ALA A1029 -10.215 235.573 23.880 1.00 70.62 N ANISOU 1860 N ALA A1029 7777 5709 13346 1743 1455 -23 N ATOM 1861 CA ALA A1029 -9.465 234.877 22.839 1.00 67.63 C ANISOU 1861 CA ALA A1029 7439 5400 12857 1724 1316 69 C ATOM 1862 C ALA A1029 -7.964 235.082 23.010 1.00 71.04 C ANISOU 1862 C ALA A1029 8009 5825 13159 1661 1338 18 C ATOM 1863 O ALA A1029 -7.179 234.143 22.822 1.00 67.95 O ANISOU 1863 O ALA A1029 7669 5521 12630 1618 1290 20 O ATOM 1864 CB ALA A1029 -9.915 235.352 21.460 1.00 66.10 C ANISOU 1864 CB ALA A1029 7196 5164 12754 1782 1174 224 C ATOM 1865 N LEU A1030 -7.550 236.308 23.345 1.00 75.96 N ANISOU 1865 N LEU A1030 8691 6341 13829 1654 1410 -28 N ATOM 1866 CA LEU A1030 -6.143 236.574 23.619 1.00 74.05 C ANISOU 1866 CA LEU A1030 8576 6084 13475 1587 1442 -91 C ATOM 1867 C LEU A1030 -5.650 235.724 24.775 1.00 71.38 C ANISOU 1867 C LEU A1030 8288 5829 13006 1526 1531 -227 C ATOM 1868 O LEU A1030 -4.518 235.226 24.750 1.00 64.76 O ANISOU 1868 O LEU A1030 7533 5040 12032 1468 1508 -251 O ATOM 1869 CB LEU A1030 -5.927 238.060 23.934 1.00 75.51 C ANISOU 1869 CB LEU A1030 8805 6136 13748 1589 1517 -133 C ATOM 1870 CG LEU A1030 -5.454 239.055 22.860 1.00 72.48 C ANISOU 1870 CG LEU A1030 8459 5661 13418 1604 1439 -25 C ATOM 1871 CD1 LEU A1030 -4.528 238.462 21.807 1.00 65.94 C ANISOU 1871 CD1 LEU A1030 7686 4889 12477 1575 1318 72 C ATOM 1872 CD2 LEU A1030 -6.643 239.746 22.211 1.00 75.29 C ANISOU 1872 CD2 LEU A1030 8719 5945 13941 1687 1396 76 C ATOM 1873 N THR A1031 -6.496 235.532 25.788 1.00 76.37 N ANISOU 1873 N THR A1031 8868 6477 13673 1538 1634 -314 N ATOM 1874 CA THR A1031 -6.109 234.732 26.945 1.00 74.85 C ANISOU 1874 CA THR A1031 8725 6363 13350 1483 1724 -442 C ATOM 1875 C THR A1031 -5.803 233.297 26.544 1.00 69.85 C ANISOU 1875 C THR A1031 8087 5856 12598 1461 1643 -401 C ATOM 1876 O THR A1031 -4.811 232.714 26.996 1.00 69.56 O ANISOU 1876 O THR A1031 8135 5878 12415 1400 1660 -470 O ATOM 1877 CB THR A1031 -7.220 234.781 27.996 1.00 76.19 C ANISOU 1877 CB THR A1031 8833 6525 13589 1506 1846 -522 C ATOM 1878 OG1 THR A1031 -7.177 236.042 28.666 1.00 75.82 O ANISOU 1878 OG1 THR A1031 8829 6372 13609 1505 1947 -602 O ATOM 1879 CG2 THR A1031 -7.069 233.667 29.025 1.00 78.00 C ANISOU 1879 CG2 THR A1031 9094 6860 13681 1459 1918 -622 C ATOM 1880 N LYS A1032 -6.641 232.707 25.696 1.00 67.18 N ANISOU 1880 N LYS A1032 7649 5557 12320 1509 1549 -289 N ATOM 1881 CA LYS A1032 -6.394 231.333 25.276 1.00 69.58 C ANISOU 1881 CA LYS A1032 7942 5977 12517 1490 1468 -248 C ATOM 1882 C LYS A1032 -5.237 231.256 24.292 1.00 72.65 C ANISOU 1882 C LYS A1032 8406 6376 12823 1464 1358 -175 C ATOM 1883 O LYS A1032 -4.551 230.229 24.209 1.00 72.40 O ANISOU 1883 O LYS A1032 8412 6432 12665 1426 1321 -180 O ATOM 1884 CB LYS A1032 -7.669 230.751 24.674 1.00 74.35 C ANISOU 1884 CB LYS A1032 8415 6619 13215 1546 1396 -155 C ATOM 1885 CG LYS A1032 -8.782 230.635 25.703 1.00 82.47 C ANISOU 1885 CG LYS A1032 9370 7651 14316 1562 1513 -230 C ATOM 1886 CD LYS A1032 -10.160 230.454 25.091 1.00 88.51 C ANISOU 1886 CD LYS A1032 9994 8416 15221 1623 1449 -138 C ATOM 1887 CE LYS A1032 -11.219 230.496 26.192 1.00 93.07 C ANISOU 1887 CE LYS A1032 10503 8978 15881 1635 1586 -219 C ATOM 1888 NZ LYS A1032 -12.576 230.111 25.728 1.00 96.52 N ANISOU 1888 NZ LYS A1032 10795 9428 16448 1683 1533 -142 N ATOM 1889 N MET A1033 -5.002 232.328 23.545 1.00 76.31 N ANISOU 1889 N MET A1033 8892 6747 13356 1484 1311 -105 N ATOM 1890 CA MET A1033 -3.855 232.378 22.655 1.00 74.05 C ANISOU 1890 CA MET A1033 8685 6457 12992 1454 1223 -37 C ATOM 1891 C MET A1033 -2.556 232.423 23.445 1.00 71.38 C ANISOU 1891 C MET A1033 8461 6121 12538 1378 1299 -153 C ATOM 1892 O MET A1033 -1.529 231.905 22.987 1.00 68.86 O ANISOU 1892 O MET A1033 8207 5845 12114 1336 1242 -127 O ATOM 1893 CB MET A1033 -4.006 233.590 21.750 1.00 75.36 C ANISOU 1893 CB MET A1033 8848 6517 13268 1494 1167 64 C ATOM 1894 CG MET A1033 -3.125 233.630 20.527 1.00 75.06 C ANISOU 1894 CG MET A1033 8871 6475 13172 1480 1053 178 C ATOM 1895 SD MET A1033 -3.440 235.134 19.564 1.00 73.69 S ANISOU 1895 SD MET A1033 8694 6172 13134 1532 1002 295 S ATOM 1896 CE MET A1033 -5.212 235.152 19.510 1.00 67.43 C ANISOU 1896 CE MET A1033 7759 5377 12487 1617 982 337 C ATOM 1897 N ARG A1034 -2.601 232.978 24.656 1.00 71.50 N ANISOU 1897 N ARG A1034 8503 6096 12567 1358 1427 -283 N ATOM 1898 CA ARG A1034 -1.385 233.167 25.435 1.00 70.88 C ANISOU 1898 CA ARG A1034 8536 6012 12384 1283 1494 -399 C ATOM 1899 C ARG A1034 -0.910 231.864 26.074 1.00 69.99 C ANISOU 1899 C ARG A1034 8455 6017 12120 1235 1513 -475 C ATOM 1900 O ARG A1034 0.287 231.560 26.048 1.00 64.67 O ANISOU 1900 O ARG A1034 7864 5372 11336 1175 1492 -503 O ATOM 1901 CB ARG A1034 -1.620 234.232 26.500 1.00 74.10 C ANISOU 1901 CB ARG A1034 8966 6337 12851 1277 1617 -513 C ATOM 1902 CG ARG A1034 -0.332 234.818 27.012 1.00 77.42 C ANISOU 1902 CG ARG A1034 9501 6719 13197 1204 1659 -607 C ATOM 1903 CD ARG A1034 -0.518 235.647 28.259 1.00 83.72 C ANISOU 1903 CD ARG A1034 10331 7458 14020 1189 1784 -743 C ATOM 1904 NE ARG A1034 0.717 235.663 29.036 1.00 89.48 N ANISOU 1904 NE ARG A1034 11171 8205 14621 1104 1822 -864 N ATOM 1905 CZ ARG A1034 1.000 236.539 29.992 1.00 98.97 C ANISOU 1905 CZ ARG A1034 12434 9346 15824 1070 1909 -984 C ATOM 1906 NH1 ARG A1034 0.142 237.497 30.300 1.00106.63 N ANISOU 1906 NH1 ARG A1034 13367 10228 16920 1115 1977 -1001 N ATOM 1907 NH2 ARG A1034 2.154 236.455 30.637 1.00 99.83 N ANISOU 1907 NH2 ARG A1034 12642 9482 15808 989 1925 -1089 N ATOM 1908 N ALA A1035 -1.820 231.085 26.661 1.00 75.64 N ANISOU 1908 N ALA A1035 9107 6800 12832 1258 1555 -507 N ATOM 1909 CA ALA A1035 -1.430 229.787 27.202 1.00 78.06 C ANISOU 1909 CA ALA A1035 9440 7222 12996 1217 1568 -566 C ATOM 1910 C ALA A1035 -0.885 228.879 26.106 1.00 74.22 C ANISOU 1910 C ALA A1035 8952 6799 12450 1212 1445 -464 C ATOM 1911 O ALA A1035 0.121 228.184 26.301 1.00 74.51 O ANISOU 1911 O ALA A1035 9058 6897 12357 1157 1437 -508 O ATOM 1912 CB ALA A1035 -2.624 229.135 27.896 1.00 77.98 C ANISOU 1912 CB ALA A1035 9351 7267 13010 1247 1631 -597 C ATOM 1913 N ALA A1036 -1.542 228.868 24.946 1.00 66.32 N ANISOU 1913 N ALA A1036 7873 5787 11540 1268 1345 -327 N ATOM 1914 CA ALA A1036 -1.031 228.119 23.806 1.00 65.33 C ANISOU 1914 CA ALA A1036 7751 5713 11360 1266 1220 -220 C ATOM 1915 C ALA A1036 0.391 228.539 23.472 1.00 65.39 C ANISOU 1915 C ALA A1036 7865 5683 11298 1212 1199 -221 C ATOM 1916 O ALA A1036 1.245 227.696 23.167 1.00 61.19 O ANISOU 1916 O ALA A1036 7381 5257 10611 1154 1134 -205 O ATOM 1917 CB ALA A1036 -1.943 228.326 22.599 1.00 70.18 C ANISOU 1917 CB ALA A1036 8279 6303 12084 1333 1112 -73 C ATOM 1918 N ALA A1037 0.670 229.843 23.526 1.00 69.42 N ANISOU 1918 N ALA A1037 8417 6089 11872 1205 1236 -237 N ATOM 1919 CA ALA A1037 2.005 230.309 23.178 1.00 69.74 C ANISOU 1919 CA ALA A1037 8552 6086 11859 1149 1217 -234 C ATOM 1920 C ALA A1037 3.016 229.897 24.237 1.00 69.15 C ANISOU 1920 C ALA A1037 8559 6065 11650 1068 1285 -375 C ATOM 1921 O ALA A1037 4.104 229.417 23.906 1.00 65.42 O ANISOU 1921 O ALA A1037 8146 5681 11028 995 1221 -359 O ATOM 1922 CB ALA A1037 2.004 231.822 22.979 1.00 73.70 C ANISOU 1922 CB ALA A1037 9072 6462 12467 1160 1239 -214 C ATOM 1923 N LEU A1038 2.666 230.035 25.516 1.00 75.68 N ANISOU 1923 N LEU A1038 9390 6888 12476 1061 1393 -506 N ATOM 1924 CA LEU A1038 3.577 229.589 26.564 1.00 81.11 C ANISOU 1924 CA LEU A1038 10158 7633 13026 985 1450 -642 C ATOM 1925 C LEU A1038 3.820 228.086 26.478 1.00 82.45 C ANISOU 1925 C LEU A1038 10324 7984 13021 946 1378 -617 C ATOM 1926 O LEU A1038 4.955 227.624 26.644 1.00 82.97 O ANISOU 1926 O LEU A1038 10459 8135 12931 866 1342 -653 O ATOM 1927 CB LEU A1038 3.024 229.975 27.935 1.00 82.95 C ANISOU 1927 CB LEU A1038 10399 7854 13263 984 1567 -773 C ATOM 1928 CG LEU A1038 2.993 231.469 28.278 1.00 88.79 C ANISOU 1928 CG LEU A1038 11164 8476 14094 982 1625 -819 C ATOM 1929 CD1 LEU A1038 3.015 231.650 29.786 1.00 91.25 C ANISOU 1929 CD1 LEU A1038 11530 8802 14338 944 1734 -979 C ATOM 1930 CD2 LEU A1038 4.142 232.238 27.636 1.00 91.26 C ANISOU 1930 CD2 LEU A1038 11540 8718 14417 937 1578 -790 C ATOM 1931 N ASP A1039 2.770 227.306 26.215 1.00 81.88 N ANISOU 1931 N ASP A1039 10166 7965 12979 1002 1354 -556 N ATOM 1932 CA AASP A1039 2.957 225.865 26.076 0.50 79.46 C ANISOU 1932 CA AASP A1039 9852 7821 12517 967 1283 -527 C ATOM 1933 CA BASP A1039 2.934 225.863 26.059 0.50 79.46 C ANISOU 1933 CA BASP A1039 9850 7821 12520 968 1282 -525 C ATOM 1934 C ASP A1039 3.848 225.539 24.886 1.00 76.33 C ANISOU 1934 C ASP A1039 9483 7487 12031 927 1155 -422 C ATOM 1935 O ASP A1039 4.658 224.609 24.953 1.00 77.92 O ANISOU 1935 O ASP A1039 9727 7810 12070 863 1110 -436 O ATOM 1936 CB AASP A1039 1.607 225.163 25.945 0.50 78.84 C ANISOU 1936 CB AASP A1039 9668 7775 12512 1035 1280 -477 C ATOM 1937 CB BASP A1039 1.568 225.209 25.862 0.50 78.87 C ANISOU 1937 CB BASP A1039 9667 7773 12526 1039 1275 -469 C ATOM 1938 CG AASP A1039 0.863 225.087 27.259 0.50 75.61 C ANISOU 1938 CG AASP A1039 9240 7350 12140 1056 1415 -592 C ATOM 1939 CG BASP A1039 1.622 223.710 25.996 0.50 79.06 C ANISOU 1939 CG BASP A1039 9683 7954 12403 1004 1232 -465 C ATOM 1940 OD1AASP A1039 1.523 224.936 28.309 0.50 72.49 O ANISOU 1940 OD1AASP A1039 8924 6993 11627 998 1482 -708 O ATOM 1941 OD1BASP A1039 2.297 223.229 26.928 0.50 79.23 O ANISOU 1941 OD1BASP A1039 9771 8046 12288 943 1278 -562 O ATOM 1942 OD2AASP A1039 -0.381 225.178 27.242 0.50 73.07 O ANISOU 1942 OD2AASP A1039 8823 6976 11964 1130 1453 -566 O ATOM 1943 OD2BASP A1039 0.996 223.015 25.169 0.50 80.11 O ANISOU 1943 OD2BASP A1039 9742 8137 12557 1037 1148 -367 O ATOM 1944 N ALA A1040 3.714 226.288 23.788 1.00 73.71 N ANISOU 1944 N ALA A1040 9132 7071 11804 966 1098 -314 N ATOM 1945 CA ALA A1040 4.592 226.085 22.639 1.00 78.52 C ANISOU 1945 CA ALA A1040 9779 7728 12327 928 989 -214 C ATOM 1946 C ALA A1040 6.042 226.397 22.992 1.00 86.58 C ANISOU 1946 C ALA A1040 10894 8755 13248 840 1009 -283 C ATOM 1947 O ALA A1040 6.961 225.688 22.561 1.00 84.57 O ANISOU 1947 O ALA A1040 10677 8601 12856 782 942 -255 O ATOM 1948 CB ALA A1040 4.138 226.952 21.466 1.00 81.18 C ANISOU 1948 CB ALA A1040 10086 7961 12800 988 934 -87 C ATOM 1949 N GLN A1041 6.267 227.460 23.772 1.00 95.01 N ANISOU 1949 N GLN A1041 11998 9713 14390 830 1100 -377 N ATOM 1950 CA GLN A1041 7.629 227.821 24.151 1.00 99.38 C ANISOU 1950 CA GLN A1041 12634 10262 14862 745 1117 -449 C ATOM 1951 C GLN A1041 8.216 226.799 25.115 1.00100.07 C ANISOU 1951 C GLN A1041 12757 10481 14785 681 1128 -551 C ATOM 1952 O GLN A1041 9.398 226.455 25.014 1.00 95.12 O ANISOU 1952 O GLN A1041 12180 9922 14042 607 1084 -562 O ATOM 1953 CB GLN A1041 7.658 229.233 24.750 1.00104.00 C ANISOU 1953 CB GLN A1041 13249 10689 15577 750 1210 -529 C ATOM 1954 CG GLN A1041 7.953 229.327 26.247 1.00105.84 C ANISOU 1954 CG GLN A1041 13530 10923 15761 706 1302 -701 C ATOM 1955 CD GLN A1041 8.160 230.762 26.702 1.00105.87 C ANISOU 1955 CD GLN A1041 13574 10766 15887 700 1383 -779 C ATOM 1956 OE1 GLN A1041 7.314 231.338 27.387 1.00104.68 O ANISOU 1956 OE1 GLN A1041 13406 10524 15843 750 1475 -847 O ATOM 1957 NE2 GLN A1041 9.294 231.346 26.323 1.00106.22 N ANISOU 1957 NE2 GLN A1041 13669 10768 15920 638 1354 -771 N ATOM 1958 N LYS A1042 7.410 226.295 26.053 1.00108.87 N ANISOU 1958 N LYS A1042 13845 11630 15890 708 1187 -624 N ATOM 1959 CA LYS A1042 7.889 225.226 26.924 1.00115.97 C ANISOU 1959 CA LYS A1042 14778 12660 16626 654 1191 -705 C ATOM 1960 C LYS A1042 8.235 223.984 26.112 1.00113.58 C ANISOU 1960 C LYS A1042 14457 12492 16206 633 1086 -613 C ATOM 1961 O LYS A1042 9.292 223.374 26.308 1.00118.78 O ANISOU 1961 O LYS A1042 15163 13241 16728 564 1050 -643 O ATOM 1962 CB LYS A1042 6.847 224.900 27.997 1.00118.64 C ANISOU 1962 CB LYS A1042 15090 13006 16982 693 1281 -784 C ATOM 1963 CG LYS A1042 6.988 225.737 29.270 1.00118.88 C ANISOU 1963 CG LYS A1042 15179 12958 17032 674 1392 -931 C ATOM 1964 CD LYS A1042 6.757 224.926 30.554 1.00116.92 C ANISOU 1964 CD LYS A1042 14957 12794 16672 657 1457 -1035 C ATOM 1965 CE LYS A1042 7.926 225.081 31.528 1.00115.53 C ANISOU 1965 CE LYS A1042 14882 12644 16371 574 1474 -1159 C ATOM 1966 NZ LYS A1042 7.526 224.939 32.957 1.00115.05 N ANISOU 1966 NZ LYS A1042 14866 12596 16253 572 1580 -1288 N ATOM 1967 N ALA A1043 7.362 223.599 25.187 1.00103.70 N ANISOU 1967 N ALA A1043 13138 11254 15010 692 1034 -501 N ATOM 1968 CA ALA A1043 7.613 222.439 24.342 1.00 97.25 C ANISOU 1968 CA ALA A1043 12305 10558 14088 676 935 -414 C ATOM 1969 C ALA A1043 8.469 222.833 23.145 1.00 96.13 C ANISOU 1969 C ALA A1043 12192 10396 13936 651 860 -323 C ATOM 1970 O ALA A1043 8.732 222.018 22.264 1.00 94.83 O ANISOU 1970 O ALA A1043 12021 10317 13692 639 777 -241 O ATOM 1971 CB ALA A1043 6.302 221.820 23.882 1.00 97.03 C ANISOU 1971 CB ALA A1043 12193 10555 14120 745 906 -340 C ATOM 1972 N LYS A1059 18.588 231.275 21.184 1.00 95.89 N ANISOU 1972 N LYS A1059 12562 9643 14228 109 1001 -401 N ATOM 1973 CA LYS A1059 18.335 232.662 21.554 1.00102.76 C ANISOU 1973 CA LYS A1059 13448 10342 15253 118 1068 -447 C ATOM 1974 C LYS A1059 17.403 233.337 20.555 1.00117.03 C ANISOU 1974 C LYS A1059 15248 12045 17173 200 1076 -312 C ATOM 1975 O LYS A1059 16.463 234.027 20.945 1.00124.50 O ANISOU 1975 O LYS A1059 16186 12889 18230 259 1120 -339 O ATOM 1976 CB LYS A1059 19.647 233.440 21.646 1.00 97.21 C ANISOU 1976 CB LYS A1059 12773 9564 14599 23 1093 -496 C ATOM 1977 N ASP A1060 17.679 233.147 19.262 1.00121.83 N ANISOU 1977 N ASP A1060 15860 12676 17754 204 1035 -165 N ATOM 1978 CA ASP A1060 16.796 233.686 18.231 1.00127.56 C ANISOU 1978 CA ASP A1060 16582 13316 18569 284 1026 -21 C ATOM 1979 C ASP A1060 15.375 233.176 18.423 1.00128.18 C ANISOU 1979 C ASP A1060 16619 13435 18647 378 1003 -10 C ATOM 1980 O ASP A1060 14.402 233.909 18.203 1.00136.01 O ANISOU 1980 O ASP A1060 17596 14317 19765 454 1020 41 O ATOM 1981 CB ASP A1060 17.323 233.307 16.845 1.00125.76 C ANISOU 1981 CB ASP A1060 16373 13141 18269 271 977 130 C ATOM 1982 CG ASP A1060 16.559 233.982 15.718 1.00122.71 C ANISOU 1982 CG ASP A1060 15997 12656 17971 346 963 287 C ATOM 1983 OD1 ASP A1060 15.309 233.984 15.751 1.00117.88 O ANISOU 1983 OD1 ASP A1060 15354 12025 17410 433 944 314 O ATOM 1984 OD2 ASP A1060 17.213 234.511 14.793 1.00124.78 O ANISOU 1984 OD2 ASP A1060 16297 12859 18254 318 971 387 O ATOM 1985 N PHE A1061 15.240 231.913 18.824 1.00110.03 N ANISOU 1985 N PHE A1061 14298 11291 16217 375 964 -54 N ATOM 1986 CA PHE A1061 13.928 231.360 19.134 1.00 98.96 C ANISOU 1986 CA PHE A1061 12851 9932 14817 455 948 -59 C ATOM 1987 C PHE A1061 13.262 232.114 20.276 1.00 94.68 C ANISOU 1987 C PHE A1061 12297 9288 14390 485 1026 -175 C ATOM 1988 O PHE A1061 12.059 232.399 20.222 1.00 90.77 O ANISOU 1988 O PHE A1061 11763 8733 13992 570 1038 -141 O ATOM 1989 CB PHE A1061 14.084 229.872 19.459 1.00 99.15 C ANISOU 1989 CB PHE A1061 12859 10136 14677 431 902 -98 C ATOM 1990 CG PHE A1061 12.967 229.296 20.276 1.00 98.74 C ANISOU 1990 CG PHE A1061 12764 10131 14621 486 913 -161 C ATOM 1991 CD1 PHE A1061 11.878 228.701 19.669 1.00 96.78 C ANISOU 1991 CD1 PHE A1061 12470 9928 14374 561 863 -70 C ATOM 1992 CD2 PHE A1061 13.022 229.324 21.657 1.00100.04 C ANISOU 1992 CD2 PHE A1061 12936 10297 14778 460 974 -313 C ATOM 1993 CE1 PHE A1061 10.858 228.164 20.424 1.00 96.44 C ANISOU 1993 CE1 PHE A1061 12381 9925 14338 608 881 -127 C ATOM 1994 CE2 PHE A1061 12.005 228.788 22.412 1.00100.38 C ANISOU 1994 CE2 PHE A1061 12943 10383 14816 509 996 -368 C ATOM 1995 CZ PHE A1061 10.922 228.204 21.794 1.00 98.53 C ANISOU 1995 CZ PHE A1061 12654 10188 14593 582 953 -275 C ATOM 1996 N ARG A1062 14.025 232.453 21.316 1.00 94.90 N ANISOU 1996 N ARG A1062 12355 9292 14410 417 1080 -315 N ATOM 1997 CA ARG A1062 13.452 233.192 22.435 1.00 93.09 C ANISOU 1997 CA ARG A1062 12126 8963 14281 439 1161 -438 C ATOM 1998 C ARG A1062 12.953 234.561 21.988 1.00 93.60 C ANISOU 1998 C ARG A1062 12189 8841 14532 490 1206 -382 C ATOM 1999 O ARG A1062 11.896 235.022 22.436 1.00 89.11 O ANISOU 1999 O ARG A1062 11593 8191 14072 560 1257 -414 O ATOM 2000 CB ARG A1062 14.485 233.336 23.553 1.00 91.59 C ANISOU 2000 CB ARG A1062 11980 8782 14039 347 1199 -597 C ATOM 2001 N HIS A1063 13.698 235.226 21.097 1.00 98.31 N ANISOU 2001 N HIS A1063 12814 9365 15174 458 1192 -295 N ATOM 2002 CA HIS A1063 13.249 236.518 20.587 1.00 97.00 C ANISOU 2002 CA HIS A1063 12651 9018 15188 507 1230 -225 C ATOM 2003 C HIS A1063 11.893 236.393 19.908 1.00 97.24 C ANISOU 2003 C HIS A1063 12630 9035 15280 620 1195 -104 C ATOM 2004 O HIS A1063 11.093 237.333 19.943 1.00103.50 O ANISOU 2004 O HIS A1063 13400 9730 16194 678 1224 -88 O ATOM 2005 CB HIS A1063 14.282 237.096 19.612 1.00 89.16 C ANISOU 2005 CB HIS A1063 11697 7966 14213 453 1214 -129 C ATOM 2006 CG HIS A1063 14.037 238.531 19.237 1.00 83.12 C ANISOU 2006 CG HIS A1063 10942 7041 13600 481 1250 -74 C ATOM 2007 ND1 HIS A1063 13.957 239.541 20.173 1.00 80.53 N ANISOU 2007 ND1 HIS A1063 10617 6636 13346 465 1312 -193 N ATOM 2008 CD2 HIS A1063 13.861 239.124 18.031 1.00 79.63 C ANISOU 2008 CD2 HIS A1063 10506 6538 13212 518 1219 88 C ATOM 2009 CE1 HIS A1063 13.740 240.693 19.561 1.00 78.21 C ANISOU 2009 CE1 HIS A1063 10326 6235 13156 493 1320 -107 C ATOM 2010 NE2 HIS A1063 13.678 240.468 18.261 1.00 78.14 N ANISOU 2010 NE2 HIS A1063 10321 6235 13135 525 1264 65 N ATOM 2011 N GLY A1064 11.612 235.237 19.300 1.00 88.42 N ANISOU 2011 N GLY A1064 11487 8065 14043 642 1114 -21 N ATOM 2012 CA GLY A1064 10.345 235.068 18.609 1.00 79.85 C ANISOU 2012 CA GLY A1064 10350 6975 13016 744 1067 96 C ATOM 2013 C GLY A1064 9.164 235.019 19.561 1.00 69.74 C ANISOU 2013 C GLY A1064 9013 5674 11813 811 1116 8 C ATOM 2014 O GLY A1064 8.192 235.762 19.402 1.00 65.73 O ANISOU 2014 O GLY A1064 8465 5081 11428 884 1125 53 O ATOM 2015 N PHE A1065 9.230 234.144 20.563 1.00 66.52 N ANISOU 2015 N PHE A1065 8597 5380 11297 777 1137 -116 N ATOM 2016 CA PHE A1065 8.129 234.023 21.507 1.00 70.71 C ANISOU 2016 CA PHE A1065 9077 5899 11890 836 1194 -203 C ATOM 2017 C PHE A1065 8.068 235.194 22.475 1.00 76.79 C ANISOU 2017 C PHE A1065 9866 6559 12753 826 1291 -321 C ATOM 2018 O PHE A1065 7.017 235.422 23.085 1.00 73.09 O ANISOU 2018 O PHE A1065 9350 6080 12342 879 1334 -366 O ATOM 2019 CB PHE A1065 8.234 232.698 22.262 1.00 73.02 C ANISOU 2019 CB PHE A1065 9364 6362 12019 798 1185 -289 C ATOM 2020 CG PHE A1065 7.727 231.517 21.471 1.00 75.06 C ANISOU 2020 CG PHE A1065 9575 6752 12193 831 1090 -180 C ATOM 2021 CD1 PHE A1065 8.570 230.824 20.609 1.00 77.75 C ANISOU 2021 CD1 PHE A1065 9945 7197 12400 781 1003 -100 C ATOM 2022 CD2 PHE A1065 6.408 231.114 21.576 1.00 74.99 C ANISOU 2022 CD2 PHE A1065 9490 6758 12245 912 1089 -160 C ATOM 2023 CE1 PHE A1065 8.100 229.739 19.873 1.00 78.52 C ANISOU 2023 CE1 PHE A1065 10003 7412 12419 810 915 -6 C ATOM 2024 CE2 PHE A1065 5.935 230.037 20.842 1.00 77.15 C ANISOU 2024 CE2 PHE A1065 9718 7148 12447 939 997 -64 C ATOM 2025 CZ PHE A1065 6.783 229.348 19.993 1.00 78.29 C ANISOU 2025 CZ PHE A1065 9899 7396 12451 887 908 10 C ATOM 2026 N ASP A1066 9.151 235.959 22.620 1.00 87.43 N ANISOU 2026 N ASP A1066 11276 7843 14100 752 1318 -369 N ATOM 2027 CA ASP A1066 9.072 237.166 23.428 1.00 93.35 C ANISOU 2027 CA ASP A1066 12042 8502 14925 739 1393 -468 C ATOM 2028 C ASP A1066 8.281 238.247 22.707 1.00 72.91 C ANISOU 2028 C ASP A1066 9418 5810 12476 808 1385 -359 C ATOM 2029 O ASP A1066 7.424 238.902 23.313 1.00 67.90 O ANISOU 2029 O ASP A1066 8753 5125 11922 851 1440 -411 O ATOM 2030 CB ASP A1066 10.470 237.663 23.778 1.00112.21 C ANISOU 2030 CB ASP A1066 14503 10855 17278 636 1415 -551 C ATOM 2031 CG ASP A1066 11.035 236.989 25.007 1.00125.08 C ANISOU 2031 CG ASP A1066 16168 12565 18791 571 1449 -716 C ATOM 2032 OD1 ASP A1066 10.266 236.325 25.734 1.00130.95 O ANISOU 2032 OD1 ASP A1066 16886 13377 19490 607 1475 -779 O ATOM 2033 OD2 ASP A1066 12.248 237.136 25.252 1.00127.91 O ANISOU 2033 OD2 ASP A1066 16580 12920 19102 481 1448 -782 O ATOM 2034 N ILE A1067 8.547 238.446 21.415 1.00 60.64 N ANISOU 2034 N ILE A1067 7870 4224 10948 819 1319 -206 N ATOM 2035 CA ILE A1067 7.723 239.359 20.634 1.00 61.48 C ANISOU 2035 CA ILE A1067 7942 4244 11175 892 1297 -87 C ATOM 2036 C ILE A1067 6.268 238.895 20.655 1.00 63.90 C ANISOU 2036 C ILE A1067 8166 4592 11521 986 1277 -52 C ATOM 2037 O ILE A1067 5.344 239.707 20.768 1.00 66.02 O ANISOU 2037 O ILE A1067 8392 4790 11903 1045 1304 -43 O ATOM 2038 CB ILE A1067 8.263 239.475 19.198 1.00 67.36 C ANISOU 2038 CB ILE A1067 8716 4967 11912 887 1221 80 C ATOM 2039 CG1 ILE A1067 9.691 240.031 19.200 1.00 71.42 C ANISOU 2039 CG1 ILE A1067 9304 5430 12403 790 1251 45 C ATOM 2040 CG2 ILE A1067 7.364 240.364 18.349 1.00 71.94 C ANISOU 2040 CG2 ILE A1067 9263 5464 12605 967 1187 211 C ATOM 2041 CD1 ILE A1067 10.345 240.081 17.797 1.00 72.96 C ANISOU 2041 CD1 ILE A1067 9537 5613 12574 774 1187 209 C ATOM 2042 N LEU A1068 6.035 237.582 20.565 1.00 63.75 N ANISOU 2042 N LEU A1068 8119 4689 11416 1000 1232 -36 N ATOM 2043 CA LEU A1068 4.657 237.100 20.507 1.00 60.91 C ANISOU 2043 CA LEU A1068 7673 4373 11098 1085 1205 6 C ATOM 2044 C LEU A1068 3.937 237.351 21.818 1.00 56.29 C ANISOU 2044 C LEU A1068 7053 3776 10559 1100 1303 -134 C ATOM 2045 O LEU A1068 2.826 237.895 21.836 1.00 55.26 O ANISOU 2045 O LEU A1068 6860 3598 10539 1168 1317 -109 O ATOM 2046 CB LEU A1068 4.616 235.613 20.170 1.00 63.19 C ANISOU 2046 CB LEU A1068 7940 4788 11283 1090 1138 46 C ATOM 2047 CG LEU A1068 3.206 235.102 19.885 1.00 66.77 C ANISOU 2047 CG LEU A1068 8297 5288 11785 1176 1090 113 C ATOM 2048 CD1 LEU A1068 2.723 235.630 18.554 1.00 69.22 C ANISOU 2048 CD1 LEU A1068 8584 5551 12166 1234 997 283 C ATOM 2049 CD2 LEU A1068 3.167 233.572 19.922 1.00 66.32 C ANISOU 2049 CD2 LEU A1068 8216 5360 11622 1171 1049 108 C ATOM 2050 N VAL A1069 4.543 236.953 22.932 1.00 56.03 N ANISOU 2050 N VAL A1069 7063 3788 10440 1037 1370 -283 N ATOM 2051 CA VAL A1069 3.861 237.090 24.214 1.00 59.10 C ANISOU 2051 CA VAL A1069 7428 4177 10849 1049 1466 -417 C ATOM 2052 C VAL A1069 3.765 238.552 24.617 1.00 61.46 C ANISOU 2052 C VAL A1069 7745 4352 11257 1051 1535 -466 C ATOM 2053 O VAL A1069 2.753 238.988 25.181 1.00 69.25 O ANISOU 2053 O VAL A1069 8682 5302 12326 1100 1595 -506 O ATOM 2054 CB VAL A1069 4.575 236.243 25.277 1.00 59.57 C ANISOU 2054 CB VAL A1069 7541 4326 10768 979 1511 -558 C ATOM 2055 CG1 VAL A1069 4.002 236.526 26.668 1.00 60.30 C ANISOU 2055 CG1 VAL A1069 7632 4413 10868 981 1618 -703 C ATOM 2056 CG2 VAL A1069 4.423 234.778 24.924 1.00 60.64 C ANISOU 2056 CG2 VAL A1069 7643 4582 10814 992 1450 -508 C ATOM 2057 N GLY A1070 4.808 239.333 24.341 1.00 55.38 N ANISOU 2057 N GLY A1070 7041 3510 10492 996 1530 -464 N ATOM 2058 CA GLY A1070 4.713 240.763 24.560 1.00 54.11 C ANISOU 2058 CA GLY A1070 6893 3220 10445 1001 1586 -493 C ATOM 2059 C GLY A1070 3.574 241.387 23.781 1.00 56.33 C ANISOU 2059 C GLY A1070 7102 3432 10867 1094 1559 -368 C ATOM 2060 O GLY A1070 2.854 242.248 24.295 1.00 57.52 O ANISOU 2060 