HEADER MEMBRANE PROTEIN 17-JUN-22 8A6E TITLE 100 PICOSECOND LIGHT ACTIVATED CRYSTAL STRUCTURE OF BOVINE RHODOPSIN TITLE 2 IN LIPIDIC CUBIC PHASE (SACLA) COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A, B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913 KEYWDS GPCR, OPSIN, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.GRUHL,T.WEINERT,M.J.RODRIGUES,C.J.MILNE,G.ORTOLANI,K.NASS,E.NANGO, AUTHOR 2 S.SEN,P.J.M.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS,P.SKOPINTSEV,D.JAMES, AUTHOR 3 F.DWORKOWSKI,P.BAATH,D.KEKILLI,D.OSEROV,R.TANAKA,H.GLOVER, AUTHOR 4 C.BACELLAR,S.BRUENLE,C.M.CASADEI,A.D.DIETHELM,D.GASHI,G.GOTTHARD, AUTHOR 5 R.GUIXA-GONZALEZ,Y.JOTI,V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL, AUTHOR 6 J.MUEHLE,S.OWADA,F.PAMULA,D.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH, AUTHOR 7 S.BOUTET,K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS, AUTHOR 8 G.F.X.SCHERTLER,V.PANNEELS REVDAT 3 12-APR-23 8A6E 1 JRNL REVDAT 2 05-APR-23 8A6E 1 JRNL REVDAT 1 29-MAR-23 8A6E 0 JRNL AUTH T.GRUHL,T.WEINERT,M.J.RODRIGUES,C.J.MILNE,G.ORTOLANI,K.NASS, JRNL AUTH 2 E.NANGO,S.SEN,P.J.M.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS, JRNL AUTH 3 P.SKOPINTSEV,D.JAMES,F.DWORKOWSKI,P.BATH,D.KEKILLI,D.OZEROV, JRNL AUTH 4 R.TANAKA,H.GLOVER,C.BACELLAR,S.BRUNLE,C.M.CASADEI, JRNL AUTH 5 A.D.DIETHELM,D.GASHI,G.GOTTHARD,R.GUIXA-GONZALEZ,Y.JOTI, JRNL AUTH 6 V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL,J.MUHLE,S.OWADA, JRNL AUTH 7 F.PAMULA,D.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH,S.BOUTET, JRNL AUTH 8 K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS, JRNL AUTH 9 G.SCHERTLER,V.PANNEELS JRNL TITL ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR JRNL TITL 2 EVENTS OF VISION. JRNL REF NATURE V. 615 939 2023 JRNL REFN ESSN 1476-4687 JRNL PMID 36949205 JRNL DOI 10.1038/S41586-023-05863-6 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.GRUHL,T.WEINERT,M.RODRIGUES,C.J.MILNE,G.ORTOLANI,K.NASS, REMARK 1 AUTH 2 E.NANGO,S.SEN,P.J.M.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS, REMARK 1 AUTH 3 P.SKOPINTSEV,D.JAMES,F.DWORKOWSKI,P.BATH,D.KEKILLI,D.OZEROV, REMARK 1 AUTH 4 R.TANAKA,H.GLOVER,C.BACELLAR,S.BRUNLE,C.M.CASADEI, REMARK 1 AUTH 5 A.D.DIETHELM,D.GASHI,G.GOTTHARD,R.GUIXA-GONZALEZ,Y.JOTI, REMARK 1 AUTH 6 V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL,J.MUHLE,S.OWADA, REMARK 1 AUTH 7 F.PAMULA,D.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH,S.BOUTET, REMARK 1 AUTH 8 K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS, REMARK 1 AUTH 9 G.F.SCHERTLER,V.PANNEELS REMARK 1 TITL ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR REMARK 1 TITL 2 EVENTS OF VISION REMARK 1 REF BIORXIV 2022 REMARK 1 REFN ISSN 2692-8205 REMARK 1 DOI 10.1101/2022.10.14.511948 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20_4459 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.47 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 87.1 REMARK 3 NUMBER OF REFLECTIONS : 68049 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.332 REMARK 3 R VALUE (WORKING SET) : 0.332 REMARK 3 FREE R VALUE : 0.369 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.450 REMARK 3 FREE R VALUE TEST SET COUNT : 989 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 10.4700 - 3.4100 0.93 10615 155 0.2353 0.2610 REMARK 3 2 3.4100 - 2.7200 0.93 10270 153 0.2755 0.3558 REMARK 3 3 2.7200 - 2.3800 0.90 9841 147 0.3443 0.3461 REMARK 3 4 2.3800 - 2.1700 0.87 9524 135 0.4110 0.4498 REMARK 3 5 2.1700 - 2.0100 0.85 9249 133 0.4812 0.5197 REMARK 3 6 2.0100 - 1.8900 0.81 8838 131 0.5542 0.5865 REMARK 3 7 1.8900 - 1.8000 0.80 8723 135 0.6064 0.6854 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.442 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 48.899 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.18 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 5497 REMARK 3 ANGLE : 0.623 7453 REMARK 3 CHIRALITY : 0.041 828 REMARK 3 PLANARITY : 0.005 912 REMARK 3 DIHEDRAL : 12.395 2017 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -5.3783 28.2035 37.5163 REMARK 3 T TENSOR REMARK 3 T11: 0.2086 T22: 0.1712 REMARK 3 T33: 0.2088 T12: -0.0168 REMARK 3 T13: 0.0510 T23: -0.0049 REMARK 3 L TENSOR REMARK 3 L11: 0.6236 L22: 0.3140 REMARK 3 L33: 0.3665 L12: -0.2580 REMARK 3 L13: -0.2924 L23: 0.0376 REMARK 3 S TENSOR REMARK 3 S11: -0.0169 S12: -0.0045 S13: 0.0574 REMARK 3 S21: 0.0020 S22: -0.0093 S23: -0.0040 REMARK 3 S31: 0.0049 S32: -0.0172 S33: 0.0000 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8A6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-22. REMARK 100 THE DEPOSITION ID IS D_1292121880. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-NOV-18 REMARK 200 TEMPERATURE (KELVIN) : 294 REMARK 200 PH : 9.0 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 : BL3 REMARK 200 X-RAY GENERATOR MODEL : SACLA BEAMLINE BL3 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.24 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MPCCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78209 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 10.470 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 679.1 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 487.5 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> 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: 1U19 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 36 % PEG 600, 100 MM BICINE PH 9.0, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 X,-Y,-Z REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.40500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.25500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.40500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 75.25500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26780 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C 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 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -45.40500 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 75.25500 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 143 REMARK 465 SER A 144 REMARK 465 ASN A 145 REMARK 465 PHE A 146 REMARK 465 VAL A 230 REMARK 465 LYS A 231 REMARK 465 GLU A 232 REMARK 465 ALA A 233 REMARK 465 ALA A 234 REMARK 465 ALA A 235 REMARK 465 GLN A 236 REMARK 465 GLN A 237 REMARK 465 GLN A 238 REMARK 465 GLU A 239 REMARK 465 SER A 240 REMARK 465 ALA A 241 REMARK 465 THR A 242 REMARK 465 THR A 243 REMARK 465 GLN A 244 REMARK 465 CYS A 323 REMARK 465 GLY A 324 REMARK 465 LYS A 325 REMARK 465 ASN A 326 REMARK 465 PRO A 327 REMARK 465 LEU A 328 REMARK 465 GLY A 329 REMARK 465 ASP A 330 REMARK 465 ASP A 331 REMARK 465 GLU A 332 REMARK 465 ALA A 333 REMARK 465 SER A 334 REMARK 465 THR A 335 REMARK 465 THR A 336 REMARK 465 VAL A 337 REMARK 465 SER A 338 REMARK 465 LYS A 339 REMARK 465 THR A 340 REMARK 465 GLU A 341 REMARK 465 THR A 342 REMARK 465 SER A 343 REMARK 465 GLN A 344 REMARK 465 VAL A 345 REMARK 465 ALA A 346 REMARK 465 PRO A 347 REMARK 465 ALA A 348 REMARK 465 MET B 143 REMARK 465 SER B 144 REMARK 465 ASN B 145 REMARK 465 PHE B 146 REMARK 465 VAL B 230 REMARK 465 LYS B 231 REMARK 465 GLU B 232 REMARK 465 ALA B 233 REMARK 465 ALA B 234 REMARK 465 ALA B 235 REMARK 465 GLN B 236 REMARK 465 GLN B 237 REMARK 465 GLN B 238 REMARK 465 GLU B 239 REMARK 465 SER B 240 REMARK 465 ALA B 241 REMARK 465 THR B 242 REMARK 465 THR B 243 REMARK 465 CYS B 323 REMARK 465 GLY B 324 REMARK 465 LYS B 325 REMARK 465 ASN B 326 REMARK 465 PRO B 327 REMARK 465 LEU B 328 REMARK 465 GLY B 329 REMARK 465 ASP B 330 REMARK 465 ASP B 331 REMARK 465 GLU B 332 REMARK 465 ALA B 333 REMARK 465 SER B 334 REMARK 465 THR B 335 REMARK 465 THR B 336 REMARK 465 VAL B 337 REMARK 465 SER B 338 REMARK 465 LYS B 339 REMARK 465 THR B 340 REMARK 465 GLU B 341 REMARK 465 THR B 342 REMARK 465 SER B 343 REMARK 465 GLN B 344 REMARK 465 VAL B 345 REMARK 465 ALA B 346 REMARK 465 PRO B 347 REMARK 465 ALA B 348 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 MET A 1 CG SD CE REMARK 470 LYS A 66 CG CD CE NZ REMARK 470 LYS A 67 CD CE NZ REMARK 470 ARG A 147 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 228 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 245 CE NZ REMARK 470 MET B 1 CG SD CE REMARK 470 LYS B 66 CG CD CE NZ REMARK 470 LYS B 67 CE NZ REMARK 470 ARG B 147 CD NE CZ NH1 NH2 REMARK 470 PHE B 228 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR B 229 OG1 CG2 REMARK 470 GLN B 244 CG CD OE1 NE2 REMARK 470 LYS B 245 CE NZ REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 ILE B 213 CA CB CG1 CG2 CD1 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 GLN A 28 39.13 -97.59 REMARK 500 SER A 176 -161.75 64.29 REMARK 500 PHE A 212 -39.52 -130.56 REMARK 500 PHE A 212 -39.15 -130.56 REMARK 500 PHE A 228 56.43 -98.26 REMARK 500 GLN B 28 35.46 -94.37 REMARK 500 PHE B 105 0.84 -68.57 REMARK 500 SER B 176 -165.37 61.50 REMARK 500 HIS B 195 62.99 39.55 REMARK 500 PHE B 212 -59.14 -125.25 REMARK 500 PHE B 228 49.13 -88.25 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 406 REMARK 610 OLC A 407 REMARK 610 OLC A 408 REMARK 610 OLC A 409 REMARK 610 OLC A 411 REMARK 610 OLC A 413 REMARK 610 OLC A 415 REMARK 610 OLC B 404 REMARK 610 OLC B 405 REMARK 610 PLM B 406 REMARK 610 OLC B 407 DBREF 8A6E A 1 348 UNP P02699 OPSD_BOVIN 1 348 DBREF 8A6E B 1 348 UNP P02699 OPSD_BOVIN 1 348 SEQRES 1 A 348 MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE SEQRES 2 A 348 SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA SEQRES 3 A 348 PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET SEQRES 4 A 348 LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE SEQRES 5 A 348 PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS SEQRES 6 A 348 LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN SEQRES 7 A 348 LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE SEQRES 8 A 348 THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL SEQRES 9 A 348 PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA SEQRES 10 A 348 THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL SEQRES 11 A 348 LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET SEQRES 12 A 348 SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY SEQRES 13 A 348 VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA SEQRES 14 A 348 PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY SEQRES 15 A 348 MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS SEQRES 16 A 348 GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE SEQRES 17 A 348 VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE SEQRES 18 A 348 CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA SEQRES 19 A 348 ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU SEQRES 20 A 348 LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA SEQRES 21 A 348 PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE SEQRES 22 A 348 TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE SEQRES 23 A 348 PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA SEQRES 24 A 348 VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN SEQRES 25 A 348 PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS SEQRES 26 A 348 ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER SEQRES 27 A 348 LYS THR GLU THR SER GLN VAL ALA PRO ALA SEQRES 1 B 348 MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE SEQRES 2 B 348 SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA SEQRES 3 B 348 PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET SEQRES 4 B 348 LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE SEQRES 5 B 348 PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS SEQRES 6 B 348 LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN SEQRES 7 B 348 LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE SEQRES 8 B 348 THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL SEQRES 9 B 348 PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA SEQRES 10 B 348 THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL SEQRES 11 B 348 LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET SEQRES 12 B 348 SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY SEQRES 13 B 348 VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA SEQRES 14 B 348 PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY SEQRES 15 B 348 MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS SEQRES 16 B 348 GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE SEQRES 17 B 348 VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE SEQRES 18 B 348 CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA SEQRES 19 B 348 ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU SEQRES 20 B 348 LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA SEQRES 21 B 348 PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE SEQRES 22 B 348 TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE SEQRES 23 B 348 PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA SEQRES 24 B 348 VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN SEQRES 25 B 348 PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS SEQRES 26 B 348 ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER SEQRES 27 B 348 LYS THR GLU THR SER GLN VAL ALA PRO ALA HET NAG C 1 14 HET NAG C 2 14 HET NAG D 1 14 HET NAG D 2 14 HET ACE A 401 3 HET RET A 402 20 HET NAG A 403 14 HET DAO A 404 14 HET OLC A 405 25 HET OLC A 406 22 HET OLC A 407 7 HET OLC A 408 10 HET OLC A 409 12 HET PLM A 410 17 HET OLC A 411 10 HET OLC A 412 25 HET OLC A 413 10 HET OLC A 414 25 HET OLC A 415 13 HET ACE B 401 3 HET RET B 402 20 HET NAG B 403 14 HET OLC B 404 19 HET OLC B 405 18 HET PLM B 406 7 HET OLC B 407 7 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM ACE ACETYL GROUP HETNAM RET RETINAL HETNAM DAO LAURIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM PLM PALMITIC ACID HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 3 NAG 6(C8 H15 N O6) FORMUL 5 ACE 2(C2 H4 O) FORMUL 6 RET 2(C20 H28 O) FORMUL 8 DAO C12 H24 O2 FORMUL 9 OLC 13(C21 H40 O4) FORMUL 14 PLM 2(C16 H32 O2) FORMUL 27 HOH *140(H2 O) HELIX 1 AA1 GLU A 33 HIS A 65 1 33 HELIX 2 AA2 THR A 70 GLY A 90 1 21 HELIX 3 AA3 GLY A 90 GLY A 101 1 12 HELIX 4 AA4 PHE A 105 LYS A 141 1 37 HELIX 5 AA5 GLY A 149 ALA A 169 1 21 HELIX 6 AA6 PRO A 170 VAL A 173 5 4 HELIX 7 AA7 HIS A 195 THR A 198 5 4 HELIX 8 AA8 ASN A 199 HIS A 211 1 13 HELIX 9 AA9 PHE A 212 PHE A 228 1 17 HELIX 10 AB1 ALA A 246 HIS A 278 1 33 HELIX 11 AB2 PRO A 285 ALA A 295 1 11 HELIX 12 AB3 LYS A 296 ALA A 299 5 4 HELIX 13 AB4 VAL A 300 ASN A 310 1 11 HELIX 14 AB5 ASN A 310 CYS A 322 1 13 HELIX 15 AB6 GLU B 33 HIS B 65 1 33 HELIX 16 AB7 THR B 70 GLY B 90 1 21 HELIX 17 AB8 GLY B 90 GLY B 101 1 12 HELIX 18 AB9 PHE B 105 LYS B 141 1 37 HELIX 19 AC1 GLY B 149 ALA B 169 1 21 HELIX 20 AC2 PRO B 170 VAL B 173 5 4 HELIX 21 AC3 HIS B 195 THR B 198 5 4 HELIX 22 AC4 ASN B 199 HIS B 211 1 13 HELIX 23 AC5 PHE B 212 PHE B 228 1 17 HELIX 24 AC6 LYS B 245 HIS B 278 1 34 HELIX 25 AC7 PRO B 285 ALA B 295 1 11 HELIX 26 AC8 LYS B 296 ALA B 299 5 4 HELIX 27 AC9 VAL B 300 ASN B 310 1 11 HELIX 28 AD1 ASN B 310 CYS B 322 1 13 SHEET 1 AA1 2 THR A 4 GLU A 5 0 SHEET 2 AA1 2 TYR A 10 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 GLU A 181 0 SHEET 2 AA2 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181 SHEET 1 AA3 2 THR B 4 GLU B 5 0 SHEET 2 AA3 2 TYR B 10 VAL B 11 -1 O VAL B 11 N THR B 4 SHEET 1 AA4 2 TYR B 178 PRO B 180 0 SHEET 2 AA4 2 CYS B 187 ILE B 189 -1 O GLY B 188 N ILE B 179 SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.03 SSBOND 2 CYS B 110 CYS B 187 1555 1555 2.03 LINK N MET A 1 C ACE A 401 1555 1555 1.33 LINK ND2 ASN A 2 C1 NAG A 403 1555 1555 1.44 LINK ND2 ASN A 15 C1 NAG C 1 1555 1555 1.45 LINK NZ LYS A 296 C15 RET A 402 1555 1555 1.34 LINK SG CYS A 322 C1 PLM A 410 1555 1555 1.77 LINK N MET B 1 C ACE B 401 1555 1555 1.33 LINK ND2 ASN B 2 C1 NAG B 403 1555 1555 1.44 LINK ND2 ASN B 15 C1 NAG D 1 1555 1555 1.44 LINK NZ LYS B 296 C15 RET B 402 1555 1555 1.34 LINK SG CYS B 322 C1 PLM B 406 1555 1555 1.77 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 CRYST1 61.290 90.810 150.510 90.00 90.00 90.00 P 2 21 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 0.016316 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011012 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006644 0.00000 ATOM 1 N MET A 1 16.064 34.440 5.181 1.00 57.81 N ANISOU 1 N MET A 1 7496 7150 7320 599 1350 1159 N ATOM 2 CA MET A 1 15.725 33.407 6.157 1.00 49.99 C ANISOU 2 CA MET A 1 6508 6167 6317 544 1284 1073 C ATOM 3 C MET A 1 16.448 32.093 5.875 1.00 51.21 C ANISOU 3 C MET A 1 6676 6351 6431 543 1276 1047 C ATOM 4 O MET A 1 16.349 31.541 4.780 1.00 48.65 O ANISOU 4 O MET A 1 6376 6081 6028 594 1285 1059 O ATOM 5 CB MET A 1 14.214 33.172 6.177 1.00 54.98 C ANISOU 5 CB MET A 1 7159 6846 6883 554 1231 1030 C ATOM 6 N ASN A 2 17.168 31.598 6.879 1.00 44.74 N ANISOU 6 N ASN A 2 5840 5495 5663 487 1260 1009 N ATOM 7 CA ASN A 2 17.968 30.388 6.765 1.00 37.19 C ANISOU 7 CA ASN A 2 4893 4556 4682 482 1257 986 C ATOM 8 C ASN A 2 17.202 29.135 7.189 1.00 39.68 C ANISOU 8 C ASN A 2 5231 4906 4941 460 1197 909 C ATOM 9 O ASN A 2 17.803 28.062 7.280 1.00 43.19 O ANISOU 9 O ASN A 2 5683 5357 5370 450 1191 882 O ATOM 10 CB ASN A 2 19.246 30.525 7.599 1.00 29.10 C ANISOU 10 CB ASN A 2 3835 3477 3744 438 1276 992 C ATOM 11 CG ASN A 2 20.161 31.623 7.090 1.00 39.86 C ANISOU 11 CG ASN A 2 5173 4805 5167 458 1343 1067 C ATOM 12 OD1 ASN A 2 20.914 31.424 6.136 1.00 36.51 O ANISOU 12 OD1 ASN A 2 4754 4396 4722 498 1387 1112 O ATOM 13 ND2 ASN A 2 20.110 32.788 7.728 1.00 40.58 N ANISOU 13 ND2 ASN A 2 5237 4846 5337 430 1354 1081 N ATOM 14 N GLY A 3 15.905 29.257 7.457 1.00 24.20 N ANISOU 14 N GLY A 3 3280 2963 2953 454 1157 874 N ATOM 15 CA GLY A 3 15.082 28.114 7.790 1.00 34.09 C ANISOU 15 CA GLY A 3 4551 4246 4154 434 1104 802 C ATOM 16 C GLY A 3 13.842 28.057 6.915 1.00 26.98 C ANISOU 16 C GLY A 3 3672 3404 3174 475 1085 791 C ATOM 17 O GLY A 3 13.668 28.854 5.986 1.00 47.97 O ANISOU 17 O GLY A 3 6333 6085 5808 526 1113 843 O ATOM 18 N THR A 4 12.977 27.105 7.250 1.00 30.54 N ANISOU 18 N THR A 4 4137 3881 3585 454 1038 722 N ATOM 19 CA THR A 4 11.770 26.832 6.485 1.00 42.53 C ANISOU 19 CA THR A 4 5672 5462 5024 486 1011 694 C ATOM 20 C THR A 4 10.552 27.064 7.364 1.00 30.87 C ANISOU 20 C THR A 4 4188 3981 3562 452 966 652 C ATOM 21 O THR A 4 10.380 26.391 8.385 1.00 28.88 O ANISOU 21 O THR A 4 3934 3705 3335 401 936 599 O ATOM 22 CB THR A 4 11.773 25.396 5.954 1.00 37.86 C ANISOU 22 CB THR A 4 5105 4910 4371 492 997 642 C ATOM 23 OG1 THR A 4 12.963 25.179 5.190 1.00 22.66 O ANISOU 23 OG1 THR A 4 3188 2987 2436 524 1042 682 O ATOM 24 CG2 THR A 4 10.569 25.153 5.086 1.00 32.34 C ANISOU 24 CG2 THR A 4 4417 4280 3589 527 970 610 C ATOM 25 N GLU A 5 9.711 28.019 6.969 1.00 38.16 N ANISOU 25 N GLU A 5 5104 4927 4467 483 964 679 N ATOM 26 CA GLU A 5 8.497 28.345 7.701 1.00 23.03 C ANISOU 26 CA GLU A 5 3179 3011 2561 458 925 645 C ATOM 27 C GLU A 5 7.294 27.714 7.018 1.00 32.21 C ANISOU 27 C GLU A 5 4353 4246 3641 482 888 598 C ATOM 28 O GLU A 5 7.071 27.923 5.820 1.00 23.89 O ANISOU 28 O GLU A 5 3305 3247 2524 540 901 624 O ATOM 29 CB GLU A 5 8.291 29.858 7.800 1.00 31.32 C ANISOU 29 CB GLU A 5 4212 4036 3650 476 946 703 C ATOM 30 CG GLU A 5 7.068 30.226 8.631 1.00 27.54 C ANISOU 30 CG GLU A 5 3724 3554 3187 449 908 669 C ATOM 31 CD GLU A 5 6.749 31.712 8.629 1.00 36.52 C ANISOU 31 CD GLU A 5 4847 4671 4358 473 931 726 C ATOM 32 OE1 GLU A 5 7.514 32.489 8.022 1.00 34.79 O ANISOU 32 OE1 GLU A 5 4626 4435 4159 508 980 794 O ATOM 33 OE2 GLU A 5 5.725 32.099 9.238 1.00 31.30 O ANISOU 33 OE2 GLU A 5 4178 4009 3707 458 902 703 O ATOM 34 N GLY A 6 6.526 26.946 7.782 1.00 23.32 N ANISOU 34 N GLY A 6 3226 3120 2514 437 846 528 N ATOM 35 CA GLY A 6 5.259 26.436 7.327 1.00 26.51 C ANISOU 35 CA GLY A 6 3632 3587 2854 449 807 476 C ATOM 36 C GLY A 6 4.114 27.181 7.976 1.00 21.59 C ANISOU 36 C GLY A 6 2991 2962 2249 436 780 468 C ATOM 37 O GLY A 6 4.311 28.183 8.671 1.00 28.89 O ANISOU 37 O GLY A 6 3905 3839 3234 424 794 508 O ATOM 38 N PRO A 7 2.886 26.709 7.753 1.00 35.62 N ANISOU 38 N PRO A 7 4765 4793 3977 438 741 414 N ATOM 39 CA PRO A 7 1.728 27.394 8.352 1.00 24.18 C ANISOU 39 CA PRO A 7 3297 3347 2543 427 714 405 C ATOM 40 C PRO A 7 1.775 27.435 9.868 1.00 25.17 C ANISOU 40 C PRO A 7 3416 3403 2745 365 706 387 C ATOM 41 O PRO A 7 1.358 28.431 10.475 1.00 31.12 O ANISOU 41 O PRO A 7 4156 4132 3536 360 705 412 O ATOM 42 CB PRO A 7 0.532 26.571 7.844 1.00 24.23 C ANISOU 42 CB PRO A 7 3298 3424 2483 433 672 336 C ATOM 43 CG PRO A 7 1.054 25.779 6.688 1.00 21.49 C ANISOU 43 CG PRO A 7 2967 3123 2075 465 682 324 C ATOM 44 CD PRO A 7 2.491 25.507 7.003 1.00 31.13 C ANISOU 44 CD PRO A 7 4205 4282 3340 445 718 352 C ATOM 45 N ASN A 8 2.279 26.374 10.502 1.00 30.76 N ANISOU 45 N ASN A 8 4134 4080 3476 319 701 345 N ATOM 46 CA ASN A 8 2.322 26.293 11.956 1.00 28.66 C ANISOU 46 CA ASN A 8 3862 3755 3274 263 692 324 C ATOM 47 C ASN A 8 3.643 25.713 12.448 1.00 22.63 C ANISOU 47 C ASN A 8 3109 2942 2547 237 714 330 C ATOM 48 O ASN A 8 3.684 25.064 13.499 1.00 19.26 O ANISOU 48 O ASN A 8 2683 2482 2153 192 702 294 O ATOM 49 CB ASN A 8 1.159 25.457 12.492 1.00 19.25 C ANISOU 49 CB ASN A 8 2665 2579 2069 229 654 253 C ATOM 50 CG ASN A 8 1.056 24.100 11.820 1.00 28.36 C ANISOU 50 CG ASN A 8 3832 3770 3176 227 644 200 C ATOM 51 OD1 ASN A 8 1.853 23.766 10.942 1.00 31.84 O ANISOU 51 OD1 ASN A 8 4286 4224 3587 254 665 215 O ATOM 52 ND2 ASN A 8 0.074 23.308 12.234 1.00 34.01 N ANISOU 52 ND2 ASN A 8 4542 4497 3885 195 616 135 N ATOM 53 N PHE A 9 4.725 25.919 11.702 1.00 24.52 N ANISOU 53 N PHE A 9 3355 3179 2781 267 747 376 N ATOM 54 CA PHE A 9 6.025 25.426 12.129 1.00 23.90 C ANISOU 54 CA PHE A 9 3283 3059 2739 246 770 385 C ATOM 55 C PHE A 9 7.121 26.293 11.531 1.00 24.33 C ANISOU 55 C PHE A 9 3334 3098 2810 279 811 455 C ATOM 56 O PHE A 9 6.929 26.968 10.516 1.00 23.15 O ANISOU 56 O PHE A 9 3185 2982 2628 325 826 493 O ATOM 57 CB PHE A 9 6.234 23.954 11.738 1.00 24.57 C ANISOU 57 CB PHE A 9 3388 3163 2787 241 767 340 C ATOM 58 CG PHE A 9 6.154 23.690 10.257 1.00 28.45 C ANISOU 58 CG PHE A 9 3891 3710 3209 289 776 344 C ATOM 59 CD1 PHE A 9 7.278 23.810 9.451 1.00 20.68 C ANISOU 59 CD1 PHE A 9 2915 2728 2214 323 812 390 C ATOM 60 CD2 PHE A 9 4.959 23.297 9.676 1.00 26.86 C ANISOU 60 CD2 PHE A 9 3690 3563 2951 301 747 298 C ATOM 61 CE1 PHE A 9 7.206 23.560 8.091 1.00 36.73 C ANISOU 61 CE1 PHE A 9 4960 4817 4178 372 821 393 C ATOM 62 CE2 PHE A 9 4.882 23.043 8.318 1.00 21.74 C ANISOU 62 CE2 PHE A 9 3052 2974 2234 348 752 295 C ATOM 63 CZ PHE A 9 6.008 23.172 7.525 1.00 25.01 C ANISOU 63 CZ PHE A 9 3478 3391 2635 384 789 344 C ATOM 64 N TYR A 10 8.282 26.263 12.183 1.00 19.19 N ANISOU 64 N TYR A 10 2679 2401 2212 255 831 472 N ATOM 65 CA TYR A 10 9.509 26.843 11.647 1.00 24.36 C ANISOU 65 CA TYR A 10 3329 3038 2889 280 874 532 C ATOM 66 C TYR A 10 10.623 25.827 11.849 1.00 23.57 C ANISOU 66 C TYR A 10 3235 2921 2799 264 886 521 C ATOM 67 O TYR A 10 11.089 25.628 12.976 1.00 26.62 O ANISOU 67 O TYR A 10 3611 3270 3234 224 879 505 O ATOM 68 CB TYR A 10 9.858 28.171 12.321 1.00 23.83 C ANISOU 68 CB TYR A 10 3238 2924 2892 266 890 572 C ATOM 69 CG TYR A 10 11.086 28.813 11.715 1.00 29.89 C ANISOU 69 CG TYR A 10 3997 3672 3688 291 938 635 C ATOM 70 CD1 TYR A 10 10.972 29.714 10.665 1.00 20.17 C ANISOU 70 CD1 TYR A 10 2766 2457 2440 340 969 690 C ATOM 71 CD2 TYR A 10 12.360 28.498 12.174 1.00 26.69 C ANISOU 71 CD2 TYR A 10 3581 3233 3325 269 956 641 C ATOM 72 CE1 TYR A 10 12.089 30.293 10.098 1.00 27.51 C ANISOU 72 CE1 TYR A 10 3688 3367 3399 363 1019 750 C ATOM 73 CE2 TYR A 10 13.482 29.069 11.613 1.00 27.08 C ANISOU 73 CE2 TYR A 10 3620 3265 3405 290 1003 698 C ATOM 74 CZ TYR A 10 13.341 29.968 10.575 1.00 36.42 C ANISOU 74 CZ TYR A 10 4804 4460 4574 336 1036 753 C ATOM 75 OH TYR A 10 14.458 30.541 10.010 1.00 31.77 O ANISOU 75 OH TYR A 10 4203 3850 4018 357 1088 812 O ATOM 76 N VAL A 11 11.048 25.190 10.764 1.00 27.47 N ANISOU 76 N VAL A 11 3745 3446 3245 297 906 529 N ATOM 77 CA VAL A 11 12.131 24.213 10.811 1.00 22.56 C ANISOU 77 CA VAL A 11 3132 2811 2629 290 923 522 C ATOM 78 C VAL A 11 13.460 24.946 10.668 1.00 29.38 C ANISOU 78 C VAL A 11 3980 3646 3538 302 965 585 C ATOM 79 O VAL A 11 13.641 25.714 9.713 1.00 28.05 O ANISOU 79 O VAL A 11 3810 3493 3357 342 994 634 O ATOM 80 CB VAL A 11 11.961 23.141 9.722 1.00 31.88 C ANISOU 80 CB VAL A 11 4339 4037 3738 320 925 496 C ATOM 81 CG1 VAL A 11 13.180 22.240 9.665 1.00 24.29 C ANISOU 81 CG1 VAL A 11 3387 3060 2784 319 951 500 C ATOM 82 CG2 VAL A 11 10.703 22.326 9.979 1.00 27.29 C ANISOU 82 CG2 VAL A 11 3769 3477 3122 298 885 426 C ATOM 83 N PRO A 12 14.407 24.754 11.588 1.00 26.98 N ANISOU 83 N PRO A 12 3660 3303 3287 270 971 585 N ATOM 84 CA PRO A 12 15.729 25.399 11.467 1.00 21.36 C ANISOU 84 CA PRO A 12 2928 2565 2624 279 1011 640 C ATOM 85 C PRO A 12 16.651 24.644 10.513 1.00 34.34 C ANISOU 85 C PRO A 12 4586 4227 4235 311 1044 660 C ATOM 86 O PRO A 12 17.694 24.108 10.898 1.00 23.12 O ANISOU 86 O PRO A 12 3156 2788 2841 299 1058 663 O ATOM 87 CB PRO A 12 16.233 25.381 12.915 1.00 30.61 C ANISOU 87 CB PRO A 12 4076 3698 3858 231 996 620 C ATOM 88 CG PRO A 12 15.613 24.154 13.502 1.00 30.06 C ANISOU 88 CG PRO A 12 4026 3640 3757 210 961 562 C ATOM 89 CD PRO A 12 14.271 23.984 12.837 1.00 21.89 C ANISOU 89 CD PRO A 12 3014 2639 2663 227 941 536 C ATOM 90 N PHE A 13 16.256 24.598 9.240 1.00 20.30 N ANISOU 90 N PHE A 13 2828 2489 2396 357 1058 674 N ATOM 91 CA PHE A 13 16.948 23.788 8.246 1.00 30.15 C ANISOU 91 CA PHE A 13 4095 3762 3600 393 1086 685 C ATOM 92 C PHE A 13 16.478 24.263 6.885 1.00 30.16 C ANISOU 92 C PHE A 13 4110 3807 3543 448 1104 715 C ATOM 93 O PHE A 13 15.270 24.279 6.626 1.00 21.09 O ANISOU 93 O PHE A 13 2973 2692 2348 457 1074 686 O ATOM 94 CB PHE A 13 16.639 22.299 8.449 1.00 30.28 C ANISOU 94 CB PHE A 13 4135 3791 3577 378 1061 621 C ATOM 95 CG PHE A 13 17.535 21.364 7.679 1.00 30.54 C ANISOU 95 CG PHE A 13 4186 3839 3580 406 1092 626 C ATOM 96 CD1 PHE A 13 17.232 20.987 6.378 1.00 33.64 C ANISOU 96 CD1 PHE A 13 4604 4278 3899 452 1103 622 C ATOM 97 CD2 PHE A 13 18.671 20.844 8.271 1.00 30.22 C ANISOU 97 CD2 PHE A 13 4135 3766 3580 389 1110 634 C ATOM 98 CE1 PHE A 13 18.060 20.116 5.682 1.00 32.19 C ANISOU 98 CE1 PHE A 13 4437 4107 3687 479 1133 625 C ATOM 99 CE2 PHE A 13 19.497 19.978 7.584 1.00 28.27 C ANISOU 99 CE2 PHE A 13 3905 3531 3306 417 1140 640 C ATOM 100 CZ PHE A 13 19.194 19.613 6.289 1.00 32.11 C ANISOU 100 CZ PHE A 13 4418 4060 3721 461 1153 635 C ATOM 101 N SER A 14 17.414 24.656 6.025 1.00 22.02 N ANISOU 101 N SER A 14 3076 2779 2511 487 1152 775 N ATOM 102 CA SER A 14 17.050 25.194 4.722 1.00 35.02 C ANISOU 102 CA SER A 14 4734 4469 4101 547 1175 814 C ATOM 103 C SER A 14 16.410 24.125 3.844 1.00 33.28 C ANISOU 103 C SER A 14 4546 4310 3788 578 1156 767 C ATOM 104 O SER A 14 16.830 22.965 3.842 1.00 28.90 O ANISOU 104 O SER A 14 4007 3758 3216 569 1154 730 O ATOM 105 CB SER A 14 18.282 25.764 4.022 1.00 33.60 C ANISOU 105 CB SER A 14 4544 4278 3945 583 1237 890 C ATOM 106 OG SER A 14 17.986 26.112 2.682 1.00 34.07 O ANISOU 106 OG SER A 14 4620 4387 3938 650 1262 929 O ATOM 107 N ASN A 15 15.388 24.524 3.082 1.00 31.94 N ANISOU 107 N ASN A 15 4386 4190 3558 616 1143 768 N ATOM 108 CA ASN A 15 14.731 23.632 2.132 1.00 33.02 C ANISOU 108 CA ASN A 15 4550 4394 3603 650 1124 721 C ATOM 109 C ASN A 15 15.204 23.866 0.699 1.00 36.43 C ANISOU 109 C ASN A 15 4994 4873 3975 724 1168 774 C ATOM 110 O ASN A 15 14.442 23.649 -0.248 1.00 23.85 O ANISOU 110 O ASN A 15 3416 3348 2298 768 1153 753 O ATOM 111 CB ASN A 15 13.209 23.771 2.220 1.00 28.86 C ANISOU 111 CB ASN A 15 4023 3904 3040 645 1075 676 C ATOM 112 CG ASN A 15 12.477 22.585 1.600 1.00 29.40 C ANISOU 112 CG ASN A 15 4113 4031 3027 656 1043 600 C ATOM 113 OD1 ASN A 15 12.993 21.471 1.591 1.00 22.88 O ANISOU 113 OD1 ASN A 15 3302 3198 2193 642 1047 561 O ATOM 114 ND2 ASN A 15 11.277 22.823 1.077 1.00 28.20 N ANISOU 114 ND2 ASN A 15 3960 3938 2816 682 1013 576 N ATOM 115 N LYS A 16 16.453 24.304 0.519 1.00 39.62 N ANISOU 115 N LYS A 16 5388 5244 4420 740 1221 842 N ATOM 116 CA LYS A 16 16.956 24.537 -0.830 1.00 30.25 C ANISOU 116 CA LYS A 16 4214 4101 3179 813 1268 898 C ATOM 117 C LYS A 16 17.028 23.239 -1.625 1.00 33.43 C ANISOU 117 C LYS A 16 4645 4553 3502 839 1263 848 C ATOM 118 O LYS A 16 16.761 23.228 -2.832 1.00 37.85 O ANISOU 118 O LYS A 16 5222 5180 3978 904 1275 859 O ATOM 119 CB LYS A 16 18.320 25.229 -0.778 1.00 42.83 C ANISOU 119 CB LYS A 16 5789 5643 4843 819 1330 979 C ATOM 120 CG LYS A 16 19.334 24.588 0.149 1.00 33.44 C ANISOU 120 CG LYS A 16 4588 4397 3722 764 1334 960 C ATOM 121 CD LYS A 16 20.577 25.463 0.270 1.00 41.36 C ANISOU 121 CD LYS A 16 5564 5349 4803 765 1391 1039 C ATOM 122 CE LYS A 16 21.625 24.830 1.174 1.00 52.04 C ANISOU 122 CE LYS A 16 6901 6653 6220 715 1394 1021 C ATOM 123 NZ LYS A 16 21.110 24.605 2.558 1.00 51.14 N ANISOU 123 NZ LYS A 16 6775 6506 6152 646 1340 962 N ATOM 124 N THR A 17 17.370 22.131 -0.966 1.00 32.12 N ANISOU 124 N THR A 17 4487 4359 3359 792 1246 790 N ATOM 125 CA THR A 17 17.400 20.838 -1.639 1.00 43.30 C ANISOU 125 CA THR A 17 5931 5815 4706 811 1241 733 C ATOM 126 C THR A 17 16.028 20.169 -1.717 1.00 35.52 C ANISOU 126 C THR A 17 4959 4875 3662 799 1184 645 C ATOM 127 O THR A 17 15.894 19.152 -2.406 1.00 30.19 O ANISOU 127 O THR A 17 4307 4241 2922 819 1178 591 O ATOM 128 CB THR A 17 18.392 19.901 -0.940 1.00 41.60 C ANISOU 128 CB THR A 17 5718 5547 4542 770 1254 713 C ATOM 129 OG1 THR A 17 18.030 19.744 0.438 1.00 31.54 O ANISOU 129 OG1 THR A 17 4430 4223 3333 700 1217 674 O ATOM 130 CG2 THR A 17 19.805 20.458 -1.027 1.00 38.21 C ANISOU 130 CG2 THR A 17 5274 5082 4164 788 1312 796 C ATOM 131 N GLY A 18 15.017 20.707 -1.036 1.00 27.67 N ANISOU 131 N GLY A 18 3949 3874 2689 767 1144 627 N ATOM 132 CA GLY A 18 13.667 20.189 -1.122 1.00 24.09 C ANISOU 132 CA GLY A 18 3502 3467 2183 757 1092 547 C ATOM 133 C GLY A 18 13.308 19.090 -0.140 1.00 28.61 C ANISOU 133 C GLY A 18 4079 4003 2789 689 1057 464 C ATOM 134 O GLY A 18 12.207 18.533 -0.242 1.00 23.70 O ANISOU 134 O GLY A 18 3461 3417 2125 677 1016 390 O ATOM 135 N VAL A 19 14.184 18.770 0.819 1.00 26.81 N ANISOU 135 N VAL A 19 3847 3706 2634 646 1073 474 N ATOM 136 CA VAL A 19 13.990 17.592 1.663 1.00 31.04 C ANISOU 136 CA VAL A 19 4391 4206 3196 591 1051 402 C ATOM 137 C VAL A 19 13.247 17.888 2.957 1.00 29.90 C ANISOU 137 C VAL A 19 4228 4024 3108 533 1014 381 C ATOM 138 O VAL A 19 12.974 16.956 3.727 1.00 22.47 O ANISOU 138 O VAL A 19 3293 3054 2192 488 996 323 O ATOM 139 CB VAL A 19 15.344 16.938 2.000 1.00 22.66 C ANISOU 139 CB VAL A 19 3337 3096 2176 580 1089 421 C ATOM 140 CG1 VAL A 19 16.081 16.584 0.725 1.00 23.22 C ANISOU 140 CG1 VAL A 19 3428 3204 2190 638 1127 440 C ATOM 141 CG2 VAL A 19 16.179 17.869 2.865 1.00 30.51 C ANISOU 141 CG2 VAL A 19 4306 4038 3250 562 1108 492 C ATOM 142 N VAL A 20 12.910 19.145 3.227 1.00 35.11 N ANISOU 142 N VAL A 20 4866 4681 3791 536 1006 427 N ATOM 143 CA VAL A 20 12.261 19.508 4.484 1.00 28.67 C ANISOU 143 CA VAL A 20 4033 3829 3031 484 974 411 C ATOM 144 C VAL A 20 10.788 19.122 4.429 1.00 32.39 C ANISOU 144 C VAL A 20 4506 4339 3462 470 928 340 C ATOM 145 O VAL A 20 10.077 19.468 3.477 1.00 28.52 O ANISOU 145 O VAL A 20 4017 3910 2910 510 917 336 O ATOM 146 CB VAL A 20 12.427 21.009 4.768 1.00 26.63 C ANISOU 146 CB VAL A 20 3752 3552 2815 492 985 484 C ATOM 147 CG1 VAL A 20 11.570 21.418 5.959 1.00 29.35 C ANISOU 147 CG1 VAL A 20 4078 3868 3205 444 949 461 C ATOM 148 CG2 VAL A 20 13.886 21.335 5.025 1.00 21.75 C ANISOU 148 CG2 VAL A 20 3125 2888 2252 492 1028 545 C ATOM 149 N AARG A 21 10.325 18.403 5.451 0.78 33.12 N ANISOU 149 N AARG A 21 4598 4398 3589 416 904 285 N ATOM 150 N BARG A 21 10.329 18.404 5.453 0.22 33.00 N ANISOU 150 N BARG A 21 4582 4381 3573 416 904 285 N ATOM 151 CA AARG A 21 8.925 18.027 5.571 0.78 30.81 C ANISOU 151 CA AARG A 21 4303 4133 3272 394 862 216 C ATOM 152 CA BARG A 21 8.938 17.999 5.588 0.22 30.78 C ANISOU 152 CA BARG A 21 4299 4128 3269 393 862 215 C ATOM 153 C AARG A 21 8.401 18.442 6.937 0.78 24.12 C ANISOU 153 C AARG A 21 3436 3241 2486 345 838 213 C ATOM 154 C BARG A 21 8.405 18.463 6.937 0.22 24.30 C ANISOU 154 C BARG A 21 3459 3264 2508 346 839 214 C ATOM 155 O AARG A 21 9.160 18.566 7.902 0.78 30.30 O ANISOU 155 O AARG A 21 4215 3968 3329 319 853 242 O ATOM 156 O BARG A 21 9.163 18.641 7.895 0.22 30.21 O ANISOU 156 O BARG A 21 4203 3958 3319 320 853 246 O ATOM 157 CB AARG A 21 8.712 16.522 5.352 0.78 30.95 C ANISOU 157 CB AARG A 21 4339 4156 3264 377 857 136 C ATOM 158 CB BARG A 21 8.778 16.476 5.450 0.22 30.91 C ANISOU 158 CB BARG A 21 4335 4145 3266 373 858 137 C ATOM 159 CG AARG A 21 8.836 16.104 3.897 0.78 29.92 C ANISOU 159 CG AARG A 21 4226 4086 3058 427 868 118 C ATOM 160 CG BARG A 21 9.210 15.939 4.095 0.22 31.98 C ANISOU 160 CG BARG A 21 4490 4326 3334 420 879 126 C ATOM 161 CD AARG A 21 8.033 14.846 3.597 0.78 35.90 C ANISOU 161 CD AARG A 21 4993 4866 3781 407 848 20 C ATOM 162 CD BARG A 21 9.235 14.413 4.063 0.22 34.23 C ANISOU 162 CD BARG A 21 4796 4597 3613 397 884 50 C ATOM 163 NE AARG A 21 8.737 13.631 3.988 0.78 33.20 N ANISOU 163 NE AARG A 21 4672 4473 3471 380 873 -10 N ATOM 164 NE BARG A 21 7.919 13.824 3.842 0.22 37.79 N ANISOU 164 NE BARG A 21 5244 5085 4032 378 848 -36 N ATOM 165 CZ AARG A 21 8.210 12.414 3.953 0.78 38.53 C ANISOU 165 CZ AARG A 21 5357 5144 4137 353 865 -94 C ATOM 166 CZ BARG A 21 7.677 12.519 3.830 0.22 39.56 C ANISOU 166 CZ BARG A 21 5481 5296 4254 351 849 -113 C ATOM 167 NH1AARG A 21 6.962 12.211 3.562 0.78 42.33 N ANISOU 167 NH1AARG A 21 5829 5673 4581 345 830 -164 N ATOM 168 NH1BARG A 21 8.641 11.636 4.036 0.22 36.58 N ANISOU 168 NH1BARG A 21 5125 4870 3903 343 885 -114 N ATOM 169 NH2AARG A 21 8.952 11.375 4.327 0.78 36.21 N ANISOU 169 NH2AARG A 21 5084 4799 3877 333 896 -110 N ATOM 170 NH2BARG A 21 6.438 12.090 3.611 0.22 38.09 N ANISOU 170 NH2BARG A 21 5286 5145 4041 333 815 -193 N ATOM 171 N SER A 22 7.091 18.661 6.999 1.00 27.66 N ANISOU 171 N SER A 22 3873 3720 2915 336 802 176 N ATOM 172 CA SER A 22 6.479 19.236 8.190 1.00 28.48 C ANISOU 172 CA SER A 22 3958 3791 3070 297 780 178 C ATOM 173 C SER A 22 6.670 18.327 9.403 1.00 26.40 C ANISOU 173 C SER A 22 3700 3471 2860 244 779 143 C ATOM 174 O SER A 22 6.571 17.099 9.286 1.00 31.24 O ANISOU 174 O SER A 22 4328 4082 3459 228 781 88 O ATOM 175 CB SER A 22 4.991 19.481 7.952 1.00 20.56 C ANISOU 175 CB SER A 22 2942 2837 2033 299 741 138 C ATOM 176 OG SER A 22 4.365 19.938 9.138 1.00 24.75 O ANISOU 176 OG SER A 22 3456 3335 2613 260 721 135 O ATOM 177 N PRO A 23 6.946 18.895 10.582 1.00 31.06 N ANISOU 177 N PRO A 23 4278 4014 3510 216 780 174 N ATOM 178 CA PRO A 23 7.064 18.068 11.793 1.00 32.88 C ANISOU 178 CA PRO A 23 4512 4195 3786 170 779 145 C ATOM 179 C PRO A 23 5.748 17.467 12.253 1.00 31.53 C ANISOU 179 C PRO A 23 4339 4030 3613 137 750 79 C ATOM 180 O PRO A 23 5.755 16.650 13.182 1.00 18.87 O ANISOU 180 O PRO A 23 2740 2387 2042 102 753 52 O ATOM 181 CB PRO A 23 7.620 19.050 12.834 1.00 29.18 C ANISOU 181 CB PRO A 23 4027 3687 3375 157 782 196 C ATOM 182 CG PRO A 23 7.154 20.386 12.365 1.00 22.26 C ANISOU 182 CG PRO A 23 3135 2837 2486 182 773 230 C ATOM 183 CD PRO A 23 7.183 20.322 10.858 1.00 31.45 C ANISOU 183 CD PRO A 23 4309 4051 3588 228 783 236 C ATOM 184 N PHE A 24 4.624 17.850 11.650 1.00 21.52 N ANISOU 184 N PHE A 24 3060 2809 2307 149 724 56 N ATOM 185 CA PHE A 24 3.332 17.248 11.941 1.00 22.73 C ANISOU 185 CA PHE A 24 3207 2975 2456 118 697 -11 C ATOM 186 C PHE A 24 2.951 16.161 10.946 1.00 27.46 C ANISOU 186 C PHE A 24 3816 3609 3007 124 695 -74 C ATOM 187 O PHE A 24 1.849 15.612 11.040 1.00 35.06 O ANISOU 187 O PHE A 24 4770 4586 3964 99 673 -137 O ATOM 188 CB PHE A 24 2.245 18.329 11.969 1.00 24.44 C ANISOU 188 CB PHE A 24 3400 3223 2663 125 666 -4 C ATOM 189 CG PHE A 24 2.482 19.399 12.998 1.00 31.05 C ANISOU 189 CG PHE A 24 4225 4023 3549 116 667 48 C ATOM 190 CD1 PHE A 24 2.765 19.063 14.312 1.00 25.08 C ANISOU 190 CD1 PHE A 24 3470 3212 2846 77 673 45 C ATOM 191 CD2 PHE A 24 2.437 20.739 12.649 1.00 34.00 C ANISOU 191 CD2 PHE A 24 4587 4417 3916 147 664 100 C ATOM 192 CE1 PHE A 24 2.988 20.043 15.262 1.00 24.19 C ANISOU 192 CE1 PHE A 24 3346 3069 2777 68 671 86 C ATOM 193 CE2 PHE A 24 2.660 21.725 13.595 1.00 28.85 C ANISOU 193 CE2 PHE A 24 3923 3726 3313 136 667 141 C ATOM 194 CZ PHE A 24 2.937 21.375 14.903 1.00 22.29 C ANISOU 194 CZ PHE A 24 3092 2844 2533 95 668 132 C ATOM 195 N GLU A 25 3.830 15.836 10.000 1.00 35.05 N ANISOU 195 N GLU A 25 4796 4585 3936 157 718 -62 N ATOM 196 CA GLU A 25 3.505 14.897 8.934 1.00 33.23 C ANISOU 196 CA GLU A 25 4575 4396 3654 168 716 -124 C ATOM 197 C GLU A 25 4.439 13.701 8.855 1.00 32.38 C ANISOU 197 C GLU A 25 4493 4252 3556 161 750 -142 C ATOM 198 O GLU A 25 3.971 12.576 8.667 1.00 25.70 O ANISOU 198 O GLU A 25 3655 3405 2703 140 750 -214 O ATOM 199 CB GLU A 25 3.505 15.622 7.580 1.00 27.85 C ANISOU 199 CB GLU A 25 3891 3784 2905 226 710 -100 C ATOM 200 CG GLU A 25 2.450 16.707 7.457 1.00 30.85 C ANISOU 200 CG GLU A 25 4245 4211 3265 240 676 -89 C ATOM 201 CD GLU A 25 2.462 17.383 6.095 1.00 47.52 C ANISOU 201 CD GLU A 25 6354 6395 5305 304 674 -61 C ATOM 202 OE1 GLU A 25 3.295 16.994 5.246 1.00 50.35 O ANISOU 202 OE1 GLU A 25 6732 6768 5629 336 699 -52 O ATOM 203 OE2 GLU A 25 1.637 18.298 5.876 1.00 52.00 O ANISOU 203 OE2 GLU A 25 6902 7006 5849 326 650 -45 O ATOM 204 N ALA A 26 5.746 13.901 8.993 1.00 26.19 N ANISOU 204 N ALA A 26 3722 3437 2792 178 781 -81 N ATOM 205 CA ALA A 26 6.693 12.838 8.693 1.00 27.74 C ANISOU 205 CA ALA A 26 3944 3610 2988 184 816 -93 C ATOM 206 C ALA A 26 7.867 12.910 9.653 1.00 27.28 C ANISOU 206 C ALA A 26 3889 3492 2984 175 844 -35 C ATOM 207 O ALA A 26 8.144 13.981 10.208 1.00 28.74 O ANISOU 207 O ALA A 26 4057 3666 3195 177 838 22 O ATOM 208 CB ALA A 26 7.188 12.942 7.243 1.00 31.46 C ANISOU 208 CB ALA A 26 4426 4132 3396 236 828 -82 C ATOM 209 N PRO A 27 8.578 11.799 9.866 1.00 31.63 N ANISOU 209 N PRO A 27 4459 4004 3553 167 875 -49 N ATOM 210 CA PRO A 27 9.773 11.841 10.716 1.00 28.68 C ANISOU 210 CA PRO A 27 4088 3583 3227 165 901 7 C ATOM 211 C PRO A 27 10.788 12.837 10.182 1.00 31.60 C ANISOU 211 C PRO A 27 4450 3970 3586 204 914 78 C ATOM 212 O PRO A 27 10.883 13.079 8.977 1.00 27.68 O ANISOU 212 O PRO A 27 3960 3517 3041 240 919 83 O ATOM 213 CB PRO A 27 10.309 10.407 10.652 1.00 31.15 C ANISOU 213 CB PRO A 27 4426 3864 3545 161 935 -25 C ATOM 214 CG PRO A 27 9.121 9.578 10.325 1.00 37.27 C ANISOU 214 CG PRO A 27 5209 4651 4302 139 922 -108 C ATOM 215 CD PRO A 27 8.257 10.427 9.436 1.00 30.12 C ANISOU 215 CD PRO A 27 4289 3809 3348 155 887 -122 C ATOM 216 N GLN A 28 11.546 13.427 11.102 1.00 33.03 N ANISOU 216 N GLN A 28 4617 4120 3813 196 921 132 N ATOM 217 CA GLN A 28 12.468 14.517 10.793 1.00 32.21 C ANISOU 217 CA GLN A 28 4499 4025 3715 224 934 201 C ATOM 218 C GLN A 28 13.897 14.020 10.608 1.00 34.36 C ANISOU 218 C GLN A 28 4780 4279 3997 245 974 235 C ATOM 219 O GLN A 28 14.853 14.660 11.054 1.00 29.02 O ANISOU 219 O GLN A 28 4085 3584 3356 250 986 289 O ATOM 220 CB GLN A 28 12.397 15.583 11.882 1.00 26.02 C ANISOU 220 CB GLN A 28 3688 3220 2979 202 915 235 C ATOM 221 CG GLN A 28 11.016 16.203 12.043 1.00 25.95 C ANISOU 221 CG GLN A 28 3668 3230 2960 186 878 209 C ATOM 222 CD GLN A 28 10.624 17.082 10.866 1.00 33.69 C ANISOU 222 CD GLN A 28 4645 4258 3897 221 872 227 C ATOM 223 OE1 GLN A 28 11.138 18.190 10.706 1.00 30.52 O ANISOU 223 OE1 GLN A 28 4230 3859 3509 240 882 284 O ATOM 224 NE2 GLN A 28 9.710 16.590 10.036 1.00 28.26 N ANISOU 224 NE2 GLN A 28 3969 3611 3158 231 858 179 N ATOM 225 N TYR A 29 14.061 12.861 9.967 1.00 29.25 N ANISOU 225 N TYR A 29 4158 3635 3321 258 994 200 N ATOM 226 CA TYR A 29 15.375 12.256 9.779 1.00 30.59 C ANISOU 226 CA TYR A 29 4338 3786 3498 280 1034 228 C ATOM 227 C TYR A 29 16.265 13.031 8.816 1.00 34.60 C ANISOU 227 C TYR A 29 4840 4321 3986 322 1057 284 C ATOM 228 O TYR A 29 17.464 12.742 8.746 1.00 28.82 O ANISOU 228 O TYR A 29 4109 3574 3268 340 1091 319 O ATOM 229 CB TYR A 29 15.217 10.817 9.286 1.00 37.83 C ANISOU 229 CB TYR A 29 5287 4699 4389 283 1053 170 C ATOM 230 CG TYR A 29 14.467 9.922 10.245 1.00 29.89 C ANISOU 230 CG TYR A 29 4288 3658 3411 242 1042 118 C ATOM 231 CD1 TYR A 29 14.477 10.175 11.612 1.00 28.34 C ANISOU 231 CD1 TYR A 29 4075 3429 3265 213 1031 139 C ATOM 232 CD2 TYR A 29 13.749 8.822 9.786 1.00 22.76 C ANISOU 232 CD2 TYR A 29 3409 2755 2484 232 1046 47 C ATOM 233 CE1 TYR A 29 13.795 9.360 12.497 1.00 27.44 C ANISOU 233 CE1 TYR A 29 3968 3283 3176 179 1026 96 C ATOM 234 CE2 TYR A 29 13.062 8.000 10.665 1.00 34.56 C ANISOU 234 CE2 TYR A 29 4909 4212 4010 194 1043 2 C ATOM 235 CZ TYR A 29 13.091 8.275 12.019 1.00 31.43 C ANISOU 235 CZ TYR A 29 4497 3784 3662 170 1035 30 C ATOM 236 OH TYR A 29 12.411 7.465 12.898 1.00 37.09 O ANISOU 236 OH TYR A 29 5219 4463 4409 136 1036 -9 O ATOM 237 N TYR A 30 15.720 13.996 8.071 1.00 30.85 N ANISOU 237 N TYR A 30 4358 3885 3480 341 1042 298 N ATOM 238 CA TYR A 30 16.553 14.812 7.194 1.00 37.28 C ANISOU 238 CA TYR A 30 5164 4721 4279 383 1068 359 C ATOM 239 C TYR A 30 17.427 15.789 7.969 1.00 36.05 C ANISOU 239 C TYR A 30 4978 4535 4184 374 1078 424 C ATOM 240 O TYR A 30 18.397 16.311 7.409 1.00 39.82 O ANISOU 240 O TYR A 30 5446 5017 4666 404 1110 479 O ATOM 241 CB TYR A 30 15.683 15.586 6.201 1.00 32.68 C ANISOU 241 CB TYR A 30 4582 4190 3645 411 1052 359 C ATOM 242 CG TYR A 30 14.768 16.582 6.869 1.00 35.06 C ANISOU 242 CG TYR A 30 4862 4490 3970 386 1017 363 C ATOM 243 CD1 TYR A 30 15.186 17.883 7.117 1.00 35.49 C ANISOU 243 CD1 TYR A 30 4891 4532 4061 391 1024 427 C ATOM 244 CD2 TYR A 30 13.492 16.216 7.274 1.00 35.27 C ANISOU 244 CD2 TYR A 30 4891 4523 3986 355 978 301 C ATOM 245 CE1 TYR A 30 14.358 18.791 7.741 1.00 29.71 C ANISOU 245 CE1 TYR A 30 4141 3795 3353 369 995 429 C ATOM 246 CE2 TYR A 30 12.656 17.119 7.898 1.00 26.31 C ANISOU 246 CE2 TYR A 30 3737 3387 2873 334 948 305 C ATOM 247 CZ TYR A 30 13.093 18.404 8.125 1.00 21.48 C ANISOU 247 CZ TYR A 30 3103 2763 2295 342 956 369 C ATOM 248 OH TYR A 30 12.261 19.304 8.745 1.00 31.49 O ANISOU 248 OH TYR A 30 4353 4026 3586 322 928 372 O ATOM 249 N LEU A 31 17.098 16.067 9.232 1.00 38.10 N ANISOU 249 N LEU A 31 5220 4765 4492 332 1052 416 N ATOM 250 CA LEU A 31 17.853 17.022 10.028 1.00 33.30 C ANISOU 250 CA LEU A 31 4580 4131 3944 319 1057 467 C ATOM 251 C LEU A 31 18.625 16.386 11.174 1.00 29.78 C ANISOU 251 C LEU A 31 4123 3648 3542 295 1062 465 C ATOM 252 O LEU A 31 19.479 17.055 11.763 1.00 28.12 O ANISOU 252 O LEU A 31 3883 3420 3380 287 1070 506 O ATOM 253 CB LEU A 31 16.926 18.122 10.579 1.00 36.40 C ANISOU 253 CB LEU A 31 4952 4522 4355 296 1024 467 C ATOM 254 CG LEU A 31 15.605 17.814 11.299 1.00 30.69 C ANISOU 254 CG LEU A 31 4237 3797 3628 262 983 411 C ATOM 255 CD1 LEU A 31 15.817 17.244 12.698 1.00 27.33 C ANISOU 255 CD1 LEU A 31 3804 3336 3246 225 973 392 C ATOM 256 CD2 LEU A 31 14.747 19.070 11.374 1.00 30.43 C ANISOU 256 CD2 LEU A 31 4187 3774 3601 257 959 422 C ATOM 257 N ALA A 32 18.347 15.129 11.513 1.00 29.38 N ANISOU 257 N ALA A 32 4095 3588 3480 283 1058 420 N ATOM 258 CA ALA A 32 19.125 14.426 12.523 1.00 21.04 C ANISOU 258 CA ALA A 32 3033 2502 2461 270 1069 423 C ATOM 259 C ALA A 32 19.035 12.929 12.269 1.00 28.97 C ANISOU 259 C ALA A 32 4071 3499 3438 277 1086 383 C ATOM 260 O ALA A 32 18.022 12.427 11.774 1.00 33.72 O ANISOU 260 O ALA A 32 4696 