O GLY A1070 7226 3506 11124 1131 1626 -414 O ATOM 2061 N GLN A1071 3.388 240.960 22.528 1.00 58.22 N ANISOU 2061 N GLN A1071 7312 3700 11108 1133 1459 -210 N ATOM 2062 CA GLN A1071 2.316 241.548 21.729 1.00 60.74 C ANISOU 2062 CA GLN A1071 7565 3959 11556 1221 1418 -85 C ATOM 2063 C GLN A1071 0.949 241.148 22.271 1.00 58.53 C ANISOU 2063 C GLN A1071 7194 3717 11328 1288 1447 -116 C ATOM 2064 O GLN A1071 0.024 241.963 22.293 1.00 57.93 O ANISOU 2064 O GLN A1071 7065 3563 11383 1349 1474 -95 O ATOM 2065 CB GLN A1071 2.468 241.140 20.267 1.00 63.16 C ANISOU 2065 CB GLN A1071 7871 4295 11832 1243 1296 91 C ATOM 2066 CG GLN A1071 3.519 241.948 19.526 1.00 64.72 C ANISOU 2066 CG GLN A1071 8145 4415 12033 1198 1274 158 C ATOM 2067 CD GLN A1071 3.869 241.372 18.178 1.00 64.23 C ANISOU 2067 CD GLN A1071 8102 4401 11900 1202 1162 317 C ATOM 2068 OE1 GLN A1071 3.784 240.162 17.972 1.00 64.80 O ANISOU 2068 OE1 GLN A1071 8156 4586 11881 1206 1107 342 O ATOM 2069 NE2 GLN A1071 4.257 242.235 17.245 1.00 63.78 N ANISOU 2069 NE2 GLN A1071 8087 4262 11884 1202 1129 428 N ATOM 2070 N ILE A1072 0.813 239.907 22.733 1.00 57.37 N ANISOU 2070 N ILE A1072 7026 3687 11083 1277 1446 -166 N ATOM 2071 CA ILE A1072 -0.432 239.468 23.362 1.00 58.32 C ANISOU 2071 CA ILE A1072 7062 3849 11247 1330 1486 -208 C ATOM 2072 C ILE A1072 -0.725 240.310 24.596 1.00 59.76 C ANISOU 2072 C ILE A1072 7252 3962 11492 1324 1616 -347 C ATOM 2073 O ILE A1072 -1.843 240.815 24.780 1.00 60.36 O ANISOU 2073 O ILE A1072 7257 3987 11689 1386 1654 -341 O ATOM 2074 CB ILE A1072 -0.348 237.969 23.708 1.00 59.01 C ANISOU 2074 CB ILE A1072 7141 4076 11204 1306 1471 -248 C ATOM 2075 CG1 ILE A1072 -0.432 237.119 22.436 1.00 56.84 C ANISOU 2075 CG1 ILE A1072 6833 3870 10894 1334 1339 -98 C ATOM 2076 CG2 ILE A1072 -1.462 237.581 24.685 1.00 63.01 C ANISOU 2076 CG2 ILE A1072 7577 4621 11741 1340 1549 -330 C ATOM 2077 CD1 ILE A1072 -0.201 235.651 22.683 1.00 54.56 C ANISOU 2077 CD1 ILE A1072 6543 3712 10475 1305 1318 -130 C ATOM 2078 N ASP A1073 0.278 240.483 25.460 1.00 61.99 N ANISOU 2078 N ASP A1073 7622 4239 11691 1247 1682 -477 N ATOM 2079 CA ASP A1073 0.069 241.273 26.676 1.00 66.18 C ANISOU 2079 CA ASP A1073 8173 4707 12263 1235 1803 -617 C ATOM 2080 C ASP A1073 -0.281 242.720 26.357 1.00 66.70 C ANISOU 2080 C ASP A1073 8225 4631 12488 1274 1826 -578 C ATOM 2081 O ASP A1073 -1.088 243.345 27.064 1.00 70.05 O ANISOU 2081 O ASP A1073 8616 4997 13004 1309 1912 -642 O ATOM 2082 CB ASP A1073 1.306 241.215 27.567 1.00 69.25 C ANISOU 2082 CB ASP A1073 8666 5119 12525 1140 1850 -757 C ATOM 2083 CG ASP A1073 1.472 239.875 28.251 1.00 71.95 C ANISOU 2083 CG ASP A1073 9023 5596 12717 1105 1860 -832 C ATOM 2084 OD1 ASP A1073 0.545 239.048 28.173 1.00 72.62 O ANISOU 2084 OD1 ASP A1073 9036 5752 12806 1156 1848 -789 O ATOM 2085 OD2 ASP A1073 2.531 239.654 28.873 1.00 73.36 O ANISOU 2085 OD2 ASP A1073 9286 5811 12776 1026 1877 -933 O ATOM 2086 N ASP A1074 0.335 243.294 25.324 1.00 63.03 N ANISOU 2086 N ASP A1074 7788 4104 12057 1267 1755 -473 N ATOM 2087 CA ASP A1074 -0.054 244.643 24.912 1.00 63.00 C ANISOU 2087 CA ASP A1074 7766 3963 12208 1311 1769 -418 C ATOM 2088 C ASP A1074 -1.531 244.688 24.535 1.00 64.14 C ANISOU 2088 C ASP A1074 7802 4093 12476 1410 1752 -332 C ATOM 2089 O ASP A1074 -2.282 245.564 24.990 1.00 65.77 O ANISOU 2089 O ASP A1074 7971 4211 12807 1451 1824 -370 O ATOM 2090 CB ASP A1074 0.800 245.104 23.734 1.00 64.35 C ANISOU 2090 CB ASP A1074 7983 4083 12383 1291 1686 -297 C ATOM 2091 CG ASP A1074 2.226 245.422 24.128 1.00 65.69 C ANISOU 2091 CG ASP A1074 8254 4230 12475 1193 1716 -386 C ATOM 2092 OD1 ASP A1074 2.508 245.520 25.337 1.00 70.44 O ANISOU 2092 OD1 ASP A1074 8892 4835 13036 1146 1803 -545 O ATOM 2093 OD2 ASP A1074 3.059 245.577 23.214 1.00 61.20 O ANISOU 2093 OD2 ASP A1074 7728 3642 11884 1162 1652 -294 O ATOM 2094 N ALA A1075 -1.963 243.758 23.679 1.00 65.22 N ANISOU 2094 N ALA A1075 7883 4314 12583 1447 1652 -214 N ATOM 2095 CA ALA A1075 -3.357 243.729 23.254 1.00 68.39 C ANISOU 2095 CA ALA A1075 8175 4709 13100 1538 1619 -127 C ATOM 2096 C ALA A1075 -4.290 243.450 24.429 1.00 72.55 C ANISOU 2096 C ALA A1075 8643 5264 13660 1558 1722 -243 C ATOM 2097 O ALA A1075 -5.438 243.911 24.431 1.00 73.18 O ANISOU 2097 O ALA A1075 8637 5290 13878 1626 1745 -214 O ATOM 2098 CB ALA A1075 -3.545 242.685 22.147 1.00 64.63 C ANISOU 2098 CB ALA A1075 7660 4330 12566 1564 1485 11 C ATOM 2099 N LEU A1076 -3.813 242.725 25.449 1.00 73.26 N ANISOU 2099 N LEU A1076 8778 5432 13625 1498 1789 -373 N ATOM 2100 CA LEU A1076 -4.653 242.433 26.609 1.00 73.83 C ANISOU 2100 CA LEU A1076 8806 5534 13712 1511 1895 -485 C ATOM 2101 C LEU A1076 -4.886 243.683 27.446 1.00 77.91 C ANISOU 2101 C LEU A1076 9340 5933 14330 1517 2014 -583 C ATOM 2102 O LEU A1076 -6.008 243.928 27.905 1.00 79.13 O ANISOU 2102 O LEU A1076 9419 6055 14590 1569 2082 -606 O ATOM 2103 CB LEU A1076 -4.023 241.334 27.468 1.00 72.69 C ANISOU 2103 CB LEU A1076 8719 5507 13394 1444 1931 -595 C ATOM 2104 CG LEU A1076 -4.315 239.877 27.109 1.00 73.64 C ANISOU 2104 CG LEU A1076 8789 5759 13431 1452 1860 -537 C ATOM 2105 CD1 LEU A1076 -3.503 238.921 27.994 1.00 72.95 C ANISOU 2105 CD1 LEU A1076 8778 5775 13166 1378 1900 -652 C ATOM 2106 CD2 LEU A1076 -5.810 239.579 27.227 1.00 74.93 C ANISOU 2106 CD2 LEU A1076 8832 5939 13698 1522 1883 -508 C ATOM 2107 N LYS A1077 -3.841 244.486 27.655 1.00 81.71 N ANISOU 2107 N LYS A1077 9917 6345 14783 1463 2041 -642 N ATOM 2108 CA LYS A1077 -3.988 245.704 28.446 1.00 85.74 C ANISOU 2108 CA LYS A1077 10452 6740 15387 1464 2151 -740 C ATOM 2109 C LYS A1077 -4.953 246.678 27.776 1.00 87.94 C ANISOU 2109 C LYS A1077 10648 6904 15861 1547 2140 -639 C ATOM 2110 O LYS A1077 -5.737 247.357 28.454 1.00 92.13 O ANISOU 2110 O LYS A1077 11143 7363 16501 1583 2238 -703 O ATOM 2111 CB LYS A1077 -2.616 246.348 28.665 1.00 86.32 C ANISOU 2111 CB LYS A1077 10642 6763 15395 1385 2164 -811 C ATOM 2112 CG LYS A1077 -2.620 247.527 29.623 1.00 89.79 C ANISOU 2112 CG LYS A1077 11122 7091 15905 1371 2280 -937 C ATOM 2113 N LEU A1078 -4.909 246.766 26.444 1.00 85.48 N ANISOU 2113 N LEU A1078 10310 6576 15593 1581 2021 -480 N ATOM 2114 CA LEU A1078 -5.909 247.540 25.717 1.00 87.97 C ANISOU 2114 CA LEU A1078 10540 6798 16086 1667 1992 -368 C ATOM 2115 C LEU A1078 -7.297 246.937 25.895 1.00 81.68 C ANISOU 2115 C LEU A1078 9625 6052 15358 1732 2004 -349 C ATOM 2116 O LEU A1078 -8.283 247.661 26.098 1.00 80.20 O ANISOU 2116 O LEU A1078 9367 5780 15325 1792 2060 -350 O ATOM 2117 CB LEU A1078 -5.533 247.608 24.236 1.00100.77 C ANISOU 2117 CB LEU A1078 12167 8409 17710 1684 1851 -197 C ATOM 2118 CG LEU A1078 -4.524 248.681 23.811 1.00116.23 C ANISOU 2118 CG LEU A1078 14213 10262 19687 1649 1842 -173 C ATOM 2119 CD1 LEU A1078 -3.403 248.855 24.825 1.00122.03 C ANISOU 2119 CD1 LEU A1078 15050 10992 20325 1557 1930 -330 C ATOM 2120 CD2 LEU A1078 -3.936 248.341 22.453 1.00120.51 C ANISOU 2120 CD2 LEU A1078 14783 10839 20166 1644 1704 -18 C ATOM 2121 N ALA A1079 -7.388 245.609 25.841 1.00 80.94 N ANISOU 2121 N ALA A1079 9507 6093 15155 1719 1955 -335 N ATOM 2122 CA ALA A1079 -8.675 244.940 25.986 1.00 84.26 C ANISOU 2122 CA ALA A1079 9812 6568 15636 1774 1962 -316 C ATOM 2123 C ALA A1079 -9.283 245.219 27.354 1.00 84.05 C ANISOU 2123 C ALA A1079 9767 6511 15658 1774 2121 -460 C ATOM 2124 O ALA A1079 -10.454 245.602 27.460 1.00 82.73 O ANISOU 2124 O ALA A1079 9504 6290 15640 1838 2163 -443 O ATOM 2125 CB ALA A1079 -8.505 243.436 25.767 1.00 85.38 C ANISOU 2125 CB ALA A1079 9944 6860 15636 1748 1889 -289 C ATOM 2126 N ASN A1080 -8.495 245.037 28.418 1.00 85.31 N ANISOU 2126 N ASN A1080 10022 6703 15690 1703 2211 -604 N ATOM 2127 CA ASN A1080 -8.995 245.283 29.766 1.00 89.07 C ANISOU 2127 CA ASN A1080 10500 7155 16188 1697 2365 -748 C ATOM 2128 C ASN A1080 -9.567 246.689 29.896 1.00 87.61 C ANISOU 2128 C ASN A1080 10286 6820 16183 1745 2436 -759 C ATOM 2129 O ASN A1080 -10.653 246.880 30.451 1.00 92.14 O ANISOU 2129 O ASN A1080 10784 7360 16865 1790 2525 -794 O ATOM 2130 CB ASN A1080 -7.881 245.068 30.788 1.00 93.46 C ANISOU 2130 CB ASN A1080 11184 7755 16571 1609 2433 -895 C ATOM 2131 CG ASN A1080 -7.575 243.610 31.014 1.00 98.00 C ANISOU 2131 CG ASN A1080 11776 8481 16977 1567 2402 -915 C ATOM 2132 OD1 ASN A1080 -8.336 242.733 30.604 1.00101.30 O ANISOU 2132 OD1 ASN A1080 12105 8972 17412 1604 2354 -837 O ATOM 2133 ND2 ASN A1080 -6.458 243.338 31.677 1.00 98.49 N ANISOU 2133 ND2 ASN A1080 11954 8592 16878 1488 2427 -1019 N ATOM 2134 N GLU A1081 -8.846 247.685 29.386 1.00 82.41 N ANISOU 2134 N GLU A1081 9684 6065 15562 1736 2401 -728 N ATOM 2135 CA GLU A1081 -9.238 249.083 29.487 1.00 86.10 C ANISOU 2135 CA GLU A1081 10137 6381 16196 1776 2467 -741 C ATOM 2136 C GLU A1081 -10.303 249.480 28.463 1.00 86.83 C ANISOU 2136 C GLU A1081 10110 6412 16469 1869 2397 -590 C ATOM 2137 O GLU A1081 -10.560 250.678 28.284 1.00 83.36 O ANISOU 2137 O GLU A1081 9657 5840 16177 1908 2425 -569 O ATOM 2138 CB GLU A1081 -7.995 249.975 29.358 1.00 96.68 C ANISOU 2138 CB GLU A1081 11590 7642 17503 1723 2458 -768 C ATOM 2139 CG GLU A1081 -7.049 249.856 30.558 1.00106.95 C ANISOU 2139 CG GLU A1081 13006 8977 18654 1634 2546 -941 C ATOM 2140 CD GLU A1081 -5.656 250.396 30.283 1.00115.37 C ANISOU 2140 CD GLU A1081 14182 10001 19654 1567 2504 -954 C ATOM 2141 OE1 GLU A1081 -5.490 251.141 29.297 1.00118.83 O ANISOU 2141 OE1 GLU A1081 14610 10352 20187 1593 2438 -844 O ATOM 2142 OE2 GLU A1081 -4.724 250.066 31.051 1.00117.79 O ANISOU 2142 OE2 GLU A1081 14583 10360 19810 1487 2537 -1073 O ATOM 2143 N GLY A1082 -10.936 248.509 27.804 1.00 94.06 N ANISOU 2143 N GLY A1082 10940 7420 17380 1904 2305 -487 N ATOM 2144 CA GLY A1082 -12.106 248.768 26.997 1.00100.32 C ANISOU 2144 CA GLY A1082 11608 8167 18343 1993 2244 -360 C ATOM 2145 C GLY A1082 -11.845 249.101 25.545 1.00100.00 C ANISOU 2145 C GLY A1082 11565 8094 18339 2024 2092 -193 C ATOM 2146 O GLY A1082 -12.796 249.100 24.752 1.00103.06 O ANISOU 2146 O GLY A1082 11849 8469 18842 2096 2012 -73 O ATOM 2147 N LYS A1083 -10.603 249.393 25.164 1.00 95.26 N ANISOU 2147 N LYS A1083 11074 7477 17643 1973 2048 -181 N ATOM 2148 CA LYS A1083 -10.300 249.790 23.789 1.00 94.02 C ANISOU 2148 CA LYS A1083 10929 7281 17514 2000 1913 -21 C ATOM 2149 C LYS A1083 -10.283 248.546 22.910 1.00 89.84 C ANISOU 2149 C LYS A1083 10374 6884 16877 2000 1773 87 C ATOM 2150 O LYS A1083 -9.258 247.883 22.762 1.00 89.69 O ANISOU 2150 O LYS A1083 10436 6944 16697 1936 1731 79 O ATOM 2151 CB LYS A1083 -8.970 250.533 23.723 1.00 97.25 C ANISOU 2151 CB LYS A1083 11465 7624 17863 1939 1925 -48 C ATOM 2152 CG LYS A1083 -9.088 252.040 23.857 1.00104.11 C ANISOU 2152 CG LYS A1083 12344 8328 18886 1967 1995 -63 C ATOM 2153 CD LYS A1083 -7.807 252.767 23.441 1.00106.69 C ANISOU 2153 CD LYS A1083 12785 8587 19166 1914 1972 -44 C ATOM 2154 CE LYS A1083 -6.651 252.493 24.395 1.00106.58 C ANISOU 2154 CE LYS A1083 12876 8616 19005 1813 2047 -197 C ATOM 2155 NZ LYS A1083 -7.013 252.736 25.824 1.00107.65 N ANISOU 2155 NZ LYS A1083 13007 8726 19170 1800 2197 -371 N ATOM 2156 N VAL A1084 -11.427 248.239 22.288 1.00 87.01 N ANISOU 2156 N VAL A1084 9901 6547 16611 2072 1697 190 N ATOM 2157 CA VAL A1084 -11.522 247.030 21.470 1.00 83.77 C ANISOU 2157 CA VAL A1084 9459 6264 16105 2075 1561 288 C ATOM 2158 C VAL A1084 -10.807 247.217 20.141 1.00 78.59 C ANISOU 2158 C VAL A1084 8866 5599 15394 2075 1421 431 C ATOM 2159 O VAL A1084 -10.130 246.305 19.657 1.00 75.85 O ANISOU 2159 O VAL A1084 8568 5354 14897 2034 1338 470 O ATOM 2160 CB VAL A1084 -12.993 246.617 21.254 1.00 89.23 C ANISOU 2160 CB VAL A1084 10005 6984 16915 2147 1521 346 C ATOM 2161 CG1 VAL A1084 -13.752 246.673 22.555 1.00 93.55 C ANISOU 2161 CG1 VAL A1084 10490 7512 17544 2153 1676 211 C ATOM 2162 CG2 VAL A1084 -13.672 247.490 20.195 1.00 91.93 C ANISOU 2162 CG2 VAL A1084 10289 7232 17407 2227 1426 491 C ATOM 2163 N LYS A1085 -10.958 248.385 19.522 1.00 78.02 N ANISOU 2163 N LYS A1085 8797 5407 15441 2121 1394 515 N ATOM 2164 CA LYS A1085 -10.340 248.618 18.222 1.00 78.93 C ANISOU 2164 CA LYS A1085 8976 5507 15506 2125 1263 661 C ATOM 2165 C LYS A1085 -8.826 248.682 18.341 1.00 75.38 C ANISOU 2165 C LYS A1085 8663 5061 14918 2039 1292 613 C ATOM 2166 O LYS A1085 -8.108 248.165 17.477 1.00 74.89 O ANISOU 2166 O LYS A1085 8663 5062 14732 2010 1190 701 O ATOM 2167 CB LYS A1085 -10.874 249.913 17.610 1.00 85.89 C ANISOU 2167 CB LYS A1085 9832 6250 16553 2196 1239 757 C ATOM 2168 CG LYS A1085 -12.381 249.955 17.471 1.00 89.74 C ANISOU 2168 CG LYS A1085 10179 6721 17196 2283 1209 808 C ATOM 2169 CD LYS A1085 -12.885 249.039 16.371 1.00 90.90 C ANISOU 2169 CD LYS A1085 10275 6971 17292 2319 1040 945 C ATOM 2170 CE LYS A1085 -14.354 249.333 16.075 1.00 96.69 C ANISOU 2170 CE LYS A1085 10871 7662 18204 2411 996 1014 C ATOM 2171 NZ LYS A1085 -14.850 248.618 14.869 1.00 99.96 N ANISOU 2171 NZ LYS A1085 11242 8160 18578 2450 814 1161 N ATOM 2172 N GLU A1086 -8.320 249.329 19.392 1.00 74.90 N ANISOU 2172 N GLU A1086 8652 4932 14876 1994 1431 474 N ATOM 2173 CA GLU A1086 -6.883 249.299 19.643 1.00 74.13 C ANISOU 2173 CA GLU A1086 8676 4846 14645 1904 1464 409 C ATOM 2174 C GLU A1086 -6.417 247.879 19.954 1.00 73.44 C ANISOU 2174 C GLU A1086 8608 4910 14387 1848 1446 354 C ATOM 2175 O GLU A1086 -5.318 247.475 19.547 1.00 70.06 O ANISOU 2175 O GLU A1086 8264 4530 13826 1788 1398 378 O ATOM 2176 CB GLU A1086 -6.539 250.261 20.784 1.00 74.39 C ANISOU 2176 CB GLU A1086 8750 4777 14737 1869 1614 260 C ATOM 2177 N ALA A1087 -7.240 247.103 20.670 1.00 75.66 N ANISOU 2177 N ALA A1087 8811 5266 14672 1865 1486 283 N ATOM 2178 CA ALA A1087 -6.888 245.717 20.975 1.00 75.36 C ANISOU 2178 CA ALA A1087 8783 5371 14478 1817 1470 235 C ATOM 2179 C ALA A1087 -6.853 244.871 19.710 1.00 72.25 C ANISOU 2179 C ALA A1087 8378 5064 14009 1833 1312 384 C ATOM 2180 O ALA A1087 -5.892 244.127 19.470 1.00 72.12 O ANISOU 2180 O ALA A1087 8432 5128 13844 1775 1268 388 O ATOM 2181 CB ALA A1087 -7.884 245.126 21.981 1.00 76.17 C ANISOU 2181 CB ALA A1087 8800 5527 14616 1837 1551 137 C ATOM 2182 N GLN A1088 -7.914 244.947 18.901 1.00 69.10 N ANISOU 2182 N GLN A1088 7891 4655 13709 1911 1223 505 N ATOM 2183 CA GLN A1088 -7.920 244.245 17.624 1.00 68.20 C ANISOU 2183 CA GLN A1088 7772 4617 13524 1930 1064 653 C ATOM 2184 C GLN A1088 -6.735 244.679 16.769 1.00 71.32 C ANISOU 2184 C GLN A1088 8283 4977 13838 1893 1006 734 C ATOM 2185 O GLN A1088 -6.065 243.844 16.148 1.00 72.78 O ANISOU 2185 O GLN A1088 8519 5251 13884 1857 923 789 O ATOM 2186 CB GLN A1088 -9.241 244.498 16.893 1.00 68.14 C ANISOU 2186 CB GLN A1088 7658 4582 13651 2021 978 768 C ATOM 2187 CG GLN A1088 -10.432 243.719 17.461 1.00 70.72 C ANISOU 2187 CG GLN A1088 7860 4977 14035 2054 998 720 C ATOM 2188 CD GLN A1088 -11.763 244.135 16.859 1.00 79.77 C ANISOU 2188 CD GLN A1088 8893 6076 15339 2142 928 819 C ATOM 2189 OE1 GLN A1088 -11.939 245.281 16.425 1.00 83.18 O ANISOU 2189 OE1 GLN A1088 9329 6393 15880 2186 917 884 O ATOM 2190 NE2 GLN A1088 -12.713 243.209 16.843 1.00 84.09 N ANISOU 2190 NE2 GLN A1088 9336 6710 15906 2168 880 831 N ATOM 2191 N ALA A1089 -6.439 245.981 16.748 1.00 71.68 N ANISOU 2191 N ALA A1089 8373 4892 13971 1898 1055 740 N ATOM 2192 CA ALA A1089 -5.333 246.456 15.928 1.00 70.31 C ANISOU 2192 CA ALA A1089 8308 4676 13730 1861 1008 821 C ATOM 2193 C ALA A1089 -3.999 245.909 16.424 1.00 68.94 C ANISOU 2193 C ALA A1089 8227 4559 13408 1763 1058 728 C ATOM 2194 O ALA A1089 -3.155 245.503 15.619 1.00 67.70 O ANISOU 2194 O ALA A1089 8140 4447 13134 1726 982 807 O ATOM 2195 CB ALA A1089 -5.309 247.976 15.909 1.00 71.52 C ANISOU 2195 CB ALA A1089 8485 4672 14017 1882 1063 834 C ATOM 2196 N ALA A1090 -3.780 245.912 17.742 1.00 70.06 N ANISOU 2196 N ALA A1090 8372 4697 13549 1720 1185 560 N ATOM 2197 CA ALA A1090 -2.568 245.312 18.294 1.00 71.61 C ANISOU 2197 CA ALA A1090 8650 4956 13604 1628 1228 462 C ATOM 2198 C ALA A1090 -2.486 243.827 17.982 1.00 73.50 C ANISOU 2198 C ALA A1090 8876 5342 13707 1613 1149 492 C ATOM 2199 O ALA A1090 -1.384 243.271 17.874 1.00 74.48 O ANISOU 2199 O ALA A1090 9075 5522 13701 1545 1134 479 O ATOM 2200 CB ALA A1090 -2.515 245.528 19.807 1.00 71.44 C ANISOU 2200 CB ALA A1090 8630 4913 13601 1592 1371 274 C ATOM 2201 N ALA A1091 -3.632 243.167 17.842 1.00 75.11 N ANISOU 2201 N ALA A1091 8984 5610 13945 1675 1099 531 N ATOM 2202 CA ALA A1091 -3.644 241.722 17.655 1.00 76.49 C ANISOU 2202 CA ALA A1091 9138 5925 13999 1662 1031 546 C ATOM 2203 C ALA A1091 -3.327 241.311 16.224 1.00 75.79 C ANISOU 2203 C ALA A1091 9082 5881 13833 1670 886 708 C ATOM 2204 O ALA A1091 -2.885 240.175 16.006 1.00 66.40 O ANISOU 2204 O ALA A1091 7912 4801 12515 1637 834 718 O ATOM 2205 CB ALA A1091 -4.999 241.146 18.076 1.00 78.32 C ANISOU 2205 CB ALA A1091 9250 6209 14298 1718 1036 521 C ATOM 2206 N GLU A1092 -3.526 242.200 15.250 1.00 85.84 N ANISOU 2206 N GLU A1092 10366 7074 15175 1713 821 834 N ATOM 2207 CA GLU A1092 -3.148 241.883 13.879 1.00 95.25 C ANISOU 2207 CA GLU A1092 11607 8305 16278 1717 688 989 C ATOM 2208 C GLU A1092 -1.636 241.911 13.692 1.00 79.83 C ANISOU 2208 C GLU A1092 9774 6348 14209 1634 708 985 C ATOM 2209 O GLU A1092 -1.124 241.291 12.750 1.00 76.69 O ANISOU 2209 O GLU A1092 9427 6017 13696 1616 615 1084 O ATOM 2210 CB GLU A1092 -3.828 242.852 12.911 1.00120.69 C ANISOU 2210 CB GLU A1092 14812 11440 19604 1788 614 1126 C ATOM 2211 CG GLU A1092 -4.169 242.243 11.562 1.00141.15 C ANISOU 2211 CG GLU A1092 17402 14104 22123 1826 451 1286 C ATOM 2212 CD GLU A1092 -5.317 241.257 11.637 1.00157.70 C ANISOU 2212 CD GLU A1092 19387 16298 24234 1872 388 1282 C ATOM 2213 OE1 GLU A1092 -5.572 240.711 12.730 1.00162.45 O ANISOU 2213 OE1 GLU A1092 19930 16941 24853 1855 472 1153 O ATOM 2214 OE2 GLU A1092 -5.972 241.033 10.598 1.00164.63 O ANISOU 2214 OE2 GLU A1092 20237 17211 25105 1923 254 1409 O ATOM 2215 N GLN A1093 -0.909 242.585 14.586 1.00 70.11 N ANISOU 2215 N GLN A1093 8588 5045 13004 1581 829 868 N ATOM 2216 CA GLN A1093 0.547 242.522 14.553 1.00 65.92 C ANISOU 2216 CA GLN A1093 8160 4518 12367 1493 858 844 C ATOM 2217 C GLN A1093 1.049 241.110 14.800 1.00 68.34 C ANISOU 2217 C GLN A1093 8477 4957 12532 1445 840 794 C ATOM 2218 O GLN A1093 2.124 240.741 14.309 1.00 68.60 O ANISOU 2218 O GLN A1093 8586 5023 12454 1387 813 831 O ATOM 2219 CB GLN A1093 1.140 243.468 15.599 1.00 64.94 C ANISOU 2219 CB GLN A1093 8072 4298 12304 1443 989 708 C ATOM 2220 N LEU A1094 0.307 240.319 15.582 1.00 71.88 N ANISOU 2220 N LEU A1094 8850 5479 12983 1466 863 708 N ATOM 2221 CA LEU A1094 0.734 238.961 15.890 1.00 70.96 C ANISOU 2221 CA LEU A1094 8740 5486 12738 1424 851 655 C ATOM 2222 C LEU A1094 0.976 238.154 14.626 1.00 75.37 C ANISOU 2222 C LEU A1094 9323 6123 13193 1428 723 797 C ATOM 2223 O LEU A1094 1.777 237.215 14.632 1.00 74.05 O ANISOU 2223 O LEU A1094 9196 6036 12903 1374 711 776 O ATOM 2224 CB LEU A1094 -0.319 238.258 16.754 1.00 63.65 C ANISOU 2224 CB LEU A1094 7718 4623 11842 1460 883 569 C ATOM 2225 CG LEU A1094 -0.611 238.898 18.109 1.00 63.77 C ANISOU 2225 CG LEU A1094 7712 4578 11941 1454 1018 417 C ATOM 2226 CD1 LEU A1094 -1.938 238.401 18.641 1.00 64.17 C ANISOU 2226 CD1 LEU A1094 7655 4674 12053 1510 1034 380 C ATOM 2227 CD2 LEU A1094 0.493 238.601 19.084 1.00 65.15 C ANISOU 2227 CD2 LEU A1094 7957 4778 12019 1368 1105 276 C ATOM 2228 N LYS A1095 0.289 238.493 13.535 1.00 78.01 N ANISOU 2228 N LYS A1095 9635 6435 13569 1491 623 941 N ATOM 2229 CA LYS A1095 0.392 237.673 12.337 1.00 77.91 C ANISOU 2229 CA LYS A1095 9646 6508 13449 1498 493 1075 C ATOM 2230 C LYS A1095 1.793 237.729 11.739 1.00 77.31 C ANISOU 2230 C LYS A1095 9685 6425 13264 1429 489 1124 C ATOM 2231 O LYS A1095 2.294 236.710 11.250 1.00 74.74 O ANISOU 2231 O LYS A1095 9391 6194 12811 1400 430 1166 O ATOM 2232 CB LYS A1095 -0.669 238.096 11.319 1.00 81.65 C ANISOU 2232 CB LYS A1095 10078 6958 13988 1580 385 1214 C ATOM 2233 CG LYS A1095 -2.092 237.836 11.805 1.00 87.48 C ANISOU 2233 CG LYS A1095 10690 7720 14827 1646 375 1175 C ATOM 2234 CD LYS A1095 -3.065 237.591 10.656 1.00 95.47 C ANISOU 2234 CD LYS A1095 11657 8773 15845 1714 225 1316 C ATOM 2235 CE LYS A1095 -3.103 238.757 9.687 1.00104.73 C ANISOU 2235 CE LYS A1095 12879 9849 17066 1751 174 1443 C ATOM 2236 NZ LYS A1095 -4.222 238.627 8.707 1.00111.00 N ANISOU 2236 NZ LYS A1095 13617 10673 17886 1825 33 1565 N ATOM 2237 N THR A1096 2.463 238.883 11.799 1.00 78.79 N ANISOU 2237 N THR A1096 9933 6503 13501 1398 557 1117 N ATOM 2238 CA THR A1096 3.814 238.940 11.248 1.00 77.79 C ANISOU 2238 CA THR A1096 9910 6369 13277 1326 563 1162 C ATOM 2239 C THR A1096 4.817 238.242 12.158 1.00 71.21 C ANISOU 2239 C THR A1096 9102 5586 12367 1244 641 1029 C ATOM 2240 O THR A1096 5.770 237.623 11.667 1.00 71.40 O ANISOU 2240 O THR A1096 9189 5664 12275 1189 618 1069 O ATOM 2241 CB THR A1096 4.237 240.390 10.990 1.00 81.19 C ANISOU 2241 CB THR A1096 10396 6666 13787 1315 610 1200 C ATOM 2242 OG1 THR A1096 4.458 241.072 12.232 1.00 83.82 O ANISOU 2242 OG1 THR A1096 10716 6925 14209 1282 732 1047 O ATOM 2243 CG2 THR A1096 3.163 241.124 10.196 1.00 81.15 C ANISOU 2243 CG2 THR A1096 10360 6604 13869 1402 536 1322 C ATOM 2244 N THR A1097 4.617 238.305 13.475 1.00 64.59 N ANISOU 2244 N THR A1097 8221 4734 11588 1233 734 872 N ATOM 2245 CA THR A1097 5.449 237.511 14.372 1.00 60.80 C ANISOU 2245 CA THR A1097 7761 4315 11025 1161 796 742 C ATOM 2246 C THR A1097 5.259 236.029 14.089 1.00 62.67 C ANISOU 2246 C THR A1097 7971 4683 11156 1171 722 772 C ATOM 2247 O THR A1097 6.231 235.265 14.030 1.00 62.36 O ANISOU 2247 O THR A1097 7980 4704 11008 1110 722 758 O ATOM 2248 CB THR A1097 5.105 237.824 15.828 1.00 60.91 C ANISOU 2248 CB THR A1097 7734 4298 11109 1156 901 570 C ATOM 2249 OG1 THR A1097 5.138 239.238 16.031 1.00 65.76 O ANISOU 2249 OG1 THR A1097 8366 4786 11833 1156 961 550 O ATOM 2250 CG2 THR A1097 6.092 237.128 16.776 1.00 57.84 C ANISOU 2250 CG2 THR A1097 7383 3965 10629 1073 966 430 C ATOM 2251 N ARG A1098 4.006 235.614 13.890 1.00 67.36 N ANISOU 2251 N ARG A1098 8486 5322 11784 1248 658 816 N ATOM 2252 CA ARG A1098 3.716 234.220 13.573 1.00 70.86 C ANISOU 2252 CA ARG A1098 8897 5890 12137 1262 579 851 C ATOM 2253 C ARG A1098 4.418 233.807 12.286 1.00 73.84 C ANISOU 2253 C ARG A1098 9343 6309 12402 1240 487 990 C ATOM 2254 O ARG A1098 5.156 232.815 12.257 1.00 75.81 O ANISOU 2254 O ARG A1098 9626 6662 12516 1184 473 968 O ATOM 2255 CB ARG A1098 2.204 234.022 13.456 1.00 69.93 C ANISOU 2255 CB ARG A1098 8677 5801 12092 1347 517 887 C ATOM 2256 CG ARG A1098 1.752 232.580 13.205 1.00 68.63 C ANISOU 2256 CG ARG A1098 8463 5764 11847 1364 433 912 C ATOM 2257 CD ARG A1098 0.327 232.555 12.681 1.00 69.72 C ANISOU 2257 CD ARG A1098 8512 5920 12059 1445 342 990 C ATOM 2258 NE ARG A1098 0.211 233.294 11.430 1.00 71.31 N ANISOU 2258 NE ARG A1098 8750 6073 12270 1478 251 1139 N ATOM 2259 CZ ARG A1098 -0.926 233.763 10.925 1.00 73.91 C ANISOU 2259 CZ ARG A1098 9018 6375 12689 1549 182 1214 C ATOM 2260 NH1 ARG A1098 -2.081 233.589 11.558 1.00 70.51 N ANISOU 2260 NH1 ARG A1098 8477 5958 12355 