4111 4004 273 1076 334 O ATOM 261 CB ALA A 32 18.649 14.756 13.943 1.00 36.22 C ANISOU 261 CB ALA A 32 4936 4404 4423 231 1037 411 C ATOM 262 N AGLU A 33 20.107 12.222 12.610 0.50 27.75 N ANISOU 262 N AGLU A 33 3916 3326 3303 288 1115 402 N ATOM 263 N BGLU A 33 20.110 12.224 12.614 0.50 27.74 N ANISOU 263 N BGLU A 33 3915 3325 3302 288 1115 402 N ATOM 264 CA AGLU A 33 20.125 10.782 12.435 0.50 29.12 C ANISOU 264 CA AGLU A 33 4122 3485 3459 296 1138 368 C ATOM 265 CA BGLU A 33 20.140 10.780 12.459 0.50 29.13 C ANISOU 265 CA BGLU A 33 4122 3484 3460 296 1138 369 C ATOM 266 C AGLU A 33 19.185 10.117 13.441 0.50 26.76 C ANISOU 266 C AGLU A 33 3833 3161 3174 263 1119 323 C ATOM 267 C BGLU A 33 19.175 10.121 13.444 0.50 26.76 C ANISOU 267 C BGLU A 33 3833 3161 3173 263 1119 323 C ATOM 268 O AGLU A 33 18.935 10.661 14.520 0.50 27.52 O ANISOU 268 O AGLU A 33 3907 3249 3301 238 1093 331 O ATOM 269 O BGLU A 33 18.894 10.675 14.511 0.50 27.54 O ANISOU 269 O BGLU A 33 3910 3252 3303 238 1092 330 O ATOM 270 CB AGLU A 33 21.543 10.242 12.602 0.50 30.50 C ANISOU 270 CB AGLU A 33 4292 3645 3653 320 1176 406 C ATOM 271 CB BGLU A 33 21.555 10.251 12.682 0.50 30.54 C ANISOU 271 CB BGLU A 33 4295 3649 3660 319 1175 407 C ATOM 272 CG AGLU A 33 22.562 10.903 11.689 0.50 27.74 C ANISOU 272 CG AGLU A 33 3927 3317 3296 353 1200 456 C ATOM 273 CG BGLU A 33 22.585 10.794 11.702 0.50 27.72 C ANISOU 273 CG BGLU A 33 3926 3312 3293 354 1201 454 C ATOM 274 CD AGLU A 33 23.894 10.184 11.685 0.50 28.16 C ANISOU 274 CD AGLU A 33 3980 3360 3362 381 1240 487 C ATOM 275 CD BGLU A 33 22.377 10.288 10.286 0.50 34.54 C ANISOU 275 CD BGLU A 33 4824 4196 4104 383 1223 432 C ATOM 276 OE1AGLU A 33 23.905 8.950 11.879 0.50 31.48 O ANISOU 276 OE1AGLU A 33 4426 3760 3777 386 1259 461 O ATOM 277 OE1BGLU A 33 21.728 9.234 10.112 0.50 40.96 O ANISOU 277 OE1BGLU A 33 5670 5000 4894 378 1227 379 O ATOM 278 OE2AGLU A 33 24.931 10.854 11.493 0.50 30.13 O ANISOU 278 OE2AGLU A 33 4201 3619 3630 398 1256 539 O ATOM 279 OE2BGLU A 33 22.865 10.949 9.344 0.50 39.89 O ANISOU 279 OE2BGLU A 33 5495 4898 4764 411 1239 467 O ATOM 280 N PRO A 34 18.647 8.940 13.107 1.00 33.86 N ANISOU 280 N PRO A 34 4765 4047 4052 262 1133 274 N ATOM 281 CA PRO A 34 17.699 8.281 14.024 1.00 25.39 C ANISOU 281 CA PRO A 34 3702 2948 2997 229 1121 231 C ATOM 282 C PRO A 34 18.253 8.010 15.413 1.00 19.36 C ANISOU 282 C PRO A 34 2925 2156 2275 222 1127 259 C ATOM 283 O PRO A 34 17.484 8.034 16.383 1.00 24.03 O ANISOU 283 O PRO A 34 3510 2734 2885 194 1106 241 O ATOM 284 CB PRO A 34 17.360 6.976 13.290 1.00 29.23 C ANISOU 284 CB PRO A 34 4225 3421 3460 235 1148 178 C ATOM 285 CG PRO A 34 17.583 7.289 11.852 1.00 20.28 C ANISOU 285 CG PRO A 34 3099 2324 2281 263 1154 178 C ATOM 286 CD PRO A 34 18.759 8.226 11.823 1.00 31.34 C ANISOU 286 CD PRO A 34 4475 3740 3692 288 1161 249 C ATOM 287 N TRP A 35 19.556 7.747 15.550 1.00 22.82 N ANISOU 287 N TRP A 35 3357 2588 2726 249 1156 302 N ATOM 288 CA TRP A 35 20.111 7.491 16.875 1.00 20.77 C ANISOU 288 CA TRP A 35 3081 2309 2500 248 1161 329 C ATOM 289 C TRP A 35 20.067 8.725 17.771 1.00 29.31 C ANISOU 289 C TRP A 35 4125 3408 3605 229 1122 354 C ATOM 290 O TRP A 35 20.164 8.585 18.995 1.00 21.49 O ANISOU 290 O TRP A 35 3121 2407 2638 222 1115 364 O ATOM 291 CB TRP A 35 21.546 6.963 16.767 1.00 27.42 C ANISOU 291 CB TRP A 35 3921 3148 3350 284 1200 371 C ATOM 292 CG TRP A 35 22.541 7.937 16.206 1.00 26.14 C ANISOU 292 CG TRP A 35 3730 3014 3188 303 1199 415 C ATOM 293 CD1 TRP A 35 22.969 8.017 14.913 1.00 29.20 C ANISOU 293 CD1 TRP A 35 4128 3416 3550 326 1220 424 C ATOM 294 CD2 TRP A 35 23.245 8.958 16.925 1.00 25.69 C ANISOU 294 CD2 TRP A 35 3628 2974 3160 299 1179 457 C ATOM 295 NE1 TRP A 35 23.888 9.029 14.780 1.00 26.93 N ANISOU 295 NE1 TRP A 35 3805 3150 3278 338 1218 472 N ATOM 296 CE2 TRP A 35 24.076 9.622 16.001 1.00 27.52 C ANISOU 296 CE2 TRP A 35 3845 3226 3388 319 1192 491 C ATOM 297 CE3 TRP A 35 23.249 9.380 18.259 1.00 36.64 C ANISOU 297 CE3 TRP A 35 4985 4360 4574 282 1152 467 C ATOM 298 CZ2 TRP A 35 24.899 10.683 16.367 1.00 37.38 C ANISOU 298 CZ2 TRP A 35 5047 4490 4666 318 1181 531 C ATOM 299 CZ3 TRP A 35 24.068 10.433 18.619 1.00 37.47 C ANISOU 299 CZ3 TRP A 35 5045 4485 4705 281 1137 503 C ATOM 300 CH2 TRP A 35 24.880 11.073 17.677 1.00 22.97 C ANISOU 300 CH2 TRP A 35 3192 2664 2870 297 1152 534 C ATOM 301 N GLN A 36 19.927 9.923 17.196 1.00 22.51 N ANISOU 301 N GLN A 36 3246 2571 2737 223 1098 363 N ATOM 302 CA GLN A 36 19.790 11.131 18.008 1.00 19.08 C ANISOU 302 CA GLN A 36 2776 2147 2327 202 1062 379 C ATOM 303 C GLN A 36 18.372 11.296 18.540 1.00 32.12 C ANISOU 303 C GLN A 36 4434 3793 3977 170 1030 340 C ATOM 304 O GLN A 36 18.182 11.744 19.678 1.00 29.32 O ANISOU 304 O GLN A 36 4059 3436 3645 153 1007 343 O ATOM 305 CB GLN A 36 20.185 12.362 17.198 1.00 22.58 C ANISOU 305 CB GLN A 36 3197 2612 2769 210 1056 408 C ATOM 306 CG GLN A 36 21.589 12.330 16.642 1.00 22.47 C ANISOU 306 CG GLN A 36 3172 2606 2761 241 1089 451 C ATOM 307 CD GLN A 36 21.849 13.488 15.712 1.00 30.61 C ANISOU 307 CD GLN A 36 4186 3655 3789 250 1090 479 C ATOM 308 OE1 GLN A 36 22.157 13.297 14.536 1.00 31.67 O ANISOU 308 OE1 GLN A 36 4336 3799 3896 276 1116 489 O ATOM 309 NE2 GLN A 36 21.721 14.703 16.232 1.00 29.71 N ANISOU 309 NE2 GLN A 36 4041 3544 3705 229 1064 492 N ATOM 310 N PHE A 37 17.364 10.965 17.727 1.00 31.44 N ANISOU 310 N PHE A 37 4374 3708 3862 164 1028 300 N ATOM 311 CA PHE A 37 15.994 10.953 18.228 1.00 18.28 C ANISOU 311 CA PHE A 37 2714 2036 2195 134 1002 258 C ATOM 312 C PHE A 37 15.819 9.887 19.300 1.00 18.23 C ANISOU 312 C PHE A 37 2720 2000 2208 124 1015 243 C ATOM 313 O PHE A 37 15.030 10.069 20.233 1.00 25.28 O ANISOU 313 O PHE A 37 3605 2886 3114 101 994 229 O ATOM 314 CB PHE A 37 15.004 10.719 17.084 1.00 19.15 C ANISOU 314 CB PHE A 37 2847 2159 2270 130 998 214 C ATOM 315 CG PHE A 37 14.884 11.880 16.135 1.00 22.71 C ANISOU 315 CG PHE A 37 3285 2643 2700 140 981 229 C ATOM 316 CD1 PHE A 37 14.005 12.917 16.397 1.00 22.22 C ANISOU 316 CD1 PHE A 37 3206 2595 2641 122 946 224 C ATOM 317 CD2 PHE A 37 15.644 11.928 14.976 1.00 29.62 C ANISOU 317 CD2 PHE A 37 4168 3536 3551 172 1003 250 C ATOM 318 CE1 PHE A 37 13.887 13.982 15.524 1.00 20.60 C ANISOU 318 CE1 PHE A 37 2991 2419 2418 136 934 242 C ATOM 319 CE2 PHE A 37 15.530 12.993 14.097 1.00 18.88 C ANISOU 319 CE2 PHE A 37 2797 2207 2170 186 992 269 C ATOM 320 CZ PHE A 37 14.650 14.020 14.373 1.00 22.67 C ANISOU 320 CZ PHE A 37 3259 2698 2655 169 959 266 C ATOM 321 N ASER A 38 16.547 8.773 19.189 0.77 18.46 N ANISOU 321 N ASER A 38 2768 2010 2237 145 1054 250 N ATOM 322 N BSER A 38 16.539 8.770 19.178 0.23 18.46 N ANISOU 322 N BSER A 38 2768 2011 2237 145 1054 249 N ATOM 323 CA ASER A 38 16.449 7.723 20.196 0.77 24.46 C ANISOU 323 CA ASER A 38 3539 2738 3014 142 1074 243 C ATOM 324 CA BSER A 38 16.462 7.721 20.187 0.23 24.44 C ANISOU 324 CA BSER A 38 3538 2737 3012 142 1075 243 C ATOM 325 C ASER A 38 17.016 8.176 21.537 0.77 22.78 C ANISOU 325 C ASER A 38 3298 2531 2825 145 1061 281 C ATOM 326 C BSER A 38 17.004 8.191 21.531 0.23 22.78 C ANISOU 326 C BSER A 38 3299 2531 2826 145 1061 281 C ATOM 327 O ASER A 38 16.491 7.810 22.594 0.77 22.27 O ANISOU 327 O ASER A 38 3236 2451 2775 134 1059 273 O ATOM 328 O BSER A 38 16.453 7.852 22.584 0.23 22.59 O ANISOU 328 O BSER A 38 3276 2492 2815 133 1058 272 O ATOM 329 CB ASER A 38 17.160 6.460 19.712 0.77 24.43 C ANISOU 329 CB ASER A 38 3562 2712 3007 168 1123 244 C ATOM 330 CB BSER A 38 17.220 6.485 19.707 0.23 24.52 C ANISOU 330 CB BSER A 38 3573 2725 3018 169 1124 247 C ATOM 331 OG ASER A 38 17.053 5.411 20.660 0.77 24.00 O ANISOU 331 OG ASER A 38 3522 2624 2972 169 1150 242 O ATOM 332 OG BSER A 38 16.701 6.010 18.478 0.23 23.22 O ANISOU 332 OG BSER A 38 3435 2558 2830 167 1136 204 O ATOM 333 N MET A 39 18.097 8.958 21.518 1.00 18.39 N ANISOU 333 N MET A 39 2715 1997 2275 162 1054 322 N ATOM 334 CA MET A 39 18.654 9.472 22.767 1.00 25.50 C ANISOU 334 CA MET A 39 3583 2910 3196 164 1036 351 C ATOM 335 C MET A 39 17.664 10.389 23.475 1.00 26.10 C ANISOU 335 C MET A 39 3643 2993 3280 133 995 332 C ATOM 336 O MET A 39 17.561 10.372 24.707 1.00 20.96 O ANISOU 336 O MET A 39 2980 2343 2640 130 984 337 O ATOM 337 CB MET A 39 19.963 10.210 22.499 1.00 23.73 C ANISOU 337 CB MET A 39 3326 2709 2981 182 1036 391 C ATOM 338 CG MET A 39 21.152 9.304 22.228 1.00 27.94 C ANISOU 338 CG MET A 39 3866 3239 3513 217 1076 419 C ATOM 339 SD MET A 39 22.659 10.235 21.885 1.00 45.21 S ANISOU 339 SD MET A 39 6009 5454 5714 236 1075 465 S ATOM 340 CE MET A 39 22.782 11.253 23.355 1.00 43.83 C ANISOU 340 CE MET A 39 5786 5300 5566 218 1032 473 C ATOM 341 N LEU A 40 16.950 11.219 22.712 1.00 20.12 N ANISOU 341 N LEU A 40 2885 2245 2514 114 973 314 N ATOM 342 CA LEU A 40 15.916 12.060 23.304 1.00 21.58 C ANISOU 342 CA LEU A 40 3059 2436 2706 87 936 294 C ATOM 343 C LEU A 40 14.839 11.217 23.972 1.00 20.69 C ANISOU 343 C LEU A 40 2966 2302 2591 72 940 263 C ATOM 344 O LEU A 40 14.373 11.548 25.069 1.00 24.25 O ANISOU 344 O LEU A 40 3406 2755 3054 59 919 259 O ATOM 345 CB LEU A 40 15.302 12.969 22.240 1.00 25.16 C ANISOU 345 CB LEU A 40 3510 2902 3147 76 919 282 C ATOM 346 CG LEU A 40 16.204 14.055 21.656 1.00 21.21 C ANISOU 346 CG LEU A 40 2985 2419 2654 87 915 316 C ATOM 347 CD1 LEU A 40 15.465 14.850 20.584 1.00 17.49 C ANISOU 347 CD1 LEU A 40 2518 1961 2166 82 902 306 C ATOM 348 CD2 LEU A 40 16.700 14.966 22.761 1.00 22.64 C ANISOU 348 CD2 LEU A 40 3130 2606 2866 78 894 336 C ATOM 349 N ALA A 41 14.427 10.124 23.326 1.00 17.59 N ANISOU 349 N ALA A 41 2606 1890 2187 73 967 238 N ATOM 350 CA ALA A 41 13.390 9.269 23.899 1.00 20.95 C ANISOU 350 CA ALA A 41 3051 2292 2618 57 976 206 C ATOM 351 C ALA A 41 13.883 8.555 25.153 1.00 22.47 C ANISOU 351 C ALA A 41 3244 2469 2826 72 998 230 C ATOM 352 O ALA A 41 13.135 8.412 26.128 1.00 18.45 O ANISOU 352 O ALA A 41 2734 1949 2326 60 992 220 O ATOM 353 CB ALA A 41 12.909 8.263 22.855 1.00 21.22 C ANISOU 353 CB ALA A 41 3116 2306 2639 54 1004 169 C ATOM 354 N ALA A 42 15.135 8.088 25.145 1.00 25.81 N ANISOU 354 N ALA A 42 3666 2890 3249 103 1024 264 N ATOM 355 CA ALA A 42 15.696 7.456 26.335 1.00 17.89 C ANISOU 355 CA ALA A 42 2661 1881 2257 126 1044 293 C ATOM 356 C ALA A 42 15.772 8.441 27.493 1.00 20.78 C ANISOU 356 C ALA A 42 2992 2275 2627 123 1006 310 C ATOM 357 O ALA A 42 15.482 8.089 28.642 1.00 20.15 O ANISOU 357 O ALA A 42 2913 2191 2552 128 1010 315 O ATOM 358 CB ALA A 42 17.078 6.884 26.023 1.00 22.00 C ANISOU 358 CB ALA A 42 3181 2402 2774 163 1076 328 C ATOM 359 N TYR A 43 16.169 9.680 27.205 1.00 30.14 N ANISOU 359 N TYR A 43 4149 3489 3813 115 972 316 N ATOM 360 CA TYR A 43 16.192 10.721 28.225 1.00 17.35 C ANISOU 360 CA TYR A 43 2496 1894 2201 107 934 323 C ATOM 361 C TYR A 43 14.791 11.013 28.752 1.00 23.12 C ANISOU 361 C TYR A 43 3233 2618 2933 79 913 292 C ATOM 362 O TYR A 43 14.596 11.167 29.964 1.00 30.59 O ANISOU 362 O TYR A 43 4168 3574 3882 81 900 295 O ATOM 363 CB TYR A 43 16.844 11.973 27.634 1.00 17.28 C ANISOU 363 CB TYR A 43 2458 1909 2200 101 909 333 C ATOM 364 CG TYR A 43 16.765 13.236 28.460 1.00 19.39 C ANISOU 364 CG TYR A 43 2690 2198 2480 85 869 330 C ATOM 365 CD1 TYR A 43 17.705 13.508 29.449 1.00 28.52 C ANISOU 365 CD1 TYR A 43 3813 3379 3644 100 857 349 C ATOM 366 CD2 TYR A 43 15.777 14.183 28.216 1.00 18.61 C ANISOU 366 CD2 TYR A 43 2589 2097 2385 56 842 306 C ATOM 367 CE1 TYR A 43 17.644 14.673 30.189 1.00 35.41 C ANISOU 367 CE1 TYR A 43 4653 4272 4531 84 820 339 C ATOM 368 CE2 TYR A 43 15.711 15.349 28.947 1.00 21.89 C ANISOU 368 CE2 TYR A 43 2974 2528 2815 42 808 301 C ATOM 369 CZ TYR A 43 16.645 15.587 29.931 1.00 27.99 C ANISOU 369 CZ TYR A 43 3715 3323 3598 54 798 315 C ATOM 370 OH TYR A 43 16.576 16.745 30.659 1.00 25.48 O ANISOU 370 OH TYR A 43 3366 3020 3296 38 764 303 O ATOM 371 N MET A 44 13.798 11.084 27.861 1.00 20.15 N ANISOU 371 N MET A 44 2875 2228 2552 56 910 262 N ATOM 372 CA MET A 44 12.437 11.381 28.299 1.00 26.31 C ANISOU 372 CA MET A 44 3659 3002 3335 29 890 232 C ATOM 373 C MET A 44 11.833 10.223 29.086 1.00 17.03 C ANISOU 373 C MET A 44 2505 1803 2163 32 918 224 C ATOM 374 O MET A 44 11.064 10.444 30.029 1.00 16.92 O ANISOU 374 O MET A 44 2486 1790 2154 21 904 215 O ATOM 375 CB MET A 44 11.553 11.733 27.104 1.00 22.72 C ANISOU 375 CB MET A 44 3214 2546 2873 7 879 202 C ATOM 376 CG MET A 44 11.831 13.097 26.505 1.00 22.74 C ANISOU 376 CG MET A 44 3194 2572 2875 3 850 210 C ATOM 377 SD MET A 44 12.013 14.400 27.738 1.00 19.56 S ANISOU 377 SD MET A 44 2755 2188 2489 -4 814 224 S ATOM 378 CE MET A 44 10.443 14.317 28.599 1.00 16.43 C ANISOU 378 CE MET A 44 2366 1782 2092 -26 800 192 C ATOM 379 N PHE A 45 12.150 8.983 28.709 1.00 18.81 N ANISOU 379 N PHE A 45 2756 2004 2389 46 960 228 N ATOM 380 CA PHE A 45 11.682 7.844 29.492 1.00 17.68 C ANISOU 380 CA PHE A 45 2632 1830 2254 52 995 226 C ATOM 381 C PHE A 45 12.259 7.884 30.901 1.00 30.89 C ANISOU 381 C PHE A 45 4290 3520 3926 79 995 262 C ATOM 382 O PHE A 45 11.569 7.554 31.874 1.00 24.87 O ANISOU 382 O PHE A 45 3533 2748 3168 78 1004 261 O ATOM 383 CB PHE A 45 12.044 6.533 28.791 1.00 17.75 C ANISOU 383 CB PHE A 45 2671 1806 2267 66 1046 225 C ATOM 384 CG PHE A 45 11.446 5.308 29.438 1.00 24.77 C ANISOU 384 CG PHE A 45 3584 2655 3173 68 1090 220 C ATOM 385 CD1 PHE A 45 10.071 5.157 29.533 1.00 38.17 C ANISOU 385 CD1 PHE A 45 5289 4332 4882 35 1090 182 C ATOM 386 CD2 PHE A 45 12.260 4.303 29.938 1.00 25.26 C ANISOU 386 CD2 PHE A 45 3659 2698 3240 105 1136 256 C ATOM 387 CE1 PHE A 45 9.520 4.031 30.124 1.00 28.10 C ANISOU 387 CE1 PHE A 45 4033 3014 3628 36 1137 179 C ATOM 388 CE2 PHE A 45 11.714 3.175 30.526 1.00 27.52 C ANISOU 388 CE2 PHE A 45 3968 2943 3546 109 1184 256 C ATOM 389 CZ PHE A 45 10.344 3.039 30.619 1.00 20.77 C ANISOU 389 CZ PHE A 45 3121 2064 2708 73 1185 217 C ATOM 390 N LEU A 46 13.524 8.291 31.031 1.00 23.33 N ANISOU 390 N LEU A 46 3312 2592 2962 104 984 294 N ATOM 391 CA LEU A 46 14.133 8.396 32.352 1.00 29.12 C ANISOU 391 CA LEU A 46 4025 3352 3689 132 978 325 C ATOM 392 C LEU A 46 13.426 9.437 33.209 1.00 30.72 C ANISOU 392 C LEU A 46 4206 3577 3890 114 935 309 C ATOM 393 O LEU A 46 13.172 9.204 34.396 1.00 23.31 O ANISOU 393 O LEU A 46 3265 2646 2944 129 939 320 O ATOM 394 CB LEU A 46 15.617 8.737 32.228 1.00 17.62 C ANISOU 394 CB LEU A 46 2542 1925 2226 159 970 355 C ATOM 395 CG LEU A 46 16.343 8.728 33.574 1.00 35.65 C ANISOU 395 CG LEU A 46 4802 4243 4499 193 963 385 C ATOM 396 CD1 LEU A 46 16.324 7.326 34.155 1.00 26.45 C ANISOU 396 CD1 LEU A 46 3664 3057 3330 228 1013 409 C ATOM 397 CD2 LEU A 46 17.767 9.243 33.443 1.00 25.82 C ANISOU 397 CD2 LEU A 46 3522 3035 3253 213 948 407 C ATOM 398 N LEU A 47 13.102 10.596 32.627 1.00 24.43 N ANISOU 398 N LEU A 47 3394 2791 3098 84 898 286 N ATOM 399 CA LEU A 47 12.447 11.649 33.397 1.00 23.07 C ANISOU 399 CA LEU A 47 3201 2638 2925 66 859 270 C ATOM 400 C LEU A 47 11.066 11.211 33.871 1.00 25.63 C ANISOU 400 C LEU A 47 3546 2941 3251 51 869 250 C ATOM 401 O LEU A 47 10.668 11.516 34.999 1.00 28.66 O ANISOU 401 O LEU A 47 3920 3339 3631 54 855 250 O ATOM 402 CB LEU A 47 12.352 12.931 32.570 1.00 20.47 C ANISOU 402 CB LEU A 47 2854 2318 2604 39 824 253 C ATOM 403 CG LEU A 47 13.665 13.622 32.199 1.00 22.75 C ANISOU 403 CG LEU A 47 3115 2629 2898 49 811 272 C ATOM 404 CD1 LEU A 47 13.385 14.963 31.540 1.00 24.33 C ANISOU 404 CD1 LEU A 47 3299 2834 3111 23 781 256 C ATOM 405 CD2 LEU A 47 14.541 13.794 33.424 1.00 35.64 C ANISOU 405 CD2 LEU A 47 4720 4294 4528 72 799 289 C ATOM 406 N ILE A 48 10.321 10.502 33.023 1.00 23.74 N ANISOU 406 N ILE A 48 3334 2668 3019 34 894 231 N ATOM 407 CA ILE A 48 8.999 10.025 33.417 1.00 26.46 C ANISOU 407 CA ILE A 48 3694 2988 3370 16 907 209 C ATOM 408 C ILE A 48 9.114 8.991 34.530 1.00 26.44 C ANISOU 408 C ILE A 48 3704 2975 3368 45 945 235 C ATOM 409 O ILE A 48 8.382 9.044 35.525 1.00 25.39 O ANISOU 409 O ILE A 48 3569 2844 3234 44 944 233 O ATOM 410 CB ILE A 48 8.250 9.457 32.200 1.00 22.97 C ANISOU 410 CB ILE A 48 3274 2517 2938 -9 925 177 C ATOM 411 CG1 ILE A 48 8.074 10.536 31.136 1.00 26.60 C ANISOU 411 CG1 ILE A 48 3720 2995 3392 -31 888 156 C ATOM 412 CG2 ILE A 48 6.901 8.900 32.616 1.00 20.42 C ANISOU 412 CG2 ILE A 48 2963 2168 2628 -29 943 153 C ATOM 413 CD1 ILE A 48 7.683 9.988 29.790 1.00 19.44 C ANISOU 413 CD1 ILE A 48 2831 2070 2485 -46 903 128 C ATOM 414 N MET A 49 10.040 8.039 34.383 1.00 28.03 N ANISOU 414 N MET A 49 3918 3163 3568 74 982 261 N ATOM 415 CA MET A 49 10.137 6.949 35.350 1.00 34.13 C ANISOU 415 CA MET A 49 4706 3921 4341 106 1027 291 C ATOM 416 C MET A 49 10.741 7.406 36.671 1.00 25.50 C ANISOU 416 C MET A 49 3591 2872 3228 140 1008 322 C ATOM 417 O MET A 49 10.519 6.764 37.703 1.00 31.86 O ANISOU 417 O MET A 49 4405 3673 4028 166 1037 344 O ATOM 418 CB MET A 49 10.949 5.793 34.765 1.00 25.84 C ANISOU 418 CB MET A 49 3678 2843 3297 130 1075 311 C ATOM 419 CG MET A 49 10.273 5.095 33.594 1.00 26.60 C ANISOU 419 CG MET A 49 3800 2892 3414 99 1104 276 C ATOM 420 SD MET A 49 8.656 4.411 34.012 1.00 34.92 S ANISOU 420 SD MET A 49 4872 3901 4493 71 1135 247 S ATOM 421 CE MET A 49 9.114 3.108 35.151 1.00 25.72 C ANISOU 421 CE MET A 49 3726 2710 3335 120 1202 298 C ATOM 422 N LEU A 50 11.522 8.484 36.664 1.00 23.20 N ANISOU 422 N LEU A 50 3269 2623 2924 142 962 323 N ATOM 423 CA LEU A 50 11.946 9.089 37.918 1.00 23.60 C ANISOU 423 CA LEU A 50 3293 2721 2954 168 935 339 C ATOM 424 C LEU A 50 10.954 10.140 38.400 1.00 26.90 C ANISOU 424 C LEU A 50 3698 3152 3372 139 896 309 C ATOM 425 O LEU A 50 10.668 10.218 39.597 1.00 28.33 O ANISOU 425 O LEU A 50 3873 3355 3538 158 891 316 O ATOM 426 CB LEU A 50 13.338 9.713 37.770 1.00 27.38 C ANISOU 426 CB LEU A 50 3740 3239 3424 184 907 352 C ATOM 427 CG LEU A 50 14.478 8.798 37.314 1.00 23.90 C ANISOU 427 CG LEU A 50 3306 2794 2982 217 942 385 C ATOM 428 CD1 LEU A 50 15.824 9.505 37.432 1.00 33.80 C ANISOU 428 CD1 LEU A 50 4520 4096 4226 235 910 398 C ATOM 429 CD2 LEU A 50 14.484 7.500 38.101 1.00 31.66 C ANISOU 429 CD2 LEU A 50 4311 3763 3954 259 992 419 C ATOM 430 N GLY A 51 10.400 10.933 37.481 1.00 21.31 N ANISOU 430 N GLY A 51 2986 2432 2678 98 870 276 N ATOM 431 CA GLY A 51 9.540 12.036 37.887 1.00 31.44 C ANISOU 431 CA GLY A 51 4254 3729 3963 72 831 249 C ATOM 432 C GLY A 51 8.240 11.591 38.530 1.00 24.77 C ANISOU 432 C GLY A 51 3428 2865 3120 65 850 240 C ATOM 433 O GLY A 51 7.754 12.230 39.467 1.00 31.17 O ANISOU 433 O GLY A 51 4225 3696 3921 66 828 231 O ATOM 434 N PHE A 52 7.643 10.506 38.024 1.00 21.13 N ANISOU 434 N PHE A 52 2994 2362 2672 57 892 238 N ATOM 435 CA PHE A 52 6.376 10.042 38.590 1.00 22.34 C ANISOU 435 CA PHE A 52 3162 2492 2834 47 915 229 C ATOM 436 C PHE A 52 6.512 9.587 40.040 1.00 26.18 C ANISOU 436 C PHE A 52 3650 2994 3303 87 936 261 C ATOM 437 O PHE A 52 5.713 10.038 40.879 1.00 25.78 O ANISOU 437 O PHE A 52 3592 2956 3247 84 924 252 O ATOM 438 CB PHE A 52 5.782 8.951 37.688 1.00 27.94 C ANISOU 438 CB PHE A 52 3897 3152 3567 27 958 215 C ATOM 439 CG PHE A 52 4.670 8.159 38.326 1.00 25.65 C ANISOU 439 CG PHE A 52 3622 2830 3292 22 997 213 C ATOM 440 CD1 PHE A 52 3.586 8.793 38.917 1.00 30.37 C ANISOU 440 CD1 PHE A 52 4210 3438 3892 5 978 195 C ATOM 441 CD2 PHE A 52 4.704 6.773 38.310 1.00 30.71 C ANISOU 441 CD2 PHE A 52 4288 3429 3951 35 1058 229 C ATOM 442 CE1 PHE A 52 2.567 8.057 39.495 1.00 38.67 C ANISOU 442 CE1 PHE A 52 5274 4459 4961 0 1017 195 C ATOM 443 CE2 PHE A 52 3.689 6.034 38.880 1.00 28.91 C ANISOU 443 CE2 PHE A 52 4073 3168 3744 30 1100 228 C ATOM 444 CZ PHE A 52 2.619 6.675 39.474 1.00 35.49 C ANISOU 444 CZ PHE A 52 4894 4013 4578 12 1080 212 C ATOM 445 N PRO A 53 7.468 8.728 40.415 1.00 31.30 N ANISOU 445 N PRO A 53 4306 3646 3941 129 969 299 N ATOM 446 CA PRO A 53 7.496 8.270 41.813 1.00 21.77 C ANISOU 446 CA PRO A 53 3100 2457 2713 173 992 332 C ATOM 447 C PRO A 53 7.975 9.323 42.791 1.00 31.64 C ANISOU 447 C PRO A 53 4321 3770 3932 194 944 334 C ATOM 448 O PRO A 53 7.421 9.427 43.892 1.00 24.97 O ANISOU 448 O PRO A 53 3475 2943 3071 212 946 340 O ATOM 449 CB PRO A 53 8.452 7.067 41.777 1.00 26.53 C ANISOU 449 CB PRO A 53 3720 3047 3314 214 1041 374 C ATOM 450 CG PRO A 53 8.581 6.704 40.342 1.00 22.50 C ANISOU 450 CG PRO A 53 3222 2496 2830 183 1053 355 C ATOM 451 CD PRO A 53 8.452 7.995 39.603 1.00 24.16 C ANISOU 451 CD PRO A 53 3412 2725 3042 142 994 316 C ATOM 452 N AILE A 54 8.986 10.115 42.430 0.58 26.94 N ANISOU 452 N AILE A 54 3701 3208 3328 193 902 326 N ATOM 453 N BILE A 54 8.999 10.099 42.426 0.42 26.96 N ANISOU 453 N BILE A 54 3703 3209 3330 194 903 327 N ATOM 454 CA AILE A 54 9.536 11.068 43.389 0.58 22.40 C ANISOU 454 CA AILE A 54 3094 2692 2725 213 858 322 C ATOM 455 CA BILE A 54 9.551 11.092 43.346 0.42 22.42 C ANISOU 455 CA BILE A 54 3096 2695 2728 212 857 322 C ATOM 456 C AILE A 54 8.528 12.172 43.693 0.58 22.02 C ANISOU 456 C AILE A 54 3036 2651 2681 181 821 285 C ATOM 457 C BILE A 54 8.498 12.133 43.695 0.42 22.05 C ANISOU 457 C BILE A 54 3040 2654 2685 181 823 285 C ATOM 458 O AILE A 54 8.439 12.648 44.832 0.58 20.28 O ANISOU 458 O AILE A 54 2800 2470 2435 202 801 282 O ATOM 459 O BILE A 54 8.345 12.519 44.861 0.42 20.26 O ANISOU 459 O BILE A 54 2802 2465 2433 204 807 284 O ATOM 460 CB AILE A 54 10.883 11.628 42.890 0.58 25.77 C ANISOU 460 CB AILE A 54 3493 3149 3150 216 826 321 C ATOM 461 CB BILE A 54 10.809 11.741 42.740 0.42 25.61 C ANISOU 461 CB BILE A 54 3473 3125 3134 209 823 316 C ATOM 462 CG1AILE A 54 11.619 12.331 44.031 0.58 25.12 C ANISOU 462 CG1AILE A 54 3376 3133 3037 247 788 320 C ATOM 463 CG1BILE A 54 11.848 10.679 42.390 0.42 26.18 C ANISOU 463 CG1BILE A 54 3554 3192 3203 242 859 354 C ATOM 464 CG2AILE A 54 10.694 12.582 41.726 0.58 25.92 C ANISOU 464 CG2AILE A 54 3503 3148 3197 165 795 286 C ATOM 465 CG2BILE A 54 11.415 12.727 43.716 0.42 25.52 C ANISOU 465 CG2BILE A 54 3423 3174 3098 226 776 305 C ATOM 466 CD1AILE A 54 12.991 12.827 43.649 0.58 24.27 C ANISOU 466 CD1AILE A 54 3234 3056 2930 252 760 319 C ATOM 467 CD1BILE A 54 13.020 11.224 41.611 0.42 23.76 C ANISOU 467 CD1BILE A 54 3222 2902 2904 235 833 350 C ATOM 468 N ASN A 55 7.752 12.599 42.693 1.00 19.08 N ANISOU 468 N ASN A 55 2670 2244 2337 133 812 255 N ATOM 469 CA ASN A 55 6.730 13.610 42.940 1.00 22.41 C ANISOU 469 CA ASN A 55 3083 2669 2764 104 781 222 C ATOM 470 C ASN A 55 5.518 13.026 43.653 1.00 18.76 C ANISOU 470 C ASN A 55 2640 2189 2300 109 812 227 C ATOM 471 O ASN A 55 4.949 13.671 44.541 1.00 18.26 O ANISOU 471 O ASN A 55 2567 2148 2224 112 793 214 O ATOM 472 CB ASN A 55 6.321 14.275 41.628 1.00 17.17 C ANISOU 472 CB ASN A 55 2418 1978 2128 58 762 194 C ATOM 473 CG ASN A 55 7.359 15.257 41.136 1.00 27.76 C ANISOU 473 CG ASN A 55 3734 3342 3474 50 724 185 C ATOM 474 OD1 ASN A 55 7.549 16.321 41.729 1.00 21.86 O ANISOU 474 OD1 ASN A 55 2961 2624 2720 50 688 168 O ATOM 475 ND2 ASN A 55 8.038 14.910 40.048 1.00 19.73 N ANISOU 475 ND2 ASN A 55 2721 2308 2467 45 735 195 N ATOM 476 N PHE A 56 5.101 11.813 43.278 1.00 20.45 N ANISOU 476 N PHE A 56 2881 2361 2529 108 862 243 N ATOM 477 CA PHE A 56 3.988 11.178 43.977 1.00 27.59 C ANISOU 477 CA PHE A 56 3801 3244 3437 114 899 251 C ATOM 478 C PHE A 56 4.329 10.940 45.441 1.00 23.17 C ANISOU 478 C PHE A 56 3239 2721 2842 166 912 283 C ATOM 479 O PHE A 56 3.490 11.154 46.325 1.00 22.58 O ANISOU 479 O PHE A 56 3164 2657 2759 173 914 280 O ATOM 480 CB PHE A 56 3.604 9.864 43.300 1.00 24.85 C ANISOU 480 CB PHE A 56 3482 2842 3119 103 956 261 C ATOM 481 CG PHE A 56 2.484 9.136 43.992 1.00 30.49 C ANISOU 481 CG PHE A 56 4211 3528 3844 106 1002 271 C ATOM 482 CD1 PHE A 56 1.172 9.547 43.832 1.00 26.75 C ANISOU 482 CD1 PHE A 56 3734 3038 3391 68 993 238 C ATOM 483 CD2 PHE A 56 2.744 8.050 44.812 1.00 37.30 C ANISOU 483 CD2 PHE A 56 5090 4382 4699 151 1056 315 C ATOM 484 CE1 PHE A 56 0.139 8.886 44.469 1.00 29.06 C ANISOU 484 CE1 PHE A 56 4038 3305 3700 69 1038 247 C ATOM 485 CE2 PHE A 56 1.714 7.384 45.451 1.00 39.58 C ANISOU 485 CE2 PHE A 56 5393 4642 5004 154 1104 327 C ATOM 486 CZ PHE A 56 0.410 7.804 45.280 1.00 39.82 C ANISOU 486 CZ PHE A 56 5418 4654 5057 112 1095 292 C ATOM 487 N ALEU A 57 5.555 10.489 45.720 0.47 24.83 N ANISOU 487 N ALEU A 57 3446 2957 3031 208 920 315 N ATOM 488 N BLEU A 57 5.556 10.492 45.716 0.53 24.81 N ANISOU 488 N BLEU A 57 3444 2954 3028 208 920 315 N ATOM 489 CA ALEU A 57 5.958 10.262 47.104 0.47 22.89 C ANISOU 489 CA ALEU A 57 3196 2756 2745 266 930 347 C ATOM 490 CA BLEU A 57 5.967 10.263 47.096 0.53 22.91 C ANISOU 490 CA BLEU A 57 3199 2759 2748 266 929 347 C ATOM 491 C ALEU A 57 5.973 11.563 47.898 0.47 25.66 C ANISOU 491 C ALEU A 57 3518 3163 3067 269 873 319 C ATOM 492 C BLEU A 57 5.970 11.562 47.893 0.53 25.67 C ANISOU 492 C BLEU A 57 3520 3164 3069 268 873 319 C ATOM 493 O ALEU A 57 5.569 11.588 49.066 0.47 26.55 O ANISOU 493 O ALEU A 57 3630 3305 3152 300 879 330 O ATOM 494 O BLEU A 57 5.557 11.583 49.058 0.53 26.55 O ANISOU 494 O BLEU A 57 3631 3305 3153 300 879 329 O ATOM 495 CB ALEU A 57 7.325 9.582 47.150 0.47 21.76 C ANISOU 495 CB ALEU A 57 3051 2635 2583 311 945 384 C ATOM 496 CB BLEU A 57 7.346 9.607 47.131 0.53 21.75 C ANISOU 496 CB BLEU A 57 3049 2634 2582 310 944 384 C ATOM 497 CG ALEU A 57 7.321 8.108 46.741 0.47 22.58 C ANISOU 497 CG ALEU A 57 3186 2685 2708 325 1015 422 C ATOM 498 CG BLEU A 57 7.823 9.190 48.521 0.53 22.21 C ANISOU 498 CG BLEU A 57 3102 2742 2593 379 960 424 C ATOM 499 CD1ALEU A 57 8.731 7.545 46.723 0.47 24.24 C ANISOU 499 CD1ALEU A 57 3392 2920 2900 371 1027 458 C ATOM 500 CD1BLEU A 57 6.803 8.258 49.155 0.53 28.19 C ANISOU 500 CD1BLEU A 57 3889 3467 3355 399 1022 454 C ATOM 501 CD2ALEU A 57 6.427 7.300 47.671 0.47 19.07 C ANISOU 501 CD2ALEU A 57 2764 2222 2261 352 1070 452 C ATOM 502 CD2BLEU A 57 9.188 8.530 48.449 0.53 19.25 C ANISOU 502 CD2BLEU A 57 2723 2389 2202 424 974 461 C ATOM 503 N THR A 58 6.435 12.655 47.282 1.00 17.93 N ANISOU 503 N THR A 58 2515 2199 2097 237 820 284 N ATOM 504 CA THR A 58 6.398 13.952 47.954 1.00 25.41 C ANISOU 504 CA THR A 58 3436 3191 3027 233 767 250 C ATOM 505 C THR A 58 4.964 14.362 48.269 1.00 30.07 C ANISOU 505 C THR A 58 4036 3764 3626 210 768 229 C ATOM 506 O THR A 58 4.678 14.867 49.362 1.00 29.58 O ANISOU 506 O THR A 58 3963 3739 3536 231 752 219 O ATOM 507 CB THR A 58 7.084 15.013 47.091 1.00 20.68 C ANISOU 507 CB THR A 58 2812 2598 2448 198 720 217 C ATOM 508 OG1 THR A 58 8.448 14.637 46.867 1.00 22.78 O ANISOU 508 OG1 THR A 58 3065 2885 2705 222 720 238 O ATOM 509 CG2 THR A 58 7.045 16.375 47.778 1.00 27.73 C ANISOU 509 CG2 THR A 58 3677 3532 3329 190 669 178 C ATOM 510 N LEU A 59 4.049 14.143 47.324 1.00 20.81 N ANISOU 510 N LEU A 59 2880 2536 2490 168 787 219 N ATOM 511 CA LEU A 59 2.638 14.429 47.560 1.00 18.58 C ANISOU 511 CA LEU A 59 2604 2234 2220 146 792 201 C ATOM 512 C LEU A 59 2.079 13.561 48.684 1.00 23.58 C ANISOU 512 C LEU A 59 3254 2871 2833 185 838 233 C ATOM 513 O LEU A 59 1.407 14.059 49.594 1.00 24.14 O ANISOU 513 O LEU A 59 3321 2965 2887 195 829 223 O ATOM 514 CB LEU A 59 1.851 14.223 46.264 1.00 23.78 C ANISOU 514 CB LEU A 59 3276 2839 2921 97 805 186 C ATOM 515 CG LEU A 59 0.327 14.356 46.242 1.00 27.26 C ANISOU 515 CG LEU A 59 3722 3253 3381 68 816 167 C ATOM 516 CD1 LEU A 59 -0.110 14.923 44.899 1.00 41.08 C ANISOU 516 CD1 LEU A 59 5468 4978 5163 19 792 135 C ATOM 517 CD2 LEU A 59 -0.348 13.015 46.484 1.00 22.95 C ANISOU 517 CD2 LEU A 59 3199 2672 2848 78 877 192 C ATOM 518 N TYR A 60 2.356 12.255 48.639 1.00 20.67 N ANISOU 518 N TYR A 60 2906 2480 2468 208 890 272 N ATOM 519 CA TYR A 60 1.763 11.333 49.604 1.00 23.78 C ANISOU 519 CA TYR A 60 3318 2867 2851 245 944 308 C ATOM 520 C TYR A 60 2.265 11.600 51.018 1.00 34.96 C ANISOU 520 C TYR A 60 4722 4348 4211 303 932 327 C ATOM 521 O TYR A 60 1.478 11.601 51.972 1.00 25.65 O ANISOU 521 O TYR A 60 3548 3181 3016 324 949 336 O ATOM 522 CB TYR A 60 2.058 9.889 49.189 1.00 37.01 C ANISOU 522 CB TYR A 60 5017 4499 4545 259 1006 347 C ATOM 523 CG TYR A 60 1.362 8.828 50.019 1.00 23.98 C ANISOU 523 CG TYR A 60 3388 2825 2897 290 1074 388 C ATOM 524 CD1 TYR A 60 1.855 8.457 51.265 1.00 43.19 C ANISOU 524 CD1 TYR A 60 5824 5301 5285 359 1096 432 C ATOM 525 CD2 TYR A 60 0.228 8.180 49.544 1.00 37.60 C ANISOU 525 CD2 TYR A 60 5130 4487 4670 254 1120 382 C ATOM 526 CE1 TYR A 60 1.230 7.491 52.022 1.00 39.60 C ANISOU 526 CE1 TYR A 60 5390 4824 4834 392 1165 475 C ATOM 527 CE2 TYR A 60 -0.404 7.206 50.296 1.00 33.74 C ANISOU 527 CE2 TYR A 60 4659 3972 4190 282 1189 420 C ATOM 528 CZ TYR A 60 0.104 6.865 51.534 1.00 42.99 C ANISOU 528 CZ TYR A 60 5835 5183 5316 352 1213 470 C ATOM 529 OH TYR A 60 -0.511 5.898 52.296 1.00 47.36 O ANISOU 529 OH TYR A 60 6408 5709 5879 384 1287 514 O ATOM 530 N VAL A 61 3.574 11.810 51.177 1.00 32.31 N ANISOU 530 N VAL A 61 4372 4060 3847 333 903 333 N ATOM 531 CA VAL A 61 4.135 12.013 52.510 1.00 28.07 C ANISOU 531 CA VAL A 61 3820 3593 3252 393 889 348 C ATOM 532 C VAL A 61 3.576 13.283 53.139 1.00 29.67 C ANISOU 532 C VAL A 61 4005 3832 3438 380 841 304 C ATOM 533 O VAL A 61 3.211 13.300 54.321 1.00 34.55 O ANISOU 533 O VAL A 61 4623 4487 4017 422 850 315 O ATOM 534 CB VAL A 61 5.674 12.039 52.445 1.00 30.48 C ANISOU 534 CB VAL A 61 4105 3943 3533 421 862 356 C ATOM 535 CG1 VAL A 61 6.253 12.454 53.784 1.00 38.00 C ANISOU 535 CG1 VAL A 61 5035 4980 4423 479 834 358 C ATOM 536 CG2 VAL A 61 6.212 10.675 52.044 1.00 19.45 C ANISOU 536 CG2 VAL A 61 2729 2516 2146 448 918 408 C ATOM 537 N THR A 62 3.487 14.360 52.356 1.00 26.07 N ANISOU 537 N THR A 62 3532 3363 3010 326 794 255 N ATOM 538 CA THR A 62 2.992 15.627 52.887 1.00 29.12 C ANISOU 538 CA THR A 62 3901 3778 3386 312 749 210 C ATOM 539 C THR A 62 1.531 15.524 53.313 1.00 35.25 C ANISOU 539 C THR A 62 4694 4529 4169 306 779 213 C ATOM 540 O THR A 62 1.136 16.096 54.336 1.00 28.63 O ANISOU 540 O THR A 62 3849 3729 3299 328 764 198 O ATOM 541 CB THR A 62 3.174 16.732 51.849 1.00 30.97 C ANISOU 541 CB THR A 62 4117 3994 3657 256 702 164 C ATOM 542 OG1 THR A 62 4.563 16.841 51.513 1.00 32.38 O ANISOU 542 OG1 THR A 62 4276 4198 3830 263 677 163 O ATOM 543 CG2 THR A 62 2.685 18.062 52.396 1.00 25.53 C ANISOU 543 CG2 THR A 62 3411 3330 2961 242 660 117 C ATOM 544 N VAL A 63 0.713 14.805 52.542 1.00 26.92 N ANISOU 544 N VAL A 63 3661 3411 3155 276 820 228 N ATOM 545 CA VAL A 63 -0.700 14.669 52.883 1.00 38.59 C ANISOU 545 CA VAL A 63 5152 4863 4647 266 851 229 C ATOM 546 C VAL A 63 -0.874 13.831 54.144 1.00 23.33 C ANISOU 546 C VAL A 63 3234 2954 2678 326 898 274 C ATOM 547 O VAL A 63 -1.691 14.157 55.015 1.00 34.48 O ANISOU 547 O VAL A 63 4646 4383 4072 341 904 270 O ATOM 548 CB VAL A 63 -1.479 14.074 51.695 1.00 31.24 C ANISOU 548 CB VAL A 63 4235 3862 3772 216 882 228 C ATOM 549 CG1 VAL A 63 -2.884 13.675 52.125 1.00 39.85 C ANISOU 549 CG1 VAL A 63 5337 4925 4878 212 925 237 C ATOM 550 CG2 VAL A 63 -1.528 15.066 50.545 1.00 37.22 C ANISOU 550 CG2 VAL A 63 4978 4604 4559 161 833 184 C ATOM 551 N GLN A 64 -0.107 12.745 54.269 1.00 34.72 N ANISOU 551 N GLN A 64 4688 4397 4107 365 936 320 N ATOM 552 CA GLN A 64 -0.279 11.842 55.403 1.00 36.78 C ANISOU 552 CA GLN A 64 4964 4674 4335 427 991 372 C ATOM 553 C GLN A 64 0.114 12.495 56.723 1.00 37.81 C ANISOU 553 C GLN A 64 5079 4887 4398 482 959 368 C ATOM 554 O GLN A 64 -0.517 12.228 57.752 1.00 34.89 O ANISOU 554 O GLN A 64 4720 4536 4002 523 993 394 O ATOM 555 CB GLN A 64 0.530 10.561 55.187 1.00 44.75 C ANISOU 555 CB GLN A 64 5990 5666 5348 459 1039 423 C ATOM 556 CG GLN A 64 0.420 9.556 56.325 1.00 45.76 C ANISOU 556 CG GLN A 64 6136 5809 5444 530 1104 486 C ATOM 557 CD GLN A 64 1.158 8.262 56.033 1.00 57.78 C ANISOU 557 CD GLN A 64 7676 7302 6975 560 1159 539 C ATOM 558 OE1 GLN A 64 1.863 8.148 55.028 1.00 56.01 O ANISOU 558 OE1 GLN A 64 7449 7056 6776 532 1143 527 O ATOM 559 NE2 GLN A 64 0.995 7.276 56.911 1.00 62.46 N ANISOU 559 NE2 GLN A 64 8288 7896 7550 621 1228 600 N ATOM 560 N HIS A 65 1.130 13.353 56.719 1.00 39.64 N ANISOU 560 N HIS A 65 5286 5170 4604 485 896 335 N ATOM 561 CA HIS A 65 1.688 13.905 57.947 1.00 35.40 C ANISOU 561 CA HIS A 65 4731 4720 4001 540 863 327 C ATOM 562 C HIS A 65 1.189 15.331 58.151 1.00 38.35 C ANISOU 562 C HIS A 65 5085 5113 4372 508 808 263 C ATOM 563 O HIS A 65 1.421 16.204 57.308 1.00 41.58 O ANISOU 563 O HIS A 65 5479 5506 4815 454 761 217 O ATOM 564 CB HIS A 65 3.214 13.857 57.906 1.00 22.33 C ANISOU 564 CB HIS A 65 3055 3113 2316 568 833 330 C ATOM 565 CG HIS A 65 3.765 12.466 57.871 1.00 22.21 C ANISOU 565 CG HIS A 65 3059 3086 2295 613 889 397 C ATOM 566 ND1 HIS A 65 4.123 11.779 59.011 1.00 48.73 N ANISOU 566 ND1 HIS A 65 6422 6500 5594 695 920 446 N ATOM 567 CD2 HIS A 65 4.007 11.627 56.836 1.00 38.79 C ANISOU 567 CD2 HIS A 65 5174 5125 4440 589 924 423 C ATOM 568 CE1 HIS A 65 4.571 10.581 58.679 1.00 48.95 C ANISOU 568 CE1 HIS A 65 6467 6497 5633 720 973 502 C ATOM 569 NE2 HIS A 65 4.511 10.464 57.365 1.00 40.03 N ANISOU 569 NE2 HIS A 65 5345 5297 4568 655 976 487 N ATOM 570 N LYS A 66 0.503 15.557 59.275 1.00 31.11 N ANISOU 570 N LYS A 66 4172 4231 3417 543 816 264 N ATOM 571 CA LYS A 66 -0.048 16.870 59.585 1.00 30.07 C ANISOU 571 CA LYS A 66 4024 4118 3281 518 770 205 C ATOM 572 C LYS A 66 1.003 17.844 60.098 1.00 30.83 C ANISOU 572 C LYS A 66 4089 4288 3337 536 704 158 C ATOM 573 O LYS A 66 0.737 19.049 60.146 1.00 39.93 O ANISOU 573 O LYS A 66 5225 5449 4497 505 660 100 O ATOM 574 CB LYS A 66 -1.174 16.739 60.615 1.00 43.34 C ANISOU 574 CB LYS A 66 5721 5810 4936 552 806 222 C ATOM 575 N LYS A 67 2.183 17.353 60.487 1.00 36.89 N ANISOU 575 N LYS A 67 4845 5109 4062 585 699 180 N ATOM 576 CA LYS A 67 3.259 18.238 60.917 1.00 37.22 C ANISOU 576 CA LYS A 67 4850 5223 4068 598 635 130 C ATOM 577 C LYS A 67 3.817 19.065 59.767 1.00 37.47 C ANISOU 577 C LYS A 67 4861 5221 4156 530 589 83 C ATOM 578 O LYS A 67 4.488 20.074 60.011 1.00 40.86 O ANISOU 578 O LYS A 67 5257 5695 4573 522 534 26 O ATOM 579 CB LYS A 67 4.383 17.423 61.562 1.00 41.68 C ANISOU 579 CB LYS A 67 5406 5857 4575 670 642 170 C ATOM 580 CG LYS A 67 5.027 16.402 60.628 1.00 37.98 C ANISOU 580 CG LYS A 67 4948 5346 4138 664 674 219 C ATOM 581 N LEU A 68 3.553 18.663 58.525 1.00 33.94 N ANISOU 581 N LEU A 68 4430 4696 3768 481 614 103 N ATOM 582 CA LEU A 68 4.133 19.315 57.353 1.00 36.32 C ANISOU 582 CA LEU A 68 4714 4965 4121 422 579 70 C ATOM 583 C LEU A 68 3.138 20.317 56.770 1.00 33.93 C ANISOU 583 C LEU A 68 4414 4610 3866 362 564 28 C ATOM 584 O LEU A 68 2.531 20.108 55.718 1.00 32.25 O ANISOU 584 O LEU A 68 4219 4331 3703 318 585 40 O ATOM 585 CB LEU A 68 4.547 18.267 56.322 1.00 32.51 C ANISOU 585 CB LEU A 68 4247 4436 3669 412 614 116 C ATOM 586 CG LEU A 68 5.489 17.169 56.820 1.00 24.06 C ANISOU 586 CG LEU A 68 3177 3408 2555 474 638 167 C ATOM 587 CD1 LEU A 68 5.810 16.191 55.699 1.00 32.47 C ANISOU 587 CD1 LEU A 68 4261 4418 3660 458 674 208 C ATOM 588 CD2 LEU A 68 6.764 17.771 57.388 1.00 33.36 C ANISOU 588 CD2 LEU A 68 4315 4665 3695 502 585 135 C ATOM 589 N ARG A 69 2.982 21.436 57.486 1.00 35.91 N ANISOU 589 N ARG A 69 4646 4898 4100 362 525 -24 N ATOM 590 CA ARG A 69 2.051 22.483 57.080 1.00 29.38 C ANISOU 590 CA ARG A 69 3820 4028 3314 312 510 -65 C ATOM 591 C ARG A 69 2.686 23.871 57.100 1.00 38.10 C ANISOU 591 C ARG A 69 4891 5153 4432 286 455 -131 C ATOM 592 O ARG A 69 1.967 24.873 57.174 1.00 32.93 O ANISOU 592 O ARG A 69 4234 4482 3797 260 440 -172 O ATOM 593 CB ARG A 69 0.798 22.464 57.960 1.00 32.20 C ANISOU 593 CB ARG A 69 4196 4391 3648 334 534 -60 C ATOM 594 CG ARG A 69 -0.030 21.188 57.845 1.00 33.28 C ANISOU 594 CG ARG A 69 4366 4493 3787 349 595 1 C ATOM 595 CD ARG A 69 -0.565 20.991 56.434 1.00 38.17 C ANISOU 595 CD ARG A 69 4998 5035 4471 292 612 13 C ATOM 596 NE ARG A 69 -1.370 19.781 56.310 1.00 37.98 N ANISOU 596 NE ARG A 69 5001 4975 4456 300 671 64 N ATOM 597 CZ ARG A 69 -0.884 18.585 56.009 1.00 40.87 C ANISOU 597 CZ ARG A 69 5380 5327 4822 317 706 110 C ATOM 598 NH1 ARG A 69 0.409 18.396 55.801 1.00 36.32 N ANISOU 598 NH1 ARG A 69 4792 4775 4233 330 688 115 N ATOM 599 NH2 ARG A 69 -1.715 17.550 55.921 1.00 28.17 N ANISOU 599 NH2 ARG A 69 3795 3679 3229 320 763 150 N ATOM 600 N THR A 70 4.012 23.957 57.036 1.00 27.46 N ANISOU 600 N THR A 70 3515 3840 3077 292 427 -144 N ATOM 601 CA THR A 70 4.666 25.247 56.917 1.00 24.78 C ANISOU 601 CA THR A 70 3142 3511 2764 260 379 -208 C ATOM 602 C THR A 70 4.504 25.779 55.495 1.00 30.59 C ANISOU 602 C THR A 70 3880 4172 3572 197 380 -213 C ATOM 603 O THR A 70 4.141 25.031 54.584 1.00 27.14 O ANISOU 603 O THR A 70 3467 3687 3157 183 412 -167 O ATOM 604 CB THR A 70 6.146 25.130 57.275 1.00 26.61 C ANISOU 604 CB THR A 70 3338 3805 2967 286 350 -221 C ATOM 605 OG1 THR A 70 6.803 24.272 56.335 1.00 28.70 O ANISOU 605 OG1 THR A 70 3608 4044 3252 280 370 -173 O ATOM 606 CG2 THR A 70 6.310 24.557 58.678 1.00 24.03 C ANISOU 606 CG2 THR A 70 3008 3559 2561 356 350 -211 C ATOM 607 N PRO A 71 4.741 27.080 55.282 1.00 27.16 N ANISOU 607 N PRO A 71 3420 3725 3174 160 346 -268 N ATOM 608 CA PRO A 71 4.656 27.608 53.910 1.00 31.65 C ANISOU 608 CA PRO A 71 3990 4226 3810 106 350 -268 C ATOM 609 C PRO A 71 5.534 26.863 52.918 1.00 22.27 C ANISOU 609 C PRO A 71 2801 3022 2639 98 361 -228 C ATOM 610 O PRO A 71 5.138 26.689 51.759 1.00 24.15 O ANISOU 610 O PRO A 71 3058 3204 2915 69 382 -201 O ATOM 611 CB PRO A 71 5.096 29.067 54.081 1.00 28.16 C ANISOU 611 CB PRO A 71 3514 3786 3399 78 313 -335 C ATOM 612 CG PRO A 71 4.658 29.416 55.452 1.00 19.65 C ANISOU 612 CG PRO A 71 2433 2756 2277 109 299 -373 C ATOM 613 CD PRO A 71 4.851 28.164 56.277 1.00 27.85 C ANISOU 613 CD PRO A 71 3481 3853 3246 165 311 -335 C ATOM 614 N LEU A 72 6.717 26.414 53.342 1.00 30.21 N ANISOU 614 N LEU A 72 3785 4079 3616 126 348 -226 N ATOM 615 CA LEU A 72 7.562 25.606 52.467 1.00 23.57 C ANISOU 615 CA LEU A 72 2943 3226 2786 125 363 -184 C ATOM 616 C LEU A 72 6.884 24.287 52.114 1.00 18.46 C ANISOU 616 C LEU A 72 2337 2553 2124 143 407 -123 C ATOM 617 O LEU A 72 6.894 23.864 50.952 1.00 30.24 O ANISOU 617 O LEU A 72 3843 3998 3648 120 428 -93 O ATOM 618 CB LEU A 72 8.915 25.354 53.134 1.00 32.13 C ANISOU 618 CB LEU A 72 3993 4378 3836 159 340 -193 C ATOM 619 CG LEU A 72 9.935 24.520 52.355 1.00 21.90 C ANISOU 619 CG LEU A 72 2692 3080 2548 165 354 -151 C ATOM 620 CD1 LEU A 72 10.630 25.348 51.289 1.00 28.84 C ANISOU 620 CD1 LEU A 72 3547 3923 3489 116 339 -173 C ATOM 621 CD2 LEU A 72 10.952 23.894 53.303 1.00 31.72 C ANISOU 621 CD2 LEU A 72 3912 4402 3737 219 342 -144 C ATOM 622 N ASN A 73 6.279 23.627 53.107 1.00 27.78 N ANISOU 622 N ASN A 73 3536 3763 3258 184 425 -105 N ATOM 623 CA ASN A 73 5.638 22.338 52.860 1.00 24.54 C ANISOU 623 CA ASN A 73 3162 3325 2837 201 472 -48 C ATOM 624 C ASN A 73 4.514 22.467 51.840 1.00 27.84 C ANISOU 624 C ASN A 73 3604 3673 3301 156 492 -43 C ATOM 625 O ASN A 73 4.378 21.624 50.945 1.00 27.47 O ANISOU 625 O ASN A 73 3577 3586 3272 146 522 -7 O ATOM 626 CB ASN A 73 5.106 21.749 54.167 1.00 24.23 C ANISOU 626 CB ASN A 73 3137 3327 2743 253 491 -31 C ATOM 627 CG ASN A 73 6.198 21.509 55.186 1.00 23.46 C ANISOU 627 CG ASN A 73 3016 3307 2592 306 473 -32 C ATOM 628 OD1 ASN A 73 6.017 21.766 56.378 1.00 26.26 O ANISOU 628 OD1 ASN A 73 3362 3715 2901 342 460 -50 O ATOM 629 ND2 ASN A 73 7.344 21.022 54.724 1.00 23.83 N ANISOU 629 ND2 ASN A 73 3049 3365 2640 314 471 -12 N ATOM 630 N TYR A 74 3.696 23.518 51.962 1.00 25.53 N ANISOU 630 N TYR A 74 3308 3367 3025 132 475 -80 N ATOM 631 CA TYR A 74 2.629 23.749 50.993 1.00 21.71 C ANISOU 631 CA TYR A 74 2843 2824 2583 92 489 -77 C ATOM 632 C TYR A 74 3.191 24.007 49.600 1.00 31.78 C ANISOU 632 C TYR A 74 4111 4062 3902 55 483 -75 C ATOM 633 O TYR A 74 2.647 23.516 48.604 1.00 31.72 O ANISOU 633 O TYR A 74 4124 4013 3917 35 506 -52 O ATOM 634 CB TYR A 74 1.756 24.925 51.434 1.00 22.60 C ANISOU 634 CB TYR A 74 2949 2933 2705 77 471 -118 C ATOM 635 CG TYR A 74 0.731 24.589 52.495 1.00 23.64 C ANISOU 635 CG TYR A 74 3097 3083 2803 106 489 -112 C ATOM 636 CD1 TYR A 74 -0.378 23.810 52.194 1.00 40.43 C ANISOU 636 CD1 TYR A 74 5249 5176 4936 102 527 -80 C ATOM 637 CD2 TYR A 74 0.859 25.066 53.793 1.00 33.63 C ANISOU 637 CD2 TYR A 74 4349 4398 4029 137 470 -141 C ATOM 638 CE1 TYR A 74 -1.323 23.505 53.158 1.00 42.57 C ANISOU 638 CE1 TYR A 74 5533 5461 5180 129 548 -72 C ATOM 639 CE2 TYR A 74 -0.082 24.763 54.763 1.00 37.71 C ANISOU 639 CE2 TYR A 74 4882 4933 4514 167 490 -133 C ATOM 640 CZ TYR A 74 -1.169 23.985 54.439 1.00 35.50 C ANISOU 640 CZ TYR A 74 4627 4616 4244 162 531 -96 C ATOM 641 OH TYR A 74 -2.103 23.690 55.404 1.00 46.51 O ANISOU 641 OH TYR A 74 6036 6027 5610 192 555 -85 O ATOM 642 N ILE A 75 4.273 24.785 49.509 1.00 18.53 N ANISOU 642 N ILE A 75 2404 2400 2236 46 453 -101 N ATOM 643 CA ILE A 75 4.826 25.148 48.207 1.00 29.44 C ANISOU 643 CA ILE A 75 3777 3747 3661 12 448 -98 C ATOM 644 C ILE A 75 5.435 23.929 47.519 1.00 25.59 C ANISOU 644 C ILE A 75 3303 3253 3168 23 473 -55 C ATOM 645 O ILE A 75 5.271 23.738 46.307 1.00 28.21 O ANISOU 645 O ILE A 75 3647 3544 3527 -1 488 -37 O ATOM 646 CB ILE A 75 5.847 26.292 48.359 1.00 32.98 C ANISOU 646 CB ILE A 75 4188 4213 4130 -1 414 -138 C ATOM 647 CG1 ILE A 75 5.146 27.587 48.777 1.00 30.51 C ANISOU 647 CG1 ILE A 75 3867 3890 3835 -19 395 -183 C ATOM 648 CG2 ILE A 75 6.609 26.523 47.063 1.00 26.91 C ANISOU 648 CG2 ILE A 75 3410 3413 3403 -28 416 -127 C ATOM 649 CD1 ILE A 75 4.177 28.125 47.746 1.00 36.26 C ANISOU 649 CD1 ILE A 75 4611 4563 4604 -51 408 -177 C ATOM 650 N LEU A 76 6.148 23.087 48.273 1.00 27.86 N ANISOU 650 N LEU A 76 3587 3580 3418 61 479 -37 N ATOM 651 CA LEU A 76 6.699 21.870 47.687 1.00 20.16 C ANISOU 651 CA LEU A 76 2626 2597 2437 75 507 6 C ATOM 652 C LEU A 76 5.605 20.876 47.322 1.00 19.46 C ANISOU 652 C LEU A 76 2574 2471 2348 74 547 36 C ATOM 653 O LEU A 76 5.734 20.157 46.325 1.00 18.26 O ANISOU 653 O LEU A 76 2438 2288 2212 64 570 61 O ATOM 654 CB LEU A 76 7.709 21.232 48.641 1.00 17.67 C ANISOU 654 CB LEU A 76 2296 2337 2079 122 505 21 C ATOM 655 CG LEU A 76 9.179 21.631 48.468 1.00 21.23 C ANISOU 655 CG LEU A 76 2711 2817 2538 123 479 9 C ATOM 656 CD1 LEU A 76 9.715 21.151 47.128 1.00 23.49 C ANISOU 656 CD1 LEU A 76 3006 3066 2854 105 498 37 C ATOM 657 CD2 LEU A 76 9.371 23.134 48.619 1.00 23.64 C ANISOU 657 CD2 LEU A 76 2984 3132 2868 94 438 -45 C ATOM 658 N LEU A 77 4.526 20.817 48.110 1.00 22.14 N ANISOU 658 N LEU A 77 2927 2814 2671 84 556 32 N ATOM 659 CA LEU A 77 3.367 20.027 47.710 1.00 23.10 C ANISOU 659 CA LEU A 77 3078 2895 2802 75 593 52 C ATOM 660 C LEU A 77 2.776 20.555 46.410 1.00 21.26 C ANISOU 660 C LEU A 77 2849 2618 2610 29 588 38 C ATOM 661 O LEU A 77 2.349 19.776 45.549 1.00 28.82 O ANISOU 661 O LEU A 77 3826 3541 3583 15 615 56 O ATOM 662 CB LEU A 77 2.316 20.033 48.821 1.00 17.09 C ANISOU 662 CB LEU A 77 2326 2147 2020 92 603 48 C ATOM 663 CG LEU A 77 0.955 19.410 48.492 1.00 27.53 C ANISOU 663 CG LEU A 77 3672 3428 3358 77 639 61 C ATOM 664 CD1 LEU A 77 1.088 17.923 48.213 1.00 19.68 C ANISOU 664 CD1 LEU A 77 2700 2414 2364 91 685 101 C ATOM 665 CD2 LEU A 77 -0.041 19.666 49.618 1.00 33.99 C ANISOU 665 CD2 LEU A 77 4493 4263 4157 93 644 52 C ATOM 666 N ASN A 78 2.739 21.880 46.254 1.00 19.64 N ANISOU 666 N ASN A 78 2625 2414 2423 6 554 6 N ATOM 667 CA ASN A 78 2.230 22.475 45.023 1.00 23.87 C ANISOU 667 CA ASN A 78 3163 2913 2995 -31 549 -4 C ATOM 668 C ASN A 78 3.095 22.091 43.830 1.00 18.15 C ANISOU 668 C ASN A 78 2439 2172 2286 -41 556 14 C ATOM 669 O ASN A 78 2.581 21.738 42.763 1.00 22.73 O ANISOU 669 O ASN A 78 3033 2721 2880 -59 571 23 O ATOM 670 CB ASN A 78 2.167 23.995 45.170 1.00 24.00 C ANISOU 670 CB ASN A 78 3158 2933 