1594 198 1155 N ATOM 2261 NH2 ARG A1098 -0.906 234.426 9.780 1.00 79.99 N ANISOU 2261 NH2 ARG A1098 9838 7103 13451 1573 101 1349 N ATOM 2262 N ASN A1099 4.214 234.577 11.213 1.00 72.47 N ANISOU 2262 N ASN A1099 9199 6084 12253 1273 423 1125 N ATOM 2263 CA ASN A1099 4.829 234.244 9.934 1.00 72.81 C ANISOU 2263 CA ASN A1099 9317 6168 12180 1254 338 1264 C ATOM 2264 C ASN A1099 6.347 234.285 10.012 1.00 73.88 C ANISOU 2264 C ASN A1099 9542 6287 12241 1163 410 1235 C ATOM 2265 O ASN A1099 7.024 233.502 9.337 1.00 73.48 O ANISOU 2265 O ASN A1099 9545 6343 12031 1115 360 1285 O ATOM 2266 CB ASN A1099 4.335 235.201 8.852 1.00 77.45 C ANISOU 2266 CB ASN A1099 9928 6690 12808 1305 268 1406 C ATOM 2267 CG ASN A1099 2.878 234.971 8.492 1.00 84.18 C ANISOU 2267 CG ASN A1099 10697 7580 13709 1393 165 1461 C ATOM 2268 OD1 ASN A1099 2.450 233.840 8.295 1.00 88.42 O ANISOU 2268 OD1 ASN A1099 11194 8225 14178 1408 88 1474 O ATOM 2269 ND2 ASN A1099 2.110 236.046 8.412 1.00 86.45 N ANISOU 2269 ND2 ASN A1099 10952 7777 14118 1448 165 1491 N ATOM 2270 N ALA A1100 6.900 235.167 10.839 1.00 76.22 N ANISOU 2270 N ALA A1100 9856 6492 12612 1121 521 1135 N ATOM 2271 CA ALA A1100 8.337 235.401 10.830 1.00 78.27 C ANISOU 2271 CA ALA A1100 10197 6721 12819 1031 587 1114 C ATOM 2272 C ALA A1100 9.116 234.526 11.804 1.00 78.71 C ANISOU 2272 C ALA A1100 10252 6897 12757 945 635 957 C ATOM 2273 O ALA A1100 10.306 234.288 11.569 1.00 80.99 O ANISOU 2273 O ALA A1100 10602 7240 12932 861 650 950 O ATOM 2274 CB ALA A1100 8.628 236.870 11.138 1.00 79.66 C ANISOU 2274 CB ALA A1100 10398 6765 13104 1011 666 1080 C ATOM 2275 N TYR A1101 8.493 234.041 12.882 1.00 77.84 N ANISOU 2275 N TYR A1101 10075 6831 12669 963 661 832 N ATOM 2276 CA TYR A1101 9.225 233.294 13.905 1.00 77.70 C ANISOU 2276 CA TYR A1101 10062 6918 12544 884 710 679 C ATOM 2277 C TYR A1101 8.556 231.974 14.273 1.00 70.31 C ANISOU 2277 C TYR A1101 9067 6129 11517 904 663 633 C ATOM 2278 O TYR A1101 9.216 230.929 14.349 1.00 60.80 O ANISOU 2278 O TYR A1101 7881 5066 10156 843 639 594 O ATOM 2279 CB TYR A1101 9.369 234.125 15.178 1.00 85.97 C ANISOU 2279 CB TYR A1101 11102 7857 13704 864 822 533 C ATOM 2280 CG TYR A1101 10.204 235.372 15.044 1.00 91.10 C ANISOU 2280 CG TYR A1101 11810 8363 14440 823 884 543 C ATOM 2281 CD1 TYR A1101 9.651 236.554 14.570 1.00 92.08 C ANISOU 2281 CD1 TYR A1101 11933 8338 14716 883 894 628 C ATOM 2282 CD2 TYR A1101 11.538 235.375 15.419 1.00 93.65 C ANISOU 2282 CD2 TYR A1101 12184 8710 14688 719 927 462 C ATOM 2283 CE1 TYR A1101 10.409 237.699 14.459 1.00 93.16 C ANISOU 2283 CE1 TYR A1101 12120 8373 14903 834 943 630 C ATOM 2284 CE2 TYR A1101 12.304 236.518 15.311 1.00 94.97 C ANISOU 2284 CE2 TYR A1101 12399 8742 14945 677 986 468 C ATOM 2285 CZ TYR A1101 11.731 237.678 14.831 1.00 94.05 C ANISOU 2285 CZ TYR A1101 12283 8483 14970 735 997 553 C ATOM 2286 OH TYR A1101 12.478 238.825 14.720 1.00 94.27 O ANISOU 2286 OH TYR A1101 12353 8410 15055 684 1045 553 O ATOM 2287 N ILE A1102 7.247 232.021 14.524 1.00 71.26 N ANISOU 2287 N ILE A1102 9113 6215 11745 989 653 637 N ATOM 2288 CA ILE A1102 6.563 230.896 15.147 1.00 65.46 C ANISOU 2288 CA ILE A1102 8316 5599 10957 1006 636 566 C ATOM 2289 C ILE A1102 6.410 229.739 14.170 1.00 62.63 C ANISOU 2289 C ILE A1102 7951 5379 10466 1010 520 663 C ATOM 2290 O ILE A1102 6.534 228.572 14.554 1.00 59.06 O ANISOU 2290 O ILE A1102 7486 5063 9893 976 504 601 O ATOM 2291 CB ILE A1102 5.202 231.355 15.694 1.00 60.52 C ANISOU 2291 CB ILE A1102 7606 4884 10504 1095 670 542 C ATOM 2292 CG1 ILE A1102 5.393 232.554 16.646 1.00 61.72 C ANISOU 2292 CG1 ILE A1102 7774 4889 10788 1089 793 440 C ATOM 2293 CG2 ILE A1102 4.501 230.208 16.401 1.00 56.08 C ANISOU 2293 CG2 ILE A1102 6976 4438 9893 1108 668 466 C ATOM 2294 CD1 ILE A1102 6.459 232.303 17.751 1.00 61.36 C ANISOU 2294 CD1 ILE A1102 7780 4896 10639 993 872 282 C ATOM 2295 N GLN A1103 6.108 230.033 12.904 1.00 66.77 N ANISOU 2295 N GLN A1103 8489 5871 11011 1055 435 816 N ATOM 2296 CA GLN A1103 5.970 228.961 11.921 1.00 75.94 C ANISOU 2296 CA GLN A1103 9654 7160 12040 1058 320 906 C ATOM 2297 C GLN A1103 7.303 228.261 11.685 1.00 69.04 C ANISOU 2297 C GLN A1103 8855 6395 10981 964 320 886 C ATOM 2298 O GLN A1103 7.343 227.040 11.506 1.00 59.27 O ANISOU 2298 O GLN A1103 7611 5296 9613 942 264 878 O ATOM 2299 CB GLN A1103 5.414 229.515 10.611 1.00 95.55 C ANISOU 2299 CB GLN A1103 12149 9578 14577 1123 228 1075 C ATOM 2300 CG GLN A1103 5.165 228.463 9.548 1.00108.91 C ANISOU 2300 CG GLN A1103 13848 11395 16136 1132 100 1170 C ATOM 2301 CD GLN A1103 4.471 229.028 8.327 1.00119.84 C ANISOU 2301 CD GLN A1103 15241 12713 17580 1206 0 1334 C ATOM 2302 OE1 GLN A1103 3.518 229.799 8.442 1.00122.14 O ANISOU 2302 OE1 GLN A1103 15471 12893 18042 1283 -5 1368 O ATOM 2303 NE2 GLN A1103 4.951 228.652 7.147 1.00124.93 N ANISOU 2303 NE2 GLN A1103 15962 13423 18082 1183 -82 1439 N ATOM 2304 N LYS A1104 8.401 229.021 11.689 1.00 72.28 N ANISOU 2304 N LYS A1104 9335 6741 11389 908 384 876 N ATOM 2305 CA LYS A1104 9.720 228.442 11.459 1.00 68.78 C ANISOU 2305 CA LYS A1104 8956 6389 10789 819 391 858 C ATOM 2306 C LYS A1104 10.108 227.476 12.568 1.00 64.82 C ANISOU 2306 C LYS A1104 8430 5997 10202 765 428 713 C ATOM 2307 O LYS A1104 10.789 226.475 12.312 1.00 60.56 O ANISOU 2307 O LYS A1104 7915 5580 9515 714 398 706 O ATOM 2308 CB LYS A1104 10.760 229.558 11.322 1.00 69.71 C ANISOU 2308 CB LYS A1104 9140 6398 10950 770 461 871 C ATOM 2309 CG LYS A1104 12.153 229.181 11.787 1.00 70.94 C ANISOU 2309 CG LYS A1104 9333 6618 11002 670 514 780 C ATOM 2310 N ATYR A1105 9.657 227.728 13.794 0.50 65.35 N ANISOU 2310 N ATYR A1105 8449 6022 10358 779 494 599 N ATOM 2311 N BTYR A1105 9.707 227.763 13.805 0.50 65.37 N ANISOU 2311 N BTYR A1105 8454 6021 10361 776 497 597 N ATOM 2312 CA ATYR A1105 9.997 226.854 14.907 0.50 64.65 C ANISOU 2312 CA ATYR A1105 8345 6033 10188 730 531 463 C ATOM 2313 CA BTYR A1105 10.061 226.881 14.908 0.50 64.67 C ANISOU 2313 CA BTYR A1105 8350 6033 10188 727 533 462 C ATOM 2314 C ATYR A1105 9.021 225.701 15.073 0.50 63.05 C ANISOU 2314 C ATYR A1105 8079 5933 9942 770 480 454 C ATOM 2315 C BTYR A1105 9.178 225.641 14.935 0.50 62.96 C ANISOU 2315 C BTYR A1105 8077 5932 9912 762 473 464 C ATOM 2316 O ATYR A1105 9.421 224.637 15.554 0.50 63.17 O ANISOU 2316 O ATYR A1105 8094 6068 9841 726 478 386 O ATOM 2317 O BTYR A1105 9.668 224.542 15.211 0.50 63.01 O ANISOU 2317 O BTYR A1105 8089 6063 9789 715 459 413 O ATOM 2318 CB ATYR A1105 10.088 227.669 16.194 0.50 65.24 C ANISOU 2318 CB ATYR A1105 8413 6015 10360 716 633 335 C ATOM 2319 CB BTYR A1105 9.973 227.629 16.237 0.50 65.25 C ANISOU 2319 CB BTYR A1105 8408 6018 10364 722 633 333 C ATOM 2320 CG ATYR A1105 11.261 228.611 16.149 0.50 64.71 C ANISOU 2320 CG ATYR A1105 8409 5866 10314 654 683 322 C ATOM 2321 CG BTYR A1105 9.722 226.734 17.426 0.50 63.45 C ANISOU 2321 CG BTYR A1105 8145 5881 10081 708 663 209 C ATOM 2322 CD1ATYR A1105 12.538 228.137 15.890 0.50 63.44 C ANISOU 2322 CD1ATYR A1105 8294 5782 10028 573 672 317 C ATOM 2323 CD1BTYR A1105 10.768 226.090 18.073 0.50 61.75 C ANISOU 2323 CD1BTYR A1105 7963 5757 9742 629 682 117 C ATOM 2324 CD2ATYR A1105 11.091 229.969 16.316 0.50 65.42 C ANISOU 2324 CD2ATYR A1105 8506 5795 10555 677 742 319 C ATOM 2325 CD2BTYR A1105 8.435 226.532 17.905 0.50 63.56 C ANISOU 2325 CD2BTYR A1105 8092 5889 10169 776 672 186 C ATOM 2326 CE1ATYR A1105 13.611 228.986 15.825 0.50 65.53 C ANISOU 2326 CE1ATYR A1105 8607 5969 10321 514 718 306 C ATOM 2327 CE1BTYR A1105 10.536 225.270 19.166 0.50 62.35 C ANISOU 2327 CE1BTYR A1105 8015 5914 9760 618 709 10 C ATOM 2328 CE2ATYR A1105 12.154 230.824 16.249 0.50 67.80 C ANISOU 2328 CE2ATYR A1105 8861 6016 10883 617 787 308 C ATOM 2329 CE2BTYR A1105 8.196 225.710 18.993 0.50 64.06 C ANISOU 2329 CE2BTYR A1105 8129 6033 10178 763 708 78 C ATOM 2330 CZ ATYR A1105 13.416 230.329 16.005 0.50 69.75 C ANISOU 2330 CZ ATYR A1105 9150 6345 11008 534 775 302 C ATOM 2331 CZ BTYR A1105 9.246 225.088 19.617 0.50 64.65 C ANISOU 2331 CZ BTYR A1105 8247 6197 10121 684 725 -8 C ATOM 2332 OH ATYR A1105 14.493 231.189 15.942 0.50 74.73 O ANISOU 2332 OH ATYR A1105 9826 6892 11676 470 823 290 O ATOM 2333 OH BTYR A1105 8.992 224.281 20.696 0.50 66.56 O ANISOU 2333 OH BTYR A1105 8469 6517 10305 674 760 -108 O ATOM 2334 N ALEU A1106 7.754 225.877 14.691 0.50 61.70 N ANISOU 2334 N ALEU A1106 7852 5719 9871 853 439 522 N ATOM 2335 N BLEU A1106 7.880 225.787 14.650 0.50 61.57 N ANISOU 2335 N BLEU A1106 7842 5715 9836 845 435 522 N ATOM 2336 CA ALEU A1106 6.885 224.721 14.499 0.50 57.36 C ANISOU 2336 CA ALEU A1106 7245 5274 9274 887 367 544 C ATOM 2337 CA BLEU A1106 7.010 224.619 14.611 0.50 57.19 C ANISOU 2337 CA BLEU A1106 7228 5265 9237 877 374 529 C ATOM 2338 C ALEU A1106 7.524 223.734 13.526 0.50 57.29 C ANISOU 2338 C ALEU A1106 7281 5385 9103 847 284 610 C ATOM 2339 C BLEU A1106 7.300 223.728 13.405 0.50 57.33 C ANISOU 2339 C BLEU A1106 7276 5387 9121 861 270 626 C ATOM 2340 O ALEU A1106 7.623 222.533 13.807 0.50 53.85 O ANISOU 2340 O ALEU A1106 6831 5070 8560 818 264 562 O ATOM 2341 O BLEU A1106 6.904 222.556 13.410 0.50 54.64 O ANISOU 2341 O BLEU A1106 6900 5155 8706 862 222 614 O ATOM 2342 CB ALEU A1106 5.514 225.181 13.990 0.50 56.26 C ANISOU 2342 CB ALEU A1106 7040 5059 9276 982 318 631 C ATOM 2343 CB BLEU A1106 5.536 225.052 14.629 0.50 55.23 C ANISOU 2343 CB BLEU A1106 6898 4940 9148 970 360 565 C ATOM 2344 CG ALEU A1106 4.624 224.160 13.260 0.50 52.82 C ANISOU 2344 CG ALEU A1106 6553 4715 8802 1022 207 704 C ATOM 2345 CG BLEU A1106 5.030 225.732 15.913 0.50 50.81 C ANISOU 2345 CG BLEU A1106 6295 4289 8722 995 470 456 C ATOM 2346 CD1ALEU A1106 4.055 223.140 14.214 0.50 51.19 C ANISOU 2346 CD1ALEU A1106 6278 4592 8580 1021 232 607 C ATOM 2347 CD1BLEU A1106 3.522 225.879 15.881 0.50 51.63 C ANISOU 2347 CD1BLEU A1106 6303 4341 8975 1087 449 494 C ATOM 2348 CD2ALEU A1106 3.505 224.871 12.500 0.50 52.23 C ANISOU 2348 CD2ALEU A1106 6429 4546 8870 1112 141 817 C ATOM 2349 CD2BLEU A1106 5.432 224.976 17.170 0.50 46.77 C ANISOU 2349 CD2BLEU A1106 5787 3861 8124 939 541 315 C ATOM 2350 N GLU A 219 7.993 224.245 12.385 1.00 61.70 N ANISOU 2350 N GLU A 219 7897 5907 9638 844 242 719 N ATOM 2351 CA GLU A 219 8.484 223.395 11.306 1.00 67.91 C ANISOU 2351 CA GLU A 219 8730 6796 10276 815 162 794 C ATOM 2352 C GLU A 219 9.737 222.636 11.714 1.00 59.89 C ANISOU 2352 C GLU A 219 7755 5876 9124 729 201 714 C ATOM 2353 O GLU A 219 9.869 221.439 11.426 1.00 57.42 O ANISOU 2353 O GLU A 219 7444 5683 8690 708 151 713 O ATOM 2354 CB GLU A 219 8.770 224.242 10.068 1.00 78.29 C ANISOU 2354 CB GLU A 219 10110 8038 11599 829 126 926 C ATOM 2355 CG GLU A 219 7.576 224.429 9.144 1.00 86.39 C ANISOU 2355 CG GLU A 219 11108 9030 12685 912 27 1047 C ATOM 2356 CD GLU A 219 7.764 225.573 8.154 1.00 91.68 C ANISOU 2356 CD GLU A 219 11841 9593 13401 934 12 1173 C ATOM 2357 OE1 GLU A 219 6.751 226.151 7.704 1.00 93.35 O ANISOU 2357 OE1 GLU A 219 12020 9728 13720 1011 -45 1259 O ATOM 2358 OE2 GLU A 219 8.926 225.898 7.829 1.00 93.26 O ANISOU 2358 OE2 GLU A 219 12120 9781 13534 876 57 1189 O ATOM 2359 N ARG A 220 10.671 223.312 12.381 1.00 58.64 N ANISOU 2359 N ARG A 220 7628 5664 8989 679 288 645 N ATOM 2360 CA ARG A 220 11.873 222.636 12.849 1.00 67.57 C ANISOU 2360 CA ARG A 220 8788 6880 10005 599 323 565 C ATOM 2361 C ARG A 220 11.538 221.568 13.876 1.00 58.95 C ANISOU 2361 C ARG A 220 7648 5883 8869 592 329 462 C ATOM 2362 O ARG A 220 12.169 220.506 13.897 1.00 56.54 O ANISOU 2362 O ARG A 220 7354 5688 8440 547 311 432 O ATOM 2363 CB ARG A 220 12.864 223.637 13.452 1.00 93.68 C ANISOU 2363 CB ARG A 220 12129 10102 13364 546 410 503 C ATOM 2364 CG ARG A 220 13.477 224.619 12.469 1.00121.97 C ANISOU 2364 CG ARG A 220 15770 13597 16977 534 418 599 C ATOM 2365 CD ARG A 220 14.146 223.925 11.292 1.00143.46 C ANISOU 2365 CD ARG A 220 18539 16403 19566 504 369 686 C ATOM 2366 NE ARG A 220 13.483 224.258 10.034 1.00160.29 N ANISOU 2366 NE ARG A 220 20696 18497 21711 561 306 828 N ATOM 2367 CZ ARG A 220 13.575 223.542 8.918 1.00172.41 C ANISOU 2367 CZ ARG A 220 22268 20110 23128 562 240 916 C ATOM 2368 NH1 ARG A 220 14.297 222.429 8.890 1.00175.75 N ANISOU 2368 NH1 ARG A 220 22703 20653 23420 511 234 875 N ATOM 2369 NH2 ARG A 220 12.934 223.938 7.827 1.00177.49 N ANISOU 2369 NH2 ARG A 220 22941 20712 23786 615 179 1044 N ATOM 2370 N ALA A 221 10.563 221.834 14.753 1.00 56.01 N ANISOU 2370 N ALA A 221 7220 5465 8597 637 360 405 N ATOM 2371 CA ALA A 221 10.228 220.854 15.781 1.00 54.25 C ANISOU 2371 CA ALA A 221 6955 5326 8332 630 377 309 C ATOM 2372 C ALA A 221 9.519 219.640 15.186 1.00 48.47 C ANISOU 2372 C ALA A 221 6187 4694 7536 658 294 362 C ATOM 2373 O ALA A 221 9.739 218.509 15.630 1.00 44.48 O ANISOU 2373 O ALA A 221 5673 4292 6935 627 289 308 O ATOM 2374 CB ALA A 221 9.371 221.498 16.865 1.00 59.69 C ANISOU 2374 CB ALA A 221 7598 5934 9146 670 446 235 C ATOM 2375 N ARG A 222 8.665 219.857 14.187 1.00 48.01 N ANISOU 2375 N ARG A 222 6108 4602 7530 716 226 467 N ATOM 2376 CA ARG A 222 8.001 218.749 13.512 1.00 50.04 C ANISOU 2376 CA ARG A 222 6334 4949 7729 739 136 520 C ATOM 2377 C ARG A 222 9.015 217.861 12.797 1.00 53.67 C ANISOU 2377 C ARG A 222 6853 5510 8029 684 93 544 C ATOM 2378 O ARG A 222 8.933 216.625 12.863 1.00 56.69 O ANISOU 2378 O ARG A 222 7217 5995 8327 668 59 519 O ATOM 2379 CB ARG A 222 6.964 219.307 12.538 1.00 51.47 C ANISOU 2379 CB ARG A 222 6488 5066 8002 811 62 632 C ATOM 2380 CG ARG A 222 6.244 218.293 11.720 1.00 54.53 C ANISOU 2380 CG ARG A 222 6846 5535 8339 837 -45 693 C ATOM 2381 CD ARG A 222 5.205 218.984 10.818 1.00 57.43 C ANISOU 2381 CD ARG A 222 7184 5827 8811 911 -124 804 C ATOM 2382 N SER A 223 9.999 218.467 12.131 1.00 53.15 N ANISOU 2382 N SER A 223 6858 5413 7925 652 102 591 N ATOM 2383 CA SER A 223 10.930 217.664 11.352 1.00 53.01 C ANISOU 2383 CA SER A 223 6895 5484 7762 604 67 621 C ATOM 2384 C SER A 223 11.919 216.927 12.252 1.00 48.17 C ANISOU 2384 C SER A 223 6288 4945 7069 539 121 517 C ATOM 2385 O SER A 223 12.333 215.809 11.923 1.00 48.60 O ANISOU 2385 O SER A 223 6356 5099 7011 510 88 515 O ATOM 2386 CB SER A 223 11.632 218.554 10.320 1.00 62.51 C ANISOU 2386 CB SER A 223 8170 6626 8955 591 68 711 C ATOM 2387 OG SER A 223 12.673 219.305 10.895 1.00 73.45 O ANISOU 2387 OG SER A 223 9584 7958 10366 542 154 659 O ATOM 2388 N THR A 224 12.272 217.503 13.407 1.00 46.81 N ANISOU 2388 N THR A 224 6105 4726 6955 517 200 429 N ATOM 2389 CA THR A 224 13.049 216.771 14.407 1.00 47.50 C ANISOU 2389 CA THR A 224 6191 4885 6972 463 241 326 C ATOM 2390 C THR A 224 12.310 215.528 14.891 1.00 42.83 C ANISOU 2390 C THR A 224 5551 4382 6341 480 212 288 C ATOM 2391 O THR A 224 12.914 214.464 15.069 1.00 42.95 O ANISOU 2391 O THR A 224 5573 4490 6254 442 203 252 O ATOM 2392 CB THR A 224 13.366 217.672 15.606 1.00 52.29 C ANISOU 2392 CB THR A 224 6795 5420 7654 442 322 235 C ATOM 2393 OG1 THR A 224 14.248 218.732 15.208 1.00 57.55 O ANISOU 2393 OG1 THR A 224 7507 6008 8352 412 354 260 O ATOM 2394 CG2 THR A 224 14.028 216.872 16.730 1.00 49.49 C ANISOU 2394 CG2 THR A 224 6437 5143 7224 393 353 128 C ATOM 2395 N ALEU A 225 11.009 215.653 15.150 0.50 42.08 N ANISOU 2395 N ALEU A 225 5403 4254 6333 537 203 292 N ATOM 2396 N BLEU A 225 11.010 215.657 15.155 0.50 42.09 N ANISOU 2396 N BLEU A 225 5403 4254 6333 537 204 292 N ATOM 2397 CA ALEU A 225 10.228 214.506 15.581 0.50 43.05 C ANISOU 2397 CA ALEU A 225 5474 4452 6431 554 181 262 C ATOM 2398 CA BLEU A 225 10.222 214.511 15.578 0.50 43.05 C ANISOU 2398 CA BLEU A 225 5473 4451 6432 555 180 262 C ATOM 2399 C ALEU A 225 10.060 213.502 14.451 0.50 42.31 C ANISOU 2399 C ALEU A 225 5383 4435 6258 559 91 334 C ATOM 2400 C BLEU A 225 10.091 213.501 14.448 0.50 42.31 C ANISOU 2400 C BLEU A 225 5384 4435 6256 558 91 333 C ATOM 2401 O ALEU A 225 10.079 212.291 14.693 0.50 42.40 O ANISOU 2401 O ALEU A 225 5379 4535 6196 541 74 301 O ATOM 2402 O BLEU A 225 10.174 212.290 14.678 0.50 42.36 O ANISOU 2402 O BLEU A 225 5378 4531 6184 537 75 301 O ATOM 2403 CB ALEU A 225 8.870 214.980 16.109 0.50 47.20 C ANISOU 2403 CB ALEU A 225 5935 4912 7087 615 202 251 C ATOM 2404 CB BLEU A 225 8.846 214.983 16.072 0.50 47.23 C ANISOU 2404 CB BLEU A 225 5938 4916 7093 616 199 254 C ATOM 2405 CG ALEU A 225 8.968 215.627 17.491 0.50 52.12 C ANISOU 2405 CG ALEU A 225 6554 5482 7766 605 301 151 C ATOM 2406 CG BLEU A 225 8.607 214.958 17.590 0.50 51.63 C ANISOU 2406 CG BLEU A 225 6468 5466 7684 612 285 146 C ATOM 2407 CD1ALEU A 225 7.829 216.585 17.733 0.50 54.60 C ANISOU 2407 CD1ALEU A 225 6819 5693 8233 668 333 159 C ATOM 2408 CD1BLEU A 225 9.787 215.491 18.382 0.50 53.96 C ANISOU 2408 CD1BLEU A 225 6817 5742 7943 558 353 69 C ATOM 2409 CD2ALEU A 225 8.997 214.541 18.579 0.50 53.42 C ANISOU 2409 CD2ALEU A 225 6703 5732 7863 579 334 65 C ATOM 2410 CD2BLEU A 225 7.380 215.767 17.948 0.50 54.46 C ANISOU 2410 CD2BLEU A 225 6769 5732 8192 675 320 145 C ATOM 2411 N GLN A 226 9.939 213.972 13.213 1.00 44.95 N ANISOU 2411 N GLN A 226 5743 4736 6600 582 34 430 N ATOM 2412 CA GLN A 226 9.845 213.032 12.104 1.00 48.80 C ANISOU 2412 CA GLN A 226 6246 5297 6997 582 -53 493 C ATOM 2413 C GLN A 226 11.156 212.290 11.900 1.00 42.40 C ANISOU 2413 C GLN A 226 5492 4564 6055 520 -42 471 C ATOM 2414 O GLN A 226 11.140 211.098 11.579 1.00 39.41 O ANISOU 2414 O GLN A 226 5111 4270 5593 508 -87 469 O ATOM 2415 CB GLN A 226 9.419 213.760 10.833 1.00 64.50 C ANISOU 2415 CB GLN A 226 8260 7232 9016 621 -119 605 C ATOM 2416 CG GLN A 226 7.904 213.883 10.713 1.00 85.47 C ANISOU 2416 CG GLN A 226 10845 9852 11777 689 -177 642 C ATOM 2417 CD GLN A 226 7.467 215.008 9.793 1.00104.88 C ANISOU 2417 CD GLN A 226 13322 12223 14306 736 -222 744 C ATOM 2418 OE1 GLN A 226 8.286 215.632 9.121 1.00111.31 O ANISOU 2418 OE1 GLN A 226 14211 13007 15075 716 -213 796 O ATOM 2419 NE2 GLN A 226 6.165 215.273 9.763 1.00111.89 N ANISOU 2419 NE2 GLN A 226 14138 13065 15309 799 -268 777 N ATOM 2420 N LYS A 227 12.293 212.951 12.135 1.00 42.83 N ANISOU 2420 N LYS A 227 5590 4587 6096 479 21 448 N ATOM 2421 CA LYS A 227 13.580 212.265 12.080 1.00 44.29 C ANISOU 2421 CA LYS A 227 5815 4841 6173 420 41 419 C ATOM 2422 C LYS A 227 13.690 211.174 13.139 1.00 40.99 C ANISOU 2422 C LYS A 227 5362 4498 5715 398 59 330 C ATOM 2423 O LYS A 227 14.246 210.094 12.877 1.00 39.22 O ANISOU 2423 O LYS A 227 5151 4355 5395 370 39 321 O ATOM 2424 CB LYS A 227 14.712 213.264 12.265 1.00 49.16 C ANISOU 2424 CB LYS A 227 6470 5400 6809 380 107 404 C ATOM 2425 CG LYS A 227 15.203 213.913 11.003 1.00 55.64 C ANISOU 2425 CG LYS A 227 7350 6182 7610 375 96 496 C ATOM 2426 CD LYS A 227 16.409 214.804 11.316 1.00 58.83 C ANISOU 2426 CD LYS A 227 7782 6531 8040 326 170 469 C ATOM 2427 N GLU A 228 13.233 211.455 14.362 1.00 39.79 N ANISOU 2427 N GLU A 228 5169 4317 5632 408 103 262 N ATOM 2428 CA GLU A 228 13.318 210.455 15.427 1.00 39.51 C ANISOU 2428 CA GLU A 228 5108 4351 5555 388 124 182 C ATOM 2429 C GLU A 228 12.413 209.264 15.146 1.00 37.28 C ANISOU 2429 C GLU A 228 4788 4131 5245 413 69 201 C ATOM 2430 O GLU A 228 12.763 208.130 15.480 1.00 37.18 O ANISOU 2430 O GLU A 228 4772 4195 5160 388 65 165 O ATOM 2431 CB GLU A 228 12.956 211.074 16.784 1.00 44.58 C ANISOU 2431 CB GLU A 228 5724 4943 6271 396 190 107 C ATOM 2432 CG GLU A 228 14.012 211.985 17.353 1.00 49.26 C ANISOU 2432 CG GLU A 228 6352 5491 6874 356 246 58 C ATOM 2433 CD GLU A 228 13.649 212.486 18.743 1.00 49.46 C ANISOU 2433 CD GLU A 228 6361 5475 6956 361 309 -28 C ATOM 2434 OE1 GLU A 228 13.670 211.697 19.719 1.00 52.07 O ANISOU 2434 OE1 GLU A 228 6681 5864 7239 346 328 -93 O ATOM 2435 OE2 GLU A 228 13.332 213.676 18.846 1.00 44.28 O ANISOU 2435 OE2 GLU A 228 5707 4727 6393 381 343 -28 O ATOM 2436 N VAL A 229 11.236 209.507 14.558 1.00 35.58 N ANISOU 2436 N VAL A 229 4542 3882 5096 463 24 257 N ATOM 2437 CA VAL A 229 10.346 208.410 14.174 1.00 37.46 C ANISOU 2437 CA VAL A 229 4741 4175 5317 485 -38 279 C ATOM 2438 C VAL A 229 11.011 207.531 13.119 1.00 38.97 C ANISOU 2438 C VAL A 229 4977 4435 5396 458 -94 316 C ATOM 2439 O VAL A 229 10.979 206.294 13.204 1.00 40.13 O ANISOU 2439 O VAL A 229 5110 4653 5485 443 -116 292 O ATOM 2440 CB VAL A 229 8.997 208.952 13.674 1.00 40.37 C ANISOU 2440 CB VAL A 229 5063 4487 5788 544 -85 336 C ATOM 2441 CG1 VAL A 229 8.158 207.822 13.050 1.00 40.48 C ANISOU 2441 CG1 VAL A 229 5040 4558 5781 560 -167 366 C ATOM 2442 CG2 VAL A 229 8.229 209.622 14.816 1.00 44.63 C ANISOU 2442 CG2 VAL A 229 5548 4964 6445 573 -20 289 C ATOM 2443 N HIS A 230 11.614 208.158 12.107 1.00 40.23 N ANISOU 2443 N HIS A 230 5192 4569 5523 451 -112 374 N ATOM 2444 CA HIS A 230 12.278 207.415 11.035 1.00 40.86 C ANISOU 2444 CA HIS A 230 5324 4708 5492 426 -155 410 C ATOM 2445 C HIS A 230 13.465 206.615 11.570 1.00 37.30 C ANISOU 2445 C HIS A 230 4891 4319 4963 375 -109 348 C ATOM 2446 O HIS A 230 13.680 205.452 11.186 1.00 34.94 O ANISOU 2446 O HIS A 230 4602 4089 4586 359 -139 342 O ATOM 2447 CB HIS A 230 12.720 208.394 9.938 1.00 45.71 C ANISOU 2447 CB HIS A 230 6001 5275 6092 428 -166 486 C ATOM 2448 CG HIS A 230 13.424 207.739 8.792 1.00 53.00 C ANISOU 2448 CG HIS A 230 6987 6253 6898 403 -197 525 C ATOM 2449 ND1 HIS A 230 14.782 207.503 8.792 1.00 56.56 N ANISOU 2449 ND1 HIS A 230 7478 6734 7278 355 -143 498 N ATOM 2450 CD2 HIS A 230 12.958 207.256 7.617 1.00 58.41 C ANISOU 2450 CD2 HIS A 230 7702 6968 7522 420 -276 583 C ATOM 2451 CE1 HIS A 230 15.123 206.900 7.669 1.00 59.98 C ANISOU 2451 CE1 HIS A 230 7964 7211 7614 344 -177 538 C ATOM 2452 NE2 HIS A 230 14.035 206.740 6.938 1.00 61.29 N ANISOU 2452 NE2 HIS A 230 8130 7379 7777 382 -260 588 N ATOM 2453 N ALA A 231 14.215 207.200 12.502 1.00 34.94 N ANISOU 2453 N ALA A 231 4593 3994 4689 350 -39 298 N ATOM 2454 CA ALA A 231 15.329 206.487 13.119 1.00 34.30 C ANISOU 2454 CA ALA A 231 4520 3967 4545 304 -1 238 C ATOM 2455 C ALA A 231 14.851 205.308 13.957 1.00 33.78 C ANISOU 2455 C ALA A 231 4412 3960 4465 307 -8 186 C ATOM 2456 O ALA A 231 15.439 204.215 13.900 1.00 34.95 O ANISOU 2456 O ALA A 231 4567 4172 4540 283 -17 167 O ATOM 2457 CB ALA A 231 16.149 207.463 13.955 1.00 35.91 C ANISOU 2457 CB ALA A 231 4731 4124 4788 278 65 194 C ATOM 2458 N ALA A 232 13.776 205.492 14.733 1.00 33.89 N ANISOU 2458 N ALA A 232 4380 3947 4550 338 0 164 N ATOM 2459 CA ALA A 232 13.270 204.405 15.560 1.00 35.78 C ANISOU 2459 CA ALA A 232 4580 4235 4780 340 2 120 C ATOM 2460 C ALA A 232 12.703 203.289 14.700 1.00 34.36 C ANISOU 2460 C ALA A 232 4388 4103 4564 351 -64 155 C ATOM 2461 O ALA A 232 12.813 202.113 15.056 1.00 33.96 O ANISOU 2461 O ALA A 232 4325 4109 4469 335 -67 125 O ATOM 2462 CB ALA A 232 12.205 204.920 16.526 1.00 37.11 C ANISOU 2462 CB ALA A 232 4703 4358 5040 371 37 91 C ATOM 2463 N LYS A 233 12.109 203.626 13.558 1.00 33.63 N ANISOU 2463 N LYS A 233 4301 3987 4489 376 -121 219 N ATOM 2464 CA LYS A 233 11.656 202.587 12.640 1.00 36.11 C ANISOU 2464 CA LYS A 233 4614 4348 4760 382 -192 249 C ATOM 2465 C LYS A 233 12.836 201.764 12.124 1.00 31.87 C ANISOU 2465 C LYS A 233 4128 3868 