3029 -47 516 -38 C ATOM 671 CG ASN A 78 1.337 24.653 44.084 1.00 29.87 C ANISOU 671 CG ASN A 78 3906 3641 3804 -78 515 -45 C ATOM 672 OD1 ASN A 78 0.257 24.173 43.742 1.00 42.15 O ANISOU 672 OD1 ASN A 78 5478 5179 5360 -85 532 -37 O ATOM 673 ND2 ASN A 78 1.838 25.757 43.536 1.00 28.55 N ANISOU 673 ND2 ASN A 78 3720 3463 3663 -95 495 -59 N ATOM 674 N LEU A 79 4.419 22.160 43.994 1.00 20.98 N ANISOU 674 N LEU A 79 2780 2553 2638 -28 544 18 N ATOM 675 CA LEU A 79 5.325 21.814 42.904 1.00 17.04 C ANISOU 675 CA LEU A 79 2280 2040 2153 -34 552 36 C ATOM 676 C LEU A 79 5.181 20.348 42.514 1.00 16.74 C ANISOU 676 C LEU A 79 2269 1987 2103 -22 588 67 C ATOM 677 O LEU A 79 5.271 20.001 41.331 1.00 20.93 O ANISOU 677 O LEU A 79 2810 2492 2649 -37 602 77 O ATOM 678 CB LEU A 79 6.769 22.122 43.298 1.00 19.63 C ANISOU 678 CB LEU A 79 2580 2400 2477 -20 533 34 C ATOM 679 CG LEU A 79 7.147 23.587 43.509 1.00 17.74 C ANISOU 679 CG LEU A 79 2310 2171 2260 -37 499 -1 C ATOM 680 CD1 LEU A 79 8.542 23.700 44.110 1.00 24.80 C ANISOU 680 CD1 LEU A 79 3172 3104 3146 -20 481 -7 C ATOM 681 CD2 LEU A 79 7.066 24.338 42.202 1.00 26.02 C ANISOU 681 CD2 LEU A 79 3357 3182 3348 -69 498 -2 C ATOM 682 N ALA A 80 4.963 19.473 43.498 1.00 17.68 N ANISOU 682 N ALA A 80 2400 2120 2196 5 608 81 N ATOM 683 CA ALA A 80 4.807 18.051 43.208 1.00 16.42 C ANISOU 683 CA ALA A 80 2267 1940 2031 17 649 109 C ATOM 684 C ALA A 80 3.607 17.805 42.303 1.00 21.83 C ANISOU 684 C ALA A 80 2971 2586 2738 -13 666 102 C ATOM 685 O ALA A 80 3.700 17.072 41.310 1.00 20.28 O ANISOU 685 O ALA A 80 2790 2364 2553 -23 688 112 O ATOM 686 CB ALA A 80 4.672 17.263 44.511 1.00 19.67 C ANISOU 686 CB ALA A 80 2687 2373 2414 55 671 128 C ATOM 687 N VAL A 81 2.470 18.426 42.624 1.00 16.15 N ANISOU 687 N VAL A 81 2249 1863 2023 -28 655 81 N ATOM 688 CA VAL A 81 1.292 18.315 41.769 1.00 18.83 C ANISOU 688 CA VAL A 81 2601 2172 2383 -58 665 69 C ATOM 689 C VAL A 81 1.580 18.907 40.396 1.00 19.78 C ANISOU 689 C VAL A 81 2715 2281 2521 -81 648 60 C ATOM 690 O VAL A 81 1.248 18.316 39.362 1.00 20.69 O ANISOU 690 O VAL A 81 2843 2374 2646 -96 664 60 O ATOM 691 CB VAL A 81 0.082 18.999 42.430 1.00 19.45 C ANISOU 691 CB VAL A 81 2674 2254 2462 -66 654 49 C ATOM 692 CG1 VAL A 81 -1.117 18.964 41.500 1.00 22.94 C ANISOU 692 CG1 VAL A 81 3121 2671 2924 -95 660 34 C ATOM 693 CG2 VAL A 81 -0.247 18.336 43.753 1.00 21.67 C ANISOU 693 CG2 VAL A 81 2963 2547 2724 -39 677 62 C ATOM 694 N ALA A 82 2.205 20.086 40.369 1.00 18.89 N ANISOU 694 N ALA A 82 2582 2182 2413 -84 616 51 N ATOM 695 CA ALA A 82 2.546 20.716 39.100 1.00 23.65 C ANISOU 695 CA ALA A 82 3178 2775 3033 -101 603 48 C ATOM 696 C ALA A 82 3.515 19.855 38.299 1.00 22.77 C ANISOU 696 C ALA A 82 3076 2656 2919 -94 622 69 C ATOM 697 O ALA A 82 3.383 19.736 37.075 1.00 16.21 O ANISOU 697 O ALA A 82 2252 1810 2096 -107 628 70 O ATOM 698 CB ALA A 82 3.133 22.104 39.347 1.00 17.40 C ANISOU 698 CB ALA A 82 2362 1996 2254 -104 573 37 C ATOM 699 N ASP A 83 4.499 19.248 38.970 1.00 15.84 N ANISOU 699 N ASP A 83 2197 1793 2029 -71 631 86 N ATOM 700 CA ASP A 83 5.414 18.347 38.276 1.00 19.14 C ANISOU 700 CA ASP A 83 2624 2204 2444 -60 653 107 C ATOM 701 C ASP A 83 4.674 17.144 37.704 1.00 23.66 C ANISOU 701 C ASP A 83 3224 2750 3017 -66 686 110 C ATOM 702 O ASP A 83 4.970 16.696 36.591 1.00 18.66 O ANISOU 702 O ASP A 83 2600 2102 2388 -72 699 114 O ATOM 703 CB ASP A 83 6.525 17.881 39.215 1.00 22.14 C ANISOU 703 CB ASP A 83 2997 2609 2809 -29 658 126 C ATOM 704 CG ASP A 83 7.473 18.996 39.600 1.00 16.80 C ANISOU 704 CG ASP A 83 2288 1960 2136 -26 625 119 C ATOM 705 OD1 ASP A 83 7.519 20.017 38.888 1.00 17.01 O ANISOU 705 OD1 ASP A 83 2301 1978 2183 -48 606 106 O ATOM 706 OD2 ASP A 83 8.180 18.848 40.619 1.00 29.63 O ANISOU 706 OD2 ASP A 83 3899 3615 3744 0 620 125 O ATOM 707 N LEU A 84 3.713 16.602 38.457 1.00 16.96 N ANISOU 707 N LEU A 84 2386 1894 2163 -64 702 105 N ATOM 708 CA LEU A 84 2.953 15.455 37.971 1.00 18.29 C ANISOU 708 CA LEU A 84 2577 2033 2338 -74 737 103 C ATOM 709 C LEU A 84 2.158 15.811 36.721 1.00 26.81 C ANISOU 709 C LEU A 84 3657 3100 3430 -104 726 78 C ATOM 710 O LEU A 84 2.004 14.980 35.818 1.00 18.32 O ANISOU 710 O LEU A 84 2596 2005 2360 -114 748 72 O ATOM 711 CB LEU A 84 2.034 14.926 39.073 1.00 25.19 C ANISOU 711 CB LEU A 84 3459 2901 3210 -68 758 103 C ATOM 712 CG LEU A 84 2.737 14.159 40.195 1.00 30.70 C ANISOU 712 CG LEU A 84 4163 3609 3892 -31 783 134 C ATOM 713 CD1 LEU A 84 1.774 13.844 41.327 1.00 29.23 C ANISOU 713 CD1 LEU A 84 3983 3421 3703 -22 802 136 C ATOM 714 CD2 LEU A 84 3.347 12.884 39.645 1.00 24.45 C ANISOU 714 CD2 LEU A 84 3391 2793 3105 -20 823 153 C ATOM 715 N PHE A 85 1.647 17.043 36.648 1.00 23.08 N ANISOU 715 N PHE A 85 3169 2641 2962 -118 693 62 N ATOM 716 CA PHE A 85 0.992 17.496 35.424 1.00 30.88 C ANISOU 716 CA PHE A 85 4154 3624 3956 -139 680 44 C ATOM 717 C PHE A 85 1.973 17.559 34.260 1.00 31.74 C ANISOU 717 C PHE A 85 4264 3734 4063 -136 678 54 C ATOM 718 O PHE A 85 1.618 17.235 33.120 1.00 22.60 O ANISOU 718 O PHE A 85 3114 2570 2904 -146 684 42 O ATOM 719 CB PHE A 85 0.338 18.859 35.646 1.00 31.90 C ANISOU 719 CB PHE A 85 4265 3766 4090 -148 648 31 C ATOM 720 CG PHE A 85 -1.050 18.782 36.213 1.00 27.31 C ANISOU 720 CG PHE A 85 3683 3182 3512 -159 651 13 C ATOM 721 CD1 PHE A 85 -2.105 18.326 35.441 1.00 33.05 C ANISOU 721 CD1 PHE A 85 4413 3900 4243 -177 659 -6 C ATOM 722 CD2 PHE A 85 -1.303 19.182 37.512 1.00 31.86 C ANISOU 722 CD2 PHE A 85 4253 3767 4086 -150 645 14 C ATOM 723 CE1 PHE A 85 -3.384 18.258 35.962 1.00 35.28 C ANISOU 723 CE1 PHE A 85 4691 4181 4532 -188 662 -23 C ATOM 724 CE2 PHE A 85 -2.580 19.119 38.036 1.00 34.70 C ANISOU 724 CE2 PHE A 85 4611 4124 4450 -159 650 0 C ATOM 725 CZ PHE A 85 -3.621 18.659 37.260 1.00 31.04 C ANISOU 725 CZ PHE A 85 4150 3650 3995 -179 660 -18 C ATOM 726 N MET A 86 3.209 17.991 34.522 1.00 25.80 N ANISOU 726 N MET A 86 3502 2992 3309 -120 670 74 N ATOM 727 CA MET A 86 4.223 18.005 33.473 1.00 19.77 C ANISOU 727 CA MET A 86 2738 2228 2544 -114 673 88 C ATOM 728 C MET A 86 4.515 16.598 32.969 1.00 21.15 C ANISOU 728 C MET A 86 2935 2388 2712 -108 706 93 C ATOM 729 O MET A 86 4.627 16.375 31.758 1.00 29.25 O ANISOU 729 O MET A 86 3970 3410 3736 -111 713 90 O ATOM 730 CB MET A 86 5.508 18.652 33.986 1.00 15.71 C ANISOU 730 CB MET A 86 2206 1729 2035 -100 661 106 C ATOM 731 CG MET A 86 5.351 20.085 34.457 1.00 17.75 C ANISOU 731 CG MET A 86 2441 1997 2305 -108 631 97 C ATOM 732 SD MET A 86 6.912 20.787 35.038 1.00 22.66 S ANISOU 732 SD MET A 86 3035 2635 2938 -96 617 111 S ATOM 733 CE MET A 86 7.874 20.796 33.522 1.00 22.92 C ANISOU 733 CE MET A 86 3069 2662 2980 -94 629 132 C ATOM 734 N VAL A 87 4.643 15.638 33.886 1.00 18.75 N ANISOU 734 N VAL A 87 2641 2076 2406 -96 729 102 N ATOM 735 CA VAL A 87 5.039 14.284 33.511 1.00 22.45 C ANISOU 735 CA VAL A 87 3132 2526 2873 -86 766 110 C ATOM 736 C VAL A 87 3.955 13.616 32.675 1.00 26.67 C ANISOU 736 C VAL A 87 3681 3039 3412 -108 782 81 C ATOM 737 O VAL A 87 4.230 13.043 31.614 1.00 26.30 O ANISOU 737 O VAL A 87 3646 2982 3363 -109 797 75 O ATOM 738 CB VAL A 87 5.364 13.459 34.768 1.00 28.28 C ANISOU 738 CB VAL A 87 3877 3261 3609 -63 792 131 C ATOM 739 CG1 VAL A 87 5.598 12.006 34.399 1.00 28.39 C ANISOU 739 CG1 VAL A 87 3916 3247 3626 -54 837 138 C ATOM 740 CG2 VAL A 87 6.573 14.039 35.473 1.00 34.49 C ANISOU 740 CG2 VAL A 87 4643 4074 4386 -39 774 155 C ATOM 741 N PHE A 88 2.707 13.683 33.135 1.00 31.24 N ANISOU 741 N PHE A 88 4258 3614 3998 -125 778 60 N ATOM 742 CA PHE A 88 1.622 12.976 32.466 1.00 24.93 C ANISOU 742 CA PHE A 88 3468 2796 3207 -148 794 28 C ATOM 743 C PHE A 88 0.955 13.812 31.383 1.00 22.13 C ANISOU 743 C PHE A 88 3103 2461 2846 -165 763 2 C ATOM 744 O PHE A 88 0.540 13.269 30.353 1.00 21.52 O ANISOU 744 O PHE A 88 3031 2377 2766 -178 771 -24 O ATOM 745 CB PHE A 88 0.583 12.518 33.492 1.00 31.20 C ANISOU 745 CB PHE A 88 4264 3576 4015 -157 811 19 C ATOM 746 CG PHE A 88 1.062 11.406 34.376 1.00 30.94 C ANISOU 746 CG PHE A 88 4247 3520 3988 -138 854 43 C ATOM 747 CD1 PHE A 88 1.354 10.164 33.842 1.00 38.76 C ANISOU 747 CD1 PHE A 88 5258 4480 4989 -137 894 40 C ATOM 748 CD2 PHE A 88 1.223 11.600 35.738 1.00 27.32 C ANISOU 748 CD2 PHE A 88 3784 3070 3525 -117 856 68 C ATOM 749 CE1 PHE A 88 1.798 9.133 34.645 1.00 51.18 C ANISOU 749 CE1 PHE A 88 6847 6030 6570 -114 938 67 C ATOM 750 CE2 PHE A 88 1.666 10.571 36.550 1.00 37.51 C ANISOU 750 CE2 PHE A 88 5090 4344 4818 -92 897 96 C ATOM 751 CZ PHE A 88 1.953 9.336 36.001 1.00 41.16 C ANISOU 751 CZ PHE A 88 5573 4773 5293 -91 940 98 C ATOM 752 N GLY A 89 0.824 15.122 31.593 1.00 16.62 N ANISOU 752 N GLY A 89 2386 1784 2144 -165 728 8 N ATOM 753 CA GLY A 89 0.227 15.957 30.566 1.00 30.92 C ANISOU 753 CA GLY A 89 4186 3614 3947 -175 702 -9 C ATOM 754 C GLY A 89 1.155 16.170 29.384 1.00 27.11 C ANISOU 754 C GLY A 89 3706 3142 3451 -162 698 3 C ATOM 755 O GLY A 89 0.736 16.086 28.224 1.00 33.02 O ANISOU 755 O GLY A 89 4457 3901 4188 -167 694 -16 O ATOM 756 N GLY A 90 2.422 16.464 29.663 1.00 28.75 N ANISOU 756 N GLY A 90 3914 3350 3661 -145 700 35 N ATOM 757 CA GLY A 90 3.351 16.842 28.618 1.00 18.58 C ANISOU 757 CA GLY A 90 2624 2071 2363 -132 698 52 C ATOM 758 C GLY A 90 4.398 15.815 28.240 1.00 18.22 C ANISOU 758 C GLY A 90 2596 2015 2314 -119 726 64 C ATOM 759 O GLY A 90 4.600 15.550 27.051 1.00 23.38 O ANISOU 759 O GLY A 90 3257 2672 2953 -114 734 59 O ATOM 760 N PHE A 91 5.060 15.213 29.232 1.00 16.49 N ANISOU 760 N PHE A 91 2380 1782 2102 -109 743 81 N ATOM 761 CA PHE A 91 6.212 14.364 28.939 1.00 16.24 C ANISOU 761 CA PHE A 91 2361 1742 2067 -91 771 100 C ATOM 762 C PHE A 91 5.822 13.071 28.239 1.00 16.45 C ANISOU 762 C PHE A 91 2411 1748 2089 -96 801 77 C ATOM 763 O PHE A 91 6.655 12.492 27.533 1.00 20.94 O ANISOU 763 O PHE A 91 2993 2313 2652 -82 822 86 O ATOM 764 CB PHE A 91 6.987 14.042 30.217 1.00 16.23 C ANISOU 764 CB PHE A 91 2356 1737 2074 -74 782 125 C ATOM 765 CG PHE A 91 7.802 15.190 30.742 1.00 16.12 C ANISOU 765 CG PHE A 91 2316 1744 2064 -66 756 146 C ATOM 766 CD1 PHE A 91 7.759 16.433 30.132 1.00 20.36 C ANISOU 766 CD1 PHE A 91 2838 2295 2605 -75 730 145 C ATOM 767 CD2 PHE A 91 8.618 15.019 31.846 1.00 29.62 C ANISOU 767 CD2 PHE A 91 4017 3462 3776 -47 760 167 C ATOM 768 CE1 PHE A 91 8.512 17.484 30.617 1.00 27.59 C ANISOU 768 CE1 PHE A 91 3727 3224 3532 -70 710 160 C ATOM 769 CE2 PHE A 91 9.375 16.065 32.336 1.00 16.12 C ANISOU 769 CE2 PHE A 91 2279 1773 2072 -42 735 179 C ATOM 770 CZ PHE A 91 9.320 17.301 31.721 1.00 19.51 C ANISOU 770 CZ PHE A 91 2692 2209 2512 -56 711 174 C ATOM 771 N THR A 92 4.589 12.601 28.425 1.00 19.06 N ANISOU 771 N THR A 92 2748 2067 2426 -116 805 45 N ATOM 772 CA THR A 92 4.124 11.437 27.679 1.00 23.78 C ANISOU 772 CA THR A 92 3365 2646 3024 -127 832 13 C ATOM 773 C THR A 92 4.089 11.727 26.183 1.00 18.86 C ANISOU 773 C THR A 92 2742 2043 2380 -128 819 -6 C ATOM 774 O THR A 92 4.448 10.870 25.365 1.00 17.09 O ANISOU 774 O THR A 92 2536 1809 2150 -122 843 -18 O ATOM 775 CB THR A 92 2.747 11.008 28.185 1.00 33.71 C ANISOU 775 CB THR A 92 4623 3890 4297 -152 837 -20 C ATOM 776 OG1 THR A 92 1.864 12.137 28.184 1.00 20.78 O ANISOU 776 OG1 THR A 92 2964 2277 2654 -165 799 -32 O ATOM 777 CG2 THR A 92 2.848 10.457 29.601 1.00 24.01 C ANISOU 777 CG2 THR A 92 3399 2638 3086 -145 862 2 C ATOM 778 N THR A 93 3.655 12.932 25.805 1.00 22.21 N ANISOU 778 N THR A 93 3148 2496 2793 -131 783 -7 N ATOM 779 CA THR A 93 3.705 13.329 24.401 1.00 17.18 C ANISOU 779 CA THR A 93 2511 1885 2131 -123 771 -16 C ATOM 780 C THR A 93 5.144 13.485 23.921 1.00 24.87 C ANISOU 780 C THR A 93 3490 2863 3097 -97 782 22 C ATOM 781 O THR A 93 5.474 13.080 22.801 1.00 28.24 O ANISOU 781 O THR A 93 3929 3298 3505 -86 794 13 O ATOM 782 CB THR A 93 2.916 14.623 24.194 1.00 22.42 C ANISOU 782 CB THR A 93 3154 2578 2786 -128 734 -18 C ATOM 783 OG1 THR A 93 1.519 14.357 24.366 1.00 17.89 O ANISOU 783 OG1 THR A 93 2574 2006 2216 -151 725 -59 O ATOM 784 CG2 THR A 93 3.144 15.184 22.796 1.00 20.52 C ANISOU 784 CG2 THR A 93 2912 2368 2518 -110 724 -14 C ATOM 785 N THR A 94 6.014 14.065 24.754 1.00 24.09 N ANISOU 785 N THR A 94 3380 2760 3013 -87 779 61 N ATOM 786 CA THR A 94 7.416 14.216 24.377 1.00 16.69 C ANISOU 786 CA THR A 94 2442 1826 2073 -64 791 96 C ATOM 787 C THR A 94 8.031 12.868 24.030 1.00 19.96 C ANISOU 787 C THR A 94 2879 2222 2482 -53 827 93 C ATOM 788 O THR A 94 8.729 12.729 23.019 1.00 23.79 O ANISOU 788 O THR A 94 3372 2714 2952 -36 840 102 O ATOM 789 CB THR A 94 8.210 14.870 25.509 1.00 25.12 C ANISOU 789 CB THR A 94 3492 2892 3161 -58 782 130 C ATOM 790 OG1 THR A 94 7.418 15.887 26.132 1.00 16.33 O ANISOU 790 OG1 THR A 94 2360 1787 2056 -73 753 124 O ATOM 791 CG2 THR A 94 9.489 15.490 24.961 1.00 25.26 C ANISOU 791 CG2 THR A 94 3498 2920 3179 -38 785 165 C ATOM 792 N LEU A 95 7.774 11.859 24.865 1.00 17.62 N ANISOU 792 N LEU A 95 2595 1900 2200 -60 848 82 N ATOM 793 CA LEU A 95 8.329 10.531 24.634 1.00 17.57 C ANISOU 793 CA LEU A 95 2612 1869 2194 -48 888 79 C ATOM 794 C LEU A 95 7.801 9.930 23.339 1.00 25.23 C ANISOU 794 C LEU A 95 3599 2839 3148 -55 898 38 C ATOM 795 O LEU A 95 8.578 9.489 22.484 1.00 22.10 O ANISOU 795 O LEU A 95 3215 2442 2738 -37 919 44 O ATOM 796 CB LEU A 95 8.004 9.618 25.815 1.00 23.80 C ANISOU 796 CB LEU A 95 3410 2628 3005 -54 912 77 C ATOM 797 CG LEU A 95 8.355 8.148 25.596 1.00 26.47 C ANISOU 797 CG LEU A 95 3775 2932 3350 -44 960 70 C ATOM 798 CD1 LEU A 95 9.839 7.991 25.312 1.00 17.59 C ANISOU 798 CD1 LEU A 95 2654 1812 2218 -12 978 108 C ATOM 799 CD2 LEU A 95 7.949 7.316 26.792 1.00 22.81 C ANISOU 799 CD2 LEU A 95 3320 2437 2909 -48 988 72 C ATOM 800 N TYR A 96 6.477 9.916 23.173 1.00 19.89 N ANISOU 800 N TYR A 96 2921 2166 2470 -81 884 -5 N ATOM 801 CA TYR A 96 5.881 9.324 21.980 1.00 24.79 C ANISOU 801 CA TYR A 96 3554 2793 3074 -90 890 -54 C ATOM 802 C TYR A 96 6.344 10.048 20.723 1.00 30.40 C ANISOU 802 C TYR A 96 4260 3541 3751 -69 873 -44 C ATOM 803 O TYR A 96 6.644 9.414 19.704 1.00 21.11 O ANISOU 803 O TYR A 96 3099 2366 2554 -58 891 -64 O ATOM 804 CB TYR A 96 4.358 9.356 22.100 1.00 29.30 C ANISOU 804 CB TYR A 96 4114 3368 3650 -121 870 -101 C ATOM 805 CG TYR A 96 3.635 8.554 21.046 1.00 48.73 C ANISOU 805 CG TYR A 96 6584 5833 6099 -135 878 -162 C ATOM 806 CD1 TYR A 96 3.493 7.178 21.172 1.00 31.94 C ANISOU 806 CD1 TYR A 96 4475 3664 3995 -149 918 -196 C ATOM 807 CD2 TYR A 96 3.088 9.171 19.927 1.00 43.11 C ANISOU 807 CD2 TYR A 96 5861 5167 5353 -133 847 -189 C ATOM 808 CE1 TYR A 96 2.831 6.438 20.213 1.00 44.97 C ANISOU 808 CE1 TYR A 96 6132 5318 5638 -166 925 -260 C ATOM 809 CE2 TYR A 96 2.424 8.441 18.962 1.00 50.20 C ANISOU 809 CE2 TYR A 96 6763 6075 6236 -145 850 -252 C ATOM 810 CZ TYR A 96 2.300 7.075 19.110 1.00 41.30 C ANISOU 810 CZ TYR A 96 5653 4905 5135 -164 888 -290 C ATOM 811 OH TYR A 96 1.637 6.345 18.151 1.00 62.73 O ANISOU 811 OH TYR A 96 8369 7629 7837 -180 891 -361 O ATOM 812 N THR A 97 6.409 11.379 20.781 1.00 26.40 N ANISOU 812 N THR A 97 3732 3060 3236 -62 842 -14 N ATOM 813 CA THR A 97 6.909 12.161 19.656 1.00 23.55 C ANISOU 813 CA THR A 97 3368 2734 2848 -39 831 5 C ATOM 814 C THR A 97 8.359 11.813 19.340 1.00 26.83 C ANISOU 814 C THR A 97 3794 3139 3261 -12 860 40 C ATOM 815 O THR A 97 8.720 11.592 18.177 1.00 19.50 O ANISOU 815 O THR A 97 2877 2228 2305 7 872 35 O ATOM 816 CB THR A 97 6.767 13.652 19.970 1.00 28.81 C ANISOU 816 CB THR A 97 4009 3420 3518 -37 800 36 C ATOM 817 OG1 THR A 97 5.378 13.993 20.068 1.00 22.48 O ANISOU 817 OG1 THR A 97 3198 2633 2712 -57 773 3 O ATOM 818 CG2 THR A 97 7.427 14.504 18.899 1.00 25.04 C ANISOU 818 CG2 THR A 97 3526 2970 3016 -9 797 68 C ATOM 819 N ASER A 98 9.209 11.756 20.369 0.66 26.06 N ANISOU 819 N ASER A 98 3692 3019 3190 -8 872 76 N ATOM 820 N BSER A 98 9.206 11.748 20.371 0.34 26.07 N ANISOU 820 N BSER A 98 3693 3020 3192 -8 872 76 N ATOM 821 CA ASER A 98 10.625 11.478 20.155 0.66 24.20 C ANISOU 821 CA ASER A 98 3462 2778 2957 18 899 113 C ATOM 822 CA BSER A 98 10.622 11.474 20.152 0.34 23.85 C ANISOU 822 CA BSER A 98 3418 2733 2912 18 899 113 C ATOM 823 C ASER A 98 10.874 10.048 19.697 0.66 23.01 C ANISOU 823 C ASER A 98 3339 2606 2799 26 937 90 C ATOM 824 C BSER A 98 10.856 10.053 19.659 0.34 22.56 C ANISOU 824 C BSER A 98 3282 2549 2740 26 936 89 C ATOM 825 O ASER A 98 11.917 9.777 19.092 0.66 22.43 O ANISOU 825 O ASER A 98 3274 2534 2716 51 960 112 O ATOM 826 O BSER A 98 11.864 9.789 18.995 0.34 22.50 O ANISOU 826 O BSER A 98 3283 2544 2723 51 959 110 O ATOM 827 CB ASER A 98 11.415 11.760 21.433 0.66 22.15 C ANISOU 827 CB ASER A 98 3186 2506 2726 21 899 153 C ATOM 828 CB BSER A 98 11.406 11.724 21.439 0.34 22.02 C ANISOU 828 CB BSER A 98 3169 2487 2708 21 900 152 C ATOM 829 OG ASER A 98 11.298 13.121 21.811 0.66 17.23 O ANISOU 829 OG ASER A 98 2536 1900 2112 14 867 172 O ATOM 830 OG BSER A 98 10.897 10.937 22.501 0.34 20.23 O ANISOU 830 OG BSER A 98 2951 2236 2500 6 909 135 O ATOM 831 N LEU A 99 9.952 9.127 19.982 1.00 29.43 N ANISOU 831 N LEU A 99 4167 3397 3620 4 946 46 N ATOM 832 CA LEU A 99 10.083 7.765 19.477 1.00 23.86 C ANISOU 832 CA LEU A 99 3488 2665 2912 8 984 17 C ATOM 833 C LEU A 99 9.920 7.721 17.962 1.00 29.08 C ANISOU 833 C LEU A 99 4159 3353 3536 17 982 -16 C ATOM 834 O LEU A 99 10.653 7.002 17.273 1.00 19.02 O ANISOU 834 O LEU A 99 2904 2071 2251 38 1013 -17 O ATOM 835 CB LEU A 99 9.063 6.855 20.160 1.00 23.56 C ANISOU 835 CB LEU A 99 3460 2594 2899 -20 998 -25 C ATOM 836 CG LEU A 99 9.298 6.562 21.643 1.00 31.65 C ANISOU 836 CG LEU A 99 4482 3588 3956 -21 1013 7 C ATOM 837 CD1 LEU A 99 8.036 6.016 22.281 1.00 22.10 C ANISOU 837 CD1 LEU A 99 3274 2352 2769 -53 1018 -33 C ATOM 838 CD2 LEU A 99 10.447 5.589 21.813 1.00 18.53 C ANISOU 838 CD2 LEU A 99 2839 1898 2306 6 1059 35 C ATOM 839 N HIS A 100 8.967 8.484 17.426 1.00 30.70 N ANISOU 839 N HIS A 100 4352 3594 3720 6 946 -41 N ATOM 840 CA HIS A 100 8.682 8.483 15.997 1.00 27.74 C ANISOU 840 CA HIS A 100 3984 3254 3303 17 940 -75 C ATOM 841 C HIS A 100 9.405 9.582 15.231 1.00 21.22 C ANISOU 841 C HIS A 100 3147 2466 2449 50 928 -29 C ATOM 842 O HIS A 100 9.352 9.590 13.997 1.00 31.17 O ANISOU 842 O HIS A 100 4414 3760 3668 69 926 -47 O ATOM 843 CB HIS A 100 7.174 8.616 15.762 1.00 28.68 C ANISOU 843 CB HIS A 100 4092 3395 3411 -9 909 -132 C ATOM 844 CG HIS A 100 6.377 7.477 16.312 1.00 30.34 C ANISOU 844 CG HIS A 100 4310 3567 3649 -43 925 -185 C ATOM 845 ND1 HIS A 100 6.279 6.261 15.671 1.00 24.64 N ANISOU 845 ND1 HIS A 100 3609 2829 2924 -48 953 -239 N ATOM 846 CD2 HIS A 100 5.647 7.364 17.447 1.00 23.29 C ANISOU 846 CD2 HIS A 100 3408 2647 2792 -72 921 -193 C ATOM 847 CE1 HIS A 100 5.521 5.449 16.385 1.00 24.64 C ANISOU 847 CE1 HIS A 100 3611 2790 2961 -81 968 -277 C ATOM 848 NE2 HIS A 100 5.124 6.094 17.467 1.00 29.52 N ANISOU 848 NE2 HIS A 100 4211 3402 3602 -96 949 -248 N ATOM 849 N GLY A 101 10.067 10.507 15.922 1.00 21.22 N ANISOU 849 N GLY A 101 3130 2464 2470 57 920 29 N ATOM 850 CA GLY A 101 10.785 11.573 15.258 1.00 29.16 C ANISOU 850 CA GLY A 101 4123 3498 3457 85 914 76 C ATOM 851 C GLY A 101 9.935 12.701 14.721 1.00 25.78 C ANISOU 851 C GLY A 101 3680 3110 3005 87 881 74 C ATOM 852 O GLY A 101 10.426 13.487 13.904 1.00 25.58 O ANISOU 852 O GLY A 101 3648 3111 2958 116 882 109 O ATOM 853 N TYR A 102 8.672 12.795 15.135 1.00 34.51 N ANISOU 853 N TYR A 102 4777 4220 4114 60 854 37 N ATOM 854 CA TYR A 102 7.815 13.922 14.783 1.00 22.22 C ANISOU 854 CA TYR A 102 3203 2699 2539 64 821 39 C ATOM 855 C TYR A 102 6.576 13.864 15.665 1.00 27.87 C ANISOU 855 C TYR A 102 3908 3406 3274 28 797 2 C ATOM 856 O TYR A 102 6.348 12.889 16.385 1.00 24.89 O ANISOU 856 O TYR A 102 3540 2997 2921 3 808 -28 O ATOM 857 CB TYR A 102 7.433 13.920 13.298 1.00 29.79 C ANISOU 857 CB TYR A 102 4170 3708 3443 90 816 15 C ATOM 858 CG TYR A 102 6.429 12.863 12.904 1.00 31.53 C ANISOU 858 CG TYR A 102 4399 3939 3641 72 809 -61 C ATOM 859 CD1 TYR A 102 6.813 11.536 12.761 1.00 19.51 C ANISOU 859 CD1 TYR A 102 2899 2392 2122 66 838 -95 C ATOM 860 CD2 TYR A 102 5.099 13.194 12.666 1.00 25.46 C ANISOU 860 CD2 TYR A 102 3615 3206 2852 62 776 -100 C ATOM 861 CE1 TYR A 102 5.903 10.566 12.397 1.00 24.54 C ANISOU 861 CE1 TYR A 102 3543 3036 2746 47 834 -170 C ATOM 862 CE2 TYR A 102 4.179 12.232 12.302 1.00 28.29 C ANISOU 862 CE2 TYR A 102 3978 3577 3195 43 769 -175 C ATOM 863 CZ TYR A 102 4.586 10.919 12.169 1.00 38.42 C ANISOU 863 CZ TYR A 102 5283 4831 4485 33 799 -211 C ATOM 864 OH TYR A 102 3.672 9.957 11.807 1.00 42.27 O ANISOU 864 OH TYR A 102 5772 5326 4962 10 794 -292 O ATOM 865 N PHE A 103 5.778 14.930 15.600 1.00 25.25 N ANISOU 865 N PHE A 103 3558 3102 2934 29 767 7 N ATOM 866 CA PHE A 103 4.544 15.032 16.379 1.00 27.99 C ANISOU 866 CA PHE A 103 3892 3445 3298 -2 742 -24 C ATOM 867 C PHE A 103 3.450 14.268 15.648 1.00 22.43 C ANISOU 867 C PHE A 103 3191 2768 2563 -11 732 -91 C ATOM 868 O PHE A 103 2.712 14.818 14.831 1.00 30.91 O ANISOU 868 O PHE A 103 4253 3889 3601 3 708 -105 O ATOM 869 CB PHE A 103 4.162 16.490 16.599 1.00 28.33 C ANISOU 869 CB PHE A 103 3914 3506 3345 5 718 9 C ATOM 870 CG PHE A 103 4.822 17.107 17.792 1.00 21.58 C ANISOU 870 CG PHE A 103 3049 2615 2534 -4 721 52 C ATOM 871 CD1 PHE A 103 4.273 16.952 19.053 1.00 23.26 C ANISOU 871 CD1 PHE A 103 3256 2803 2779 -34 712 36 C ATOM 872 CD2 PHE A 103 5.992 17.833 17.659 1.00 22.12 C ANISOU 872 CD2 PHE A 103 3114 2677 2612 17 735 105 C ATOM 873 CE1 PHE A 103 4.871 17.513 20.160 1.00 18.59 C ANISOU 873 CE1 PHE A 103 2655 2185 2223 -41 713 70 C ATOM 874 CE2 PHE A 103 6.600 18.397 18.764 1.00 23.16 C ANISOU 874 CE2 PHE A 103 3234 2781 2786 6 736 136 C ATOM 875 CZ PHE A 103 6.038 18.235 20.018 1.00 26.03 C ANISOU 875 CZ PHE A 103 3591 3124 3175 -22 723 117 C ATOM 876 N VAL A 104 3.359 12.969 15.946 1.00 30.31 N ANISOU 876 N VAL A 104 4203 3736 3577 -35 751 -133 N ATOM 877 CA VAL A 104 2.310 12.137 15.361 1.00 31.63 C ANISOU 877 CA VAL A 104 4370 3922 3726 -52 743 -206 C ATOM 878 C VAL A 104 0.936 12.661 15.760 1.00 33.46 C ANISOU 878 C VAL A 104 4577 4173 3963 -73 710 -231 C ATOM 879 O VAL A 104 -0.007 12.649 14.960 1.00 28.63 O ANISOU 879 O VAL A 104 3952 3606 3319 -73 688 -278 O ATOM 880 CB VAL A 104 2.502 10.667 15.779 1.00 37.79 C ANISOU 880 CB VAL A 104 5170 4653 4535 -76 777 -242 C ATOM 881 CG1 VAL A 104 1.549 9.763 15.012 1.00 28.95 C ANISOU 881 CG1 VAL A 104 4050 3552 3398 -94 774 -324 C ATOM 882 CG2 VAL A 104 3.940 10.236 15.563 1.00 38.14 C ANISOU 882 CG2 VAL A 104 5238 4675 4580 -52 812 -207 C ATOM 883 N PHE A 105 0.805 13.138 17.001 1.00 37.80 N ANISOU 883 N PHE A 105 5118 4694 4551 -90 706 -202 N ATOM 884 CA PHE A 105 -0.447 13.708 17.492 1.00 34.40 C ANISOU 884 CA PHE A 105 4663 4278 4129 -108 677 -219 C ATOM 885 C PHE A 105 -0.796 15.038 16.836 1.00 35.12 C ANISOU 885 C PHE A 105 4736 4421 4187 -81 647 -195 C ATOM 886 O PHE A 105 -1.870 15.579 17.124 1.00 37.79 O ANISOU 886 O PHE A 105 5053 4778 4528 -91 622 -208 O ATOM 887 CB PHE A 105 -0.387 13.907 19.008 1.00 38.06 C ANISOU 887 CB PHE A 105 5123 4697 4639 -128 684 -191 C ATOM 888 CG PHE A 105 -0.195 12.639 19.791 1.00 49.24 C ANISOU 888 CG PHE A 105 6555 6063 6090 -153 716 -210 C ATOM 889 CD1 PHE A 105 -0.576 11.413 19.270 1.00 51.36 C ANISOU 889 CD1 PHE A 105 6833 6325 6358 -169 733 -267 C ATOM 890 CD2 PHE A 105 0.360 12.680 21.061 1.00 46.08 C ANISOU 890 CD2 PHE A 105 6161 5625 5724 -157 731 -172 C ATOM 891 CE1 PHE A 105 -0.398 10.252 19.998 1.00 48.51 C ANISOU 891 CE1 PHE A 105 6487 5911 6032 -190 769 -281 C ATOM 892 CE2 PHE A 105 0.540 11.524 21.794 1.00 54.82 C ANISOU 892 CE2 PHE A 105 7282 6686 6860 -173 764 -183 C ATOM 893 CZ PHE A 105 0.159 10.308 21.263 1.00 58.99 C ANISOU 893 CZ PHE A 105 7822 7202 7392 -189 786 -235 C ATOM 894 N GLY A 106 0.074 15.586 15.991 1.00 34.57 N ANISOU 894 N GLY A 106 4674 4372 4088 -44 651 -156 N ATOM 895 CA GLY A 106 -0.189 16.845 15.339 1.00 18.87 C ANISOU 895 CA GLY A 106 2670 2429 2069 -12 630 -124 C ATOM 896 C GLY A 106 -0.134 18.016 16.299 1.00 35.56 C ANISOU 896 C GLY A 106 4772 4522 4218 -14 623 -75 C ATOM 897 O GLY A 106 0.422 17.924 17.399 1.00 17.95 O ANISOU 897 O GLY A 106 2547 2244 2029 -33 636 -55 O ATOM 898 N PRO A 107 -0.717 19.148 15.895 1.00 26.90 N ANISOU 898 N PRO A 107 3659 3461 3102 9 603 -54 N ATOM 899 CA PRO A 107 -0.656 20.352 16.740 1.00 18.07 C ANISOU 899 CA PRO A 107 2529 2321 2018 9 599 -8 C ATOM 900 C PRO A 107 -1.321 20.196 18.098 1.00 20.94 C ANISOU 900 C PRO A 107 2884 2652 2421 -29 590 -30 C ATOM 901 O PRO A 107 -1.006 20.971 19.009 1.00 25.85 O ANISOU 901 O PRO A 107 3501 3245 3078 -34 592 4 O ATOM 902 CB PRO A 107 -1.365 21.413 15.887 1.00 28.56 C ANISOU 902 CB PRO A 107 3842 3700 3312 44 581 9 C ATOM 903 CG PRO A 107 -1.190 20.934 14.478 1.00 20.78 C ANISOU 903 CG PRO A 107 2865 2760 2272 74 584 -4 C ATOM 904 CD PRO A 107 -1.280 19.437 14.564 1.00 26.87 C ANISOU 904 CD PRO A 107 3647 3521 3042 43 587 -65 C ATOM 905 N THR A 108 -2.243 19.243 18.265 1.00 21.61 N ANISOU 905 N THR A 108 2965 2742 2503 -55 581 -86 N ATOM 906 CA THR A 108 -2.758 18.959 19.601 1.00 23.08 C ANISOU 906 CA THR A 108 3146 2894 2730 -91 580 -103 C ATOM 907 C THR A 108 -1.647 18.449 20.512 1.00 27.89 C ANISOU 907 C THR A 108 3773 3452 3372 -103 605 -82 C ATOM 908 O THR A 108 -1.552 18.855 21.676 1.00 26.62 O ANISOU 908 O THR A 108 3608 3262 3243 -115 606 -63 O ATOM 909 CB THR A 108 -3.899 17.943 19.532 1.00 22.38 C ANISOU 909 CB THR A 108 3049 2817 2636 -117 572 -168 C ATOM 910 OG1 THR A 108 -5.004 18.506 18.816 1.00 46.36 O ANISOU 910 OG1 THR A 108 6063 5908 5643 -105 544 -188 O ATOM 911 CG2 THR A 108 -4.360 17.555 20.928 1.00 28.64 C ANISOU 911 CG2 THR A 108 3839 3570 3472 -152 579 -181 C ATOM 912 N GLY A 109 -0.788 17.569 19.992 1.00 23.87 N ANISOU 912 N GLY A 109 3282 2933 2853 -98 627 -86 N ATOM 913 CA GLY A 109 0.335 17.090 20.784 1.00 26.82 C ANISOU 913 CA GLY A 109 3672 3265 3255 -104 652 -63 C ATOM 914 C GLY A 109 1.341 18.183 21.099 1.00 19.44 C ANISOU 914 C GLY A 109 2732 2320 2333 -86 653 -6 C ATOM 915 O GLY A 109 1.934 18.202 22.183 1.00 30.15 O ANISOU 915 O GLY A 109 4090 3646 3720 -95 661 14 O ATOM 916 N CYS A 110 1.566 19.093 20.151 1.00 22.94 N ANISOU 916 N CYS A 110 3170 2790 2755 -59 646 20 N ATOM 917 CA CYS A 110 2.453 20.223 20.402 1.00 18.36 C ANISOU 917 CA CYS A 110 2583 2199 2195 -45 650 72 C ATOM 918 C CYS A 110 1.885 21.139 21.478 1.00 23.90 C ANISOU 918 C CYS A 110 3267 2888 2926 -59 633 78 C ATOM 919 O CYS A 110 2.627 21.634 22.337 1.00 21.77 O ANISOU 919 O CYS A 110 2992 2592 2688 -64 638 103 O ATOM 920 CB CYS A 110 2.693 20.993 19.105 1.00 20.18 C ANISOU 920 CB CYS A 110 2810 2459 2397 -11 652 100 C ATOM 921 SG CYS A 110 3.808 22.417 19.227 1.00 24.09 S ANISOU 921 SG CYS A 110 3293 2935 2923 7 665 164 S ATOM 922 N ASN A 111 0.573 21.380 21.446 1.00 19.77 N ANISOU 922 N ASN A 111 2734 2384 2392 -65 613 53 N ATOM 923 CA ASN A 111 -0.055 22.172 22.500 1.00 16.62 C ANISOU 923 CA ASN A 111 2321 1974 2020 -78 598 55 C ATOM 924 C ASN A 111 0.100 21.503 23.859 1.00 26.40 C ANISOU 924 C ASN A 111 3564 3180 3286 -104 604 41 C ATOM 925 O ASN A 111 0.396 22.173 24.854 1.00 16.20 O ANISOU 925 O ASN A 111 2264 1869 2022 -109 601 58 O ATOM 926 CB ASN A 111 -1.533 22.399 22.181 1.00 18.45 C ANISOU 926 CB ASN A 111 2541 2236 2234 -78 578 28 C ATOM 927 CG ASN A 111 -1.750 23.479 21.141 1.00 24.01 C ANISOU 927 CG ASN A 111 3236 2972 2916 -46 570 55 C ATOM 928 OD1 ASN A 111 -0.960 24.414 21.028 1.00 30.95 O ANISOU 928 OD1 ASN A 111 4113 3838 3808 -29 580 98 O ATOM 929 ND2 ASN A 111 -2.828 23.358 20.378 1.00 27.92 N ANISOU 929 ND2 ASN A 111 3722 3508 3377 -37 554 29 N ATOM 930 N LEU A 112 -0.092 20.182 23.920 1.00 21.41 N ANISOU 930 N LEU A 112 2944 2544 2648 -118 614 10 N ATOM 931 CA LEU A 112 0.074 19.466 25.182 1.00 22.31 C ANISOU 931 CA LEU A 112 3064 2628 2785 -137 625 2 C ATOM 932 C LEU A 112 1.499 19.598 25.704 1.00 17.42 C ANISOU 932 C LEU A 112 2449 1988 2181 -127 638 37 C ATOM 933 O LEU A 112 1.716 19.923 26.877 1.00 17.43 O ANISOU 933 O LEU A 112 2444 1976 2204 -133 635 46 O ATOM 934 CB LEU A 112 -0.290 17.990 25.007 1.00 19.76 C ANISOU 934 CB LEU A 112 2755 2298 2455 -151 642 -34 C ATOM 935 CG LEU A 112 -1.754 17.624 24.767 1.00 26.41 C ANISOU 935 CG LEU A 112 3589 3155 3290 -168 631 -78 C ATOM 936 CD1 LEU A 112 -1.889 16.128 24.523 1.00 16.80 C ANISOU 936 CD1 LEU A 112 2386 1924 2073 -183 654 -114 C ATOM 937 CD2 LEU A 112 -2.600 18.054 25.950 1.00 23.36 C ANISOU 937 CD2 LEU A 112 3189 2760 2925 -183 621 -82 C ATOM 938 N GLU A 113 2.486 19.350 24.838 1.00 24.41 N ANISOU 938 N GLU A 113 3343 2877 3056 -112 652 54 N ATOM 939 CA GLU A 113 3.880 19.334 25.272 1.00 17.12 C ANISOU 939 CA GLU A 113 2421 1938 2148 -103 666 84 C ATOM 940 C GLU A 113 4.327 20.707 25.761 1.00 20.07 C ANISOU 940 C GLU A 113 2774 2309 2543 -99 653 111 C ATOM 941 O GLU A 113 4.977 20.820 26.808 1.00 20.60 O ANISOU 941 O GLU A 113 2834 2364 2631 -103 654 121 O ATOM 942 CB GLU A 113 4.770 18.857 24.124 1.00 16.34 C ANISOU 942 CB GLU A 113 2333 1844 2030 -85 685 97 C ATOM 943 CG GLU A 113 6.005 18.098 24.553 1.00 20.02 C ANISOU 943 CG GLU A 113 2807 2292 2506 -79 708 114 C ATOM 944 CD GLU A 113 7.100 18.993 25.095 1.00 18.68 C ANISOU 944 CD GLU A 113 2619 2118 2360 -71 705 149 C ATOM 945 OE1 GLU A 113 7.331 20.076 24.520 1.00 16.28 O ANISOU 945 OE1 GLU A 113 2302 1822 2061 -63 698 169 O ATOM 946 OE2 GLU A 113 7.738 18.609 26.096 1.00 21.95 O ANISOU 946 OE2 GLU A 113 3030 2522 2789 -72 711 156 O ATOM 947 N GLY A 114 3.984 21.758 25.021 1.00 16.42 N ANISOU 947 N GLY A 114 2302 1859 2076 -91 643 122 N ATOM 948 CA GLY A 114 4.397 23.103 25.364 1.00 16.09 C ANISOU 948 CA GLY A 114 2242 1810 2062 -88 636 146 C ATOM 949 C GLY A 114 3.663 23.698 26.548 1.00 15.95 C ANISOU 949 C GLY A 114 2212 1784 2063 -103 618 131 C ATOM 950 O GLY A 114 4.283 24.338 27.400 1.00 18.99 O ANISOU 950 O GLY A 114 2584 2155 2476 -108 615 140 O ATOM 951 N PHE A 115 2.344 23.486 26.618 1.00 17.25 N ANISOU 951 N PHE A 115 2381 1958 2214 -111 607 106 N ATOM 952 CA PHE A 115 1.535 24.123 27.657 1.00 20.68 C ANISOU 952 CA PHE A 115 2804 2388 2665 -123 591 92 C ATOM 953 C PHE A 115 1.902 23.617 29.047 1.00 22.24 C ANISOU 953 C PHE A 115 3002 2572 2876 -134 592 83 C ATOM 954 O PHE A 115 2.101 24.411 29.973 1.00 15.82 O ANISOU 954 O PHE A 115 2177 1751 2084 -138 583 85 O ATOM 955 CB PHE A 115 0.048 23.896 27.378 1.00 16.93 C ANISOU 955 CB PHE A 115 2332 1930 2172 -128 580 67 C ATOM 956 CG PHE A 115 -0.846 24.227 28.541 1.00 15.75 C ANISOU 956 CG PHE A 115 2173 1774 2036 -141 568 50 C ATOM 957 CD1 PHE A 115 -1.138 25.544 28.855 1.00 17.57 C ANISOU 957 CD1 PHE A 115 2390 2001 2284 -137 557 59 C ATOM 958 CD2 PHE A 115 -1.395 23.221 29.320 1.00 26.63 C ANISOU 958 CD2 PHE A 115 3558 3149 3412 -155 571 26 C ATOM 959 CE1 PHE A 115 -1.962 25.851 29.929 1.00 23.35 C ANISOU 959 CE1 PHE A 115 3115 2729 3028 -147 547 42 C ATOM 960 CE2 PHE A 115 -2.220 23.522 30.390 1.00 22.35 C ANISOU 960 CE2 PHE A 115 3008 2603 2880 -164 563 12 C ATOM 961 CZ PHE A 115 -2.502 24.837 30.696 1.00 23.66 C ANISOU 961 CZ PHE A 115 3161 2768 3061 -160 549 19 C ATOM 962 N PHE A 116 2.001 22.296 29.215 1.00 19.02 N ANISOU 962 N PHE A 116 2609 2162 2455 -138 604 72 N ATOM 963 CA PHE A 116 2.215 21.746 30.551 1.00 22.93 C ANISOU 963 CA PHE A 116 3105 2648 2957 -143 608 66 C ATOM 964 C PHE A 116 3.627 22.014 31.060 1.00 20.95 C ANISOU 964 C PHE A 116 2846 2394 2720 -134 610 86 C ATOM 965 O PHE A 116 3.825 22.172 32.272 1.00 19.08 O ANISOU 965 O PHE A 116 2600 2157 2491 -135 604 83 O ATOM 966 CB PHE A 116 1.904 20.248 30.560 1.00 22.04 C ANISOU 966 CB PHE A 116 3012 2531 2832 -147 627 52 C ATOM 967 CG PHE A 116 0.438 19.942 30.715 1.00 24.42 C ANISOU 967 CG PHE A 116 3315 2834 3129 -161 624 25 C ATOM 968 CD1 PHE A 116 -0.230 20.288 31.880 1.00 19.91 C ANISOU 968 CD1 PHE A 116 2736 2261 2568 -167 616 17 C ATOM 969 CD2 PHE A 116 -0.272 19.321 29.700 1.00 20.50 C ANISOU 969 CD2 PHE A 116 2826 2342 2620 -168 630 5 C ATOM 970 CE1 PHE A 116 -1.575 20.023 32.032 1.00 24.07 C ANISOU 970 CE1 PHE A 116 3262 2790 3095 -180 615 -7 C ATOM 971 CE2 PHE A 116 -1.619 19.051 29.847 1.00 28.45 C ANISOU 971 CE2 PHE A 116 3829 3353 3628 -183 626 -24 C ATOM 972 CZ PHE A 116 -2.271 19.403 31.015 1.00 25.66 C ANISOU 972 CZ PHE A 116 3468 2996 3287 -190 620 -27 C ATOM 973 N ALA A 117 4.616 22.061 30.166 1.00 16.03 N ANISOU 973 N ALA A 117 2223 1772 2098 -125 620 106 N ATOM 974 CA ALA A 117 5.963 22.429 30.590 1.00 20.30 C ANISOU 974 CA ALA A 117 2748 2310 2654 -118 621 124 C ATOM 975 C ALA A 117 6.057 23.920 30.887 1.00 24.33 C ANISOU 975 C ALA A 117 3235 2818 3191 -124 604 126 C ATOM 976 O ALA A 117 6.689 24.322 31.871 1.00 24.79 O ANISOU 976 O ALA A 117 3276 2878 3267 -127 595 122 O ATOM 977 CB ALA A 117 6.983 22.019 29.528 1.00 15.80 C ANISOU 977 CB ALA A 117 2183 1741 2080 -106 639 147 C ATOM 978 N THR A 118 5.434 24.757 30.049 1.00 24.49 N ANISOU 978 N THR A 118 3253 2834 3216 -126 601 130 N ATOM 979 CA THR A 118 5.375 26.189 30.336 1.00 25.24 C ANISOU 979 CA THR A 118 3329 2920 3341 -131 590 130 C ATOM 980 C THR A 118 4.600 26.452 31.621 1.00 16.43 C ANISOU 980 C THR A 118 2208 1804 2230 -141 573 104 C ATOM 981 O THR A 118 5.016 27.270 32.451 1.00 22.57 O ANISOU 981 O THR A 118 2967 2576 3032 -148 564 96 O ATOM 982 CB THR A 118 4.733 26.942 29.166 1.00 18.80 C ANISOU 982 CB THR A 118 2517 2102 2526 -124 595 144 C ATOM 983 OG1 THR A 118 5.370 26.571 27.936 1.00 18.12 O ANISOU 983 OG1 THR A 118 2438 2021 2427 -110 612 168 O ATOM 984 CG2 THR A 118 4.855 28.449 29.354 1.00 17.59 C ANISOU 984 CG2 THR A 118 2343 1931 2410 -127 593 151 C ATOM 985 N LEU A 119 3.470 25.763 31.802 1.00 18.71 N ANISOU 985 N LEU A 119 2513 2101 2496 -144 570 88 N ATOM 986 CA LEU A 119 2.687 25.913 33.024 1.00 19.57 C ANISOU 986 CA LEU A 119 2618 2211 2605 -150 557 66 C ATOM 987 C LEU A 119 3.473 25.460 34.249 1.00 23.65 C ANISOU 987 C LEU A 119 3130 2735 3122 -149 555 59 C ATOM 988 O LEU A 119 3.491 26.150 35.276 1.00 20.90 O ANISOU 988 O LEU A 119 2767 2388 2785 -151 542 44 O ATOM 989 CB LEU A 119 1.385 25.122 32.907 1.00 20.05 C ANISOU 989 CB LEU A 119 2695 2279 2644 -154 559 52 C ATOM 990 CG LEU A 119 0.511 25.047 34.158 1.00 27.82 C ANISOU 990 CG LEU A 119 3678 3266 3626 -159 552 32 C ATOM 991 CD1 LEU A 119 -0.328 26.310 34.299 1.00 21.19 C ANISOU 991 CD1 LEU A 119 2827 2423 2801 -162 538 23 C ATOM 992 CD2 LEU A 119 -0.366 23.805 34.125 1.00 19.81 C ANISOU 992 CD2 LEU A 119 2680 2256 2592 -163 564 21 C ATOM 993 N GLY A 120 4.131 24.303 34.160 1.00 20.39 N ANISOU 993 N GLY A 120 2727 2327 2692 -141 568 69 N ATOM 994 CA GLY A 120 4.850 23.784 35.312 1.00 19.60 C ANISOU 994 CA GLY A 120 2622 2239 2586 -132 568 67 C ATOM 995 C GLY A 120 6.051 24.630 35.687 1.00 18.53 C ANISOU 995 C GLY A 120 2461 2110 2472 -131 556 68 C ATOM 996 O GLY A 120 6.324 24.846 36.871 1.00 24.12 O ANISOU 996 O GLY A 120 3154 2831 3178 -127 543 54 O ATOM 997 N GLY A 121 6.791 25.111 34.688 1.00 18.05 N ANISOU 997 N GLY A 121 2390 2038 2428 -134 562 84 N ATOM 998 CA GLY A 121 7.930 25.966 34.974 1.00 25.55 C ANISOU 998 CA GLY A 121 3311 2990 3406 -137 553 83 C ATOM 999 C GLY A 121 7.526 27.304 35.563 1.00 24.92 C ANISOU 999 C GLY A 121 3213 2902 3353 -150 536 59 C ATOM 1000 O GLY A 121 8.228 27.853 36.415 1.00 20.76 O ANISOU 1000 O GLY A 121 2660 2384 2843 -154 523 41 O ATOM 1001 N GLU A 122 6.395 27.852 35.110 1.00 19.67 N ANISOU 1001 N GLU A 122 2559 2221 2692 -157 537 57 N ATOM 1002 CA GLU A 122 5.917 29.118 35.656 1.00 21.72 C ANISOU 1002 CA GLU A 122 2804 2469 2979 -168 524 35 C ATOM 1003 C GLU A 122 5.354 28.951 37.062 1.00 22.23 C ANISOU 1003 C GLU A 122 2870 2552 3026 -166 508 6 C ATOM 1004 O GLU A 122 5.407 29.892 37.862 1.00 20.26 O ANISOU 1004 O GLU A 122 2602 2300 2798 -173 494 -21 O ATOM 1005 CB GLU A 122 4.870 29.730 34.727 1.00 18.33 C ANISOU 1005 CB GLU A 122 2386 2021 2556 -169 532 46 C ATOM 1006 CG GLU A 122 5.467 30.406 33.507 1.00 16.50 C ANISOU 1006 CG GLU A 122 2147 1770 2351 -168 548 73 C ATOM 1007 CD GLU A 122 6.299 31.620 33.870 1.00 19.18 C ANISOU 1007 CD GLU A 122 2458 2090 2740 -180 549 63 C ATOM 1008 OE1 GLU A 122 5.998 32.261 34.899 1.00 34.13 O ANISOU 1008 OE1 GLU A 122 4340 3979 4648 -189 535 32 O ATOM 1009 OE2 GLU A 122 7.257 31.932 33.132 1.00 22.67 O ANISOU 1009 OE2 GLU A 122 2887 2518 3207 -181 565 84 O ATOM 1010 N ILE A 123 4.801 27.777 37.375 1.00 20.68 N ANISOU 1010 N ILE A 123 2694 2371 2793 -156 511 9 N ATOM 1011 CA ILE A 123 4.413 27.487 38.752 1.00 18.10 C ANISOU 1011 CA ILE A 123 2367 2064 2446 -149 500 -13 C ATOM 1012 C ILE A 123 5.642 27.486 39.651 1.00 25.82 C ANISOU 1012 C ILE A 123 3323 3064 3422 -141 489 -24 C ATOM 1013 O ILE A 123 5.610 27.999 40.776 1.00 23.14 O ANISOU 1013 O ILE A 123 2970 2741 3083 -139 472 -52 O ATOM 1014 CB ILE A 123 3.644 26.154 38.822 1.00 20.98 C ANISOU 1014 CB ILE A 123 2758 2436 2777 -139 514 -2 C ATOM 1015 CG1 ILE A 123 2.257 26.317 38.201 1.00 20.24 C ANISOU 1015 CG1 ILE A 123 2679 2327 2686 -148 519 -3 C ATOM 1016 CG2 ILE A 123 3.522 25.664 40.261 1.00 23.16 C ANISOU 1016 CG2 ILE A 123 3035 2736 3029 -124 510 -14 C ATOM 1017 CD1 ILE A 123 1.618 25.017 37.781 1.00 21.96 C ANISOU 1017 CD1 ILE A 123 2919 2544 2881 -145 537 8 C ATOM 1018 N ALA A 124 6.750 26.924 39.161 1.00 19.62 N ANISOU 1018 N ALA A 124 2533 2285 2638 -136 497 -4 N ATOM 1019 CA ALA A 124 7.989 26.923 39.930 1.00 20.92 C ANISOU 1019 CA ALA A 124 2671 2476 2801 -127 485 -14 C ATOM 1020 C ALA A 124 8.502 28.338 40.165 1.00 21.94 C ANISOU 1020 C ALA A 124 2766 2599 2970 -145 468 -43 C ATOM 1021 O ALA A 124 8.905 28.681 41.283 1.00 29.40 O ANISOU 1021 O ALA A 124 3688 3570 3911 -141 447 -74 O ATOM 1022 CB ALA A 124 9.046 26.085 39.214 1.00 16.41 C ANISOU 1022 CB ALA A 124 2099 1909 2225 -117 500 16 C ATOM 1023 N LEU A 125 8.489 29.175 39.126 1.00 17.96 N ANISOU 1023 N LEU A 125 2259 2061 2504 -163 477 -35 N ATOM 1024 CA LEU A 125 9.036 30.523 39.251 1.00 28.76 C ANISOU 1024 CA LEU A 125 3594 3414 3920 -182 468 -60 C ATOM 1025 C LEU A 125 8.213 31.371 40.213 1.00 27.49 C ANISOU 1025 C LEU A 125 3429 3251 3765 -189 452 -99 C ATOM 1026 O LEU A 125 8.761 32.004 41.123 1.00 20.73 O ANISOU 1026 O LEU A 125 2544 2408 2924 -196 434 -138 O ATOM 1027 CB LEU A 125 9.110 31.186 37.875 1.00 20.02 C ANISOU 1027 CB LEU A 125 2488 2267 2851 -194 490 -34 C ATOM 1028 CG LEU A 125 9.581 32.642 37.829 1.00 26.32 C ANISOU 1028 CG LEU A 125 3256 3036 3709 -216 491 -54 C ATOM 1029 CD1 LEU A 125 10.973 32.799 38.432 1.00 25.50 C ANISOU 1029 CD1 LEU A 125 3111 2950 3626 -224 479 -78 C ATOM 1030 CD2 LEU A 125 9.562 33.147 36.399 1.00 24.11 C ANISOU 1030 CD2 LEU A 125 2982 2718 3459 -220 519 -17 C ATOM 1031 N TRP A 126 6.891 31.397 40.028 1.00 16.76 N ANISOU 1031 N TRP A 126 2098 1877 2394 -187 458 -92 N ATOM 1032 CA TRP A 126 6.044 32.186 40.913 1.00 26.14 C ANISOU 1032 CA TRP A 126 3284 3062 3587 -191 446 -127 C ATOM 1033 C TRP A 126 5.984 31.606 42.320 1.00 19.89 C ANISOU 1033 C TRP A 126 2491 2312 2754 -175 427 -153 C ATOM 1034 O TRP A 126 5.665 32.339 43.262 1.00 30.23 O ANISOU 1034 O TRP A 126 3790 3628 4069 -177 412 -191 O ATOM 1035 CB TRP A 126 4.640 32.318 40.321 1.00 21.19 C ANISOU 1035 CB TRP A 126 2683 2412 2956 -190 458 -111 C ATOM 1036 CG TRP A 126 4.591 33.277 39.161 1.00 22.58 C ANISOU 1036 CG TRP A 126 2856 2548 3175 -202 474 -93 C ATOM 1037 CD1 TRP A 126 4.413 32.968 37.842 1.00 26.66 C ANISOU 1037 CD1 TRP A 126 3388 3051 3690 -198 492 -53 C ATOM 1038 CD2 TRP A 126 4.751 34.702 39.219 1.00 21.19 C ANISOU 1038 CD2 TRP A 126 2659 2340 3050 -216 477 -114 C ATOM 1039 NE1 TRP A 126 4.435 34.113 37.079 1.00 26.21 N ANISOU 1039 NE1 TRP A 126 3323 2960 3677 -205 507 -43 N ATOM 1040 CE2 TRP A 126 4.642 35.190 37.901 1.00 23.24 C ANISOU 1040 CE2 TRP A 126 2925 2568 3337 -218 500 -78 C ATOM 1041 CE3 TRP A 126 4.964 35.612 40.260 1.00 18.62 C ANISOU 1041 CE3 TRP A 126 2312 2012 2752 -228 464 -160 C ATOM 1042 CZ2 TRP A 126 4.744 36.546 37.598 1.00 21.52 C ANISOU 1042 CZ2 TRP A 126 2692 2309 3175 -229 514 -83 C ATOM 1043 CZ3 TRP A 126 5.063 36.956 39.957 1.00 17.53 C ANISOU 1043 CZ3 TRP A 126 2159 1832 2672 -243 477 -170 C ATOM 1044 CH2 TRP A 126 4.953 37.411 38.638 1.00 17.52 C ANISOU 1044 CH2 TRP A 126 2165 1794 2700 -243 504 -129 C ATOM 1045 N SER A 127 6.277 30.312 42.483 1.00 18.54 N ANISOU 1045 N SER A 127 2331 2170 2542 -156 430 -131 N ATOM 1046 CA SER A 127 6.421 29.754 43.824 1.00 26.53 C ANISOU 1046 CA SER A 127 3339 3228 3515 -134 416 -150 C ATOM 1047 C SER A 127 7.667 30.298 44.512 1.00 20.05 C ANISOU 1047 C SER A 127 2479 2434 2706 -136 394 -183 C ATOM 1048 O SER A 127 7.643 30.584 45.714 1.00 29.77 O ANISOU 1048 O SER A 127 3697 3697 3919 -126 373 -220 O ATOM 1049 CB SER A 127 6.467 28.227 43.765 1.00 17.43 C ANISOU 1049 CB SER A 127 2208 2094 2321 -111 431 -113 C ATOM 1050 OG SER A 127 5.323 27.703 43.111 1.00 21.75 O ANISOU 1050 OG SER A 127 2788 2616 2861 -113 451 -89 O ATOM 1051 N LEU A 128 8.768 30.439 43.767 1.00 25.78 N ANISOU 1051 N LEU A 128 3184 3150 3461 -148 397 -173 N ATOM 1052 CA LEU A 128 9.974 31.040 44.330 1.00 23.52 C ANISOU 1052 CA LEU A 128 2854 2887 3194 -154 376 -209 C ATOM 1053 C LEU A 128 9.711 32.469 44.783 1.00 28.16 C ANISOU 1053 C LEU A 128 3422 3457 3822 -178 362 -260 C ATOM 1054 O LEU A 128 10.248 32.914 45.804 1.00 22.13 O ANISOU 1054 O LEU A 128 2625 2725 3056 -177 337 -308 O ATOM 1055 CB LEU A 128 11.109 31.008 43.306 1.00 17.89 C ANISOU 1055 CB LEU A 128 2122 2159 2515 -166 388 -185 C ATOM 1056 CG LEU A 128 11.588 29.638 42.825 1.00 32.54 C ANISOU 1056 CG LEU A 128 3994 4033 4337 -143 402 -138 C ATOM 1057 CD1 LEU A 128 12.637 29.791 41.730 1.00 30.61 C ANISOU 1057 CD1 LEU A 128 3730 3768 4131 -157 417 -116 C ATOM 1058 CD2 LEU A 128 12.125 28.808 43.985 1.00 34.11 C ANISOU 1058 CD2 LEU A 128 4181 4292 4487 -112 385 -147 C ATOM 1059 N VAL A 129 8.898 33.206 44.024 1.00 22.76 N ANISOU 1059 N VAL A 129 2754 2721 3174 -197 379 -252 N ATOM 1060 CA VAL A 129 8.488 34.542 44.446 1.00 33.12 C ANISOU 1060 CA VAL A 129 4052 4008 4524 -216 372 -297 C ATOM 1061 C VAL A 129 7.783 34.473 45.792 1.00 27.94 C ANISOU 1061 C VAL A 129 3402 3387 3826 -199 352 -333 C ATOM 1062 O VAL A 129 8.055 35.265 46.701 1.00 19.71 O ANISOU 1062 O VAL A 129 2333 2358 2796 -206 332 -389 O ATOM 1063 CB VAL A 129 7.593 35.190 43.373 1.00 28.97 C ANISOU 1063 CB VAL A 129 3549 3424 4035 -230 398 -270 C ATOM 1064 CG1 VAL A 129 6.962 36.471 43.902 1.00 18.22 C ANISOU 1064 CG1 VAL A 129 2180 2036 2707 -244 395 -314 C ATOM 1065 CG2 VAL A 129 8.398 35.469 42.114 1.00 18.01 C ANISOU 1065 CG2 VAL A 129 2148 2001 2692 -246 419 -240 C ATOM 1066 N VAL A 130 6.870 33.512 45.940 1.00 18.77 N ANISOU 1066 N VAL A 130 2276 2242 2615 -175 359 -303 N ATOM 1067 CA VAL A 130 6.153 33.346 47.200 1.00 23.44 C ANISOU 1067 CA VAL A 130 2876 2868 3162 -154 345 -329 C ATOM 1068 C VAL A 130 7.124 33.035 48.332 1.00 30.32 C ANISOU 1068 C VAL A 130 3720 3800 4000 -135 319 -361 C ATOM 1069 O VAL A 130 7.013 33.588 49.433 1.00 31.81 O ANISOU 1069 O VAL A 130 3894 4016 4175 -128 299 -411 O ATOM 1070 CB VAL A 130 5.078 32.254 47.054 1.00 23.75 C ANISOU 1070 CB VAL A 130 2955 2909 3159 -133 363 -285 C ATOM 1071 CG1 VAL A 130 4.480 31.911 48.409 1.00 24.24 C ANISOU 1071 CG1 VAL A 130 3025 3013 3171 -105 354 -305 C ATOM 1072 CG2 VAL A 130 3.996 32.698 46.077 1.00 26.14 C ANISOU 1072 CG2 VAL A 130 3280 3161 3492 -150 383 -264 C ATOM 1073 N LEU A 131 8.091 32.146 48.085 1.00 23.63 N ANISOU 1073 N LEU A 131 2864 2979 3136 -123 320 -334 N ATOM 1074 CA LEU A 131 9.044 31.781 49.130 1.00 29.06 C ANISOU 1074 CA LEU A 131 3523 3732 3785 -99 295 -359 C ATOM 1075 C LEU A 131 9.980 32.939 49.461 1.00 25.90 C ANISOU 1075 C LEU A 131 3074 3339 3427 -123 270 -421 C ATOM 1076 O LEU A 131 10.374 33.114 50.620 1.00 32.17 O ANISOU 1076 O LEU A 131 3842 4188 4192 -107 241 -468 O ATOM 1077 CB LEU A 131 9.840 30.546 48.713 1.00 22.73 C ANISOU 1077 CB LEU A 131 2724 2953 2959 -78 305 -311 C ATOM 1078 CG LEU A 131 9.060 29.231 48.702 1.00 34.06 C ANISOU 1078 CG LEU A 131 4202 4393 4345 -48 329 -258 C ATOM 1079 CD1 LEU A 131 9.963 28.071 48.308 1.00 34.30 C ANISOU 1079 CD1 LEU A 131 4233 4444 4357 -27 341 -215 C ATOM 1080 CD2 LEU A 131 8.424 28.982 50.059 1.00 32.51 C ANISOU 1080 CD2 LEU A 131 4015 4241 4096 -14 320 -276 C ATOM 1081 N ALA A 132 10.361 33.731 48.456 1.00 22.97 N ANISOU 1081 N ALA A 132 2689 2915 3123 -160 281 -422 N ATOM 1082 CA ALA A 132 11.217 34.885 48.713 1.00 31.64 C ANISOU 1082 CA ALA A 132 3740 4011 4272 -189 262 -482 C ATOM 1083 C ALA A 132 10.504 35.915 49.578 1.00 30.11 C ANISOU 1083 C ALA A 132 3541 3811 4087 -198 249 -543 C ATOM 1084 O ALA A 132 11.106 36.492 50.493 1.00 28.05 O ANISOU 1084 O ALA A 132 3242 3586 3831 -203 221 -609 O ATOM 1085 CB ALA A 132 11.672 35.508 47.395 1.00 26.90 C ANISOU 1085 CB ALA A 132 3129 3347 3745 -226 287 -462 C ATOM 1086 N ILE A 133 9.220 36.156 49.306 1.00 25.04 N ANISOU 1086 N ILE A 133 2938 3127 3450 -200 269 -524 N ATOM 1087 CA ILE A 133 8.432 37.057 50.140 1.00 26.32 C ANISOU 1087 CA ILE A 133 3102 3283 3616 -204 259 -577 C ATOM 1088 C ILE A 133 8.297 36.497 51.550 1.00 29.09 C ANISOU 1088 C ILE A 133 3452 3709 3893 -166 233 -606 C ATOM 1089 O ILE A 133 8.407 37.232 52.539 1.00 28.26 O ANISOU 1089 O ILE A 133 3322 3628 3786 -168 209 -674 O ATOM 1090 CB ILE A 133 7.059 37.308 49.491 1.00 34.65 C ANISOU 1090 CB ILE A 133 4198 4281 4686 -208 288 -542 C ATOM 1091 CG1 ILE A 133 7.215 38.216 48.269 1.00 28.30 C ANISOU 1091 CG1 ILE A 133 3388 3404 3960 -243 313 -528 C ATOM 1092 CG2 ILE A 133 6.074 37.877 50.507 1.00 23.80 C ANISOU 1092 CG2 ILE A 133 2834 2914 3294 -198 280 -585 C ATOM 1093 CD1 ILE A 133 5.947 38.390 47.468 1.00 27.52 C ANISOU 1093 CD1 ILE A 133 3328 3256 3874 -243 341 -485 C ATOM 1094 N GLU A 134 8.046 35.191 51.665 1.00 31.03 N ANISOU 1094 N GLU A 134 3723 3990 4076 -130 238 -554 N ATOM 1095 CA GLU A 134 7.887 34.571 52.976 1.00 32.83 C ANISOU 1095 CA GLU A 134 3955 4290 4230 -88 219 -570 C ATOM 1096 C GLU A 134 9.175 34.656 53.790 1.00 35.81 C ANISOU 1096 C GLU A 134 4284 4734 4589 -78 184 -620 C ATOM 1097 O GLU A 134 9.142 34.959 54.991 1.00 21.08 O ANISOU 1097 O GLU A 134 2403 2920 2686 -58 159 -675 O ATOM 1098 CB GLU A 134 7.439 33.119 52.807 1.00 29.73 C ANISOU 1098 CB GLU A 134 3599 3913 3784 -53 240 -498 C ATOM 1099 CG GLU A 134 7.192 32.376 54.112 1.00 37.74 C ANISOU 1099 CG GLU A 134 4622 4998 4720 -2 231 -501 C ATOM 1100 CD GLU A 134 8.393 31.567 54.561 1.00 28.44 C ANISOU 1100 CD GLU A 134 3419 3888 3500 29 214 -494 C ATOM 1101 OE1 GLU A 134 9.341 31.425 53.762 1.00 37.39 O ANISOU 1101 OE1 GLU A 134 4534 5008 4665 11 214 -478 O ATOM 1102 OE2 GLU A 134 8.389 31.075 55.711 1.00 30.13 O ANISOU 1102 OE2 GLU A 134 3632 4169 3648 75 202 -501 O ATOM 1103 N ARG A 135 10.319 34.388 53.155 1.00 20.67 N ANISOU 1103 N ARG A 135 2341 2819 2695 -89 182 -605 N ATOM 1104 CA ARG A 135 11.598 34.511 53.847 1.00 26.30 C ANISOU 1104 CA ARG A 135 3000 3596 3395 -83 147 -654 C ATOM 1105 C ARG A 135 11.874 35.954 54.246 1.00 34.29 C ANISOU 1105 C ARG A 135 3973 4596 4460 -119 125 -742 C ATOM 1106 O ARG A 135 12.335 36.218 55.363 1.00 35.27 O ANISOU 1106 O ARG A 135 4063 4787 4553 -104 90 -807 O ATOM 1107 CB ARG A 135 12.730 33.979 52.968 1.00 27.30 C ANISOU 1107 CB ARG A 135 3108 3721 3546 -91 154 -616 C ATOM 1108 CG ARG A 135 12.725 32.471 52.756 1.00 32.72 C ANISOU 1108 CG ARG A 135 3824 4432 4175 -49 171 -540 C ATOM 1109 CD ARG A 135 13.097 31.719 54.024 1.00 31.69 C ANISOU 1109 CD ARG A 135 3681 4397 3965 5 147 -550 C ATOM 1110 NE ARG A 135 11.939 31.442 54.866 1.00 34.58 N ANISOU 1110 NE ARG A 135 4083 4781 4276 38 152 -545 N ATOM 1111 CZ ARG A 135 12.009 30.951 56.095 1.00 24.71 C ANISOU 1111 CZ ARG A 135 2826 3610 2951 89 134 -558 C ATOM 1112 NH1 ARG A 135 13.171 30.685 56.668 1.00 28.00 N ANISOU 1112 NH1 ARG A 135 3200 4102 3335 116 106 -578 N ATOM 1113 NH2 ARG A 135 10.884 30.724 56.767 1.00 28.72 N ANISOU 1113 NH2 ARG A 135 3371 4127 3416 117 145 -548 N ATOM 1114 N TYR A 136 11.599 36.901 53.347 1.00 36.51 N ANISOU 1114 N TYR A 136 4257 4794 4820 -166 147 -747 N ATOM 1115 CA TYR A 136 11.826 38.307 53.662 1.00 25.27 C ANISOU 1115 CA TYR A 136 2799 3347 3458 -204 134 -829 C ATOM 1116 C TYR A 136 10.963 38.756 54.835 1.00 36.87 C ANISOU 1116 C TYR A 136 4278 4841 4888 -186 118 -883 C ATOM 1117 O TYR A 136 11.399 39.565 55.662 1.00 38.50 O ANISOU 1117 O TYR A 136 4445 5076 5107 -198 90 -969 O ATOM 1118 CB TYR A 136 11.551 39.174 52.436 1.00 33.76 C ANISOU 1118 CB TYR A 136 3883 4322 4622 -250 170 -810 C ATOM 1119 CG TYR A 136 11.363 40.632 52.774 1.00 30.48 C ANISOU 1119 CG TYR A 136 3447 3865 4269 -285 168 -886 C ATOM 1120 CD1 TYR A 136 12.452 41.439 53.073 1.00 42.21 C ANISOU 1120 CD1 TYR A 136 4874 5358 5806 -317 150 -961 C ATOM 1121 CD2 TYR A 136 10.096 41.202 52.806 1.00 23.85 C ANISOU 1121 CD2 TYR A 136 2643 2978 3439 -286 188 -887 C ATOM 1122 CE1 TYR A 136 12.287 42.773 53.386 1.00 40.42 C ANISOU 1122 CE1 TYR A 136 4628 5088 5642 -351 152 -1035 C ATOM 1123 CE2 TYR A 136 9.923 42.537 53.117 1.00 41.58 C ANISOU 1123 CE2 TYR A 136 4872 5183 5745 -316 190 -956 C ATOM 1124 CZ TYR A 136 11.023 43.316 53.405 1.00 29.14 C ANISOU 1124 CZ TYR A 136 3240 3610 4222 -350 174 -1031 C ATOM 1125 OH TYR A 136 10.855 44.643 53.717 1.00 57.02 O ANISOU 1125 OH TYR A 136 6753 7093 7817 -382 180 -1104 O ATOM 1126 N VAL A 137 9.730 38.256 54.913 1.00 23.72 N ANISOU 1126 N VAL A 137 2664 3167 3180 -159 136 -838 N ATOM 1127 CA VAL A 137 8.857 38.601 56.029 1.00 37.56 C ANISOU 1127 CA VAL A 137 4430 4947 4893 -137 124 -882 C ATOM 1128 C VAL A 137 9.359 37.965 57.320 1.00 37.38 C ANISOU 1128 C VAL A 137 4387 5029 4786 -91 88 -914 C ATOM 1129 O VAL A 137 9.468 38.630 58.356 1.00 45.22 O ANISOU 1129 O VAL A 137 5356 6064 5764 -86 60 -993 O ATOM 1130 CB VAL A 137 7.408 38.185 55.721 1.00 39.62 C ANISOU 1130 CB VAL A 137 4749 5172 5133 -120 156 -821 C ATOM 1131 CG1 VAL A 137 6.594 38.106 57.003 1.00 38.54 C ANISOU 1131 CG1 VAL A 137 4628 5085 4930 -81 144 -850 C ATOM 1132 CG2 VAL A 137 6.779 39.161 54.748 1.00 31.89 C ANISOU 1132 CG2 VAL A 137 3785 4099 4234 -161 185 -814 C ATOM 1133 N VAL A 138 9.686 36.672 57.274 1.00 34.85 N ANISOU 1133 N VAL A 138 4078 4755 4410 -54 90 -852 N ATOM 1134 CA VAL A 138 10.061 35.962 58.494 1.00 31.60 C ANISOU 1134 CA VAL A 138 3651 4444 3909 1 62 -867 C ATOM 1135 C VAL A 138 11.412 36.446 59.008 1.00 41.55 C ANISOU 1135 C VAL A 138 4847 5763 5176 -8 20 -942 C ATOM 1136 O VAL A 138 11.590 36.670 60.212 1.00 50.62 O ANISOU 1136 O VAL A 138 5971 6987 6274 20 -14 -1007 O ATOM 1137 CB VAL A 138 10.051 34.442 58.251 1.00 30.73 C ANISOU 1137 CB VAL A 138 3571 4361 3744 43 82 -776 C ATOM 1138 CG1 VAL A 138 10.767 33.714 59.382 1.00 41.16 C ANISOU 1138 CG1 VAL A 138 4868 5790 4981 101 53 -788 C ATOM 1139 CG2 VAL A 138 8.616 33.938 58.114 1.00 40.68 C ANISOU 1139 CG2 VAL A 138 4891 5583 4984 60 118 -718 C ATOM 1140 N VAL A 139 12.381 36.622 58.114 1.00 35.86 N ANISOU 1140 N VAL A 139 4096 5012 4517 -46 20 -938 N ATOM 1141 CA VAL A 139 13.718 37.007 58.546 1.00 34.83 C ANISOU 1141 CA VAL A 139 3898 4939 4397 -56 -19 -1007 C ATOM 1142 C VAL A 139 13.773 38.490 58.889 1.00 43.02 C ANISOU 1142 C VAL A 139 4901 5950 5496 -102 -36 -1109 C ATOM 1143 O VAL A 139 14.185 38.870 59.991 1.00 59.29 O ANISOU 1143 O VAL A 139 6922 8084 7523 -88 -76 -1192 O ATOM 1144 CB VAL A 139 14.754 36.639 57.471 1.00 30.44 C ANISOU 1144 CB VAL A 139 3319 4359 3887 -80 -8 -964 C ATOM 1145 CG1 VAL A 139 16.121 37.182 57.851 1.00 41.97 C ANISOU 1145 CG1 VAL A 139 4704 5870 5372 -99 -47 -1042 C ATOM 1146 CG2 VAL A 139 14.802 35.136 57.282 1.00 33.05 C ANISOU 1146 CG2 VAL A 139 3680 4726 4153 -29 7 -872 C ATOM 1147 N CYS A 140 13.366 39.352 57.955 1.00 48.35 N ANISOU 1147 N CYS A 140 5589 6521 6260 -155 -5 -1107 N ATOM 1148 CA CYS A 140 13.548 40.785 58.150 1.00 50.30 C ANISOU 1148 CA CYS A 140 5800 6732 6581 -204 -15 -1202 C ATOM 1149 C CYS A 140 12.443 41.437 58.966 1.00 59.72 C ANISOU 1149 C CYS A 140 7019 7918 7755 -195 -16 -1250 C ATOM 1150 O CYS A 140 12.593 42.601 59.349 1.00 64.17 O ANISOU 1150 O CYS A 140 7550 8462 8369 -230 -28 -1341 O ATOM 1151 CB CYS A 140 13.664 41.492 56.799 1.00 52.98 C ANISOU 1151 CB CYS A 140 6139 6961 7029 -263 24 -1177 C ATOM 1152 SG CYS A 140 15.242 41.205 55.965 1.00 62.22 S ANISOU 1152 SG CYS A 140 7257 8137 8247 -289 21 -1158 S ATOM 1153 N LYS A 141 11.339 40.730 59.216 1.00 57.89 N ANISOU 1153 N LYS A 141 6843 7698 7457 -152 -2 -1193 N ATOM 1154 CA LYS A 141 10.239 41.155 60.082 1.00 62.68 C ANISOU 1154 CA LYS A 141 7476 8310 8028 -131 -2 -1229 C ATOM 1155 C LYS A 141 9.846 42.617 59.904 1.00 70.33 C ANISOU 1155 C LYS A 141 8439 9198 9084 -181 12 -1293 C ATOM 1156 O LYS A 141 9.828 43.371 60.886 1.00 77.40 O ANISOU 1156 O LYS A 141 9313 10124 9972 -182 -13 -1385 O ATOM 1157 CB LYS A 141 10.609 40.897 61.546 1.00 55.31 C ANISOU 1157 CB LYS A 141 6516 7493 7007 -85 -48 -1292 C ATOM 1158 CG LYS A 141 10.675 39.424 61.922 1.00 54.96 C ANISOU 1158 CG LYS A 141 6490 7529 6862 -20 -54 -1221 C ATOM 1159 CD LYS A 141 11.278 39.236 63.305 1.00 61.23 C ANISOU 1159 CD LYS A 141 7247 8446 7573 27 -102 -1286 C ATOM 1160 CE LYS A 141 11.438 37.762 63.656 1.00 63.04 C ANISOU 1160 CE LYS A 141 7492 8755 7706 95 -103 -1210 C ATOM 1161 NZ LYS A 141 12.445 37.087 62.783 1.00 58.71 N ANISOU 1161 NZ LYS A 141 6924 8202 7182 84 -99 -1156 N ATOM 1162 N PRO A 142 9.524 43.071 58.681 1.00 69.37 N ANISOU 1162 N PRO A 142 8337 8975 9046 -222 52 -1249 N ATOM 1163 CA PRO A 142 9.137 44.483 58.548 1.00 74.53 C ANISOU 1163 CA PRO A 142 8985 9549 9783 -265 70 -1308 C ATOM 1164 C PRO A 142 7.784 44.788 59.189 1.00 71.70 C ANISOU 1164 C PRO A 142 8668 9182 9391 -240 80 -1319 C ATOM 1165 O PRO A 142 7.732 45.540 60.165 1.00 70.13 O ANISOU 1165 O PRO A 142 8452 9007 9189 -241 61 -1410 O ATOM 1166 CB PRO A 142 9.081 44.691 57.032 1.00 61.96 C ANISOU 1166 CB PRO A 142 7410 7860 8274 -301 114 -1237 C ATOM 1167 CG PRO A 142 8.754 43.346 56.492 1.00 64.27 C ANISOU 1167 CG PRO A 142 7740 8173 8506 -266 125 -1134 C ATOM 1168 CD PRO A 142 9.456 42.359 57.392 1.00 60.66 C ANISOU 1168 CD PRO A 142 7262 7824 7963 -227 84 -1146 C ATOM 1169 N ARG A 147 2.470 37.799 60.825 1.00 65.19 N ANISOU 1169 N ARG A 147 8103 8574 8090 63 159 -884 N ATOM 1170 CA ARG A 147 3.398 36.794 60.316 1.00 59.30 C ANISOU 1170 CA ARG A 147 7348 7851 7331 68 156 -835 C ATOM 1171 C ARG A 147 2.798 36.030 59.136 1.00 69.20 C ANISOU 1171 C ARG A 147 8637 9047 8610 57 193 -746 C ATOM 1172 O ARG A 147 1.592 36.093 58.885 1.00 72.32 O ANISOU 1172 O ARG A 147 9064 9399 9016 54 220 -718 O ATOM 1173 CB ARG A 147 3.797 35.815 61.425 1.00 63.29 C ANISOU 1173 CB ARG A 147 7849 8455 7744 129 140 -828 C ATOM 1174 N PHE A 148 3.660 35.306 58.423 1.00 71.62 N ANISOU 1174 N PHE A 148 8935 9355 8924 50 194 -705 N ATOM 1175 CA PHE A 148 3.273 34.543 57.236 1.00 65.21 C ANISOU 1175 CA PHE A 148 8151 8491 8135 37 226 -627 C ATOM 1176 C PHE A 148 2.848 33.146 57.680 1.00 64.08 C ANISOU 1176 C PHE A 148 8035 8388 7924 85 246 -568 C ATOM 1177 O PHE A 148 3.687 32.334 58.084 1.00 67.11 O ANISOU 1177 O PHE A 148 8408 8828 8264 116 236 -553 O ATOM 1178 CB PHE A 148 4.439 34.485 56.251 1.00 59.85 C ANISOU 1178 CB PHE A 148 7449 7792 7500 8 220 -615 C ATOM 1179 CG PHE A 148 4.031 34.235 54.825 1.00 57.18 C ANISOU 1179 CG PHE A 148 7134 7383 7208 -21 251 -556 C ATOM 1180 CD1 PHE A 148 3.465 33.029 54.446 1.00 56.56 C ANISOU 1180 CD1 PHE A 148 7088 7301 7100 -1 277 -488 C ATOM 1181 CD2 PHE A 148 4.261 35.195 53.853 1.00 55.75 C ANISOU 1181 CD2 PHE A 148 6940 7142 7100 -66 254 -570 C ATOM 1182 CE1 PHE A 148 3.110 32.796 53.126 1.00 55.37 C ANISOU 1182 CE1 PHE A 148 6956 7092 6990 -27 302 -440 C ATOM 1183 CE2 PHE A 148 3.908 34.971 52.534 1.00 55.69 C ANISOU 1183 CE2 PHE A 148 6953 7078 7130 -87 280 -516 C ATOM 1184 CZ PHE A 148 3.327 33.772 52.170 1.00 55.34 C ANISOU 1184 CZ PHE A 148 6940 7035 7052 -68 302 -454 C ATOM 1185 N GLY A 149 1.546 32.864 57.603 1.00 51.42 N ANISOU 1185 N GLY A 149 6466 6755 6315 92 275 -533 N ATOM 1186 CA GLY A 149 0.988 31.628 58.092 1.00 42.92 C ANISOU 1186 CA GLY A 149 5416 5709 5181 136 300 -480 C ATOM 1187 C GLY A 149 0.457 30.736 56.989 1.00 47.39 C ANISOU 1187 C GLY A 149 6011 6225 5772 121 336 -410 C ATOM 1188 O GLY A 149 0.776 30.901 55.804 1.00 42.24 O ANISOU 1188 O GLY A 149 5354 5525 5170 83 337 -398 O ATOM 1189 N GLU A 150 -0.374 29.765 57.391 1.00 43.22 N ANISOU 1189 N GLU A 150 5509 5707 5206 153 367 -366 N ATOM 1190 CA GLU A 150 -0.934 28.810 56.436 1.00 42.06 C ANISOU 1190 CA GLU A 150 5387 5516 5079 141 402 -304 C ATOM 1191 C GLU A 150 -1.823 29.505 55.413 1.00 38.92 C ANISOU 1191 C GLU A 150 4996 5052 4739 96 410 -307 C ATOM 1192 O GLU A 150 -1.722 29.243 54.208 1.00 34.98 O ANISOU 1192 O GLU A 150 4502 4512 4277 67 419 -280 O ATOM 1193 CB GLU A 150 -1.727 27.723 57.167 1.00 48.01 C ANISOU 1193 CB GLU A 150 6165 6290 5787 182 438 -262 C ATOM 1194 CG GLU A 150 -0.911 26.799 58.045 1.00 46.70 C ANISOU 1194 CG GLU A 150 5997 6186 5561 233 441 -240 C ATOM 1195 CD GLU A 150 -1.679 25.539 58.406 1.00 50.04 C ANISOU 1195 CD GLU A 150 6448 6609 5956 267 490 -181 C ATOM 1196 OE1 GLU A 150 -2.406 25.017 57.535 1.00 45.88 O ANISOU 1196 OE1 GLU A 150 5940 6028 5466 241 521 -147 O ATOM 1197 OE2 GLU A 150 -1.570 25.074 59.560 1.00 46.87 O ANISOU 1197 OE2 GLU A 150 6049 6263 5495 322 498 -170 O ATOM 1198 N ASN A 151 -2.701 30.403 55.876 1.00 37.97 N ANISOU 1198 N ASN A 151 4878 4925 4625 93 406 -340 N ATOM 1199 CA ASN A 151 -3.603 31.097 54.961 1.00 33.56 C ANISOU 1199 CA ASN A 151 4325 4308 4118 58 415 -340 C ATOM 1200 C ASN A 151 -2.824 31.859 53.901 1.00 31.95 C ANISOU 1200 C ASN A 151 4104 4069 3966 19 396 -356 C ATOM 1201 O ASN A 151 -3.212 31.882 52.727 1.00 31.79 O ANISOU 1201 O ASN A 151 4091 4003 3984 -8 409 -331 O ATOM 1202 CB ASN A 151 -4.519 32.047 55.734 1.00 38.47 C ANISOU 1202 CB ASN A 151 4948 4932 4738 65 412 -378 C ATOM 1203 CG ASN A 151 -5.409 31.327 56.729 1.00 44.91 C ANISOU 1203 CG ASN A 151 5780 5778 5505 104 436 -358 C ATOM 1204 OD1 ASN A 151 -5.576 30.106 56.667 1.00 38.87 O ANISOU 1204 OD1 ASN A 151 5030 5021 4720 119 461 -310 O ATOM 1205 ND2 ASN A 151 -5.985 32.082 57.657 1.00 40.46 N ANISOU 1205 ND2 ASN A 151 5215 5231 4925 120 431 -395 N ATOM 1206 N HIS A 152 -1.716 32.485 54.298 1.00 28.37 N ANISOU 1206 N HIS A 152 3626 3638 3514 17 368 -398 N ATOM 1207 CA HIS A 152 -0.886 33.188 53.329 1.00 40.50 C ANISOU 1207 CA HIS A 152 5145 5141 5103 -19 355 -412 C ATOM 1208 C HIS A 152 -0.173 32.219 52.392 1.00 39.54 C ANISOU 1208 C HIS A 152 5026 5013 4985 -25 364 -365 C ATOM 1209 O HIS A 152 0.126 32.575 51.248 1.00 23.62 O ANISOU 1209 O HIS A 152 3004 2955 3015 -55 366 -354 O ATOM 1210 CB HIS A 152 0.126 34.076 54.060 1.00 38.59 C ANISOU 1210 CB HIS A 152 4872 4927 4865 -21 324 -474 C ATOM 1211 CG HIS A 152 -0.502 35.069 54.991 1.00 48.47 C ANISOU 1211 CG HIS A 152 6119 6184 6113 -14 315 -527 C ATOM 1212 ND1 HIS A 152 -0.298 35.045 56.354 1.00 47.52 N ANISOU 1212 ND1 HIS A 152 5990 6125 5941 18 297 -566 N ATOM 1213 CD2 HIS A 152 -1.331 36.113 54.752 1.00 47.34 C ANISOU 1213 CD2 HIS A 152 5980 5995 6010 -34 323 -547 C ATOM 1214 CE1 HIS A 152 -0.974 36.032 56.916 1.00 59.24 C ANISOU 1214 CE1 HIS A 152 7474 7599 7434 17 294 -611 C ATOM 1215 NE2 HIS A 152 -1.611 36.694 55.966 1.00 53.14 N ANISOU 1215 NE2 HIS A 152 6710 6760 6720 -14 311 -600 N ATOM 1216 N ALA A 153 0.120 31.003 52.860 1.00 37.70 N ANISOU 1216 N ALA A 153 4801 4819 4705 5 371 -336 N ATOM 1217 CA ALA A 153 0.761 30.012 52.001 1.00 34.78 C ANISOU 1217 CA ALA A 153 4436 4442 4337 1 383 -292 C ATOM 1218 C ALA A 153 -0.209 29.477 50.953 1.00 33.05 C ANISOU 1218 C ALA A 153 4242 4177 4139 -14 412 -249 C ATOM 1219 O ALA A 153 0.136 29.373 49.769 1.00 29.34 O ANISOU 1219 O ALA A 153 3772 3676 3699 -38 417 -228 O ATOM 1220 CB ALA A 153 1.324 28.872 52.852 1.00 27.30 C ANISOU 1220 CB ALA A 153 3490 3547 3333 43 387 -271 C ATOM 1221 N ILE A 154 -1.431 29.134 51.370 1.00 29.14 N ANISOU 1221 N ILE A 154 3766 3680 3625 -2 431 -237 N ATOM 1222 CA ILE A 154 -2.430 28.627 50.434 1.00 26.46 C ANISOU 1222 CA ILE A 154 3446 3303 3305 -18 457 -203 C ATOM 1223 C ILE A 154 -2.817 29.705 49.431 1.00 28.20 C ANISOU 1223 C ILE A 154 3660 3481 3572 -50 449 -216 C ATOM 1224 O ILE A 154 -3.050 29.422 48.249 1.00 30.20 O ANISOU 1224 O ILE A 154 3921 3705 3849 -69 460 -191 O ATOM 1225 CB ILE A 154 -3.654 28.099 51.203 1.00 42.04 C ANISOU 1225 CB ILE A 154 5436 5285 5251 3 480 -192 C ATOM 1226 CG1 ILE A 154 -3.230 27.005 52.185 1.00 38.65 C ANISOU 1226 CG1 ILE A 154 5014 4896 4774 41 493 -172 C ATOM 1227 CG2 ILE A 154 -4.707 27.571 50.241 1.00 43.82 C ANISOU 1227 CG2 ILE A 154 5676 5474 5500 -16 504 -163 C ATOM 1228 CD1 ILE A 154 -4.305 26.641 53.189 1.00 45.90 C ANISOU 1228 CD1 ILE A 154 5945 5830 5664 68 516 -164 C ATOM 1229 N MET A 155 -2.882 30.959 49.883 1.00 32.28 N ANISOU 1229 N MET A 155 4164 3996 4105 -55 431 -256 N ATOM 1230 CA MET A 155 -3.148 32.061 48.967 1.00 25.21 C ANISOU 1230 CA MET A 155 3262 3060 3258 -82 428 -265 C ATOM 1231 C MET A 155 -2.029 32.198 47.943 1.00 34.58 C ANISOU 1231 C MET A 155 4438 4229 4474 -102 422 -256 C ATOM 1232 O MET A 155 -2.278 32.521 46.775 1.00 28.63 O ANISOU 1232 O MET A 155 3687 3440 3752 -120 430 -238 O ATOM 1233 CB MET A 155 -3.326 33.358 49.754 1.00 36.08 C ANISOU 1233 CB MET A 155 4626 4434 4647 -82 414 -313 C ATOM 1234 CG MET A 155 -3.963 34.484 48.964 1.00 41.27 C ANISOU 1234 CG MET A 155 5281 5046 5352 -102 419 -318 C ATOM 1235 SD MET A 155 -3.742 36.070 49.791 1.00 53.27 S ANISOU 1235 SD MET A 155 6784 6558 6900 -106 403 -379 S ATOM 1236 CE MET A 155 -4.007 35.611 51.502 1.00 43.32 C ANISOU 1236 CE MET A 155 5527 5353 5580 -74 395 -408 C ATOM 1237 N GLY A 156 -0.783 31.965 48.369 1.00 25.07 N ANISOU 1237 N GLY A 156 3219 3050 3257 -96 408 -267 N ATOM 1238 CA GLY A 156 0.326 31.961 47.427 1.00 29.84 C ANISOU 1238 CA GLY A 156 3810 3640 3886 -112 405 -254 C ATOM 1239 C GLY A 156 0.231 30.827 46.426 1.00 25.97 C ANISOU 1239 C GLY A 156 3338 3140 3387 -112 424 -206 C ATOM 1240 O GLY A 156 0.551 30.999 45.246 1.00 28.73 O ANISOU 1240 O GLY A 156 3688 3463 3767 -130 430 -188 O ATOM 1241 N VAL A 157 -0.222 29.656 46.878 1.00 30.71 N ANISOU 1241 N VAL A 157 3957 3762 3949 -93 437 -186 N ATOM 1242 CA VAL A 157 -0.362 28.513 45.981 1.00 32.04 C ANISOU 1242 CA VAL A 157 4143 3918 4112 -94 458 -146 C ATOM 1243 C VAL A 157 -1.369 28.822 44.882 1.00 33.79 C ANISOU 1243 C VAL A 157 4374 4105 4358 -114 468 -135 C ATOM 1244 O VAL A 157 -1.102 28.610 43.693 1.00 21.91 O ANISOU 1244 O VAL A 157 2872 2582 2869 -126 475 -114 O ATOM 1245 CB VAL A 157 -0.764 27.258 46.775 1.00 21.01 C ANISOU 1245 CB VAL A 157 2762 2545 2674 -70 476 -128 C ATOM 1246 CG1 VAL A 157 -1.279 26.189 45.831 1.00 40.06 C ANISOU 1246 CG1 VAL A 157 5194 4936 5089 -77 502 -95 C ATOM 1247 CG2 VAL A 157 0.417 26.748 47.579 1.00 24.46 C ANISOU 1247 CG2 VAL A 157 3191 3020 3083 -45 469 -127 C ATOM 1248 N ALA A 158 -2.540 29.339 45.264 1.00 29.29 N ANISOU 1248 N ALA A 158 3808 3531 3792 -113 469 -148 N ATOM 1249 CA ALA A 158 -3.524 29.746 44.268 1.00 25.36 C ANISOU 1249 CA ALA A 158 3313 3005 3315 -128 476 -139 C ATOM 1250 C ALA A 158 -2.962 30.834 43.365 1.00 29.77 C ANISOU 1250 C ALA A 158 3860 3540 3910 -142 467 -142 C ATOM 1251 O ALA A 158 -3.249 30.867 42.162 1.00 20.15 O ANISOU 1251 O ALA A 158 2645 2305 2706 -151 474 -122 O ATOM 1252 CB ALA A 158 -4.804 30.222 44.956 1.00 21.62 C ANISOU 1252 CB ALA A 158 2842 2533 2839 -122 478 -155 C ATOM 1253 N PHE A 159 -2.149 31.729 43.931 1.00 24.12 N ANISOU 1253 N PHE A 159 3129 2826 3211 -144 453 -167 N ATOM 1254 CA PHE A 159 -1.550 32.806 43.150 1.00 27.40 C ANISOU 1254 CA PHE A 159 3530 3213 3667 -159 450 -169 C ATOM 1255 C PHE A 159 -0.622 32.263 42.069 1.00 27.41 C ANISOU 1255 C PHE A 159 3531 3209 3674 -165 457 -140 C ATOM 1256 O PHE A 159 -0.588 32.789 40.951 1.00 21.38 O ANISOU 1256 O PHE A 159 2766 2420 2938 -173 465 -123 O ATOM 1257 CB PHE A 159 -0.803 33.759 44.085 1.00 28.42 C ANISOU 1257 CB PHE A 159 3639 3344 3815 -162 435 -209 C ATOM 1258 CG PHE A 159 -0.089 34.876 43.378 1.00 32.84 C ANISOU 1258 CG PHE A 159 4182 3871 4426 -179 438 -214 C ATOM 1259 CD1 PHE A 159 -0.781 35.994 42.937 1.00 18.79 C ANISOU 1259 CD1 PHE A 159 2402 2056 2681 -185 448 -215 C ATOM 1260 CD2 PHE A 159 1.279 34.815 43.168 1.00 34.31 C ANISOU 1260 CD2 PHE A 159 4351 4060 4626 -188 433 -215 C ATOM 1261 CE1 PHE A 159 -0.120 37.025 42.292 1.00 45.86 C ANISOU 1261 CE1 PHE A 159 5815 5449 6161 -199 456 -216 C ATOM 1262 CE2 PHE A 159 1.945 35.842 42.526 1.00 33.58 C ANISOU 1262 CE2 PHE A 159 4241 3933 4585 -205 440 -217 C ATOM 1263 CZ PHE A 159 1.245 36.948 42.086 1.00 36.83 C ANISOU 1263 CZ PHE A 159 4654 4306 5034 -210 454 -217 C ATOM 1264 N THR A 160 0.143 31.212 42.382 1.00 25.52 N ANISOU 1264 N THR A 160 3294 2994 3409 -158 455 -133 N ATOM 1265 CA THR A 160 1.057 30.651 41.389 1.00 25.19 C ANISOU 1265 CA THR A 160 3253 2948 3371 -161 463 -106 C ATOM 1266 C THR A 160 0.299 30.099 40.189 1.00 18.80 C ANISOU 1266 C THR A 160 2462 2126 2556 -163 478 -77 C ATOM 1267 O THR A 160 0.736 30.259 39.045 1.00 24.33 O ANISOU 1267 O THR A 160 3161 2812 3273 -168 486 -57 O ATOM 1268 CB THR A 160 1.928 29.558 42.011 1.00 21.27 C ANISOU 1268 CB THR A 160 2756 2480 2844 -148 461 -102 C ATOM 1269 OG1 THR A 160 1.103 28.464 42.431 1.00 18.85 O ANISOU 1269 OG1 THR A 160 2470 2189 2504 -135 472 -92 O ATOM 1270 CG2 THR A 160 2.702 30.100 43.200 1.00 21.20 C ANISOU 1270 CG2 THR A 160 2725 2494 2837 -144 442 -135 C ATOM 1271 N TRP A 161 -0.837 29.441 40.430 1.00 24.26 N ANISOU 1271 N TRP A 161 3169 2826 3224 -158 484 -76 N ATOM 1272 CA TRP A 161 -1.604 28.868 39.328 1.00 27.52 C ANISOU 1272 CA TRP A 161 3594 3231 3630 -161 496 -56 C ATOM 1273 C TRP A 161 -2.190 29.948 38.426 1.00 21.38 C ANISOU 1273 C TRP A 161 2812 2436 2876 -165 495 -51 C ATOM 1274 O TRP A 161 -2.171 29.813 37.197 1.00 33.88 O ANISOU 1274 O TRP A 161 4399 4015 4460 -166 502 -31 O ATOM 1275 CB TRP A 161 -2.704 27.962 39.874 1.00 23.42 C ANISOU 1275 CB TRP A 161 3088 2724 3087 -157 504 -60 C ATOM 1276 CG TRP A 161 -2.197 26.625 40.288 1.00 23.23 C ANISOU 1276 CG TRP A 161 3074 2711 3040 -150 516 -51 C ATOM 1277 CD1 TRP A 161 -1.682 26.282 41.502 1.00 20.34 C ANISOU 1277 CD1 TRP A 161 2708 2362 2658 -136 515 -57 C ATOM 1278 CD2 TRP A 161 -2.146 25.446 39.481 1.00 15.47 C ANISOU 1278 CD2 TRP A 161 2106 1726 2048 -152 533 -35 C ATOM 1279 NE1 TRP A 161 -1.317 24.957 41.502 1.00 25.56 N ANISOU 1279 NE1 TRP A 161 3382 3029 3301 -128 533 -40 N ATOM 1280 CE2 TRP A 161 -1.594 24.421 40.273 1.00 21.30 C ANISOU 1280 CE2 TRP A 161 2851 2474 2767 -140 545 -28 C ATOM 1281 CE3 TRP A 161 -2.516 25.157 38.164 1.00 35.32 C ANISOU 1281 CE3 TRP A 161 4624 4230 4564 -162 539 -26 C ATOM 1282 CZ2 TRP A 161 -1.400 23.128 39.791 1.00 25.08 C ANISOU 1282 CZ2 TRP A 161 3345 2948 3237 -139 567 -12 C ATOM 1283 CZ3 TRP A 161 -2.325 23.873 37.689 1.00 26.69 C ANISOU 1283 CZ3 TRP A 161 3545 3136 3460 -162 557 -17 C ATOM 1284 CH2 TRP A 161 -1.774 22.875 38.500 1.00 23.75 C ANISOU 1284 CH2 TRP A 161 3182 2766 3074 -152 572 -10 C ATOM 1285 N VAL A 162 -2.720 31.023 39.015 1.00 25.33 N ANISOU 1285 N VAL A 162 3303 2928 3393 -165 488 -69 N ATOM 1286 CA VAL A 162 -3.285 32.106 38.214 1.00 18.08 C ANISOU 1286 CA VAL A 162 2380 1992 2498 -164 491 -60 C ATOM 1287 C VAL A 162 -2.202 32.751 37.360 1.00 26.37 C ANISOU 1287 C VAL A 162 3421 3023 3575 -167 496 -44 C ATOM 1288 O VAL A 162 -2.381 32.968 36.155 1.00 23.97 O ANISOU 1288 O VAL A 162 3119 2712 3275 -162 505 -19 O ATOM 1289 CB VAL A 162 -3.978 33.143 39.118 1.00 32.71 C ANISOU 1289 CB VAL A 162 4225 3836 4367 -162 486 -84 C ATOM 1290 CG1 VAL A 162 -4.481 34.319 38.290 1.00 23.90 C ANISOU 1290 CG1 VAL A 162 3104 2698 3279 -157 493 -71 C ATOM 1291 CG2 VAL A 162 -5.116 32.500 39.894 1.00 26.07 C ANISOU 1291 CG2 VAL A 162 3391 3013 3499 -157 484 -96 C ATOM 1292 N MET A 163 -1.055 33.057 37.973 1.00 16.94 N ANISOU 1292 N MET A 163 2215 1823 2398 -174 492 -57 N ATOM 1293 CA MET A 163 0.047 33.655 37.225 1.00 30.65 C ANISOU 1293 CA MET A 163 3940 3539 4166 -179 500 -42 C ATOM 1294 C MET A 163 0.578 32.699 36.164 1.00 24.00 C ANISOU 1294 C MET A 163 3107 2707 3305 -175 509 -12 C ATOM 1295 O MET A 163 0.895 33.120 35.046 1.00 25.92 O ANISOU 1295 O MET A 163 3349 2936 3565 -172 522 14 O ATOM 1296 CB MET A 163 1.164 34.080 38.177 1.00 23.66 C ANISOU 1296 CB MET A 163 3036 2652 3304 -189 491 -70 C ATOM 1297 CG MET A 163 0.747 35.163 39.161 1.00 29.05 C ANISOU 1297 CG MET A 163 3708 3321 4009 -194 484 -105 C ATOM 1298 SD MET A 163 -0.018 36.575 38.336 1.00 32.11 S ANISOU 1298 SD MET A 163 4095 3667 4440 -192 503 -91 S ATOM 1299 CE MET A 163 1.364 37.199 37.386 1.00 29.56 C ANISOU 1299 CE MET A 163 3754 3314 4164 -202 521 -70 C ATOM 1300 N ALA A 164 0.689 31.410 36.498 1.00 17.60 N ANISOU 1300 N ALA A 164 2307 1920 2460 -173 505 -14 N ATOM 1301 CA ALA A 164 1.157 30.435 35.517 1.00 22.94 C ANISOU 1301 CA ALA A 164 2994 2604 3118 -169 515 10 C ATOM 1302 C ALA A 164 0.188 30.318 34.349 1.00 24.29 C ANISOU 1302 C ALA A 164 3177 2777 3276 -162 522 28 C ATOM 1303 O ALA A 164 0.609 30.232 33.190 1.00 20.69 O ANISOU 1303 O ALA A 164 2724 2319 2819 -156 533 52 O ATOM 1304 CB ALA A 164 1.357 29.073 36.178 1.00 20.21 C ANISOU 1304 CB ALA A 164 2659 2280 2741 -166 513 4 C ATOM 1305 N LEU A 165 -1.117 30.306 34.636 1.00 25.89 N ANISOU 1305 N LEU A 165 3385 2987 3467 -161 517 16 N ATOM 1306 CA LEU A 165 -2.108 30.223 33.567 1.00 22.09 C ANISOU 1306 CA LEU A 165 2910 2513 2970 -154 520 27 C ATOM 1307 C LEU A 165 -2.110 31.487 32.717 1.00 27.23 C ANISOU 1307 C LEU A 165 3553 3150 3644 -143 526 48 C ATOM 1308 O LEU A 165 -2.305 31.420 31.498 1.00 23.86 O ANISOU 1308 O LEU A 165 3129 2733 3203 -131 533 69 O ATOM 1309 CB LEU A 165 -3.494 29.962 34.156 1.00 22.40 C ANISOU 1309 CB LEU A 165 2951 2564 2995 -156 513 8 C ATOM 1310 CG LEU A 165 -3.759 28.522 34.601 1.00 15.53 C ANISOU 1310 CG LEU A 165 2092 1708 2100 -163 515 -6 C ATOM 1311 CD1 LEU A 165 -4.926 28.470 35.568 1.00 25.56 C ANISOU 1311 CD1 LEU A 165 3360 2984 3367 -166 511 -26 C ATOM 1312 CD2 LEU A 165 -4.023 27.624 33.391 1.00 27.14 C ANISOU 1312 CD2 LEU A 165 3570 3191 3549 -162 521 1 C ATOM 1313 N ALA A 166 -1.889 32.648 33.339 1.00 16.00 N ANISOU 1313 N ALA A 166 2118 1705 2256 -146 527 42 N ATOM 1314 CA ALA A 166 -1.818 33.893 32.584 1.00 29.30 C ANISOU 1314 CA ALA A 166 3795 3368 3969 -135 540 65 C ATOM 1315 C ALA A 166 -0.691 33.876 31.559 1.00 23.74 C ANISOU 1315 C ALA A 166 3090 2657 3273 -130 555 95 C ATOM 1316 O ALA A 166 -0.740 34.632 30.583 1.00 21.52 O ANISOU 1316 O ALA A 166 2807 2365 3003 -113 571 125 O ATOM 1317 CB ALA A 166 -1.648 35.077 33.538 1.00 18.28 C ANISOU 1317 CB ALA A 166 2387 1943 2615 -143 541 48 C ATOM 1318 N CYS A 167 0.321 33.033 31.760 1.00 21.42 N ANISOU 1318 N CYS A 167 2797 2369 2971 -140 553 90 N ATOM 1319 CA CYS A 167 1.399 32.864 30.796 1.00 20.27 C ANISOU 1319 CA CYS A 167 2651 2220 2829 -134 569 118 C ATOM 1320 C CYS A 167 1.135 31.695 29.854 1.00 21.47 C ANISOU 1320 C CYS A 167 2821 2401 2937 -123 570 130 C ATOM 1321 O CYS A 167 1.331 31.814 28.641 1.00 22.00 O ANISOU 1321 O CYS A 167 2892 2472 2996 -106 584 159 O ATOM 1322 CB CYS A 167 2.728 32.662 31.532 1.00 25.42 C ANISOU 1322 CB CYS A 167 3292 2864 3502 -149 568 107 C ATOM 1323 SG CYS A 167 4.179 32.490 30.474 1.00 26.97 S ANISOU 1323 SG CYS A 167 3483 3054 3708 -144 589 141 S ATOM 1324 N ALA A 168 0.683 30.564 30.399 1.00 20.47 N ANISOU 1324 N ALA A 168 2704 2293 2780 -131 557 107 N ATOM 1325 CA ALA A 168 0.615 29.331 29.623 1.00 25.79 C ANISOU 1325 CA ALA A 168 3392 2988 3417 -126 560 110 C ATOM 1326 C ALA A 168 -0.612 29.279 28.714 1.00 18.88 C ANISOU 1326 C ALA A 168 2523 2135 2516 -113 556 112 C ATOM 1327 O ALA A 168 -0.545 28.713 27.616 1.00 26.33 O ANISOU 1327 O ALA A 168 3475 3096 3433 -102 562 122 O ATOM 1328 CB ALA A 168 0.632 28.128 30.566 1.00 15.74 C ANISOU 1328 CB ALA A 168 2127 1723 2129 -139 553 86 C ATOM 1329 N ALA A 169 -1.732 29.855 29.145 1.00 22.84 N ANISOU 1329 N ALA A 169 3019 2639 3022 -114 546 99 N ATOM 1330 CA ALA A 169 -3.007 29.682 28.457 1.00 22.46 C ANISOU 1330 CA ALA A 169 2971 2618 2946 -103 538 94 C ATOM 1331 C ALA A 169 -3.167 30.467 27.152 1.00 27.11 C ANISOU 1331 C ALA A 169 3556 3218 3526 -76 545 124 C ATOM 1332 O ALA A 169 -3.740 29.923 26.199 1.00 17.21 O ANISOU 1332 O ALA A 169 2305 1997 2237 -63 541 122 O ATOM 1333 CB ALA A 169 -4.164 30.039 29.396 1.00 24.26 C ANISOU 1333 CB ALA A 169 3191 2845 3181 -111 526 72 C ATOM 1334 N PRO A 170 -2.729 31.728 27.059 1.00 28.25 N ANISOU 1334 N PRO A 170 3694 3340 3702 -64 558 152 N ATOM 1335 CA PRO A 170 -3.009 32.525 25.844 1.00 25.83 C ANISOU 1335 CA PRO A 170 3384 3045 3385 -31 569 187 C ATOM 1336 C PRO A 170 -2.527 31.863 24.562 1.00 23.46 C ANISOU 1336 C PRO A 170 3092 2771 3050 -13 577 204 C ATOM 1337 O PRO A 170 -3.243 31.916 23.553 1.00 26.97 O ANISOU 1337 O PRO A 170 3536 3252 3461 14 574 215 O ATOM 1338 CB PRO A 170 -2.269 33.844 26.105 1.00 25.33 C ANISOU 1338 CB PRO A 170 3312 2939 3372 -27 590 213 C ATOM 1339 CG PRO A 170 -2.290 33.975 27.563 1.00 30.25 C ANISOU 1339 CG PRO A 170 3930 3538 4025 -55 579 181 C ATOM 1340 CD PRO A 170 -2.149 32.581 28.115 1.00 22.80 C ANISOU 1340 CD PRO A 170 2995 2610 3056 -77 563 150 C ATOM 1341 N PRO A 171 -1.338 31.236 24.530 1.00 23.97 N ANISOU 1341 N PRO A 171 3164 2824 3119 -24 586 207 N ATOM 1342 CA PRO A 171 -0.913 30.599 23.270 1.00 23.94 C ANISOU 1342 CA PRO A 171 3171 2847 3079 -5 595 222 C ATOM 1343 C PRO A 171 -1.822 29.475 22.827 1.00 22.97 C ANISOU 1343 C PRO A 171 3053 2766 2908 -5 576 190 C ATOM 1344 O PRO A 171 -1.759 29.074 21.656 1.00 30.53 O ANISOU 1344 O PRO A 171 4017 3754 3828 17 580 198 O ATOM 1345 CB PRO A 171 0.500 30.094 23.579 1.00 21.21 C ANISOU 1345 CB PRO A 171 2829 2476 2752 -21 608 226 C ATOM 1346 CG PRO A 171 0.965 30.973 24.665 1.00 21.19 C ANISOU 1346 CG PRO A 171 2814 2434 2800 -38 611 228 C ATOM 1347 CD PRO A 171 -0.238 31.200 25.516 1.00 25.49 C ANISOU 1347 CD PRO A 171 3355 2982 3349 -49 592 201 C ATOM 1348 N LEU A 172 -2.654 28.942 23.719 1.00 28.18 N ANISOU 1348 N LEU A 172 3711 3428 3569 -29 558 152 N ATOM 1349 CA LEU A 172 -3.661 27.971 23.310 1.00 28.37 C ANISOU 1349 CA LEU A 172 3736 3490 3555 -32 542 117 C ATOM 1350 C LEU A 172 -4.831 28.616 22.578 1.00 27.74 C ANISOU 1350 C LEU A 172 3642 3447 3451 -6 530 121 C ATOM 1351 O LEU A 172 -5.516 27.930 21.812 1.00 21.29 O ANISOU 1351 O LEU A 172 2822 2672 2594 1 518 98 O ATOM 1352 CB LEU A 172 -4.179 27.207 24.528 1.00 16.55 C ANISOU 1352 CB LEU A 172 2238 1978 2071 -66 532 78 C ATOM 1353 CG LEU A 172 -3.225 26.247 25.241 1.00 24.01 C ANISOU 1353 CG LEU A 172 3196 2896 3030 -89 542 67 C ATOM 1354 CD1 LEU A 172 -3.863 25.718 26.513 1.00 27.04 C ANISOU 1354 CD1 LEU A 172 3579 3268 3428 -115 536 37 C ATOM 1355 CD2 LEU A 172 -2.853 25.104 24.313 1.00 24.33 C ANISOU 1355 CD2 LEU A 172 3250 2954 3041 -87 550 56 C ATOM 1356 N VAL A 173 -5.085 29.906 22.793 1.00 25.06 N ANISOU 1356 N VAL A 173 3294 3096 3134 10 534 149 N ATOM 1357 CA VAL A 173 -6.340 30.500 22.341 1.00 30.34 C ANISOU 1357 CA VAL A 173 3947 3800 3782 34 522 152 C ATOM 1358 C VAL A 173 -6.115 31.742 21.488 1.00 32.31 C ANISOU 1358 C VAL A 173 4193 4053 4030 78 539 205 C ATOM 1359 O VAL A 173 -6.991 32.610 21.409 1.00 27.23 O ANISOU 1359 O VAL A 173 3537 3422 3386 101 536 219 O ATOM 1360 CB VAL A 173 -7.237 30.840 23.543 1.00 23.60 C ANISOU 1360 CB VAL A 173 3082 2929 2954 15 511 131 C ATOM 1361 CG1 VAL A 173 -7.744 29.567 24.195 1.00 19.27 C ANISOU 1361 CG1 VAL A 173 2534 2389 2400 -20 496 80 C ATOM 1362 CG2 VAL A 173 -6.465 31.677 24.530 1.00 18.51 C ANISOU 1362 CG2 VAL A 173 2443 2231 2361 3 526 149 C ATOM 1363 N GLY A 174 -4.951 31.843 20.848 1.00 27.69 N ANISOU 1363 N GLY A 174 3619 3455 3446 91 561 237 N ATOM 1364 CA GLY A 174 -4.761 32.817 19.791 1.00 26.94 C ANISOU 1364 CA GLY A 174 3523 3372 3341 138 582 290 C ATOM 1365 C GLY A 174 -3.845 33.986 20.087 1.00 23.78 C ANISOU 1365 C GLY A 174 3124 2916 2995 143 614 335 C ATOM 1366 O GLY A 174 -3.687 34.852 19.217 1.00 28.13 O ANISOU 1366 O GLY A 174 3674 3472 3543 185 638 384 O ATOM 1367 N TRP A 175 -3.245 34.067 21.272 1.00 22.88 N ANISOU 1367 N TRP A 175 3011 2752 2931 104 617 319 N ATOM 1368 CA TRP A 175 -2.204 35.058 21.546 1.00 20.14 C ANISOU 1368 CA TRP A 175 2662 2351 2640 102 648 352 C ATOM 1369 C TRP A 175 -0.886 34.297 21.597 1.00 23.01 C ANISOU 1369 C TRP A 175 3033 2699 3012 80 655 347 C ATOM 1370 O TRP A 175 -0.597 33.612 22.582 1.00 25.12 O ANISOU 1370 O TRP A 175 3301 2952 3291 43 639 310 O ATOM 1371 CB TRP A 175 -2.461 35.827 22.837 1.00 25.49 C ANISOU 1371 CB TRP A 175 3330 2985 3369 78 646 335 C ATOM 1372 CG TRP A 175 -1.564 37.018 22.968 1.00 30.38 C ANISOU 1372 CG TRP A 175 3944 3550 4048 79 680 369 C ATOM 1373 CD1 TRP A 175 -0.867 37.628 21.964 1.00 25.22 C ANISOU 1373 CD1 TRP A 175 3292 2886 3407 109 715 421 C ATOM 1374 CD2 TRP A 175 -1.253 37.738 24.167 1.00 22.85 C ANISOU 1374 CD2 TRP A 175 2981 2545 3155 50 685 351 C ATOM 1375 NE1 TRP A 175 -0.146 38.684 22.462 1.00 27.67 N ANISOU 1375 NE1 TRP A 175 3592 3136 3785 97 744 436 N ATOM 1376 CE2 TRP A 175 -0.364 38.774 23.812 1.00 29.57 C ANISOU 1376 CE2 TRP A 175 3826 3353 4057 60 724 390 C ATOM 1377 CE3 TRP A 175 -1.640 37.608 25.504 1.00 19.52 C ANISOU 1377 CE3 TRP A 175 2556 2112 2750 17 661 304 C ATOM 1378 CZ2 TRP A 175 0.146 39.674 24.745 1.00 29.09 C ANISOU 1378 CZ2 TRP A 175 3753 3236 4064 34 738 378 C ATOM 1379 CZ3 TRP A 175 -1.132 38.506 26.431 1.00 31.96 C ANISOU 1379 CZ3 TRP A 175 4121 3637 4386 -4 673 293 C ATOM 1380 CH2 TRP A 175 -0.249 39.526 26.046 1.00 23.77 C ANISOU 1380 CH2 TRP A 175 3075 2555 3400 3 711 327 C ATOM 1381 N SER A 176 -0.090 34.433 20.533 1.00 23.17 N ANISOU 1381 N SER A 176 3057 2723 3023 107 681 388 N ATOM 1382 CA SER A 176 1.066 33.585 20.259 1.00 19.83 C ANISOU 1382 CA SER A 176 2642 2299 2593 96 689 388 C ATOM 1383 C SER A 176 0.606 32.152 20.015 1.00 29.30 C ANISOU 1383 C SER A 176 3853 3543 3736 90 662 349 C ATOM 1384 O SER A 176 -0.575 31.918 19.733 1.00 24.13 O ANISOU 1384 O SER A 176 3198 2926 3043 102 641 330 O ATOM 1385 CB SER A 176 2.093 33.649 21.393 1.00 24.89 C ANISOU 1385 CB SER A 176 3275 2891 3289 57 693 373 C ATOM 1386 OG SER A 176 3.328 33.087 20.989 1.00 20.75 O ANISOU 1386 OG SER A 176 2755 2363 2765 55 709 386 O ATOM 1387 N ARG A 177 1.520 31.191 20.120 1.00 22.58 N ANISOU 1387 N ARG A 177 3010 2687 2882 72 664 335 N ATOM 1388 CA ARG A 177 1.209 29.802 19.805 1.00 21.35 C ANISOU 1388 CA ARG A 177 2866 2567 2678 66 646 299 C ATOM 1389 C ARG A 177 2.367 28.924 20.250 1.00 28.75 C ANISOU 1389 C ARG A 177 3811 3483 3630 42 653 288 C ATOM 1390 O ARG A 177 3.498 29.391 20.414 1.00 30.63 O ANISOU 1390 O ARG A 177 4043 3690 3904 40 674 316 O ATOM 1391 CB ARG A 177 0.945 29.608 18.307 1.00 25.39 C ANISOU 1391 CB ARG A 177 3386 3127 3135 107 651 316 C ATOM 1392 CG ARG A 177 2.073 30.090 17.410 1.00 19.78 C ANISOU 1392 CG ARG A 177 2678 2408 2428 136 686 368 C ATOM 1393 CD ARG A 177 1.698 29.966 15.940 1.00 26.04 C ANISOU 1393 CD ARG A 177 3478 3256 3159 183 690 385 C ATOM 1394 NE ARG A 177 2.798 30.344 15.059 1.00 18.79 N ANISOU 1394 NE ARG A 177 2565 2333 2243 214 727 437 N ATOM 1395 CZ ARG A 177 2.756 30.264 13.736 1.00 26.93 C ANISOU 1395 CZ ARG A 177 3604 3410 3220 261 738 460 C ATOM 1396 NH1 ARG A 177 1.676 29.837 13.103 1.00 19.38 N ANISOU 1396 NH1 ARG A 177 2648 2512 2202 282 712 433 N ATOM 1397 NH2 ARG A 177 3.828 30.616 13.031 1.00 23.48 N ANISOU 1397 NH2 ARG A 177 3170 2962 2788 288 776 511 N ATOM 1398 N TYR A 178 2.067 27.645 20.445 1.00 24.43 N ANISOU 1398 N TYR A 178 3274 2951 3056 25 638 248 N ATOM 1399 CA TYR A 178 3.098 26.650 20.695 1.00 24.43 C ANISOU 1399 CA TYR A 178 3283 2937 3060 10 648 239 C ATOM 1400 C TYR A 178 3.569 26.078 19.367 1.00 23.02 C ANISOU 1400 C TYR A 178 3119 2786 2844 37 663 252 C ATOM 1401 O TYR A 178 2.754 25.676 18.531 1.00 19.83 O ANISOU 1401 O TYR A 178 2721 2420 2395 52 653 234 O ATOM 1402 CB TYR A 178 2.582 25.545 21.613 1.00 16.77 C ANISOU 1402 CB TYR A 178 2320 1965 2087 -20 631 192 C ATOM 1403 CG TYR A 178 2.359 26.029 23.024 1.00 24.36 C ANISOU 1403 CG TYR A 178 3270 2900 3087 -44 619 182 C ATOM 1404 CD1 TYR A 178 3.426 26.456 23.803 1.00 19.91 C ANISOU 1404 CD1 TYR A 178 2698 2307 2562 -54 628 198 C ATOM 1405 CD2 TYR A 178 1.085 26.077 23.575 1.00 28.60 C ANISOU 1405 CD2 TYR A 178 3802 3444 3619 -56 599 154 C ATOM 1406 CE1 TYR A 178 3.233 26.910 25.088 1.00 16.27 C ANISOU 1406 CE1 TYR A 178 2226 1826 2131 -74 616 185 C ATOM 1407 CE2 TYR A 178 0.881 26.527 24.865 1.00 20.81 C ANISOU 1407 CE2 TYR A 178 2806 2435 2664 -75 590 144 C ATOM 1408 CZ TYR A 178 1.959 26.941 25.616 1.00 19.54 C ANISOU 1408 CZ TYR A 178 2639 2248 2538 -83 598 159 C ATOM 1409 OH TYR A 178 1.763 27.392 26.900 1.00 17.19 O ANISOU 1409 OH TYR A 178 2332 1933 2268 -100 587 145 O ATOM 1410 N ILE A 179 4.883 26.052 19.176 1.00 21.27 N ANISOU 1410 N ILE A 179 2898 2546 2637 43 686 280 N ATOM 1411 CA ILE A 179 5.465 25.667 17.895 1.00 18.99 C ANISOU 1411 CA ILE A 179 2622 2280 2315 72 706 300 C ATOM 1412 C ILE A 179 6.636 24.735 18.189 1.00 24.04 C ANISOU 1412 C ILE A 179 3268 2901 2965 60 721 298 C ATOM 1413 O ILE A 179 7.304 24.900 19.217 1.00 17.25 O ANISOU 1413 O ILE A 179 2398 2009 2148 38 723 302 O ATOM 1414 CB ILE A 179 5.878 26.920 17.091 1.00 23.66 C ANISOU 1414 CB ILE A 179 3203 2871 2914 105 730 356 C ATOM 1415 CG1 ILE A 179 6.311 26.548 15.672 1.00 18.19 C ANISOU 1415 CG1 ILE A 179 2525 2211 2177 144 750 377 C ATOM 1416 CG2 ILE A 179 6.983 27.674 17.803 1.00 22.99 C ANISOU 1416 CG2 ILE A 179 3102 2741 2891 91 748 386 C ATOM 1417 CD1 ILE A 179 6.693 27.737 14.834 1.00 27.12 C ANISOU 1417 CD1 ILE A 179 3648 3343 3313 181 779 437 C ATOM 1418 N PRO A 180 6.903 23.727 17.348 1.00 17.60 N ANISOU 1418 N PRO A 180 2470 2106 2112 75 732 288 N ATOM 1419 CA PRO A 180 8.033 22.825 17.616 1.00 17.52 C ANISOU 1419 CA PRO A 180 2468 2078 2113 67 749 288 C ATOM 1420 C PRO A 180 9.370 23.558 17.606 1.00 17.59 C ANISOU 1420 C PRO A 180 2462 2065 2157 76 774 337 C ATOM 1421 O PRO A 180 9.557 24.546 16.891 1.00 17.92 O ANISOU 1421 O PRO A 180 2496 2112 2202 100 788 375 O ATOM 1422 CB PRO A 180 7.949 21.802 16.483 1.00 24.96 C ANISOU 1422 CB PRO A 180 3432 3050 3004 87 758 270 C ATOM 1423 CG PRO A 180 6.509 21.777 16.106 1.00 23.14 C ANISOU 1423 CG PRO A 180 3203 2850 2738 89 733 235 C ATOM 1424 CD PRO A 180 6.030 23.196 16.285 1.00 23.40 C ANISOU 1424 CD PRO A 180 3219 2884 2790 94 723 263 C ATOM 1425 N GLU A 181 10.310 23.050 18.404 1.00 20.49 N ANISOU 1425 N GLU A 181 2824 2408 2552 60 781 336 N ATOM 1426 CA GLU A 181 11.621 23.667 18.564 1.00 22.33 C ANISOU 1426 CA GLU A 181 3038 2621 2825 63 802 375 C ATOM 1427 C GLU A 181 12.728 22.653 18.318 1.00 19.29 C ANISOU 1427 C GLU A 181 2661 2236 2433 73 824 383 C ATOM 1428 O GLU A 181 12.574 21.461 18.595 1.00 19.24 O ANISOU 1428 O GLU A 181 2672 2233 2406 66 820 353 O ATOM 1429 CB GLU A 181 11.816 24.258 19.966 1.00 23.98 C ANISOU 1429 CB GLU A 181 3222 2804 3084 33 787 369 C ATOM 1430 CG GLU A 181 10.849 25.362 20.343 1.00 25.80 C ANISOU 1430 CG GLU A 181 3442 3028 3332 23 768 363 C ATOM 1431 CD GLU A 181 11.317 26.125 21.563 1.00 20.59 C ANISOU 1431 CD GLU A 181 2755 2343 2726 -2 760 361 C ATOM 1432 OE1 GLU A 181 12.114 27.071 21.399 1.00 27.73 O ANISOU 1432 OE1 GLU A 181 3638 3230 3669 0 778 391 O ATOM 1433 OE2 GLU A 181 10.911 25.760 22.687 1.00 26.70 O ANISOU 1433 OE2 GLU A 181 3527 3113 3503 -24 737 328 O ATOM 1434 N GLY A 182 13.853 23.149 17.813 1.00 20.24 N ANISOU 1434 N GLY A 182 2767 2350 2572 89 851 424 N ATOM 1435 CA GLY A 182 15.040 22.321 17.676 1.00 18.24 C ANISOU 1435 CA GLY A 182 2516 2094 2319 99 874 437 C ATOM 1436 C GLY A 182 14.816 21.184 16.702 1.00 18.21 C ANISOU 1436 C GLY A 182 2544 2112 2261 121 886 423 C ATOM 1437 O GLY A 182 14.473 21.394 15.533 1.00 27.33 O ANISOU 1437 O GLY A 182 3712 3289 3382 147 896 434 O ATOM 1438 N MET A 183 15.014 19.958 17.180 1.00 19.25 N ANISOU 1438 N MET A 183 2690 2239 2384 114 886 397 N ATOM 1439 CA MET A 183 14.792 18.764 16.371 1.00 27.26 C ANISOU 1439 CA MET A 183 3736 3268 3353 130 898 374 C ATOM 1440 C MET A 183 13.318 18.467 16.156 1.00 19.32 C ANISOU 1440 C MET A 183 2748 2278 2313 122 874 329 C ATOM 1441 O MET A 183 13.027 17.387 15.629 1.00 21.26 O ANISOU 1441 O MET A 183 3019 2532 2525 128 882 298 O ATOM 1442 CB MET A 183 15.485 17.560 17.013 1.00 18.79 C ANISOU 1442 CB MET A 183 2671 2180 2289 126 911 364 C ATOM 1443 CG MET A 183 17.003 17.600 16.928 1.00 20.07 C ANISOU 1443 CG MET A 183 2817 2335 2473 143 939 406 C ATOM 1444 SD MET A 183 17.796 16.261 17.836 1.00 24.76 S ANISOU 1444 SD MET A 183 3416 2912 3078 142 953 398 S ATOM 1445 CE MET A 183 16.938 14.842 17.166 1.00 22.40 C ANISOU 1445 CE MET A 183 3163 2615 2734 148 963 353 C ATOM 1446 N GLN A 184 12.451 19.393 16.575 1.00 25.48 N ANISOU 1446 N GLN A 184 3516 3060 3106 106 849 325 N ATOM 1447 CA GLN A 184 11.005 19.364 16.369 1.00 17.92 C ANISOU 1447 CA GLN A 184 2568 2121 2121 99 824 287 C ATOM 1448 C GLN A 184 10.301 18.328 17.233 1.00 18.42 C ANISOU 1448 C GLN A 184 2642 2172 2186 70 809 238 C ATOM 1449 O GLN A 184 9.192 17.906 16.897 1.00 20.39 O ANISOU 1449 O GLN A 184 2902 2437 2407 65 795 198 O ATOM 1450 CB GLN A 184 10.642 19.122 14.897 1.00 19.29 C ANISOU 1450 CB GLN A 184 2758 2331 2240 129 831 279 C ATOM 1451 CG GLN A 184 11.349 20.050 13.928 1.00 28.16 C ANISOU 1451 CG GLN A 184 3874 3469 3356 164 852 332 C ATOM 1452 CD GLN A 184 10.979 21.499 14.144 1.00 25.34 C ANISOU 1452 CD GLN A 184 3495 3109 3023 164 842 362 C ATOM 1453 OE1 GLN A 184 9.883 21.929 13.789 1.00 26.45 O ANISOU 1453 OE1 GLN A 184 3636 3275 3138 170 822 349 O ATOM 1454 NE2 GLN A 184 11.890 22.261 14.736 1.00 19.01 N ANISOU 1454 NE2 GLN A 184 2673 2278 2272 156 855 400 N ATOM 1455 N CYS A 185 10.910 17.896 18.337 1.00 30.64 N ANISOU 1455 N CYS A 185 4185 3692 3765 54 815 241 N ATOM 1456 CA CYS A 185 10.307 16.907 19.222 1.00 27.26 C ANISOU 1456 CA CYS A 185 3768 3248 3343 31 808 203 C ATOM 1457 C CYS A 185 9.860 17.490 20.556 1.00 20.51 C ANISOU 1457 C CYS A 185 2894 2379 2519 8 786 200 C ATOM 1458 O CYS A 185 9.371 16.742 21.412 1.00 27.66 O ANISOU 1458 O CYS A 185 3807 3270 3431 -10 783 174 O ATOM 1459 CB CYS A 185 11.279 15.745 19.455 1.00 21.06 C ANISOU 1459 CB CYS A 185 2995 2444 2562 38 837 207 C ATOM 1460 SG CYS A 185 11.491 14.678 18.010 1.00 26.49 S ANISOU 1460 SG CYS A 185 3712 3143 3210 61 864 190 S ATOM 1461 N SER A 186 10.027 18.794 20.762 1.00 22.10 N ANISOU 1461 N SER A 186 3074 2584 2741 7 773 227 N ATOM 1462 CA SER A 186 9.439 19.501 21.890 1.00 25.69 C ANISOU 1462 CA SER A 186 3511 3029 3220 -14 749 220 C ATOM 1463 C SER A 186 8.843 20.794 21.357 1.00 22.63 C ANISOU 1463 C SER A 186 3112 2655 2833 -9 735 231 C ATOM 1464 O SER A 186 9.123 21.208 20.229 1.00 21.16 O ANISOU 1464 O SER A 186 2927 2482 2631 12 747 253 O ATOM 1465 CB SER A 186 10.466 19.779 22.996 1.00 16.62 C ANISOU 1465 CB SER A 186 2343 1865 2107 -19 750 240 C ATOM 1466 OG SER A 186 11.383 20.783 22.600 1.00 16.73 O ANISOU 1466 OG SER A 186 2337 1879 2141 -9 758 275 O ATOM 1467 N CYS A 187 8.007 21.435 22.167 1.00 17.87 N ANISOU 1467 N CYS A 187 2497 2046 2245 -27 713 217 N ATOM 1468 CA CYS A 187 7.341 22.652 21.736 1.00 20.39 C ANISOU 1468 CA CYS A 187 2806 2376 2566 -21 701 228 C ATOM 1469 C CYS A 187 