4115 343 -194 242 C ATOM 2466 O LYS A 233 12.743 200.534 12.014 1.00 30.91 O ANISOU 2466 O LYS A 233 3997 3798 3950 334 -220 225 O ATOM 2467 CB LYS A 233 10.888 203.212 11.475 1.00 51.04 C ANISOU 2467 CB LYS A 233 6511 6202 6680 415 -261 322 C ATOM 2468 CG LYS A 233 9.503 203.719 11.842 1.00 69.25 C ANISOU 2468 CG LYS A 233 8750 8459 9103 460 -277 333 C ATOM 2469 CD LYS A 233 8.741 204.164 10.593 1.00 86.96 C ANISOU 2469 CD LYS A 233 10999 10675 11369 495 -366 411 C ATOM 2470 CE LYS A 233 7.326 204.612 10.921 1.00101.36 C ANISOU 2470 CE LYS A 233 12741 12448 13323 543 -388 425 C ATOM 2471 NZ LYS A 233 6.585 205.076 9.714 1.00110.44 N ANISOU 2471 NZ LYS A 233 13894 13570 14499 580 -486 506 N ATOM 2472 N SER A 234 13.952 202.428 11.815 1.00 30.56 N ANISOU 2472 N SER A 234 4012 3688 3912 321 -160 253 N ATOM 2473 CA SER A 234 15.133 201.735 11.307 1.00 31.12 C ANISOU 2473 CA SER A 234 4127 3806 3891 287 -151 246 C ATOM 2474 C SER A 234 15.668 200.761 12.340 1.00 31.64 C ANISOU 2474 C SER A 234 4168 3919 3937 263 -117 182 C ATOM 2475 O SER A 234 15.992 199.608 12.026 1.00 33.53 O ANISOU 2475 O SER A 234 4415 4208 4116 249 -133 171 O ATOM 2476 CB SER A 234 16.194 202.756 10.921 1.00 31.93 C ANISOU 2476 CB SER A 234 4276 3874 3980 266 -109 269 C ATOM 2477 OG SER A 234 15.751 203.556 9.871 1.00 35.37 O ANISOU 2477 OG SER A 234 4745 4270 4423 288 -143 337 O ATOM 2478 N LEU A 235 15.775 201.212 13.590 1.00 29.95 N ANISOU 2478 N LEU A 235 3926 3684 3768 258 -69 139 N ATOM 2479 CA LEU A 235 16.286 200.360 14.647 1.00 30.04 C ANISOU 2479 CA LEU A 235 3919 3737 3756 237 -41 82 C ATOM 2480 C LEU A 235 15.316 199.238 14.995 1.00 31.36 C ANISOU 2480 C LEU A 235 4049 3936 3929 253 -66 70 C ATOM 2481 O LEU A 235 15.757 198.133 15.336 1.00 32.18 O ANISOU 2481 O LEU A 235 4149 4086 3990 237 -63 44 O ATOM 2482 CB LEU A 235 16.637 201.217 15.868 1.00 30.99 C ANISOU 2482 CB LEU A 235 4031 3828 3917 227 12 39 C ATOM 2483 CG LEU A 235 17.730 202.226 15.597 1.00 33.96 C ANISOU 2483 CG LEU A 235 4439 4173 4293 203 40 44 C ATOM 2484 CD1 LEU A 235 17.806 203.264 16.726 1.00 34.13 C ANISOU 2484 CD1 LEU A 235 4452 4148 4367 197 83 1 C ATOM 2485 CD2 LEU A 235 19.088 201.559 15.413 1.00 36.75 C ANISOU 2485 CD2 LEU A 235 4809 4571 4584 167 48 31 C ATOM 2486 N ALA A 236 14.007 199.470 14.863 1.00 31.72 N ANISOU 2486 N ALA A 236 4063 3955 4033 285 -93 91 N ATOM 2487 CA ALA A 236 13.042 198.408 15.112 1.00 32.50 C ANISOU 2487 CA ALA A 236 4120 4078 4148 297 -116 82 C ATOM 2488 C ALA A 236 13.133 197.308 14.055 1.00 31.73 C ANISOU 2488 C ALA A 236 4040 4022 3993 288 -171 102 C ATOM 2489 O ALA A 236 12.848 196.146 14.352 1.00 31.71 O ANISOU 2489 O ALA A 236 4014 4052 3982 283 -180 82 O ATOM 2490 CB ALA A 236 11.610 198.972 15.141 1.00 33.87 C ANISOU 2490 CB ALA A 236 4247 4209 4414 334 -134 103 C ATOM 2491 N ILE A 237 13.483 197.662 12.809 1.00 32.47 N ANISOU 2491 N ILE A 237 4178 4113 4049 287 -207 141 N ATOM 2492 CA ILE A 237 13.654 196.667 11.758 1.00 32.13 C ANISOU 2492 CA ILE A 237 4163 4107 3938 277 -254 153 C ATOM 2493 C ILE A 237 14.756 195.684 12.140 1.00 31.34 C ANISOU 2493 C ILE A 237 4077 4049 3781 248 -217 115 C ATOM 2494 O ILE A 237 14.659 194.498 11.826 1.00 31.79 O ANISOU 2494 O ILE A 237 4134 4139 3806 241 -244 103 O ATOM 2495 CB ILE A 237 13.966 197.340 10.407 1.00 34.03 C ANISOU 2495 CB ILE A 237 4462 4334 4134 279 -285 203 C ATOM 2496 CG1 ILE A 237 12.736 198.011 9.811 1.00 37.73 C ANISOU 2496 CG1 ILE A 237 4916 4768 4652 312 -347 250 C ATOM 2497 CG2 ILE A 237 14.512 196.304 9.426 1.00 32.40 C ANISOU 2497 CG2 ILE A 237 4301 4171 3838 261 -311 202 C ATOM 2498 CD1 ILE A 237 13.068 199.026 8.692 1.00 41.22 C ANISOU 2498 CD1 ILE A 237 5420 5183 5059 319 -366 308 C ATOM 2499 N ILE A 238 15.853 196.190 12.731 1.00 28.30 N ANISOU 2499 N ILE A 238 3706 3661 3384 231 -161 96 N ATOM 2500 CA ILE A 238 16.941 195.341 13.231 1.00 28.27 C ANISOU 2500 CA ILE A 238 3707 3694 3340 206 -128 61 C ATOM 2501 C ILE A 238 16.397 194.287 14.196 1.00 28.12 C ANISOU 2501 C ILE A 238 3647 3696 3340 210 -128 30 C ATOM 2502 O ILE A 238 16.800 193.101 14.156 1.00 27.44 O ANISOU 2502 O ILE A 238 3562 3643 3219 199 -131 14 O ATOM 2503 CB ILE A 238 18.030 196.191 13.922 1.00 29.85 C ANISOU 2503 CB ILE A 238 3913 3881 3546 189 -76 43 C ATOM 2504 CG1 ILE A 238 18.592 197.263 12.987 1.00 35.17 C ANISOU 2504 CG1 ILE A 238 4627 4527 4209 182 -67 76 C ATOM 2505 CG2 ILE A 238 19.168 195.294 14.498 1.00 29.88 C ANISOU 2505 CG2 ILE A 238 3913 3924 3516 166 -50 8 C ATOM 2506 CD1 ILE A 238 19.395 196.751 11.918 1.00 41.42 C ANISOU 2506 CD1 ILE A 238 5456 5342 4940 168 -68 91 C ATOM 2507 N VAL A 239 15.553 194.724 15.139 1.00 29.26 N ANISOU 2507 N VAL A 239 3756 3819 3541 224 -113 21 N ATOM 2508 CA VAL A 239 14.958 193.802 16.111 1.00 29.85 C ANISOU 2508 CA VAL A 239 3794 3909 3637 227 -103 -3 C ATOM 2509 C VAL A 239 14.082 192.789 15.393 1.00 29.55 C ANISOU 2509 C VAL A 239 3738 3882 3606 234 -151 11 C ATOM 2510 O VAL A 239 14.088 191.593 15.720 1.00 29.00 O ANISOU 2510 O VAL A 239 3657 3837 3525 225 -149 -6 O ATOM 2511 CB VAL A 239 14.146 194.557 17.183 1.00 31.40 C ANISOU 2511 CB VAL A 239 3960 4076 3895 243 -69 -15 C ATOM 2512 CG1 VAL A 239 13.520 193.550 18.192 1.00 33.58 C ANISOU 2512 CG1 VAL A 239 4203 4368 4188 244 -47 -36 C ATOM 2513 CG2 VAL A 239 15.012 195.560 17.930 1.00 30.00 C ANISOU 2513 CG2 VAL A 239 3804 3884 3708 232 -24 -38 C ATOM 2514 N GLY A 240 13.315 193.249 14.399 1.00 30.88 N ANISOU 2514 N GLY A 240 3905 4031 3796 249 -198 41 N ATOM 2515 CA GLY A 240 12.424 192.342 13.686 1.00 30.25 C ANISOU 2515 CA GLY A 240 3807 3959 3728 253 -256 50 C ATOM 2516 C GLY A 240 13.177 191.250 12.952 1.00 28.76 C ANISOU 2516 C GLY A 240 3655 3804 3468 233 -275 40 C ATOM 2517 O GLY A 240 12.762 190.084 12.955 1.00 28.53 O ANISOU 2517 O GLY A 240 3606 3788 3446 227 -295 25 O ATOM 2518 N LEU A 241 14.279 191.614 12.298 1.00 28.52 N ANISOU 2518 N LEU A 241 3678 3783 3375 223 -265 47 N ATOM 2519 CA LEU A 241 15.116 190.636 11.600 1.00 28.53 C ANISOU 2519 CA LEU A 241 3718 3813 3310 206 -269 34 C ATOM 2520 C LEU A 241 15.843 189.699 12.565 1.00 27.00 C ANISOU 2520 C LEU A 241 3508 3639 3112 193 -224 1 C ATOM 2521 O LEU A 241 16.049 188.520 12.250 1.00 27.16 O ANISOU 2521 O LEU A 241 3535 3676 3107 185 -234 -16 O ATOM 2522 CB LEU A 241 16.100 191.367 10.721 1.00 30.68 C ANISOU 2522 CB LEU A 241 4047 4086 3525 199 -256 52 C ATOM 2523 CG LEU A 241 15.432 192.005 9.489 1.00 36.35 C ANISOU 2523 CG LEU A 241 4798 4789 4225 211 -313 91 C ATOM 2524 CD1 LEU A 241 16.395 192.885 8.775 1.00 40.47 C ANISOU 2524 CD1 LEU A 241 5377 5304 4696 204 -285 116 C ATOM 2525 CD2 LEU A 241 14.901 190.954 8.557 1.00 38.78 C ANISOU 2525 CD2 LEU A 241 5124 5114 4497 208 -372 84 C ATOM 2526 N PHE A 242 16.239 190.189 13.732 1.00 26.03 N ANISOU 2526 N PHE A 242 3366 3513 3012 193 -179 -9 N ATOM 2527 CA PHE A 242 16.766 189.282 14.753 1.00 26.71 C ANISOU 2527 CA PHE A 242 3435 3617 3095 185 -146 -34 C ATOM 2528 C PHE A 242 15.737 188.207 15.084 1.00 26.09 C ANISOU 2528 C PHE A 242 3324 3539 3051 189 -164 -40 C ATOM 2529 O PHE A 242 16.053 186.999 15.113 1.00 25.17 O ANISOU 2529 O PHE A 242 3207 3435 2920 181 -163 -53 O ATOM 2530 CB PHE A 242 17.173 190.088 16.008 1.00 27.29 C ANISOU 2530 CB PHE A 242 3497 3686 3185 184 -104 -44 C ATOM 2531 CG PHE A 242 17.755 189.248 17.099 1.00 26.67 C ANISOU 2531 CG PHE A 242 3408 3628 3096 177 -78 -64 C ATOM 2532 CD1 PHE A 242 16.939 188.576 17.971 1.00 28.69 C ANISOU 2532 CD1 PHE A 242 3638 3883 3378 183 -70 -68 C ATOM 2533 CD2 PHE A 242 19.138 189.058 17.187 1.00 26.39 C ANISOU 2533 CD2 PHE A 242 3388 3611 3027 165 -63 -74 C ATOM 2534 CE1 PHE A 242 17.476 187.775 18.965 1.00 31.96 C ANISOU 2534 CE1 PHE A 242 4051 4316 3777 179 -49 -78 C ATOM 2535 CE2 PHE A 242 19.656 188.263 18.179 1.00 29.36 C ANISOU 2535 CE2 PHE A 242 3754 4005 3396 163 -49 -87 C ATOM 2536 CZ PHE A 242 18.834 187.627 19.047 1.00 32.11 C ANISOU 2536 CZ PHE A 242 4085 4353 3760 170 -44 -87 C ATOM 2537 N ALA A 243 14.484 188.626 15.353 1.00 27.68 N ANISOU 2537 N ALA A 243 3492 3719 3307 201 -176 -30 N ATOM 2538 CA ALA A 243 13.426 187.666 15.682 1.00 28.55 C ANISOU 2538 CA ALA A 243 3561 3823 3463 202 -187 -34 C ATOM 2539 C ALA A 243 13.180 186.694 14.527 1.00 29.56 C ANISOU 2539 C ALA A 243 3697 3956 3577 194 -241 -37 C ATOM 2540 O ALA A 243 13.036 185.482 14.744 1.00 29.46 O ANISOU 2540 O ALA A 243 3671 3946 3576 185 -240 -50 O ATOM 2541 CB ALA A 243 12.130 188.400 16.056 1.00 29.50 C ANISOU 2541 CB ALA A 243 3637 3917 3656 219 -189 -22 C ATOM 2542 N ALEU A 244 13.142 187.209 13.288 0.50 28.63 N ANISOU 2542 N ALEU A 244 3609 3837 3432 197 -287 -24 N ATOM 2543 N BLEU A 244 13.095 187.204 13.296 0.50 28.63 N ANISOU 2543 N BLEU A 244 3608 3837 3435 197 -288 -24 N ATOM 2544 CA ALEU A 244 12.886 186.365 12.124 0.50 29.04 C ANISOU 2544 CA ALEU A 244 3679 3894 3460 187 -344 -32 C ATOM 2545 CA BLEU A 244 12.880 186.311 12.166 0.50 28.85 C ANISOU 2545 CA BLEU A 244 3654 3870 3437 187 -342 -33 C ATOM 2546 C ALEU A 244 13.985 185.329 11.924 0.50 26.71 C ANISOU 2546 C ALEU A 244 3420 3617 3110 173 -321 -56 C ATOM 2547 C BLEU A 244 13.974 185.253 12.099 0.50 26.95 C ANISOU 2547 C BLEU A 244 3445 3647 3147 172 -315 -57 C ATOM 2548 O ALEU A 244 13.722 184.250 11.386 0.50 27.45 O ANISOU 2548 O ALEU A 244 3518 3710 3200 162 -351 -75 O ATOM 2549 O BLEU A 244 13.694 184.074 11.883 0.50 27.53 O ANISOU 2549 O BLEU A 244 3512 3720 3230 162 -334 -77 O ATOM 2550 CB ALEU A 244 12.757 187.217 10.864 0.50 29.76 C ANISOU 2550 CB ALEU A 244 3810 3983 3515 194 -395 -9 C ATOM 2551 CB BLEU A 244 12.830 187.102 10.866 0.50 29.72 C ANISOU 2551 CB BLEU A 244 3806 3979 3506 192 -393 -12 C ATOM 2552 CG ALEU A 244 12.706 186.473 9.519 0.50 29.66 C ANISOU 2552 CG ALEU A 244 3840 3980 3448 182 -454 -20 C ATOM 2553 CG BLEU A 244 11.521 187.812 10.545 0.50 32.36 C ANISOU 2553 CG BLEU A 244 4108 4293 3896 208 -451 14 C ATOM 2554 CD1ALEU A 244 11.376 185.765 9.352 0.50 30.39 C ANISOU 2554 CD1ALEU A 244 3886 4060 3599 179 -518 -29 C ATOM 2555 CD1BLEU A 244 11.706 188.549 9.237 0.50 35.98 C ANISOU 2555 CD1BLEU A 244 4625 4754 4293 213 -499 40 C ATOM 2556 CD2ALEU A 244 12.935 187.442 8.361 0.50 32.30 C ANISOU 2556 CD2ALEU A 244 4234 4318 3722 189 -487 9 C ATOM 2557 CD2BLEU A 244 10.357 186.809 10.446 0.50 32.78 C ANISOU 2557 CD2BLEU A 244 4112 4338 4004 201 -503 -1 C ATOM 2558 N CYS A 245 15.232 185.658 12.291 1.00 26.04 N ANISOU 2558 N CYS A 245 3360 3545 2989 172 -269 -58 N ATOM 2559 CA CYS A 245 16.333 184.734 12.065 1.00 24.33 C ANISOU 2559 CA CYS A 245 3171 3343 2730 162 -245 -79 C ATOM 2560 C CYS A 245 16.498 183.707 13.192 1.00 24.64 C ANISOU 2560 C CYS A 245 3179 3383 2803 160 -213 -92 C ATOM 2561 O CYS A 245 17.012 182.618 12.939 1.00 26.49 O ANISOU 2561 O CYS A 245 3425 3619 3023 154 -207 -111 O ATOM 2562 CB CYS A 245 17.639 185.487 11.901 1.00 25.49 C ANISOU 2562 CB CYS A 245 3351 3502 2833 161 -206 -74 C ATOM 2563 SG CYS A 245 17.784 186.384 10.314 1.00 27.41 S ANISOU 2563 SG CYS A 245 3655 3745 3017 159 -231 -56 S ATOM 2564 N TRP A 246 16.086 184.033 14.417 1.00 23.69 N ANISOU 2564 N TRP A 246 3021 3257 2722 166 -191 -82 N ATOM 2565 CA TRP A 246 16.290 183.132 15.557 1.00 24.55 C ANISOU 2565 CA TRP A 246 3109 3367 2852 165 -158 -87 C ATOM 2566 C TRP A 246 15.055 182.329 15.938 1.00 24.91 C ANISOU 2566 C TRP A 246 3117 3394 2953 162 -168 -85 C ATOM 2567 O TRP A 246 15.185 181.218 16.498 1.00 24.71 O ANISOU 2567 O TRP A 246 3083 3363 2942 159 -149 -89 O ATOM 2568 CB TRP A 246 16.789 183.943 16.773 1.00 24.37 C ANISOU 2568 CB TRP A 246 3081 3354 2826 171 -119 -79 C ATOM 2569 CG TRP A 246 18.226 184.273 16.645 1.00 25.46 C ANISOU 2569 CG TRP A 246 3244 3509 2921 169 -103 -84 C ATOM 2570 CD1 TRP A 246 18.773 185.443 16.212 1.00 27.07 C ANISOU 2570 CD1 TRP A 246 3465 3716 3103 167 -100 -82 C ATOM 2571 CD2 TRP A 246 19.317 183.372 16.866 1.00 24.67 C ANISOU 2571 CD2 TRP A 246 3148 3419 2805 168 -88 -92 C ATOM 2572 NE1 TRP A 246 20.154 185.340 16.174 1.00 26.81 N ANISOU 2572 NE1 TRP A 246 3445 3697 3044 162 -81 -90 N ATOM 2573 CE2 TRP A 246 20.503 184.069 16.569 1.00 24.99 C ANISOU 2573 CE2 TRP A 246 3205 3472 2819 164 -75 -96 C ATOM 2574 CE3 TRP A 246 19.403 182.038 17.279 1.00 25.01 C ANISOU 2574 CE3 TRP A 246 3181 3459 2862 170 -83 -94 C ATOM 2575 CZ2 TRP A 246 21.753 183.471 16.669 1.00 23.19 C ANISOU 2575 CZ2 TRP A 246 2976 3255 2581 165 -60 -103 C ATOM 2576 CZ3 TRP A 246 20.662 181.445 17.393 1.00 23.90 C ANISOU 2576 CZ3 TRP A 246 3045 3327 2709 174 -69 -98 C ATOM 2577 CH2 TRP A 246 21.818 182.176 17.110 1.00 23.18 C ANISOU 2577 CH2 TRP A 246 2963 3250 2595 172 -59 -104 C ATOM 2578 N LEU A 247 13.856 182.856 15.681 1.00 25.19 N ANISOU 2578 N LEU A 247 3128 3416 3028 165 -195 -78 N ATOM 2579 CA LEU A 247 12.655 182.154 16.138 1.00 25.11 C ANISOU 2579 CA LEU A 247 3071 3384 3085 160 -197 -76 C ATOM 2580 C LEU A 247 12.507 180.747 15.568 1.00 26.68 C ANISOU 2580 C LEU A 247 3269 3571 3298 145 -223 -92 C ATOM 2581 O LEU A 247 12.024 179.859 16.299 1.00 28.65 O ANISOU 2581 O LEU A 247 3488 3803 3594 138 -199 -90 O ATOM 2582 CB LEU A 247 11.415 182.995 15.812 1.00 27.98 C ANISOU 2582 CB LEU A 247 3399 3733 3500 167 -229 -65 C ATOM 2583 CG LEU A 247 11.069 184.049 16.866 1.00 34.67 C ANISOU 2583 CG LEU A 247 4223 4574 4375 181 -184 -51 C ATOM 2584 CD1 LEU A 247 9.883 184.907 16.397 1.00 37.93 C ANISOU 2584 CD1 LEU A 247 4597 4967 4847 193 -220 -40 C ATOM 2585 CD2 LEU A 247 10.726 183.420 18.188 1.00 38.14 C ANISOU 2585 CD2 LEU A 247 4635 5006 4850 178 -125 -49 C ATOM 2586 N PRO A 248 12.880 180.461 14.314 1.00 27.80 N ANISOU 2586 N PRO A 248 3445 3717 3400 138 -265 -111 N ATOM 2587 CA PRO A 248 12.718 179.093 13.825 1.00 27.25 C ANISOU 2587 CA PRO A 248 3377 3631 3347 122 -286 -134 C ATOM 2588 C PRO A 248 13.432 178.060 14.670 1.00 26.20 C ANISOU 2588 C PRO A 248 3246 3491 3220 122 -235 -135 C ATOM 2589 O PRO A 248 12.833 177.022 14.986 1.00 27.08 O ANISOU 2589 O PRO A 248 3328 3575 3384 110 -232 -140 O ATOM 2590 CB PRO A 248 13.265 179.173 12.383 1.00 29.83 C ANISOU 2590 CB PRO A 248 3758 3970 3607 118 -328 -156 C ATOM 2591 CG PRO A 248 12.986 180.569 12.000 1.00 30.74 C ANISOU 2591 CG PRO A 248 3879 4098 3702 129 -353 -136 C ATOM 2592 CD PRO A 248 13.225 181.381 13.220 1.00 30.05 C ANISOU 2592 CD PRO A 248 3770 4018 3631 143 -300 -111 C ATOM 2593 N ALEU A 249 14.666 178.324 15.098 0.50 25.17 N ANISOU 2593 N ALEU A 249 3142 3381 3042 134 -197 -128 N ATOM 2594 N BLEU A 249 14.700 178.287 15.041 0.50 25.17 N ANISOU 2594 N BLEU A 249 3143 3380 3040 133 -198 -130 N ATOM 2595 CA ALEU A 249 15.369 177.339 15.903 0.50 26.00 C ANISOU 2595 CA ALEU A 249 3246 3478 3153 137 -158 -124 C ATOM 2596 CA BLEU A 249 15.379 177.338 15.917 0.50 26.00 C ANISOU 2596 CA BLEU A 249 3247 3478 3154 137 -157 -123 C ATOM 2597 C ALEU A 249 14.697 177.151 17.252 0.50 25.24 C ANISOU 2597 C ALEU A 249 3116 3371 3104 138 -125 -97 C ATOM 2598 C BLEU A 249 14.599 177.143 17.203 0.50 25.66 C ANISOU 2598 C BLEU A 249 3168 3422 3160 137 -127 -98 C ATOM 2599 O ALEU A 249 14.619 176.027 17.759 0.50 26.14 O ANISOU 2599 O ALEU A 249 3219 3461 3250 134 -105 -90 O ATOM 2600 O BLEU A 249 14.360 176.011 17.628 0.50 26.26 O ANISOU 2600 O BLEU A 249 3230 3473 3275 131 -111 -93 O ATOM 2601 CB ALEU A 249 16.820 177.770 16.079 0.50 25.70 C ANISOU 2601 CB ALEU A 249 3236 3465 3063 150 -132 -121 C ATOM 2602 CB BLEU A 249 16.796 177.805 16.251 0.50 25.88 C ANISOU 2602 CB BLEU A 249 3256 3488 3087 151 -129 -117 C ATOM 2603 CG ALEU A 249 17.915 176.764 16.362 0.50 25.57 C ANISOU 2603 CG ALEU A 249 3230 3443 3042 158 -107 -123 C ATOM 2604 CG BLEU A 249 17.953 177.360 15.351 0.50 28.39 C ANISOU 2604 CG BLEU A 249 3607 3810 3371 154 -128 -140 C ATOM 2605 CD1ALEU A 249 17.706 175.424 15.657 0.50 27.10 C ANISOU 2605 CD1ALEU A 249 3428 3604 3263 150 -118 -147 C ATOM 2606 CD1BLEU A 249 19.204 178.095 15.805 0.50 25.55 C ANISOU 2606 CD1BLEU A 249 3255 3476 2976 165 -101 -129 C ATOM 2607 CD2ALEU A 249 19.234 177.379 15.930 0.50 26.28 C ANISOU 2607 CD2ALEU A 249 3343 3557 3084 166 -97 -131 C ATOM 2608 CD2BLEU A 249 18.171 175.858 15.408 0.50 26.92 C ANISOU 2608 CD2BLEU A 249 3417 3595 3214 153 -117 -150 C ATOM 2609 N HIS A 250 14.238 178.247 17.868 1.00 24.31 N ANISOU 2609 N HIS A 250 2983 3265 2987 144 -112 -81 N ATOM 2610 CA HIS A 250 13.524 178.142 19.143 1.00 23.69 C ANISOU 2610 CA HIS A 250 2877 3176 2947 145 -71 -57 C ATOM 2611 C HIS A 250 12.215 177.355 18.994 1.00 24.08 C ANISOU 2611 C HIS A 250 2885 3191 3073 129 -78 -58 C ATOM 2612 O HIS A 250 11.854 176.534 19.839 1.00 23.68 O ANISOU 2612 O HIS A 250 2818 3119 3059 124 -41 -40 O ATOM 2613 CB HIS A 250 13.234 179.558 19.688 1.00 23.72 C ANISOU 2613 CB HIS A 250 2876 3197 2941 154 -53 -49 C ATOM 2614 CG HIS A 250 14.444 180.303 20.148 1.00 24.97 C ANISOU 2614 CG HIS A 250 3069 3383 3034 165 -38 -48 C ATOM 2615 ND1 HIS A 250 15.161 179.927 21.261 1.00 24.94 N ANISOU 2615 ND1 HIS A 250 3083 3391 3002 170 -5 -34 N ATOM 2616 CD2 HIS A 250 15.008 181.451 19.712 1.00 26.67 C ANISOU 2616 CD2 HIS A 250 3303 3617 3214 170 -52 -57 C ATOM 2617 CE1 HIS A 250 16.140 180.790 21.475 1.00 24.90 C ANISOU 2617 CE1 HIS A 250 3102 3411 2948 176 -5 -39 C ATOM 2618 NE2 HIS A 250 16.090 181.706 20.526 1.00 26.21 N ANISOU 2618 NE2 HIS A 250 3269 3580 3112 175 -30 -54 N ATOM 2619 N ILE A 251 11.470 177.627 17.945 1.00 25.01 N ANISOU 2619 N ILE A 251 2984 3301 3219 121 -128 -75 N ATOM 2620 CA ILE A 251 10.196 176.938 17.728 1.00 25.64 C ANISOU 2620 CA ILE A 251 3015 3347 3382 103 -147 -80 C ATOM 2621 C ILE A 251 10.412 175.457 17.498 1.00 25.53 C ANISOU 2621 C ILE A 251 3008 3306 3387 87 -150 -93 C ATOM 2622 O ILE A 251 9.689 174.627 18.040 1.00 27.11 O ANISOU 2622 O ILE A 251 3172 3473 3656 72 -125 -83 O ATOM 2623 CB ILE A 251 9.442 177.621 16.566 1.00 26.44 C ANISOU 2623 CB ILE A 251 3097 3449 3501 99 -216 -97 C ATOM 2624 CG1 ILE A 251 8.960 178.990 17.026 1.00 29.06 C ANISOU 2624 CG1 ILE A 251 3406 3791 3844 117 -201 -77 C ATOM 2625 CG2 ILE A 251 8.248 176.760 16.126 1.00 26.24 C ANISOU 2625 CG2 ILE A 251 3020 3387 3563 76 -254 -110 C ATOM 2626 CD1 ILE A 251 8.590 179.900 15.854 1.00 32.00 C ANISOU 2626 CD1 ILE A 251 3778 4171 4210 123 -272 -84 C ATOM 2627 N ILE A 252 11.442 175.087 16.734 1.00 24.17 N ANISOU 2627 N ILE A 252 2881 3143 3159 89 -173 -115 N ATOM 2628 CA ILE A 252 11.775 173.679 16.561 1.00 24.34 C ANISOU 2628 CA ILE A 252 2914 3135 3200 78 -168 -130 C ATOM 2629 C ILE A 252 12.093 173.031 17.908 1.00 24.37 C ANISOU 2629 C ILE A 252 2914 3125 3222 85 -103 -95 C ATOM 2630 O ILE A 252 11.606 171.947 18.217 1.00 24.86 O ANISOU 2630 O ILE A 252 2955 3146 3345 70 -86 -89 O ATOM 2631 CB ILE A 252 12.950 173.525 15.581 1.00 26.36 C ANISOU 2631 CB ILE A 252 3223 3405 3389 84 -189 -160 C ATOM 2632 CG1 ILE A 252 12.506 173.928 14.183 1.00 28.22 C ANISOU 2632 CG1 ILE A 252 3471 3646 3604 73 -255 -194 C ATOM 2633 CG2 ILE A 252 13.534 172.089 15.616 1.00 27.85 C ANISOU 2633 CG2 ILE A 252 3426 3558 3597 81 -168 -172 C ATOM 2634 CD1 ILE A 252 13.656 173.943 13.156 1.00 30.02 C ANISOU 2634 CD1 ILE A 252 3759 3892 3754 79 -266 -224 C ATOM 2635 N ASN A 253 12.897 173.687 18.735 1.00 25.40 N ANISOU 2635 N ASN A 253 3066 3286 3298 106 -70 -69 N ATOM 2636 CA ASN A 253 13.174 173.144 20.065 1.00 26.39 C ANISOU 2636 CA ASN A 253 3196 3404 3429 114 -15 -31 C ATOM 2637 C ASN A 253 11.896 172.940 20.874 1.00 25.65 C ANISOU 2637 C ASN A 253 3062 3283 3400 101 21 -6 C ATOM 2638 O ASN A 253 11.777 171.963 21.600 1.00 26.41 O ANISOU 2638 O ASN A 253 3156 3350 3529 96 60 21 O ATOM 2639 CB ASN A 253 14.157 174.061 20.812 1.00 26.81 C ANISOU 2639 CB ASN A 253 3277 3499 3408 136 4 -12 C ATOM 2640 CG ASN A 253 15.593 173.984 20.246 1.00 25.33 C ANISOU 2640 CG ASN A 253 3123 3330 3170 150 -17 -28 C ATOM 2641 OD1 ASN A 253 15.946 173.048 19.525 1.00 26.04 O ANISOU 2641 OD1 ASN A 253 3219 3397 3279 147 -31 -47 O ATOM 2642 ND2 ASN A 253 16.407 174.983 20.553 1.00 23.95 N ANISOU 2642 ND2 ASN A 253 2967 3194 2940 164 -16 -24 N ATOM 2643 N CYS A 254 10.935 173.866 20.788 1.00 24.60 N ANISOU 2643 N CYS A 254 2897 3159 3291 96 16 -11 N ATOM 2644 CA CYS A 254 9.644 173.667 21.444 1.00 26.28 C ANISOU 2644 CA CYS A 254 3061 3342 3581 81 55 8 C ATOM 2645 C CYS A 254 8.937 172.400 20.973 1.00 26.50 C ANISOU 2645 C CYS A 254 3054 3319 3695 55 42 -2 C ATOM 2646 O CYS A 254 8.336 171.692 21.794 1.00 29.72 O ANISOU 2646 O CYS A 254 3438 3693 4160 42 96 26 O ATOM 2647 CB CYS A 254 8.753 174.911 21.244 1.00 27.83 C ANISOU 2647 CB CYS A 254 3220 3551 3801 84 43 -2 C ATOM 2648 SG CYS A 254 9.291 176.376 22.168 1.00 30.31 S ANISOU 2648 SG CYS A 254 3568 3911 4039 111 83 13 S ATOM 2649 N PHE A 255 8.959 172.098 19.659 1.00 26.03 N ANISOU 2649 N PHE A 255 2994 3251 3647 43 -27 -43 N ATOM 2650 CA PHE A 255 8.364 170.842 19.194 1.00 27.25 C ANISOU 2650 CA PHE A 255 3120 3353 3881 14 -44 -61 C ATOM 2651 C PHE A 255 9.109 169.635 19.743 1.00 28.45 C ANISOU 2651 C PHE A 255 3303 3476 4031 15 -2 -41 C ATOM 2652 O PHE A 255 8.489 168.651 20.178 1.00 30.59 O ANISOU 2652 O PHE A 255 3546 3697 4381 -5 31 -25 O ATOM 2653 CB PHE A 255 8.337 170.783 17.659 1.00 27.39 C ANISOU 2653 CB PHE A 255 3143 3371 3893 1 -130 -115 C ATOM 2654 CG PHE A 255 7.150 171.507 17.045 1.00 28.82 C ANISOU 2654 CG PHE A 255 3272 3555 4123 -12 -183 -131 C ATOM 2655 CD1 PHE A 255 5.960 170.825 16.850 1.00 31.03 C ANISOU 2655 CD1 PHE A 255 3490 3789 4511 -44 -204 -144 C ATOM 2656 CD2 PHE A 255 7.210 172.860 16.741 1.00 29.74 C ANISOU 2656 CD2 PHE A 255 3397 3715 4188 8 -211 -129 C ATOM 2657 CE1 PHE A 255 4.869 171.484 16.330 1.00 31.53 C ANISOU 2657 CE1 PHE A 255 3497 3854 4629 -54 -259 -156 C ATOM 2658 CE2 PHE A 255 6.126 173.512 16.231 1.00 32.11 C ANISOU 2658 CE2 PHE A 255 3646 4014 4540 1 -262 -138 C ATOM 2659 CZ PHE A 255 4.962 172.838 16.031 1.00 31.37 C ANISOU 2659 CZ PHE A 255 3487 3879 4553 -28 -288 -150 C ATOM 2660 N THR A 256 10.445 169.675 19.715 1.00 26.11 N ANISOU 2660 N THR A 256 3061 3206 3653 40 -3 -41 N ATOM 2661 CA THR A 256 11.210 168.553 20.246 1.00 25.29 C ANISOU 2661 CA THR A 256 2986 3073 3552 48 32 -18 C ATOM 2662 C THR A 256 10.889 168.313 21.712 1.00 26.55 C ANISOU 2662 C THR A 256 3139 3220 3731 51 102 43 C ATOM 2663 O THR A 256 10.711 167.162 22.140 1.00 27.98 O ANISOU 2663 O THR A 256 3315 3349 3967 40 136 67 O ATOM 2664 CB THR A 256 12.701 168.837 20.051 1.00 25.72 C ANISOU 2664 CB THR A 256 3089 3163 3519 77 19 -23 C ATOM 2665 OG1 THR A 256 12.965 168.962 18.651 1.00 25.84 O ANISOU 2665 OG1 THR A 256 3117 3186 3515 72 -35 -79 O ATOM 2666 CG2 THR A 256 13.571 167.724 20.619 1.00 27.65 C ANISOU 2666 CG2 THR A 256 3358 3378 3769 92 50 5 C ATOM 2667 N PHE A 257 10.822 169.390 22.509 1.00 27.53 N ANISOU 2667 N PHE A 257 3267 3386 3807 65 129 68 N ATOM 2668 CA PHE A 257 10.582 169.290 23.955 1.00 28.59 C ANISOU 2668 CA PHE A 257 3409 3516 3937 70 201 124 C ATOM 2669 C PHE A 257 9.139 168.938 24.313 1.00 28.03 C ANISOU 2669 C PHE A 257 3286 3402 3961 42 247 139 C ATOM 2670 O PHE A 257 8.890 168.048 25.138 1.00 28.57 O ANISOU 2670 O PHE A 257 3359 3432 4066 34 304 183 O ATOM 2671 CB PHE A 257 10.968 170.625 24.604 1.00 29.55 C ANISOU 2671 CB PHE A 257 3557 3697 3974 92 213 134 C ATOM 2672 CG PHE A 257 10.908 170.633 26.080 1.00 30.85 C ANISOU 2672 CG PHE A 257 3748 3867 4107 101 282 186 C ATOM 2673 CD1 PHE A 257 11.679 169.755 26.822 1.00 30.96 C ANISOU 2673 CD1 PHE A 257 3804 3869 4089 113 303 230 C ATOM 2674 CD2 PHE A 257 10.102 171.532 26.742 1.00 34.14 C ANISOU 2674 CD2 PHE A 257 4152 4299 4519 99 328 193 C ATOM 2675 CE1 PHE A 257 11.633 169.790 28.225 1.00 34.58 C ANISOU 2675 CE1 PHE A 257 4300 4337 4502 121 364 282 C ATOM 2676 CE2 PHE A 257 10.056 171.557 28.133 1.00 38.16 C ANISOU 2676 CE2 PHE A 257 4697 4816 4986 106 398 239 C ATOM 2677 CZ PHE A 257 10.823 170.673 28.863 1.00 38.99 C ANISOU 2677 CZ PHE A 257 4852 4913 5049 116 414 284 C ATOM 2678 N PHE A 258 8.174 169.667 23.773 1.00 27.58 N ANISOU 2678 N PHE A 258 3179 3351 3949 29 226 109 N ATOM 2679 CA PHE A 258 6.784 169.543 24.192 1.00 29.22 C ANISOU 2679 CA PHE A 258 3326 3523 4252 5 275 124 C ATOM 2680 C PHE A 258 6.015 168.441 23.463 1.00 32.60 C ANISOU 2680 C PHE A 258 3703 3890 4795 -31 251 103 C ATOM 2681 O PHE A 258 4.938 168.052 23.927 1.00 33.86 O ANISOU 2681 O PHE A 258 3809 4007 5048 -55 302 123 O ATOM 2682 CB PHE A 258 6.044 170.872 23.979 1.00 28.93 C ANISOU 2682 CB PHE A 258 3250 3516 4227 9 263 103 C ATOM 2683 CG PHE A 258 6.466 171.976 24.919 1.00 29.84 C ANISOU 2683 CG PHE A 258 3405 3679 4255 37 308 124 C ATOM 2684 CD1 PHE A 258 6.384 171.798 26.289 1.00 32.05 C ANISOU 2684 CD1 PHE A 258 3710 3954 4514 42 399 170 C ATOM 2685 CD2 PHE A 258 6.878 173.195 24.435 1.00 28.28 C ANISOU 2685 CD2 PHE A 258 3221 3526 3998 57 262 96 C ATOM 2686 CE1 PHE A 258 6.711 172.822 27.157 1.00 30.89 C ANISOU 2686 CE1 PHE A 258 3603 3849 4285 64 438 181 C ATOM 2687 CE2 PHE A 258 7.218 174.223 25.293 1.00 29.51 C ANISOU 2687 CE2 PHE A 258 3412 3719 4081 79 302 108 C ATOM 2688 CZ PHE A 258 7.128 174.036 26.663 1.00 30.36 C ANISOU 2688 CZ PHE A 258 3546 3824 4166 82 389 147 C ATOM 2689 N CYS A 259 6.511 167.916 22.341 1.00 33.77 N ANISOU 2689 N CYS A 259 3863 4027 4940 -37 178 61 N ATOM 2690 CA CYS A 259 5.772 166.903 21.585 1.00 35.72 C ANISOU 2690 CA CYS A 259 4064 4215 5293 -75 146 31 C ATOM 2691 C CYS A 259 6.601 165.633 21.430 1.00 37.46 C ANISOU 2691 C CYS A 259 4327 4395 5510 -77 146 30 C ATOM 2692 O CYS A 259 7.143 165.350 20.345 1.00 36.92 O ANISOU 2692 O CYS A 259 4282 4326 5421 -78 80 -20 O ATOM 2693 CB CYS A 259 5.324 167.416 20.217 1.00 36.06 C ANISOU 2693 CB CYS A 259 4076 4272 5354 -88 51 -30 C ATOM 2694 SG CYS A 259 4.177 166.204 19.426 1.00 37.96 S ANISOU 2694 SG CYS A 259 4247 4434 5740 -142 9 -71 S ATOM 2695 N PRO A 260 6.673 164.802 22.470 1.00 43.42 N ANISOU 2695 N PRO A 260 5094 5111 6292 -78 220 84 N ATOM 2696 CA PRO A 260 7.422 163.536 22.330 1.00 47.61 C ANISOU 2696 CA PRO A 260 5661 5593 6835 -78 221 86 C ATOM 2697 C PRO A 260 6.781 162.547 21.372 1.00 47.40 C ANISOU 2697 C PRO A 260 5596 5500 6915 -119 182 36 C ATOM 2698 O PRO A 260 7.459 161.600 20.961 1.00 49.33 O ANISOU 2698 O PRO A 260 5872 5705 7167 -117 169 18 O ATOM 2699 CB PRO A 260 7.457 162.976 23.759 1.00 52.79 C ANISOU 2699 CB PRO A 260 6336 6221 7500 -70 313 167 C ATOM 2700 CG PRO A 260 6.258 163.553 24.434 1.00 52.98 C ANISOU 2700 CG PRO A 260 6311 6250 7569 -88 367 192 C ATOM 2701 CD PRO A 260 6.081 164.943 23.813 1.00 47.55 C ANISOU 2701 CD PRO A 260 5604 5628 6835 -78 312 147 C ATOM 2702 N ASP A 261 5.515 162.723 21.014 1.00 45.48 N ANISOU 2702 N ASP A 261 5283 5239 6759 -155 164 10 N ATOM 2703 CA ASP A 261 4.861 161.899 19.999 1.00 50.22 C ANISOU 2703 CA ASP A 261 5843 5781 7459 -198 109 -49 C ATOM 2704 C ASP A 261 5.186 162.334 18.572 1.00 41.23 C ANISOU 2704 C ASP A 261 4724 4676 6264 -197 5 -126 C ATOM 2705 O ASP A 261 4.860 161.614 17.624 1.00 40.25 O ANISOU 2705 O ASP A 261 4587 4508 6198 -230 -51 -186 O ATOM 2706 CB ASP A 261 3.338 161.942 20.196 1.00 69.56 C ANISOU 2706 CB ASP A 261 8200 8197 10033 -239 123 -45 C ATOM 2707 CG ASP A 261 2.870 161.103 21.371 1.00 87.67 C ANISOU 2707 CG ASP A 261 10470 10427 12413 -257 228 20 C ATOM 2708 OD1 ASP A 261 3.474 160.040 21.623 1.00 96.39 O ANISOU 2708 OD1 ASP A 261 11616 11482 13526 -257 260 40 O ATOM 2709 OD2 ASP A 261 1.892 161.503 22.040 1.00 92.02 O ANISOU 2709 OD2 ASP A 261 10962 10975 13026 -270 281 53 O ATOM 2710 N CYS A 262 5.752 163.513 18.399 1.00 37.49 N ANISOU 2710 N CYS A 262 4282 4279 5682 -162 -21 -128 N ATOM 2711 CA CYS A 262 6.091 164.043 17.090 1.00 37.55 C ANISOU 2711 CA CYS A 262 4318 4327 5624 -158 -111 -191 C ATOM 2712 C CYS A 262 7.452 163.545 16.656 1.00 37.46 C ANISOU 2712 C CYS A 262 4382 4317 5536 -135 -115 -213 C ATOM 2713 O CYS A 262 8.388 163.469 17.456 1.00 39.78 O ANISOU 2713 O CYS A 262 4713 4622 5781 -103 -57 -168 O ATOM 2714 CB CYS A 262 6.126 165.571 17.133 1.00 36.45 C ANISOU 2714 CB CYS A 262 4180 4264 5407 -130 -128 -176 C ATOM 2715 SG CYS A 262 4.570 166.393 17.452 1.00 38.55 S ANISOU 2715 SG CYS A 262 4353 4533 5759 -148 -132 -159 S ATOM 2716 N SER A 263 7.577 163.234 15.374 1.00 34.61 N ANISOU 2716 N SER A 263 4045 3946 5161 -151 -184 -284 N ATOM 2717 CA SER A 263 8.893 162.942 14.832 1.00 34.25 C ANISOU 2717 CA SER A 263 4070 3908 5034 -126 -185 -312 C ATOM 2718 C SER A 263 9.784 164.153 15.028 1.00 30.93 C ANISOU 2718 C SER A 263 3685 3565 4500 -83 -175 -284 C ATOM 2719 O SER A 263 9.317 165.285 14.978 1.00 31.26 O ANISOU 2719 O SER A 263 3708 3657 4512 -80 -202 -275 O ATOM 2720 CB SER A 263 8.779 162.591 13.348 1.00 44.17 C ANISOU 2720 CB SER A 263 5352 5150 6279 -152 -262 -399 C ATOM 2721 OG SER A 263 8.249 161.298 13.241 1.00 53.88 O ANISOU 2721 OG SER A 263 6561 6298 7613 -188 -261 -429 O ATOM 2722 N HIS A 264 11.071 163.911 15.271 1.00 29.55 N ANISOU 2722 N HIS A 264 3557 3397 4272 -50 -136 -270 N ATOM 2723 CA HIS A 264 12.019 165.006 15.371 1.00 31.62 C ANISOU 2723 CA HIS A 264 3852 3729 4432 -14 -130 -251 C ATOM 2724 C HIS A 264 12.102 165.710 14.027 1.00 31.40 C ANISOU 2724 C HIS A 264 3854 3739 4338 -19 -192 -308 C ATOM 2725 O HIS A 264 12.036 165.065 12.980 1.00 30.58 O ANISOU 2725 O HIS A 264 3771 3605 4240 -38 -228 -368 O ATOM 2726 CB HIS A 264 13.391 164.458 15.762 1.00 32.13 C ANISOU 2726 CB HIS A 264 3953 3784 4469 20 -84 -232 C ATOM 2727 CG HIS A 264 14.341 165.496 16.275 1.00 30.64 C ANISOU 2727 CG HIS A 264 3783 3660 4198 56 -66 -196 C ATOM 2728 ND1 HIS A 264 14.905 166.462 15.462 1.00 28.35 N ANISOU 2728 ND1 HIS A 264 3521 3422 3828 67 -94 -226 N ATOM 2729 CD2 HIS A 264 14.836 165.713 17.519 1.00 31.45 C ANISOU 2729 CD2 HIS A 264 3883 3780 4286 81 -24 -133 C ATOM 2730 CE1 HIS A 264 15.712 167.220 16.182 1.00 29.18 C ANISOU 2730 CE1 HIS A 264 3633 3572 3883 95 -70 -185 C ATOM 2731 NE2 HIS A 264 15.685 166.791 17.432 1.00 30.28 N ANISOU 2731 NE2 HIS A 264 3755 3693 4056 105 -32 -131 N ATOM 2732 N ALA A 265 12.194 167.030 14.055 1.00 31.71 N ANISOU 2732 N ALA A 265 3896 3840 4312 -3 -205 -289 N ATOM 2733 CA ALA A 265 12.505 167.776 12.841 1.00 32.72 C ANISOU 2733 CA ALA A 265 4064 4008 4360 0 -255 -331 C ATOM 2734 C ALA A 265 13.657 167.111 12.084 1.00 30.78 C ANISOU 2734 C ALA A 265 3875 3749 4070 10 -242 -373 C ATOM 2735 O ALA A 265 14.661 166.705 12.693 1.00 28.24 O ANISOU 2735 O ALA A 265 3563 3419 3748 35 -187 -350 O ATOM 2736 CB ALA A 265 12.873 169.222 13.178 1.00 33.83 C ANISOU 2736 CB ALA A 265 4210 4211 4434 24 -247 -294 C ATOM 2737 N PRO A 266 13.577 167.017 10.764 1.00 31.61 N ANISOU 2737 N PRO A 266 4020 3854 4137 -6 -289 -434 N ATOM 2738 CA PRO A 266 14.638 166.342 10.019 1.00 32.36 C ANISOU 2738 CA PRO A 266 4171 3932 4194 3 -266 -481 C ATOM 2739 C PRO A 266 15.939 167.127 10.032 1.00 31.19 C ANISOU 2739 C PRO A 266 4054 3831 3967 38 -225 -461 C ATOM 2740 O PRO A 266 15.986 168.351 10.220 1.00 30.03 O ANISOU 2740 O PRO A 266 3903 3736 3773 49 -232 -426 O ATOM 2741 CB PRO A 266 14.069 166.219 8.596 1.00 34.39 C ANISOU 2741 CB PRO A 266 4468 4183 4414 -27 -334 -551 C ATOM 2742 CG PRO A 266 13.037 167.215 8.497 1.00 36.59 C ANISOU 2742 CG PRO A 266 4720 4498 4685 -40 -396 -531 C ATOM 2743 CD PRO A 266 12.492 167.475 9.888 1.00 33.20 C ANISOU 2743 CD PRO A 266 4218 4067 4330 -34 -369 -464 C ATOM 2744 N LEU A 267 17.023 166.381 9.834 1.00 32.02 N ANISOU 2744 N LEU A 267 4187 3910 4068 56 -178 -484 N ATOM 2745 CA LEU A 267 18.354 166.975 9.932 1.00 34.22 C ANISOU 2745 CA LEU A 267 4484 4226 4294 89 -131 -464 C ATOM 2746 C LEU A 267 18.544 168.121 8.948 1.00 31.00 C ANISOU 2746 C LEU A 267 4118 3869 3789 87 -152 -482 C ATOM 2747 O LEU A 267 19.179 169.137 9.279 1.00 30.71 O ANISOU 2747 O LEU A 267 4078 3878 3714 105 -132 -445 O ATOM 2748 CB LEU A 267 19.413 165.898 9.716 1.00 44.98 C ANISOU 2748 CB LEU A 267 5866 5545 5681 108 -78 -495 C ATOM 2749 CG LEU A 267 20.860 166.326 9.866 1.00 57.00 C ANISOU 2749 CG LEU A 267 7392 7094 7171 143 -25 -476 C ATOM 2750 CD1 LEU A 267 21.660 165.155 10.413 1.00 60.69 C ANISOU 2750 CD1 LEU A 267 7840 7508 7712 169 24 -471 C ATOM 2751 CD2 LEU A 267 21.438 166.788 8.527 1.00 64.17 C ANISOU 2751 CD2 LEU A 267 8359 8026 7997 141 -13 -528 C ATOM 2752 N TRP A 268 18.022 167.997 7.728 1.00 29.08 N ANISOU 2752 N TRP A 268 3922 3622 3504 63 -195 -538 N ATOM 2753 CA TRP A 268 18.222 169.098 6.784 1.00 29.70 C ANISOU 2753 CA TRP A 268 4051 3750 3484 62 -214 -546 C ATOM 2754 C TRP A 268 17.586 170.387 7.292 1.00 28.86 C ANISOU 2754 C TRP A 268 3911 3686 3367 62 -250 -491 C ATOM 2755 O TRP A 268 18.125 171.492 7.076 1.00 27.71 O ANISOU 2755 O TRP A 268 3787 3583 3159 75 -237 -468 O ATOM 2756 CB TRP A 268 17.671 168.751 5.397 1.00 30.89 C ANISOU 2756 CB TRP A 268 4264 3890 3582 35 -265 -613 C ATOM 2757 CG TRP A 268 16.173 168.553 5.299 1.00 33.34 C ANISOU 2757 CG TRP A 268 4551 4186 3932 3 -351 -625 C ATOM 2758 CD1 TRP A 268 15.497 167.372 5.336 1.00 35.92 C ANISOU 2758 CD1 TRP A 268 4858 4458 4331 -21 -375 -663 C ATOM 2759 CD2 TRP A 268 15.185 169.572 5.094 1.00 34.32 C ANISOU 2759 CD2 TRP A 268 4664 4346 4032 -9 -425 -599 C ATOM 2760 NE1 TRP A 268 14.143 167.598 5.179 1.00 35.89 N ANISOU 2760 NE1 TRP A 268 4826 4456 4353 -49 -461 -663 N ATOM 2761 CE2 TRP A 268 13.931 168.939 5.030 1.00 35.21 C ANISOU 2761 CE2 TRP A 268 4744 4425 4210 -40 -494 -623 C ATOM 2762 CE3 TRP A 268 15.246 170.960 4.950 1.00 37.73 C ANISOU 2762 CE3 TRP A 268 5107 4828 4400 4 -440 -556 C ATOM 2763 CZ2 TRP A 268 12.743 169.649 4.842 1.00 37.69 C ANISOU 2763 CZ2 TRP A 268 5030 4758 4531 -55 -578 -606 C ATOM 2764 CZ3 TRP A 268 14.078 171.662 4.764 1.00 40.20 C ANISOU 2764 CZ3 TRP A 268 5398 5158 4717 -9 -521 -538 C ATOM 2765 CH2 TRP A 268 12.838 171.010 4.715 1.00 40.12 C ANISOU 2765 CH2 TRP A 268 5351 5118 4777 -37 -591 -562 C ATOM 2766 N LEU A 269 16.448 170.269 7.971 1.00 28.49 N ANISOU 2766 N LEU A 269 3811 3625 3387 48 -289 -469 N ATOM 2767 CA LEU A 269 15.765 171.443 8.496 1.00 27.90 C ANISOU 2767 CA LEU A 269 3700 3584 3315 51 -318 -419 C ATOM 2768 C LEU A 269 16.499 172.007 9.696 1.00 25.36 C ANISOU 2768 C LEU A 269 3347 3283 3006 76 -261 -366 C ATOM 2769 O LEU A 269 16.534 173.227 9.890 1.00 26.29 O ANISOU 2769 O LEU A 269 3461 3438 3092 86 -264 -333 O ATOM 2770 CB LEU A 269 14.336 171.078 8.859 1.00 32.45 C ANISOU 2770 CB LEU A 269 4225 4135 3970 28 -367 -416 C ATOM 2771 CG LEU A 269 13.486 172.228 9.413 1.00 36.31 C ANISOU 2771 CG LEU A 269 4669 4651 4478 31 -394 -369 C ATOM 2772 CD1 LEU A 269 13.332 173.349 8.404 1.00 39.60 C ANISOU 2772 CD1 LEU A 269 5123 5103 4819 32 -446 -371 C ATOM 2773 CD2 LEU A 269 12.113 171.723 9.825 1.00 37.12 C ANISOU 2773 CD2 LEU A 269 4708 4720 4676 8 -429 -367 C ATOM 2774 N MET A 270 17.084 171.130 10.534 1.00 24.43 N ANISOU 2774 N MET A 270 3207 3139 2936 88 -211 -356 N ATOM 2775 CA MET A 270 17.868 171.635 11.649 1.00 25.30 C ANISOU 2775 CA MET A 270 3293 3270 3049 112 -166 -309 C ATOM 2776 C MET A 270 18.984 172.540 11.145 1.00 24.41 C ANISOU 2776 C MET A 270 3213 3195 2866 127 -144 -310 C ATOM 2777 O MET A 270 19.238 173.610 11.709 1.00 23.93 O ANISOU 2777 O MET A 270 3139 3167 2786 137 -136 -275 O ATOM 2778 CB MET A 270 18.487 170.502 12.485 1.00 26.55 C ANISOU 2778 CB MET A 270 3433 3395 3262 126 -122 -297 C ATOM 2779 CG MET A 270 17.520 169.569 13.163 1.00 27.82 C ANISOU 2779 CG MET A 270 3559 3512 3498 113 -128 -285 C ATOM 2780 SD MET A 270 16.337 170.411 14.249 1.00 27.55 S ANISOU 2780 SD MET A 270 3479 3498 3490 104 -141 -235 S ATOM 2781 CE MET A 270 17.430 171.237 15.350 1.00 27.78 C ANISOU 2781 CE MET A 270 3507 3569 3481 134 -101 -187 C ATOM 2782 N TYR A 271 19.712 172.089 10.144 1.00 24.60 N ANISOU 2782 N TYR A 271 3280 3211 2857 128 -127 -351 N ATOM 2783 CA TYR A 271 20.867 172.839 9.654 1.00 25.28 C ANISOU 2783 CA TYR A 271 3395 3326 2885 141 -92 -352 C ATOM 2784 C TYR A 271 20.453 174.076 8.873 1.00 25.61 C ANISOU 2784 C TYR A 271 3469 3401 2860 130 -124 -348 C ATOM 2785 O TYR A 271 21.181 175.063 8.894 1.00 26.29 O ANISOU 2785 O TYR A 271 3561 3516 2912 139 -99 -327 O ATOM 2786 CB TYR A 271 21.799 171.913 8.846 1.00 28.65 C ANISOU 2786 CB TYR A 271 3856 3728 3302 148 -50 -399 C ATOM 2787 CG TYR A 271 22.610 171.088 9.835 1.00 33.05 C ANISOU 2787 CG TYR A 271 4370 4260 3927 171 -7 -382 C ATOM 2788 CD1 TYR A 271 23.634 171.676 10.560 1.00 35.60 C ANISOU 2788 CD1 TYR A 271 4663 4607 4257 192 25 -346 C ATOM 2789 CD2 TYR A 271 22.295 169.762 10.120 1.00 35.94 C ANISOU 2789 CD2 TYR A 271 4722 4577 4355 171 -7 -397 C ATOM 2790 CE1 TYR A 271 24.362 170.952 11.497 1.00 39.00 C ANISOU 2790 CE1 TYR A 271 5052 5016 4748 215 52 -325 C ATOM 2791 CE2 TYR A 271 23.026 169.035 11.076 1.00 39.23 C ANISOU 2791 CE2 TYR A 271 5100 4969 4835 196 27 -371 C ATOM 2792 CZ TYR A 271 24.051 169.652 11.748 1.00 40.10 C ANISOU 2792 CZ TYR A 271 5183 5108 4944 219 52 -334 C ATOM 2793 OH TYR A 271 24.777 168.987 12.697 1.00 40.18 O ANISOU 2793 OH TYR A 271 5156 5098 5014 245 74 -304 O ATOM 2794 N LEU A 272 19.300 174.050 8.203 1.00 27.05 N ANISOU 2794 N LEU A 272 3671 3579 3027 111 -183 -366 N ATOM 2795 CA LEU A 272 18.791 175.263 7.579 1.00 27.22 C ANISOU 2795 CA LEU A 272 3718 3630 2994 104 -224 -351 C ATOM 2796 C LEU A 272 18.455 176.300 8.646 1.00 26.29 C ANISOU 2796 C LEU A 272 3551 3530 2907 113 -228 -298 C ATOM 2797 O LEU A 272 18.738 177.488 8.498 1.00 25.20 O ANISOU 2797 O LEU A 272 3426 3417 2730 118 -223 -274 O ATOM 2798 CB LEU A 272 17.550 174.926 6.752 1.00 28.96 C ANISOU 2798 CB LEU A 272 3960 3839 3206 83 -299 -379 C ATOM 2799 CG LEU A 272 16.892 176.104 6.053 1.00 36.67 C ANISOU 2799 CG LEU A 272 4962 4841 4130 78 -356 -359 C ATOM 2800 CD1 LEU A 272 17.908 176.698 5.091 1.00 39.27 C ANISOU 2800 CD1 LEU A 272 5363 5193 4365 83 -322 -363 C ATOM 2801 CD2 LEU A 272 15.629 175.631 5.307 1.00 43.47 C ANISOU 2801 CD2 LEU A 272 5833 5688 4995 56 -443 -388 C ATOM 2802 N ALA A 273 17.876 175.859 9.747 1.00 24.80 N ANISOU 2802 N ALA A 273 3307 3326 2789 113 -230 -282 N ATOM 2803 CA ALA A 273 17.560 176.788 10.838 1.00 23.85 C ANISOU 2803 CA ALA A 273 3144 3221 2697 122 -225 -238 C ATOM 2804 C ALA A 273 18.826 177.338 11.479 1.00 24.08 C ANISOU 2804 C ALA A 273 3172 3270 2709 138 -172 -218 C ATOM 2805 O ALA A 273 18.857 178.480 11.913 1.00 24.52 O ANISOU 2805 O ALA A 273 3218 3345 2756 143 -168 -192 O ATOM 2806 CB ALA A 273 16.718 176.082 11.878 1.00 24.73 C ANISOU 2806 CB ALA A 273 3205 3309 2883 118 -227 -226 C ATOM 2807 N ILE A 274 19.871 176.510 11.597 1.00 24.25 N ANISOU 2807 N ILE A 274 3196 3282 2735 146 -133 -232 N ATOM 2808 CA ILE A 274 21.133 176.988 12.131 1.00 23.76 C ANISOU 2808 CA ILE A 274 3126 3238 2664 160 -90 -216 C ATOM 2809 C ILE A 274 21.738 178.042 11.200 1.00 23.07 C ANISOU 2809 C ILE A 274 3074 3171 2519 157 -79 -219 C ATOM 2810 O ILE A 274 22.161 179.102 11.639 1.00 25.94 O ANISOU 2810 O ILE A 274 3426 3553 2874 160 -67 -196 O ATOM 2811 CB ILE A 274 22.077 175.801 12.357 1.00 25.39 C ANISOU 2811 CB ILE A 274 3323 3425 2898 172 -56 -229 C ATOM 2812 CG1 ILE A 274 21.590 174.948 13.533 1.00 25.55 C ANISOU 2812 CG1 ILE A 274 3308 3425 2975 177 -60 -209 C ATOM 2813 CG2 ILE A 274 23.499 176.309 12.626 1.00 27.41 C ANISOU 2813 CG2 ILE A 274 3568 3699 3146 185 -17 -219 C ATOM 2814 CD1 ILE A 274 22.341 173.620 13.686 1.00 26.62 C ANISOU 2814 CD1 ILE A 274 3435 3530 3148 191 -33 -220 C ATOM 2815 N AVAL A 275 21.813 177.743 9.899 0.50 24.16 N ANISOU 2815 N AVAL A 275 3259 3304 2616 150 -81 -249 N ATOM 2816 N BVAL A 275 21.766 177.752 9.899 0.50 24.13 N ANISOU 2816 N BVAL A 275 3256 3301 2612 150 -82 -249 N ATOM 2817 CA AVAL A 275 22.353 178.704 8.927 0.50 24.64 C ANISOU 2817 CA AVAL A 275 3364 3382 2614 146 -64 -249 C ATOM 2818 CA BVAL A 275 22.333 178.671 8.907 0.50 24.60 C ANISOU 2818 CA BVAL A 275 3360 3377 2610 146 -65 -250 C ATOM 2819 C AVAL A 275 21.560 180.004 8.971 0.50 24.07 C ANISOU 2819 C AVAL A 275 3294 3325 2527 141 -101 -217 C ATOM 2820 C BVAL A 275 21.550 179.980 8.873 0.50 24.40 C ANISOU 2820 C BVAL A 275 3340 3367 2565 140 -102 -219 C ATOM 2821 O AVAL A 275 22.132 181.100 8.947 0.50 25.17 O ANISOU 2821 O AVAL A 275 3439 3477 2646 141 -78 -195 O ATOM 2822 O BVAL A 275 22.125 181.060 8.711 0.50 24.92 O ANISOU 2822 O BVAL A 275 3418 3446 2605 140 -79 -199 O ATOM 2823 CB AVAL A 275 22.364 178.089 7.513 0.50 26.74 C ANISOU 2823 CB AVAL A 275 3693 3640 2827 138 -64 -288 C ATOM 2824 CB BVAL A 275 22.381 177.972 7.534 0.50 26.53 C ANISOU 2824 CB BVAL A 275 3664 3612 2804 138 -63 -290 C ATOM 2825 CG1AVAL A 275 22.834 179.094 6.452 0.50 28.08 C ANISOU 2825 CG1AVAL A 275 3918 3827 2922 132 -44 -281 C ATOM 2826 CG1BVAL A 275 21.943 178.864 6.390 0.50 28.01 C ANISOU 2826 CG1BVAL A 275 3911 3813 2916 127 -91 -285 C ATOM 2827 CG2AVAL A 275 23.257 176.846 7.498 0.50 25.47 C ANISOU 2827 CG2AVAL A 275 3527 3459 2692 147 -15 -322 C ATOM 2828 CG2BVAL A 275 23.766 177.415 7.313 0.50 25.70 C ANISOU 2828 CG2BVAL A 275 3565 3500 2700 148 8 -313 C ATOM 2829 N LEU A 276 20.231 179.910 9.048 1.00 25.42 N ANISOU 2829 N LEU A 276 3454 3489 2716 136 -157 -213 N ATOM 2830 CA LEU A 276 19.433 181.120 9.102 1.00 25.81 C ANISOU 2830 CA LEU A 276 3498 3546 2762 136 -192 -182 C ATOM 2831 C LEU A 276 19.783 181.966 10.316 1.00 26.29 C ANISOU 2831 C LEU A 276 3518 3614 2857 144 -163 -154 C ATOM 2832 O LEU A 276 19.890 183.201 10.201 1.00 26.70 O ANISOU 2832 O LEU A 276 3580 3672 2892 145 -160 -131 O ATOM 2833 CB LEU A 276 17.955 180.765 9.099 1.00 28.00 C ANISOU 2833 CB LEU A 276 3756 3811 3073 131 -255 -184 C ATOM 2834 CG LEU A 276 16.951 181.926 9.211 1.00 33.47 C ANISOU 2834 CG LEU A 276 4430 4504 3782 135 -296 -152 C ATOM 2835 CD1 LEU A 276 16.957 182.808 7.958 1.00 35.65 C ANISOU 2835 CD1 LEU A 276 4764 4790 3993 134 -325 -139 C ATOM 2836 CD2 LEU A 276 15.574 181.365 9.478 1.00 37.16 C ANISOU 2836 CD2 LEU A 276 4856 4956 4309 130 -346 -156 C ATOM 2837 N SER A 277 20.030 181.338 11.479 1.00 25.13 N ANISOU 2837 N SER A 277 3330 3464 2755 149 -141 -156 N ATOM 2838 CA SER A 277 20.383 182.125 12.651 1.00 23.10 C ANISOU 2838 CA SER A 277 3042 3216 2520 154 -118 -135 C ATOM 2839 C SER A 277 21.704 182.862 12.433 1.00 23.57 C ANISOU 2839 C SER A 277 3116 3287 2552 153 -81 -132 C ATOM 2840 O SER A 277 21.863 184.021 12.829 1.00 24.92 O ANISOU 2840 O SER A 277 3281 3463 2725 152 -73 -116 O ATOM 2841 CB SER A 277 20.433 181.218 13.901 1.00 22.47 C ANISOU 2841 CB SER A 277 2925 3131 2481 160 -104 -134 C ATOM 2842 OG SER A 277 21.608 180.405 13.935 1.00 24.63 O ANISOU 2842 OG SER A 277 3199 3406 2754 165 -76 -146 O ATOM 2843 N HIS A 278 22.652 182.224 11.766 1.00 23.34 N ANISOU 2843 N HIS A 278 3105 3258 2504 153 -54 -150 N ATOM 2844 CA HIS A 278 23.953 182.847 11.513 1.00 23.27 C ANISOU 2844 CA HIS A 278 3103 3258 2481 150 -11 -149 C ATOM 2845 C HIS A 278 23.860 183.966 10.489 1.00 24.81 C ANISOU 2845 C HIS A 278 3340 3455 2633 141 -9 -136 C ATOM 2846 O HIS A 278 24.658 184.909 10.531 1.00 26.08 O ANISOU 2846 O HIS A 278 3498 3618 2793 134 22 -124 O ATOM 2847 CB HIS A 278 24.930 181.781 11.026 1.00 23.46 C ANISOU 2847 CB HIS A 278 3131 3277 2504 154 25 -173 C ATOM 2848 CG HIS A 278 25.217 180.717 12.033 1.00 25.74 C ANISOU 2848 CG HIS A 278 3378 3561 2840 166 26 -179 C ATOM 2849 ND1 HIS A 278 25.909 179.570 11.707 1.00 26.91 N ANISOU 2849 ND1 HIS A 278 3524 3696 3004 176 53 -201 N ATOM 2850 CD2 HIS A 278 24.943 180.631 13.355 1.00 26.25 C ANISOU 2850 CD2 HIS A 278 3405 3628 2939 172 6 -163 C ATOM 2851 CE1 HIS A 278 26.025 178.806 12.781 1.00 27.85 C ANISOU 2851 CE1 HIS A 278 3604 3809 3168 188 45 -193 C ATOM 2852 NE2 HIS A 278 25.470 179.434 13.799 1.00 26.70 N ANISOU 2852 NE2 HIS A 278 3440 3676 3030 185 17 -169 N ATOM 2853 N THR A 279 22.934 183.873 9.542 1.00 26.17 N ANISOU 2853 N THR A 279 3553 3622 2769 139 -43 -137 N ATOM 2854 CA THR A 279 22.779 184.949 8.561 1.00 27.23 C ANISOU 2854 CA THR A 279 3734 3756 2856 133 -48 -116 C ATOM 2855 C THR A 279 22.374 186.251 9.223 1.00 24.22 C ANISOU 2855 C THR A 279 3331 3370 2502 134 -61 -85 C ATOM 2856 O THR A 279 22.609 187.320 8.655 1.00 24.08 O ANISOU 2856 O THR A 279 3342 3347 2459 129 -49 -61 O ATOM 2857 CB THR A 279 21.735 184.634 7.466 1.00 32.75 C ANISOU 2857 CB THR A 279 4482 4453 3510 132 -101 -119 C ATOM 2858 OG1 THR A 279 20.429 184.581 8.038 1.00 40.34 O ANISOU 2858 OG1 THR A 279 5408 5408 4511 137 -159 -112 O ATOM 2859 CG2 THR A 279 22.077 183.337 6.761 1.00 28.61 C ANISOU 2859 CG2 THR A 279 3986 3929 2954 129 -88 -158 C ATOM 2860 N ASN A 280 21.814 186.203 10.423 1.00 24.22 N ANISOU 2860 N ASN A 280 3282 3368 2553 140 -80 -85 N ATOM 2861 CA ASN A 280 21.502 187.440 11.112 1.00 26.80 C ANISOU 2861 CA ASN A 280 3589 3686 2907 142 -83 -63 C ATOM 2862 C ASN A 280 22.750 188.294 11.321 1.00 29.12 C ANISOU 2862 C ASN A 280 3882 3980 3204 132 -35 -59 C ATOM 2863 O ASN A 280 22.667 189.524 11.325 1.00 31.02 O ANISOU 2863 O ASN A 280 4129 4206 3452 128 -31 -39 O ATOM 2864 CB ASN A 280 20.850 187.173 12.453 1.00 24.93 C ANISOU 2864 CB ASN A 280 3305 3448 2719 149 -95 -69 C ATOM 2865 CG ASN A 280 20.436 188.475 13.154 1.00 25.39 C ANISOU 2865 CG ASN A 280 3348 3494 2806 152 -94 -54 C ATOM 2866 OD1 ASN A 280 20.990 188.833 14.203 1.00 28.43 O ANISOU 2866 OD1 ASN A 280 3712 3881 3210 148 -69 -62 O ATOM 2867 ND2 ASN A 280 19.532 189.193 12.551 1.00 25.38 N ANISOU 2867 ND2 ASN A 280 3360 3476 2806 158 -122 -33 N ATOM 2868 N SER A 281 23.911 187.662 11.470 1.00 26.13 N ANISOU 2868 N SER A 281 3490 3612 2826 126 0 -77 N ATOM 2869 CA SER A 281 25.167 188.390 11.663 1.00 25.19 C ANISOU 2869 CA SER A 281 3358 3491 2721 113 44 -76 C ATOM 2870 C SER A 281 25.654 189.104 10.393 1.00 26.65 C ANISOU 2870 C SER A 281 3588 3666 2871 103 76 -59 C ATOM 2871 O SER A 281 26.675 189.791 10.475 1.00 28.73 O ANISOU 2871 O SER A 281 3839 3923 3153 88 117 -56 O ATOM 2872 CB SER A 281 26.233 187.434 12.210 1.00 27.18 C ANISOU 2872 CB SER A 281 3574 3756 2996 114 66 -99 C ATOM 2873 OG SER A 281 25.821 186.962 13.507 1.00 27.78 O ANISOU 2873 OG SER A 281 3615 3840 3101 123 37 -106 O ATOM 2874 N VAL A 282 24.938 189.005 9.258 1.00 27.04 N ANISOU 2874 N VAL A 282 3690 3713 2870 107 58 -46 N ATOM 2875 CA VAL A 282 25.317 189.634 7.982 1.00 27.42 C ANISOU 2875 CA VAL A 282 3796 3754 2870 98 89 -24 C ATOM 2876 C VAL A 282 24.466 