7.537 23.761 22.758 1.00 18.10 C ANISOU 1469 C CYS A 187 2493 2066 2319 -35 692 240 C ATOM 1470 O CYS A 187 7.753 23.508 23.946 1.00 16.40 O ANISOU 1470 O CYS A 187 2271 1837 2122 -52 684 226 O ATOM 1471 CB CYS A 187 5.849 22.406 21.482 1.00 22.13 C ANISOU 1471 CB CYS A 187 3035 2616 2758 -26 683 194 C ATOM 1472 SG CYS A 187 5.562 21.637 19.885 1.00 20.90 S ANISOU 1472 SG CYS A 187 2898 2493 2550 -2 692 182 S ATOM 1473 N GLY A 188 7.477 24.996 22.268 1.00 21.00 N ANISOU 1473 N GLY A 188 2848 2433 2700 -24 694 265 N ATOM 1474 CA GLY A 188 7.629 26.173 23.096 1.00 24.81 C ANISOU 1474 CA GLY A 188 3309 2893 3226 -36 688 274 C ATOM 1475 C GLY A 188 6.942 27.373 22.481 1.00 20.92 C ANISOU 1475 C GLY A 188 2809 2401 2737 -23 690 292 C ATOM 1476 O GLY A 188 6.176 27.236 21.524 1.00 26.14 O ANISOU 1476 O GLY A 188 3483 3088 3361 -3 689 294 O ATOM 1477 N ILE A 189 7.205 28.557 23.033 1.00 16.88 N ANISOU 1477 N ILE A 189 2278 1864 2272 -32 693 305 N ATOM 1478 CA ILE A 189 6.620 29.782 22.505 1.00 20.71 C ANISOU 1478 CA ILE A 189 2756 2343 2768 -16 700 328 C ATOM 1479 C ILE A 189 7.279 30.139 21.175 1.00 21.97 C ANISOU 1479 C ILE A 189 2917 2507 2922 14 732 374 C ATOM 1480 O ILE A 189 8.458 29.849 20.938 1.00 23.77 O ANISOU 1480 O ILE A 189 3142 2728 3162 16 751 391 O ATOM 1481 CB ILE A 189 6.751 30.910 23.547 1.00 22.78 C ANISOU 1481 CB ILE A 189 2997 2572 3087 -37 698 323 C ATOM 1482 CG1 ILE A 189 5.795 30.654 24.713 1.00 24.81 C ANISOU 1482 CG1 ILE A 189 3256 2833 3339 -58 667 280 C ATOM 1483 CG2 ILE A 189 6.492 32.282 22.940 1.00 17.82 C ANISOU 1483 CG2 ILE A 189 2360 1926 2484 -19 718 357 C ATOM 1484 CD1 ILE A 189 4.394 30.305 24.271 1.00 29.16 C ANISOU 1484 CD1 ILE A 189 3822 3412 3846 -46 652 268 C ATOM 1485 N ASP A 190 6.500 30.751 20.285 1.00 26.95 N ANISOU 1485 N ASP A 190 3554 3153 3533 42 739 396 N ATOM 1486 CA ASP A 190 6.947 31.074 18.930 1.00 17.97 C ANISOU 1486 CA ASP A 190 2420 2026 2379 80 770 444 C ATOM 1487 C ASP A 190 7.802 32.335 18.965 1.00 21.25 C ANISOU 1487 C ASP A 190 2816 2400 2858 81 803 485 C ATOM 1488 O ASP A 190 7.304 33.459 18.880 1.00 18.80 O ANISOU 1488 O ASP A 190 2499 2074 2571 93 815 506 O ATOM 1489 CB ASP A 190 5.746 31.240 18.007 1.00 18.15 C ANISOU 1489 CB ASP A 190 2455 2089 2354 114 764 452 C ATOM 1490 CG ASP A 190 6.136 31.374 16.544 1.00 32.21 C ANISOU 1490 CG ASP A 190 4243 3893 4101 160 794 498 C ATOM 1491 OD1 ASP A 190 7.345 31.373 16.230 1.00 18.67 O ANISOU 1491 OD1 ASP A 190 2526 2161 2407 165 823 527 O ATOM 1492 OD2 ASP A 190 5.217 31.484 15.704 1.00 20.77 O ANISOU 1492 OD2 ASP A 190 2802 2484 2604 195 788 506 O ATOM 1493 N TYR A 191 9.114 32.142 19.081 1.00 23.37 N ANISOU 1493 N TYR A 191 3075 2650 3157 69 822 495 N ATOM 1494 CA TYR A 191 10.078 33.224 18.934 1.00 26.56 C ANISOU 1494 CA TYR A 191 3456 3013 3621 71 860 535 C ATOM 1495 C TYR A 191 10.614 33.335 17.514 1.00 25.92 C ANISOU 1495 C TYR A 191 3384 2945 3522 112 900 590 C ATOM 1496 O TYR A 191 11.518 34.140 17.270 1.00 32.06 O ANISOU 1496 O TYR A 191 4142 3688 4350 116 939 629 O ATOM 1497 CB TYR A 191 11.256 33.034 19.891 1.00 28.47 C ANISOU 1497 CB TYR A 191 3677 3229 3912 34 858 516 C ATOM 1498 CG TYR A 191 10.975 32.166 21.094 1.00 23.78 C ANISOU 1498 CG TYR A 191 3085 2647 3304 3 816 460 C ATOM 1499 CD1 TYR A 191 10.307 32.674 22.199 1.00 22.62 C ANISOU 1499 CD1 TYR A 191 2928 2484 3181 -22 792 426 C ATOM 1500 CD2 TYR A 191 11.404 30.845 21.134 1.00 17.85 C ANISOU 1500 CD2 TYR A 191 2345 1920 2517 1 804 444 C ATOM 1501 CE1 TYR A 191 10.061 31.889 23.304 1.00 21.43 C ANISOU 1501 CE1 TYR A 191 2780 2345 3016 -46 757 380 C ATOM 1502 CE2 TYR A 191 11.160 30.049 22.235 1.00 25.61 C ANISOU 1502 CE2 TYR A 191 3330 2912 3489 -23 772 399 C ATOM 1503 CZ TYR A 191 10.488 30.578 23.316 1.00 17.38 C ANISOU 1503 CZ TYR A 191 2279 1857 2469 -45 748 368 C ATOM 1504 OH TYR A 191 10.241 29.791 24.414 1.00 17.10 O ANISOU 1504 OH TYR A 191 2246 1832 2419 -65 719 328 O ATOM 1505 N TYR A 192 10.086 32.545 16.582 1.00 20.86 N ANISOU 1505 N TYR A 192 2767 2350 2808 144 893 593 N ATOM 1506 CA TYR A 192 10.685 32.363 15.266 1.00 26.79 C ANISOU 1506 CA TYR A 192 3528 3123 3529 185 927 638 C ATOM 1507 C TYR A 192 10.040 33.207 14.177 1.00 34.48 C ANISOU 1507 C TYR A 192 4509 4113 4478 234 951 685 C ATOM 1508 O TYR A 192 10.737 33.669 13.268 1.00 29.76 O ANISOU 1508 O TYR A 192 3909 3511 3887 267 995 740 O ATOM 1509 CB TYR A 192 10.610 30.887 14.867 1.00 21.22 C ANISOU 1509 CB TYR A 192 2844 2461 2756 192 906 607 C ATOM 1510 CG TYR A 192 11.228 29.969 15.895 1.00 19.80 C ANISOU 1510 CG TYR A 192 2660 2267 2595 151 886 566 C ATOM 1511 CD1 TYR A 192 12.595 29.737 15.905 1.00 27.83 C ANISOU 1511 CD1 TYR A 192 3666 3266 3641 145 911 584 C ATOM 1512 CD2 TYR A 192 10.452 29.349 16.868 1.00 24.15 C ANISOU 1512 CD2 TYR A 192 3216 2823 3136 120 845 512 C ATOM 1513 CE1 TYR A 192 13.174 28.909 16.845 1.00 18.54 C ANISOU 1513 CE1 TYR A 192 2483 2081 2479 113 893 550 C ATOM 1514 CE2 TYR A 192 11.026 28.515 17.815 1.00 24.19 C ANISOU 1514 CE2 TYR A 192 3218 2818 3156 89 831 480 C ATOM 1515 CZ TYR A 192 12.388 28.302 17.795 1.00 18.17 C ANISOU 1515 CZ TYR A 192 2445 2041 2420 87 854 500 C ATOM 1516 OH TYR A 192 12.970 27.477 18.727 1.00 29.17 O ANISOU 1516 OH TYR A 192 3832 3427 3824 62 841 472 O ATOM 1517 N THR A 193 8.729 33.413 14.241 1.00 25.10 N ANISOU 1517 N THR A 193 3328 2948 3260 243 925 668 N ATOM 1518 CA THR A 193 7.974 34.038 13.170 1.00 27.23 C ANISOU 1518 CA THR A 193 3606 3249 3491 297 941 708 C ATOM 1519 C THR A 193 7.176 35.218 13.701 1.00 25.54 C ANISOU 1519 C THR A 193 3381 3007 3316 294 941 718 C ATOM 1520 O THR A 193 6.701 35.189 14.842 1.00 25.23 O ANISOU 1520 O THR A 193 3334 2948 3303 253 909 672 O ATOM 1521 CB THR A 193 7.011 33.034 12.517 1.00 26.90 C ANISOU 1521 CB THR A 193 3585 3278 3360 321 906 676 C ATOM 1522 OG1 THR A 193 5.896 32.804 13.389 1.00 25.42 O ANISOU 1522 OG1 THR A 193 3395 3097 3167 291 861 623 O ATOM 1523 CG2 THR A 193 7.713 31.707 12.258 1.00 28.17 C ANISOU 1523 CG2 THR A 193 3758 3459 3487 312 899 650 C ATOM 1524 N PRO A 194 7.017 36.276 12.898 1.00 24.91 N ANISOU 1524 N PRO A 194 3300 2924 3242 341 980 779 N ATOM 1525 CA PRO A 194 6.188 37.411 13.327 1.00 25.32 C ANISOU 1525 CA PRO A 194 3342 2950 3329 345 984 790 C ATOM 1526 C PRO A 194 4.723 37.031 13.486 1.00 30.91 C ANISOU 1526 C PRO A 194 4058 3707 3980 351 936 750 C ATOM 1527 O PRO A 194 4.117 37.325 14.522 1.00 36.84 O ANISOU 1527 O PRO A 194 4800 4433 4763 318 912 716 O ATOM 1528 CB PRO A 194 6.390 38.435 12.202 1.00 34.58 C ANISOU 1528 CB PRO A 194 4516 4118 4506 405 1043 872 C ATOM 1529 CG PRO A 194 7.707 38.067 11.596 1.00 32.13 C ANISOU 1529 CG PRO A 194 4207 3802 4201 412 1077 902 C ATOM 1530 CD PRO A 194 7.748 36.571 11.654 1.00 29.51 C ANISOU 1530 CD PRO A 194 3887 3516 3810 391 1031 845 C ATOM 1531 N HIS A 195 4.151 36.394 12.459 1.00 43.51 N ANISOU 1531 N HIS A 195 5666 5373 5492 394 921 752 N ATOM 1532 CA HIS A 195 2.807 35.816 12.498 1.00 31.77 C ANISOU 1532 CA HIS A 195 4183 3943 3945 398 872 706 C ATOM 1533 C HIS A 195 1.781 36.751 13.128 1.00 34.34 C ANISOU 1533 C HIS A 195 4498 4252 4299 397 864 706 C ATOM 1534 O HIS A 195 1.305 36.491 14.238 1.00 31.25 O ANISOU 1534 O HIS A 195 4101 3843 3930 350 830 653 O ATOM 1535 CB HIS A 195 2.801 34.471 13.229 1.00 31.09 C ANISOU 1535 CB HIS A 195 4102 3867 3845 345 828 632 C ATOM 1536 CG HIS A 195 1.674 33.573 12.814 1.00 30.41 C ANISOU 1536 CG HIS A 195 4021 3850 3683 357 786 587 C ATOM 1537 ND1 HIS A 195 0.592 33.305 13.625 1.00 41.43 N ANISOU 1537 ND1 HIS A 195 5410 5254 5076 328 746 536 N ATOM 1538 CD2 HIS A 195 1.452 32.901 11.659 1.00 39.06 C ANISOU 1538 CD2 HIS A 195 5126 5012 4702 396 778 584 C ATOM 1539 CE1 HIS A 195 -0.241 32.497 12.993 1.00 31.09 C ANISOU 1539 CE1 HIS A 195 4104 4012 3698 344 716 501 C ATOM 1540 NE2 HIS A 195 0.257 32.237 11.798 1.00 37.97 N ANISOU 1540 NE2 HIS A 195 4985 4920 4523 385 733 527 N ATOM 1541 N GLU A 196 1.455 37.849 12.440 1.00 42.48 N ANISOU 1541 N GLU A 196 5526 5286 5329 450 897 767 N ATOM 1542 CA GLU A 196 0.625 38.904 13.020 1.00 39.81 C ANISOU 1542 CA GLU A 196 5177 4920 5028 454 901 777 C ATOM 1543 C GLU A 196 -0.746 38.416 13.477 1.00 35.09 C ANISOU 1543 C GLU A 196 4576 4368 4390 442 846 722 C ATOM 1544 O GLU A 196 -1.383 39.091 14.294 1.00 32.82 O ANISOU 1544 O GLU A 196 4279 4050 4142 428 841 712 O ATOM 1545 CB GLU A 196 0.434 40.042 12.013 1.00 40.50 C ANISOU 1545 CB GLU A 196 5265 5015 5109 525 949 858 C ATOM 1546 CG GLU A 196 1.638 40.962 11.837 1.00 58.45 C ANISOU 1546 CG GLU A 196 7536 7218 7453 532 1015 920 C ATOM 1547 CD GLU A 196 2.674 40.418 10.864 1.00 63.91 C ANISOU 1547 CD GLU A 196 8237 7931 8114 554 1040 950 C ATOM 1548 OE1 GLU A 196 2.495 39.282 10.370 1.00 65.09 O ANISOU 1548 OE1 GLU A 196 8397 8148 8188 562 1003 917 O ATOM 1549 OE2 GLU A 196 3.665 41.135 10.594 1.00 65.78 O ANISOU 1549 OE2 GLU A 196 8472 8117 8406 564 1098 1006 O ATOM 1550 N GLU A 197 -1.222 37.278 12.964 1.00 39.21 N ANISOU 1550 N GLU A 197 5101 4959 4836 449 808 683 N ATOM 1551 CA GLU A 197 -2.556 36.804 13.321 1.00 33.43 C ANISOU 1551 CA GLU A 197 4361 4272 4067 439 759 630 C ATOM 1552 C GLU A 197 -2.668 36.532 14.815 1.00 35.14 C ANISOU 1552 C GLU A 197 4573 4441 4336 371 734 575 C ATOM 1553 O GLU A 197 -3.681 36.867 15.441 1.00 31.90 O ANISOU 1553 O GLU A 197 4153 4032 3936 363 715 555 O ATOM 1554 CB GLU A 197 -2.892 35.546 12.524 1.00 44.82 C ANISOU 1554 CB GLU A 197 5808 5793 5428 450 726 591 C ATOM 1555 CG GLU A 197 -4.316 35.060 12.706 1.00 55.84 C ANISOU 1555 CG GLU A 197 7191 7244 6783 445 677 538 C ATOM 1556 CD GLU A 197 -4.668 33.929 11.755 1.00 69.47 C ANISOU 1556 CD GLU A 197 8918 9050 8427 462 648 500 C ATOM 1557 OE1 GLU A 197 -3.737 33.256 11.256 1.00 68.97 O ANISOU 1557 OE1 GLU A 197 8870 8989 8348 460 659 498 O ATOM 1558 OE2 GLU A 197 -5.875 33.724 11.501 1.00 70.70 O ANISOU 1558 OE2 GLU A 197 9057 9267 8536 478 615 469 O ATOM 1559 N THR A 198 -1.641 35.924 15.404 1.00 35.34 N ANISOU 1559 N THR A 198 4606 4427 4395 324 736 551 N ATOM 1560 CA THR A 198 -1.609 35.649 16.833 1.00 27.76 C ANISOU 1560 CA THR A 198 3642 3423 3482 264 716 503 C ATOM 1561 C THR A 198 -0.814 36.689 17.615 1.00 22.87 C ANISOU 1561 C THR A 198 3018 2729 2944 243 747 527 C ATOM 1562 O THR A 198 -0.622 36.523 18.825 1.00 26.60 O ANISOU 1562 O THR A 198 3486 3165 3457 195 733 488 O ATOM 1563 CB THR A 198 -1.041 34.250 17.092 1.00 28.09 C ANISOU 1563 CB THR A 198 3692 3472 3507 226 695 456 C ATOM 1564 OG1 THR A 198 0.208 34.099 16.405 1.00 23.84 O ANISOU 1564 OG1 THR A 198 3163 2924 2970 238 724 489 O ATOM 1565 CG2 THR A 198 -2.015 33.179 16.616 1.00 20.76 C ANISOU 1565 CG2 THR A 198 2766 2610 2511 232 659 414 C ATOM 1566 N ASN A 199 -0.355 37.751 16.952 1.00 28.54 N ANISOU 1566 N ASN A 199 3734 3424 3686 280 791 589 N ATOM 1567 CA ASN A 199 0.355 38.859 17.590 1.00 36.92 C ANISOU 1567 CA ASN A 199 4786 4410 4830 263 826 613 C ATOM 1568 C ASN A 199 1.522 38.342 18.435 1.00 25.81 C ANISOU 1568 C ASN A 199 3376 2964 3465 209 823 580 C ATOM 1569 O ASN A 199 1.604 38.557 19.646 1.00 26.84 O ANISOU 1569 O ASN A 199 3499 3056 3644 166 811 545 O ATOM 1570 CB ASN A 199 -0.618 39.709 18.413 1.00 31.70 C ANISOU 1570 CB ASN A 199 4118 3727 4202 257 819 600 C ATOM 1571 CG ASN A 199 -1.795 40.211 17.586 1.00 38.65 C ANISOU 1571 CG ASN A 199 4997 4650 5037 314 822 634 C ATOM 1572 OD1 ASN A 199 -1.802 41.349 17.116 1.00 36.06 O ANISOU 1572 OD1 ASN A 199 4667 4298 4736 353 864 690 O ATOM 1573 ND2 ASN A 199 -2.793 39.355 17.401 1.00 46.43 N ANISOU 1573 ND2 ASN A 199 5984 5702 5957 321 780 600 N ATOM 1574 N ASN A 200 2.436 37.645 17.751 1.00 24.60 N ANISOU 1574 N ASN A 200 3230 2826 3289 214 833 593 N ATOM 1575 CA ASN A 200 3.511 36.923 18.429 1.00 20.88 C ANISOU 1575 CA ASN A 200 2756 2333 2844 169 825 562 C ATOM 1576 C ASN A 200 4.408 37.860 19.226 1.00 27.79 C ANISOU 1576 C ASN A 200 3614 3140 3805 140 851 568 C ATOM 1577 O ASN A 200 4.750 37.576 20.381 1.00 19.42 O ANISOU 1577 O ASN A 200 2545 2058 2775 94 830 523 O ATOM 1578 CB ASN A 200 4.344 36.150 17.407 1.00 31.01 C ANISOU 1578 CB ASN A 200 4049 3644 4089 189 839 584 C ATOM 1579 CG ASN A 200 3.787 34.777 17.121 1.00 28.61 C ANISOU 1579 CG ASN A 200 3760 3399 3713 190 802 545 C ATOM 1580 OD1 ASN A 200 2.687 34.435 17.554 1.00 24.13 O ANISOU 1580 OD1 ASN A 200 3195 2855 3119 181 767 507 O ATOM 1581 ND2 ASN A 200 4.548 33.978 16.383 1.00 25.53 N ANISOU 1581 ND2 ASN A 200 3380 3029 3291 202 811 554 N ATOM 1582 N GLU A 201 4.802 38.984 18.622 1.00 20.12 N ANISOU 1582 N GLU A 201 2636 2135 2874 166 899 623 N ATOM 1583 CA GLU A 201 5.815 39.841 19.230 1.00 31.79 C ANISOU 1583 CA GLU A 201 4094 3547 4440 136 930 629 C ATOM 1584 C GLU A 201 5.346 40.398 20.567 1.00 28.28 C ANISOU 1584 C GLU A 201 3637 3067 4041 99 911 583 C ATOM 1585 O GLU A 201 6.116 40.445 21.534 1.00 25.38 O ANISOU 1585 O GLU A 201 3253 2666 3725 54 904 548 O ATOM 1586 CB GLU A 201 6.181 40.977 18.277 1.00 31.05 C ANISOU 1586 CB GLU A 201 3996 3421 4382 174 992 700 C ATOM 1587 CG GLU A 201 7.115 42.009 18.882 1.00 37.00 C ANISOU 1587 CG GLU A 201 4725 4098 5236 142 1030 704 C ATOM 1588 CD GLU A 201 7.536 43.072 17.884 1.00 47.70 C ANISOU 1588 CD GLU A 201 6076 5416 6632 181 1099 780 C ATOM 1589 OE1 GLU A 201 6.898 43.172 16.812 1.00 51.39 O ANISOU 1589 OE1 GLU A 201 6561 5919 7047 239 1115 830 O ATOM 1590 OE2 GLU A 201 8.512 43.801 18.168 1.00 49.47 O ANISOU 1590 OE2 GLU A 201 6278 5579 6941 156 1138 788 O ATOM 1591 N SER A 202 4.085 40.823 20.644 1.00 24.89 N ANISOU 1591 N SER A 202 3215 2648 3593 118 900 582 N ATOM 1592 CA SER A 202 3.580 41.386 21.890 1.00 25.67 C ANISOU 1592 CA SER A 202 3305 2715 3735 86 883 540 C ATOM 1593 C SER A 202 3.542 40.349 23.005 1.00 30.40 C ANISOU 1593 C SER A 202 3903 3335 4312 44 832 473 C ATOM 1594 O SER A 202 3.725 40.699 24.177 1.00 28.58 O ANISOU 1594 O SER A 202 3660 3072 4128 7 822 432 O ATOM 1595 CB SER A 202 2.196 41.996 21.672 1.00 24.13 C ANISOU 1595 CB SER A 202 3117 2532 3519 121 883 556 C ATOM 1596 OG SER A 202 1.252 41.018 21.277 1.00 31.26 O ANISOU 1596 OG SER A 202 4034 3502 4339 140 846 544 O ATOM 1597 N PHE A 203 3.302 39.076 22.677 1.00 23.38 N ANISOU 1597 N PHE A 203 3029 2501 3355 49 802 460 N ATOM 1598 CA PHE A 203 3.313 38.056 23.721 1.00 26.66 C ANISOU 1598 CA PHE A 203 3444 2933 3752 12 761 403 C ATOM 1599 C PHE A 203 4.723 37.810 24.245 1.00 29.91 C ANISOU 1599 C PHE A 203 3842 3321 4201 -20 766 388 C ATOM 1600 O PHE A 203 4.917 37.636 25.453 1.00 26.32 O ANISOU 1600 O PHE A 203 3378 2857 3767 -54 743 343 O ATOM 1601 CB PHE A 203 2.706 36.745 23.223 1.00 18.01 C ANISOU 1601 CB PHE A 203 2366 1896 2580 25 733 391 C ATOM 1602 CG PHE A 203 2.625 35.684 24.291 1.00 24.90 C ANISOU 1602 CG PHE A 203 3241 2783 3436 -9 696 338 C ATOM 1603 CD1 PHE A 203 3.695 34.833 24.532 1.00 17.44 C ANISOU 1603 CD1 PHE A 203 2296 1839 2490 -29 693 325 C ATOM 1604 CD2 PHE A 203 1.489 35.558 25.073 1.00 24.87 C ANISOU 1604 CD2 PHE A 203 3240 2792 3418 -19 669 303 C ATOM 1605 CE1 PHE A 203 3.629 33.875 25.523 1.00 28.60 C ANISOU 1605 CE1 PHE A 203 3713 3266 3889 -55 664 282 C ATOM 1606 CE2 PHE A 203 1.417 34.597 26.067 1.00 24.43 C ANISOU 1606 CE2 PHE A 203 3188 2748 3348 -47 641 259 C ATOM 1607 CZ PHE A 203 2.489 33.756 26.291 1.00 28.96 C ANISOU 1607 CZ PHE A 203 3761 3321 3920 -64 640 250 C ATOM 1608 N VAL A 204 5.716 37.769 23.354 1.00 26.07 N ANISOU 1608 N VAL A 204 3353 2830 3722 -6 795 426 N ATOM 1609 CA VAL A 204 7.078 37.466 23.788 1.00 26.23 C ANISOU 1609 CA VAL A 204 3357 2833 3775 -35 799 414 C ATOM 1610 C VAL A 204 7.571 38.528 24.761 1.00 24.64 C ANISOU 1610 C VAL A 204 3129 2581 3651 -66 809 392 C ATOM 1611 O VAL A 204 8.168 38.213 25.797 1.00 28.11 O ANISOU 1611 O VAL A 204 3554 3018 4109 -99 787 350 O ATOM 1612 CB VAL A 204 8.013 37.325 22.573 1.00 27.96 C ANISOU 1612 CB VAL A 204 3577 3055 3990 -11 834 463 C ATOM 1613 CG1 VAL A 204 9.436 37.029 23.024 1.00 34.48 C ANISOU 1613 CG1 VAL A 204 4382 3865 4853 -39 839 451 C ATOM 1614 CG2 VAL A 204 7.520 36.230 21.637 1.00 31.38 C ANISOU 1614 CG2 VAL A 204 4036 3542 4344 19 822 475 C ATOM 1615 N AILE A 205 7.328 39.803 24.447 0.66 21.59 N ANISOU 1615 N AILE A 205 2736 2155 3311 -54 842 420 N ATOM 1616 N BILE A 205 7.330 39.802 24.448 0.34 21.70 N ANISOU 1616 N BILE A 205 2751 2170 3326 -54 842 420 N ATOM 1617 CA AILE A 205 7.681 40.874 25.375 0.66 29.57 C ANISOU 1617 CA AILE A 205 3723 3114 4400 -85 854 393 C ATOM 1618 CA BILE A 205 7.687 40.867 25.381 0.34 29.49 C ANISOU 1618 CA BILE A 205 3712 3104 4389 -85 853 393 C ATOM 1619 C AILE A 205 6.890 40.736 26.673 0.66 26.91 C ANISOU 1619 C AILE A 205 3386 2786 4051 -107 811 334 C ATOM 1620 C BILE A 205 6.893 40.730 26.676 0.34 26.88 C ANISOU 1620 C BILE A 205 3383 2783 4047 -108 811 334 C ATOM 1621 O AILE A 205 7.418 40.970 27.767 0.66 29.12 O ANISOU 1621 O AILE A 205 3645 3047 4371 -143 798 288 O ATOM 1622 O BILE A 205 7.421 40.958 27.772 0.34 29.04 O ANISOU 1622 O BILE A 205 3635 3037 4360 -143 797 288 O ATOM 1623 CB AILE A 205 7.456 42.246 24.711 0.66 30.07 C ANISOU 1623 CB AILE A 205 3782 3128 4514 -63 904 439 C ATOM 1624 CB BILE A 205 7.480 42.244 24.722 0.34 30.03 C ANISOU 1624 CB BILE A 205 3777 3123 4510 -63 904 438 C ATOM 1625 CG1AILE A 205 8.259 42.352 23.412 0.66 28.81 C ANISOU 1625 CG1AILE A 205 3623 2962 4363 -36 950 503 C ATOM 1626 CG1BILE A 205 8.370 42.381 23.487 0.34 28.75 C ANISOU 1626 CG1BILE A 205 3612 2950 4362 -40 951 500 C ATOM 1627 CG2AILE A 205 7.838 43.383 25.652 0.66 31.58 C ANISOU 1627 CG2AILE A 205 3948 3260 4794 -98 920 406 C ATOM 1628 CG2BILE A 205 7.790 43.374 25.689 0.34 31.52 C ANISOU 1628 CG2BILE A 205 3940 3252 4783 -98 918 404 C ATOM 1629 CD1AILE A 205 9.764 42.365 23.611 0.66 24.75 C ANISOU 1629 CD1AILE A 205 3080 2421 3904 -67 968 495 C ATOM 1630 CD1BILE A 205 8.333 43.752 22.855 0.34 32.82 C ANISOU 1630 CD1BILE A 205 4122 3411 4938 -18 1010 550 C ATOM 1631 N TYR A 206 5.614 40.355 26.573 1.00 21.12 N ANISOU 1631 N TYR A 206 2677 2086 3262 -87 789 333 N ATOM 1632 CA TYR A 206 4.801 40.149 27.771 1.00 23.09 C ANISOU 1632 CA TYR A 206 2929 2348 3496 -105 751 281 C ATOM 1633 C TYR A 206 5.348 39.016 28.633 1.00 23.77 C ANISOU 1633 C TYR A 206 3011 2464 3556 -131 716 239 C ATOM 1634 O TYR A 206 5.324 39.098 29.867 1.00 27.15 O ANISOU 1634 O TYR A 206 3428 2888 3998 -155 693 191 O ATOM 1635 CB TYR A 206 3.356 39.869 27.367 1.00 24.00 C ANISOU 1635 CB TYR A 206 3066 2496 3555 -76 737 293 C ATOM 1636 CG TYR A 206 2.513 39.179 28.413 1.00 34.29 C ANISOU 1636 CG TYR A 206 4377 3829 4823 -91 696 244 C ATOM 1637 CD1 TYR A 206 2.068 39.861 29.537 1.00 17.97 C ANISOU 1637 CD1 TYR A 206 2302 1739 2787 -108 687 208 C ATOM 1638 CD2 TYR A 206 2.136 37.854 28.254 1.00 30.00 C ANISOU 1638 CD2 TYR A 206 3849 3334 4216 -86 670 236 C ATOM 1639 CE1 TYR A 206 1.280 39.233 30.484 1.00 30.39 C ANISOU 1639 CE1 TYR A 206 3881 3339 4326 -118 652 168 C ATOM 1640 CE2 TYR A 206 1.355 37.219 29.191 1.00 30.85 C ANISOU 1640 CE2 TYR A 206 3963 3464 4295 -99 638 196 C ATOM 1641 CZ TYR A 206 0.927 37.910 30.303 1.00 31.49 C ANISOU 1641 CZ TYR A 206 4035 3525 4404 -113 630 164 C ATOM 1642 OH TYR A 206 0.144 37.266 31.234 1.00 27.46 O ANISOU 1642 OH TYR A 206 3531 3038 3863 -122 602 128 O ATOM 1643 N MET A 207 5.848 37.950 28.003 1.00 21.89 N ANISOU 1643 N MET A 207 2782 2257 3277 -122 712 256 N ATOM 1644 CA MET A 207 6.301 36.785 28.762 1.00 29.31 C ANISOU 1644 CA MET A 207 3722 3228 4188 -140 682 222 C ATOM 1645 C MET A 207 7.611 37.060 29.493 1.00 26.69 C ANISOU 1645 C MET A 207 3361 2877 3905 -167 683 200 C ATOM 1646 O MET A 207 7.772 36.672 30.657 1.00 34.49 O ANISOU 1646 O MET A 207 4340 3879 4888 -186 656 157 O ATOM 1647 CB MET A 207 6.450 35.577 27.838 1.00 20.05 C ANISOU 1647 CB MET A 207 2567 2090 2960 -122 682 247 C ATOM 1648 CG MET A 207 6.838 34.299 28.566 1.00 25.71 C ANISOU 1648 CG MET A 207 3288 2836 3645 -135 656 218 C ATOM 1649 SD MET A 207 7.161 32.918 27.458 1.00 26.05 S ANISOU 1649 SD MET A 207 3352 2912 3634 -115 662 244 S ATOM 1650 CE MET A 207 8.486 33.594 26.466 1.00 17.34 C ANISOU 1650 CE MET A 207 2232 1785 2572 -106 701 288 C ATOM 1651 N PHE A 208 8.566 37.711 28.830 1.00 20.62 N ANISOU 1651 N PHE A 208 2574 2077 3182 -168 717 229 N ATOM 1652 CA PHE A 208 9.855 37.948 29.473 1.00 27.29 C ANISOU 1652 CA PHE A 208 3386 2908 4077 -195 718 205 C ATOM 1653 C PHE A 208 9.757 38.999 30.568 1.00 31.80 C ANISOU 1653 C PHE A 208 3934 3448 4700 -221 711 159 C ATOM 1654 O PHE A 208 10.485 38.921 31.562 1.00 28.92 O ANISOU 1654 O PHE A 208 3544 3090 4354 -246 691 116 O ATOM 1655 CB PHE A 208 10.902 38.360 28.442 1.00 24.14 C ANISOU 1655 CB PHE A 208 2972 2484 3718 -190 759 248 C ATOM 1656 CG PHE A 208 11.550 37.201 27.741 1.00 39.79 C ANISOU 1656 CG PHE A 208 4963 4499 5656 -175 761 275 C ATOM 1657 CD1 PHE A 208 12.453 36.388 28.407 1.00 41.59 C ANISOU 1657 CD1 PHE A 208 5175 4752 5876 -190 739 249 C ATOM 1658 CD2 PHE A 208 11.265 36.931 26.414 1.00 37.11 C ANISOU 1658 CD2 PHE A 208 4648 4168 5283 -142 784 327 C ATOM 1659 CE1 PHE A 208 13.055 35.324 27.762 1.00 32.14 C ANISOU 1659 CE1 PHE A 208 3988 3583 4641 -174 744 275 C ATOM 1660 CE2 PHE A 208 11.868 35.870 25.763 1.00 44.09 C ANISOU 1660 CE2 PHE A 208 5542 5082 6128 -128 787 348 C ATOM 1661 CZ PHE A 208 12.762 35.066 26.438 1.00 32.87 C ANISOU 1661 CZ PHE A 208 4106 3680 4703 -144 768 323 C ATOM 1662 N VAL A 209 8.875 39.982 30.409 1.00 26.54 N ANISOU 1662 N VAL A 209 3276 2750 4058 -214 727 167 N ATOM 1663 CA VAL A 209 8.784 41.064 31.385 1.00 27.50 C ANISOU 1663 CA VAL A 209 3377 2836 4236 -239 726 123 C ATOM 1664 C VAL A 209 7.958 40.633 32.590 1.00 30.56 C ANISOU 1664 C VAL A 209 3774 3254 4583 -245 683 73 C ATOM 1665 O VAL A 209 8.446 40.615 33.726 1.00 24.47 O ANISOU 1665 O VAL A 209 2981 2492 3823 -268 659 21 O ATOM 1666 CB VAL A 209 8.206 42.329 30.728 1.00 22.92 C ANISOU 1666 CB VAL A 209 2802 2205 3703 -226 767 155 C ATOM 1667 CG1 VAL A 209 7.926 43.382 31.779 1.00 19.60 C ANISOU 1667 CG1 VAL A 209 2365 1747 3335 -249 765 104 C ATOM 1668 CG2 VAL A 209 9.168 42.862 29.685 1.00 28.89 C ANISOU 1668 CG2 VAL A 209 3543 2924 4510 -222 816 201 C ATOM 1669 N VAL A 210 6.693 40.274 32.355 1.00 27.53 N ANISOU 1669 N VAL A 210 3422 2891 4149 -222 674 89 N ATOM 1670 CA VAL A 210 5.795 39.923 33.449 1.00 30.26 C ANISOU 1670 CA VAL A 210 3777 3262 4459 -224 639 47 C ATOM 1671 C VAL A 210 6.148 38.561 34.038 1.00 36.66 C ANISOU 1671 C VAL A 210 4591 4122 5215 -228 607 27 C ATOM 1672 O VAL A 210 6.026 38.350 35.252 1.00 20.89 O ANISOU 1672 O VAL A 210 2588 2144 3205 -238 579 -18 O ATOM 1673 CB VAL A 210 4.332 39.972 32.963 1.00 26.38 C ANISOU 1673 CB VAL A 210 3314 2776 3934 -199 642 71 C ATOM 1674 CG1 VAL A 210 3.383 39.525 34.065 1.00 17.73 C ANISOU 1674 CG1 VAL A 210 2228 1708 2800 -201 610 32 C ATOM 1675 CG2 VAL A 210 3.981 41.375 32.493 1.00 23.12 C ANISOU 1675 CG2 VAL A 210 2896 2313 3576 -191 677 92 C ATOM 1676 N HIS A 211 6.589 37.618 33.208 1.00 22.22 N ANISOU 1676 N HIS A 211 2772 2316 3355 -216 612 62 N ATOM 1677 CA HIS A 211 6.791 36.249 33.664 1.00 20.98 C ANISOU 1677 CA HIS A 211 2623 2202 3145 -214 586 50 C ATOM 1678 C HIS A 211 8.250 35.809 33.647 1.00 21.87 C ANISOU 1678 C HIS A 211 2715 2325 3269 -222 588 52 C ATOM 1679 O HIS A 211 8.520 34.621 33.846 1.00 19.67 O ANISOU 1679 O HIS A 211 2445 2081 2947 -215 574 52 O ATOM 1680 CB HIS A 211 5.939 35.286 32.831 1.00 23.94 C ANISOU 1680 CB HIS A 211 3031 2602 3465 -192 587 81 C ATOM 1681 CG HIS A 211 4.465 35.471 33.022 1.00 32.52 C ANISOU 1681 CG HIS A 211 4134 3691 4530 -184 579 73 C ATOM 1682 ND1 HIS A 211 3.828 35.186 34.211 1.00 31.89 N ANISOU 1682 ND1 HIS A 211 4058 3628 4431 -189 555 36 N ATOM 1683 CD2 HIS A 211 3.504 35.918 32.178 1.00 36.23 C ANISOU 1683 CD2 HIS A 211 4617 4152 4996 -167 592 99 C ATOM 1684 CE1 HIS A 211 2.539 35.450 34.092 1.00 27.08 C ANISOU 1684 CE1 HIS A 211 3462 3018 3810 -180 554 39 C ATOM 1685 NE2 HIS A 211 2.315 35.892 32.868 1.00 30.32 N ANISOU 1685 NE2 HIS A 211 3877 3415 4228 -166 575 76 N ATOM 1686 N PHE A 212 9.190 36.699 33.351 1.00 25.90 N ANISOU 1686 N PHE A 212 3198 2804 3838 -235 609 57 N ATOM 1687 CA PHE A 212 10.565 36.328 33.678 1.00 26.75 C ANISOU 1687 CA PHE A 212 3278 2927 3959 -247 603 45 C ATOM 1688 C PHE A 212 11.341 37.392 34.447 1.00 30.01 C ANISOU 1688 C PHE A 212 3650 3317 4437 -275 602 3 C ATOM 1689 O PHE A 212 12.087 37.049 35.369 1.00 36.94 O ANISOU 1689 O PHE A 212 4502 4222 5309 -285 578 -33 O ATOM 1690 CB PHE A 212 11.316 35.975 32.385 1.00 30.39 C ANISOU 1690 CB PHE A 212 3742 3383 4423 -235 632 95 C ATOM 1691 CG PHE A 212 12.789 35.753 32.579 1.00 33.99 C ANISOU 1691 CG PHE A 212 4164 3849 4903 -247 632 88 C ATOM 1692 CD1 PHE A 212 13.252 34.768 33.437 1.00 23.09 C ANISOU 1692 CD1 PHE A 212 2777 2512 3486 -246 604 64 C ATOM 1693 CD2 PHE A 212 13.711 36.525 31.891 1.00 27.31 C ANISOU 1693 CD2 PHE A 212 3291 2969 4116 -257 664 109 C ATOM 1694 CE1 PHE A 212 14.604 34.560 33.610 1.00 35.04 C ANISOU 1694 CE1 PHE A 212 4256 4039 5019 -254 603 59 C ATOM 1695 CE2 PHE A 212 15.063 36.323 32.060 1.00 44.32 C ANISOU 1695 CE2 PHE A 212 5410 5134 6294 -268 665 102 C ATOM 1696 CZ PHE A 212 15.511 35.339 32.922 1.00 26.32 C ANISOU 1696 CZ PHE A 212 3122 2903 3976 -266 633 76 C ATOM 1697 N AILE A 213 11.174 38.668 34.112 0.80 27.70 N ANISOU 1697 N AILE A 213 3348 2975 4204 -286 628 6 N ATOM 1698 N BILE A 213 11.164 38.671 34.112 0.20 27.87 N ANISOU 1698 N BILE A 213 3369 2996 4224 -286 628 6 N ATOM 1699 CA AILE A 213 12.013 39.708 34.701 0.80 30.89 C ANISOU 1699 CA AILE A 213 3708 3349 4679 -316 633 -35 C ATOM 1700 CA BILE A 213 11.995 39.724 34.691 0.20 30.74 C ANISOU 1700 CA BILE A 213 3690 3330 4661 -316 633 -35 C ATOM 1701 C AILE A 213 11.420 40.234 36.000 0.80 29.78 C ANISOU 1701 C AILE A 213 3560 3210 4543 -330 606 -97 C ATOM 1702 C BILE A 213 11.409 40.216 36.007 0.20 29.91 C ANISOU 1702 C BILE A 213 3577 3228 4558 -330 605 -97 C ATOM 1703 O AILE A 213 12.139 40.417 36.986 0.80 30.91 O ANISOU 1703 O AILE A 213 3669 3369 4707 -351 584 -151 O ATOM 1704 O BILE A 213 12.123 40.359 37.006 0.20 30.91 O ANISOU 1704 O BILE A 213 3670 3371 4703 -350 583 -151 O ATOM 1705 CB AILE A 213 12.246 40.841 33.681 0.80 24.29 C ANISOU 1705 CB AILE A 213 2863 2452 3914 -322 682 0 C ATOM 1706 CB BILE A 213 12.173 40.878 33.685 0.20 24.54 C ANISOU 1706 CB BILE A 213 2896 2482 3946 -321 683 0 C ATOM 1707 CG1AILE A 213 13.296 40.414 32.651 0.80 30.45 C ANISOU 1707 CG1AILE A 213 3633 3233 4702 -315 708 47 C ATOM 1708 CG1BILE A 213 13.140 40.471 32.571 0.20 30.37 C ANISOU 1708 CG1BILE A 213 3628 3220 4692 -313 710 51 C ATOM 1709 CG2AILE A 213 12.658 42.126 34.383 0.80 27.50 C ANISOU 1709 CG2AILE A 213 3232 2816 4402 -355 691 -50 C ATOM 1710 CG2BILE A 213 12.663 42.137 34.388 0.20 27.58 C ANISOU 1710 CG2BILE A 213 3242 2826 4413 -355 691 -51 C ATOM 1711 CD1AILE A 213 13.684 41.498 31.674 0.80 32.24 C ANISOU 1711 CD1AILE A 213 3846 3400 5002 -319 762 85 C ATOM 1712 CD1BILE A 213 14.558 40.239 33.046 0.20 29.52 C ANISOU 1712 CD1BILE A 213 3476 3128 4610 -335 700 23 C ATOM 1713 N AILE A 214 10.110 40.487 36.020 0.80 28.70 N ANISOU 1713 N AILE A 214 3454 3063 4387 -317 606 -92 N ATOM 1714 N BILE A 214 10.103 40.495 36.024 0.20 28.59 N ANISOU 1714 N BILE A 214 3441 3049 4374 -317 606 -92 N ATOM 1715 CA AILE A 214 9.461 40.931 37.254 0.80 30.94 C ANISOU 1715 CA AILE A 214 3736 3351 4669 -326 582 -149 C ATOM 1716 CA BILE A 214 9.456 40.934 37.261 0.20 30.71 C ANISOU 1716 CA BILE A 214 3706 3322 4639 -326 582 -149 C ATOM 1717 C AILE A 214 9.598 39.906 38.375 0.80 28.59 C ANISOU 1717 C AILE A 214 3436 3116 4311 -321 538 -185 C ATOM 1718 C BILE A 214 9.598 39.906 38.379 0.20 28.58 C ANISOU 1718 C BILE A 214 3435 3115 4311 -321 538 -185 C ATOM 1719 O AILE A 214 9.934 40.302 39.504 0.80 32.37 O ANISOU 1719 O AILE A 214 3888 3606 4805 -337 516 -245 O ATOM 1720 O BILE A 214 9.937 40.299 39.507 0.20 32.09 O ANISOU 1720 O BILE A 214 3853 3571 4770 -338 516 -245 O ATOM 1721 CB AILE A 214 7.999 41.321 36.970 0.80 26.85 C ANISOU 1721 CB AILE A 214 3252 2813 4138 -308 593 -128 C ATOM 1722 CB BILE A 214 7.991 41.317 36.985 0.20 26.99 C ANISOU 1722 CB BILE A 214 3270 2831 4156 -308 593 -129 C ATOM 1723 CG1AILE A 214 7.926 42.764 36.463 0.80 27.89 C ANISOU 1723 CG1AILE A 214 3373 2877 4346 -318 633 -120 C ATOM 1724 CG1BILE A 214 7.922 42.616 36.178 0.20 27.96 C ANISOU 1724 CG1BILE A 214 3387 2888 4349 -312 637 -105 C ATOM 1725 CG2AILE A 214 7.133 41.122 38.206 0.80 28.19 C ANISOU 1725 CG2AILE A 214 3431 3011 4267 -304 560 -174 C ATOM 1726 CG2BILE A 214 7.217 41.456 38.285 0.20 28.83 C ANISOU 1726 CG2BILE A 214 3506 3081 4367 -310 564 -183 C ATOM 1727 CD1AILE A 214 6.520 43.263 36.214 0.80 27.25 C ANISOU 1727 CD1AILE A 214 3321 2774 4257 -297 647 -101 C ATOM 1728 CD1BILE A 214 8.554 43.802 36.874 0.20 28.04 C ANISOU 1728 CD1BILE A 214 3361 2856 4437 -344 647 -158 C ATOM 1729 N PRO A 215 9.355 38.604 38.158 1.00 27.07 N ANISOU 1729 N PRO A 215 3269 2965 4052 -299 526 -154 N ATOM 1730 CA PRO A 215 9.594 37.642 39.251 1.00 26.61 C ANISOU 1730 CA PRO A 215 3206 2964 3941 -291 491 -184 C ATOM 1731 C PRO A 215 11.022 37.641 39.775 1.00 33.38 C ANISOU 1731 C PRO A 215 4020 3842 4819 -306 477 -216 C ATOM 1732 O PRO A 215 11.223 37.536 40.991 1.00 26.10 O ANISOU 1732 O PRO A 215 3081 2958 3878 -307 447 -265 O ATOM 1733 CB PRO A 215 9.230 36.294 38.614 1.00 26.08 C ANISOU 1733 CB PRO A 215 3174 2923 3813 -267 493 -135 C ATOM 1734 CG PRO A 215 8.260 36.636 37.560 1.00 27.75 C ANISOU 1734 CG PRO A 215 3412 3100 4031 -259 518 -97 C ATOM 1735 CD PRO A 215 8.736 37.936 36.995 1.00 28.05 C ANISOU 1735 CD PRO A 215 3428 3088 4141 -277 544 -94 C ATOM 1736 N LEU A 216 12.020 37.775 38.899 1.00 26.64 N ANISOU 1736 N LEU A 216 3147 2970 4005 -316 499 -190 N ATOM 1737 CA LEU A 216 13.404 37.818 39.367 1.00 30.16 C ANISOU 1737 CA LEU A 216 3546 3437 4477 -331 486 -221 C ATOM 1738 C LEU A 216 13.678 39.092 40.158 1.00 38.94 C ANISOU 1738 C LEU A 216 4619 4527 5649 -361 479 -287 C ATOM 1739 O LEU A 216 14.434 39.070 41.136 1.00 31.41 O ANISOU 1739 O LEU A 216 3628 3612 4694 -370 449 -339 O ATOM 1740 CB LEU A 216 14.371 37.700 38.190 1.00 33.24 C ANISOU 1740 CB LEU A 216 3923 3808 4899 -335 516 -175 C ATOM 1741 CG LEU A 216 14.477 36.350 37.476 1.00 25.80 C ANISOU 1741 CG LEU A 216 3009 2894 3900 -307 521 -120 C ATOM 1742 CD1 LEU A 216 15.614 36.373 36.463 1.00 44.26 C ANISOU 1742 CD1 LEU A 216 5325 5215 6275 -312 549 -84 C ATOM 1743 CD2 LEU A 216 14.676 35.221 38.475 1.00 30.03 C ANISOU 1743 CD2 LEU A 216 3545 3494 4372 -288 486 -139 C ATOM 1744 N ILE A 217 13.078 40.211 39.746 1.00 31.26 N ANISOU 1744 N ILE A 217 3654 3495 4729 -376 506 -286 N ATOM 1745 CA ILE A 217 13.253 41.463 40.477 1.00 33.34 C ANISOU 1745 CA ILE A 217 3883 3729 5056 -406 503 -351 C ATOM 1746 C ILE A 217 12.742 41.317 41.905 1.00 34.03 C ANISOU 1746 C ILE A 217 3971 3862 5098 -400 461 -412 C ATOM 1747 O ILE A 217 13.389 41.755 42.864 1.00 30.76 O ANISOU 1747 O ILE A 217 3516 3468 4705 -419 438 -480 O ATOM 1748 CB ILE A 217 12.548 42.618 39.742 1.00 31.46 C ANISOU 1748 CB ILE A 217 3660 3415 4878 -415 545 -331 C ATOM 1749 CG1 ILE A 217 13.304 42.978 38.463 1.00 32.48 C ANISOU 1749 CG1 ILE A 217 3777 3499 5067 -424 590 -281 C ATOM 1750 CG2 ILE A 217 12.417 43.835 40.648 1.00 35.59 C ANISOU 1750 CG2 ILE A 217 4159 3908 5457 -442 542 -403 C ATOM 1751 CD1 ILE A 217 12.607 44.024 37.623 1.00 44.71 C ANISOU 1751 CD1 ILE A 217 5344 4975 6669 -424 637 -246 C ATOM 1752 N VAL A 218 11.572 40.695 42.066 1.00 26.52 N ANISOU 1752 N VAL A 218 3064 2930 4081 -372 452 -390 N ATOM 1753 CA VAL A 218 11.025 40.474 43.401 1.00 35.20 C ANISOU 1753 CA VAL A 218 4169 4076 5132 -360 416 -439 C ATOM 1754 C VAL A 218 11.935 39.559 44.211 1.00 42.33 C ANISOU 1754 C VAL A 218 5046 5050 5986 -349 381 -463 C ATOM 1755 O VAL A 218 12.205 39.815 45.392 1.00 26.48 O ANISOU 1755 O VAL A 218 3012 3080 3970 -352 351 -528 O ATOM 1756 CB VAL A 218 9.596 39.907 43.305 1.00 24.11 C ANISOU 1756 CB VAL A 218 2816 2676 3670 -332 419 -402 C ATOM 1757 CG1 VAL A 218 9.024 39.668 44.697 1.00 26.09 C ANISOU 1757 CG1 VAL A 218 3072 2973 3869 -317 386 -449 C ATOM 1758 CG2 VAL A 218 8.706 40.847 42.507 1.00 22.39 C ANISOU 1758 CG2 VAL A 218 2619 2392 3498 -339 453 -378 C ATOM 1759 N ILE A 219 12.422 38.480 43.593 1.00 24.74 N ANISOU 1759 N ILE A 219 2827 2846 3725 -332 385 -411 N ATOM 1760 CA ILE A 219 13.242 37.508 44.315 1.00 31.81 C ANISOU 1760 CA ILE A 219 3703 3813 4571 -314 355 -423 C ATOM 1761 C ILE A 219 14.542 38.150 44.786 1.00 35.91 C ANISOU 1761 C ILE A 219 4160 4347 5136 -339 339 -479 C ATOM 1762 O ILE A 219 14.946 37.998 45.945 1.00 35.04 O ANISOU 1762 O ILE A 219 4023 4296 4995 -330 303 -531 O ATOM 1763 CB ILE A 219 13.508 36.270 43.440 1.00 29.07 C ANISOU 1763 CB ILE A 219 3379 3479 4187 -292 370 -353 C ATOM 1764 CG1 ILE A 219 12.204 35.537 43.126 1.00 26.14 C ANISOU 1764 CG1 ILE A 219 3064 3101 3766 -268 381 -308 C ATOM 1765 CG2 ILE A 219 14.473 35.325 44.133 1.00 34.91 C ANISOU 1765 CG2 ILE A 219 4094 4288 4882 -271 344 -362 C ATOM 1766 CD1 ILE A 219 12.340 34.493 42.044 1.00 30.99 C ANISOU 1766 CD1 ILE A 219 3704 3713 4358 -252 403 -242 C ATOM 1767 N PHE A 220 15.213 38.887 43.899 1.00 41.76 N ANISOU 1767 N PHE A 220 4877 5037 5953 -369 366 -471 N ATOM 1768 CA PHE A 220 16.496 39.476 44.261 1.00 37.04 C ANISOU 1768 CA PHE A 220 4216 4451 5408 -397 354 -525 C ATOM 1769 C PHE A 220 16.353 40.734 45.106 1.00 43.22 C ANISOU 1769 C PHE A 220 4969 5214 6238 -426 342 -607 C ATOM 1770 O PHE A 220 17.336 41.161 45.721 1.00 29.82 O ANISOU 1770 O PHE A 220 3215 3542 4572 -448 321 -670 O ATOM 1771 CB PHE A 220 17.322 39.767 43.005 1.00 31.72 C ANISOU 1771 CB PHE A 220 3524 3729 4801 -418 392 -484 C ATOM 1772 CG PHE A 220 17.978 38.545 42.427 1.00 37.86 C ANISOU 1772 CG PHE A 220 4307 4543 5537 -393 394 -426 C ATOM 1773 CD1 PHE A 220 19.166 38.068 42.956 1.00 49.86 C ANISOU 1773 CD1 PHE A 220 5779 6122 7044 -390 368 -451 C ATOM 1774 CD2 PHE A 220 17.400 37.863 41.371 1.00 28.37 C ANISOU 1774 CD2 PHE A 220 3155 3318 4306 -371 422 -349 C ATOM 1775 CE1 PHE A 220 19.770 36.939 42.436 1.00 49.27 C ANISOU 1775 CE1 PHE A 220 5710 6078 6931 -364 374 -396 C ATOM 1776 CE2 PHE A 220 17.998 36.733 40.848 1.00 31.18 C ANISOU 1776 CE2 PHE A 220 3518 3706 4625 -348 427 -300 C ATOM 1777 CZ PHE A 220 19.184 36.270 41.382 1.00 39.78 C ANISOU 1777 CZ PHE A 220 4562 4849 5703 -344 404 -321 C ATOM 1778 N PHE A 221 15.163 41.337 45.159 1.00 26.09 N ANISOU 1778 N PHE A 221 2835 3003 4076 -428 355 -611 N ATOM 1779 CA PHE A 221 14.929 42.378 46.153 1.00 40.97 C ANISOU 1779 CA PHE A 221 4696 4879 5990 -448 339 -695 C ATOM 1780 C PHE A 221 14.874 41.783 47.553 1.00 35.45 C ANISOU 1780 C PHE A 221 3990 4267 5213 -422 288 -745 C ATOM 1781 O PHE A 221 15.505 42.298 48.485 1.00 37.92 O ANISOU 1781 O PHE A 221 4255 4611 5541 -439 259 -826 O ATOM 1782 CB PHE A 221 13.637 43.141 45.852 1.00 41.70 C ANISOU 1782 CB PHE A 221 4831 4907 6108 -451 367 -682 C ATOM 1783 CG PHE A 221 13.226 44.075 46.956 1.00 37.31 C ANISOU 1783 CG PHE A 221 4261 4347 5569 -465 350 -766 C ATOM 1784 CD1 PHE A 221 13.799 45.331 47.068 1.00 36.86 C ANISOU 1784 CD1 PHE A 221 4160 4242 5603 -507 363 -829 C ATOM 1785 CD2 PHE A 221 12.282 43.689 47.895 1.00 40.84 C ANISOU 1785 CD2 PHE A 221 4737 4838 5943 -435 324 -784 C ATOM 1786 CE1 PHE A 221 13.434 46.187 48.091 1.00 35.54 C ANISOU 1786 CE1 PHE A 221 3980 4071 5453 -520 348 -912 C ATOM 1787 CE2 PHE A 221 11.914 44.539 48.920 1.00 46.93 C ANISOU 1787 CE2 PHE A 221 5496 5609 6727 -445 308 -864 C ATOM 1788 CZ PHE A 221 12.491 45.790 49.018 1.00 39.84 C ANISOU 1788 CZ PHE A 221 4556 4664 5919 -488 320 -930 C ATOM 1789 N CYS A 222 14.115 40.695 47.719 1.00 34.95 N ANISOU 1789 N CYS A 222 3972 4243 5064 -381 279 -699 N ATOM 1790 CA CYS A 222 14.016 40.047 49.024 1.00 26.48 C ANISOU 1790 CA CYS A 222 2896 3253 3910 -349 237 -736 C ATOM 1791 C CYS A 222 15.367 39.507 49.469 1.00 33.51 C ANISOU 1791 C CYS A 222 3738 4214 4781 -342 207 -759 C ATOM 1792 O CYS A 222 15.740 39.633 50.641 1.00 29.88 O ANISOU 1792 O CYS A 222 3244 3817 4293 -334 169 -828 O ATOM 1793 CB CYS A 222 12.976 38.927 48.979 1.00 34.46 C ANISOU 1793 CB CYS A 222 3965 4284 4842 -307 242 -671 C ATOM 1794 SG CYS A 222 11.308 39.479 48.549 1.00 27.29 S ANISOU 1794 SG CYS A 222 3112 3307 3949 -309 273 -646 S ATOM 1795 N TYR A 223 16.114 38.898 48.543 1.00 48.17 N ANISOU 1795 N TYR A 223 5588 6064 6648 -342 224 -703 N ATOM 1796 CA TYR A 223 17.467 38.448 48.853 1.00 47.87 C ANISOU 1796 CA TYR A 223 5499 6090 6601 -337 199 -722 C ATOM 1797 C TYR A 223 18.375 39.630 49.178 1.00 48.85 C ANISOU 1797 C TYR A 223 5555 6205 6800 -381 186 -805 C ATOM 1798 O TYR A 223 19.243 39.532 50.054 1.00 48.05 O ANISOU 1798 O TYR A 223 5404 6176 6679 -375 147 -861 O ATOM 1799 CB TYR A 223 18.003 37.608 47.685 1.00 57.65 C ANISOU 1799 CB TYR A 223 6749 7314 7842 -328 226 -640 C ATOM 1800 CG TYR A 223 19.386 37.947 47.164 1.00 59.37 C ANISOU 1800 CG TYR A 223 6908 7524 8123 -357 232 -651 C ATOM 1801 CD1 TYR A 223 19.570 38.967 46.232 1.00 58.27 C ANISOU 1801 CD1 TYR A 223 6756 7304 8078 -401 267 -650 C ATOM 1802 CD2 TYR A 223 20.499 37.210 47.560 1.00 58.34 C ANISOU 1802 CD2 TYR A 223 6739 7469 7960 -337 206 -657 C ATOM 1803 CE1 TYR A 223 20.827 39.269 45.737 1.00 54.92 C ANISOU 1803 CE1 TYR A 223 6278 6871 7716 -428 277 -657 C ATOM 1804 CE2 TYR A 223 21.760 37.499 47.068 1.00 64.82 C ANISOU 1804 CE2 TYR A 223 7503 8284 8840 -363 213 -665 C ATOM 1805 CZ TYR A 223 21.920 38.530 46.158 1.00 70.52 C ANISOU 1805 CZ TYR A 223 8212 8923 9659 -411 249 -666 C ATOM 1806 OH TYR A 223 23.176 38.820 45.669 1.00 75.08 O ANISOU 1806 OH TYR A 223 8732 9494 10300 -437 259 -673 O ATOM 1807 N GLY A 224 18.179 40.760 48.492 1.00 43.54 N ANISOU 1807 N GLY A 224 4881 5446 6217 -424 219 -815 N ATOM 1808 CA GLY A 224 18.933 41.957 48.828 1.00 39.90 C ANISOU 1808 CA GLY A 224 4358 4966 5837 -471 212 -900 C ATOM 1809 C GLY A 224 18.680 42.421 50.249 1.00 42.11 C ANISOU 1809 C GLY A 224 4617 5294 6089 -468 170 -994 C ATOM 1810 O GLY A 224 19.597 42.879 50.937 1.00 45.66 O ANISOU 1810 O GLY A 224 5002 5783 6563 -489 140 -1076 O ATOM 1811 N GLN A 225 17.431 42.311 50.706 1.00 44.82 N ANISOU 1811 N GLN A 225 5012 5638 6379 -442 167 -987 N ATOM 1812 CA GLN A 225 17.114 42.656 52.088 1.00 39.06 C ANISOU 1812 CA GLN A 225 4269 4962 5611 -432 128 -1072 C ATOM 1813 C GLN A 225 17.734 41.662 53.061 1.00 46.13 C ANISOU 1813 C GLN A 225 5140 5973 6414 -390 79 -1090 C ATOM 1814 O GLN A 225 18.302 42.058 54.084 1.00 42.88 O ANISOU 1814 O GLN A 225 4677 5621 5994 -394 39 -1180 O ATOM 1815 CB GLN A 225 15.599 42.720 52.279 1.00 34.69 C ANISOU 1815 CB GLN A 225 3779 4379 5021 -411 142 -1050 C ATOM 1816 CG GLN A 225 14.927 43.828 51.493 1.00 42.51 C ANISOU 1816 CG GLN A 225 4791 5261 6099 -448 187 -1043 C ATOM 1817 CD GLN A 225 15.273 45.204 52.022 1.00 41.52 C ANISOU 1817 CD GLN A 225 4619 5105 6051 -492 182 -1145 C ATOM 1818 OE1 GLN A 225 16.295 45.784 51.655 1.00 51.85 O ANISOU 1818 OE1 GLN A 225 5876 6385 7437 -532 191 -1176 O ATOM 1819 NE2 GLN A 225 14.423 45.734 52.894 1.00 48.90 N ANISOU 1819 NE2 GLN A 225 5570 6042 6967 -485 171 -1200 N ATOM 1820 N LEU A 226 17.638 40.364 52.755 1.00 51.52 N ANISOU 1820 N LEU A 226 5857 6691 7028 -346 83 -1006 N ATOM 1821 CA LEU A 226 18.181 39.351 53.655 1.00 47.21 C ANISOU 1821 CA LEU A 226 5292 6255 6391 -298 43 -1012 C ATOM 1822 C LEU A 226 19.674 39.548 53.861 1.00 43.24 C ANISOU 1822 C LEU A 226 4711 5801 5918 -316 15 -1066 C ATOM 1823 O LEU A 226 20.168 39.510 54.994 1.00 61.33 O ANISOU 1823 O LEU A 226 6960 8182 8163 -296 -31 -1133 O ATOM 1824 CB LEU A 226 17.899 37.946 53.114 1.00 50.88 C ANISOU 1824 CB LEU A 226 5806 6732 6792 -254 62 -907 C ATOM 1825 CG LEU A 226 16.455 37.439 53.120 1.00 43.44 C ANISOU 1825 CG LEU A 226 4937 5768 5800 -224 82 -853 C ATOM 1826 CD1 LEU A 226 16.427 35.919 53.205 1.00 45.44 C ANISOU 1826 CD1 LEU A 226 5221 6076 5968 -168 84 -780 C ATOM 1827 CD2 LEU A 226 15.659 38.051 54.263 1.00 49.56 C ANISOU 1827 CD2 LEU A 226 5718 6565 6546 -216 61 -920 C ATOM 1828 N VAL A 227 20.413 39.766 52.776 1.00 46.89 N ANISOU 1828 N VAL A 227 5151 6209 6457 -353 42 -1037 N ATOM 1829 CA VAL A 227 21.858 39.931 52.889 1.00 40.95 C ANISOU 1829 CA VAL A 227 4319 5500 5738 -372 19 -1084 C ATOM 1830 C VAL A 227 22.190 41.262 53.548 1.00 51.57 C ANISOU 1830 C VAL A 227 5606 6839 7148 -420 -3 -1202 C ATOM 1831 O VAL A 227 22.893 41.317 54.562 1.00 50.35 O ANISOU 1831 O VAL A 227 5394 6772 6965 -411 -51 -1280 O ATOM 1832 CB VAL A 227 22.520 39.804 51.505 1.00 50.10 C ANISOU 1832 CB VAL A 227 5472 6599 6964 -398 60 -1018 C ATOM 1833 CG1 VAL A 227 23.941 40.344 51.538 1.00 34.79 C ANISOU 1833 CG1 VAL A 227 3446 4681 5091 -435 44 -1079 C ATOM 1834 CG2 VAL A 227 22.507 38.356 51.062 1.00 48.68 C ANISOU 1834 CG2 VAL A 227 5333 6452 6711 -347 70 -919 C ATOM 1835 N PHE A 228 21.668 42.349 52.992 1.00 56.11 N ANISOU 1835 N PHE A 228 6196 7312 7811 -468 33 -1217 N ATOM 1836 CA PHE A 228 22.109 43.695 53.358 1.00 58.00 C ANISOU 1836 CA PHE A 228 6376 7522 8139 -524 26 -1324 C ATOM 1837 C PHE A 228 21.167 44.337 54.376 1.00 57.53 C ANISOU 1837 C PHE A 228 6335 7468 8055 -520 7 -1397 C ATOM 1838 O PHE A 228 20.629 45.423 54.162 1.00 52.43 O ANISOU 1838 O PHE A 228 5700 6736 7485 -560 36 -1429 O ATOM 1839 CB PHE A 228 22.241 44.559 52.107 1.00 37.10 C ANISOU 1839 CB PHE A 228 3727 4754 5614 -579 84 -1297 C ATOM 1840 N THR A 229 20.985 43.646 55.501 1.00 68.64 N ANISOU 1840 N THR A 229 7746 8979 9354 -468 -40 -1420 N ATOM 1841 CA THR A 229 20.375 44.225 56.699 1.00 68.03 C ANISOU 1841 CA THR A 229 7669 8936 9244 -461 -71 -1510 C ATOM 1842 C THR A 229 20.976 43.572 57.941 1.00 75.91 C ANISOU 1842 C THR A 229 8626 10073 10143 -414 -134 -1562 C ATOM 1843 O THR A 229 20.705 42.407 58.233 1.00 74.56 O ANISOU 1843 O THR A 229 8489 9970 9870 -352 -146 -1498 O ATOM 1844 CB THR A 229 18.828 44.059 56.743 1.00 74.47 C ANISOU 1844 CB THR A 229 8568 9714 10013 -430 -48 -1458 C ATOM 1845 OG1 THR A 229 18.469 42.707 56.435 1.00 74.81 O ANISOU 1845 OG1 THR A 229 8661 9790 9972 -377 -40 -1351 O ATOM 1846 CG2 THR A 229 18.124 45.017 55.778 1.00 65.61 C ANISOU 1846 CG2 THR A 229 7480 8460 8990 -477 8 -1435 C ATOM 1847 N LYS A 245 17.614 28.393 64.177 1.00 48.44 N ANISOU 1847 N LYS A 245 5562 7427 5415 507 -107 -730 N ATOM 1848 CA LYS A 245 18.342 27.523 63.254 1.00 55.19 C ANISOU 1848 CA LYS A 245 6417 8258 6295 509 -82 -656 C ATOM 1849 C LYS A 245 17.389 26.644 62.450 1.00 50.01 C ANISOU 1849 C LYS A 245 5835 7508 5656 508 -18 -557 C ATOM 1850 O LYS A 245 17.797 26.000 61.480 1.00 52.47 O ANISOU 1850 O LYS A 245 6158 7775 6004 496 11 -496 O ATOM 1851 CB LYS A 245 19.354 26.655 64.007 1.00 59.00 C ANISOU 1851 CB LYS A 245 6863 8860 6693 590 -102 -633 C ATOM 1852 CG LYS A 245 20.643 27.387 64.354 1.00 52.24 C ANISOU 1852 CG LYS A 245 5920 8085 5843 577 -164 -722 C ATOM 1853 CD LYS A 245 21.635 26.462 65.028 1.00 54.65 C ANISOU 1853 CD LYS A 245 6189 8512 6063 662 -181 -691 C ATOM 1854 N ALA A 246 16.123 26.616 62.863 1.00 46.62 N ANISOU 1854 N ALA A 246 5457 7054 5203 521 6 -543 N ATOM 1855 CA ALA A 246 15.093 26.038 62.009 1.00 54.84 C ANISOU 1855 CA ALA A 246 6564 7994 6279 501 64 -468 C ATOM 1856 C ALA A 246 14.836 26.924 60.799 1.00 45.91 C ANISOU 1856 C ALA A 246 5437 6757 5250 412 68 -493 C ATOM 1857 O ALA A 246 14.720 26.429 59.672 1.00 41.83 O ANISOU 1857 O ALA A 246 4949 6166 4780 385 105 -435 O ATOM 1858 CB ALA A 246 13.803 25.825 62.805 1.00 59.37 C ANISOU 1858 CB ALA A 246 7185 8571 6803 538 87 -450 C ATOM 1859 N GLU A 247 14.754 28.241 61.014 1.00 34.60 N ANISOU 1859 N GLU A 247 3976 5318 3852 367 34 -580 N ATOM 1860 CA GLU A 247 14.569 29.155 59.894 1.00 40.76 C