190.875 7.714 1.00 27.93 C ANISOU 2876 C VAL A 282 3888 3799 2927 101 58 15 C ATOM 2877 O VAL A 282 24.896 191.794 7.007 1.00 30.38 O ANISOU 2877 O VAL A 282 4235 4094 3214 91 90 44 O ATOM 2878 CB VAL A 282 25.208 188.631 6.804 1.00 28.77 C ANISOU 2878 CB VAL A 282 4020 3935 2975 102 88 -37 C ATOM 2879 CG1 VAL A 282 25.621 189.291 5.493 1.00 32.40 C ANISOU 2879 CG1 VAL A 282 4550 4389 3372 92 127 -11 C ATOM 2880 CG2 VAL A 282 26.068 187.422 7.015 1.00 28.12 C ANISOU 2880 CG2 VAL A 282 3911 3863 2909 103 125 -75 C ATOM 2881 N VAL A 283 23.242 190.912 8.250 1.00 27.22 N ANISOU 2881 N VAL A 283 3778 3705 2860 115 -1 19 N ATOM 2882 CA VAL A 283 22.247 191.829 7.696 1.00 28.38 C ANISOU 2882 CA VAL A 283 3956 3833 2993 124 -41 57 C ATOM 2883 C VAL A 283 22.335 193.259 8.255 1.00 27.18 C ANISOU 2883 C VAL A 283 3788 3652 2889 121 -24 81 C ATOM 2884 O VAL A 283 22.007 194.208 7.543 1.00 28.21 O ANISOU 2884 O VAL A 283 3956 3759 3003 125 -33 122 O ATOM 2885 CB VAL A 283 20.823 191.278 7.890 1.00 33.16 C ANISOU 2885 CB VAL A 283 4544 4443 3614 141 -112 53 C ATOM 2886 CG1 VAL A 283 20.701 189.910 7.298 1.00 36.95 C ANISOU 2886 CG1 VAL A 283 5043 4944 4052 140 -132 26 C ATOM 2887 CG2 VAL A 283 20.426 191.254 9.331 1.00 32.20 C ANISOU 2887 CG2 VAL A 283 4356 4317 3561 147 -116 35 C ATOM 2888 N ASN A 284 22.767 193.460 9.486 1.00 26.35 N ANISOU 2888 N ASN A 284 3631 3544 2838 115 0 58 N ATOM 2889 CA ASN A 284 22.651 194.791 10.073 1.00 27.47 C ANISOU 2889 CA ASN A 284 3757 3653 3027 113 9 72 C ATOM 2890 C ASN A 284 23.411 195.829 9.269 1.00 27.43 C ANISOU 2890 C ASN A 284 3791 3622 3010 98 50 105 C ATOM 2891 O ASN A 284 22.855 196.910 9.034 1.00 28.67 O ANISOU 2891 O ASN A 284 3966 3744 3183 105 39 139 O ATOM 2892 CB ASN A 284 23.108 194.815 11.538 1.00 31.03 C ANISOU 2892 CB ASN A 284 4154 4107 3528 105 27 35 C ATOM 2893 CG ASN A 284 22.180 194.021 12.451 1.00 33.90 C ANISOU 2893 CG ASN A 284 4485 4487 3909 121 -8 12 C ATOM 2894 OD1 ASN A 284 21.069 193.669 12.058 1.00 32.81 O ANISOU 2894 OD1 ASN A 284 4354 4349 3764 139 -47 26 O ATOM 2895 ND2 ASN A 284 22.635 193.735 13.666 1.00 35.59 N ANISOU 2895 ND2 ASN A 284 4662 4713 4146 114 5 -20 N ATOM 2896 N PRO A 285 24.648 195.591 8.831 1.00 26.69 N ANISOU 2896 N PRO A 285 3708 3539 2895 77 101 98 N ATOM 2897 CA PRO A 285 25.331 196.603 8.005 1.00 27.88 C ANISOU 2897 CA PRO A 285 3898 3660 3035 60 149 135 C ATOM 2898 C PRO A 285 24.519 197.054 6.801 1.00 28.89 C ANISOU 2898 C PRO A 285 4095 3773 3111 75 123 188 C ATOM 2899 O PRO A 285 24.630 198.217 6.395 1.00 29.87 O ANISOU 2899 O PRO A 285 4247 3858 3244 69 145 230 O ATOM 2900 CB PRO A 285 26.625 195.901 7.591 1.00 28.52 C ANISOU 2900 CB PRO A 285 3979 3763 3095 41 207 116 C ATOM 2901 CG PRO A 285 26.893 194.926 8.701 1.00 28.43 C ANISOU 2901 CG PRO A 285 3905 3780 3118 43 194 66 C ATOM 2902 CD PRO A 285 25.527 194.446 9.152 1.00 27.89 C ANISOU 2902 CD PRO A 285 3830 3723 3043 69 125 59 C ATOM 2903 N PHE A 286 23.697 196.173 6.207 1.00 29.16 N ANISOU 2903 N PHE A 286 4156 3832 3089 94 72 189 N ATOM 2904 CA PHE A 286 22.883 196.582 5.074 1.00 27.86 C ANISOU 2904 CA PHE A 286 4059 3657 2871 109 31 240 C ATOM 2905 C PHE A 286 21.750 197.504 5.493 1.00 28.47 C ANISOU 2905 C PHE A 286 4116 3700 3000 130 -22 269 C ATOM 2906 O PHE A 286 21.389 198.426 4.736 1.00 29.94 O ANISOU 2906 O PHE A 286 4351 3857 3170 139 -36 325 O ATOM 2907 CB PHE A 286 22.323 195.356 4.363 1.00 29.15 C ANISOU 2907 CB PHE A 286 4254 3856 2964 119 -17 225 C ATOM 2908 CG PHE A 286 23.343 194.649 3.540 1.00 32.36 C ANISOU 2908 CG PHE A 286 4707 4286 3302 102 39 210 C ATOM 2909 CD1 PHE A 286 24.173 193.706 4.111 1.00 36.56 C ANISOU 2909 CD1 PHE A 286 5195 4840 3855 91 81 158 C ATOM 2910 CD2 PHE A 286 23.504 194.983 2.197 1.00 34.72 C ANISOU 2910 CD2 PHE A 286 5095 4582 3515 98 54 251 C ATOM 2911 CE1 PHE A 286 25.137 193.065 3.337 1.00 41.14 C ANISOU 2911 CE1 PHE A 286 5814 5436 4381 78 142 142 C ATOM 2912 CE2 PHE A 286 24.460 194.338 1.439 1.00 38.99 C ANISOU 2912 CE2 PHE A 286 5681 5141 3991 83 119 234 C ATOM 2913 CZ PHE A 286 25.271 193.380 2.029 1.00 41.75 C ANISOU 2913 CZ PHE A 286 5979 5510 4374 73 165 177 C ATOM 2914 N AILE A 287 21.133 197.241 6.652 0.50 27.09 N ANISOU 2914 N AILE A 287 3875 3529 2890 141 -50 234 N ATOM 2915 N BILE A 287 21.190 197.297 6.687 0.50 27.07 N ANISOU 2915 N BILE A 287 3871 3524 2889 140 -47 234 N ATOM 2916 CA AILE A 287 20.124 198.163 7.178 0.50 29.71 C ANISOU 2916 CA AILE A 287 4179 3823 3286 163 -85 255 C ATOM 2917 CA BILE A 287 20.105 198.160 7.157 0.50 29.71 C ANISOU 2917 CA BILE A 287 4180 3824 3285 163 -86 255 C ATOM 2918 C AILE A 287 20.737 199.542 7.365 0.50 29.36 C ANISOU 2918 C AILE A 287 4141 3731 3283 151 -35 278 C ATOM 2919 C BILE A 287 20.638 199.537 7.548 0.50 29.33 C ANISOU 2919 C BILE A 287 4127 3726 3289 153 -38 273 C ATOM 2920 O AILE A 287 20.229 200.546 6.852 0.50 32.10 O ANISOU 2920 O AILE A 287 4516 4036 3643 166 -51 330 O ATOM 2921 O BILE A 287 19.959 200.549 7.359 0.50 32.15 O ANISOU 2921 O BILE A 287 4495 4040 3680 171 -59 314 O ATOM 2922 CB AILE A 287 19.531 197.628 8.494 0.50 29.36 C ANISOU 2922 CB AILE A 287 4064 3790 3300 172 -102 207 C ATOM 2923 CB BILE A 287 19.370 197.460 8.311 0.50 29.41 C ANISOU 2923 CB BILE A 287 4075 3802 3297 175 -114 210 C ATOM 2924 CG1AILE A 287 18.808 196.295 8.261 0.50 32.25 C ANISOU 2924 CG1AILE A 287 4422 4195 3636 182 -154 189 C ATOM 2925 CG1BILE A 287 18.916 196.064 7.865 0.50 32.10 C ANISOU 2925 CG1BILE A 287 4422 4185 3591 180 -159 192 C ATOM 2926 CG2AILE A 287 18.580 198.655 9.155 0.50 29.14 C ANISOU 2926 CG2AILE A 287 4004 3719 3351 194 -120 221 C ATOM 2927 CG2BILE A 287 18.166 198.264 8.776 0.50 29.22 C ANISOU 2927 CG2BILE A 287 4020 3740 3341 202 -150 229 C ATOM 2928 CD1AILE A 287 17.700 196.346 7.225 0.50 32.74 C ANISOU 2928 CD1AILE A 287 4515 4252 3674 204 -227 230 C ATOM 2929 CD1BILE A 287 18.857 195.082 8.979 0.50 34.47 C ANISOU 2929 CD1BILE A 287 4666 4510 3923 177 -153 141 C ATOM 2930 N TYR A 288 21.858 199.611 8.081 1.00 29.97 N ANISOU 2930 N TYR A 288 4191 3810 3386 124 26 242 N ATOM 2931 CA TYR A 288 22.464 200.915 8.336 1.00 29.53 C ANISOU 2931 CA TYR A 288 4135 3704 3380 107 73 256 C ATOM 2932 C TYR A 288 22.720 201.656 7.030 1.00 30.07 C ANISOU 2932 C TYR A 288 4272 3744 3411 103 93 322 C ATOM 2933 O TYR A 288 22.457 202.865 6.923 1.00 32.88 O ANISOU 2933 O TYR A 288 4642 4043 3807 109 99 362 O ATOM 2934 CB TYR A 288 23.772 200.765 9.115 1.00 30.93 C ANISOU 2934 CB TYR A 288 4275 3893 3583 73 129 207 C ATOM 2935 CG TYR A 288 23.645 200.033 10.403 1.00 30.05 C ANISOU 2935 CG TYR A 288 4107 3812 3499 75 111 148 C ATOM 2936 CD1 TYR A 288 22.557 200.209 11.230 1.00 30.29 C ANISOU 2936 CD1 TYR A 288 4111 3831 3568 98 75 134 C ATOM 2937 CD2 TYR A 288 24.631 199.163 10.808 1.00 29.39 C ANISOU 2937 CD2 TYR A 288 3996 3766 3404 56 133 108 C ATOM 2938 CE1 TYR A 288 22.463 199.534 12.427 1.00 31.04 C ANISOU 2938 CE1 TYR A 288 4161 3953 3678 99 66 82 C ATOM 2939 CE2 TYR A 288 24.514 198.455 11.976 1.00 27.94 C ANISOU 2939 CE2 TYR A 288 3768 3612 3238 60 114 60 C ATOM 2940 CZ TYR A 288 23.436 198.655 12.781 1.00 30.10 C ANISOU 2940 CZ TYR A 288 4024 3875 3539 80 82 49 C ATOM 2941 OH TYR A 288 23.355 197.965 13.956 1.00 31.35 O ANISOU 2941 OH TYR A 288 4145 4060 3706 82 70 6 O ATOM 2942 N ALA A 289 23.218 200.948 6.026 1.00 28.00 N ANISOU 2942 N ALA A 289 4055 3514 3068 95 107 335 N ATOM 2943 CA ALA A 289 23.582 201.593 4.769 1.00 29.95 C ANISOU 2943 CA ALA A 289 4378 3738 3265 87 138 399 C ATOM 2944 C ALA A 289 22.359 202.096 4.016 1.00 31.70 C ANISOU 2944 C ALA A 289 4647 3936 3460 121 70 462 C ATOM 2945 O ALA A 289 22.402 203.169 3.404 1.00 33.98 O ANISOU 2945 O ALA A 289 4983 4178 3750 121 88 524 O ATOM 2946 CB ALA A 289 24.403 200.624 3.896 1.00 30.82 C ANISOU 2946 CB ALA A 289 4530 3892 3290 70 177 391 C ATOM 2947 N TYR A 290 21.252 201.362 4.071 1.00 32.27 N ANISOU 2947 N TYR A 290 4706 4038 3518 148 -10 449 N ATOM 2948 CA TYR A 290 20.068 201.749 3.319 1.00 36.19 C ANISOU 2948 CA TYR A 290 5240 4517 3992 181 -87 508 C ATOM 2949 C TYR A 290 19.220 202.769 4.056 1.00 37.46 C ANISOU 2949 C TYR A 290 5353 4624 4255 207 -114 525 C ATOM 2950 O TYR A 290 18.520 203.553 3.417 1.00 39.22 O ANISOU 2950 O TYR A 290 5611 4810 4481 232 -157 590 O ATOM 2951 CB TYR A 290 19.222 200.501 2.998 1.00 44.59 C ANISOU 2951 CB TYR A 290 6304 5632 5004 198 -166 485 C ATOM 2952 CG TYR A 290 19.691 199.788 1.748 1.00 65.53 C ANISOU 2952 CG TYR A 290 9039 8322 7535 185 -162 496 C ATOM 2953 CD1 TYR A 290 19.359 200.268 0.488 1.00 78.37 C ANISOU 2953 CD1 TYR A 290 10753 9937 9085 197 -199 566 C ATOM 2954 CD2 TYR A 290 20.487 198.654 1.824 1.00 77.97 C ANISOU 2954 CD2 TYR A 290 10611 9943 9072 162 -119 438 C ATOM 2955 CE1 TYR A 290 19.798 199.630 -0.661 1.00 88.41 C ANISOU 2955 CE1 TYR A 290 12113 11244 10235 183 -190 573 C ATOM 2956 CE2 TYR A 290 20.928 198.011 0.686 1.00 88.19 C ANISOU 2956 CE2 TYR A 290 11984 11267 10255 151 -106 443 C ATOM 2957 CZ TYR A 290 20.579 198.504 -0.559 1.00 93.40 C ANISOU 2957 CZ TYR A 290 12737 11918 10831 160 -140 508 C ATOM 2958 OH TYR A 290 21.013 197.872 -1.707 1.00 98.69 O ANISOU 2958 OH TYR A 290 13498 12619 11380 148 -122 509 O ATOM 2959 N ARG A 291 19.260 202.774 5.389 1.00 36.84 N ANISOU 2959 N ARG A 291 5199 4539 4259 202 -90 467 N ATOM 2960 CA ARG A 291 18.323 203.559 6.182 1.00 37.92 C ANISOU 2960 CA ARG A 291 5286 4629 4492 229 -115 469 C ATOM 2961 C ARG A 291 18.933 204.758 6.894 1.00 39.58 C ANISOU 2961 C ARG A 291 5480 4781 4779 214 -49 463 C ATOM 2962 O ARG A 291 18.173 205.622 7.357 1.00 41.29 O ANISOU 2962 O ARG A 291 5669 4944 5075 239 -62 475 O ATOM 2963 CB ARG A 291 17.681 202.686 7.261 1.00 38.95 C ANISOU 2963 CB ARG A 291 5345 4792 4662 239 -140 405 C ATOM 2964 CG ARG A 291 16.889 201.486 6.757 1.00 45.27 C ANISOU 2964 CG ARG A 291 6144 5643 5412 254 -211 402 C ATOM 2965 CD ARG A 291 15.394 201.733 6.558 1.00 52.60 C ANISOU 2965 CD ARG A 291 7049 6549 6388 295 -291 436 C ATOM 2966 NE ARG A 291 14.786 202.689 7.490 1.00 56.51 N ANISOU 2966 NE ARG A 291 7490 6990 6992 317 -276 433 N ATOM 2967 CZ ARG A 291 13.516 203.077 7.430 1.00 60.29 C ANISOU 2967 CZ ARG A 291 7935 7437 7537 356 -333 464 C ATOM 2968 NH1 ARG A 291 12.711 202.575 6.493 1.00 61.13 N ANISOU 2968 NH1 ARG A 291 8054 7565 7609 375 -420 500 N ATOM 2969 NH2 ARG A 291 13.050 203.963 8.308 1.00 62.08 N ANISOU 2969 NH2 ARG A 291 8114 7610 7865 376 -305 455 N ATOM 2970 N ILE A 292 20.256 204.830 7.040 1.00 38.69 N ANISOU 2970 N ILE A 292 5377 4672 4653 173 22 439 N ATOM 2971 CA ILE A 292 20.879 205.854 7.890 1.00 39.51 C ANISOU 2971 CA ILE A 292 5454 4723 4837 152 81 415 C ATOM 2972 C ILE A 292 21.948 206.543 7.078 1.00 37.13 C ANISOU 2972 C ILE A 292 5202 4389 4515 121 140 459 C ATOM 2973 O ILE A 292 23.048 205.997 6.887 1.00 35.73 O ANISOU 2973 O ILE A 292 5032 4248 4297 87 184 439 O ATOM 2974 CB ILE A 292 21.473 205.287 9.187 1.00 40.54 C ANISOU 2974 CB ILE A 292 5525 4885 4992 127 108 330 C ATOM 2975 CG1 ILE A 292 20.431 204.477 9.963 1.00 40.13 C ANISOU 2975 CG1 ILE A 292 5429 4869 4951 155 59 290 C ATOM 2976 CG2 ILE A 292 22.040 206.447 10.062 1.00 42.39 C ANISOU 2976 CG2 ILE A 292 5737 5060 5310 103 159 301 C ATOM 2977 CD1 ILE A 292 20.997 203.794 11.202 1.00 38.82 C ANISOU 2977 CD1 ILE A 292 5216 4740 4793 133 80 213 C ATOM 2978 N ARG A 293 21.639 207.780 6.656 1.00 37.18 N ANISOU 2978 N ARG A 293 5240 4324 4563 134 146 520 N ATOM 2979 CA ARG A 293 22.476 208.497 5.701 1.00 41.97 C ANISOU 2979 CA ARG A 293 5906 4892 5147 110 200 581 C ATOM 2980 C ARG A 293 23.908 208.639 6.196 1.00 37.47 C ANISOU 2980 C ARG A 293 5310 4317 4609 56 282 535 C ATOM 2981 O ARG A 293 24.858 208.490 5.415 1.00 33.68 O ANISOU 2981 O ARG A 293 4868 3849 4080 27 334 560 O ATOM 2982 CB ARG A 293 21.873 209.880 5.422 1.00 59.29 C ANISOU 2982 CB ARG A 293 8126 6997 7404 133 194 649 C ATOM 2983 CG ARG A 293 22.767 210.827 4.619 1.00 83.18 C ANISOU 2983 CG ARG A 293 11209 9966 10430 104 264 713 C ATOM 2984 CD ARG A 293 22.032 212.113 4.226 1.00108.95 C ANISOU 2984 CD ARG A 293 14506 13140 13749 135 247 793 C ATOM 2985 NE ARG A 293 21.151 211.906 3.075 1.00132.01 N ANISOU 2985 NE ARG A 293 17491 16078 16590 178 177 876 N ATOM 2986 CZ ARG A 293 21.253 212.531 1.902 1.00151.18 C ANISOU 2986 CZ ARG A 293 20003 18468 18972 182 188 975 C ATOM 2987 NH1 ARG A 293 22.192 213.445 1.683 1.00158.81 N ANISOU 2987 NH1 ARG A 293 20999 19371 19972 147 275 1010 N ATOM 2988 NH2 ARG A 293 20.390 212.245 0.935 1.00157.15 N ANISOU 2988 NH2 ARG A 293 20815 19247 19647 222 108 1043 N ATOM 2989 N GLU A 294 24.098 208.930 7.487 1.00 40.17 N ANISOU 2989 N GLU A 294 5589 4641 5034 41 295 466 N ATOM 2990 CA GLU A 294 25.456 209.191 7.966 1.00 42.26 C ANISOU 2990 CA GLU A 294 5824 4892 5340 -12 363 423 C ATOM 2991 C GLU A 294 26.320 207.933 7.877 1.00 38.84 C ANISOU 2991 C GLU A 294 5375 4538 4845 -34 378 386 C ATOM 2992 O GLU A 294 27.516 208.016 7.563 1.00 38.72 O ANISOU 2992 O GLU A 294 5359 4519 4835 -74 441 387 O ATOM 2993 CB GLU A 294 25.424 209.730 9.398 1.00 48.20 C ANISOU 2993 CB GLU A 294 6519 5612 6183 -23 363 351 C ATOM 2994 CG GLU A 294 26.743 210.328 9.861 1.00 55.87 C ANISOU 2994 CG GLU A 294 7462 6549 7218 -80 425 313 C ATOM 2995 CD GLU A 294 27.090 211.642 9.174 1.00 61.02 C ANISOU 2995 CD GLU A 294 8150 7112 7922 -99 478 375 C ATOM 2996 OE1 GLU A 294 28.292 211.902 8.965 1.00 59.51 O ANISOU 2996 OE1 GLU A 294 7950 6903 7756 -148 539 373 O ATOM 2997 OE2 GLU A 294 26.161 212.419 8.852 1.00 64.77 O ANISOU 2997 OE2 GLU A 294 8659 7529 8420 -65 461 426 O ATOM 2998 N PHE A 295 25.736 206.751 8.119 1.00 35.80 N ANISOU 2998 N PHE A 295 4974 4222 4408 -8 325 355 N ATOM 2999 CA PHE A 295 26.476 205.501 7.886 1.00 34.62 C ANISOU 2999 CA PHE A 295 4816 4141 4197 -23 338 328 C ATOM 3000 C PHE A 295 26.765 205.296 6.406 1.00 33.51 C ANISOU 3000 C PHE A 295 4745 4011 3978 -24 367 391 C ATOM 3001 O PHE A 295 27.890 204.982 6.018 1.00 34.32 O ANISOU 3001 O PHE A 295 4848 4129 4064 -54 428 386 O ATOM 3002 CB PHE A 295 25.699 204.293 8.419 1.00 34.97 C ANISOU 3002 CB PHE A 295 4833 4247 4205 6 274 287 C ATOM 3003 CG PHE A 295 26.003 203.966 9.876 1.00 36.18 C ANISOU 3003 CG PHE A 295 4918 4421 4409 -7 267 210 C ATOM 3004 CD1 PHE A 295 27.237 203.467 10.238 1.00 35.62 C ANISOU 3004 CD1 PHE A 295 4811 4377 4345 -40 302 169 C ATOM 3005 CD2 PHE A 295 25.060 204.175 10.854 1.00 38.27 C ANISOU 3005 CD2 PHE A 295 5157 4674 4711 15 227 181 C ATOM 3006 CE1 PHE A 295 27.524 203.172 11.582 1.00 35.61 C ANISOU 3006 CE1 PHE A 295 4753 4396 4382 -51 285 102 C ATOM 3007 CE2 PHE A 295 25.339 203.881 12.211 1.00 38.48 C ANISOU 3007 CE2 PHE A 295 5132 4721 4770 3 222 112 C ATOM 3008 CZ PHE A 295 26.571 203.377 12.554 1.00 35.91 C ANISOU 3008 CZ PHE A 295 4776 4426 4443 -30 245 75 C ATOM 3009 N ARG A 296 25.742 205.428 5.570 1.00 32.95 N ANISOU 3009 N ARG A 296 4732 3932 3855 10 323 450 N ATOM 3010 CA ARG A 296 25.897 205.243 4.144 1.00 34.16 C ANISOU 3010 CA ARG A 296 4965 4097 3916 12 343 511 C ATOM 3011 C ARG A 296 27.019 206.114 3.596 1.00 35.95 C ANISOU 3011 C ARG A 296 5221 4276 4162 -26 436 550 C ATOM 3012 O ARG A 296 27.917 205.631 2.897 1.00 37.38 O ANISOU 3012 O ARG A 296 5430 4483 4291 -48 497 556 O ATOM 3013 CB ARG A 296 24.559 205.571 3.466 1.00 37.36 C ANISOU 3013 CB ARG A 296 5426 4487 4284 55 269 575 C ATOM 3014 CG ARG A 296 24.605 205.424 1.985 1.00 45.08 C ANISOU 3014 CG ARG A 296 6499 5477 5152 59 276 641 C ATOM 3015 CD ARG A 296 23.232 205.488 1.359 1.00 51.56 C ANISOU 3015 CD ARG A 296 7367 6297 5927 104 180 695 C ATOM 3016 NE ARG A 296 22.542 206.745 1.603 1.00 56.93 N ANISOU 3016 NE ARG A 296 8039 6906 6685 126 154 743 N ATOM 3017 CZ ARG A 296 21.469 206.895 2.370 1.00 63.06 C ANISOU 3017 CZ ARG A 296 8759 7668 7531 158 86 725 C ATOM 3018 NH1 ARG A 296 20.934 205.861 3.018 1.00 60.71 N ANISOU 3018 NH1 ARG A 296 8408 7424 7237 171 36 660 N ATOM 3019 NH2 ARG A 296 20.933 208.099 2.501 1.00 70.03 N ANISOU 3019 NH2 ARG A 296 9640 8478 8489 179 74 772 N ATOM 3020 N GLN A 297 26.995 207.408 3.925 1.00 39.58 N ANISOU 3020 N GLN A 297 5673 4663 4704 -34 455 576 N ATOM 3021 CA GLN A 297 28.010 208.318 3.389 1.00 47.75 C ANISOU 3021 CA GLN A 297 6733 5642 5766 -72 546 619 C ATOM 3022 C GLN A 297 29.391 207.939 3.894 1.00 39.88 C ANISOU 3022 C GLN A 297 5674 4664 4813 -120 617 558 C ATOM 3023 O GLN A 297 30.380 208.055 3.164 1.00 37.67 O ANISOU 3023 O GLN A 297 5419 4373 4519 -151 701 586 O ATOM 3024 CB GLN A 297 27.705 209.766 3.764 1.00 66.41 C ANISOU 3024 CB GLN A 297 9092 7916 8225 -74 551 650 C ATOM 3025 CG GLN A 297 26.249 210.185 3.650 1.00 87.49 C ANISOU 3025 CG GLN A 297 11792 10560 10889 -21 469 694 C ATOM 3026 CD GLN A 297 25.955 211.026 2.436 1.00103.68 C ANISOU 3026 CD GLN A 297 13933 12558 12903 -7 481 803 C ATOM 3027 OE1 GLN A 297 26.068 210.560 1.303 1.00107.46 O ANISOU 3027 OE1 GLN A 297 14485 13071 13274 -3 489 854 O ATOM 3028 NE2 GLN A 297 25.547 212.268 2.663 1.00109.60 N ANISOU 3028 NE2 GLN A 297 14684 13222 13739 3 479 840 N ATOM 3029 N THR A 298 29.491 207.483 5.142 1.00 36.20 N ANISOU 3029 N THR A 298 5127 4226 4403 -125 584 475 N ATOM 3030 CA THR A 298 30.809 207.124 5.650 1.00 36.56 C ANISOU 3030 CA THR A 298 5106 4288 4496 -167 638 419 C ATOM 3031 C THR A 298 31.311 205.826 5.031 1.00 36.39 C ANISOU 3031 C THR A 298 5094 4336 4396 -165 661 408 C ATOM 3032 O THR A 298 32.505 205.699 4.742 1.00 38.35 O ANISOU 3032 O THR A 298 5322 4585 4664 -200 739 401 O ATOM 3033 CB THR A 298 30.783 206.993 7.169 1.00 37.72 C ANISOU 3033 CB THR A 298 5171 4447 4715 -173 590 336 C ATOM 3034 OG1 THR A 298 30.232 208.177 7.749 1.00 38.24 O ANISOU 3034 OG1 THR A 298 5233 4446 4850 -171 571 340 O ATOM 3035 CG2 THR A 298 32.194 206.770 7.704 1.00 38.75 C ANISOU 3035 CG2 THR A 298 5229 4588 4907 -219 638 283 C ATOM 3036 N PHE A 299 30.431 204.828 4.876 1.00 33.85 N ANISOU 3036 N PHE A 299 4798 4070 3994 -126 596 400 N ATOM 3037 CA PHE A 299 30.809 203.615 4.149 1.00 34.23 C ANISOU 3037 CA PHE A 299 4869 4176 3960 -120 618 392 C ATOM 3038 C PHE A 299 31.347 203.953 2.768 1.00 38.03 C ANISOU 3038 C PHE A 299 5428 4637 4384 -136 701 456 C ATOM 3039 O PHE A 299 32.348 203.385 2.317 1.00 39.54 O ANISOU 3039 O PHE A 299 5614 4849 4559 -156 775 443 O ATOM 3040 CB PHE A 299 29.606 202.673 3.976 1.00 33.62 C ANISOU 3040 CB PHE A 299 4824 4148 3801 -76 533 387 C ATOM 3041 CG PHE A 299 29.121 202.016 5.243 1.00 34.42 C ANISOU 3041 CG PHE A 299 4855 4281 3942 -61 463 322 C ATOM 3042 CD1 PHE A 299 29.821 202.121 6.426 1.00 35.91 C ANISOU 3042 CD1 PHE A 299 4961 4465 4216 -83 475 268 C ATOM 3043 CD2 PHE A 299 27.940 201.293 5.224 1.00 35.03 C ANISOU 3043 CD2 PHE A 299 4950 4393 3968 -24 384 317 C ATOM 3044 CE1 PHE A 299 29.342 201.503 7.590 1.00 36.72 C ANISOU 3044 CE1 PHE A 299 5010 4598 4342 -68 412 213 C ATOM 3045 CE2 PHE A 299 27.458 200.658 6.365 1.00 35.89 C ANISOU 3045 CE2 PHE A 299 4998 4529 4109 -10 329 263 C ATOM 3046 CZ PHE A 299 28.158 200.784 7.552 1.00 37.28 C ANISOU 3046 CZ PHE A 299 5102 4701 4361 -31 345 213 C ATOM 3047 N AARG A 300 30.661 204.849 2.060 0.50 40.25 N ANISOU 3047 N AARG A 300 5785 4878 4632 -123 691 529 N ATOM 3048 N BARG A 300 30.661 204.855 2.066 0.50 40.26 N ANISOU 3048 N BARG A 300 5785 4878 4633 -123 690 529 N ATOM 3049 CA AARG A 300 31.105 205.253 0.728 0.50 43.29 C ANISOU 3049 CA AARG A 300 6258 5240 4951 -136 769 601 C ATOM 3050 CA BARG A 300 31.086 205.274 0.731 0.50 43.28 C ANISOU 3050 CA BARG A 300 6257 5237 4949 -136 768 602 C ATOM 3051 C AARG A 300 32.511 205.844 0.767 0.50 43.49 C ANISOU 3051 C AARG A 300 6245 5224 5057 -187 885 601 C ATOM 3052 C BARG A 300 32.494 205.863 0.755 0.50 43.50 C ANISOU 3052 C BARG A 300 6247 5224 5057 -187 884 602 C ATOM 3053 O AARG A 300 33.361 205.519 -0.073 0.50 43.14 O ANISOU 3053 O AARG A 300 6232 5190 4968 -207 976 617 O ATOM 3054 O BARG A 300 33.328 205.554 -0.106 0.50 43.15 O ANISOU 3054 O BARG A 300 6238 5190 4967 -206 975 620 O ATOM 3055 CB AARG A 300 30.108 206.254 0.149 0.50 49.41 C ANISOU 3055 CB AARG A 300 7111 5968 5694 -113 728 684 C ATOM 3056 CB BARG A 300 30.079 206.289 0.187 0.50 49.38 C ANISOU 3056 CB BARG A 300 7105 5962 5694 -112 725 683 C ATOM 3057 CG AARG A 300 30.337 206.611 -1.299 0.50 55.49 C ANISOU 3057 CG AARG A 300 7995 6720 6370 -118 792 769 C ATOM 3058 CG BARG A 300 30.046 206.426 -1.313 0.50 55.38 C ANISOU 3058 CG BARG A 300 7987 6719 6338 -107 764 766 C ATOM 3059 CD AARG A 300 29.117 207.342 -1.863 0.50 60.94 C ANISOU 3059 CD AARG A 300 8764 7378 7011 -82 716 850 C ATOM 3060 CD BARG A 300 28.791 207.190 -1.772 0.50 60.89 C ANISOU 3060 CD BARG A 300 8755 7382 6998 -70 684 843 C ATOM 3061 NE AARG A 300 27.933 206.481 -1.870 0.50 62.79 N ANISOU 3061 NE AARG A 300 9012 7668 7177 -37 599 829 N ATOM 3062 NE BARG A 300 28.749 208.566 -1.264 0.50 63.67 N ANISOU 3062 NE BARG A 300 9079 7651 7461 -79 696 878 N ATOM 3063 CZ AARG A 300 26.772 206.761 -1.286 0.50 64.67 C ANISOU 3063 CZ AARG A 300 9220 7893 7459 -3 497 830 C ATOM 3064 CZ BARG A 300 27.727 209.119 -0.610 0.50 65.37 C ANISOU 3064 CZ BARG A 300 9264 7834 7738 -49 612 881 C ATOM 3065 NH1AARG A 300 25.777 205.889 -1.371 0.50 62.02 N ANISOU 3065 NH1AARG A 300 8893 7610 7062 32 399 809 N ATOM 3066 NH1BARG A 300 27.817 210.378 -0.197 0.50 62.59 N ANISOU 3066 NH1BARG A 300 8890 7399 7490 -61 639 909 N ATOM 3067 NH2AARG A 300 26.588 207.904 -0.635 0.50 66.09 N ANISOU 3067 NH2AARG A 300 9360 8005 7747 -3 495 848 N ATOM 3068 NH2BARG A 300 26.613 208.436 -0.369 0.50 66.16 N ANISOU 3068 NH2BARG A 300 9353 7980 7805 -7 505 856 N ATOM 3069 N LYS A 301 32.773 206.729 1.731 1.00 45.71 N ANISOU 3069 N LYS A 301 6454 5454 5459 -210 885 581 N ATOM 3070 CA LYS A 301 34.108 207.318 1.861 1.00 54.08 C ANISOU 3070 CA LYS A 301 7462 6471 6614 -263 986 574 C ATOM 3071 C LYS A 301 35.172 206.252 2.097 1.00 48.92 C ANISOU 3071 C LYS A 301 6739 5869 5979 -283 1031 510 C ATOM 3072 O LYS A 301 36.251 206.292 1.501 1.00 49.28 O ANISOU 3072 O LYS A 301 6781 5900 6042 -316 1137 525 O ATOM 3073 CB LYS A 301 34.107 208.338 3.006 1.00 67.49 C ANISOU 3073 CB LYS A 301 9091 8111 8440 -284 959 546 C ATOM 3074 CG LYS A 301 35.478 208.745 3.546 1.00 79.24 C ANISOU 3074 CG LYS A 301 10491 9565 10050 -342 1032 507 C ATOM 3075 CD LYS A 301 36.205 209.673 2.592 1.00 87.74 C ANISOU 3075 CD LYS A 301 11610 10575 11152 -380 1146 579 C ATOM 3076 N ILE A 302 34.902 205.315 3.004 1.00 45.11 N ANISOU 3076 N ILE A 302 6196 5440 5502 -262 953 439 N ATOM 3077 CA ILE A 302 35.875 204.281 3.342 1.00 45.32 C ANISOU 3077 CA ILE A 302 6149 5513 5558 -274 983 378 C ATOM 3078 C ILE A 302 36.186 203.430 2.121 1.00 48.30 C ANISOU 3078 C ILE A 302 6588 5925 5838 -265 1051 401 C ATOM 3079 O ILE A 302 37.347 203.119 1.834 1.00 51.46 O ANISOU 3079 O ILE A 302 6951 6327 6274 -290 1143 387 O ATOM 3080 CB ILE A 302 35.340 203.407 4.486 1.00 44.60 C ANISOU 3080 CB ILE A 302 6000 5473 5474 -247 880 310 C ATOM 3081 CG1 ILE A 302 35.288 204.215 5.775 1.00 46.38 C ANISOU 3081 CG1 ILE A 302 6157 5665 5801 -265 829 275 C ATOM 3082 CG2 ILE A 302 36.200 202.137 4.663 1.00 44.39 C ANISOU 3082 CG2 ILE A 302 5912 5498 5457 -248 902 257 C ATOM 3083 CD1 ILE A 302 34.608 203.461 6.917 1.00 46.61 C ANISOU 3083 CD1 ILE A 302 6144 5740 5824 -236 728 216 C ATOM 3084 N ILE A 303 35.145 203.001 1.413 1.00 48.31 N ANISOU 3084 N ILE A 303 6683 5955 5718 -226 1004 431 N ATOM 3085 CA ILE A 303 35.336 202.121 0.267 1.00 49.46 C ANISOU 3085 CA ILE A 303 6899 6137 5756 -215 1059 443 C ATOM 3086 C ILE A 303 36.087 202.857 -0.837 1.00 49.15 C ANISOU 3086 C ILE A 303 6922 6056 5697 -245 1184 506 C ATOM 3087 O ILE A 303 37.118 202.394 -1.324 1.00 47.16 O ANISOU 3087 O ILE A 303 6659 5812 5448 -264 1287 493 O ATOM 3088 CB ILE A 303 33.972 201.586 -0.213 1.00 53.08 C ANISOU 3088 CB ILE A 303 7446 6632 6091 -170 966 459 C ATOM 3089 CG1 ILE A 303 33.441 200.560 0.794 1.00 53.90 C ANISOU 3089 CG1 ILE A 303 7482 6784 6214 -144 869 388 C ATOM 3090 CG2 ILE A 303 34.069 200.984 -1.619 1.00 54.94 C ANISOU 3090 CG2 ILE A 303 7787 6892 6195 -163 1025 486 C ATOM 3091 CD1 ILE A 303 31.932 200.407 0.787 1.00 53.55 C ANISOU 3091 CD1 ILE A 303 7487 6757 6102 -106 753 402 C ATOM 3092 N ARG A 304 35.601 204.026 -1.227 1.00 54.68 N ANISOU 3092 N ARG A 304 7686 6706 6384 -249 1182 577 N ATOM 3093 CA ARG A 304 36.265 204.758 -2.303 1.00 67.76 C ANISOU 3093 CA ARG A 304 9412 8318 8015 -278 1304 648 C ATOM 3094 C ARG A 304 37.727 205.041 -1.967 1.00 68.24 C ANISOU 3094 C ARG A 304 9378 8346 8205 -328 1418 623 C ATOM 3095 O ARG A 304 38.603 204.915 -2.828 1.00 65.44 O ANISOU 3095 O ARG A 304 9053 7986 7827 -350 1543 645 O ATOM 3096 CB ARG A 304 35.519 206.056 -2.587 1.00 86.31 C ANISOU 3096 CB ARG A 304 11832 10609 10354 -275 1275 730 C ATOM 3097 CG ARG A 304 34.207 205.861 -3.310 1.00107.76 C ANISOU 3097 CG ARG A 304 14662 13351 12930 -228 1186 777 C ATOM 3098 CD ARG A 304 33.414 207.150 -3.301 1.00129.64 C ANISOU 3098 CD ARG A 304 17473 16059 15724 -219 1137 849 C ATOM 3099 NE ARG A 304 32.279 207.120 -4.217 1.00149.61 N ANISOU 3099 NE ARG A 304 20123 18605 18118 -178 1065 914 N ATOM 3100 CZ ARG A 304 31.329 208.049 -4.257 1.00166.30 C ANISOU 3100 CZ ARG A 304 22276 20673 20237 -154 994 978 C ATOM 3101 NH1 ARG A 304 31.365 209.079 -3.421 1.00170.99 N ANISOU 3101 NH1 ARG A 304 22802 21201 20964 -168 992 982 N ATOM 3102 NH2 ARG A 304 30.332 207.943 -5.124 1.00173.45 N ANISOU 3102 NH2 ARG A 304 23287 21599 21018 -116 921 1036 N ATOM 3103 N SER A 305 38.017 205.400 -0.718 1.00 72.75 N ANISOU 3103 N SER A 305 9832 8896 8913 -347 1377 575 N ATOM 3104 CA SER A 305 39.378 205.794 -0.348 1.00 76.00 C ANISOU 3104 CA SER A 305 10145 9271 9463 -399 1471 552 C ATOM 3105 C SER A 305 40.266 204.581 -0.085 1.00 81.15 C ANISOU 3105 C SER A 305 10712 9974 10148 -400 1503 482 C ATOM 3106 O SER A 305 41.199 204.303 -0.845 1.00 82.78 O ANISOU 3106 O SER A 305 10920 10177 10354 -420 1625 492 O ATOM 3107 CB SER A 305 39.332 206.707 0.879 1.00 75.28 C ANISOU 3107 CB SER A 305 9968 9134 9502 -422 1407 525 C ATOM 3108 OG SER A 305 38.614 207.894 0.586 1.00 79.37 O ANISOU 3108 OG SER A 305 10560 9592 10005 -422 1394 593 O ATOM 3109 N HIS A 306 39.987 203.847 0.991 1.00 86.25 N ANISOU 3109 N HIS A 306 11283 10664 10825 -378 1398 412 N ATOM 3110 CA HIS A 306 40.873 202.790 1.469 1.00 91.89 C ANISOU 3110 CA HIS A 306 11898 11417 11599 -380 1414 344 C ATOM 3111 C HIS A 306 40.691 201.463 0.747 1.00 85.59 C ANISOU 3111 C HIS A 306 11155 10678 10690 -342 1430 330 C ATOM 3112 O HIS A 306 41.308 200.479 1.165 1.00 83.28 O ANISOU 3112 O HIS A 306 10782 10418 10443 -334 1433 274 O ATOM 3113 CB HIS A 306 40.660 202.553 2.964 1.00103.82 C ANISOU 3113 CB HIS A 306 13313 12950 13186 -372 1292 279 C ATOM 3114 CG HIS A 306 40.922 203.753 3.814 1.00117.05 C ANISOU 3114 CG HIS A 306 14925 14571 14978 -411 1270 273 C ATOM 3115 ND1 HIS A 306 40.037 204.804 3.911 1.00121.92 N ANISOU 3115 ND1 HIS A 306 15599 15147 15577 -411 1226 309 N ATOM 3116 CD2 HIS A 306 41.968 204.065 4.613 1.00124.21 C ANISOU 3116 CD2 HIS A 306 15715 15455 16025 -452 1283 232 C ATOM 3117 CE1 HIS A 306 40.527 205.714 4.733 1.00126.19 C ANISOU 3117 CE1 HIS A 306 16066 15640 16240 -452 1217 287 C ATOM 3118 NE2 HIS A 306 41.698 205.290 5.172 1.00127.67 N ANISOU 3118 NE2 HIS A 306 16147 15839 16522 -479 1248 240 N ATOM 3119 N VAL A 307 39.870 201.392 -0.298 1.00 86.98 N ANISOU 3119 N VAL A 307 11461 10864 10723 -318 1435 377 N ATOM 3120 CA VAL A 307 39.610 200.118 -0.962 1.00 95.62 C ANISOU 3120 CA VAL A 307 12614 12011 11705 -283 1440 356 C ATOM 3121 C VAL A 307 39.666 200.270 -2.476 1.00104.42 C ANISOU 3121 C VAL A 307 13858 13117 12702 -286 1544 414 C ATOM 3122 O VAL A 307 39.606 199.276 -3.208 1.00112.84 O ANISOU 3122 O VAL A 307 14984 14220 13669 -264 1574 396 O ATOM 3123 CB VAL A 307 38.248 199.540 -0.530 1.00 95.50 C ANISOU 3123 CB VAL A 307 12634 12038 11614 -239 1295 336 C ATOM 3124 N LEU A 308 39.801 201.501 -2.957 1.00101.16 N ANISOU 3124 N LEU A 308 13491 12650 12295 -315 1605 483 N ATOM 3125 CA LEU A 308 39.681 201.775 -4.383 1.00 97.23 C ANISOU 3125 CA LEU A 308 13135 12142 11666 -316 1690 552 C ATOM 3126 C LEU A 308 40.716 202.802 -4.839 1.00 99.85 C ANISOU 3126 C LEU A 308 13460 12411 12068 -365 1835 605 C ATOM 3127 O LEU A 308 41.571 203.228 -4.061 1.00 99.90 O ANISOU 3127 O LEU A 308 13342 12383 12231 -399 1869 581 O ATOM 3128 CB LEU A 308 38.267 202.272 -4.697 1.00 89.69 C ANISOU 3128 CB LEU A 308 12292 11188 10600 -288 1581 607 C ATOM 3129 CG LEU A 308 37.264 201.322 -5.362 1.00 80.28 C ANISOU 3129 CG LEU A 308 11205 10052 9244 -245 1506 599 C ATOM 3130 CD1 LEU A 308 37.074 200.034 -4.611 1.00 75.39 C ANISOU 3130 CD1 LEU A 308 10511 9487 8646 -220 1429 510 C ATOM 3131 CD2 LEU A 308 35.928 202.024 -5.512 1.00 77.21 C ANISOU 3131 CD2 LEU A 308 10899 9654 8785 -222 1391 659 C TER 3132 LEU A 308 HETATM 3133 C1 ZMA A1201 21.790 167.030 14.888 1.00 40.67 C HETATM 3134 C2 ZMA A1201 21.551 165.675 15.042 1.00 44.47 C HETATM 3135 C3 ZMA A1201 20.404 165.249 15.692 1.00 46.38 C HETATM 3136 O4 ZMA A1201 20.199 163.925 15.917 1.00 54.46 O HETATM 3137 C5 ZMA A1201 19.487 166.184 16.149 1.00 36.87 C HETATM 3138 C6 ZMA A1201 19.738 167.531 15.988 1.00 32.05 C HETATM 3139 C7 ZMA A1201 20.895 167.976 15.373 1.00 34.47 C HETATM 3140 C8 ZMA A1201 21.251 169.445 15.387 1.00 31.49 C HETATM 3141 C9 ZMA A1201 22.196 169.727 16.519 1.00 27.97 C HETATM 3142 N10 ZMA A1201 22.482 171.143 16.663 1.00 25.63 N HETATM 3143 C11 ZMA A1201 21.651 171.984 17.271 1.00 25.96 C HETATM 3144 N12 ZMA A1201 22.074 173.281 17.403 1.00 24.26 N HETATM 3145 N13 ZMA A1201 20.471 171.501 17.721 1.00 27.10 N HETATM 3146 C14 ZMA A1201 19.640 172.351 18.324 1.00 25.08 C HETATM 3147 N15 ZMA A1201 18.480 171.880 18.802 1.00 24.01 N HETATM 3148 N16 ZMA A1201 19.997 173.667 18.463 1.00 24.42 N HETATM 3149 N17 ZMA A1201 19.318 174.688 19.057 1.00 24.14 N HETATM 3150 C18 ZMA A1201 21.223 174.101 18.014 1.00 23.02 C HETATM 3151 N19 ZMA A1201 21.385 175.389 18.328 1.00 22.85 N HETATM 3152 C20 ZMA A1201 20.188 175.678 18.976 1.00 23.88 C HETATM 3153 C21 ZMA A1201 19.859 176.999 19.461 1.00 24.82 C HETATM 3154 C22 ZMA A1201 20.533 178.157 19.568 1.00 25.19 C HETATM 3155 C23 ZMA A1201 19.584 179.122 20.013 1.00 25.83 C HETATM 3156 C24 ZMA A1201 18.430 178.495 20.143 1.00 26.78 C HETATM 3157 O25 ZMA A1201 18.549 177.181 19.826 1.00 27.48 O HETATM 3158 C10 OLC A1202 36.904 187.768 18.491 1.00 58.64 C HETATM 3159 C9 OLC A1202 36.580 188.858 17.772 1.00 60.10 C HETATM 3160 C8 OLC A1202 35.754 189.963 18.386 1.00 61.35 C HETATM 3161 C24 OLC A1202 35.236 203.361 18.457 1.00 84.76 C HETATM 3162 C7 OLC A1202 36.101 191.265 17.700 1.00 63.25 C HETATM 3163 C6 OLC A1202 35.846 192.435 18.624 1.00 65.25 C HETATM 3164 C5 OLC A1202 36.184 193.723 17.902 1.00 67.28 C HETATM 3165 C4 OLC A1202 35.713 194.911 18.717 1.00 71.33 C HETATM 3166 C3 OLC A1202 36.189 196.184 18.055 1.00 75.80 C HETATM 3167 C2 OLC A1202 35.705 197.396 18.822 1.00 81.26 C HETATM 3168 C21 OLC A1202 35.791 200.977 18.016 1.00 84.43 C HETATM 3169 C1 OLC A1202 36.068 198.649 18.044 1.00 87.63 C HETATM 3170 C22 OLC A1202 34.682 201.972 18.256 1.00 85.32 C HETATM 3171 O19 OLC A1202 37.122 198.709 17.439 1.00 92.15 O HETATM 3172 O25 OLC A1202 34.423 204.073 19.365 1.00 85.26 O HETATM 3173 O23 OLC A1202 33.849 201.981 17.131 1.00 88.36 O HETATM 3174 O20 OLC A1202 35.212 199.695 18.009 1.00 86.96 O HETATM 3175 C9 OLC A1203 33.888 187.665 22.139 1.00 69.26 C HETATM 3176 C8 OLC A1203 33.838 189.138 21.803 1.00 70.15 C HETATM 3177 C24 OLC A1203 32.733 201.928 22.430 1.00 81.82 C HETATM 3178 C7 OLC A1203 34.465 189.874 22.967 1.00 70.40 C HETATM 3179 C6 OLC A1203 33.629 191.059 23.404 1.00 66.27 C HETATM 3180 C5 OLC A1203 34.137 192.336 22.762 1.00 60.08 C HETATM 3181 C4 OLC A1203 33.469 193.506 23.440 1.00 58.91 C HETATM 3182 C3 OLC A1203 33.549 194.732 22.560 1.00 63.92 C HETATM 3183 C2 OLC A1203 32.602 195.786 23.088 1.00 70.63 C HETATM 3184 C21 OLC A1203 32.824 199.442 22.245 1.00 73.06 C HETATM 3185 C1 OLC A1203 32.833 197.101 22.372 1.00 76.01 C HETATM 3186 C22 OLC A1203 32.443 200.614 23.121 1.00 81.10 C HETATM 3187 O19 OLC A1203 33.392 197.097 21.300 1.00 85.20 O HETATM 3188 O25 OLC A1203 32.778 202.983 23.375 1.00 83.16 O HETATM 3189 O23 OLC A1203 31.066 200.527 23.382 1.00 88.33 O HETATM 3190 O20 OLC A1203 32.430 198.270 22.918 1.00 71.18 O HETATM 3191 C10 OLC A1204 20.741 178.227 1.438 1.00 68.48 C HETATM 3192 C9 OLC A1204 20.862 176.907 1.691 1.00 66.29 C HETATM 3193 C11 OLC A1204 21.323 179.269 2.367 1.00 70.23 C HETATM 3194 C8 OLC A1204 21.594 176.414 2.919 1.00 64.91 C HETATM 3195 C24 OLC A1204 25.503 165.734 7.945 1.00 82.70 C HETATM 3196 C7 OLC A1204 21.246 174.958 3.151 1.00 64.20 C HETATM 3197 C6 OLC A1204 22.266 174.344 4.080 1.00 64.18 C HETATM 3198 C5 OLC A1204 21.696 173.089 4.709 1.00 65.59 C HETATM 3199 C4 OLC A1204 21.732 171.941 3.720 1.00 69.49 C HETATM 3200 C3 OLC A1204 21.619 170.617 4.451 1.00 75.59 C HETATM 3201 C2 OLC A1204 22.970 170.206 4.993 1.00 82.19 C HETATM 3202 C21 OLC A1204 24.463 167.600 6.738 1.00 86.16 C HETATM 3203 C1 OLC A1204 22.817 169.020 5.917 1.00 88.68 C HETATM 3204 C22 OLC A1204 25.057 167.171 8.066 1.00 81.80 C HETATM 3205 O19 OLC A1204 21.861 168.279 5.791 1.00 93.05 O HETATM 3206 O25 OLC A1204 26.349 165.465 9.040 1.00 83.85 O HETATM 3207 O23 OLC A1204 26.175 167.958 8.429 1.00 77.35 O HETATM 3208 O20 OLC A1204 23.732 168.792 6.887 1.00 88.61 O HETATM 3209 C10 OLC A1205 4.558 181.034 14.911 1.00 64.15 C HETATM 3210 C9 OLC A1205 4.264 180.045 14.046 1.00 61.28 C HETATM 3211 C8 OLC A1205 4.179 178.615 14.526 1.00 61.31 C HETATM 3212 C24 OLC A1205 2.931 166.423 13.741 1.00 67.19 C HETATM 3213 C7 OLC A1205 3.430 177.803 13.495 1.00 65.69 C HETATM 3214 C6 OLC A1205 3.452 176.351 13.898 1.00 70.84 C HETATM 3215 C5 OLC A1205 2.288 175.604 13.270 1.00 75.30 C HETATM 3216 C4 OLC A1205 2.288 174.193 13.821 1.00 77.52 C HETATM 3217 C3 OLC A1205 1.156 173.383 13.243 1.00 77.51 C HETATM 3218 C2 OLC A1205 0.890 172.193 14.148 1.00 77.39 C HETATM 3219 C21 OLC A1205 2.292 168.811 13.558 1.00 71.16 C HETATM 3220 C1 OLC A1205 1.804 171.047 13.791 1.00 78.56 C HETATM 3221 C22 OLC A1205 1.861 167.443 14.029 1.00 71.07 C HETATM 3222 O19 OLC A1205 2.738 171.244 13.047 1.00 84.50 O HETATM 3223 O25 OLC A1205 2.556 165.167 14.263 1.00 66.98 O HETATM 3224 O23 OLC A1205 1.652 167.506 15.413 1.00 76.15 O HETATM 3225 O20 OLC A1205 1.595 169.804 14.279 1.00 73.61 O HETATM 3226 C10 OLC A1206 3.673 183.320 24.514 1.00 86.99 C HETATM 3227 C9 OLC A1206 3.093 182.139 24.812 1.00 82.62 C HETATM 3228 C8 OLC A1206 3.954 180.929 25.100 1.00 75.44 C HETATM 3229 C24 OLC A1206 3.514 168.550 27.164 1.00 77.45 C HETATM 3230 C7 OLC A1206 3.125 179.809 25.699 1.00 66.07 C HETATM 3231 C6 OLC A1206 3.521 178.483 25.068 1.00 57.87 C HETATM 3232 C5 OLC A1206 3.132 177.345 25.977 1.00 54.46 C HETATM 3233 C4 OLC A1206 3.262 176.020 25.261 1.00 53.12 C HETATM 3234 C3 OLC A1206 2.769 174.898 26.152 1.00 50.71 C HETATM 3235 C2 OLC A1206 2.841 173.596 25.391 1.00 50.56 C HETATM 3236 C21 OLC A1206 1.829 170.262 26.686 1.00 60.24 C HETATM 3237 C1 OLC A1206 2.376 172.433 26.228 1.00 56.16 C HETATM 3238 C22 OLC A1206 2.266 168.853 26.366 1.00 67.92 C HETATM 3239 O19 OLC A1206 1.992 172.620 27.357 1.00 62.23 O HETATM 3240 O25 OLC A1206 4.054 167.294 26.795 1.00 81.27 O HETATM 3241 O23 OLC A1206 1.257 167.943 26.736 1.00 66.55 O HETATM 3242 O20 OLC A1206 2.371 171.172 25.754 1.00 57.12 O HETATM 3243 C24 OLC A1207 38.082 173.093 30.081 1.00 87.45 C HETATM 3244 C4 OLC A1207 38.865 181.121 27.246 1.00 81.02 C HETATM 3245 C3 OLC A1207 39.342 179.954 28.083 1.00 84.79 C HETATM 3246 C2 OLC A1207 38.468 178.744 27.817 1.00 89.72 C HETATM 3247 C21 OLC A1207 38.554 175.468 29.553 1.00 91.65 C HETATM 3248 C1 OLC A1207 38.806 177.644 28.804 1.00 92.88 C HETATM 3249 C22 OLC A1207 37.784 174.233 29.136 1.00 87.72 C HETATM 3250 O19 OLC A1207 39.854 177.682 29.426 1.00 93.05 O HETATM 3251 O25 OLC A1207 37.398 171.929 29.660 1.00 87.47 O HETATM 3252 O23 OLC A1207 36.409 174.513 29.182 1.00 84.57 O HETATM 3253 O20 OLC A1207 37.950 176.613 28.989 1.00 93.73 O HETATM 3254 C24 OLC A1208 42.773 168.963 9.135 1.00 80.62 C HETATM 3255 C4 OLC A1208 42.552 177.327 9.121 1.00 84.65 C HETATM 3256 C3 OLC A1208 42.908 176.084 8.337 1.00 85.24 C HETATM 3257 C2 OLC A1208 41.912 174.995 8.670 1.00 85.14 C HETATM 3258 C21 OLC A1208 42.714 171.384 8.629 1.00 79.93 C HETATM 3259 C1 OLC A1208 42.475 173.662 8.234 1.00 82.48 C HETATM 3260 C22 OLC A1208 41.876 170.137 8.800 1.00 80.57 C HETATM 3261 O19 OLC A1208 43.467 173.629 7.532 1.00 79.61 O HETATM 3262 O25 OLC A1208 43.982 169.075 8.412 1.00 78.58 O HETATM 3263 O23 OLC A1208 40.924 170.343 9.822 1.00 80.92 O HETATM 3264 O20 OLC A1208 41.873 172.514 8.620 1.00 81.39 O HETATM 3265 C24 OLC A1209 8.697 195.769 16.150 1.00 83.78 C HETATM 3266 C4 OLC A1209 7.860 188.582 18.944 1.00 69.72 C HETATM 3267 C3 OLC A1209 8.919 189.634 18.714 1.00 74.21 C HETATM 3268 C2 OLC A1209 8.357 190.755 17.871 1.00 84.36 C HETATM 3269 C21 OLC A1209 10.006 193.736 16.696 1.00 89.95 C HETATM 3270 C1 OLC A1209 9.244 191.973 18.007 1.00 95.87 C HETATM 3271 C22 OLC A1209 9.901 195.231 16.892 1.00 86.37 C HETATM 3272 O19 OLC A1209 10.236 191.925 18.701 1.00105.08 O HETATM 3273 O25 OLC A1209 8.265 196.975 16.745 1.00 82.95 O HETATM 3274 O23 OLC A1209 9.748 195.484 18.267 1.00 86.66 O HETATM 3275 O20 OLC A1209 8.934 193.120 17.370 1.00 94.01 O HETATM 3276 C10 OLC A1210 5.548 185.898 28.752 1.00 77.16 C HETATM 3277 C9 OLC A1210 5.376 184.654 28.254 1.00 80.65 C HETATM 3278 C8 OLC A1210 6.205 183.492 28.774 1.00 88.42 C HETATM 3279 C24 OLC A1210 4.911 170.910 30.350 1.00109.74 C HETATM 3280 C7 OLC A1210 5.618 182.156 28.333 1.00 98.92 C HETATM 3281 C6 OLC A1210 4.900 181.444 29.472 1.00110.14 C HETATM 3282 C5 OLC A1210 4.954 179.934 29.289 1.00120.62 C HETATM 3283 C4 OLC A1210 4.324 179.217 30.474 1.00129.99 C HETATM 3284 C3 OLC A1210 4.916 177.832 30.694 1.00138.49 C HETATM 3285 C2 OLC A1210 4.090 176.745 30.023 1.00144.62 C HETATM 3286 C21 OLC A1210 4.596 173.273 31.138 1.00129.71 C HETATM 3287 C1 OLC A1210 3.958 175.504 30.898 1.00146.11 C HETATM 3288 C22 OLC A1210 3.946 171.915 30.950 1.00118.53 C HETATM 3289 O19 OLC A1210 3.849 175.618 32.100 1.00149.09 O HETATM 3290 O25 OLC A1210 4.529 169.602 30.712 1.00103.73 O HETATM 3291 O23 OLC A1210 3.522 171.427 32.200 1.00117.27 O HETATM 3292 O20 OLC A1210 3.944 174.258 30.362 1.00139.93 O HETATM 3293 C1 CLR A1211 3.128 172.357 21.891 1.00 39.11 C HETATM 3294 C2 CLR A1211 3.030 170.849 21.843 1.00 39.93 C HETATM 3295 C3 CLR A1211 1.982 170.414 20.841 1.00 40.34 C HETATM 3296 C4 CLR A1211 2.404 170.887 19.447 1.00 39.50 C HETATM 3297 C5 CLR A1211 2.639 172.377 19.487 1.00 39.58 C HETATM 3298 C6 CLR A1211 2.057 173.159 18.560 1.00 40.40 C HETATM 3299 C7 CLR A1211 2.277 174.642 18.459 1.00 39.98 C HETATM 3300 C8 CLR A1211 3.485 175.115 19.250 1.00 38.79 C HETATM 3301 C9 CLR A1211 3.454 174.468 20.633 1.00 37.73 C HETATM 3302 C10 CLR A1211 3.552 172.950 20.548 1.00 39.75 C HETATM 3303 C11 CLR A1211 4.502 175.092 21.583 1.00 37.05 C HETATM 3304 C12 CLR A1211 4.462 176.624 21.604 1.00 38.43 C HETATM 3305 C13 CLR A1211 4.579 177.204 20.199 1.00 40.32 C HETATM 3306 C14 CLR A1211 3.428 176.617 19.407 1.00 39.70 C HETATM 3307 C15 CLR A1211 3.368 177.432 18.123 1.00 40.34 C HETATM 3308 C16 CLR A1211 3.831 178.813 18.584 1.00 42.00 C HETATM 3309 C17 CLR A1211 4.303 178.689 20.038 1.00 43.61 C HETATM 3310 C18 CLR A1211 5.927 176.857 19.540 1.00 40.07 C HETATM 3311 C19 CLR A1211 4.968 172.511 20.168 1.00 43.35 C HETATM 3312 C20 CLR A1211 5.424 179.701 20.351 1.00 49.02 C HETATM 3313 C21 CLR A1211 5.983 179.561 21.756 1.00 49.13 C HETATM 3314 C22 CLR A1211 4.913 181.133 20.201 1.00 54.49 C HETATM 3315 C23 CLR A1211 6.018 182.177 20.069 1.00 60.18 C HETATM 3316 C24 CLR A1211 5.422 183.556 20.314 1.00 67.09 C HETATM 3317 C25 CLR A1211 6.125 184.663 19.542 1.00 74.73 C HETATM 3318 C26 CLR A1211 5.898 184.558 18.036 1.00 77.85 C HETATM 3319 C27 CLR A1211 5.637 186.011 20.064 1.00 77.37 C HETATM 3320 O1 CLR A1211 1.893 169.006 20.919 1.00 41.29 O HETATM 3321 C1 CLR A1212 8.334 169.820 13.977 1.00 46.64 C HETATM 3322 C2 CLR A1212 8.392 168.299 14.050 1.00 48.55 C HETATM 3323 C3 CLR A1212 7.056 167.661 13.685 1.00 46.30 C HETATM 3324 C4 CLR A1212 6.557 168.111 12.323 1.00 45.28 C HETATM 3325 C5 CLR A1212 6.634 169.612 12.196 1.00 46.33 C HETATM 3326 C6 CLR A1212 5.567 170.267 11.685 1.00 51.45 C HETATM 3327 C7 CLR A1212 5.535 171.753 11.450 1.00 55.54 C HETATM 3328 C8 CLR A1212 6.917 172.386 11.495 1.00 51.61 C HETATM 3329 C9 CLR A1212 7.697 171.843 12.691 1.00 46.15 C HETATM 3330 C10 CLR A1212 7.903 170.323 12.609 1.00 45.63 C HETATM 3331 C11 CLR A1212 8.997 172.617 12.874 1.00 43.11 C HETATM 3332 C12 CLR A1212 8.793 174.132 12.950 1.00 43.20 C HETATM 3333 C13 CLR A1212 8.111 174.659 11.701 1.00 45.91 C HETATM 3334 C14 CLR A1212 6.785 173.900 11.628 1.00 49.53 C HETATM 3335 C15 CLR A1212 6.006 174.618 10.540 1.00 50.97 C HETATM 3336 C16 CLR A1212 6.431 176.075 10.719 1.00 50.96 C HETATM 3337 C17 CLR A1212 7.624 176.098 11.686 1.00 46.38 C HETATM 3338 C18 CLR A1212 8.955 174.416 10.453 1.00 43.83 C HETATM 3339 C19 CLR A1212 8.954 169.948 11.563 1.00 48.03 C HETATM 3340 C20 CLR A1212 8.609 177.225 11.320 1.00 42.21 C HETATM 3341 C21 CLR A1212 9.837 177.166 12.214 1.00 41.14 C HETATM 3342 C22 CLR A1212 7.925 178.561 11.506 1.00 41.25 C HETATM 3343 C23 CLR A1212 8.781 179.767 11.092 1.00 47.20 C HETATM 3344 C24 CLR A1212 7.913 181.020 11.166 1.00 56.08 C HETATM 3345 C25 CLR A1212 8.678 182.345 11.075 1.00 64.32 C HETATM 3346 C26 CLR A1212 9.204 182.775 12.435 1.00 64.37 C HETATM 3347 C27 CLR A1212 9.808 182.297 10.054 1.00 69.81 C HETATM 3348 O1 CLR A1212 7.266 166.254 13.672 1.00 43.95 O HETATM 3349 C1 CLR A1213 38.915 169.955 22.478 1.00 47.58 C HETATM 3350 C2 CLR A1213 38.516 168.509 22.762 1.00 49.52 C HETATM 3351 C3 CLR A1213 38.710 168.161 24.230 1.00 47.73 C HETATM 3352 C4 CLR A1213 37.896 169.120 25.099 1.00 46.35 C HETATM 3353 C5 CLR A1213 38.183 170.559 24.756 1.00 45.25 C HETATM 3354 C6 CLR A1213 38.412 171.399 25.776 1.00 44.90 C HETATM 3355 C7 CLR A1213 38.652 172.878 25.585 1.00 43.73 C HETATM 3356 C8 CLR A1213 38.330 173.371 24.182 1.00 42.90 C HETATM 3357 C9 CLR A1213 38.843 172.359 23.162 1.00 40.53 C HETATM 3358 C10 CLR A1213 38.160 170.998 23.315 1.00 44.87 C HETATM 3359 C11 CLR A1213 38.738 172.911 21.744 1.00 38.25 C HETATM 3360 C12 CLR A1213 39.418 174.272 21.575 1.00 41.13 C HETATM 3361 C13 CLR A1213 38.848 175.288 22.551 1.00 45.20 C HETATM 3362 C14 CLR A1213 39.026 174.701 23.941 1.00 46.63 C HETATM 3363 C15 CLR A1213 38.705 175.843 24.897 1.00 51.17 C HETATM 3364 C16 CLR A1213 39.251 177.065 24.145 1.00 50.56 C HETATM 3365 C17 CLR A1213 39.603 176.610 22.714 1.00 47.89 C HETATM 3366 C18 CLR A1213 37.371 175.578 22.257 1.00 46.10 C HETATM 3367 C19 CLR A1213 36.697 171.055 22.868 1.00 47.59 C HETATM 3368 C20 CLR A1213 39.370 177.744 21.706 1.00 51.34 C HETATM 3369 C21 CLR A1213 39.628 177.310 20.271 1.00 49.62 C HETATM 3370 C22 CLR A1213 40.233 178.956 22.079 1.00 59.77 C HETATM 3371 C23 CLR A1213 40.205 180.083 21.045 1.00 68.73 C HETATM 3372 C24 CLR A1213 40.727 181.390 21.640 1.00 74.99 C HETATM 3373 C25 CLR A1213 41.510 182.239 20.638 1.00 79.15 C HETATM 3374 C26 CLR A1213 40.718 182.539 19.369 1.00 78.45 C HETATM 3375 C27 CLR A1213 41.955 183.546 21.289 1.00 82.22 C HETATM 3376 O1 CLR A1213 38.272 166.814 24.478 1.00 45.97 O HETATM 3377 C1 OLB A1214 32.013 178.970 38.350 1.00 92.96 C HETATM 3378 C2 OLB A1214 31.241 180.143 37.826 1.00 97.58 C HETATM 3379 C3 OLB A1214 31.424 181.378 38.680 1.00 99.67 C HETATM 3380 C4 OLB A1214 30.776 182.603 38.074 1.00100.81 C HETATM 3381 C5 OLB A1214 31.020 183.859 38.876 1.00 99.59 C HETATM 3382 O19 OLB A1214 32.701 178.990 39.328 1.00 92.89 O HETATM 3383 O20 OLB A1214 31.871 177.894 37.569 1.00 86.51 O HETATM 3384 C21 OLB A1214 32.612 176.678 37.890 1.00 79.48 C HETATM 3385 C22 OLB A1214 32.242 175.603 36.902 1.00 76.72 C HETATM 3386 O23 OLB A1214 32.578 176.012 35.578 1.00 81.91 O HETATM 3387 C24 OLB A1214 32.941 174.292 37.218 1.00 71.42 C HETATM 3388 O25 OLB A1214 32.546 173.262 36.318 1.00 70.21 O HETATM 3389 C6 OLB A1214 30.536 185.154 38.248 1.00 93.40 C HETATM 3390 C7 OLB A1214 29.054 185.269 37.986 1.00 82.50 C HETATM 3391 C8 OLB A1214 28.684 186.631 37.416 1.00 72.49 C HETATM 3392 C9 OLB A1214 27.219 186.792 37.210 1.00 69.01 C HETATM 3393 C10 OLB A1214 26.483 187.710 37.819 1.00 69.53 C HETATM 3394 C1 OLA A1215 20.347 166.147 3.388 1.00108.12 C HETATM 3395 O1 OLA A1215 19.211 165.956 2.905 1.00111.38 O HETATM 3396 O2 OLA A1215 20.677 165.710 4.513 1.00108.18 O HETATM 3397 C2 OLA A1215 21.361 166.937 2.588 1.00102.34 C HETATM 3398 C3 OLA A1215 20.786 167.383 1.246 1.00 94.19 C HETATM 3399 C4 OLA A1215 21.475 168.646 0.740 1.00 87.45 C HETATM 3400 C5 OLA A1215 20.835 169.138 -0.551 1.00 83.94 C HETATM 3401 C6 OLA A1215 21.523 170.396 -1.079 1.00 80.01 C HETATM 3402 C7 OLA A1215 21.525 170.433 -2.608 1.00 75.02 C HETATM 3403 C8 OLA A1215 22.408 171.551 -3.159 1.00 72.34 C HETATM 3404 C9 OLA A1215 21.570 172.781 -3.419 1.00 71.07 C HETATM 3405 C10 OLA A1215 22.015 174.026 -3.218 1.00 66.79 C HETATM 3406 C11 OLA A1215 23.412 174.361 -2.734 1.00 59.87 C HETATM 3407 C12 OLA A1215 23.581 175.871 -2.852 1.00 57.03 C HETATM 3408 C13 OLA A1215 24.891 176.382 -2.278 1.00 60.63 C HETATM 3409 C14 OLA A1215 24.849 177.903 -2.152 1.00 64.73 C HETATM 3410 C1 OLA A1216 20.794 202.814 28.324 1.00 71.28 C HETATM 3411 O1 OLA A1216 21.391 201.878 27.767 1.00 76.08 O HETATM 3412 O2 OLA A1216 20.814 203.984 27.895 1.00 69.08 O HETATM 3413 C2 OLA A1216 20.014 202.517 29.575 1.00 69.43 C HETATM 3414 C3 OLA A1216 20.472 201.192 30.182 1.00 68.01 C HETATM 3415 C4 OLA A1216 19.653 200.022 29.655 1.00 64.43 C HETATM 3416 C5 OLA A1216 20.246 198.695 30.105 1.00 60.37 C HETATM 3417 C6 OLA A1216 19.496 197.522 29.495 1.00 57.68 C HETATM 3418 C7 OLA A1216 20.119 196.192 29.893 1.00 56.57 C HETATM 3419 C1 OLA A1217 34.560 170.483 2.402 1.00 90.58 C HETATM 3420 O1 OLA A1217 33.360 170.599 2.090 1.00 93.95 O HETATM 3421 O2 OLA A1217 34.996 169.489 