ANISOU 1860 CA GLU A 247 4757 6000 4729 286 40 -604 C ATOM 1861 C GLU A 247 15.799 29.213 59.004 1.00 37.19 C ANISOU 1861 C GLU A 247 4265 5535 4330 254 32 -603 C ATOM 1862 O GLU A 247 15.676 29.488 57.805 1.00 30.24 O ANISOU 1862 O GLU A 247 3399 4566 3524 200 55 -583 O ATOM 1863 CB GLU A 247 14.210 30.556 60.396 1.00 34.38 C ANISOU 1863 CB GLU A 247 3928 5187 3948 250 9 -698 C ATOM 1864 CG GLU A 247 12.903 30.623 61.189 1.00 46.18 C ANISOU 1864 CG GLU A 247 5464 6684 5398 276 21 -702 C ATOM 1865 CD GLU A 247 11.650 30.400 60.343 1.00 36.66 C ANISOU 1865 CD GLU A 247 4319 5380 4230 251 69 -641 C ATOM 1866 OE1 GLU A 247 11.739 29.796 59.249 1.00 40.82 O ANISOU 1866 OE1 GLU A 247 4866 5851 4793 233 100 -578 O ATOM 1867 OE2 GLU A 247 10.564 30.838 60.784 1.00 49.73 O ANISOU 1867 OE2 GLU A 247 6000 7017 5877 251 77 -660 O ATOM 1868 N LYS A 248 16.986 28.976 59.568 1.00 33.90 N ANISOU 1868 N LYS A 248 3797 5208 3877 287 -1 -625 N ATOM 1869 CA LYS A 248 18.194 28.932 58.751 1.00 31.55 C ANISOU 1869 CA LYS A 248 3459 4904 3626 261 -7 -618 C ATOM 1870 C LYS A 248 18.105 27.821 57.713 1.00 34.52 C ANISOU 1870 C LYS A 248 3879 5224 4013 270 42 -519 C ATOM 1871 O LYS A 248 18.491 28.011 56.554 1.00 28.90 O ANISOU 1871 O LYS A 248 3162 4447 3370 222 58 -503 O ATOM 1872 CB LYS A 248 19.425 28.746 59.641 1.00 36.48 C ANISOU 1872 CB LYS A 248 4019 5644 4196 306 -50 -654 C ATOM 1873 CG LYS A 248 20.747 29.012 58.942 1.00 29.34 C ANISOU 1873 CG LYS A 248 3057 4742 3350 271 -66 -672 C ATOM 1874 CD LYS A 248 21.930 28.786 59.872 1.00 46.49 C ANISOU 1874 CD LYS A 248 5163 7039 5464 320 -111 -708 C ATOM 1875 CE LYS A 248 22.060 27.320 60.251 1.00 41.31 C ANISOU 1875 CE LYS A 248 4531 6445 4720 406 -91 -623 C ATOM 1876 NZ LYS A 248 23.291 27.061 61.048 1.00 38.73 N ANISOU 1876 NZ LYS A 248 4137 6243 4337 457 -134 -650 N ATOM 1877 N GLU A 249 17.586 26.657 58.111 1.00 26.37 N ANISOU 1877 N GLU A 249 2890 4215 2914 330 70 -452 N ATOM 1878 CA GLU A 249 17.486 25.529 57.190 1.00 43.02 C ANISOU 1878 CA GLU A 249 5042 6273 5032 341 119 -361 C ATOM 1879 C GLU A 249 16.577 25.850 56.008 1.00 30.94 C ANISOU 1879 C GLU A 249 3556 4630 3572 280 152 -342 C ATOM 1880 O GLU A 249 16.908 25.535 54.860 1.00 30.39 O ANISOU 1880 O GLU A 249 3495 4506 3547 254 177 -302 O ATOM 1881 CB GLU A 249 16.983 24.294 57.936 1.00 39.29 C ANISOU 1881 CB GLU A 249 4609 5841 4478 415 147 -299 C ATOM 1882 CG GLU A 249 17.200 22.991 57.189 1.00 35.40 C ANISOU 1882 CG GLU A 249 4147 5318 3984 440 194 -210 C ATOM 1883 CD GLU A 249 16.312 21.868 57.697 1.00 46.90 C ANISOU 1883 CD GLU A 249 5659 6776 5386 496 238 -144 C ATOM 1884 OE1 GLU A 249 15.167 22.155 58.112 1.00 43.48 O ANISOU 1884 OE1 GLU A 249 5256 6322 4944 490 246 -157 O ATOM 1885 OE2 GLU A 249 16.764 20.701 57.685 1.00 38.80 O ANISOU 1885 OE2 GLU A 249 4644 5771 4328 546 268 -80 O ATOM 1886 N VAL A 250 15.428 26.478 56.269 1.00 30.58 N ANISOU 1886 N VAL A 250 3536 4550 3533 260 154 -369 N ATOM 1887 CA VAL A 250 14.508 26.830 55.188 1.00 36.51 C ANISOU 1887 CA VAL A 250 4326 5201 4347 206 183 -353 C ATOM 1888 C VAL A 250 15.158 27.836 54.247 1.00 34.98 C ANISOU 1888 C VAL A 250 4098 4960 4232 144 170 -389 C ATOM 1889 O VAL A 250 15.089 27.701 53.020 1.00 26.60 O ANISOU 1889 O VAL A 250 3058 3831 3220 112 198 -351 O ATOM 1890 CB VAL A 250 13.185 27.368 55.760 1.00 28.03 C ANISOU 1890 CB VAL A 250 3281 4108 3262 201 184 -379 C ATOM 1891 CG1 VAL A 250 12.240 27.769 54.632 1.00 26.69 C ANISOU 1891 CG1 VAL A 250 3147 3839 3155 148 212 -363 C ATOM 1892 CG2 VAL A 250 12.533 26.331 56.656 1.00 25.09 C ANISOU 1892 CG2 VAL A 250 2942 3776 2814 264 204 -337 C ATOM 1893 N THR A 251 15.806 28.858 54.812 1.00 24.38 N ANISOU 1893 N THR A 251 2703 3656 2905 127 129 -465 N ATOM 1894 CA THR A 251 16.423 29.894 53.991 1.00 38.36 C ANISOU 1894 CA THR A 251 4438 5380 4757 66 120 -503 C ATOM 1895 C THR A 251 17.504 29.315 53.088 1.00 21.82 C ANISOU 1895 C THR A 251 2324 3279 2686 63 133 -460 C ATOM 1896 O THR A 251 17.616 29.697 51.916 1.00 30.72 O ANISOU 1896 O THR A 251 3456 4337 3881 19 153 -444 O ATOM 1897 CB THR A 251 17.003 30.991 54.883 1.00 31.08 C ANISOU 1897 CB THR A 251 3458 4508 3845 51 74 -597 C ATOM 1898 OG1 THR A 251 15.961 31.550 55.692 1.00 22.64 O ANISOU 1898 OG1 THR A 251 2408 3439 2754 55 64 -638 O ATOM 1899 CG2 THR A 251 17.621 32.091 54.040 1.00 33.41 C ANISOU 1899 CG2 THR A 251 3714 4746 4234 -14 71 -636 C ATOM 1900 N ARG A 252 18.308 28.389 53.614 1.00 22.17 N ANISOU 1900 N ARG A 252 2350 3399 2675 114 123 -437 N ATOM 1901 CA ARG A 252 19.358 27.772 52.810 1.00 30.02 C ANISOU 1901 CA ARG A 252 3327 4393 3687 117 137 -394 C ATOM 1902 C ARG A 252 18.777 26.994 51.637 1.00 26.90 C ANISOU 1902 C ARG A 252 2990 3923 3308 112 186 -316 C ATOM 1903 O ARG A 252 19.311 27.047 50.522 1.00 33.09 O ANISOU 1903 O ARG A 252 3767 4661 4143 82 204 -294 O ATOM 1904 CB ARG A 252 20.216 26.862 53.685 1.00 29.15 C ANISOU 1904 CB ARG A 252 3189 4382 3506 182 119 -380 C ATOM 1905 CG ARG A 252 21.102 27.619 54.649 1.00 28.95 C ANISOU 1905 CG ARG A 252 3092 4438 3470 185 66 -460 C ATOM 1906 CD ARG A 252 21.828 26.682 55.588 1.00 31.40 C ANISOU 1906 CD ARG A 252 3377 4855 3698 258 48 -442 C ATOM 1907 NE ARG A 252 22.972 27.339 56.205 1.00 24.63 N ANISOU 1907 NE ARG A 252 2439 4076 2842 256 -2 -516 N ATOM 1908 CZ ARG A 252 23.785 26.765 57.080 1.00 46.14 C ANISOU 1908 CZ ARG A 252 5124 6907 5498 317 -29 -518 C ATOM 1909 NH1 ARG A 252 23.594 25.522 57.490 1.00 43.71 N ANISOU 1909 NH1 ARG A 252 4852 6641 5115 390 -7 -447 N ATOM 1910 NH2 ARG A 252 24.814 27.459 57.560 1.00 41.74 N ANISOU 1910 NH2 ARG A 252 4488 6420 4951 306 -78 -594 N ATOM 1911 N MET A 253 17.688 26.258 51.868 1.00 21.07 N ANISOU 1911 N MET A 253 2307 3171 2527 140 210 -276 N ATOM 1912 CA MET A 253 17.093 25.472 50.794 1.00 30.70 C ANISOU 1912 CA MET A 253 3580 4323 3760 134 257 -209 C ATOM 1913 C MET A 253 16.519 26.366 49.700 1.00 27.94 C ANISOU 1913 C MET A 253 3246 3889 3481 74 269 -220 C ATOM 1914 O MET A 253 16.674 26.070 48.509 1.00 20.99 O ANISOU 1914 O MET A 253 2382 2960 2634 55 296 -181 O ATOM 1915 CB MET A 253 16.019 24.543 51.355 1.00 30.10 C ANISOU 1915 CB MET A 253 3556 4252 3629 175 280 -171 C ATOM 1916 CG MET A 253 15.232 23.806 50.292 1.00 33.15 C ANISOU 1916 CG MET A 253 3996 4565 4033 163 327 -114 C ATOM 1917 SD MET A 253 14.142 22.551 50.983 1.00 28.40 S ANISOU 1917 SD MET A 253 3448 3971 3371 213 361 -66 S ATOM 1918 CE MET A 253 12.918 22.429 49.679 1.00 33.47 C ANISOU 1918 CE MET A 253 4142 4515 4058 169 399 -39 C ATOM 1919 N VAL A 254 15.863 27.466 50.082 1.00 27.53 N ANISOU 1919 N VAL A 254 3188 3822 3450 45 250 -273 N ATOM 1920 CA VAL A 254 15.299 28.380 49.091 1.00 28.90 C ANISOU 1920 CA VAL A 254 3375 3918 3689 -8 264 -281 C ATOM 1921 C VAL A 254 16.405 28.999 48.245 1.00 27.23 C ANISOU 1921 C VAL A 254 3123 3685 3539 -42 262 -292 C ATOM 1922 O VAL A 254 16.236 29.218 47.039 1.00 25.01 O ANISOU 1922 O VAL A 254 2859 3340 3304 -72 288 -264 O ATOM 1923 CB VAL A 254 14.437 29.456 49.781 1.00 25.19 C ANISOU 1923 CB VAL A 254 2905 3439 3229 -26 245 -337 C ATOM 1924 CG1 VAL A 254 13.885 30.438 48.760 1.00 26.30 C ANISOU 1924 CG1 VAL A 254 3057 3500 3438 -76 262 -343 C ATOM 1925 CG2 VAL A 254 13.296 28.805 50.537 1.00 25.90 C ANISOU 1925 CG2 VAL A 254 3035 3545 3258 9 253 -320 C ATOM 1926 N ILE A 255 17.555 29.286 48.862 1.00 28.15 N ANISOU 1926 N ILE A 255 3183 3856 3655 -38 232 -332 N ATOM 1927 CA ILE A 255 18.706 29.767 48.101 1.00 30.01 C ANISOU 1927 CA ILE A 255 3375 4077 3950 -68 232 -339 C ATOM 1928 C ILE A 255 19.069 28.771 47.008 1.00 27.40 C ANISOU 1928 C ILE A 255 3069 3724 3620 -56 267 -266 C ATOM 1929 O ILE A 255 19.330 29.153 45.861 1.00 25.55 O ANISOU 1929 O ILE A 255 2833 3435 3441 -88 289 -248 O ATOM 1930 CB ILE A 255 19.897 30.034 49.042 1.00 25.28 C ANISOU 1930 CB ILE A 255 2708 3554 3341 -58 193 -393 C ATOM 1931 CG1 ILE A 255 19.650 31.287 49.883 1.00 36.10 C ANISOU 1931 CG1 ILE A 255 4049 4934 4735 -85 161 -476 C ATOM 1932 CG2 ILE A 255 21.194 30.166 48.255 1.00 21.62 C ANISOU 1932 CG2 ILE A 255 2200 3085 2929 -79 199 -385 C ATOM 1933 CD1 ILE A 255 20.841 31.692 50.716 1.00 25.24 C ANISOU 1933 CD1 ILE A 255 2600 3631 3360 -84 120 -541 C ATOM 1934 N ILE A 256 19.077 27.479 47.341 1.00 29.09 N ANISOU 1934 N ILE A 256 3306 3977 3771 -7 275 -223 N ATOM 1935 CA ILE A 256 19.411 26.453 46.358 1.00 19.98 C ANISOU 1935 CA ILE A 256 2177 2802 2613 9 309 -157 C ATOM 1936 C ILE A 256 18.299 26.296 45.325 1.00 30.07 C ANISOU 1936 C ILE A 256 3512 4005 3907 -10 344 -120 C ATOM 1937 O ILE A 256 18.571 26.017 44.150 1.00 19.41 O ANISOU 1937 O ILE A 256 2175 2616 2583 -21 372 -82 O ATOM 1938 CB ILE A 256 19.729 25.130 47.079 1.00 27.48 C ANISOU 1938 CB ILE A 256 3135 3814 3493 69 311 -123 C ATOM 1939 CG1 ILE A 256 20.987 25.296 47.935 1.00 27.75 C ANISOU 1939 CG1 ILE A 256 3104 3928 3513 89 276 -157 C ATOM 1940 CG2 ILE A 256 19.912 23.996 46.082 1.00 32.42 C ANISOU 1940 CG2 ILE A 256 3794 4410 4114 86 352 -55 C ATOM 1941 CD1 ILE A 256 22.205 25.729 47.141 1.00 33.45 C ANISOU 1941 CD1 ILE A 256 3778 4640 4290 62 275 -162 C ATOM 1942 N MET A 257 17.039 26.475 45.732 1.00 26.57 N ANISOU 1942 N MET A 257 3103 3545 3447 -13 343 -132 N ATOM 1943 CA MET A 257 15.941 26.404 44.773 1.00 22.97 C ANISOU 1943 CA MET A 257 2697 3024 3008 -32 372 -103 C ATOM 1944 C MET A 257 16.065 27.492 43.713 1.00 26.10 C ANISOU 1944 C MET A 257 3080 3367 3471 -77 379 -113 C ATOM 1945 O MET A 257 15.813 27.244 42.528 1.00 23.35 O ANISOU 1945 O MET A 257 2760 2973 3140 -87 408 -75 O ATOM 1946 CB MET A 257 14.598 26.512 45.495 1.00 18.51 C ANISOU 1946 CB MET A 257 2162 2455 2416 -27 368 -119 C ATOM 1947 CG MET A 257 14.300 25.348 46.427 1.00 19.66 C ANISOU 1947 CG MET A 257 2329 2645 2497 20 372 -98 C ATOM 1948 SD MET A 257 12.679 25.478 47.207 1.00 25.80 S ANISOU 1948 SD MET A 257 3141 3413 3247 25 372 -113 S ATOM 1949 CE MET A 257 11.605 25.287 45.785 1.00 26.49 C ANISOU 1949 CE MET A 257 3275 3423 3366 -4 407 -78 C ATOM 1950 N VAL A 258 16.447 28.705 44.119 1.00 22.58 N ANISOU 1950 N VAL A 258 2593 2924 3064 -103 356 -164 N ATOM 1951 CA VAL A 258 16.636 29.789 43.156 1.00 26.60 C ANISOU 1951 CA VAL A 258 3087 3380 3642 -144 367 -172 C ATOM 1952 C VAL A 258 17.793 29.472 42.213 1.00 32.68 C ANISOU 1952 C VAL A 258 3837 4144 4437 -146 386 -138 C ATOM 1953 O VAL A 258 17.687 29.660 40.994 1.00 18.83 O ANISOU 1953 O VAL A 258 2099 2339 2715 -162 414 -106 O ATOM 1954 CB VAL A 258 16.848 31.128 43.887 1.00 25.60 C ANISOU 1954 CB VAL A 258 2915 3255 3555 -173 341 -239 C ATOM 1955 CG1 VAL A 258 17.144 32.238 42.890 1.00 26.98 C ANISOU 1955 CG1 VAL A 258 3073 3371 3808 -214 361 -242 C ATOM 1956 CG2 VAL A 258 15.626 31.476 44.722 1.00 31.25 C ANISOU 1956 CG2 VAL A 258 3655 3971 4247 -170 328 -269 C ATOM 1957 N ILE A 259 18.914 28.988 42.758 1.00 23.68 N ANISOU 1957 N ILE A 259 2660 3058 3280 -126 370 -144 N ATOM 1958 CA ILE A 259 20.062 28.648 41.923 1.00 19.48 C ANISOU 1958 CA ILE A 259 2107 2525 2770 -125 388 -112 C ATOM 1959 C ILE A 259 19.712 27.513 40.970 1.00 23.84 C ANISOU 1959 C ILE A 259 2710 3055 3293 -103 422 -48 C ATOM 1960 O ILE A 259 20.043 27.559 39.778 1.00 19.43 O ANISOU 1960 O ILE A 259 2157 2459 2767 -115 449 -16 O ATOM 1961 CB ILE A 259 21.279 28.287 42.795 1.00 27.63 C ANISOU 1961 CB ILE A 259 3088 3629 3782 -103 362 -132 C ATOM 1962 CG1 ILE A 259 21.635 29.438 43.737 1.00 33.93 C ANISOU 1962 CG1 ILE A 259 3831 4453 4610 -127 326 -205 C ATOM 1963 CG2 ILE A 259 22.476 27.938 41.920 1.00 26.70 C ANISOU 1963 CG2 ILE A 259 2946 3510 3690 -100 382 -97 C ATOM 1964 CD1 ILE A 259 22.663 29.065 44.787 1.00 22.04 C ANISOU 1964 CD1 ILE A 259 2273 3030 3070 -99 293 -232 C ATOM 1965 N ALA A 260 19.036 26.479 41.477 1.00 18.81 N ANISOU 1965 N ALA A 260 2112 2439 2597 -70 423 -30 N ATOM 1966 CA ALA A 260 18.675 25.347 40.632 1.00 18.73 C ANISOU 1966 CA ALA A 260 2149 2406 2561 -51 456 24 C ATOM 1967 C ALA A 260 17.726 25.774 39.521 1.00 22.17 C ANISOU 1967 C ALA A 260 2621 2780 3023 -77 478 38 C ATOM 1968 O ALA A 260 17.828 25.290 38.389 1.00 19.23 O ANISOU 1968 O ALA A 260 2270 2380 2655 -75 506 76 O ATOM 1969 CB ALA A 260 18.049 24.234 41.469 1.00 18.34 C ANISOU 1969 CB ALA A 260 2132 2385 2450 -14 457 37 C ATOM 1970 N PHE A 261 16.790 26.674 39.828 1.00 22.88 N ANISOU 1970 N PHE A 261 2716 2850 3127 -99 465 7 N ATOM 1971 CA PHE A 261 15.896 27.188 38.799 1.00 22.31 C ANISOU 1971 CA PHE A 261 2672 2724 3079 -121 483 19 C ATOM 1972 C PHE A 261 16.675 27.929 37.719 1.00 25.66 C ANISOU 1972 C PHE A 261 3075 3119 3557 -142 500 32 C ATOM 1973 O PHE A 261 16.429 27.742 36.521 1.00 24.27 O ANISOU 1973 O PHE A 261 2924 2911 3386 -143 526 67 O ATOM 1974 CB PHE A 261 14.843 28.100 39.428 1.00 23.71 C ANISOU 1974 CB PHE A 261 2854 2889 3265 -138 466 -18 C ATOM 1975 CG PHE A 261 13.828 28.623 38.450 1.00 28.17 C ANISOU 1975 CG PHE A 261 3448 3404 3850 -156 484 -4 C ATOM 1976 CD1 PHE A 261 14.051 29.805 37.759 1.00 25.54 C ANISOU 1976 CD1 PHE A 261 3096 3035 3572 -181 492 -8 C ATOM 1977 CD2 PHE A 261 12.650 27.931 38.220 1.00 30.90 C ANISOU 1977 CD2 PHE A 261 3838 3742 4162 -145 493 13 C ATOM 1978 CE1 PHE A 261 13.120 30.284 36.857 1.00 20.61 C ANISOU 1978 CE1 PHE A 261 2498 2371 2962 -189 510 9 C ATOM 1979 CE2 PHE A 261 11.715 28.407 37.319 1.00 20.61 C ANISOU 1979 CE2 PHE A 261 2558 2402 2873 -157 507 25 C ATOM 1980 CZ PHE A 261 11.952 29.583 36.637 1.00 24.61 C ANISOU 1980 CZ PHE A 261 3046 2876 3428 -177 515 25 C ATOM 1981 N LEU A 262 17.621 28.778 38.127 1.00 23.13 N ANISOU 1981 N LEU A 262 2704 2809 3277 -159 486 3 N ATOM 1982 CA LEU A 262 18.365 29.576 37.157 1.00 23.38 C ANISOU 1982 CA LEU A 262 2710 2807 3367 -181 506 15 C ATOM 1983 C LEU A 262 19.218 28.698 36.249 1.00 21.43 C ANISOU 1983 C LEU A 262 2466 2565 3111 -162 531 61 C ATOM 1984 O LEU A 262 19.298 28.945 35.043 1.00 26.87 O ANISOU 1984 O LEU A 262 3165 3218 3825 -169 560 94 O ATOM 1985 CB LEU A 262 19.228 30.612 37.875 1.00 18.95 C ANISOU 1985 CB LEU A 262 2089 2257 2854 -205 486 -33 C ATOM 1986 CG LEU A 262 18.484 31.801 38.488 1.00 35.71 C ANISOU 1986 CG LEU A 262 4204 4358 5007 -231 471 -80 C ATOM 1987 CD1 LEU A 262 19.463 32.764 39.136 1.00 28.21 C ANISOU 1987 CD1 LEU A 262 3190 3418 4109 -257 454 -132 C ATOM 1988 CD2 LEU A 262 17.643 32.512 37.438 1.00 30.26 C ANISOU 1988 CD2 LEU A 262 3543 3605 4348 -246 500 -56 C ATOM 1989 N ILE A 263 19.863 27.671 36.806 1.00 18.50 N ANISOU 1989 N ILE A 263 2087 2240 2702 -136 522 67 N ATOM 1990 CA ILE A 263 20.612 26.736 35.971 1.00 28.30 C ANISOU 1990 CA ILE A 263 3336 3485 3930 -114 548 113 C ATOM 1991 C ILE A 263 19.678 26.055 34.981 1.00 31.88 C ANISOU 1991 C ILE A 263 3849 3908 4356 -103 574 149 C ATOM 1992 O ILE A 263 20.005 25.898 33.798 1.00 30.35 O ANISOU 1992 O ILE A 263 3666 3693 4174 -100 603 184 O ATOM 1993 CB ILE A 263 21.352 25.707 36.845 1.00 18.66 C ANISOU 1993 CB ILE A 263 2100 2321 2670 -82 534 114 C ATOM 1994 CG1 ILE A 263 22.468 26.378 37.642 1.00 19.13 C ANISOU 1994 CG1 ILE A 263 2093 2417 2759 -92 508 78 C ATOM 1995 CG2 ILE A 263 21.931 24.590 35.995 1.00 20.66 C ANISOU 1995 CG2 ILE A 263 2373 2575 2903 -55 565 163 C ATOM 1996 CD1 ILE A 263 23.203 25.425 38.559 1.00 19.36 C ANISOU 1996 CD1 ILE A 263 2102 2509 2744 -55 492 79 C ATOM 1997 N CYS A 264 18.495 25.654 35.449 1.00 24.58 N ANISOU 1997 N CYS A 264 2961 2984 3394 -97 565 139 N ATOM 1998 CA CYS A 264 17.562 24.920 34.603 1.00 22.80 C ANISOU 1998 CA CYS A 264 2788 2735 3140 -87 587 166 C ATOM 1999 C CYS A 264 17.072 25.770 33.435 1.00 23.47 C ANISOU 1999 C CYS A 264 2884 2779 3255 -107 603 177 C ATOM 2000 O CYS A 264 17.014 25.299 32.293 1.00 23.62 O ANISOU 2000 O CYS A 264 2929 2782 3264 -97 628 208 O ATOM 2001 CB CYS A 264 16.386 24.427 35.448 1.00 23.85 C ANISOU 2001 CB CYS A 264 2951 2876 3235 -80 573 149 C ATOM 2002 SG CYS A 264 15.131 23.497 34.551 1.00 27.68 S ANISOU 2002 SG CYS A 264 3494 3334 3687 -73 597 171 S ATOM 2003 N TRP A 265 16.729 27.032 33.691 1.00 22.49 N ANISOU 2003 N TRP A 265 2742 2638 3167 -131 590 152 N ATOM 2004 CA TRP A 265 15.966 27.813 32.725 1.00 17.63 C ANISOU 2004 CA TRP A 265 2143 1984 2571 -143 605 164 C ATOM 2005 C TRP A 265 16.753 28.896 32.000 1.00 29.70 C ANISOU 2005 C TRP A 265 3642 3488 4157 -158 623 176 C ATOM 2006 O TRP A 265 16.346 29.293 30.906 1.00 18.93 O ANISOU 2006 O TRP A 265 2295 2096 2802 -157 646 202 O ATOM 2007 CB TRP A 265 14.753 28.453 33.409 1.00 23.68 C ANISOU 2007 CB TRP A 265 2919 2742 3337 -156 585 133 C ATOM 2008 CG TRP A 265 13.691 27.452 33.731 1.00 21.76 C ANISOU 2008 CG TRP A 265 2715 2512 3042 -142 578 130 C ATOM 2009 CD1 TRP A 265 13.417 26.907 34.951 1.00 19.61 C ANISOU 2009 CD1 TRP A 265 2443 2265 2740 -135 558 107 C ATOM 2010 CD2 TRP A 265 12.776 26.853 32.808 1.00 34.02 C ANISOU 2010 CD2 TRP A 265 4306 4052 4566 -133 593 151 C ATOM 2011 NE1 TRP A 265 12.377 26.013 34.846 1.00 26.07 N ANISOU 2011 NE1 TRP A 265 3301 3085 3521 -124 563 114 N ATOM 2012 CE2 TRP A 265 11.966 25.963 33.540 1.00 20.83 C ANISOU 2012 CE2 TRP A 265 2659 2398 2857 -125 583 138 C ATOM 2013 CE3 TRP A 265 12.560 26.988 31.433 1.00 22.01 C ANISOU 2013 CE3 TRP A 265 2802 2512 3048 -130 615 178 C ATOM 2014 CZ2 TRP A 265 10.957 25.210 32.943 1.00 22.79 C ANISOU 2014 CZ2 TRP A 265 2943 2640 3075 -119 594 146 C ATOM 2015 CZ3 TRP A 265 11.557 26.242 30.844 1.00 22.58 C ANISOU 2015 CZ3 TRP A 265 2911 2586 3084 -121 621 185 C ATOM 2016 CH2 TRP A 265 10.767 25.365 31.598 1.00 21.15 C ANISOU 2016 CH2 TRP A 265 2748 2416 2870 -118 610 167 C ATOM 2017 N LEU A 266 17.850 29.396 32.571 1.00 24.38 N ANISOU 2017 N LEU A 266 2921 2823 3521 -171 616 158 N ATOM 2018 CA LEU A 266 18.597 30.465 31.906 1.00 22.78 C ANISOU 2018 CA LEU A 266 2686 2590 3381 -188 638 170 C ATOM 2019 C LEU A 266 19.103 30.074 30.523 1.00 30.56 C ANISOU 2019 C LEU A 266 3684 3564 4365 -171 675 221 C ATOM 2020 O LEU A 266 18.968 30.889 29.593 1.00 29.30 O ANISOU 2020 O LEU A 266 3526 3368 4237 -176 703 245 O ATOM 2021 CB LEU A 266 19.745 30.943 32.801 1.00 24.77 C ANISOU 2021 CB LEU A 266 2879 2858 3673 -206 622 136 C ATOM 2022 CG LEU A 266 19.396 32.020 33.829 1.00 32.04 C ANISOU 2022 CG LEU A 266 3774 3771 4628 -233 598 82 C ATOM 2023 CD1 LEU A 266 20.636 32.450 34.588 1.00 36.34 C ANISOU 2023 CD1 LEU A 266 4257 4336 5214 -251 583 46 C ATOM 2024 CD2 LEU A 266 18.760 33.209 33.131 1.00 25.90 C ANISOU 2024 CD2 LEU A 266 3005 2938 3896 -250 622 91 C ATOM 2025 N PRO A 267 19.699 28.892 30.306 1.00 27.34 N ANISOU 2025 N PRO A 267 3286 3183 3921 -149 681 242 N ATOM 2026 CA PRO A 267 20.090 28.541 28.930 1.00 26.24 C ANISOU 2026 CA PRO A 267 3162 3031 3776 -130 718 290 C ATOM 2027 C PRO A 267 18.928 28.554 27.955 1.00 25.83 C ANISOU 2027 C PRO A 267 3157 2960 3698 -120 732 311 C ATOM 2028 O PRO A 267 19.080 29.036 26.826 1.00 18.16 O ANISOU 2028 O PRO A 267 2189 1968 2745 -114 763 345 O ATOM 2029 CB PRO A 267 20.683 27.135 29.086 1.00 20.45 C ANISOU 2029 CB PRO A 267 2438 2333 3000 -106 716 300 C ATOM 2030 CG PRO A 267 21.141 27.074 30.490 1.00 32.97 C ANISOU 2030 CG PRO A 267 3989 3948 4590 -114 684 264 C ATOM 2031 CD PRO A 267 20.130 27.860 31.266 1.00 23.64 C ANISOU 2031 CD PRO A 267 2810 2756 3416 -135 659 226 C ATOM 2032 N TYR A 268 17.762 28.049 28.361 1.00 19.51 N ANISOU 2032 N TYR A 268 2390 2169 2854 -116 711 292 N ATOM 2033 CA TYR A 268 16.605 28.104 27.476 1.00 20.54 C ANISOU 2033 CA TYR A 268 2560 2286 2960 -107 721 306 C ATOM 2034 C TYR A 268 16.127 29.536 27.282 1.00 18.59 C ANISOU 2034 C TYR A 268 2301 2009 2755 -122 726 306 C ATOM 2035 O TYR A 268 15.784 29.935 26.163 1.00 26.29 O ANISOU 2035 O TYR A 268 3291 2969 3729 -109 750 337 O ATOM 2036 CB TYR A 268 15.470 27.241 28.017 1.00 20.80 C ANISOU 2036 CB TYR A 268 2625 2334 2942 -103 698 282 C ATOM 2037 CG TYR A 268 14.261 27.263 27.121 1.00 20.58 C ANISOU 2037 CG TYR A 268 2632 2299 2888 -94 704 292 C ATOM 2038 CD1 TYR A 268 14.244 26.540 25.940 1.00 21.00 C ANISOU 2038 CD1 TYR A 268 2712 2360 2908 -73 725 317 C ATOM 2039 CD2 TYR A 268 13.143 28.017 27.446 1.00 23.02 C ANISOU 2039 CD2 TYR A 268 2946 2598 3203 -105 689 274 C ATOM 2040 CE1 TYR A 268 13.147 26.559 25.111 1.00 20.69 C ANISOU 2040 CE1 TYR A 268 2699 2320 2840 -63 728 321 C ATOM 2041 CE2 TYR A 268 12.037 28.042 26.622 1.00 24.81 C ANISOU 2041 CE2 TYR A 268 3200 2825 3403 -95 693 282 C ATOM 2042 CZ TYR A 268 12.046 27.311 25.454 1.00 26.66 C ANISOU 2042 CZ TYR A 268 3458 3070 3603 -74 711 304 C ATOM 2043 OH TYR A 268 10.953 27.324 24.619 1.00 23.36 O ANISOU 2043 OH TYR A 268 3063 2659 3154 -61 712 308 O ATOM 2044 N ALA A 269 16.087 30.319 28.361 1.00 27.37 N ANISOU 2044 N ALA A 269 3386 3112 3901 -145 706 272 N ATOM 2045 CA ALA A 269 15.645 31.704 28.253 1.00 28.37 C ANISOU 2045 CA ALA A 269 3500 3204 4073 -160 714 270 C ATOM 2046 C ALA A 269 16.600 32.522 27.393 1.00 25.51 C ANISOU 2046 C ALA A 269 3113 2814 3764 -162 752 303 C ATOM 2047 O ALA A 269 16.165 33.363 26.597 1.00 23.61 O ANISOU 2047 O ALA A 269 2881 2545 3545 -156 778 330 O ATOM 2048 CB ALA A 269 15.508 32.318 29.646 1.00 32.15 C ANISOU 2048 CB ALA A 269 3954 3681 4579 -185 685 220 C ATOM 2049 N GLY A 270 17.906 32.294 27.542 1.00 21.10 N ANISOU 2049 N GLY A 270 2523 2265 3231 -167 759 305 N ATOM 2050 CA GLY A 270 18.868 33.045 26.753 1.00 32.08 C ANISOU 2050 CA GLY A 270 3886 3627 4677 -170 798 338 C ATOM 2051 C GLY A 270 18.789 32.724 25.271 1.00 23.15 C ANISOU 2051 C GLY A 270 2785 2493 3518 -139 834 393 C ATOM 2052 O GLY A 270 18.810 33.624 24.426 1.00 26.20 O ANISOU 2052 O GLY A 270 3167 2848 3939 -133 870 428 O ATOM 2053 N VAL A 271 18.702 31.436 24.936 1.00 23.62 N ANISOU 2053 N VAL A 271 2875 2587 3514 -115 826 403 N ATOM 2054 CA VAL A 271 18.639 31.042 23.531 1.00 22.41 C ANISOU 2054 CA VAL A 271 2750 2437 3326 -83 858 450 C ATOM 2055 C VAL A 271 17.334 31.512 22.903 1.00 18.58 C ANISOU 2055 C VAL A 271 2298 1943 2818 -69 862 462 C ATOM 2056 O VAL A 271 17.310 31.966 21.752 1.00 20.95 O ANISOU 2056 O VAL A 271 2607 2232 3120 -46 896 505 O ATOM 2057 CB VAL A 271 18.825 29.520 23.393 1.00 26.78 C ANISOU 2057 CB VAL A 271 3329 3026 3820 -63 849 450 C ATOM 2058 CG1 VAL A 271 18.534 29.072 21.968 1.00 26.16 C ANISOU 2058 CG1 VAL A 271 3286 2957 3697 -29 876 488 C ATOM 2059 CG2 VAL A 271 20.238 29.133 23.792 1.00 29.79 C ANISOU 2059 CG2 VAL A 271 3676 3418 4226 -69 854 451 C ATOM 2060 N ALA A 272 16.229 31.411 23.645 1.00 18.29 N ANISOU 2060 N ALA A 272 2277 1913 2758 -79 827 426 N ATOM 2061 CA ALA A 272 14.950 31.884 23.131 1.00 23.17 C ANISOU 2061 CA ALA A 272 2922 2527 3356 -66 828 435 C ATOM 2062 C ALA A 272 14.997 33.377 22.834 1.00 30.01 C ANISOU 2062 C ALA A 272 3768 3354 4281 -69 856 458 C ATOM 2063 O ALA A 272 14.526 33.822 21.780 1.00 27.24 O ANISOU 2063 O ALA A 272 3434 2998 3919 -42 882 497 O ATOM 2064 CB ALA A 272 13.832 31.565 24.123 1.00 23.19 C ANISOU 2064 CB ALA A 272 2938 2542 3330 -80 787 390 C ATOM 2065 N PHE A 273 15.574 34.168 23.741 1.00 29.60 N ANISOU 2065 N PHE A 273 3680 3274 4294 -100 855 436 N ATOM 2066 CA PHE A 273 15.661 35.603 23.495 1.00 32.54 C ANISOU 2066 CA PHE A 273 4031 3600 4732 -107 888 456 C ATOM 2067 C PHE A 273 16.605 35.912 22.340 1.00 27.89 C ANISOU 2067 C PHE A 273 3432 2995 4171 -88 939 511 C ATOM 2068 O PHE A 273 16.368 36.856 21.578 1.00 25.66 O ANISOU 2068 O PHE A 273 3152 2683 3916 -72 977 551 O ATOM 2069 CB PHE A 273 16.095 36.345 24.757 1.00 33.59 C ANISOU 2069 CB PHE A 273 4124 3706 4930 -148 873 410 C ATOM 2070 CG PHE A 273 15.988 37.838 24.635 1.00 36.04 C ANISOU 2070 CG PHE A 273 4417 3963 5313 -158 907 421 C ATOM 2071 CD1 PHE A 273 14.758 38.437 24.416 1.00 36.73 C ANISOU 2071 CD1 PHE A 273 4529 4037 5390 -143 910 431 C ATOM 2072 CD2 PHE A 273 17.114 38.640 24.725 1.00 33.60 C ANISOU 2072 CD2 PHE A 273 4064 3616 5085 -182 937 423 C ATOM 2073 CE1 PHE A 273 14.650 39.806 24.297 1.00 33.91 C ANISOU 2073 CE1 PHE A 273 4157 3626 5100 -149 946 445 C ATOM 2074 CE2 PHE A 273 17.013 40.012 24.609 1.00 24.70 C ANISOU 2074 CE2 PHE A 273 2922 2433 4031 -192 974 434 C ATOM 2075 CZ PHE A 273 15.779 40.596 24.396 1.00 32.85 C ANISOU 2075 CZ PHE A 273 3981 3449 5050 -174 979 446 C ATOM 2076 N TYR A 274 17.686 35.140 22.196 1.00 26.78 N ANISOU 2076 N TYR A 274 3278 2872 4023 -88 944 518 N ATOM 2077 CA TYR A 274 18.559 35.346 21.045 1.00 26.77 C ANISOU 2077 CA TYR A 274 3270 2859 4042 -66 994 574 C ATOM 2078 C TYR A 274 17.812 35.095 19.743 1.00 23.74 C ANISOU 2078 C TYR A 274 2929 2494 3598 -19 1014 620 C ATOM 2079 O TYR A 274 17.946 35.862 18.783 1.00 23.86 O ANISOU 2079 O TYR A 274 2943 2487 3635 4 1061 672 O ATOM 2080 CB TYR A 274 19.788 34.444 21.121 1.00 28.22 C ANISOU 2080 CB TYR A 274 3435 3064 4222 -70 994 572 C ATOM 2081 CG TYR A 274 20.650 34.575 19.887 1.00 28.33 C ANISOU 2081 CG TYR A 274 3444 3070 4251 -43 1048 633 C ATOM 2082 CD1 TYR A 274 21.530 35.639 19.750 1.00 30.54 C ANISOU 2082 CD1 TYR A 274 3683 3307 4615 -58 1091 655 C ATOM 2083 CD2 TYR A 274 20.564 33.655 18.847 1.00 30.05 C ANISOU 2083 CD2 TYR A 274 3697 3321 4399 -3 1059 666 C ATOM 2084 CE1 TYR A 274 22.310 35.778 18.623 1.00 30.54 C ANISOU 2084 CE1 TYR A 274 3678 3298 4630 -32 1145 714 C ATOM 2085 CE2 TYR A 274 21.340 33.788 17.712 1.00 29.13 C ANISOU 2085 CE2 TYR A 274 3577 3199 4293 25 1111 722 C ATOM 2086 CZ TYR A 274 22.211 34.852 17.608 1.00 32.27 C ANISOU 2086 CZ TYR A 274 3934 3553 4774 11 1155 749 C ATOM 2087 OH TYR A 274 22.990 34.997 16.485 1.00 45.68 O ANISOU 2087 OH TYR A 274 5628 5245 6485 40 1210 809 O ATOM 2088 N ILE A 275 17.027 34.018 19.690 1.00 25.48 N ANISOU 2088 N ILE A 275 3184 2756 3740 -4 980 601 N ATOM 2089 CA ILE A 275 16.257 33.713 18.489 1.00 30.14 C ANISOU 2089 CA ILE A 275 3813 3374 4266 40 992 634 C ATOM 2090 C ILE A 275 15.235 34.808 18.219 1.00 28.17 C ANISOU 2090 C ILE A 275 3570 3106 4028 53 1002 652 C ATOM 2091 O ILE A 275 15.064 35.254 17.077 1.00 24.42 O ANISOU 2091 O ILE A 275 3108 2633 3539 92 1038 703 O ATOM 2092 CB ILE A 275 15.590 32.332 18.623 1.00 22.70 C ANISOU 2092 CB ILE A 275 2901 2476 3246 46 951 599 C ATOM 2093 CG1 ILE A 275 16.641 31.223 18.522 1.00 23.86 C ANISOU 2093 CG1 ILE A 275 3047 2643 3376 47 954 598 C ATOM 2094 CG2 ILE A 275 14.501 32.159 17.577 1.00 19.61 C ANISOU 2094 CG2 ILE A 275 2545 2115 2790 84 952 617 C ATOM 2095 CD1 ILE A 275 16.066 29.824 18.579 1.00 21.38 C ANISOU 2095 CD1 ILE A 275 2765 2367 2992 54 923 566 C ATOM 2096 N PHE A 276 14.547 35.265 19.268 1.00 24.57 N ANISOU 2096 N PHE A 276 3107 2633 3595 24 973 612 N ATOM 2097 CA PHE A 276 13.517 36.288 19.113 1.00 23.81 C ANISOU 2097 CA PHE A 276 3018 2520 3510 36 981 625 C ATOM 2098 C PHE A 276 14.081 37.559 18.483 1.00 34.39 C ANISOU 2098 C PHE A 276 4338 3813 4914 49 1040 679 C ATOM 2099 O PHE A 276 13.402 38.219 17.686 1.00 23.87 O ANISOU 2099 O PHE A 276 3021 2477 3570 85 1066 720 O ATOM 2100 CB PHE A 276 12.886 36.580 20.476 1.00 31.15 C ANISOU 2100 CB PHE A 276 3938 3434 4464 -1 943 570 C ATOM 2101 CG PHE A 276 11.825 37.643 20.451 1.00 29.19 C ANISOU 2101 CG PHE A 276 3696 3165 4232 10 951 579 C ATOM 2102 CD1 PHE A 276 10.666 37.474 19.711 1.00 30.35 C ANISOU 2102 CD1 PHE A 276 3871 3345 4316 48 944 598 C ATOM 2103 CD2 PHE A 276 11.979 38.804 21.192 1.00 32.21 C ANISOU 2103 CD2 PHE A 276 4051 3495 4690 -17 964 567 C ATOM 2104 CE1 PHE A 276 9.687 38.452 19.700 1.00 27.79 C ANISOU 2104 CE1 PHE A 276 3550 3003 4005 61 952 609 C ATOM 2105 CE2 PHE A 276 11.005 39.782 21.187 1.00 27.92 C ANISOU 2105 CE2 PHE A 276 3515 2930 4165 -5 975 577 C ATOM 2106 CZ PHE A 276 9.856 39.605 20.442 1.00 29.55 C ANISOU 2106 CZ PHE A 276 3750 3170 4307 36 969 600 C ATOM 2107 N THR A 277 15.322 37.913 18.820 1.00 29.41 N ANISOU 2107 N THR A 277 3674 3147 4353 22 1063 680 N ATOM 2108 CA THR A 277 15.964 39.106 18.284 1.00 25.95 C ANISOU 2108 CA THR A 277 3214 2658 3989 28 1124 729 C ATOM 2109 C THR A 277 16.796 38.835 17.034 1.00 27.32 C ANISOU 2109 C THR A 277 3391 2843 4148 64 1170 790 C ATOM 2110 O THR A 277 17.289 39.788 16.421 1.00 29.32 O ANISOU 2110 O THR A 277 3629 3056 4457 78 1229 841 O ATOM 2111 CB THR A 277 16.849 39.759 19.357 1.00 35.59 C ANISOU 2111 CB THR A 277 4388 3831 5302 -25 1128 692 C ATOM 2112 OG1 THR A 277 17.817 38.814 19.829 1.00 26.27 O ANISOU 2112 OG1 THR A 277 3191 2676 4116 -48 1103 662 O ATOM 2113 CG2 THR A 277 16.000 40.234 20.528 1.00 26.72 C ANISOU 2113 CG2 THR A 277 3262 2692 4199 -56 1091 636 C ATOM 2114 N HIS A 278 16.951 37.576 16.635 1.00 25.57 N ANISOU 2114 N HIS A 278 3190 2673 3854 82 1149 786 N ATOM 2115 CA HIS A 278 17.665 37.196 15.418 1.00 31.44 C ANISOU 2115 CA HIS A 278 3942 3435 4571 121 1189 840 C ATOM 2116 C HIS A 278 16.827 36.217 14.604 1.00 32.94 C ANISOU 2116 C HIS A 278 4175 3687 4656 164 1167 846 C ATOM 2117 O HIS A 278 17.289 35.146 14.204 1.00 26.16 O ANISOU 2117 O HIS A 278 3328 2863 3748 177 1160 843 O ATOM 2118 CB HIS A 278 19.032 36.589 15.727 1.00 34.16 C ANISOU 2118 CB HIS A 278 4259 3778 4943 96 1192 828 C ATOM 2119 CG HIS A 278 19.968 37.520 16.433 1.00 40.23 C ANISOU 2119 CG HIS A 278 4978 4491 5816 53 1216 821 C ATOM 2120 ND1 HIS A 278 19.813 37.871 17.757 1.00 21.46 N ANISOU 2120 ND1 HIS A 278 2578 2093 3484 5 1180 762 N ATOM 2121 CD2 HIS A 278 21.081 38.161 16.002 1.00 29.58 C ANISOU 2121 CD2 HIS A 278 3597 3106 4537 51 1273 862 C ATOM 2122 CE1 HIS A 278 20.783 38.696 18.108 1.00 22.49 C ANISOU 2122 CE1 HIS A 278 2662 2177 3708 -27 1211 762 C ATOM 2123 NE2 HIS A 278 21.567 38.888 17.062 1.00 42.06 N ANISOU 2123 NE2 HIS A 278 5132 4642 6205 -1 1269 823 N ATOM 2124 N GLN A 279 15.560 36.562 14.382 1.00 30.60 N ANISOU 2124 N GLN A 279 3901 3404 4323 186 1154 848 N ATOM 2125 CA GLN A 279 14.685 35.709 13.589 1.00 34.81 C ANISOU 2125 CA GLN A 279 4470 3997 4757 227 1132 847 C ATOM 2126 C GLN A 279 15.237 35.528 12.179 1.00 32.30 C ANISOU 2126 C GLN A 279 4166 3705 4403 280 1176 907 C ATOM 2127 O GLN A 279 15.748 36.469 11.565 1.00 27.95 O ANISOU 2127 O GLN A 279 3602 3124 3893 303 1233 967 O ATOM 2128 CB GLN A 279 13.276 36.299 13.534 1.00 28.12 C ANISOU 2128 CB GLN A 279 3638 3161 3886 246 1116 846 C ATOM 2129 CG GLN A 279 12.525 36.228 14.851 1.00 20.45 C ANISOU 2129 CG GLN A 279 2662 2180 2929 200 1065 782 C ATOM 2130 CD GLN A 279 11.145 36.837 14.761 1.00 31.97 C ANISOU 2130 CD GLN A 279 4133 3650 4366 222 1052 785 C ATOM 2131 OE1 GLN A 279 10.796 37.464 13.761 1.00 34.40 O ANISOU 2131 OE1 GLN A 279 4450 3967 4655 271 1086 838 O ATOM 2132 NE2 GLN A 279 10.349 36.655 15.808 1.00 27.27 N ANISOU 2132 NE2 GLN A 279 3537 3054 3769 188 1006 729 N ATOM 2133 N GLY A 280 15.148 34.297 11.676 1.00 27.88 N ANISOU 2133 N GLY A 280 3630 3198 3765 298 1154 889 N ATOM 2134 CA GLY A 280 15.609 33.971 10.344 1.00 38.92 C ANISOU 2134 CA GLY A 280 5043 4628 5115 351 1191 936 C ATOM 2135 C GLY A 280 17.098 33.750 10.210 1.00 38.80 C ANISOU 2135 C GLY A 280 5010 4592 5139 343 1228 961 C ATOM 2136 O GLY A 280 17.552 33.346 9.130 1.00 36.39 O ANISOU 2136 O GLY A 280 4720 4316 4790 387 1258 997 O ATOM 2137 N SER A 281 17.875 33.987 11.265 1.00 37.78 N ANISOU 2137 N SER A 281 4849 4416 5089 291 1226 940 N ATOM 2138 CA SER A 281 19.317 33.819 11.191 1.00 33.08 C ANISOU 2138 CA SER A 281 4231 3802 4537 282 1260 962 C ATOM 2139 C SER A 281 19.678 32.337 11.088 1.00 34.78 C ANISOU 2139 C SER A 281 4464 4059 4692 286 1236 932 C ATOM 2140 O SER A 281 18.830 31.447 11.198 1.00 30.85 O ANISOU 2140 O SER A 281 3994 3598 4129 288 1191 888 O ATOM 2141 CB SER A 281 19.995 34.460 12.403 1.00 29.66 C ANISOU 2141 CB SER A 281 3753 3314 4201 225 1258 939 C ATOM 2142 OG SER A 281 19.555 33.878 13.618 1.00 23.64 O ANISOU 2142 OG SER A 281 2990 2559 3432 182 1197 869 O ATOM 2143 N ASP A 282 20.966 32.078 10.883 1.00 34.05 N ANISOU 2143 N ASP A 282 4352 3956 4628 286 1268 955 N ATOM 2144 CA ASP A 282 21.458 30.729 10.611 1.00 33.91 C ANISOU 2144 CA ASP A 282 4351 3974 4557 298 1258 939 C ATOM 2145 C ASP A 282 21.718 30.018 11.933 1.00 31.35 C ANISOU 2145 C ASP A 282 4012 3644 4255 248 1213 879 C ATOM 2146 O ASP A 282 22.746 30.238 12.580 1.00 39.96 O ANISOU 2146 O ASP A 282 5065 4708 5411 219 1224 880 O ATOM 2147 CB ASP A 282 22.718 30.784 9.752 1.00 39.30 C ANISOU 2147 CB ASP A 282 5022 4653 5259 326 1317 996 C ATOM 2148 CG ASP A 282 23.070 29.437 9.153 1.00 37.55 C ANISOU 2148 CG ASP A 282 4827 4474 4968 354 1316 987 C ATOM 2149 OD1 ASP A 282 22.277 28.489 9.331 1.00 42.65 O ANISOU 2149 OD1 ASP A 282 5503 5151 5552 353 1271 938 O ATOM 2150 OD2 ASP A 282 24.131 29.322 8.503 1.00 56.64 O ANISOU 2150 OD2 ASP A 282 7235 6892 7396 378 1362 1029 O ATOM 2151 N PHE A 283 20.778 29.169 12.345 1.00 27.75 N ANISOU 2151 N PHE A 283 3584 3215 3745 240 1164 827 N ATOM 2152 CA PHE A 283 21.007 28.234 13.436 1.00 24.23 C ANISOU 2152 CA PHE A 283 3133 2771 3301 206 1126 776 C ATOM 2153 C PHE A 283 20.401 26.888 13.068 1.00 28.37 C ANISOU 2153 C PHE A 283 3700 3335 3746 225 1104 745 C ATOM 2154 O PHE A 283 19.443 26.809 12.294 1.00 29.80 O ANISOU 2154 O PHE A 283 3911 3542 3871 251 1099 744 O ATOM 2155 CB PHE A 283 20.444 28.740 14.780 1.00 24.79 C ANISOU 2155 CB PHE A 283 3186 2820 3414 160 1086 734 C ATOM 2156 CG PHE A 283 19.001 29.162 14.732 1.00 21.56 C ANISOU 2156 CG PHE A 283 2799 2418 2977 163 1063 719 C ATOM 2157 CD1 PHE A 283 17.987 28.249 14.972 1.00 22.05 C ANISOU 2157 CD1 PHE A 283 2891 2507 2980 161 1023 674 C ATOM 2158 CD2 PHE A 283 18.661 30.483 14.480 1.00 24.08 C ANISOU 2158 CD2 PHE A 283 3106 2713 3331 168 1083 749 C ATOM 2159 CE1 PHE A 283 16.661 28.641 14.943 1.00 24.58 C ANISOU 2159 CE1 PHE A 283 3227 2836 3275 164 1000 659 C ATOM 2160 CE2 PHE A 283 17.337 30.881 14.449 1.00 23.33 C ANISOU 2160 CE2 PHE A 283 3030 2626 3209 174 1062 737 C ATOM 2161 CZ PHE A 283 16.336 29.958 14.679 1.00 30.55 C ANISOU 2161 CZ PHE A 283 3971 3572 4063 172 1019 691 C ATOM 2162 N GLY A 284 20.979 25.827 13.628 1.00 26.75 N ANISOU 2162 N GLY A 284 3493 3135 3535 212 1091 719 N ATOM 2163 CA GLY A 284 20.578 24.478 13.312 1.00 21.42 C ANISOU 2163 CA GLY A 284 2856 2489 2794 227 1078 689 C ATOM 2164 C GLY A 284 19.667 23.867 14.356 1.00 21.45 C ANISOU 2164 C GLY A 284 2871 2494 2784 197 1031 632 C ATOM 2165 O GLY A 284 19.299 24.504 15.348 1.00 26.67 O ANISOU 2165 O GLY A 284 3513 3137 3483 165 1006 615 O ATOM 2166 N PRO A 285 19.276 22.607 14.138 1.00 25.03 N ANISOU 2166 N PRO A 285 3358 2968 3185 207 1021 600 N ATOM 2167 CA PRO A 285 18.340 21.957 15.072 1.00 20.33 C ANISOU 2167 CA PRO A 285 2776 2372 2577 179 982 547 C ATOM 2168 C PRO A 285 18.897 21.752 16.473 1.00 24.00 C ANISOU 2168 C PRO A 285 3216 2817 3084 149 966 533 C ATOM 2169 O PRO A 285 18.125 21.788 17.439 1.00 23.35 O ANISOU 2169 O PRO A 285 3133 2729 3010 123 934 500 O ATOM 2170 CB PRO A 285 18.038 20.616 14.388 1.00 19.88 C ANISOU 2170 CB PRO A 285 2756 2336 2461 199 987 522 C ATOM 2171 CG PRO A 285 18.407 20.822 12.947 1.00 21.07 C ANISOU 2171 CG PRO A 285 2918 2507 2582 240 1020 557 C ATOM 2172 CD PRO A 285 19.568 21.763 12.969 1.00 20.20 C ANISOU 2172 CD PRO A 285 2774 2379 2523 244 1048 609 C ATOM 2173 N ILE A 286 20.204 21.525 16.621 1.00 18.64 N ANISOU 2173 N ILE A 286 2518 2133 2432 155 988 556 N ATOM 2174 CA ILE A 286 20.759 21.254 17.944 1.00 33.89 C ANISOU 2174 CA ILE A 286 4426 4055 4397 132 972 542 C ATOM 2175 C ILE A 286 20.765 22.502 18.820 1.00 24.25 C ANISOU 2175 C ILE A 286 3166 2819 3228 103 953 541 C ATOM 2176 O ILE A 286 20.744 22.389 20.052 1.00 22.37 O ANISOU 2176 O ILE A 286 2913 2579 3009 80 927 515 O ATOM 2177 CB ILE A 286 22.172 20.653 17.806 1.00 34.01 C ANISOU 2177 CB ILE A 286 4426 4073 4422 150 1001 568 C ATOM 2178 CG1 ILE A 286 22.116 19.377 16.966 1.00 31.46 C ANISOU 2178 CG1 ILE A 286 4144 3762 4047 178 1021 563 C ATOM 2179 CG2 ILE A 286 22.781 20.341 19.165 1.00 27.55 C ANISOU 2179 CG2 ILE A 286 3580 3254 3633 132 983 554 C ATOM 2180 CD1 ILE A 286 21.195 18.317 17.528 1.00 39.47 C ANISOU 2180 CD1 ILE A 286 5190 4777 5030 169 999 519 C ATOM 2181 N PHE A 287 20.742 23.691 18.210 1.00 20.49 N ANISOU 2181 N PHE A 287 2676 2333 2777 104 967 568 N ATOM 2182 CA PHE A 287 20.937 24.935 18.954 1.00 27.67 C ANISOU 2182 CA PHE A 287 3546 3222 3746 77 958 569 C ATOM 2183 C PHE A 287 19.898 25.103 20.060 1.00 29.69 C ANISOU 2183 C PHE A 287 3804 3474 4003 50 916 526 C ATOM 2184 O PHE A 287 20.238 25.456 21.195 1.00 23.38 O ANISOU 2184 O PHE A 287 2974 2668 3242 24 897 506 O ATOM 2185 CB PHE A 287 20.904 26.116 17.981 1.00 30.02 C ANISOU 2185 CB PHE A 287 3836 3504 4065 88 987 607 C ATOM 2186 CG PHE A 287 21.097 27.458 18.633 1.00 36.97 C ANISOU 2186 CG PHE A 287 4676 4356 5014 60 986 608 C ATOM 2187 CD1 PHE A 287 22.182 27.700 19.459 1.00 30.50 C ANISOU 2187 CD1 PHE A 287 3812 3526 4249 37 985 602 C ATOM 2188 CD2 PHE A 287 20.202 28.488 18.392 1.00 19.14 C ANISOU 2188 CD2 PHE A 287 2424 2082 2767 58 986 614 C ATOM 2189 CE1 PHE A 287 22.359 28.941 20.049 1.00 36.73 C ANISOU 2189 CE1 PHE A 287 4563 4288 5106 8 984 596 C ATOM 2190 CE2 PHE A 287 20.374 29.729 18.975 1.00 20.62 C ANISOU 2190 CE2 PHE A 287 2576 2238 3022 31 989 613 C ATOM 2191 CZ PHE A 287 21.453 29.956 19.805 1.00 33.46 C ANISOU 2191 CZ PHE A 287 4157 3852 4705 4 987 602 C ATOM 2192 N MET A 288 18.624 24.849 19.753 1.00 18.28 N ANISOU 2192 N MET A 288 2394 2037 2514 55 902 508 N ATOM 2193 CA MET A 288 17.576 24.931 20.763 1.00 29.23 C ANISOU 2193 CA MET A 288 3786 3422 3899 31 864 468 C ATOM 2194 C MET A 288 17.255 23.585 21.407 1.00 17.63 C ANISOU 2194 C MET A 288 2338 1966 2394 29 846 436 C ATOM 2195 O MET A 288 16.715 23.565 22.517 1.00 26.57 O ANISOU 2195 O MET A 288 3466 3097 3532 9 818 406 O ATOM 2196 CB MET A 288 16.294 25.529 20.156 1.00 25.44 C ANISOU 2196 CB MET A 288 3325 2942 3398 37 858 467 C ATOM 2197 CG MET A 288 15.147 25.746 21.149 1.00 26.64 C ANISOU 2197 CG MET A 288 3480 3091 3550 13 823 428 C ATOM 2198 SD MET A 288 15.658 26.595 22.660 1.00 25.54 S ANISOU 2198 SD MET A 288 3300 2932 3473 -20 804 411 S ATOM 2199 CE MET A 288 14.964 28.226 22.410 1.00 26.11 C ANISOU 2199 CE MET A 288 3360 2980 3580 -26 808 423 C ATOM 2200 N THR A 289 17.603 22.470 20.759 1.00 22.53 N ANISOU 2200 N THR A 289 2981 2598 2980 50 864 443 N ATOM 2201 CA THR A 289 17.222 21.158 21.278 1.00 25.61 C ANISOU 2201 CA THR A 289 3395 2995 3338 50 854 414 C ATOM 2202 C THR A 289 17.802 20.908 22.667 1.00 21.22 C ANISOU 2202 C THR A 289 2818 2439 2808 37 840 403 C ATOM 2203 O THR A 289 17.091 20.460 23.576 1.00 17.20 O ANISOU 2203 O THR A 289 2318 1930 2288 25 819 374 O ATOM 2204 CB THR A 289 17.675 20.060 20.311 1.00 23.13 C ANISOU 2204 CB THR A 289 3107 2690 2991 77 883 425 C ATOM 2205 OG1 THR A 289 17.004 20.214 19.056 1.00 24.59 O ANISOU 2205 OG1 THR A 289 3315 2884 3144 92 891 427 O ATOM 2206 CG2 THR A 289 17.367 18.674 20.877 1.00 18.95 C ANISOU 2206 CG2 THR A 289 2603 2161 2438 76 879 396 C ATOM 2207 N AILE A 290 19.086 21.190 22.855 0.69 26.01 N ANISOU 2207 N AILE A 290 3391 3046 3445 40 852 426 N ATOM 2208 N BILE A 290 19.105 21.176 22.841 0.31 25.99 N ANISOU 2208 N BILE A 290 3389 3044 3442 41 852 426 N ATOM 2209 CA AILE A 290 19.757 20.912 24.124 0.69 23.50 C ANISOU 2209 CA AILE A 290 3047 2736 3144 34 838 417 C ATOM 2210 CA BILE A 290 19.749 20.908 24.125 0.31 23.86 C ANISOU 2210 CA BILE A 290 3094 2782 3190 34 838 416 C ATOM 2211 C AILE A 290 19.182 21.764 25.256 0.69 24.38 C ANISOU 2211 C AILE A 290 3138 2846 3278 8 804 390 C ATOM 2212 C BILE A 290 19.173 21.761 25.250 0.31 24.38 C ANISOU 2212 C BILE A 290 3138 2845 3278 8 804 390 C ATOM 2213 O AILE A 290 18.830 21.206 26.303 0.69 17.30 O ANISOU 2213 O AILE A 290 2247 1959 2369 4 785 367 O ATOM 2214 O BILE A 290 18.805 21.195 26.294 0.31 17.78 O ANISOU 2214 O BILE A 290 2309 2019 2429 4 785 367 O ATOM 2215 CB AILE A 290 21.280 21.093 24.003 0.69 23.79 C ANISOU 2215 CB AILE A 290 3048 2779 3211 44 857 445 C ATOM 2216 CB BILE A 290 21.276 21.056 23.992 0.31 23.79 C ANISOU 2216 CB BILE A 290 3050 2780 3210 45 857 445 C ATOM 2217 CG1AILE A 290 21.817 20.265 22.833 0.69 27.69 C ANISOU 2217 CG1AILE A 290 3565 3276 3681 73 893 473 C ATOM 2218 CG1BILE A 290 21.833 20.047 22.987 0.31 27.30 C ANISOU 2218 CG1BILE A 290 3518 3228 3628 75 891 470 C ATOM 2219 CG2AILE A 290 21.964 20.679 25.295 0.69 23.52 C ANISOU 2219 CG2AILE A 290 2987 2764 3187 44 840 434 C ATOM 2220 CG2BILE A 290 21.952 20.907 25.342 0.31 24.04 C ANISOU 2220 CG2BILE A 290 3047 2828 3259 39 838 433 C ATOM 2221 CD1AILE A 290 21.448 18.793 22.898 0.69 28.53 C ANISOU 2221 CD1AILE A 290 3711 3386 3744 90 899 460 C ATOM 2222 CD1BILE A 290 23.323 20.168 22.782 0.31 25.08 C ANISOU 2222 CD1BILE A 290 3201 2955 3375 87 914 501 C ATOM 2223 N PRO A 291 19.065 23.092 25.124 1.00 26.53 N ANISOU 2223 N PRO A 291 3388 3106 3585 -10 798 391 N ATOM 2224 CA PRO A 291 18.430 23.858 26.211 1.00 23.64 C ANISOU 2224 CA PRO A 291 3006 2736 3239 -34 767 361 C ATOM 2225 C PRO A 291 16.983 23.471 26.453 1.00 23.66 C ANISOU 2225 C PRO A 291 3045 2739 3208 -38 749 336 C ATOM 2226 O PRO A 291 16.523 23.503 27.603 1.00 26.13 O ANISOU 2226 O PRO A 291 3352 3057 3520 -50 724 309 O ATOM 2227 CB PRO A 291 18.548 25.317 25.743 1.00 31.11 C ANISOU 2227 CB PRO A 291 3928 3662 4230 -48 774 372 C ATOM 2228 CG PRO A 291 19.624 25.313 24.725 1.00 23.45 C ANISOU 2228 CG PRO A 291 2947 2688 3273 -32 808 410 C ATOM 2229 CD PRO A 291 19.505 23.992 24.041 1.00 17.75 C ANISOU 2229 CD PRO A 291 2264 1980 2500 -6 823 422 C ATOM 2230 N ALA A 292 16.255 23.092 25.401 1.00 17.05 N ANISOU 2230 N ALA A 292 2242 1897 2339 -27 763 344 N ATOM 2231 CA ALA A 292 14.836 22.784 25.542 1.00 20.38 C ANISOU 2231 CA ALA A 292 2692 2319 2732 -33 747 318 C ATOM 2232 C ALA A 292 14.620 21.491 26.316 1.00 19.60 C ANISOU 2232 C ALA A 292 2611 2228 2607 -30 742 299 C ATOM 2233 O ALA A 292 13.667 21.381 27.096 1.00 17.21 O ANISOU 2233 O ALA A 292 2316 1925 2296 -41 723 274 O ATOM 2234 CB ALA A 292 14.178 22.700 24.167 1.00 22.30 C ANISOU 2234 CB ALA A 292 2962 2562 2948 -20 761 328 C ATOM 2235 N PHE A 293 15.477 20.494 26.104 1.00 23.77 N ANISOU 2235 N PHE A 293 3146 2762 3123 -12 762 314 N ATOM 2236 CA PHE A 293 15.331 19.239 26.827 1.00 19.24 C ANISOU 2236 CA PHE A 293 2590 2192 2528 -5 765 302 C ATOM 2237 C PHE A 293 16.028 19.259 28.178 1.00 22.04 C ANISOU 2237 C PHE A 293 2917 2559 2897 -4 752 301 C ATOM 2238 O PHE A 293 15.610 18.537 29.090 1.00 16.68 O ANISOU 2238 O PHE A 293 2250 1884 2204 0 747 288 O ATOM 2239 CB PHE A 293 15.851 18.074 25.983 1.00 16.84 C ANISOU 2239 CB PHE A 293 2310 1886 2203 17 797 316 C ATOM 2240 CG PHE A 293 14.820 17.504 25.057 1.00 19.19 C ANISOU 2240 CG PHE A 293 2643 2175 2472 17 806 300 C ATOM 2241 CD1 PHE A 293 14.424 18.201 23.928 1.00 23.50 C ANISOU 2241 CD1 PHE A 293 3193 2724 3012 16 805 302 C ATOM 2242 CD2 PHE A 293 14.231 16.282 25.325 1.00 16.77 C ANISOU 2242 CD2 PHE A 293 2365 1861 2147 18 816 280 C ATOM 2243 CE1 PHE A 293 13.467 17.682 23.077 1.00 31.08 C ANISOU 2243 CE1 PHE A 293 4183 3685 3943 16 810 282 C ATOM 2244 CE2 PHE A 293 13.275 15.757 24.479 1.00 17.89 C ANISOU 2244 CE2 PHE A 293 2535 1996 2266 14 823 257 C ATOM 2245 CZ PHE A 293 12.891 16.458 23.354 1.00 20.70 C ANISOU 2245 CZ PHE A 293 2892 2361 2610 13 818 256 C ATOM 2246 N PHE A 294 17.078 20.068 28.327 1.00 23.22 N ANISOU 2246 N PHE A 294 3030 2717 3076 -5 747 314 N ATOM 2247 CA PHE A 294 17.680 20.248 29.643 1.00 21.44 C ANISOU 2247 CA PHE A 294 2771 2511 2863 -6 728 305 C ATOM 2248 C PHE A 294 16.688 20.878 30.611 1.00 25.24 C ANISOU 2248 C PHE A 294 3250 2993 3348 -25 698 275 C ATOM 2249 O PHE A 294 16.628 20.500 31.787 1.00 25.04 O ANISOU 2249 O PHE A 294 3219 2986 3311 -18 684 262 O ATOM 2250 CB PHE A 294 18.943 21.102 29.533 1.00 23.10 C ANISOU 2250 CB PHE A 294 2937 2729 3110 -9 727 318 C ATOM 2251 CG PHE A 294 19.688 21.249 30.827 1.00 30.89 C ANISOU 2251 CG PHE A 294 3885 3744 4108 -7 706 306 C ATOM 2252 CD1 PHE A 294 20.195 20.136 31.476 1.00 26.72 C ANISOU 2252 CD1 PHE A 294 3358 3240 3553 20 710 314 C ATOM 2253 CD2 PHE A 294 19.894 22.498 31.388 1.00 26.72 C ANISOU 2253 CD2 PHE A 294 3316 3220 3616 -30 682 284 C ATOM 2254 CE1 PHE A 294 20.887 20.264 32.664 1.00 39.01 C ANISOU 2254 CE1 PHE A 294 4877 4831 5114 27 688 302 C ATOM 2255 CE2 PHE A 294 20.584 22.633 32.579 1.00 32.82 C ANISOU 2255 CE2 PHE A 294 4050 4025 4395 -27 659 266 C ATOM 2256 CZ PHE A 294 21.081 21.514 33.218 1.00 44.82 C ANISOU 2256 CZ PHE A 294 5571 5576 5883 2 660 276 C ATOM 2257 N ALA A 295 15.889 21.833 30.128 1.00 21.47 N ANISOU 2257 N ALA A 295 2776 2499 2884 -44 690 265 N ATOM 2258 CA ALA A 295 14.912 22.500 30.978 1.00 21.20 C ANISOU 2258 CA ALA A 295 2739 2463 2855 -62 664 236 C ATOM 2259 C ALA A 295 13.843 21.548 31.498 1.00 16.45 C ANISOU 2259 C ALA A 295 2168 1862 2218 -57 662 222 C ATOM 2260 O ALA A 295 13.165 21.877 32.476 1.00 20.24 O ANISOU 2260 O ALA A 295 2645 2348 2698 -66 642 199 O ATOM 2261 CB ALA A 295 14.256 23.653 30.216 1.00 21.53 C ANISOU 2261 CB ALA A 295 2780 2484 2917 -79 662 234 C ATOM 2262 N LYS A 296 13.683 20.375 30.881 1.00 16.63 N ANISOU 2262 N LYS A 296 2222 1880 2216 -43 685 234 N ATOM 2263 CA LYS A 296 12.655 19.435 31.305 1.00 16.28 C ANISOU 2263 CA LYS A 296 2207 1831 2146 -41 689 220 C ATOM 2264 C LYS A 296 13.014 18.689 32.582 1.00 21.80 C ANISOU 2264 C LYS A 296 2903 2547 2834 -25 690 221 C ATOM 2265 O LYS A 296 12.134 18.049 33.168 1.00 16.28 O ANISOU 2265 O LYS A 296 2223 1843 2119 -24 694 210 O ATOM 2266 CB LYS A 296 12.354 18.443 30.180 1.00 19.40 C ANISOU 2266 CB LYS A 296 2635 2212 2523 -35 716 226 C ATOM 2267 CG LYS A 296 11.820 19.127 28.925 1.00 18.17 C ANISOU 2267 CG LYS A 296 2486 2049 2370 -46 714 224 C ATOM 2268 CD LYS A 296 11.403 18.124 27.871 1.00 16.27 C ANISOU 2268 CD LYS A 296 2277 1799 2106 -40 737 220 C ATOM 2269 CE LYS A 296 11.164 18.789 26.523 1.00 16.32 C ANISOU 2269 CE LYS A 296 2285 1806 2108 -41 737 225 C ATOM 2270 NZ LYS A 296 10.183 19.862 26.593 1.00 16.22 N ANISOU 2270 NZ LYS A 296 2264 1795 2102 -56 714 212 N ATOM 2271 N THR A 297 14.269 18.763 33.038 1.00 16.53 N ANISOU 2271 N THR A 297 2208 1899 2173 -10 687 235 N ATOM 2272 CA THR A 297 14.585 18.292 34.382 1.00 20.87 C ANISOU 2272 CA THR A 297 2748 2474 2709 9 681 235 C ATOM 2273 C THR A 297 13.873 19.106 35.449 1.00 16.60 C ANISOU 2273 C THR A 297 2192 1944 2169 -4 651 207 C ATOM 2274 O THR A 297 13.954 18.754 36.630 1.00 22.05 O ANISOU 2274 O THR A 297 2876 2659 2842 14 644 204 O ATOM 2275 CB THR A 297 16.093 18.343 34.651 1.00 16.91 C ANISOU 2275 CB THR A 297 2211 1999 2213 28 678 251 C ATOM 2276 OG1 THR A 297 16.532 19.707 34.662 1.00 20.38 O ANISOU 2276 OG1 THR A 297 2613 2448 2684 7 652 236 O ATOM 2277 CG2 THR A 297 16.860 17.575 33.595 1.00 24.01 C ANISOU 2277 CG2 THR A 297 3122 2888 3112 43 710 280 C ATOM 2278 N SER A 298 13.186 20.184 35.060 1.00 16.46 N ANISOU 2278 N SER A 298 2171 1912 2171 -31 635 188 N ATOM 2279 CA SER A 298 12.456 21.010 36.011 1.00 19.89 C ANISOU 2279 CA SER A 298 2594 2353 2609 -44 608 161 C ATOM 2280 C SER A 298 11.379 20.232 36.751 1.00 22.18 C ANISOU 2280 C SER A 298 2911 2644 2873 -36 614 154 C ATOM 2281 O SER A 298 10.952 20.658 37.828 1.00 24.12 O ANISOU 2281 O SER A 298 3147 2905 3113 -36 595 135 O ATOM 2282 CB SER A 298 11.824 22.204 35.294 1.00 16.30 C ANISOU 2282 CB SER A 298 2136 1877 2181 -71 598 147 C ATOM 2283 OG SER A 298 10.883 21.774 34.325 1.00 24.31 O ANISOU 2283 OG SER A 298 3183 2868 3186 -77 614 153 O ATOM 2284 N ALA A 299 10.930 19.110 36.201 1.00 18.13 N ANISOU 2284 N ALA A 299 2430 2112 2346 -29 642 168 N ATOM 2285 CA ALA A 299 9.863 18.347 36.828 1.00 27.97 C ANISOU 2285 CA ALA A 299 3701 3352 3574 -24 654 163 C ATOM 2286 C ALA A 299 10.360 17.378 37.892 1.00 19.56 C ANISOU 2286 C ALA A 299 2638 2307 2486 8 669 180 C ATOM 2287 O ALA A 299 9.533 16.721 38.533 1.00 19.27 O ANISOU 2287 O ALA A 299 2620 2264 2436 16 683 180 O ATOM 2288 CB ALA A 299 9.077 17.577 35.763 1.00 17.86 C ANISOU 2288 CB ALA A 299 2452 2040 2292 -35 679 164 C ATOM 2289 N AVAL A 300 11.673 17.263 38.095 0.41 21.41 N ANISOU 2289 N AVAL A 300 2852 2565 2716 30 667 197 N ATOM 2290 N BVAL A 300 11.671 17.265 38.101 0.59 21.41 N ANISOU 2290 N BVAL A 300 2853 2566 2717 30 667 196 N ATOM 2291 CA AVAL A 300 12.206 16.249 38.999 0.41 21.46 C ANISOU 2291 CA AVAL A 300 2862 2593 2698 68 686 220 C ATOM 2292 CA BVAL A 300 12.183 16.256 39.021 0.59 21.45 C ANISOU 2292 CA BVAL A 300 2861 2592 2697 68 685 219 C ATOM 2293 C AVAL A 300 13.093 16.865 40.077 0.41 22.64 C ANISOU 2293 C AVAL A 300 2973 2792 2837 88 656 214 C ATOM 2294 C BVAL A 300 13.096 16.864 40.082 0.59 22.67 C ANISOU 2294 C BVAL A 300 2976 2796 2841 88 656 214 C ATOM 2295 O AVAL A 300 13.177 16.340 41.194 0.41 27.47 O ANISOU 2295 O AVAL A 300 3583 3432 3422 120 660 224 O ATOM 2296 O BVAL A 300 13.210 16.328 41.189 0.59 27.62 O ANISOU 2296 O BVAL A 300 3602 3452 3440 121 660 225 O ATOM 2297 CB AVAL A 300 12.984 15.177 38.210 0.41 22.53 C ANISOU 2297 CB AVAL A 300 3013 2715 2834 87 720 250 C ATOM 2298 CB BVAL A 300 12.910 15.138 38.245 0.59 22.51 C ANISOU 2298 CB BVAL A 300 3012 2711 2830 87 721 249 C ATOM 2299 CG1AVAL A 300 13.474 14.074 39.134 0.41 29.79 C ANISOU 2299 CG1AVAL A 300 3938 3654 3728 131 745 279 C ATOM 2300 CG1BVAL A 300 14.199 15.658 37.613 0.59 21.53 C ANISOU 2300 CG1BVAL A 300 2859 2601 2719 87 709 257 C ATOM 2301 CG2AVAL A 300 12.121 14.593 37.102 0.41 19.22 C ANISOU 2301 CG2AVAL A 300 2629 2250 2424 66 747 246 C ATOM 2302 CG2BVAL A 300 13.184 13.946 39.151 0.59 30.37 C ANISOU 2302 CG2BVAL A 300 4019 3719 3800 129 750 278 C ATOM 2303 N TYR A 301 13.732 17.999 39.774 1.00 23.56 N ANISOU 2303 N TYR A 301 3056 2920 2975 68 626 196 N ATOM 2304 CA TYR A 301 14.830 18.455 40.630 1.00 24.93 C ANISOU 2304 CA TYR A 301 3188 3143 3143 86 600 190 C ATOM 2305 C TYR A 301 14.353 19.037 41.958 1.00 25.17 C ANISOU 2305 C TYR A 301 3203 3205 3156 91 572 161 C ATOM 2306 O TYR A 301 15.053 18.898 42.968 1.00 27.79 O ANISOU 2306 O TYR A 301 3510 3586 3462 122 558 161 O ATOM 2307 CB TYR A 301 15.731 19.454 39.886 1.00 19.98 C ANISOU 2307 CB TYR A 301 2526 2514 2552 62 583 178 C ATOM 2308 CG TYR A 301 15.220 20.873 39.736 1.00 19.22 C ANISOU 2308 CG TYR A 301 2414 2402 2486 23 557 143 C ATOM 2309 CD1 TYR A 301 15.258 21.774 40.795 1.00 17.46 C ANISOU 2309 CD1 TYR A 301 2160 2210 2265 18 523 107 C ATOM 2310 CD2 TYR A 301 14.762 21.330 38.514 1.00 23.27 C ANISOU 2310 CD2 TYR A 301 2943 2872 3028 -6 567 145 C ATOM 2311 CE1 TYR A 301 14.806 23.073 40.649 1.00 26.31 C ANISOU 2311 CE1 TYR A 301 3268 3310 3419 -17 504 75 C ATOM 2312 CE2 TYR A 301 14.316 22.626 38.356 1.00 22.29 C ANISOU 2312 CE2 TYR A 301 2805 2731 2934 -37 548 118 C ATOM 2313 CZ TYR A 301 14.340 23.494 39.423 1.00 23.92 C ANISOU 2313 CZ TYR A 301 2982 2960 3145 -44 518 83 C ATOM 2314 OH TYR A 301 13.888 24.784 39.250 1.00 26.89 O ANISOU 2314 OH TYR A 301 3346 3314 3556 -74 504 57 O ATOM 2315 N ASN A 302 13.199 19.702 41.988 1.00 20.31 N ANISOU 2315 N ASN A 302 2600 2566 2550 64 562 136 N ATOM 2316 CA ASN A 302 12.773 20.350 43.227 1.00 24.56 C ANISOU 2316 CA ASN A 302 3123 3136 3074 68 534 105 C ATOM 2317 C ASN A 302 12.549 19.374 44.379 1.00 26.60 C ANISOU 2317 C ASN A 302 3394 3425 3286 112 547 123 C ATOM 2318 O ASN A 302 12.990 19.684 45.500 1.00 22.70 O ANISOU 2318 O ASN A 302 2874 2984 2768 135 522 106 O ATOM 2319 CB ASN A 302 11.527 21.210 42.971 1.00 19.70 C ANISOU 2319 CB ASN A 302 2520 2485 2478 33 525 79 C ATOM 2320 CG ASN A 302 11.875 22.613 42.501 1.00 28.81 C ANISOU 2320 CG ASN A 302 3644 3629 3673 -1 500 50 C ATOM 2321 OD1 ASN A 302 12.703 23.294 43.107 1.00 30.32 O ANISOU 2321 OD1 ASN A 302 3798 3853 3871 0 473 25 O ATOM 2322 ND2 ASN A 302 11.242 23.050 41.418 1.00 17.66 N ANISOU 2322 ND2 ASN A 302 2248 2172 2289 -31 508 51 N ATOM 2323 N PRO A 303 11.887 18.223 44.206 1.00 19.73 N ANISOU 2323 N PRO A 303 2564 2530 2403 126 586 154 N ATOM 2324 CA PRO A 303 11.826 17.260 45.321 1.00 25.33 C ANISOU 2324 CA PRO A 303 3285 3270 3071 174 605 178 C ATOM 2325 C PRO A 303 13.187 16.736 45.754 1.00 26.60 C ANISOU 2325 C PRO A 303 3422 3477 3206 217 605 202 C ATOM 2326 O PRO A 303 13.349 16.366 46.924 1.00 19.62 O ANISOU 2326 O PRO A 303 2532 2641 2283 262 605 212 O ATOM 2327 CB PRO A 303 10.939 16.138 44.766 1.00 33.58 C ANISOU 2327 CB PRO A 303 4374 4263 4121 172 653 207 C ATOM 2328 CG PRO A 303 10.120 16.795 43.710 1.00 22.34 C ANISOU 2328 CG PRO A 303 2961 2794 2733 121 646 183 C ATOM 2329 CD PRO A 303 11.019 17.811 43.087 1.00 27.00 C ANISOU 2329 CD PRO A 303 3520 3393 3346 99 614 164 C ATOM 2330 N VAL A 304 14.167 16.674 44.848 1.00 23.14 N ANISOU 2330 N VAL A 304 2971 3031 2789 210 607 213 N ATOM 2331 CA VAL A 304 15.495 16.189 45.222 1.00 21.22 C ANISOU 2331 CA VAL A 304 2702 2836 2524 252 607 236 C ATOM 2332 C VAL A 304 16.146 17.138 46.222 1.00 22.84 C ANISOU 2332 C VAL A 304 2858 3107 2714 262 558 201 C ATOM 2333 O VAL A 304 16.724 16.710 47.228 1.00 28.28 O ANISOU 2333 O VAL A 304 3529 3855 3361 311 554 213 O ATOM 2334 CB VAL A 304 16.372 15.999 43.973 1.00 22.85 C ANISOU 2334 CB VAL A 304 2904 3018 2761 238 620 252 C ATOM 2335 CG1 VAL A 304 17.687 15.334 44.352 1.00 29.41 C ANISOU 2335 CG1 VAL A 304 3710 3896 3567 287 626 282 C ATOM 2336 CG2 VAL A 304 15.637 15.175 42.937 1.00 31.44 C ANISOU 2336 CG2 VAL A 304 4040 4041 3866 223 664 275 C ATOM 2337 N ILE A 305 16.064 18.443 45.953 1.00 18.64 N ANISOU 2337 N ILE A 305 2302 2567 2214 216 523 155 N ATOM 2338 CA ILE A 305 16.566 19.435 46.900 1.00 24.80 C ANISOU 2338 CA ILE A 305 3033 3404 2984 218 476 111 C ATOM 2339 C ILE A 305 15.817 19.326 48.221 1.00 27.14 C ANISOU 2339 C ILE A 305 3340 3737 3236 249 469 100 C ATOM 2340 O ILE A 305 16.400 19.482 49.301 1.00 23.35 O ANISOU 2340 O ILE A 305 2826 3326 2720 282 442 83 O ATOM 2341 CB ILE A 305 16.443 20.848 46.299 1.00 32.47 C ANISOU 2341 CB ILE A 305 3984 4345 4007 160 449 64 C ATOM 2342 CG1 ILE A 305 17.253 20.952 45.005 1.00 23.71 C ANISOU 2342 CG1 ILE A 305 2864 3204 2942 135 460 79 C ATOM 2343 CG2 ILE A 305 16.881 21.900 47.304 1.00 23.55 C ANISOU 2343 CG2 ILE A 305 2806 3269 2874 157 403 10 C ATOM 2344 CD1 ILE A 305 17.075 22.267 44.294 1.00 24.59 C ANISOU 2344 CD1 ILE A 305 2960 3275 3106 81 445 45 C ATOM 2345 N TYR A 306 14.512 19.060 48.145 1.00 28.11 N ANISOU 2345 N TYR A 306 3507 3817 3358 238 493 110 N ATOM 2346 CA TYR A 306 13.685 18.895 49.336 1.00 27.66 C ANISOU 2346 CA TYR A 306 3464 3787 3260 268 493 106 C ATOM 2347 C TYR A 306 14.245 17.812 50.251 1.00 21.83 C ANISOU 2347 C TYR A 306 2725 3104 2467 336 511 146 C ATOM 2348 O TYR A 306 14.443 18.034 51.451 1.00 25.87 O ANISOU 2348 O TYR A 306 3214 3681 2934 373 487 129 O ATOM 2349 CB TYR A 306 12.260 18.550 48.899 1.00 27.25 C ANISOU 2349 CB TYR A 306 3460 3671 3223 246 527 121 C ATOM 2350 CG TYR A 306 11.160 18.828 49.895 1.00 27.48 C ANISOU 2350 CG TYR A 306 3502 3713 3228 255 522 103 C ATOM 2351 CD1 TYR A 306 11.402 19.543 51.059 1.00 19.00 C ANISOU 2351 CD1 TYR A 306 2396 2700 2121 275 485 67 C ATOM 2352 CD2 TYR A 306 9.871 18.365 49.663 1.00 31.12 C ANISOU 2352 CD2 TYR A 306 4003 4124 3698 243 556 120 C ATOM 2353 CE1 TYR A 306 10.386 19.793 51.962 1.00 28.67 C ANISOU 2353 CE1 TYR A 306 3634 3937 3323 286 484 52 C ATOM 2354 CE2 TYR A 306 8.851 18.605 50.559 1.00 18.43 C ANISOU 2354 CE2 TYR A 306 2406 2527 2070 252 556 106 C ATOM 2355 CZ TYR A 306 9.112 19.323 51.705 1.00 26.70 C ANISOU 2355 CZ TYR A 306 3425 3635 3083 274 520 74 C ATOM 2356 OH TYR A 306 8.095 19.565 52.601 1.00 21.85 O ANISOU 2356 OH TYR A 306 2823 3033 2447 286 521 61 O ATOM 2357 N ILE A 307 14.519 16.633 49.690 1.00 19.70 N ANISOU 2357 N ILE A 307 2479 2808 2196 357 554 198 N ATOM 2358 CA ILE A 307 14.983 15.504 50.491 1.00 20.85 C ANISOU 2358 CA ILE A 307 2630 2998 2294 427 581 245 C ATOM 2359 C ILE A 307 16.362 15.785 51.074 1.00 27.51 C ANISOU 2359 C ILE A 307 3422 3923 3109 461 544 234 C ATOM 2360 O ILE A 307 16.642 15.453 52.232 1.00 28.81 O ANISOU 2360 O ILE A 307 3573 4156 3218 520 539 246 O ATOM 2361 CB ILE A 307 14.971 14.222 49.640 1.00 23.34 C ANISOU 2361 CB ILE A 307 2985 3259 2625 436 639 301 C ATOM 2362 CG1 ILE A 307 13.529 13.804 49.350 1.00 35.34 C ANISOU 2362 CG1 ILE A 307 4554 4711 4164 412 677 310 C ATOM 2363 CG2 ILE A 307 15.740 13.106 50.327 1.00 25.35 C ANISOU 2363 CG2 ILE A 307 3239 3559 2836 510 668 353 C ATOM 2364 CD1 ILE A 307 13.397 12.780 48.247 1.00 44.84 C ANISOU 2364 CD1 ILE A 307 5792 5846 5398 400 729 346 C ATOM 2365 N MET A 308 17.244 16.402 50.287 1.00 25.64 N ANISOU 2365 N MET A 308 3151 3682 2908 427 518 211 N ATOM 2366 CA MET A 308 18.601 16.644 50.760 1.00 25.11 C ANISOU 2366 CA MET A 308 3028 3691 2820 456 484 198 C ATOM 2367 C MET A 308 18.661 17.732 51.827 1.00 21.81 C ANISOU 2367 C MET A 308 2568 3339 2379 455 428 137 C ATOM 2368 O MET A 308 19.503 17.661 52.729 1.00 31.21 O ANISOU 2368 O MET A 308 3719 4614 3525 503 403 131 O ATOM 2369 CB MET A 308 19.507 17.008 49.585 1.00 31.32 C ANISOU 2369 CB MET A 308 3791 4452 3658 416 476 191 C ATOM 2370 CG MET A 308 19.769 15.851 48.634 1.00 37.13 C ANISOU 2370 CG MET A 308 4559 5142 4406 430 528 250 C ATOM 2371 SD MET A 308 20.963 16.274 47.351 1.00 63.51 S ANISOU 2371 SD MET A 308 7866 8464 7800 393 519 245 S ATOM 2372 CE MET A 308 22.213 17.123 48.317 1.00 53.27 C ANISOU 2372 CE MET A 308 6489 7266 6486 411 460 201 C ATOM 2373 N MET A 309 17.789 18.741 51.752 1.00 20.72 N ANISOU 2373 N MET A 309 2437 3167 2270 404 409 90 N ATOM 2374 CA MET A 309 17.964 19.953 52.545 1.00 21.03 C ANISOU 2374 CA MET A 309 2431 3258 2303 390 354 20 C ATOM 2375 C MET A 309 16.836 20.234 53.534 1.00 28.80 C ANISOU 2375 C MET A 309 3435 4255 3253 402 348 -2 C ATOM 2376 O MET A 309 16.811 21.321 54.121 1.00 32.04 O ANISOU 2376 O MET A 309 3814 4697 3664 384 305 -65 O ATOM 2377 CB MET A 309 18.138 21.162 51.625 1.00 30.31 C ANISOU 2377 CB MET A 309 3583 4386 3549 318 331 -27 C ATOM 2378 CG MET A 309 19.342 21.068 50.713 1.00 30.44 C ANISOU 2378 CG MET A 309 3569 4395 3600 304 333 -13 C ATOM 2379 SD MET A 309 19.680 22.612 49.847 1.00 30.77 S ANISOU 2379 SD MET A 309 3573 4394 3724 226 306 -72 S ATOM 2380 CE MET A 309 20.311 23.637 51.175 1.00 32.29 C ANISOU 2380 CE MET A 309 3697 4673 3897 232 245 -151 C ATOM 2381 N ASN A 310 15.900 19.311 53.734 1.00 20.90 N ANISOU 2381 N ASN A 310 2485 3230 2226 431 391 47 N ATOM 2382 CA ASN A 310 14.905 19.455 54.793 1.00 31.10 C ANISOU 2382 CA ASN A 310 3795 4544 3477 454 389 33 C ATOM 2383 C ASN A 310 14.960 18.207 55.663 1.00 28.52 C ANISOU 2383 C ASN A 310 3486 4265 3084 533 421 91 C ATOM 2384 O ASN A 310 14.521 17.131 55.243 1.00 34.15 O ANISOU 2384 O ASN A 310 4243 4931 3802 548 475 152 O ATOM 2385 CB ASN A 310 13.502 19.684 54.235 1.00 25.81 C ANISOU 2385 CB ASN A 310 3169 3792 2845 407 413 32 C ATOM 2386 CG ASN A 310 12.581 20.359 55.242 1.00 34.12 C ANISOU 2386 CG ASN A 310 4225 4868 3872 412 394 -7 C ATOM 2387 OD1 ASN A 310 11.836 19.696 55.964 1.00 25.93 O ANISOU 2387 OD1 ASN A 310 3217 3842 2794 453 423 24 O ATOM 2388 ND2 ASN A 310 12.643 21.684 55.303 1.00 30.94 N ANISOU 2388 ND2 ASN A 310 3790 4471 3494 371 350 -75 N ATOM 2389 N LYS A 311 15.501 18.360 56.873 1.00 30.49 N ANISOU 2389 N LYS A 311 3701 4610 3272 586 390 72 N ATOM 2390 CA LYS A 311 15.628 17.230 57.787 1.00 22.46 C ANISOU 2390 CA LYS A 311 2697 3650 2186 671 420 129 C ATOM 2391 C LYS A 311 14.262 16.667 58.162 1.00 30.17 C ANISOU 2391 C LYS A 311 3728 4587 3147 688 468 166 C ATOM 2392 O LYS A 311 14.085 15.445 58.242 1.00 26.38 O ANISOU 2392 O LYS A 311 3282 4092 2648 735 524 237 O ATOM 2393 CB LYS A 311 16.398 17.668 59.033 1.00 32.81 C ANISOU 2393 CB LYS A 311 3957 5078 3430 723 370 91 C ATOM 2394 CG LYS A 311 16.647 16.574 60.054 1.00 32.83 C ANISOU 2394 CG LYS A 311 3966 5154 3352 821 397 151 C ATOM 2395 CD LYS A 311 17.343 17.140 61.280 1.00 35.87 C ANISOU 2395 CD LYS A 311 4297 5663 3668 870 340 102 C ATOM 2396 CE LYS A 311 17.527 16.093 62.364 1.00 46.74 C ANISOU 2396 CE LYS A 311 5681 7120 4956 976 367 165 C ATOM 2397 NZ LYS A 311 18.226 16.657 63.564 1.00 59.26 N ANISOU 2397 NZ LYS A 311 7211 8838 6468 1028 307 112 N ATOM 2398 N GLN A 312 13.282 17.544 58.391 1.00 22.09 N ANISOU 2398 N GLN A 312 2713 3543 2137 651 450 120 N ATOM 2399 CA GLN A 312 11.958 17.093 58.807 1.00 31.25 C ANISOU 2399 CA GLN A 312 3920 4670 3283 666 494 150 C ATOM 2400 C GLN A 312 11.288 16.264 57.717 1.00 36.16 C ANISOU 2400 C GLN A 312 4588 5192 3959 634 552 200 C ATOM 2401 O GLN A 312 10.768 15.174 57.984 1.00 24.17 O ANISOU 2401 O GLN A 312 3106 3654 2422 673 609 260 O ATOM 2402 CB GLN A 312 11.093 18.297 59.179 1.00 29.73 C ANISOU 2402 CB GLN A 312 3723 4475 3100 628 460 85 C ATOM 2403 CG GLN A 312 9.837 17.955 59.957 1.00 31.30 C ANISOU 2403 CG GLN A 312 3958 4666 3267 658 496 109 C ATOM 2404 CD GLN A 312 9.067 19.197 60.376 1.00 43.62 C ANISOU 2404 CD GLN A 312 5510 6230 4832 625 460 42 C ATOM 2405 OE1 GLN A 312 8.973 20.167 59.622 1.00 41.15 O ANISOU 2405 OE1 GLN A 312 5185 5874 4575 557 431 -8 O ATOM 2406 NE2 GLN A 312 8.525 19.178 61.590 1.00 49.53 N ANISOU 2406 NE2 GLN A 312 6266 7032 5522 676 466 42 N ATOM 2407 N PHE A 313 11.292 16.764 56.477 1.00 31.82 N ANISOU 2407 N PHE A 313 4037 4577 3476 562 540 175 N ATOM 2408 CA PHE A 313 10.638 16.041 55.390 1.00 25.49 C ANISOU 2408 CA PHE A 313 3276 3684 2723 528 590 213 C ATOM 2409 C PHE A 313 11.352 14.732 55.079 1.00 25.41 C ANISOU 2409 C PHE A 313 3280 3668 2707 568 635 276 C ATOM 2410 O PHE A 313 10.704 13.717 54.797 1.00 23.27 O ANISOU 2410 O PHE A 313 3050 3343 2450 575 693 324 O ATOM 2411 CB PHE A 313 10.558 16.909 54.135 1.00 21.19 C ANISOU 2411 CB PHE A 313 2725 3081 2245 449 566 172 C ATOM 2412 CG PHE A 313 10.015 16.180 52.940 1.00 28.49 C ANISOU 2412 CG PHE A 313 3687 3921 3217 416 611 205 C ATOM 2413 CD1 PHE A 313 8.654 15.955 52.811 1.00 24.75 C ANISOU 2413 CD1 PHE A 313 3247 3394 2761 395 643 212 C ATOM 2414 CD2 PHE A 313 10.864 15.703 51.955 1.00 27.62 C ANISOU 2414 CD2 PHE A 313 3575 3788 3132 406 622 226 C ATOM 2415 CE1 PHE A 313 8.148 15.277 51.716 1.00 33.55 C ANISOU 2415 CE1 PHE A 313 4393 4436 3919 363 682 235 C ATOM 2416 CE2 PHE A 313 10.364 15.022 50.857 1.00 30.70 C ANISOU 2416 CE2 PHE A 313 3998 4103 3563 376 663 251 C ATOM 2417 CZ PHE A 313 9.004 14.811 50.738 1.00 26.87 C ANISOU 2417 CZ PHE A 313 3546 3568 3095 354 692 253 C ATOM 2418 N ARG A 314 12.686 14.737 55.111 1.00 29.56 N ANISOU 2418 N ARG A 314 3770 4246 3214 593 609 277 N ATOM 2419 CA ARG A 314 13.431 13.508 54.861 1.00 31.30 C ANISOU 2419 CA ARG A 314 4002 4465 3425 637 651 339 C ATOM 2420 C ARG A 314 13.091 12.443 55.898 1.00 33.00 C ANISOU 2420 C ARG A 314 4242 4707 3588 712 701 397 C ATOM 2421 O ARG A 314 12.900 11.270 55.555 1.00 38.44 O ANISOU 2421 O ARG A 314 4968 5348 4291 732 764 455 O ATOM 2422 CB ARG A 314 14.932 13.798 54.849 1.00 24.52 C ANISOU 2422 CB ARG A 314 3094 3671 2552 655 610 325 C ATOM 2423 CG ARG A 314 15.808 12.566 54.708 1.00 29.03 C ANISOU 2423 CG ARG A 314 3671 4252 3106 710 652 390 C ATOM 2424 CD ARG A 314 17.256 12.933 54.403 1.00 37.02 C ANISOU 2424 CD ARG A 314 4632 5313 4119 712 611 373 C ATOM 2425 NE ARG A 314 17.922 13.592 55.523 1.00 40.22 N ANISOU 2425 NE ARG A 314 4986 5823 4471 749 556 338 N ATOM 2426 CZ ARG A 314 18.146 14.896 55.604 1.00 40.08 C ANISOU 2426 CZ ARG A 314 4926 5835 4467 706 494 264 C ATOM 2427 NH1 ARG A 314 17.759 15.726 54.649 1.00 39.89 N ANISOU 2427 NH1 ARG A 314 4905 5744 4507 626 479 223 N ATOM 2428 NH2 ARG A 314 18.781 15.380 56.667 1.00 35.55 N ANISOU 2428 NH2 ARG A 314 4304 5361 3840 746 447 231 N ATOM 2429 N ASN A 315 12.997 12.837 57.170 1.00 36.65 N ANISOU 2429 N ASN A 315 4687 5245 3992 757 676 383 N ATOM 2430 CA ASN A 315 12.639 11.883 58.215 1.00 27.57 C ANISOU 2430 CA ASN A 315 3561 4125 2789 835 725 441 C ATOM 2431 C ASN A 315 11.218 11.363 58.037 1.00 30.70 C ANISOU 2431 C ASN A 315 4009 4440 3218 813 784 468 C ATOM 2432 O ASN A 315 10.966 10.165 58.207 1.00 39.73 O ANISOU 2432 O ASN A 315 5185 5556 4355 856 852 534 O ATOM 2433 CB ASN A 315 12.817 12.526 59.591 1.00 39.60 C ANISOU 2433 CB ASN A 315 5054 5754 4240 886 681 413 C ATOM 2434 CG ASN A 315 14.260 12.895 59.878 1.00 32.37 C ANISOU 2434 CG ASN A 315 4083 4929 3287 916 626 389 C ATOM 2435 OD1 ASN A 315 15.176 12.436 59.195 1.00 38.57 O ANISOU 2435 OD1 ASN A 315 4858 5705 4092 918 634 413 O ATOM 2436 ND2 ASN A 315 14.470 13.729 60.889 1.00 54.56 N ANISOU 2436 ND2 ASN A 315 6856 7829 6044 941 572 340 N ATOM 2437 N CYS A 316 10.274 12.245 57.694 1.00 28.38 N ANISOU 2437 N CYS A 316 3720 4104 2960 746 760 416 N ATOM 2438 CA CYS A 316 8.899 11.804 57.475 1.00 26.26 C ANISOU 2438 CA CYS A 316 3492 3758 2726 720 812 435 C ATOM 2439 C CYS A 316 8.805 10.853 56.287 1.00 39.42 C ANISOU 2439 C CYS A 316 5189 5337 4450 689 864 470 C ATOM 2440 O CYS A 316 8.031 9.889 56.315 1.00 39.09 O ANISOU 2440 O CYS A 316 5184 5244 4425 701 931 514 O ATOM 2441 CB CYS A 316 7.978 13.009 57.273 1.00 28.49 C ANISOU 2441 CB CYS A 316 3770 4018 3037 655 772 371 C ATOM 2442 SG CYS A 316 7.310 13.727 58.807 1.00 48.99 S ANISOU 2442 SG CYS A 316 6357 6685 5572 695 750 346 S ATOM 2443 N MET A 317 9.572 11.119 55.226 1.00 31.22 N ANISOU 2443 N MET A 317 4136 4280 3446 649 837 448 N ATOM 2444 CA MET A 317 9.538 10.246 54.056 1.00 33.86 C ANISOU 2444 CA MET A 317 4497 4535 3832 620 883 475 C ATOM 2445 C MET A 317 10.114 8.871 54.368 1.00 33.24 C ANISOU 2445 C MET A 317 4437 4460 3734 687 944 546 C ATOM 2446 O MET A 317 9.568 7.851 53.932 1.00 34.35 O ANISOU 2446 O MET A 317 4613 4530 3908 683 1009 582 O ATOM 2447 CB MET A 317 10.293 10.887 52.894 1.00 32.82 C ANISOU 2447 CB MET A 317 4344 4390 3737 568 839 438 C ATOM 2448 CG MET A 317 10.321 10.020 51.644 1.00 43.16 C ANISOU 2448 CG MET A 317 5681 5624 5096 540 884 461 C ATOM 2449 SD MET A 317 11.647 10.478 50.517 1.00 63.89 S ANISOU 2449 SD MET A 317 8278 8256 7743 511 844 440 S ATOM 2450 CE MET A 317 12.996 10.643 51.685 1.00 49.32 C ANISOU 2450 CE MET A 317 6390 6516 5834 583 811 453 C ATOM 2451 N VAL A 318 11.220 8.819 55.113 1.00 30.76 N ANISOU 2451 N VAL A 318 4096 4227 3365 751 925 566 N ATOM 2452 CA VAL A 318 11.765 7.530 55.530 1.00 30.65 C ANISOU 2452 CA VAL A 318 4098 4223 3325 826 985 640 C ATOM 2453 C VAL A 318 10.790 6.817 56.460 1.00 44.67 C ANISOU 2453 C VAL A 318 5905 5986 5080 871 1046 685 C ATOM 2454 O VAL A 318 10.641 5.591 56.403 1.00 53.72 O ANISOU 2454 O VAL A 318 7085 7086 6242 903 1122 745 O ATOM 2455 CB VAL A 318 13.147 7.717 56.180 1.00 35.87 C ANISOU 2455 CB VAL A 318 4717 4985 3926 889 945 648 C ATOM 2456 CG1 VAL A 318 13.678 6.389 56.690 1.00 45.07 C ANISOU 2456 CG1 VAL A 318 5899 6166 5059 976 1010 730 C ATOM 2457 CG2 VAL A 318 14.119 8.317 55.180 1.00 47.19 C ANISOU 2457 CG2 VAL A 318 6119 6420 5389 843 896 609 C ATOM 2458 N THR A 319 10.110 7.571 57.328 1.00 30.66 N ANISOU 2458 N THR A 319 4122 4253 3274 874 1017 657 N ATOM 2459 CA THR A 319 9.099 6.981 58.199 1.00 37.70 C ANISOU 2459 CA THR A 319 5043 5131 4150 913 1075 698 C ATOM 2460 C THR A 319 7.995 6.312 57.388 1.00 47.14 C ANISOU 2460 C THR A 319 6278 6214 5417 859 1138 710 C ATOM 2461 O THR A 319 7.652 5.147 57.623 1.00 59.03 O ANISOU 2461 O THR A 319 7815 7679 6934 897 1218 771 O ATOM 2462 CB THR A 319 8.514 8.056 59.120 1.00 48.77 C ANISOU 2462 CB THR A 319 6428 6592 5512 914 1027 654 C ATOM 2463 OG1 THR A 319 9.428 8.321 60.192 1.00 56.11 O ANISOU 2463 OG1 THR A 319 7326 7632 6362 988 991 661 O ATOM 2464 CG2 THR A 319 7.164 7.619 59.693 1.00 44.60 C ANISOU 2464 CG2 THR A 319 5932 6024 4990 924 1086 683 C ATOM 2465 N THR A 320 7.435 7.035 56.417 1.00 50.75 N ANISOU 2465 N THR A 320 6733 6622 5928 772 1103 650 N ATOM 2466 CA THR A 320 6.330 6.492 55.635 1.00 42.89 C ANISOU 2466 CA THR A 320 5769 5527 4999 718 1154 650 C ATOM 2467 C THR A 320 6.787 5.345 54.745 1.00 47.41 C ANISOU 2467 C THR A 320 6364 6037 5613 715 1209 686 C ATOM 2468 O THR A 320 6.118 4.309 54.665 1.00 61.46 O ANISOU 2468 O THR A 320 8175 7751 7428 718 1285 722 O ATOM 2469 CB THR A 320 5.691 7.600 54.800 1.00 42.00 C ANISOU 2469 CB THR A 320 5644 5388 4926 631 1098 578 C ATOM 2470 OG1 THR A 320 5.040 8.536 55.669 1.00 53.14 O ANISOU 2470 OG1 THR A 320 7042 6843 6306 634 1063 549 O ATOM 2471 CG2 THR A 320 4.682 7.020 53.824 1.00 45.69 C ANISOU 2471 CG2 THR A 320 6139 5758 5462 572 1145 572 C ATOM 2472 N LEU A 321 7.930 5.507 54.076 1.00 44.19 N ANISOU 2472 N LEU A 321 5939 5648 5204 710 1174 675 N ATOM 2473 CA LEU A 321 8.413 4.495 53.146 1.00 44.68 C ANISOU 2473 CA LEU A 321 6020 5651 5304 705 1222 702 C ATOM 2474 C LEU A 321 8.923 3.242 53.848 1.00 44.57 C ANISOU 2474 C LEU A 321 6025 5644 5267 789 1293 781 C ATOM 2475 O LEU A 321 9.124 2.220 53.183 1.00 48.33 O ANISOU 2475 O LEU A 321 6526 6058 5781 790 1351 810 O ATOM 2476 CB LEU A 321 9.520 5.084 52.269 1.00 43.29 C ANISOU 2476 CB LEU A 321 5819 5498 5132 680 1164 670 C ATOM 2477 CG LEU A 321 9.519 4.679 50.795 1.00 50.42 C ANISOU 2477 CG LEU A 321 6739 6324 6096 623 1182 653 C ATOM 2478 CD1 LEU A 321 8.203 5.076 50.151 1.00 44.25 C ANISOU 2478 CD1 LEU A 321 5969 5483 5361 547 1177 606 C ATOM 2479 CD2 LEU A 321 10.686 5.319 50.061 1.00 49.08 C ANISOU 2479 CD2 LEU A 321 6540 6186 5921 607 1126 628 C ATOM 2480 N CYS A 322 9.138 3.295 55.158 1.00 52.34 N ANISOU 2480 N CYS A 322 6998 6702 6187 862 1292 815 N ATOM 2481 CA CYS A 322 9.699 2.161 55.885 1.00 54.47 C ANISOU 2481 CA CYS A 322 7283 6989 6426 953 1359 896 C ATOM 2482 C CYS A 322 8.864 1.813 57.112 1.00 60.04 C ANISOU 2482 C CYS A 322 8004 7707 7102 1005 1407 938 C ATOM 2483 O CYS A 322 9.386 1.728 58.225 1.00 66.40 O ANISOU 2483 O CYS A 322 8799 8593 7839 1090 1408 980 O ATOM 2484 CB CYS A 322 11.143 2.456 56.304 1.00 51.27 C ANISOU 2484 CB CYS A 322 6842 6681 5957 1013 1310 908 C ATOM 2485 SG CYS A 322 12.150 3.238 55.016 1.00 72.56 S ANISOU 2485 SG CYS A 322 9508 9383 8680 949 1235 847 S TER 2486 CYS A 322 ATOM 2487 N MET B 1 -14.520 22.505 70.567 1.00 25.03 N ANISOU 2487 N MET B 1 3455 3661 2396 785 1005 106 N ATOM 2488 CA MET B 1 -14.711 23.343 69.388 1.00 31.48 C ANISOU 2488 CA MET B 1 4256 4421 3283 703 961 55 C ATOM 2489 C MET B 1 -13.949 24.653 69.523 1.00 39.09 C ANISOU 2489 C MET B 1 5207 5425 4219 698 884 -24 C ATOM 2490 O MET B 1 -13.953 25.280 70.584 1.00 32.28 O ANISOU 2490 O MET B 1 4345 4623 3297 745 870 -56 O ATOM 2491 CB MET B 1 -16.198 23.619 69.158 1.00 35.02 C ANISOU 2491 CB MET B 1 4702 4821 3783 672 992 57 C ATOM 2492 N ASN B 2 -13.293 25.062 68.440 1.00 34.11 N ANISOU 2492 N ASN B 2 4564 4762 3635 639 837 -58 N ATOM 2493 CA ASN B 2 -12.468 26.262 68.443 1.00 40.28 C ANISOU 2493 CA ASN B 2 5330 5572 4403 626 768 -133 C ATOM 2494 C ASN B 2 -13.226 27.511 68.016 1.00 40.05 C ANISOU 2494 C ASN B 2 5292 5505 4420 580 744 -187 C ATOM 2495 O ASN B 2 -12.654 28.606 68.049 1.00 40.75 O ANISOU 2495 O ASN B 2 5368 5610 4505 567 691 -253 O ATOM 2496 CB ASN B 2 -11.246 26.060 67.546 1.00 28.83 C ANISOU 2496 CB ASN B 2 3870 4109 2976 592 732 -139 C ATOM 2497 CG ASN B 2 -10.252 25.091 68.140 1.00 33.30 C ANISOU 2497 CG ASN B 2 4440 4729 3482 647 742 -102 C ATOM 2498 OD1 ASN B 2 -9.439 25.463 68.984 1.00 43.17 O ANISOU 2498 OD1 ASN B 2 5682 6051 4669 690 708 -135 O ATOM 2499 ND2 ASN B 2 -10.309 23.838 67.705 1.00 36.56 N ANISOU 2499 ND2 ASN B 2 4866 5110 3916 647 789 -34 N ATOM 2500 N GLY B 3 -14.488 27.377 67.625 1.00 25.92 N ANISOU 2500 N GLY B 3 3507 3665 2677 556 782 -160 N ATOM 2501 CA GLY B 3 -15.309 28.529 67.324 1.00 21.62 C ANISOU 2501 CA GLY B 3 2954 3089 2170 524 766 -204 C ATOM 2502 C GLY B 3 -16.471 28.624 68.287 1.00 31.67 C ANISOU 2502 C GLY B 3 4235 4380 3417 563 806 -193 C ATOM 2503 O GLY B 3 -16.467 27.974 69.337 1.00 37.81 O ANISOU 2503 O GLY B 3 5024 5206 4135 623 837 -162 O ATOM 2504 N THR B 4 -17.472 29.428 67.945 1.00 30.05 N ANISOU 2504 N THR B 4 4023 4138 3254 535 806 -215 N ATOM 2505 CA THR B 4 -18.671 29.585 68.758 1.00 22.17 C ANISOU 2505 CA THR B 4 3031 3152 2241 568 846 -206 C ATOM 2506 C THR B 4 -19.875 29.216 67.906 1.00 31.74 C ANISOU 2506 C THR B 4 4235 4303 3520 527 883 -168 C ATOM 2507 O THR B 4 -20.063 29.776 66.820 1.00 34.66 O ANISOU 2507 O THR B 4 4593 4627 3949 474 858 -189 O ATOM 2508 CB THR B 4 -18.796 31.017 69.281 1.00 24.92 C ANISOU 2508 CB THR B 4 3376 3520 2572 578 812 -275 C ATOM 2509 OG1 THR B 4 -17.615 31.365 70.013 1.00 23.75 O ANISOU 2509 OG1 THR B 4 3230 3430 2364 610 772 -319 O ATOM 2510 CG2 THR B 4 -20.009 31.154 70.188 1.00 22.79 C ANISOU 2510 CG2 THR B 4 3113 3266 2280 618 855 -263 C ATOM 2511 N GLU B 5 -20.687 28.281 68.391 1.00 26.37 N ANISOU 2511 N GLU B 5 3561 3625 2833 554 944 -113 N ATOM 2512 CA GLU B 5 -21.908 27.894 67.700 1.00 27.62 C ANISOU 2512 CA GLU B 5 3707 3731 3054 518 983 -80 C ATOM 2513 C GLU B 5 -23.102 28.574 68.352 1.00 22.17 C ANISOU 2513 C GLU B 5 3014 3050 2361 541 1006 -91 C ATOM 2514 O GLU B 5 -23.297 28.471 69.568 1.00 36.63 O ANISOU 2514 O GLU B 5 4857 4925 4136 599 1034 -79 O ATOM 2515 CB GLU B 5 -22.111 26.378 67.703 1.00 21.98 C ANISOU 2515 CB GLU B 5 2998 3003 2350 526 1042 -12 C ATOM 2516 CG GLU B 5 -23.436 25.965 67.068 1.00 36.04 C ANISOU 2516 CG GLU B 5 4762 4734 4198 488 1084 16 C ATOM 2517 CD GLU B 5 -23.478 24.504 66.657 1.00 51.95 C ANISOU 2517 CD GLU B 5 6776 6717 6245 472 1133 71 C ATOM 2518 OE1 GLU B 5 -22.556 23.748 67.034 1.00 47.28 O ANISOU 2518 OE1 GLU B 5 6202 6145 5617 502 1144 98 O ATOM 2519 OE2 GLU B 5 -24.435 24.117 65.950 1.00 41.94 O ANISOU 2519 OE2 GLU B 5 5490 5405 5040 431 1161 86 O ATOM 2520 N GLY B 6 -23.887 29.274 67.541 1.00 29.77 N ANISOU 2520 N GLY B 6 3959 3972 3380 498 993 -112 N ATOM 2521 CA GLY B 6 -25.131 29.847 67.987 1.00 22.45 C ANISOU 2521 CA GLY B 6 3024 3045 2460 513 1019 -116 C ATOM 2522 C GLY B 6 -26.302 29.118 67.365 1.00 26.69 C ANISOU 2522 C GLY B 6 3542 3543 3058 482 1064 -73 C ATOM 2523 O GLY B 6 -26.135 28.095 66.693 1.00 26.50 O ANISOU 2523 O GLY B 6 3512 3492 3063 453 1080 -40 O ATOM 2524 N PRO B 7 -27.517 29.620 67.595 1.00 27.02 N ANISOU 2524 N PRO B 7 3571 3580 3117 489 1088 -75 N ATOM 2525 CA PRO B 7 -28.696 28.961 67.006 1.00 25.24 C ANISOU 2525 CA PRO B 7 3320 3320 2952 458 1131 -39 C ATOM 2526 C PRO B 7 -28.667 28.924 65.489 1.00 32.19 C ANISOU 2526 C PRO B 7 4179 4157 3894 393 1100 -48 C ATOM 2527 O PRO B 7 -29.081 27.924 64.888 1.00 28.10 O ANISOU 2527 O PRO B 7 3646 3613 3419 361 1129 -16 O ATOM 2528 CB PRO B 7 -29.866 29.807 67.530 1.00 33.30 C ANISOU 2528 CB PRO B 7 4329 4348 3974 480 1149 -51 C ATOM 2529 CG PRO B 7 -29.325 30.511 68.741 1.00 34.63 C ANISOU 2529 CG PRO B 7 4524 4563 4071 538 1137 -78 C ATOM 2530 CD PRO B 7 -27.884 30.770 68.438 1.00 41.85 C ANISOU 2530 CD PRO B 7 5454 5484 4961 527 1080 -111 C ATOM 2531 N ASN B 8 -28.172 29.987 64.851 1.00 28.76 N ANISOU 2531 N ASN B 8 3744 3716 3466 372 1042 -92 N ATOM 2532 CA ASN B 8 -28.185 30.091 63.397 1.00 30.02 C ANISOU 2532 CA ASN B 8 3884 3840 3680 316 1011 -102 C ATOM 2533 C ASN B 8 -26.875 30.656 62.863 1.00 30.42 C ANISOU 2533 C ASN B 8 3949 3889 3720 301 953 -135 C ATOM 2534 O ASN B 8 -26.857 31.297 61.806 1.00 20.63 O ANISOU 2534 O ASN B 8 2697 2627 2517 266 919 -155 O ATOM 2535 CB ASN B 8 -29.356 30.956 62.922 1.00 34.61 C ANISOU 2535 CB ASN B 8 4440 4410 4302 302 1007 -116 C ATOM 2536 CG ASN B 8 -29.508 32.226 63.737 1.00 33.91 C ANISOU 2536 CG ASN B 8 4362 4340 4183 341 996 -148 C ATOM 2537 OD1 ASN B 8 -28.735 32.479 64.661 1.00 31.70 O ANISOU 2537 OD1 ASN B 8 4107 4085 3852 376 988 -166 O ATOM 2538 ND2 ASN B 8 -30.504 33.036 63.394 1.00 36.56 N ANISOU 2538 ND2 ASN B 8 4677 4665 4551 335 995 -159 N ATOM 2539 N PHE B 9 -25.773 30.435 63.574 1.00 21.16 N ANISOU 2539 N PHE B 9 2801 2741 2499 328 944 -139 N ATOM 2540 CA PHE B 9 -24.489 30.946 63.120 1.00 27.19 C ANISOU 2540 CA PHE B 9 3574 3503 3253 313 892 -171 C ATOM 2541 C PHE B 9 -23.372 30.085 63.688 1.00 26.56 C ANISOU 2541 C PHE B 9 3514 3450 3129 335 895 -155 C ATOM 2542 O PHE B 9 -23.570 29.316 64.632 1.00 23.93 O ANISOU 2542 O PHE B 9 3190 3140 2761 373 936 -124 O ATOM 2543 CB PHE B 9 -24.296 32.420 63.511 1.00 29.52 C ANISOU 2543 CB PHE B 9 3874 3809 3533 329 858 -222 C ATOM 2544 CG PHE B 9 -24.403 32.693 64.994 1.00 23.76 C ANISOU 2544 CG PHE B 9 3160 3122 2747 385 875 -235 C ATOM 2545 CD1 PHE B 9 -23.280 32.643 65.808 1.00 23.04 C ANISOU 2545 CD1 PHE B 9 3085 3068 2599 415 858 -254 C ATOM 2546 CD2 PHE B 9 -25.621 33.029 65.567 1.00 25.36 C ANISOU 2546 CD2 PHE B 9 3356 3329 2950 408 908 -231 C ATOM 2547 CE1 PHE B 9 -23.373 32.907 67.163 1.00 25.28 C ANISOU 2547 CE1 PHE B 9 3382 3397 2826 470 871 -269 C ATOM 2548 CE2 PHE B 9 -25.719 33.297 66.924 1.00 30.26 C ANISOU 2548 CE2 PHE B 9 3991 3990 3515 462 924 -244 C ATOM 2549 CZ PHE B 9 -24.593 33.237 67.721 1.00 29.23 C ANISOU 2549 CZ PHE B 9 3879 3900 3326 494 905 -264 C ATOM 2550 N TYR B 10 -22.194 30.219 63.080 1.00 25.95 N ANISOU 2550 N TYR B 10 3441 3367 3053 314 854 -174 N ATOM 2551 CA TYR B 10 -20.968 29.605 63.591 1.00 29.41 C ANISOU 2551 CA TYR B 10 3895 3834 3445 337 846 -167 C ATOM 2552 C TYR B 10 -19.839 30.609 63.391 1.00 20.22 C ANISOU 2552 C TYR B 10 2733 2678 2272 328 790 -217 C ATOM 2553 O TYR B 10 -19.328 30.766 62.279 1.00 33.29 O ANISOU 2553 O TYR B 10 4380 4303 3965 286 761 -226 O ATOM 2554 CB TYR B 10 -20.650 28.285 62.904 1.00 21.19 C ANISOU 2554 CB TYR B 10 2855 2772 2424 315 866 -123 C ATOM 2555 CG TYR B 10 -19.446 27.608 63.509 1.00 20.28 C ANISOU 2555 CG TYR B 10 2755 2690 2260 346 865 -110 C ATOM 2556 CD1 TYR B 10 -19.566 26.847 64.662 1.00 25.58 C ANISOU 2556 CD1 TYR B 10 3440 3395 2884 398 908 -76 C ATOM 2557 CD2 TYR B 10 -18.186 27.748 62.944 1.00 21.01 C ANISOU 2557 CD2 TYR B 10 2849 2783 2351 328 822 -129 C ATOM 2558 CE1 TYR B 10 -18.471 26.234 65.230 1.00 27.38 C ANISOU 2558 CE1 TYR B 10 3681 3659 3063 434 907 -60 C ATOM 2559 CE2 TYR B 10 -17.086 27.136 63.502 1.00 20.98 C ANISOU 2559 CE2 TYR B 10 2857 2814 2301 360 820 -117 C ATOM 2560 CZ TYR B 10 -17.232 26.382 64.646 1.00 23.65 C ANISOU 2560 CZ TYR B 10 3207 3188 2590 414 861 -82 C ATOM 2561 OH TYR B 10 -16.128 25.777 65.201 1.00 35.78 O ANISOU 2561 OH TYR B 10 4754 4764 4077 451 859 -67 O ATOM 2562 N VAL B 11 -19.449 31.277 64.469 1.00 20.58 N ANISOU 2562 N VAL B 11 2786 2764 2269 367 774 -253 N ATOM 2563 CA VAL B 11 -18.412 32.302 64.422 1.00 20.58 C ANISOU 2563 CA VAL B 11 2784 2772 2262 359 723 -309 C ATOM 2564 C VAL B 11 -17.058 31.611 64.558 1.00 26.33 C ANISOU 2564 C VAL B 11 3518 3530 2957 369 705 -302 C ATOM 2565 O VAL B 11 -16.819 30.943 65.577 1.00 24.40 O ANISOU 2565 O VAL B 11 3283 3332 2655 416 724 -284 O ATOM 2566 CB VAL B 11 -18.612 33.348 65.524 1.00 29.00 C ANISOU 2566 CB VAL B 11 3854 3870 3293 395 714 -358 C ATOM 2567 CG1 VAL B 11 -17.418 34.281 65.593 1.00 26.20 C ANISOU 2567 CG1 VAL B 11 3495 3529 2930 388 663 -420 C ATOM 2568 CG2 VAL B 11 -19.890 34.135 65.268 1.00 31.74 C ANISOU 2568 CG2 VAL B 11 4195 4185 3681 383 729 -366 C ATOM 2569 N PRO B 12 -16.156 31.738 63.575 1.00 27.89 N ANISOU 2569 N PRO B 12 3707 3703 3186 330 672 -314 N ATOM 2570 CA PRO B 12 -14.828 31.123 63.711 1.00 28.50 C ANISOU 2570 CA PRO B 12 3787 3811 3231 341 655 -309 C ATOM 2571 C PRO B 12 -13.949 31.861 64.710 1.00 20.72 C ANISOU 2571 C PRO B 12 2798 2878 2196 373 620 -364 C ATOM 2572 O PRO B 12 -12.836 32.277 64.378 1.00 22.61 O ANISOU 2572 O PRO B 12 3028 3121 2443 354 580 -398 O ATOM 2573 CB PRO B 12 -14.259 31.205 62.288 1.00 19.82 C ANISOU 2573 CB PRO B 12 2678 2666 2186 287 631 -309 C ATOM 2574 CG PRO B 12 -14.957 32.375 61.680 1.00 26.45 C ANISOU 2574 CG PRO B 12 3509 3465 3075 256 619 -339 C ATOM 2575 CD PRO B 12 -16.342 32.373 62.258 1.00 26.37 C ANISOU 2575 CD PRO B 12 3504 3457 3059 277 654 -324 C ATOM 2576 N PHE B 13 -14.441 32.021 65.938 1.00 25.29 N ANISOU 2576 N PHE B 13 3384 3499 2725 421 635 -376 N ATOM 2577 CA PHE B 13 -13.734 32.751 66.980 1.00 26.69 C ANISOU 2577 CA PHE B 13 3558 3733 2851 455 603 -435 C ATOM 2578 C PHE B 13 -14.131 32.168 68.328 1.00 35.04 C ANISOU 2578 C PHE B 13 4628 4851 3834 522 634 -413 C ATOM 2579 O PHE B 13 -15.308 31.880 68.561 1.00 25.25 O ANISOU 2579 O PHE B 13 3399 3599 2597 537 678 -378 O ATOM 2580 CB PHE B 13 -14.058 34.250 66.921 1.00 32.13 C ANISOU 2580 CB PHE B 13 4239 4397 3571 432 578 -502 C ATOM 2581 CG PHE B 13 -13.045 35.119 67.607 1.00 30.58 C ANISOU 2581 CG PHE B 13 4031 4244 3344 445 534 -577 C ATOM 2582 CD1 PHE B 13 -11.937 35.585 66.920 1.00 35.86 C ANISOU 2582 CD1 PHE B 13 4683 4895 4046 406 494 -613 C ATOM 2583 CD2 PHE B 13 -13.203 35.476 68.935 1.00 35.88 C ANISOU 2583 CD2 PHE B 13 4707 4974 3953 496 533 -616 C ATOM 2584 CE1 PHE B 13 -11.001 36.385 67.547 1.00 40.85 C ANISOU 2584 CE1 PHE B 13 5300 5566 4655 414 453 -688 C ATOM 2585 CE2 PHE B 13 -12.270 36.277 69.568 1.00 44.64 C ANISOU 2585 CE2 PHE B 13 5803 6126 5034 507 489 -693 C ATOM 2586 CZ PHE B 13 -11.168 36.732 68.873 1.00 31.45 C ANISOU 2586 CZ PHE B 13 4113 4436 3402 463 449 -731 C ATOM 2587 N SER B 14 -13.147 31.988 69.206 1.00 23.30 N ANISOU 2587 N SER B 14 3140 3433 2280 566 613 -433 N ATOM 2588 CA SER B 14 -13.397 31.391 70.512 1.00 23.14 C ANISOU 2588 CA SER B 14 3132 3480 2181 639 643 -409 C ATOM 2589 C SER B 14 -14.047 32.403 71.443 1.00 25.19 C ANISOU 2589 C SER B 14 3394 3767 2412 667 639 -462 C ATOM 2590 O SER B 14 -13.598 33.549 71.542 1.00 31.18 O ANISOU 2590 O SER B 14 4139 4532 3174 651 594 -540 O ATOM 2591 CB SER B 14 -12.095 30.880 71.126 1.00 35.92 C ANISOU 2591 CB SER B 14 4745 5171 3733 681 619 -412 C ATOM 2592 OG SER B 14 -12.263 30.521 72.488 1.00 30.46 O ANISOU 2592 OG SER B 14 4064 4555 2956 759 640 -400 O ATOM 2593 N ASN B 15 -15.106 31.975 72.131 1.00 23.82 N ANISOU 2593 N ASN B 15 3236 3606 2210 709 689 -421 N ATOM 2594 CA ASN B 15 -15.754 32.804 73.138 1.00 24.32 C ANISOU 2594 CA ASN B 15 3303 3702 2234 746 693 -465 C ATOM 2595 C ASN B 15 -15.209 32.548 74.540 1.00 27.98 C ANISOU 2595 C ASN B 15 3772 4265 2595 826 689 -477 C ATOM 2596 O ASN B 15 -15.924 32.763 75.529 1.00 27.29 O ANISOU 2596 O ASN B 15 3695 4214 2459 876 714 -483 O ATOM 2597 CB ASN B 15 -17.269 32.594 73.103 1.00 26.03 C ANISOU 2597 CB ASN B 15 3531 3879 2480 748 750 -417 C ATOM 2598 CG ASN B 15 -18.030 33.785 73.655 1.00 24.51 C ANISOU 2598 CG ASN B 15 3340 3689 2284 759 746 -474 C ATOM 2599 OD1 ASN B 15 -17.567 34.917 73.565 1.00 27.42 O ANISOU 2599 OD1 ASN B 15 3698 4054 2665 736 700 -550 O ATOM 2600 ND2 ASN B 15 -19.199 33.536 74.226 1.00 24.73 N ANISOU 2600 ND2 ASN B 15 3378 3722 2296 794 798 -436 N ATOM 2601 N LYS B 16 -13.959 32.091 74.655 1.00 25.56 N ANISOU 2601 N LYS B 16 3458 4005 2250 842 659 -480 N ATOM 2602 CA LYS B 16 -13.379 31.856 75.972 1.00 33.69 C ANISOU 2602 CA LYS B 16 4488 5137 3175 922 651 -494 C ATOM 2603 C LYS B 16 -13.134 33.154 76.728 1.00 31.99 C ANISOU 2603 C LYS B 16 4262 4969 2923 936 604 -597 C ATOM 2604 O LYS B 16 -12.922 33.115 77.945 1.00 46.56 O ANISOU 2604 O LYS B 16 6109 6904 4676 1008 601 -616 O ATOM 2605 CB LYS B 16 -12.074 31.065 75.852 1.00 29.45 C ANISOU 2605 CB LYS B 16 3942 4641 2608 935 629 -472 C ATOM 2606 CG LYS B 16 -10.931 31.827 75.207 1.00 44.12 C ANISOU 2606 CG LYS B 16 5774 6490 4501 881 561 -545 C ATOM 2607 CD LYS B 16 -9.717 30.928 75.005 1.00 39.28 C ANISOU 2607 CD LYS B 16 5151 5911 3864 894 546 -512 C ATOM 2608 CE LYS B 16 -8.706 31.562 74.052 1.00 53.93 C ANISOU 2608 CE LYS B 16 6980 7734 5778 826 489 -568 C ATOM 2609 NZ LYS B 16 -7.500 30.704 73.832 1.00 44.26 N ANISOU 2609 NZ LYS B 16 5743 6543 4531 839 474 -536 N ATOM 2610 N THR B 17 -13.153 34.294 76.038 1.00 30.11 N ANISOU 2610 N THR B 17 4011 4673 2755 870 570 -663 N ATOM 2611 CA THR B 17 -13.067 35.599 76.677 1.00 30.51 C ANISOU 2611 CA THR B 17 4052 4752 2786 876 533 -765 C ATOM 2612 C THR B 17 -14.399 36.336 76.695 1.00 35.38 C ANISOU 2612 C THR B 17 4682 5318 3440 865 563 -776 C ATOM 2613 O THR B 17 -14.466 37.452 77.219 1.00 31.20 O ANISOU 2613 O THR B 17 4149 4804 2902 869 539 -859 O ATOM 2614 CB THR B 17 -12.008 36.468 75.989 1.00 41.81 C ANISOU 2614 CB THR B 17 5457 6158 4269 814 472 -842 C ATOM 2615 OG1 THR B 17 -12.428 36.773 74.653 1.00 36.02 O ANISOU 2615 OG1 THR B 17 4725 5321 3641 739 481 -823 O ATOM 2616 CG2 THR B 17 -10.674 35.742 75.943 1.00 41.06 C ANISOU 2616 CG2 THR B 17 5346 6114 4140 825 442 -831 C ATOM 2617 N GLY B 18 -15.456 35.747 76.136 1.00 28.21 N ANISOU 2617 N GLY B 18 3790 4352 2577 850 615 -696 N ATOM 2618 CA GLY B 18 -16.791 36.296 76.257 1.00 30.26 C ANISOU 2618 CA GLY B 18 4061 4574 2863 851 651 -695 C ATOM 2619 C GLY B 18 -17.152 37.401 75.290 1.00 26.18 C ANISOU 2619 C GLY B 18 3536 3974 2439 782 634 -738 C ATOM 2620 O GLY B 18 -18.230 37.989 75.431 1.00 25.78 O ANISOU 2620 O GLY B 18 3493 3896 2408 785 660 -745 O ATOM 2621 N VAL B 19 -16.304 37.701 74.303 1.00 25.32 N ANISOU 2621 N VAL B 19 3410 3823 2386 722 595 -762 N ATOM 2622 CA VAL B 19 -16.564 38.852 73.440 1.00 28.51 C ANISOU 2622 CA VAL B 19 3806 4151 2874 662 580 -806 C ATOM 2623 C VAL B 19 -17.465 38.528 72.255 1.00 35.45 C ANISOU 2623 C VAL B 19 4688 4951 3829 619 613 -737 C ATOM 2624 O VAL B 19 -18.045 39.449 71.666 1.00 29.60 O ANISOU 2624 O VAL B 19 3945 4151 3151 584 615 -760 O ATOM 2625 CB VAL B 19 -15.255 39.466 72.913 1.00 24.98 C ANISOU 2625 CB VAL B 19 3340 3693 2459 618 526 -869 C ATOM 2626 CG1 VAL B 19 -14.355 39.876 74.068 1.00 25.72 C ANISOU 2626 CG1 VAL B 19 3424 3866 2481 657 488 -949 C ATOM 2627 CG2 VAL B 19 -14.545 38.494 71.990 1.00 24.45 C ANISOU 2627 CG2 VAL B 19 3266 3609 2415 588 519 -811 C ATOM 2628 N VAL B 20 -17.610 37.250 71.891 1.00 29.35 N ANISOU 2628 N VAL B 20 3921 4178 3053 621 641 -656 N ATOM 2629 CA VAL B 20 -18.325 36.896 70.668 1.00 23.39 C ANISOU 2629 CA VAL B 20 3164 3352 2371 575 665 -598 C ATOM 2630 C VAL B 20 -19.788 37.298 70.784 1.00 37.65 C ANISOU 2630 C VAL B 20 4975 5130 4200 583 703 -584 C ATOM 2631 O VAL B 20 -20.442 37.051 71.804 1.00 23.85 O ANISOU 2631 O VAL B 20 3237 3422 2401 635 735 -571 O ATOM 2632 CB VAL B 20 -18.181 35.396 70.377 1.00 28.00 C ANISOU 2632 CB VAL B 20 3751 3943 2943 579 690 -519 C ATOM 2633 CG1 VAL B 20 -19.089 34.987 69.229 1.00 26.90 C ANISOU 2633 CG1 VAL B 20 3609 3738 2874 536 719 -463 C ATOM 2634 CG2 VAL B 20 -16.741 35.059 70.051 1.00 23.50 C ANISOU 2634 CG2 VAL B 20 3174 3391 2363 564 651 -530 C ATOM 2635 N ARG B 21 -20.303 37.936 69.733 1.00 23.06 N ANISOU 2635 N ARG B 21 3119 3216 2427 535 701 -586 N ATOM 2636 CA ARG B 21 -21.708 38.297 69.636 1.00 26.55 C ANISOU 2636 CA ARG B 21 3561 3627 2900 537 736 -568 C ATOM 2637 C ARG B 21 -22.249 37.853 68.284 1.00 24.67 C ANISOU 2637 C ARG B 21 3312 3332 2731 489 750 -514 C ATOM 2638 O ARG B 21 -21.495 37.702 67.316 1.00 22.20 O ANISOU 2638 O ARG B 21 2992 2993 2452 448 724 -509 O ATOM 2639 CB ARG B 21 -21.928 39.808 69.831 1.00 24.26 C ANISOU 2639 CB ARG B 21 3269 3316 2631 535 721 -637 C ATOM 2640 CG ARG B 21 -21.580 40.297 71.231 1.00 35.57 C ANISOU 2640 CG ARG B 21 4712 4808 3995 586 711 -698 C ATOM 2641 CD ARG B 21 -22.351 41.554 71.612 1.00 53.59 C ANISOU 2641 CD ARG B 21 6998 7070 6294 598 721 -748 C ATOM 2642 NE ARG B 21 -21.780 42.765 71.032 1.00 67.30 N ANISOU 2642 NE ARG B 21 8727 8761 8085 558 687 -812 N ATOM 2643 CZ ARG B 21 -22.294 43.979 71.179 1.00 53.24 C ANISOU 2643 CZ ARG B 21 6948 6949 6333 560 692 -860 C ATOM 2644 NH1 ARG B 21 -23.406 44.181 71.867 1.00 41.45 N ANISOU 2644 NH1 ARG B 21 5464 5468 4819 599 728 -854 N ATOM 2645 NH2 ARG B 21 -21.686 45.014 70.607 1.00 51.02 N ANISOU 2645 NH2 ARG B 21 6659 6620 6106 522 666 -914 N ATOM 2646 N SER B 22 -23.559 37.640 68.234 1.00 22.45 N ANISOU 2646 N SER B 22 3027 3036 2468 496 790 -474 N ATOM 2647 CA SER B 22 -24.186 37.093 67.042 1.00 30.31 C ANISOU 2647 CA SER B 22 4009 3988 3521 456 806 -423 C ATOM 2648 C SER B 22 -23.977 38.022 65.849 1.00 28.03 C ANISOU 2648 C SER B 22 3709 3648 3294 410 774 -448 C ATOM 2649 O SER B 22 -24.093 