3.027 1.00 92.28 O HETATM 3422 C2 OLA A1217 35.514 171.589 2.009 1.00 83.37 C HETATM 3423 C3 OLA A1217 34.810 172.692 1.224 1.00 75.81 C HETATM 3424 C4 OLA A1217 35.326 174.065 1.640 1.00 70.95 C HETATM 3425 C5 OLA A1217 35.491 174.986 0.438 1.00 69.53 C HETATM 3426 C6 OLA A1217 35.890 176.386 0.879 1.00 68.94 C HETATM 3427 C7 OLA A1217 34.808 177.410 0.548 1.00 67.10 C HETATM 3428 C1 OLA A1218 49.063 166.140 8.149 1.00 82.47 C HETATM 3429 O1 OLA A1218 49.503 165.853 7.016 1.00 84.64 O HETATM 3430 O2 OLA A1218 48.688 165.279 8.977 1.00 84.33 O HETATM 3431 C2 OLA A1218 48.985 167.593 8.537 1.00 77.27 C HETATM 3432 C3 OLA A1218 49.235 168.480 7.329 1.00 73.08 C HETATM 3433 C4 OLA A1218 48.639 169.859 7.568 1.00 71.13 C HETATM 3434 C5 OLA A1218 49.171 170.905 6.600 1.00 70.26 C HETATM 3435 C6 OLA A1218 48.289 172.149 6.638 1.00 70.85 C HETATM 3436 C7 OLA A1218 49.111 173.432 6.716 1.00 73.93 C HETATM 3437 C8 OLA A1218 49.770 173.753 5.385 1.00 78.02 C HETATM 3438 C9 OLA A1218 50.473 175.089 5.469 1.00 79.62 C HETATM 3439 C10 OLA A1218 51.593 175.303 4.779 1.00 79.45 C HETATM 3440 C1 OLA A1219 36.445 196.208 4.832 1.00 92.60 C HETATM 3441 O1 OLA A1219 36.765 195.121 5.356 1.00 94.15 O HETATM 3442 O2 OLA A1219 36.568 197.293 5.437 1.00 92.50 O HETATM 3443 C2 OLA A1219 35.892 196.211 3.420 1.00 90.33 C HETATM 3444 C3 OLA A1219 34.403 195.872 3.417 1.00 84.47 C HETATM 3445 C4 OLA A1219 33.840 195.787 1.998 1.00 73.29 C HETATM 3446 C5 OLA A1219 32.316 195.694 2.001 1.00 62.38 C HETATM 3447 C6 OLA A1219 31.851 194.266 2.225 1.00 54.22 C HETATM 3448 C7 OLA A1219 30.434 194.194 2.780 1.00 48.80 C HETATM 3449 C8 OLA A1219 30.039 192.738 2.953 1.00 47.26 C HETATM 3450 C9 OLA A1219 28.725 192.616 3.666 1.00 46.13 C HETATM 3451 C1 OLA A1220 9.792 198.272 6.406 1.00102.71 C HETATM 3452 O1 OLA A1220 9.683 198.855 5.306 1.00104.18 O HETATM 3453 O2 OLA A1220 9.279 198.719 7.459 1.00103.23 O HETATM 3454 C2 OLA A1220 10.584 196.983 6.466 1.00 99.84 C HETATM 3455 C3 OLA A1220 9.776 195.911 7.190 1.00 95.95 C HETATM 3456 C4 OLA A1220 10.654 194.756 7.670 1.00 89.95 C HETATM 3457 C5 OLA A1220 10.270 194.353 9.093 1.00 82.51 C HETATM 3458 C6 OLA A1220 10.923 193.037 9.492 1.00 77.02 C HETATM 3459 C7 OLA A1220 9.929 191.881 9.452 1.00 74.65 C HETATM 3460 C8 OLA A1220 9.316 191.552 10.817 1.00 73.64 C HETATM 3461 C9 OLA A1220 8.983 190.076 10.895 1.00 72.98 C HETATM 3462 C10 OLA A1220 8.647 189.502 12.055 1.00 72.61 C HETATM 3463 C11 OLA A1220 8.567 190.315 13.326 1.00 72.36 C HETATM 3464 C1 OLA A1221 16.457 163.136 1.986 1.00102.24 C HETATM 3465 O1 OLA A1221 15.796 162.089 1.801 1.00 97.35 O HETATM 3466 O2 OLA A1221 17.308 163.268 2.896 1.00110.15 O HETATM 3467 C2 OLA A1221 16.212 164.293 1.051 1.00 97.05 C HETATM 3468 C3 OLA A1221 15.859 165.554 1.833 1.00 89.40 C HETATM 3469 C4 OLA A1221 14.968 166.456 0.987 1.00 81.37 C HETATM 3470 C5 OLA A1221 14.937 167.892 1.495 1.00 74.64 C HETATM 3471 C6 OLA A1221 16.296 168.565 1.351 1.00 70.55 C HETATM 3472 C7 OLA A1221 16.122 170.045 1.026 1.00 68.43 C HETATM 3473 C8 OLA A1221 17.360 170.852 1.391 1.00 66.64 C HETATM 3474 C9 OLA A1221 17.276 172.215 0.747 1.00 65.51 C HETATM 3475 C10 OLA A1221 17.514 173.314 1.454 1.00 64.99 C HETATM 3476 C1 OLA A1222 36.882 170.592 8.063 1.00 95.76 C HETATM 3477 O1 OLA A1222 35.857 169.884 7.968 1.00 94.88 O HETATM 3478 O2 OLA A1222 37.621 170.566 9.071 1.00 99.93 O HETATM 3479 C2 OLA A1222 37.240 171.526 6.927 1.00 91.00 C HETATM 3480 C3 OLA A1222 36.552 172.867 7.125 1.00 86.38 C HETATM 3481 C4 OLA A1222 37.474 174.031 6.785 1.00 85.10 C HETATM 3482 C5 OLA A1222 37.704 174.155 5.284 1.00 86.87 C HETATM 3483 C6 OLA A1222 38.848 175.115 4.978 1.00 89.37 C HETATM 3484 C7 OLA A1222 38.674 176.448 5.697 1.00 90.36 C HETATM 3485 C8 OLA A1222 39.657 177.488 5.177 1.00 88.88 C HETATM 3486 C9 OLA A1222 39.657 178.671 6.118 1.00 86.57 C HETATM 3487 C9 OLA A1223 39.007 199.322 14.134 1.00 81.21 C HETATM 3488 C10 OLA A1223 38.006 198.447 14.214 1.00 80.13 C HETATM 3489 C11 OLA A1223 38.072 197.144 13.454 1.00 78.30 C HETATM 3490 C12 OLA A1223 37.889 195.971 14.417 1.00 76.61 C HETATM 3491 C13 OLA A1223 38.649 194.750 13.915 1.00 76.05 C HETATM 3492 C14 OLA A1223 38.284 193.461 14.642 1.00 76.88 C HETATM 3493 C15 OLA A1223 38.899 192.271 13.900 1.00 77.10 C HETATM 3494 C16 OLA A1223 38.663 190.948 14.624 1.00 75.25 C HETATM 3495 C17 OLA A1223 39.324 189.786 13.888 1.00 73.50 C HETATM 3496 C1 OLA A1224 44.616 205.703 13.627 1.00 77.20 C HETATM 3497 O1 OLA A1224 45.247 205.673 12.548 1.00 81.17 O HETATM 3498 O2 OLA A1224 44.549 206.719 14.358 1.00 76.42 O HETATM 3499 C2 OLA A1224 43.898 204.458 14.084 1.00 73.66 C HETATM 3500 C3 OLA A1224 44.651 203.193 13.682 1.00 72.14 C HETATM 3501 C4 OLA A1224 43.845 201.924 13.978 1.00 72.61 C HETATM 3502 C5 OLA A1224 43.180 201.936 15.357 1.00 74.04 C HETATM 3503 C6 OLA A1224 42.356 200.677 15.598 1.00 74.98 C HETATM 3504 C1 OLA A1225 34.141 196.729 27.373 1.00 77.91 C HETATM 3505 O1 OLA A1225 35.011 196.949 28.236 1.00 83.11 O HETATM 3506 O2 OLA A1225 33.491 197.652 26.850 1.00 75.82 O HETATM 3507 C2 OLA A1225 33.878 195.300 26.948 1.00 74.78 C HETATM 3508 C3 OLA A1225 34.709 194.356 27.806 1.00 74.04 C HETATM 3509 C4 OLA A1225 34.315 192.898 27.591 1.00 75.48 C HETATM 3510 C5 OLA A1225 34.587 192.089 28.859 1.00 76.76 C HETATM 3511 C6 OLA A1225 34.070 190.659 28.734 1.00 77.15 C HETATM 3512 C7 OLA A1225 34.928 189.681 29.532 1.00 77.74 C HETATM 3513 C8 OLA A1225 34.077 188.656 30.278 1.00 80.30 C HETATM 3514 C9 OLA A1225 34.881 187.386 30.471 1.00 83.09 C HETATM 3515 C10 OLA A1225 34.680 186.554 31.497 1.00 82.96 C HETATM 3516 C11 OLA A1225 33.614 186.801 32.541 1.00 80.49 C HETATM 3517 C12 OLA A1225 33.360 185.520 33.336 1.00 78.64 C HETATM 3518 C13 OLA A1225 31.866 185.225 33.476 1.00 78.13 C HETATM 3519 C14 OLA A1225 31.594 183.912 34.213 1.00 78.51 C HETATM 3520 C15 OLA A1225 31.401 182.734 33.259 1.00 78.42 C HETATM 3521 C16 OLA A1225 30.698 181.574 33.947 1.00 77.10 C HETATM 3522 C1 OLA A1226 37.273 167.251 13.602 1.00 72.14 C HETATM 3523 O1 OLA A1226 38.404 167.259 13.082 1.00 78.08 O HETATM 3524 O2 OLA A1226 36.775 166.211 14.078 1.00 71.80 O HETATM 3525 C2 OLA A1226 36.479 168.535 13.634 1.00 66.77 C HETATM 3526 C3 OLA A1226 37.358 169.760 13.370 1.00 62.98 C HETATM 3527 C4 OLA A1226 36.706 170.729 12.396 1.00 58.26 C HETATM 3528 C5 OLA A1226 37.415 172.074 12.423 1.00 56.05 C HETATM 3529 C6 OLA A1226 36.807 173.014 11.392 1.00 56.64 C HETATM 3530 C7 OLA A1226 37.304 174.440 11.574 1.00 57.99 C HETATM 3531 C8 OLA A1226 37.222 175.211 10.262 1.00 63.41 C HETATM 3532 C9 OLA A1226 37.422 176.684 10.513 1.00 70.80 C HETATM 3533 C10 OLA A1226 38.590 177.263 10.245 1.00 74.14 C HETATM 3534 C1 OLA A1227 39.508 164.346 18.329 1.00146.75 C HETATM 3535 O1 OLA A1227 39.869 164.051 17.170 1.00151.80 O HETATM 3536 O2 OLA A1227 38.759 163.622 19.018 1.00152.43 O HETATM 3537 C2 OLA A1227 40.003 165.642 18.918 1.00131.04 C HETATM 3538 C3 OLA A1227 40.041 166.678 17.808 1.00115.12 C HETATM 3539 C4 OLA A1227 39.947 168.093 18.348 1.00104.06 C HETATM 3540 C5 OLA A1227 38.992 168.914 17.505 1.00 92.62 C HETATM 3541 C6 OLA A1227 38.854 170.325 18.061 1.00 78.28 C HETATM 3542 C7 OLA A1227 38.447 171.281 16.953 1.00 67.69 C HETATM 3543 C8 OLA A1227 38.945 172.704 17.162 1.00 63.18 C HETATM 3544 C9 OLA A1227 37.756 173.584 17.436 1.00 60.18 C HETATM 3545 C10 OLA A1227 37.694 174.869 17.077 1.00 56.99 C HETATM 3546 C11 OLA A1227 38.784 175.580 16.327 1.00 55.57 C HETATM 3547 C12 OLA A1227 38.182 176.873 15.830 1.00 55.17 C HETATM 3548 C13 OLA A1227 39.229 177.820 15.270 1.00 56.93 C HETATM 3549 C14 OLA A1227 39.534 178.923 16.272 1.00 59.75 C HETATM 3550 C15 OLA A1227 40.221 180.100 15.597 1.00 62.18 C HETATM 3551 NA NA A1228 23.991 189.213 16.766 1.00 33.17 NA HETATM 3552 O HOH A1301 13.253 217.283 28.460 1.00 50.49 O HETATM 3553 O HOH A1302 13.170 163.036 12.119 1.00 62.81 O HETATM 3554 O HOH A1303 24.417 210.856 25.451 1.00 99.08 O HETATM 3555 O HOH A1304 13.142 214.503 21.222 1.00 48.15 O HETATM 3556 O HOH A1305 29.267 168.395 9.021 1.00 45.30 O HETATM 3557 O HOH A1306 22.841 204.598 29.283 1.00 92.70 O HETATM 3558 O HOH A1307 22.573 205.255 15.037 1.00 57.60 O HETATM 3559 O HOH A1308 26.164 195.517 24.849 1.00 36.67 O HETATM 3560 O HOH A1309 24.310 165.516 33.881 1.00 48.05 O HETATM 3561 O HOH A1310 18.555 167.916 24.475 1.00 40.89 O HETATM 3562 O HOH A1311 17.082 206.183 9.712 1.00 55.13 O HETATM 3563 O HOH A1312 23.831 185.406 14.327 1.00 30.53 O HETATM 3564 O HOH A1313 10.736 214.916 22.181 1.00 43.91 O HETATM 3565 O HOH A1314 28.205 177.943 17.275 1.00 24.76 O HETATM 3566 O HOH A1315 2.206 167.222 22.888 1.00 82.41 O HETATM 3567 O HOH A1316 25.589 196.680 14.711 1.00 25.64 O HETATM 3568 O HOH A1317 25.778 194.027 13.581 1.00 28.27 O HETATM 3569 O HOH A1318 28.674 164.186 9.492 1.00 93.47 O HETATM 3570 O HOH A1319 22.462 187.295 15.855 1.00 30.13 O HETATM 3571 O HOH A1320 26.517 162.039 22.631 1.00 34.03 O HETATM 3572 O HOH A1321 23.535 176.933 17.773 1.00 37.33 O HETATM 3573 O HOH A1322 24.149 191.783 11.480 1.00 28.81 O HETATM 3574 O HOH A1323 21.202 183.482 24.562 1.00 30.81 O HETATM 3575 O HOH A1324 26.434 193.077 21.800 1.00 32.61 O HETATM 3576 O HOH A1325 15.200 170.558 18.523 1.00 27.32 O HETATM 3577 O HOH A1326 19.495 182.252 22.232 1.00 29.46 O HETATM 3578 O HOH A1327 16.726 198.126 19.430 1.00 29.74 O HETATM 3579 O HOH A1328 9.738 165.478 19.513 1.00 78.72 O HETATM 3580 O HOH A1329 14.531 207.694 17.522 1.00 37.11 O HETATM 3581 O HOH A1330 11.499 168.418 16.403 1.00 32.11 O HETATM 3582 O HOH A1331 17.881 163.145 17.162 1.00 55.33 O HETATM 3583 O HOH A1332 26.412 172.992 13.724 1.00 30.36 O HETATM 3584 O HOH A1333 16.171 209.871 10.933 1.00 57.35 O HETATM 3585 O HOH A1334 20.052 216.482 26.684 1.00 56.92 O HETATM 3586 O HOH A1335 32.023 157.423 27.495 1.00 97.85 O HETATM 3587 O HOH A1336 21.167 164.089 19.281 1.00 39.97 O HETATM 3588 O HOH A1337 4.841 218.613 21.529 1.00 62.63 O HETATM 3589 O HOH A1338 14.240 208.867 19.994 1.00 41.20 O HETATM 3590 O HOH A1339 19.154 191.981 13.211 1.00 30.56 O HETATM 3591 O HOH A1340 16.637 179.874 13.169 1.00 28.20 O HETATM 3592 O HOH A1341 26.528 161.531 25.420 1.00 40.05 O HETATM 3593 O HOH A1342 34.298 167.110 31.318 1.00 47.69 O HETATM 3594 O HOH A1343 24.798 163.737 2.310 1.00 41.67 O HETATM 3595 O HOH A1344 18.777 170.601 23.541 1.00116.90 O HETATM 3596 O HOH A1345 29.114 178.156 19.915 1.00 27.87 O HETATM 3597 O HOH A1346 25.880 175.500 19.097 1.00 28.80 O HETATM 3598 O HOH A1347 22.141 209.877 9.254 1.00 48.02 O HETATM 3599 O HOH A1348 24.841 173.726 17.398 1.00 38.30 O HETATM 3600 O HOH A1349 23.253 209.175 21.603 1.00 44.45 O HETATM 3601 O HOH A1350 18.324 164.533 19.395 1.00 43.56 O HETATM 3602 O HOH A1351 24.743 185.089 17.709 1.00 38.40 O HETATM 3603 O HOH A1352 18.122 183.637 20.223 1.00 30.87 O HETATM 3604 O HOH A1353 10.223 160.998 21.008 1.00 79.34 O HETATM 3605 O HOH A1354 16.570 208.966 17.061 1.00 58.78 O HETATM 3606 O HOH A1355 22.493 162.518 26.728 1.00 60.72 O HETATM 3607 O HOH A1356 19.375 163.497 22.796 1.00 77.88 O HETATM 3608 O HOH A1357 22.822 190.680 15.348 1.00 34.58 O HETATM 3609 O HOH A1358 25.687 177.777 16.100 1.00 32.78 O HETATM 3610 O HOH A1359 27.676 192.192 6.528 1.00 42.31 O HETATM 3611 O HOH A1360 22.218 166.849 18.502 1.00 32.81 O HETATM 3612 O HOH A1361 28.588 169.130 35.197 1.00 49.36 O HETATM 3613 O HOH A1362 4.691 206.963 25.331 1.00 51.65 O HETATM 3614 O HOH A1363 4.333 244.963 18.191 1.00 71.68 O HETATM 3615 O HOH A1364 21.076 192.212 15.565 1.00 47.59 O HETATM 3616 O HOH A1365 18.146 198.145 16.982 1.00 41.08 O HETATM 3617 O HOH A1366 0.454 244.084 19.968 1.00 75.73 O HETATM 3618 O HOH A1367 5.195 163.921 13.864 1.00 65.62 O HETATM 3619 O HOH A1368 26.431 193.171 25.874 1.00 40.73 O HETATM 3620 O HOH A1369 36.246 161.644 17.313 1.00 56.78 O HETATM 3621 O HOH A1370 15.350 177.140 22.314 1.00 25.21 O HETATM 3622 O HOH A1371 25.784 168.943 17.117 1.00 30.52 O HETATM 3623 O HOH A1372 16.667 163.475 9.403 1.00 48.67 O HETATM 3624 O HOH A1373 20.200 168.027 32.995 1.00 60.57 O HETATM 3625 O HOH A1374 23.471 212.772 36.196 1.00 54.34 O HETATM 3626 O HOH A1375 28.321 175.250 18.179 1.00 38.36 O HETATM 3627 O HOH A1376 25.563 210.594 22.877 1.00 48.92 O HETATM 3628 O HOH A1377 19.194 208.957 7.904 1.00 50.14 O HETATM 3629 O HOH A1378 23.207 178.996 16.070 1.00 36.14 O HETATM 3630 O HOH A1379 25.098 170.808 15.198 1.00 37.58 O HETATM 3631 O HOH A1380 25.738 187.733 17.755 1.00 39.05 O HETATM 3632 O HOH A1381 25.804 163.531 27.153 1.00 40.46 O HETATM 3633 O HOH A1382 17.445 167.149 26.787 1.00 45.12 O HETATM 3634 O HOH A1383 31.187 210.499 29.525 1.00 57.27 O HETATM 3635 O HOH A1384 15.498 168.361 29.063 1.00 37.94 O HETATM 3636 O HOH A1385 9.211 167.123 17.549 1.00 38.91 O HETATM 3637 O HOH A1386 -15.775 236.555 18.125 1.00 64.87 O HETATM 3638 O HOH A1387 3.340 164.519 22.397 1.00 54.77 O HETATM 3639 O HOH A1388 17.707 165.141 6.456 1.00 46.67 O HETATM 3640 O HOH A1389 5.444 212.413 25.400 1.00 61.73 O HETATM 3641 O HOH A1390 8.693 170.327 32.284 1.00 83.08 O HETATM 3642 O HOH A1391 30.940 160.158 3.734 1.00 54.50 O HETATM 3643 O HOH A1392 11.706 170.063 32.975 1.00 53.86 O HETATM 3644 O HOH A1393 16.028 163.687 12.770 1.00 60.35 O HETATM 3645 O HOH A1394 17.392 167.023 30.474 1.00 77.52 O HETATM 3646 O HOH A1395 23.734 207.534 13.519 1.00 66.60 O HETATM 3647 O HOH A1396 17.881 168.549 33.114 1.00 89.63 O HETATM 3648 O HOH A1397 16.221 166.457 22.733 1.00 74.66 O HETATM 3649 O HOH A1398 7.357 168.752 28.434 1.00 79.19 O HETATM 3650 O HOH A1399 23.696 210.330 13.563 1.00118.05 O HETATM 3651 O HOH A1400 13.660 166.782 24.696 1.00 48.64 O HETATM 3652 O HOH A1401 18.337 208.260 10.700 1.00 53.90 O HETATM 3653 O HOH A1402 25.454 174.857 15.585 1.00 51.76 O HETATM 3654 O HOH A1403 31.404 203.009 -2.934 1.00 43.36 O HETATM 3655 O HOH A1404 23.349 163.703 36.221 1.00 81.76 O HETATM 3656 O HOH A1405 19.833 208.330 12.725 1.00 68.42 O CONECT 415 3551 CONECT 553 1238 CONECT 569 1139 CONECT 589 1282 CONECT 708 3551 CONECT 1139 569 CONECT 1238 553 CONECT 1282 589 CONECT 2694 2715 CONECT 2715 2694 CONECT 3133 3134 3139 CONECT 3134 3133 3135 CONECT 3135 3134 3136 3137 CONECT 3136 3135 CONECT 3137 3135 3138 CONECT 3138 3137 3139 CONECT 3139 3133 3138 3140 CONECT 3140 3139 3141 CONECT 3141 3140 3142 CONECT 3142 3141 3143 CONECT 3143 3142 3144 3145 CONECT 3144 3143 3150 CONECT 3145 3143 3146 CONECT 3146 3145 3147 3148 CONECT 3147 3146 CONECT 3148 3146 3149 3150 CONECT 3149 3148 3152 CONECT 3150 3144 3148 3151 CONECT 3151 3150 3152 CONECT 3152 3149 3151 3153 CONECT 3153 3152 3154 3157 CONECT 3154 3153 3155 CONECT 3155 3154 3156 CONECT 3156 3155 3157 CONECT 3157 3153 3156 CONECT 3158 3159 CONECT 3159 3158 3160 CONECT 3160 3159 3162 CONECT 3161 3170 3172 CONECT 3162 3160 3163 CONECT 3163 3162 3164 CONECT 3164 3163 3165 CONECT 3165 3164 3166 CONECT 3166 3165 3167 CONECT 3167 3166 3169 CONECT 3168 3170 3174 CONECT 3169 3167 3171 3174 CONECT 3170 3161 3168 3173 CONECT 3171 3169 CONECT 3172 3161 CONECT 3173 3170 CONECT 3174 3168 3169 CONECT 3175 3176 CONECT 3176 3175 3178 CONECT 3177 3186 3188 CONECT 3178 3176 3179 CONECT 3179 3178 3180 CONECT 3180 3179 3181 CONECT 3181 3180 3182 CONECT 3182 3181 3183 CONECT 3183 3182 3185 CONECT 3184 3186 3190 CONECT 3185 3183 3187 3190 CONECT 3186 3177 3184 3189 CONECT 3187 3185 CONECT 3188 3177 CONECT 3189 3186 CONECT 3190 3184 3185 CONECT 3191 3192 3193 CONECT 3192 3191 3194 CONECT 3193 3191 CONECT 3194 3192 3196 CONECT 3195 3204 3206 CONECT 3196 3194 3197 CONECT 3197 3196 3198 CONECT 3198 3197 3199 CONECT 3199 3198 3200 CONECT 3200 3199 3201 CONECT 3201 3200 3203 CONECT 3202 3204 3208 CONECT 3203 3201 3205 3208 CONECT 3204 3195 3202 3207 CONECT 3205 3203 CONECT 3206 3195 CONECT 3207 3204 CONECT 3208 3202 3203 CONECT 3209 3210 CONECT 3210 3209 3211 CONECT 3211 3210 3213 CONECT 3212 3221 3223 CONECT 3213 3211 3214 CONECT 3214 3213 3215 CONECT 3215 3214 3216 CONECT 3216 3215 3217 CONECT 3217 3216 3218 CONECT 3218 3217 3220 CONECT 3219 3221 3225 CONECT 3220 3218 3222 3225 CONECT 3221 3212 3219 3224 CONECT 3222 3220 CONECT 3223 3212 CONECT 3224 3221 CONECT 3225 3219 3220 CONECT 3226 3227 CONECT 3227 3226 3228 CONECT 3228 3227 3230 CONECT 3229 3238 3240 CONECT 3230 3228 3231 CONECT 3231 3230 3232 CONECT 3232 3231 3233 CONECT 3233 3232 3234 CONECT 3234 3233 3235 CONECT 3235 3234 3237 CONECT 3236 3238 3242 CONECT 3237 3235 3239 3242 CONECT 3238 3229 3236 3241 CONECT 3239 3237 CONECT 3240 3229 CONECT 3241 3238 CONECT 3242 3236 3237 CONECT 3243 3249 3251 CONECT 3244 3245 CONECT 3245 3244 3246 CONECT 3246 3245 3248 CONECT 3247 3249 3253 CONECT 3248 3246 3250 3253 CONECT 3249 3243 3247 3252 CONECT 3250 3248 CONECT 3251 3243 CONECT 3252 3249 CONECT 3253 3247 3248 CONECT 3254 3260 3262 CONECT 3255 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3259 CONECT 3258 3260 3264 CONECT 3259 3257 3261 3264 CONECT 3260 3254 3258 3263 CONECT 3261 3259 CONECT 3262 3254 CONECT 3263 3260 CONECT 3264 3258 3259 CONECT 3265 3271 3273 CONECT 3266 3267 CONECT 3267 3266 3268 CONECT 3268 3267 3270 CONECT 3269 3271 3275 CONECT 3270 3268 3272 3275 CONECT 3271 3265 3269 3274 CONECT 3272 3270 CONECT 3273 3265 CONECT 3274 3271 CONECT 3275 3269 3270 CONECT 3276 3277 CONECT 3277 3276 3278 CONECT 3278 3277 3280 CONECT 3279 3288 3290 CONECT 3280 3278 3281 CONECT 3281 3280 3282 CONECT 3282 3281 3283 CONECT 3283 3282 3284 CONECT 3284 3283 3285 CONECT 3285 3284 3287 CONECT 3286 3288 3292 CONECT 3287 3285 3289 3292 CONECT 3288 3279 3286 3291 CONECT 3289 3287 CONECT 3290 3279 CONECT 3291 3288 CONECT 3292 3286 3287 CONECT 3293 3294 3302 CONECT 3294 3293 3295 CONECT 3295 3294 3296 3320 CONECT 3296 3295 3297 CONECT 3297 3296 3298 3302 CONECT 3298 3297 3299 CONECT 3299 3298 3300 CONECT 3300 3299 3301 3306 CONECT 3301 3300 3302 3303 CONECT 3302 3293 3297 3301 3311 CONECT 3303 3301 3304 CONECT 3304 3303 3305 CONECT 3305 3304 3306 3309 3310 CONECT 3306 3300 3305 3307 CONECT 3307 3306 3308 CONECT 3308 3307 3309 CONECT 3309 3305 3308 3312 CONECT 3310 3305 CONECT 3311 3302 CONECT 3312 3309 3313 3314 CONECT 3313 3312 CONECT 3314 3312 3315 CONECT 3315 3314 3316 CONECT 3316 3315 3317 CONECT 3317 3316 3318 3319 CONECT 3318 3317 CONECT 3319 3317 CONECT 3320 3295 CONECT 3321 3322 3330 CONECT 3322 3321 3323 CONECT 3323 3322 3324 3348 CONECT 3324 3323 3325 CONECT 3325 3324 3326 3330 CONECT 3326 3325 3327 CONECT 3327 3326 3328 CONECT 3328 3327 3329 3334 CONECT 3329 3328 3330 3331 CONECT 3330 3321 3325 3329 3339 CONECT 3331 3329 3332 CONECT 3332 3331 3333 CONECT 3333 3332 3334 3337 3338 CONECT 3334 3328 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3333 3336 3340 CONECT 3338 3333 CONECT 3339 3330 CONECT 3340 3337 3341 3342 CONECT 3341 3340 CONECT 3342 3340 3343 CONECT 3343 3342 3344 CONECT 3344 3343 3345 CONECT 3345 3344 3346 3347 CONECT 3346 3345 CONECT 3347 3345 CONECT 3348 3323 CONECT 3349 3350 3358 CONECT 3350 3349 3351 CONECT 3351 3350 3352 3376 CONECT 3352 3351 3353 CONECT 3353 3352 3354 3358 CONECT 3354 3353 3355 CONECT 3355 3354 3356 CONECT 3356 3355 3357 3362 CONECT 3357 3356 3358 3359 CONECT 3358 3349 3353 3357 3367 CONECT 3359 3357 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3362 3365 3366 CONECT 3362 3356 3361 3363 CONECT 3363 3362 3364 CONECT 3364 3363 3365 CONECT 3365 3361 3364 3368 CONECT 3366 3361 CONECT 3367 3358 CONECT 3368 3365 3369 3370 CONECT 3369 3368 CONECT 3370 3368 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 3375 CONECT 3374 3373 CONECT 3375 3373 CONECT 3376 3351 CONECT 3377 3378 3382 3383 CONECT 3378 3377 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3389 CONECT 3382 3377 CONECT 3383 3377 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 3387 CONECT 3386 3385 CONECT 3387 3385 3388 CONECT 3388 3387 CONECT 3389 3381 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 CONECT 3394 3395 3396 3397 CONECT 3395 3394 CONECT 3396 3394 CONECT 3397 3394 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 CONECT 3403 3402 3404 CONECT 3404 3403 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 CONECT 3408 3407 3409 CONECT 3409 3408 CONECT 3410 3411 3412 3413 CONECT 3411 3410 CONECT 3412 3410 CONECT 3413 3410 3414 CONECT 3414 3413 3415 CONECT 3415 3414 3416 CONECT 3416 3415 3417 CONECT 3417 3416 3418 CONECT 3418 3417 CONECT 3419 3420 3421 3422 CONECT 3420 3419 CONECT 3421 3419 CONECT 3422 3419 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 CONECT 3428 3429 3430 3431 CONECT 3429 3428 CONECT 3430 3428 CONECT 3431 3428 3432 CONECT 3432 3431 3433 CONECT 3433 3432 3434 CONECT 3434 3433 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3437 CONECT 3437 3436 3438 CONECT 3438 3437 3439 CONECT 3439 3438 CONECT 3440 3441 3442 3443 CONECT 3441 3440 CONECT 3442 3440 CONECT 3443 3440 3444 CONECT 3444 3443 3445 CONECT 3445 3444 3446 CONECT 3446 3445 3447 CONECT 3447 3446 3448 CONECT 3448 3447 3449 CONECT 3449 3448 3450 CONECT 3450 3449 CONECT 3451 3452 3453 3454 CONECT 3452 3451 CONECT 3453 3451 CONECT 3454 3451 3455 CONECT 3455 3454 3456 CONECT 3456 3455 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3459 CONECT 3459 3458 3460 CONECT 3460 3459 3461 CONECT 3461 3460 3462 CONECT 3462 3461 3463 CONECT 3463 3462 CONECT 3464 3465 3466 3467 CONECT 3465 3464 CONECT 3466 3464 CONECT 3467 3464 3468 CONECT 3468 3467 3469 CONECT 3469 3468 3470 CONECT 3470 3469 3471 CONECT 3471 3470 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 3475 CONECT 3475 3474 CONECT 3476 3477 3478 3479 CONECT 3477 3476 CONECT 3478 3476 CONECT 3479 3476 3480 CONECT 3480 3479 3481 CONECT 3481 3480 3482 CONECT 3482 3481 3483 CONECT 3483 3482 3484 CONECT 3484 3483 3485 CONECT 3485 3484 3486 CONECT 3486 3485 CONECT 3487 3488 CONECT 3488 3487 3489 CONECT 3489 3488 3490 CONECT 3490 3489 3491 CONECT 3491 3490 3492 CONECT 3492 3491 3493 CONECT 3493 3492 3494 CONECT 3494 3493 3495 CONECT 3495 3494 CONECT 3496 3497 3498 3499 CONECT 3497 3496 CONECT 3498 3496 CONECT 3499 3496 3500 CONECT 3500 3499 3501 CONECT 3501 3500 3502 CONECT 3502 3501 3503 CONECT 3503 3502 CONECT 3504 3505 3506 3507 CONECT 3505 3504 CONECT 3506 3504 CONECT 3507 3504 3508 CONECT 3508 3507 3509 CONECT 3509 3508 3510 CONECT 3510 3509 3511 CONECT 3511 3510 3512 CONECT 3512 3511 3513 CONECT 3513 3512 3514 CONECT 3514 3513 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 CONECT 3522 3523 3524 3525 CONECT 3523 3522 CONECT 3524 3522 CONECT 3525 3522 3526 CONECT 3526 3525 3527 CONECT 3527 3526 3528 CONECT 3528 3527 3529 CONECT 3529 3528 3530 CONECT 3530 3529 3531 CONECT 3531 3530 3532 CONECT 3532 3531 3533 CONECT 3533 3532 CONECT 3534 3535 3536 3537 CONECT 3535 3534 CONECT 3536 3534 CONECT 3537 3534 3538 CONECT 3538 3537 3539 CONECT 3539 3538 3540 CONECT 3540 3539 3541 CONECT 3541 3540 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3545 3547 CONECT 3547 3546 3548 CONECT 3548 3547 3549 CONECT 3549 3548 3550 CONECT 3550 3549 CONECT 3551 415 708 3570 3608 CONECT 3551 3631 CONECT 3570 3551 CONECT 3608 3551 CONECT 3631 3551 MASTER 474 0 28 19 2 0 33 6 3511 1 433 34 END