39.247 65.987 1.00 23.93 O ANISOU 2649 O SER B 22 3190 3113 2788 414 761 -494 O ATOM 2650 CB SER B 22 -25.682 36.878 67.278 1.00 28.77 C ANISOU 2650 CB SER B 22 3806 3789 3336 474 853 -386 C ATOM 2651 OG SER B 22 -26.375 36.746 66.050 1.00 25.19 O ANISOU 2651 OG SER B 22 3333 3291 2946 432 859 -355 O ATOM 2652 N PRO B 23 -23.673 37.478 64.664 1.00 28.98 N ANISOU 2652 N PRO B 23 3819 3740 3452 368 762 -417 N ATOM 2653 CA PRO B 23 -23.543 38.326 63.470 1.00 20.90 C ANISOU 2653 CA PRO B 23 2785 2670 2487 328 737 -433 C ATOM 2654 C PRO B 23 -24.866 38.868 62.955 1.00 20.89 C ANISOU 2654 C PRO B 23 2769 2639 2527 323 758 -418 C ATOM 2655 O PRO B 23 -24.878 39.531 61.912 1.00 34.67 O ANISOU 2655 O PRO B 23 4505 4347 4321 296 742 -422 O ATOM 2656 CB PRO B 23 -22.898 37.380 62.447 1.00 20.46 C ANISOU 2656 CB PRO B 23 2724 2601 2448 292 725 -398 C ATOM 2657 CG PRO B 23 -23.342 36.026 62.866 1.00 27.32 C ANISOU 2657 CG PRO B 23 3594 3495 3290 307 758 -352 C ATOM 2658 CD PRO B 23 -23.417 36.058 64.367 1.00 31.80 C ANISOU 2658 CD PRO B 23 4175 4106 3800 357 775 -368 C ATOM 2659 N PHE B 24 -25.977 38.591 63.635 1.00 22.55 N ANISOU 2659 N PHE B 24 2978 2868 2723 352 794 -398 N ATOM 2660 CA PHE B 24 -27.261 39.201 63.329 1.00 21.21 C ANISOU 2660 CA PHE B 24 2792 2678 2588 355 815 -388 C ATOM 2661 C PHE B 24 -27.661 40.241 64.366 1.00 34.88 C ANISOU 2661 C PHE B 24 4535 4419 4300 394 825 -428 C ATOM 2662 O PHE B 24 -28.787 40.749 64.321 1.00 26.77 O ANISOU 2662 O PHE B 24 3496 3380 3296 406 848 -420 O ATOM 2663 CB PHE B 24 -28.348 38.128 63.216 1.00 26.08 C ANISOU 2663 CB PHE B 24 3393 3304 3211 355 852 -335 C ATOM 2664 CG PHE B 24 -28.068 37.086 62.170 1.00 29.54 C ANISOU 2664 CG PHE B 24 3820 3732 3672 316 844 -300 C ATOM 2665 CD1 PHE B 24 -27.989 37.432 60.832 1.00 29.94 C ANISOU 2665 CD1 PHE B 24 3855 3751 3767 280 820 -298 C ATOM 2666 CD2 PHE B 24 -27.896 35.758 62.523 1.00 31.26 C ANISOU 2666 CD2 PHE B 24 4041 3969 3866 317 865 -268 C ATOM 2667 CE1 PHE B 24 -27.736 36.473 59.865 1.00 20.10 C ANISOU 2667 CE1 PHE B 24 2599 2498 2540 245 813 -270 C ATOM 2668 CE2 PHE B 24 -27.641 34.795 61.562 1.00 28.85 C ANISOU 2668 CE2 PHE B 24 3726 3650 3584 280 861 -240 C ATOM 2669 CZ PHE B 24 -27.564 35.153 60.231 1.00 24.09 C ANISOU 2669 CZ PHE B 24 3108 3020 3024 244 833 -243 C ATOM 2670 N GLU B 25 -26.770 40.565 65.302 1.00 29.40 N ANISOU 2670 N GLU B 25 3860 3748 3564 416 810 -472 N ATOM 2671 CA GLU B 25 -27.099 41.472 66.395 1.00 32.47 C ANISOU 2671 CA GLU B 25 4260 4151 3926 456 821 -516 C ATOM 2672 C GLU B 25 -26.149 42.650 66.521 1.00 29.00 C ANISOU 2672 C GLU B 25 3830 3696 3493 450 787 -585 C ATOM 2673 O GLU B 25 -26.599 43.763 66.803 1.00 34.90 O ANISOU 2673 O GLU B 25 4580 4424 4256 465 794 -621 O ATOM 2674 CB GLU B 25 -27.118 40.705 67.721 1.00 38.05 C ANISOU 2674 CB GLU B 25 4980 4914 4563 500 842 -510 C ATOM 2675 CG GLU B 25 -28.186 39.635 67.823 1.00 46.81 C ANISOU 2675 CG GLU B 25 6079 6037 5668 512 887 -446 C ATOM 2676 CD GLU B 25 -28.101 38.876 69.134 1.00 35.33 C ANISOU 2676 CD GLU B 25 4641 4638 4144 560 912 -435 C ATOM 2677 OE1 GLU B 25 -27.320 39.300 70.015 1.00 48.54 O ANISOU 2677 OE1 GLU B 25 6332 6345 5768 589 892 -483 O ATOM 2678 OE2 GLU B 25 -28.804 37.852 69.278 1.00 48.63 O ANISOU 2678 OE2 GLU B 25 6319 6334 5824 570 952 -380 O ATOM 2679 N ALA B 26 -24.850 42.441 66.328 1.00 30.41 N ANISOU 2679 N ALA B 26 4012 3879 3662 429 753 -605 N ATOM 2680 CA ALA B 26 -23.874 43.458 66.681 1.00 22.94 C ANISOU 2680 CA ALA B 26 3074 2928 2716 426 723 -677 C ATOM 2681 C ALA B 26 -22.711 43.408 65.706 1.00 24.46 C ANISOU 2681 C ALA B 26 3259 3094 2940 381 688 -681 C ATOM 2682 O ALA B 26 -22.437 42.351 65.126 1.00 29.83 O ANISOU 2682 O ALA B 26 3934 3781 3617 363 685 -633 O ATOM 2683 CB ALA B 26 -23.368 43.257 68.115 1.00 32.45 C ANISOU 2683 CB ALA B 26 4292 4194 3846 467 717 -718 C ATOM 2684 N PRO B 27 -22.011 44.526 65.507 1.00 24.76 N ANISOU 2684 N PRO B 27 3296 3100 3012 362 666 -738 N ATOM 2685 CA PRO B 27 -20.836 44.510 64.630 1.00 22.98 C ANISOU 2685 CA PRO B 27 3063 2851 2818 321 636 -743 C ATOM 2686 C PRO B 27 -19.789 43.525 65.128 1.00 24.54 C ANISOU 2686 C PRO B 27 3262 3101 2961 326 613 -746 C ATOM 2687 O PRO B 27 -19.606 43.337 66.333 1.00 29.32 O ANISOU 2687 O PRO B 27 3874 3760 3506 361 610 -776 O ATOM 2688 CB PRO B 27 -20.328 45.954 64.691 1.00 33.43 C ANISOU 2688 CB PRO B 27 4385 4136 4181 309 623 -815 C ATOM 2689 CG PRO B 27 -21.514 46.762 65.100 1.00 22.99 C ANISOU 2689 CG PRO B 27 3069 2795 2870 336 653 -826 C ATOM 2690 CD PRO B 27 -22.311 45.878 66.010 1.00 33.33 C ANISOU 2690 CD PRO B 27 4386 4161 4116 377 673 -798 C ATOM 2691 N GLN B 28 -19.090 42.905 64.182 1.00 21.83 N ANISOU 2691 N GLN B 28 2911 2745 2637 293 597 -712 N ATOM 2692 CA GLN B 28 -18.125 41.846 64.471 1.00 25.98 C ANISOU 2692 CA GLN B 28 3437 3317 3116 296 579 -702 C ATOM 2693 C GLN B 28 -16.710 42.388 64.600 1.00 26.40 C ANISOU 2693 C GLN B 28 3483 3376 3173 280 541 -762 C ATOM 2694 O GLN B 28 -15.738 41.746 64.191 1.00 21.73 O ANISOU 2694 O GLN B 28 2884 2795 2576 262 521 -748 O ATOM 2695 CB GLN B 28 -18.206 40.773 63.390 1.00 26.34 C ANISOU 2695 CB GLN B 28 3480 3348 3181 272 586 -630 C ATOM 2696 CG GLN B 28 -19.603 40.195 63.196 1.00 20.99 C ANISOU 2696 CG GLN B 28 2804 2665 2507 283 623 -574 C ATOM 2697 CD GLN B 28 -20.077 39.382 64.386 1.00 26.02 C ANISOU 2697 CD GLN B 28 3451 3355 3081 327 647 -557 C ATOM 2698 OE1 GLN B 28 -19.626 38.258 64.602 1.00 30.51 O ANISOU 2698 OE1 GLN B 28 4022 3955 3613 336 649 -527 O ATOM 2699 NE2 GLN B 28 -20.996 39.944 65.161 1.00 25.55 N ANISOU 2699 NE2 GLN B 28 3396 3304 3009 357 668 -574 N ATOM 2700 N TYR B 29 -16.580 43.595 65.155 1.00 27.54 N ANISOU 2700 N TYR B 29 3625 3510 3328 284 532 -833 N ATOM 2701 CA TYR B 29 -15.277 44.229 65.309 1.00 30.72 C ANISOU 2701 CA TYR B 29 4016 3915 3742 264 498 -902 C ATOM 2702 C TYR B 29 -14.357 43.458 66.249 1.00 35.71 C ANISOU 2702 C TYR B 29 4643 4624 4299 290 472 -922 C ATOM 2703 O TYR B 29 -13.142 43.681 66.227 1.00 31.05 O ANISOU 2703 O TYR B 29 4038 4044 3716 271 440 -966 O ATOM 2704 CB TYR B 29 -15.464 45.662 65.811 1.00 29.88 C ANISOU 2704 CB TYR B 29 3908 3782 3663 266 499 -978 C ATOM 2705 CG TYR B 29 -16.215 46.551 64.844 1.00 29.72 C ANISOU 2705 CG TYR B 29 3890 3683 3721 242 523 -961 C ATOM 2706 CD1 TYR B 29 -15.997 46.461 63.476 1.00 36.74 C ANISOU 2706 CD1 TYR B 29 4771 4521 4666 205 524 -914 C ATOM 2707 CD2 TYR B 29 -17.142 47.478 65.301 1.00 24.45 C ANISOU 2707 CD2 TYR B 29 3230 2992 3067 262 547 -990 C ATOM 2708 CE1 TYR B 29 -16.677 47.268 62.588 1.00 24.11 C ANISOU 2708 CE1 TYR B 29 3172 2855 3132 189 548 -894 C ATOM 2709 CE2 TYR B 29 -17.829 48.289 64.421 1.00 32.97 C ANISOU 2709 CE2 TYR B 29 4310 4001 4215 246 571 -970 C ATOM 2710 CZ TYR B 29 -17.593 48.181 63.064 1.00 42.58 C ANISOU 2710 CZ TYR B 29 5520 5173 5486 210 571 -921 C ATOM 2711 OH TYR B 29 -18.276 48.987 62.179 1.00 34.93 O ANISOU 2711 OH TYR B 29 4552 4140 4582 200 597 -897 O ATOM 2712 N TYR B 30 -14.905 42.562 67.073 1.00 36.78 N ANISOU 2712 N TYR B 30 4792 4816 4367 335 489 -889 N ATOM 2713 CA TYR B 30 -14.095 41.792 68.009 1.00 31.05 C ANISOU 2713 CA TYR B 30 4063 4168 3564 369 469 -901 C ATOM 2714 C TYR B 30 -13.191 40.776 67.321 1.00 32.17 C ANISOU 2714 C TYR B 30 4198 4318 3706 350 455 -855 C ATOM 2715 O TYR B 30 -12.284 40.251 67.973 1.00 35.88 O ANISOU 2715 O TYR B 30 4662 4852 4120 374 433 -870 O ATOM 2716 CB TYR B 30 -14.992 41.066 69.012 1.00 32.94 C ANISOU 2716 CB TYR B 30 4321 4461 3735 426 499 -867 C ATOM 2717 CG TYR B 30 -15.894 40.036 68.376 1.00 22.99 C ANISOU 2717 CG TYR B 30 3071 3178 2487 424 537 -774 C ATOM 2718 CD1 TYR B 30 -15.474 38.722 68.206 1.00 26.79 C ANISOU 2718 CD1 TYR B 30 3554 3686 2940 432 542 -714 C ATOM 2719 CD2 TYR B 30 -17.165 40.378 67.942 1.00 22.80 C ANISOU 2719 CD2 TYR B 30 3052 3105 2504 416 569 -747 C ATOM 2720 CE1 TYR B 30 -16.297 37.781 67.620 1.00 24.23 C ANISOU 2720 CE1 TYR B 30 3237 3337 2632 426 579 -636 C ATOM 2721 CE2 TYR B 30 -17.995 39.445 67.356 1.00 29.26 C ANISOU 2721 CE2 TYR B 30 3876 3905 3337 411 602 -669 C ATOM 2722 CZ TYR B 30 -17.557 38.150 67.199 1.00 24.64 C ANISOU 2722 CZ TYR B 30 3292 3344 2727 414 607 -616 C ATOM 2723 OH TYR B 30 -18.387 37.224 66.617 1.00 22.63 O ANISOU 2723 OH TYR B 30 3040 3067 2491 406 642 -545 O ATOM 2724 N LEU B 31 -13.421 40.473 66.040 1.00 22.32 N ANISOU 2724 N LEU B 31 2951 3014 2516 311 468 -799 N ATOM 2725 CA LEU B 31 -12.600 39.507 65.322 1.00 27.28 C ANISOU 2725 CA LEU B 31 3574 3645 3146 292 458 -754 C ATOM 2726 C LEU B 31 -11.803 40.102 64.170 1.00 31.42 C ANISOU 2726 C LEU B 31 4083 4117 3740 239 436 -770 C ATOM 2727 O LEU B 31 -10.940 39.408 63.621 1.00 30.29 O ANISOU 2727 O LEU B 31 3932 3979 3597 224 423 -744 O ATOM 2728 CB LEU B 31 -13.461 38.343 64.795 1.00 25.27 C ANISOU 2728 CB LEU B 31 3333 3378 2891 296 494 -667 C ATOM 2729 CG LEU B 31 -14.790 38.573 64.063 1.00 29.36 C ANISOU 2729 CG LEU B 31 3856 3841 3457 279 524 -632 C ATOM 2730 CD1 LEU B 31 -14.580 39.033 62.624 1.00 24.45 C ANISOU 2730 CD1 LEU B 31 3225 3156 2908 228 515 -622 C ATOM 2731 CD2 LEU B 31 -15.628 37.305 64.093 1.00 20.94 C ANISOU 2731 CD2 LEU B 31 2802 2789 2367 298 560 -561 C ATOM 2732 N ALA B 32 -12.064 41.350 63.785 1.00 27.71 N ANISOU 2732 N ALA B 32 3608 3594 3328 213 436 -809 N ATOM 2733 CA ALA B 32 -11.281 42.012 62.752 1.00 32.76 C ANISOU 2733 CA ALA B 32 4233 4181 4035 166 420 -826 C ATOM 2734 C ALA B 32 -11.401 43.517 62.935 1.00 32.44 C ANISOU 2734 C ALA B 32 4185 4100 4039 153 418 -894 C ATOM 2735 O ALA B 32 -12.391 44.011 63.481 1.00 32.22 O ANISOU 2735 O ALA B 32 4169 4068 4005 175 437 -909 O ATOM 2736 CB ALA B 32 -11.733 41.606 61.346 1.00 30.63 C ANISOU 2736 CB ALA B 32 3967 3858 3811 138 439 -754 C ATOM 2737 N AGLU B 33 -10.382 44.237 62.479 0.37 32.77 N ANISOU 2737 N AGLU B 33 4209 4112 4130 118 399 -937 N ATOM 2738 N BGLU B 33 -10.382 44.233 62.467 0.64 32.76 N ANISOU 2738 N BGLU B 33 4208 4110 4130 117 399 -936 N ATOM 2739 CA AGLU B 33 -10.378 45.682 62.624 0.37 33.02 C ANISOU 2739 CA AGLU B 33 4232 4098 4214 101 400 -1006 C ATOM 2740 CA BGLU B 33 -10.363 45.681 62.584 0.64 33.01 C ANISOU 2740 CA BGLU B 33 4232 4097 4215 100 400 -1004 C ATOM 2741 C AGLU B 33 -11.378 46.315 61.656 0.37 31.31 C ANISOU 2741 C AGLU B 33 4027 3807 4061 87 434 -967 C ATOM 2742 C BGLU B 33 -11.409 46.301 61.659 0.64 31.35 C ANISOU 2742 C BGLU B 33 4033 3812 4066 87 434 -965 C ATOM 2743 O AGLU B 33 -11.674 45.750 60.599 0.37 24.36 O ANISOU 2743 O AGLU B 33 3153 2904 3200 75 447 -895 O ATOM 2744 O BGLU B 33 -11.765 45.715 60.633 0.64 24.26 O ANISOU 2744 O BGLU B 33 3141 2892 3184 77 448 -892 O ATOM 2745 CB AGLU B 33 -8.979 46.242 62.384 0.37 34.33 C ANISOU 2745 CB AGLU B 33 4373 4251 4422 65 374 -1060 C ATOM 2746 CB BGLU B 33 -8.982 46.223 62.231 0.64 34.44 C ANISOU 2746 CB BGLU B 33 4387 4258 4441 62 376 -1053 C ATOM 2747 CG AGLU B 33 -7.950 45.790 63.411 0.37 33.02 C ANISOU 2747 CG AGLU B 33 4190 4164 4193 81 337 -1112 C ATOM 2748 CG BGLU B 33 -7.821 45.493 62.890 0.64 36.53 C ANISOU 2748 CG BGLU B 33 4634 4597 4649 71 339 -1080 C ATOM 2749 CD AGLU B 33 -6.657 46.578 63.331 0.37 38.32 C ANISOU 2749 CD AGLU B 33 4828 4819 4911 44 311 -1185 C ATOM 2750 CD BGLU B 33 -7.335 46.181 64.150 0.64 32.77 C ANISOU 2750 CD BGLU B 33 4142 4163 4146 84 314 -1180 C ATOM 2751 OE1AGLU B 33 -6.723 47.815 63.165 0.37 41.46 O ANISOU 2751 OE1AGLU B 33 5220 5157 5376 18 322 -1235 O ATOM 2752 OE1BGLU B 33 -8.178 46.558 64.990 0.64 39.86 O ANISOU 2752 OE1BGLU B 33 5053 5074 5016 114 326 -1209 O ATOM 2753 OE2AGLU B 33 -5.574 45.961 63.427 0.37 32.23 O ANISOU 2753 OE2AGLU B 33 4038 4095 4112 41 282 -1191 O ATOM 2754 OE2BGLU B 33 -6.106 46.356 64.292 0.64 38.85 O ANISOU 2754 OE2BGLU B 33 4883 4954 4924 64 284 -1233 O ATOM 2755 N PRO B 34 -11.921 47.488 62.001 1.00 34.08 N ANISOU 2755 N PRO B 34 4382 4122 4445 90 449 -1014 N ATOM 2756 CA PRO B 34 -12.906 48.133 61.115 1.00 31.61 C ANISOU 2756 CA PRO B 34 4078 3740 4192 83 483 -975 C ATOM 2757 C PRO B 34 -12.379 48.430 59.721 1.00 26.56 C ANISOU 2757 C PRO B 34 3429 3040 3622 44 489 -942 C ATOM 2758 O PRO B 34 -13.158 48.418 58.760 1.00 21.97 O ANISOU 2758 O PRO B 34 2856 2422 3069 43 513 -879 O ATOM 2759 CB PRO B 34 -13.264 49.421 61.871 1.00 32.97 C ANISOU 2759 CB PRO B 34 4253 3886 4388 92 496 -1048 C ATOM 2760 CG PRO B 34 -12.936 49.133 63.291 1.00 23.64 C ANISOU 2760 CG PRO B 34 3069 2776 3135 118 472 -1108 C ATOM 2761 CD PRO B 34 -11.727 48.246 63.249 1.00 30.06 C ANISOU 2761 CD PRO B 34 3868 3637 3917 105 438 -1105 C ATOM 2762 N TRP B 35 -11.080 48.706 59.575 1.00 27.94 N ANISOU 2762 N TRP B 35 3586 3206 3826 14 468 -982 N ATOM 2763 CA TRP B 35 -10.541 48.937 58.240 1.00 26.56 C ANISOU 2763 CA TRP B 35 3402 2975 3715 -20 477 -945 C ATOM 2764 C TRP B 35 -10.620 47.680 57.384 1.00 29.84 C ANISOU 2764 C TRP B 35 3822 3413 4101 -20 473 -862 C ATOM 2765 O TRP B 35 -10.682 47.776 56.152 1.00 23.56 O ANISOU 2765 O TRP B 35 3028 2574 3350 -36 489 -810 O ATOM 2766 CB TRP B 35 -9.099 49.444 58.320 1.00 32.47 C ANISOU 2766 CB TRP B 35 4126 3712 4500 -54 457 -1007 C ATOM 2767 CG TRP B 35 -8.101 48.437 58.811 1.00 38.58 C ANISOU 2767 CG TRP B 35 4886 4556 5216 -54 419 -1020 C ATOM 2768 CD1 TRP B 35 -7.623 48.316 60.078 1.00 22.99 C ANISOU 2768 CD1 TRP B 35 2902 2643 3190 -39 391 -1088 C ATOM 2769 CD2 TRP B 35 -7.443 47.424 58.035 1.00 26.08 C ANISOU 2769 CD2 TRP B 35 3298 2991 3620 -66 407 -964 C ATOM 2770 NE1 TRP B 35 -6.720 47.284 60.148 1.00 34.76 N ANISOU 2770 NE1 TRP B 35 4381 4191 4636 -39 362 -1073 N ATOM 2771 CE2 TRP B 35 -6.592 46.720 58.906 1.00 30.87 C ANISOU 2771 CE2 TRP B 35 3891 3670 4167 -56 373 -998 C ATOM 2772 CE3 TRP B 35 -7.495 47.043 56.691 1.00 33.19 C ANISOU 2772 CE3 TRP B 35 4204 3858 4550 -81 422 -889 C ATOM 2773 CZ2 TRP B 35 -5.802 45.658 58.478 1.00 33.07 C ANISOU 2773 CZ2 TRP B 35 4163 3982 4420 -61 356 -957 C ATOM 2774 CZ3 TRP B 35 -6.711 45.989 56.270 1.00 35.28 C ANISOU 2774 CZ3 TRP B 35 4462 4155 4788 -88 405 -852 C ATOM 2775 CH2 TRP B 35 -5.875 45.310 57.158 1.00 34.34 C ANISOU 2775 CH2 TRP B 35 4331 4103 4615 -79 373 -886 C ATOM 2776 N GLN B 36 -10.605 46.501 58.010 1.00 23.84 N ANISOU 2776 N GLN B 36 3068 2722 3268 0 455 -848 N ATOM 2777 CA GLN B 36 -10.795 45.264 57.260 1.00 22.41 C ANISOU 2777 CA GLN B 36 2894 2561 3061 2 456 -771 C ATOM 2778 C GLN B 36 -12.198 45.193 56.669 1.00 21.92 C ANISOU 2778 C GLN B 36 2846 2476 3007 16 484 -714 C ATOM 2779 O GLN B 36 -12.369 44.840 55.496 1.00 21.03 O ANISOU 2779 O GLN B 36 2735 2341 2916 3 493 -657 O ATOM 2780 CB GLN B 36 -10.532 44.054 58.156 1.00 30.33 C ANISOU 2780 CB GLN B 36 3900 3638 3986 25 438 -769 C ATOM 2781 CG GLN B 36 -9.124 43.977 58.721 1.00 37.77 C ANISOU 2781 CG GLN B 36 4824 4615 4911 17 406 -819 C ATOM 2782 CD GLN B 36 -8.951 42.807 59.668 1.00 37.75 C ANISOU 2782 CD GLN B 36 4826 4690 4828 49 392 -812 C ATOM 2783 OE1 GLN B 36 -8.772 42.991 60.872 1.00 49.67 O ANISOU 2783 OE1 GLN B 36 6332 6244 6295 73 377 -866 O ATOM 2784 NE2 GLN B 36 -9.014 41.594 59.130 1.00 43.92 N ANISOU 2784 NE2 GLN B 36 5616 5487 5585 52 398 -745 N ATOM 2785 N PHE B 37 -13.216 45.524 57.469 1.00 20.75 N ANISOU 2785 N PHE B 37 2707 2336 2840 43 498 -731 N ATOM 2786 CA PHE B 37 -14.583 45.541 56.958 1.00 22.45 C ANISOU 2786 CA PHE B 37 2932 2533 3066 57 525 -682 C ATOM 2787 C PHE B 37 -14.769 46.614 55.892 1.00 21.32 C ANISOU 2787 C PHE B 37 2785 2323 2994 41 544 -669 C ATOM 2788 O PHE B 37 -15.572 46.435 54.969 1.00 24.83 O ANISOU 2788 O PHE B 37 3230 2752 3452 44 559 -613 O ATOM 2789 CB PHE B 37 -15.575 45.749 58.104 1.00 20.84 C ANISOU 2789 CB PHE B 37 2737 2353 2828 90 538 -706 C ATOM 2790 CG PHE B 37 -15.654 44.590 59.061 1.00 30.70 C ANISOU 2790 CG PHE B 37 3992 3669 4005 114 530 -701 C ATOM 2791 CD1 PHE B 37 -16.425 43.477 58.761 1.00 30.11 C ANISOU 2791 CD1 PHE B 37 3922 3616 3903 124 542 -638 C ATOM 2792 CD2 PHE B 37 -14.969 44.621 60.265 1.00 31.79 C ANISOU 2792 CD2 PHE B 37 4129 3847 4101 128 512 -758 C ATOM 2793 CE1 PHE B 37 -16.502 42.410 59.641 1.00 30.50 C ANISOU 2793 CE1 PHE B 37 3977 3721 3889 148 542 -628 C ATOM 2794 CE2 PHE B 37 -15.042 43.559 61.150 1.00 23.03 C ANISOU 2794 CE2 PHE B 37 3026 2801 2922 156 508 -747 C ATOM 2795 CZ PHE B 37 -15.811 42.453 60.839 1.00 31.41 C ANISOU 2795 CZ PHE B 37 4094 3878 3961 166 526 -679 C ATOM 2796 N ASER B 38 -14.043 47.730 55.998 0.48 21.91 N ANISOU 2796 N ASER B 38 2852 2358 3115 25 543 -721 N ATOM 2797 N BSER B 38 -14.050 47.734 56.007 0.52 21.90 N ANISOU 2797 N BSER B 38 2851 2356 3113 26 543 -721 N ATOM 2798 CA ASER B 38 -14.147 48.773 54.984 0.48 22.39 C ANISOU 2798 CA ASER B 38 2910 2350 3247 13 567 -705 C ATOM 2799 CA BSER B 38 -14.132 48.775 54.989 0.52 22.38 C ANISOU 2799 CA BSER B 38 2909 2348 3246 13 566 -706 C ATOM 2800 C ASER B 38 -13.598 48.306 53.643 0.48 23.50 C ANISOU 2800 C ASER B 38 3045 2476 3408 -8 564 -650 C ATOM 2801 C BSER B 38 -13.624 48.273 53.644 0.52 23.50 C ANISOU 2801 C BSER B 38 3045 2477 3406 -8 564 -648 C ATOM 2802 O ASER B 38 -14.091 48.729 52.591 0.48 25.57 O ANISOU 2802 O ASER B 38 3308 2700 3709 -6 586 -604 O ATOM 2803 O BSER B 38 -14.164 48.635 52.592 0.52 25.56 O ANISOU 2803 O BSER B 38 3307 2703 3702 -5 585 -601 O ATOM 2804 CB ASER B 38 -13.419 50.033 55.451 0.48 21.66 C ANISOU 2804 CB ASER B 38 2811 2214 3206 -2 571 -778 C ATOM 2805 CB BSER B 38 -13.344 50.007 55.432 0.52 21.66 C ANISOU 2805 CB BSER B 38 2810 2214 3205 -4 570 -778 C ATOM 2806 OG ASER B 38 -13.716 51.140 54.617 0.48 24.86 O ANISOU 2806 OG ASER B 38 3216 2548 3682 -6 604 -761 O ATOM 2807 OG BSER B 38 -13.904 50.584 56.597 0.52 23.13 O ANISOU 2807 OG BSER B 38 3003 2408 3378 18 576 -833 O ATOM 2808 N MET B 39 -12.575 47.446 53.658 1.00 25.88 N ANISOU 2808 N MET B 39 3340 2810 3683 -25 538 -652 N ATOM 2809 CA MET B 39 -12.038 46.910 52.412 1.00 26.98 C ANISOU 2809 CA MET B 39 3475 2941 3837 -44 535 -600 C ATOM 2810 C MET B 39 -13.046 46.003 51.713 1.00 23.65 C ANISOU 2810 C MET B 39 3061 2541 3384 -29 541 -533 C ATOM 2811 O MET B 39 -13.153 46.022 50.481 1.00 22.93 O ANISOU 2811 O MET B 39 2968 2427 3318 -34 552 -485 O ATOM 2812 CB MET B 39 -10.731 46.163 52.679 1.00 23.35 C ANISOU 2812 CB MET B 39 3006 2515 3352 -62 506 -620 C ATOM 2813 CG MET B 39 -9.576 47.062 53.099 1.00 40.81 C ANISOU 2813 CG MET B 39 5202 4701 5603 -84 498 -685 C ATOM 2814 SD MET B 39 -8.003 46.184 53.051 1.00 52.29 S ANISOU 2814 SD MET B 39 6639 6191 7036 -107 467 -693 S ATOM 2815 CE MET B 39 -7.947 45.680 51.331 1.00 57.18 C ANISOU 2815 CE MET B 39 7262 6784 7679 -118 481 -609 C ATOM 2816 N LEU B 40 -13.782 45.191 52.477 1.00 21.87 N ANISOU 2816 N LEU B 40 2843 2363 3105 -10 536 -530 N ATOM 2817 CA LEU B 40 -14.832 44.374 51.875 1.00 30.07 C ANISOU 2817 CA LEU B 40 3884 3420 4120 2 545 -473 C ATOM 2818 C LEU B 40 -15.910 45.247 51.245 1.00 23.88 C ANISOU 2818 C LEU B 40 3099 2602 3372 16 569 -449 C ATOM 2819 O LEU B 40 -16.376 44.968 50.133 1.00 21.52 O ANISOU 2819 O LEU B 40 2796 2300 3081 16 575 -400 O ATOM 2820 CB LEU B 40 -15.448 43.441 52.919 1.00 19.67 C ANISOU 2820 CB LEU B 40 2573 2154 2746 21 542 -477 C ATOM 2821 CG LEU B 40 -14.582 42.381 53.603 1.00 19.01 C ANISOU 2821 CG LEU B 40 2493 2115 2617 17 522 -489 C ATOM 2822 CD1 LEU B 40 -15.455 41.463 54.443 1.00 24.53 C ANISOU 2822 CD1 LEU B 40 3198 2856 3264 41 530 -477 C ATOM 2823 CD2 LEU B 40 -13.787 41.573 52.588 1.00 18.66 C ANISOU 2823 CD2 LEU B 40 2444 2071 2575 -5 511 -454 C ATOM 2824 N ALA B 41 -16.316 46.314 51.940 1.00 19.69 N ANISOU 2824 N ALA B 41 2570 2048 2862 30 583 -485 N ATOM 2825 CA ALA B 41 -17.358 47.196 51.422 1.00 25.91 C ANISOU 2825 CA ALA B 41 3357 2803 3684 49 609 -462 C ATOM 2826 C ALA B 41 -16.906 47.916 50.156 1.00 25.37 C ANISOU 2826 C ALA B 41 3284 2687 3669 39 621 -435 C ATOM 2827 O ALA B 41 -17.673 48.023 49.191 1.00 33.27 O ANISOU 2827 O ALA B 41 4280 3680 4680 53 635 -385 O ATOM 2828 CB ALA B 41 -17.771 48.203 52.495 1.00 20.32 C ANISOU 2828 CB ALA B 41 2655 2077 2989 66 624 -512 C ATOM 2829 N ALA B 42 -15.671 48.423 50.140 1.00 27.34 N ANISOU 2829 N ALA B 42 3532 2904 3951 16 617 -465 N ATOM 2830 CA ALA B 42 -15.153 49.070 48.938 1.00 20.42 C ANISOU 2830 CA ALA B 42 2651 1981 3127 7 633 -435 C ATOM 2831 C ALA B 42 -15.021 48.072 47.795 1.00 32.87 C ANISOU 2831 C ALA B 42 4225 3584 4681 1 621 -378 C ATOM 2832 O ALA B 42 -15.284 48.409 46.635 1.00 19.68 O ANISOU 2832 O ALA B 42 2551 1892 3034 11 638 -330 O ATOM 2833 CB ALA B 42 -13.807 49.731 49.231 1.00 21.94 C ANISOU 2833 CB ALA B 42 2839 2136 3362 -20 631 -484 C ATOM 2834 N TYR B 43 -14.601 46.846 48.111 1.00 23.54 N ANISOU 2834 N TYR B 43 3044 2450 3452 -13 594 -382 N ATOM 2835 CA TYR B 43 -14.526 45.784 47.113 1.00 25.46 C ANISOU 2835 CA TYR B 43 3284 2720 3668 -18 583 -334 C ATOM 2836 C TYR B 43 -15.899 45.495 46.519 1.00 26.73 C ANISOU 2836 C TYR B 43 3442 2902 3812 4 591 -290 C ATOM 2837 O TYR B 43 -16.059 45.428 45.294 1.00 22.74 O ANISOU 2837 O TYR B 43 2933 2395 3314 9 596 -246 O ATOM 2838 CB TYR B 43 -13.928 44.534 47.760 1.00 19.53 C ANISOU 2838 CB TYR B 43 2536 2015 2871 -33 557 -351 C ATOM 2839 CG TYR B 43 -13.895 43.294 46.899 1.00 27.97 C ANISOU 2839 CG TYR B 43 3603 3114 3909 -40 546 -308 C ATOM 2840 CD1 TYR B 43 -12.905 43.114 45.941 1.00 27.53 C ANISOU 2840 CD1 TYR B 43 3545 3047 3868 -56 542 -287 C ATOM 2841 CD2 TYR B 43 -14.837 42.286 47.070 1.00 19.81 C ANISOU 2841 CD2 TYR B 43 2572 2121 2835 -31 543 -291 C ATOM 2842 CE1 TYR B 43 -12.866 41.971 45.161 1.00 32.07 C ANISOU 2842 CE1 TYR B 43 4120 3650 4414 -62 533 -253 C ATOM 2843 CE2 TYR B 43 -14.804 41.142 46.300 1.00 17.71 C ANISOU 2843 CE2 TYR B 43 2305 1880 2546 -39 535 -258 C ATOM 2844 CZ TYR B 43 -13.818 40.989 45.349 1.00 34.95 C ANISOU 2844 CZ TYR B 43 4487 4052 4741 -54 529 -240 C ATOM 2845 OH TYR B 43 -13.787 39.849 44.585 1.00 25.71 O ANISOU 2845 OH TYR B 43 3316 2906 3546 -62 522 -212 O ATOM 2846 N MET B 44 -16.912 45.353 47.376 1.00 20.43 N ANISOU 2846 N MET B 44 2645 2126 2990 20 594 -304 N ATOM 2847 CA MET B 44 -18.260 45.078 46.891 1.00 27.62 C ANISOU 2847 CA MET B 44 3549 3060 3885 41 601 -267 C ATOM 2848 C MET B 44 -18.838 46.264 46.135 1.00 25.83 C ANISOU 2848 C MET B 44 3316 2798 3698 64 624 -242 C ATOM 2849 O MET B 44 -19.603 46.073 45.183 1.00 26.12 O ANISOU 2849 O MET B 44 3343 2853 3728 79 627 -200 O ATOM 2850 CB MET B 44 -19.176 44.693 48.051 1.00 18.82 C ANISOU 2850 CB MET B 44 2435 1976 2740 54 602 -288 C ATOM 2851 CG MET B 44 -18.813 43.367 48.698 1.00 18.57 C ANISOU 2851 CG MET B 44 2407 1983 2664 38 585 -300 C ATOM 2852 SD MET B 44 -18.642 42.039 47.487 1.00 24.75 S ANISOU 2852 SD MET B 44 3183 2793 3427 21 571 -257 S ATOM 2853 CE MET B 44 -20.283 42.008 46.767 1.00 20.43 C ANISOU 2853 CE MET B 44 2619 2265 2879 41 583 -222 C ATOM 2854 N PHE B 45 -18.496 47.488 46.544 1.00 25.50 N ANISOU 2854 N PHE B 45 3282 2710 3699 69 642 -268 N ATOM 2855 CA PHE B 45 -18.975 48.662 45.823 1.00 25.84 C ANISOU 2855 CA PHE B 45 3321 2713 3784 94 671 -240 C ATOM 2856 C PHE B 45 -18.446 48.679 44.394 1.00 26.08 C ANISOU 2856 C PHE B 45 3348 2732 3830 92 674 -194 C ATOM 2857 O PHE B 45 -19.184 48.998 43.455 1.00 26.26 O ANISOU 2857 O PHE B 45 3362 2757 3857 120 688 -147 O ATOM 2858 CB PHE B 45 -18.577 49.936 46.566 1.00 23.29 C ANISOU 2858 CB PHE B 45 3006 2333 3509 94 693 -283 C ATOM 2859 CG PHE B 45 -19.195 51.181 46.004 1.00 21.08 C ANISOU 2859 CG PHE B 45 2726 2009 3276 124 729 -256 C ATOM 2860 CD1 PHE B 45 -20.570 51.295 45.893 1.00 24.51 C ANISOU 2860 CD1 PHE B 45 3153 2463 3695 160 740 -227 C ATOM 2861 CD2 PHE B 45 -18.404 52.241 45.597 1.00 23.38 C ANISOU 2861 CD2 PHE B 45 3020 2235 3626 120 755 -257 C ATOM 2862 CE1 PHE B 45 -21.144 52.440 45.381 1.00 21.11 C ANISOU 2862 CE1 PHE B 45 2722 1994 3306 193 776 -198 C ATOM 2863 CE2 PHE B 45 -18.972 53.389 45.084 1.00 21.38 C ANISOU 2863 CE2 PHE B 45 2768 1937 3417 152 795 -227 C ATOM 2864 CZ PHE B 45 -20.344 53.491 44.980 1.00 35.65 C ANISOU 2864 CZ PHE B 45 4571 3769 5207 191 805 -196 C ATOM 2865 N ALEU B 46 -17.167 48.341 44.211 0.67 23.49 N ANISOU 2865 N ALEU B 46 3023 2395 3507 63 662 -204 N ATOM 2866 N BLEU B 46 -17.167 48.340 44.212 0.33 23.53 N ANISOU 2866 N BLEU B 46 3028 2400 3512 63 662 -204 N ATOM 2867 CA ALEU B 46 -16.608 48.282 42.865 0.67 24.16 C ANISOU 2867 CA ALEU B 46 3104 2472 3603 62 666 -159 C ATOM 2868 CA BLEU B 46 -16.596 48.276 42.871 0.33 24.23 C ANISOU 2868 CA BLEU B 46 3113 2480 3611 61 666 -159 C ATOM 2869 C ALEU B 46 -17.290 47.203 42.033 0.67 28.73 C ANISOU 2869 C ALEU B 46 3675 3107 4133 71 648 -119 C ATOM 2870 C BLEU B 46 -17.277 47.199 42.034 0.33 28.62 C ANISOU 2870 C BLEU B 46 3661 3093 4120 71 648 -119 C ATOM 2871 O ALEU B 46 -17.593 47.418 40.853 0.67 25.84 O ANISOU 2871 O ALEU B 46 3303 2745 3770 93 658 -72 O ATOM 2872 O BLEU B 46 -17.562 47.409 40.849 0.33 25.88 O ANISOU 2872 O BLEU B 46 3308 2749 3776 92 658 -72 O ATOM 2873 CB ALEU B 46 -15.101 48.034 42.928 0.67 25.68 C ANISOU 2873 CB ALEU B 46 3300 2648 3808 27 655 -181 C ATOM 2874 CB BLEU B 46 -15.088 48.028 42.964 0.33 25.70 C ANISOU 2874 CB BLEU B 46 3304 2651 3811 27 654 -183 C ATOM 2875 CG ALEU B 46 -14.398 48.050 41.568 0.67 27.51 C ANISOU 2875 CG ALEU B 46 3530 2867 4056 26 663 -135 C ATOM 2876 CG BLEU B 46 -14.214 48.042 41.703 0.33 27.59 C ANISOU 2876 CG BLEU B 46 3540 2874 4068 21 662 -143 C ATOM 2877 CD1ALEU B 46 -14.340 49.466 41.017 0.67 32.68 C ANISOU 2877 CD1ALEU B 46 4185 3462 4771 46 703 -113 C ATOM 2878 CD1BLEU B 46 -14.165 46.674 41.028 0.33 28.67 C ANISOU 2878 CD1BLEU B 46 3676 3066 4154 14 636 -117 C ATOM 2879 CD2ALEU B 46 -13.009 47.447 41.652 0.67 26.13 C ANISOU 2879 CD2ALEU B 46 3356 2694 3880 -8 646 -156 C ATOM 2880 CD2BLEU B 46 -14.685 49.112 40.730 0.33 31.38 C ANISOU 2880 CD2BLEU B 46 4019 3319 4585 53 697 -96 C ATOM 2881 N LEU B 47 -17.546 46.037 42.635 1.00 22.44 N ANISOU 2881 N LEU B 47 2877 2356 3292 56 623 -138 N ATOM 2882 CA LEU B 47 -18.195 44.952 41.905 1.00 29.42 C ANISOU 2882 CA LEU B 47 3752 3292 4135 60 607 -109 C ATOM 2883 C LEU B 47 -19.595 45.345 41.450 1.00 31.00 C ANISOU 2883 C LEU B 47 3937 3509 4331 94 618 -81 C ATOM 2884 O LEU B 47 -20.013 45.001 40.338 1.00 24.13 O ANISOU 2884 O LEU B 47 3055 2669 3443 108 612 -45 O ATOM 2885 CB LEU B 47 -18.254 43.691 42.768 1.00 20.21 C ANISOU 2885 CB LEU B 47 2587 2163 2930 39 586 -137 C ATOM 2886 CG LEU B 47 -16.955 42.937 43.054 1.00 29.79 C ANISOU 2886 CG LEU B 47 3810 3376 4132 8 571 -156 C ATOM 2887 CD1 LEU B 47 -17.248 41.760 43.968 1.00 27.31 C ANISOU 2887 CD1 LEU B 47 3498 3099 3780 -3 558 -177 C ATOM 2888 CD2 LEU B 47 -16.312 42.462 41.765 1.00 30.31 C ANISOU 2888 CD2 LEU B 47 3874 3448 4193 0 564 -124 C ATOM 2889 N ILE B 48 -20.340 46.054 42.299 1.00 22.82 N ANISOU 2889 N ILE B 48 2902 2460 3310 111 632 -98 N ATOM 2890 CA ILE B 48 -21.671 46.513 41.913 1.00 26.43 C ANISOU 2890 CA ILE B 48 3343 2933 3765 147 645 -70 C ATOM 2891 C ILE B 48 -21.579 47.519 40.772 1.00 40.90 C ANISOU 2891 C ILE B 48 5174 4740 5627 176 666 -27 C ATOM 2892 O ILE B 48 -22.322 47.432 39.787 1.00 19.62 O ANISOU 2892 O ILE B 48 2463 2079 2915 203 664 12 O ATOM 2893 CB ILE B 48 -22.406 47.104 43.128 1.00 32.40 C ANISOU 2893 CB ILE B 48 4102 3676 4533 160 660 -99 C ATOM 2894 CG1 ILE B 48 -22.626 46.032 44.192 1.00 31.33 C ANISOU 2894 CG1 ILE B 48 3967 3574 4363 139 642 -133 C ATOM 2895 CG2 ILE B 48 -23.735 47.713 42.710 1.00 35.22 C ANISOU 2895 CG2 ILE B 48 4442 4046 4894 202 676 -68 C ATOM 2896 CD1 ILE B 48 -23.322 46.546 45.424 1.00 25.16 C ANISOU 2896 CD1 ILE B 48 3189 2784 3587 154 657 -162 C ATOM 2897 N MET B 49 -20.658 48.483 40.880 1.00 26.71 N ANISOU 2897 N MET B 49 3391 2882 3874 173 687 -34 N ATOM 2898 CA MET B 49 -20.578 49.557 39.896 1.00 30.13 C ANISOU 2898 CA MET B 49 3825 3282 4342 204 717 10 C ATOM 2899 C MET B 49 -20.015 49.090 38.559 1.00 30.43 C ANISOU 2899 C MET B 49 3859 3340 4364 205 708 51 C ATOM 2900 O MET B 49 -20.263 49.741 37.539 1.00 25.28 O ANISOU 2900 O MET B 49 3201 2682 3722 242 730 101 O ATOM 2901 CB MET B 49 -19.733 50.714 40.435 1.00 25.32 C ANISOU 2901 CB MET B 49 3231 2596 3793 196 747 -13 C ATOM 2902 CG MET B 49 -20.300 51.384 41.685 1.00 30.63 C ANISOU 2902 CG MET B 49 3908 3243 4486 201 761 -54 C ATOM 2903 SD MET B 49 -21.914 52.144 41.422 1.00 34.79 S ANISOU 2903 SD MET B 49 4423 3779 5015 258 787 -16 S ATOM 2904 CE MET B 49 -21.508 53.303 40.120 1.00 42.46 C ANISOU 2904 CE MET B 49 5397 4699 6035 292 829 44 C ATOM 2905 N LEU B 50 -19.249 48.003 38.541 1.00 27.85 N ANISOU 2905 N LEU B 50 3535 3036 4010 169 681 34 N ATOM 2906 CA LEU B 50 -18.839 47.404 37.277 1.00 25.84 C ANISOU 2906 CA LEU B 50 3276 2810 3731 171 670 70 C ATOM 2907 C LEU B 50 -19.811 46.323 36.826 1.00 23.98 C ANISOU 2907 C LEU B 50 3022 2646 3441 178 642 79 C ATOM 2908 O LEU B 50 -20.054 46.169 35.624 1.00 29.09 O ANISOU 2908 O LEU B 50 3660 3328 4066 202 639 117 O ATOM 2909 CB LEU B 50 -17.427 46.823 37.395 1.00 28.48 C ANISOU 2909 CB LEU B 50 3622 3129 4070 130 658 49 C ATOM 2910 CG LEU B 50 -16.273 47.818 37.554 1.00 47.82 C ANISOU 2910 CG LEU B 50 6083 5511 6576 120 684 43 C ATOM 2911 CD1 LEU B 50 -14.929 47.113 37.427 1.00 41.12 C ANISOU 2911 CD1 LEU B 50 5240 4660 5723 84 670 30 C ATOM 2912 CD2 LEU B 50 -16.385 48.946 36.536 1.00 44.72 C ANISOU 2912 CD2 LEU B 50 5689 5086 6216 159 722 96 C ATOM 2913 N GLY B 51 -20.377 45.578 37.779 1.00 27.51 N ANISOU 2913 N GLY B 51 3465 3119 3867 158 624 42 N ATOM 2914 CA GLY B 51 -21.214 44.440 37.427 1.00 24.03 C ANISOU 2914 CA GLY B 51 3006 2743 3381 156 599 42 C ATOM 2915 C GLY B 51 -22.487 44.834 36.702 1.00 27.45 C ANISOU 2915 C GLY B 51 3416 3212 3802 198 603 74 C ATOM 2916 O GLY B 51 -22.851 44.226 35.692 1.00 19.20 O ANISOU 2916 O GLY B 51 2354 2218 2724 208 586 93 O ATOM 2917 N PHE B 52 -23.191 45.847 37.213 1.00 24.32 N ANISOU 2917 N PHE B 52 3017 2795 3430 226 624 79 N ATOM 2918 CA PHE B 52 -24.439 46.258 36.572 1.00 30.02 C ANISOU 2918 CA PHE B 52 3714 3554 4139 271 629 111 C ATOM 2919 C PHE B 52 -24.237 46.737 35.139 1.00 31.45 C ANISOU 2919 C PHE B 52 3890 3747 4314 308 637 162 C ATOM 2920 O PHE B 52 -24.936 46.231 34.244 1.00 22.12 O ANISOU 2920 O PHE B 52 2682 2628 3094 327 618 180 O ATOM 2921 CB PHE B 52 -25.147 47.324 37.418 1.00 33.92 C ANISOU 2921 CB PHE B 52 4208 4016 4664 296 655 108 C ATOM 2922 CG PHE B 52 -26.162 48.129 36.646 1.00 40.77 C ANISOU 2922 CG PHE B 52 5054 4906 5529 354 671 153 C ATOM 2923 CD1 PHE B 52 -27.248 47.509 36.043 1.00 34.71 C ANISOU 2923 CD1 PHE B 52 4253 4212 4722 372 649 164 C ATOM 2924 CD2 PHE B 52 -26.027 49.503 36.518 1.00 39.95 C ANISOU 2924 CD2 PHE B 52 4963 4750 5466 390 709 183 C ATOM 2925 CE1 PHE B 52 -28.176 48.243 35.326 1.00 34.92 C ANISOU 2925 CE1 PHE B 52 4257 4267 4743 429 661 207 C ATOM 2926 CE2 PHE B 52 -26.957 50.244 35.806 1.00 44.69 C ANISOU 2926 CE2 PHE B 52 5544 5372 6063 449 726 229 C ATOM 2927 CZ PHE B 52 -28.032 49.612 35.210 1.00 33.26 C ANISOU 2927 CZ PHE B 52 4062 4006 4570 470 700 242 C ATOM 2928 N PRO B 53 -23.327 47.672 34.837 1.00 25.83 N ANISOU 2928 N PRO B 53 3198 2980 3638 320 664 186 N ATOM 2929 CA PRO B 53 -23.233 48.141 33.442 1.00 20.58 C ANISOU 2929 CA PRO B 53 2527 2330 2963 363 677 243 C ATOM 2930 C PRO B 53 -22.785 47.067 32.466 1.00 29.78 C ANISOU 2930 C PRO B 53 3686 3544 4084 349 648 248 C ATOM 2931 O PRO B 53 -23.423 46.881 31.421 1.00 23.28 O ANISOU 2931 O PRO B 53 2842 2782 3223 384 637 278 O ATOM 2932 CB PRO B 53 -22.224 49.298 33.529 1.00 20.78 C ANISOU 2932 CB PRO B 53 2579 2273 3045 368 718 260 C ATOM 2933 CG PRO B 53 -22.239 49.718 34.948 1.00 45.03 C ANISOU 2933 CG PRO B 53 5661 5294 6155 343 729 216 C ATOM 2934 CD PRO B 53 -22.435 48.445 35.718 1.00 24.45 C ANISOU 2934 CD PRO B 53 3049 2726 3513 300 690 166 C ATOM 2935 N ILE B 54 -21.701 46.348 32.772 1.00 19.96 N ANISOU 2935 N ILE B 54 2461 2280 2844 300 636 219 N ATOM 2936 CA ILE B 54 -21.167 45.389 31.809 1.00 26.25 C ANISOU 2936 CA ILE B 54 3255 3117 3602 289 613 225 C ATOM 2937 C ILE B 54 -22.116 44.218 31.596 1.00 20.65 C ANISOU 2937 C ILE B 54 2521 2483 2844 281 577 202 C ATOM 2938 O ILE B 54 -22.081 43.583 30.534 1.00 21.11 O ANISOU 2938 O ILE B 54 2568 2590 2863 289 559 214 O ATOM 2939 CB ILE B 54 -19.770 44.898 32.238 1.00 26.34 C ANISOU 2939 CB ILE B 54 3290 3087 3630 240 611 199 C ATOM 2940 CG1 ILE B 54 -19.048 44.259 31.047 1.00 31.16 C ANISOU 2940 CG1 ILE B 54 3903 3726 4211 241 600 220 C ATOM 2941 CG2 ILE B 54 -19.868 43.923 33.409 1.00 28.84 C ANISOU 2941 CG2 ILE B 54 3608 3409 3940 194 588 144 C ATOM 2942 CD1 ILE B 54 -17.617 43.863 31.331 1.00 28.17 C ANISOU 2942 CD1 ILE B 54 3546 3308 3851 200 601 202 C ATOM 2943 N ASN B 55 -22.975 43.909 32.569 1.00 19.58 N ANISOU 2943 N ASN B 55 2372 2357 2709 265 568 169 N ATOM 2944 CA ASN B 55 -23.963 42.861 32.348 1.00 22.69 C ANISOU 2944 CA ASN B 55 2738 2820 3064 257 538 147 C ATOM 2945 C ASN B 55 -25.208 43.406 31.662 1.00 26.52 C ANISOU 2945 C ASN B 55 3191 3356 3530 309 537 176 C ATOM 2946 O ASN B 55 -25.800 42.726 30.814 1.00 20.16 O ANISOU 2946 O ASN B 55 2357 2619 2684 318 512 173 O ATOM 2947 CB ASN B 55 -24.324 42.188 33.669 1.00 19.27 C ANISOU 2947 CB ASN B 55 2304 2378 2640 217 531 100 C ATOM 2948 CG ASN B 55 -23.270 41.204 34.119 1.00 25.06 C ANISOU 2948 CG ASN B 55 3060 3090 3374 167 522 70 C ATOM 2949 OD1 ASN B 55 -23.099 40.140 33.519 1.00 18.71 O ANISOU 2949 OD1 ASN B 55 2248 2319 2541 147 502 59 O ATOM 2950 ND2 ASN B 55 -22.556 41.550 35.182 1.00 18.65 N ANISOU 2950 ND2 ASN B 55 2273 2222 2592 147 536 55 N ATOM 2951 N PHE B 56 -25.625 44.622 32.021 1.00 24.32 N ANISOU 2951 N PHE B 56 2914 3047 3280 345 564 200 N ATOM 2952 CA PHE B 56 -26.741 45.246 31.319 1.00 20.80 C ANISOU 2952 CA PHE B 56 2438 2649 2816 403 567 235 C ATOM 2953 C PHE B 56 -26.391 45.504 29.860 1.00 26.69 C ANISOU 2953 C PHE B 56 3181 3426 3534 445 568 282 C ATOM 2954 O PHE B 56 -27.228 45.306 28.972 1.00 27.35 O ANISOU 2954 O PHE B 56 3232 3585 3577 480 549 296 O ATOM 2955 CB PHE B 56 -27.156 46.547 32.004 1.00 21.07 C ANISOU 2955 CB PHE B 56 2479 2635 2890 435 602 256 C ATOM 2956 CG PHE B 56 -28.269 47.269 31.296 1.00 33.66 C ANISOU 2956 CG PHE B 56 4045 4277 4469 501 610 298 C ATOM 2957 CD1 PHE B 56 -29.589 46.918 31.521 1.00 31.58 C ANISOU 2957 CD1 PHE B 56 3743 4070 4185 510 592 281 C ATOM 2958 CD2 PHE B 56 -27.995 48.284 30.392 1.00 27.54 C ANISOU 2958 CD2 PHE B 56 3276 3489 3698 557 638 357 C ATOM 2959 CE1 PHE B 56 -30.617 47.572 30.865 1.00 39.04 C ANISOU 2959 CE1 PHE B 56 4657 5065 5112 575 597 321 C ATOM 2960 CE2 PHE B 56 -29.017 48.941 29.733 1.00 27.30 C ANISOU 2960 CE2 PHE B 56 3217 3505 3649 624 646 400 C ATOM 2961 CZ PHE B 56 -30.330 48.586 29.971 1.00 41.82 C ANISOU 2961 CZ PHE B 56 5018 5407 5466 633 623 381 C ATOM 2962 N ALEU B 57 -25.161 45.953 29.596 0.55 23.12 N ANISOU 2962 N ALEU B 57 2761 2920 3104 443 590 305 N ATOM 2963 N BLEU B 57 -25.163 45.959 29.595 0.45 23.13 N ANISOU 2963 N BLEU B 57 2762 2921 3105 443 590 305 N ATOM 2964 CA ALEU B 57 -24.736 46.173 28.218 0.55 25.16 C ANISOU 2964 CA ALEU B 57 3019 3205 3335 483 595 352 C ATOM 2965 CA BLEU B 57 -24.736 46.173 28.216 0.45 25.16 C ANISOU 2965 CA BLEU B 57 3019 3206 3335 483 595 352 C ATOM 2966 C ALEU B 57 -24.708 44.864 27.439 0.55 29.25 C ANISOU 2966 C ALEU B 57 3521 3794 3799 464 555 328 C ATOM 2967 C BLEU B 57 -24.710 44.863 27.439 0.45 29.24 C ANISOU 2967 C BLEU B 57 3520 3793 3798 464 555 328 C ATOM 2968 O ALEU B 57 -25.086 44.825 26.262 0.55 28.59 O ANISOU 2968 O ALEU B 57 3417 3776 3669 508 543 356 O ATOM 2969 O BLEU B 57 -25.089 44.823 26.263 0.45 28.59 O ANISOU 2969 O BLEU B 57 3416 3776 3669 508 543 356 O ATOM 2970 CB ALEU B 57 -23.365 46.848 28.192 0.55 26.19 C ANISOU 2970 CB ALEU B 57 3187 3258 3507 477 630 378 C ATOM 2971 CB BLEU B 57 -23.363 46.845 28.186 0.45 26.19 C ANISOU 2971 CB BLEU B 57 3187 3259 3507 477 630 378 C ATOM 2972 CG ALEU B 57 -22.827 47.224 26.810 0.55 24.40 C ANISOU 2972 CG ALEU B 57 2964 3048 3260 524 646 435 C ATOM 2973 CG BLEU B 57 -23.354 48.353 28.439 0.45 24.98 C ANISOU 2973 CG BLEU B 57 3047 3041 3405 516 679 419 C ATOM 2974 CD1ALEU B 57 -23.823 48.103 26.072 0.55 26.82 C ANISOU 2974 CD1ALEU B 57 3249 3394 3547 601 663 490 C ATOM 2975 CD1BLEU B 57 -21.933 48.889 28.462 0.45 25.53 C ANISOU 2975 CD1BLEU B 57 3149 3031 3522 499 712 434 C ATOM 2976 CD2ALEU B 57 -21.480 47.919 26.930 0.55 22.10 C ANISOU 2976 CD2ALEU B 57 2706 2670 3020 512 686 457 C ATOM 2977 CD2BLEU B 57 -24.177 49.063 27.378 0.45 28.01 C ANISOU 2977 CD2BLEU B 57 3410 3472 3762 594 694 480 C ATOM 2978 N THR B 58 -24.262 43.780 28.080 1.00 25.92 N ANISOU 2978 N THR B 58 3108 3360 3379 400 534 276 N ATOM 2979 CA THR B 58 -24.269 42.476 27.425 1.00 28.64 C ANISOU 2979 CA THR B 58 3438 3767 3678 377 498 246 C ATOM 2980 C THR B 58 -25.691 42.045 27.079 1.00 29.21 C ANISOU 2980 C THR B 58 3465 3921 3713 395 470 229 C ATOM 2981 O THR B 58 -25.942 41.520 25.987 1.00 21.10 O ANISOU 2981 O THR B 58 2416 2964 2637 414 446 229 O ATOM 2982 CB THR B 58 -23.592 41.435 28.320 1.00 27.68 C ANISOU 2982 CB THR B 58 3335 3610 3572 307 487 196 C ATOM 2983 OG1 THR B 58 -22.215 41.786 28.511 1.00 23.28 O ANISOU 2983 OG1 THR B 58 2815 2986 3046 292 510 210 O ATOM 2984 CG2 THR B 58 -23.670 40.050 27.695 1.00 19.91 C ANISOU 2984 CG2 THR B 58 2335 2683 2546 281 454 161 C ATOM 2985 N LEU B 59 -26.634 42.266 27.998 1.00 22.30 N ANISOU 2985 N LEU B 59 2574 3042 2859 391 472 213 N ATOM 2986 CA LEU B 59 -28.040 41.992 27.714 1.00 28.89 C ANISOU 2986 CA LEU B 59 3361 3954 3664 412 449 199 C ATOM 2987 C LEU B 59 -28.552 42.878 26.584 1.00 26.62 C ANISOU 2987 C LEU B 59 3052 3719 3345 488 452 252 C ATOM 2988 O LEU B 59 -29.160 42.392 25.623 1.00 25.94 O ANISOU 2988 O LEU B 59 2930 3718 3210 510 423 245 O ATOM 2989 CB LEU B 59 -28.866 42.197 28.987 1.00 25.57 C ANISOU 2989 CB LEU B 59 2930 3508 3277 396 458 178 C ATOM 2990 CG LEU B 59 -30.368 41.896 29.040 1.00 22.13 C ANISOU 2990 CG LEU B 59 2442 3140 2824 407 438 157 C ATOM 2991 CD1 LEU B 59 -30.754 41.546 30.466 1.00 33.36 C ANISOU 2991 CD1 LEU B 59 3867 4526 4283 363 446 119 C ATOM 2992 CD2 LEU B 59 -31.200 43.075 28.571 1.00 33.83 C ANISOU 2992 CD2 LEU B 59 3903 4655 4298 480 450 205 C ATOM 2993 N TYR B 60 -28.302 44.187 26.682 1.00 22.79 N ANISOU 2993 N TYR B 60 2588 3184 2888 530 490 304 N ATOM 2994 CA TYR B 60 -28.861 45.138 25.726 1.00 29.91 C ANISOU 2994 CA TYR B 60 3471 4130 3765 610 501 362 C ATOM 2995 C TYR B 60 -28.355 44.879 24.312 1.00 27.82 C ANISOU 2995 C TYR B 60 3204 3918 3449 641 489 388 C ATOM 2996 O TYR B 60 -29.134 44.914 23.353 1.00 29.38 O ANISOU 2996 O TYR B 60 3365 4202 3595 694 470 406 O ATOM 2997 CB TYR B 60 -28.527 46.566 26.162 1.00 26.68 C ANISOU 2997 CB TYR B 60 3091 3641 3405 644 552 413 C ATOM 2998 CG TYR B 60 -29.133 47.651 25.296 1.00 27.78 C ANISOU 2998 CG TYR B 60 3214 3816 3526 732 574 480 C ATOM 2999 CD1 TYR B 60 -28.478 48.107 24.156 1.00 31.20 C ANISOU 2999 CD1 TYR B 60 3660 4257 3938 780 592 536 C ATOM 3000 CD2 TYR B 60 -30.355 48.228 25.624 1.00 23.81 C ANISOU 3000 CD2 TYR B 60 2681 3337 3027 771 580 492 C ATOM 3001 CE1 TYR B 60 -29.024 49.097 23.362 1.00 39.73 C ANISOU 3001 CE1 TYR B 60 4726 5371 5000 867 616 604 C ATOM 3002 CE2 TYR B 60 -30.910 49.224 24.835 1.00 40.90 C ANISOU 3002 CE2 TYR B 60 4830 5536 5174 857 602 558 C ATOM 3003 CZ TYR B 60 -30.237 49.652 23.706 1.00 38.18 C ANISOU 3003 CZ TYR B 60 4500 5199 4806 906 620 615 C ATOM 3004 OH TYR B 60 -30.771 50.638 22.910 1.00 51.33 O ANISOU 3004 OH TYR B 60 6151 6899 6452 997 646 686 O ATOM 3005 N VAL B 61 -27.054 44.624 24.162 1.00 26.36 N ANISOU 3005 N VAL B 61 3057 3686 3275 611 498 389 N ATOM 3006 CA VAL B 61 -26.491 44.386 22.835 1.00 28.65 C ANISOU 3006 CA VAL B 61 3348 4022 3517 641 491 415 C ATOM 3007 C VAL B 61 -27.109 43.142 22.211 1.00 30.99 C ANISOU 3007 C VAL B 61 3607 4414 3754 627 439 365 C ATOM 3008 O VAL B 61 -27.518 43.148 21.043 1.00 40.01 O ANISOU 3008 O VAL B 61 4723 5640 4838 680 423 386 O ATOM 3009 CB VAL B 61 -24.958 44.275 22.910 1.00 31.90 C ANISOU 3009 CB VAL B 61 3805 4359 3956 605 511 420 C ATOM 3010 CG1 VAL B 61 -24.398 43.798 21.580 1.00 30.31 C ANISOU 3010 CG1 VAL B 61 3605 4212 3701 629 499 437 C ATOM 3011 CG2 VAL B 61 -24.342 45.613 23.282 1.00 34.22 C ANISOU 3011 CG2 VAL B 61 4131 4566 4306 629 564 473 C ATOM 3012 N THR B 62 -27.194 42.057 22.986 1.00 24.74 N ANISOU 3012 N THR B 62 2810 3612 2976 555 415 298 N ATOM 3013 CA THR B 62 -27.691 40.793 22.450 1.00 27.27 C ANISOU 3013 CA THR B 62 3097 4013 3250 531 370 242 C ATOM 3014 C THR B 62 -29.124 40.928 21.949 1.00 33.34 C ANISOU 3014 C THR B 62 3810 4877 3980 576 345 240 C ATOM 3015 O THR B 62 -29.467 40.409 20.880 1.00 42.12 O ANISOU 3015 O THR B 62 4891 6078 5035 599 314 224 O ATOM 3016 CB THR B 62 -27.599 39.701 23.516 1.00 27.33 C ANISOU 3016 CB THR B 62 3111 3983 3291 448 359 176 C ATOM 3017 OG1 THR B 62 -26.250 39.605 23.988 1.00 24.82 O ANISOU 3017 OG1 THR B 62 2843 3583 3007 410 381 181 O ATOM 3018 CG2 THR B 62 -28.026 38.355 22.950 1.00 27.33 C ANISOU 3018 CG2 THR B 62 3078 4055 3252 417 318 116 C ATOM 3019 N VAL B 63 -29.974 41.624 22.706 1.00 32.02 N ANISOU 3019 N VAL B 63 3627 4695 3842 592 359 252 N ATOM 3020 CA VAL B 63 -31.362 41.812 22.298 1.00 35.03 C ANISOU 3020 CA VAL B 63 3953 5167 4191 637 336 251 C ATOM 3021 C VAL B 63 -31.453 42.720 21.075 1.00 48.57 C ANISOU 3021 C VAL B 63 5658 6938 5858 729 344 318 C ATOM 3022 O VAL B 63 -32.276 42.498 20.178 1.00 46.94 O ANISOU 3022 O VAL B 63 5404 6837 5595 769 311 310 O ATOM 3023 CB VAL B 63 -32.186 42.361 23.478 1.00 45.20 C ANISOU 3023 CB VAL B 63 5230 6418 5526 632 354 251 C ATOM 3024 CG1 VAL B 63 -33.588 42.736 23.027 1.00 44.82 C ANISOU 3024 CG1 VAL B 63 5124 6462 5446 690 336 262 C ATOM 3025 CG2 VAL B 63 -32.239 41.336 24.599 1.00 47.66 C ANISOU 3025 CG2 VAL B 63 5544 6691 5875 548 344 184 C ATOM 3026 N AGLN B 64 -30.610 43.752 21.015 0.46 45.98 N ANISOU 3026 N AGLN B 64 5374 6544 5553 764 387 384 N ATOM 3027 N BGLN B 64 -30.604 43.746 21.010 0.54 46.00 N ANISOU 3027 N BGLN B 64 5376 6546 5554 764 387 384 N ATOM 3028 CA AGLN B 64 -30.686 44.743 19.948 0.46 42.89 C ANISOU 3028 CA AGLN B 64 4978 6194 5123 857 406 459 C ATOM 3029 CA BGLN B 64 -30.690 44.740 19.948 0.54 42.89 C ANISOU 3029 CA BGLN B 64 4978 6194 5123 857 406 458 C ATOM 3030 C AGLN B 64 -30.165 44.230 18.611 0.46 44.40 C ANISOU 3030 C AGLN B 64 5167 6454 5249 882 385 464 C ATOM 3031 C BGLN B 64 -30.136 44.246 18.616 0.54 44.39 C ANISOU 3031 C BGLN B 64 5168 6451 5250 882 386 466 C ATOM 3032 O AGLN B 64 -30.354 44.906 17.594 0.46 52.23 O ANISOU 3032 O AGLN B 64 6147 7503 6195 966 394 523 O ATOM 3033 O BGLN B 64 -30.275 44.949 17.610 0.54 52.25 O ANISOU 3033 O BGLN B 64 6154 7499 6201 966 397 526 O ATOM 3034 CB AGLN B 64 -29.911 46.006 20.341 0.46 44.78 C ANISOU 3034 CB AGLN B 64 5266 6331 5418 882 466 526 C ATOM 3035 CB BGLN B 64 -29.959 46.018 20.377 0.54 44.79 C ANISOU 3035 CB BGLN B 64 5265 6332 5420 882 466 526 C ATOM 3036 CG AGLN B 64 -30.428 47.278 19.682 0.46 47.71 C ANISOU 3036 CG AGLN B 64 5626 6731 5772 982 497 608 C ATOM 3037 CG BGLN B 64 -30.432 47.296 19.687 0.54 47.72 C ANISOU 3037 CG BGLN B 64 5627 6731 5773 983 498 608 C ATOM 3038 CD AGLN B 64 -29.420 48.411 19.712 0.46 48.27 C ANISOU 3038 CD AGLN B 64 5746 6703 5890 1010 560 678 C ATOM 3039 CD BGLN B 64 -31.747 47.831 20.237 0.54 46.89 C ANISOU 3039 CD BGLN B 64 5486 6650 5680 1013 498 612 C ATOM 3040 OE1AGLN B 64 -28.258 48.217 20.070 0.46 44.65 O ANISOU 3040 OE1AGLN B 64 5329 6166 5470 957 577 665 O ATOM 3041 OE1BGLN B 64 -32.487 47.126 20.925 0.54 45.54 O ANISOU 3041 OE1BGLN B 64 5287 6502 5516 964 466 549 O ATOM 3042 NE2AGLN B 64 -29.860 49.603 19.326 0.46 50.25 N ANISOU 3042 NE2AGLN B 64 5993 6960 6141 1094 598 752 N ATOM 3043 NE2BGLN B 64 -32.041 49.091 19.933 0.54 47.14 N ANISOU 3043 NE2BGLN B 64 5519 6674 5717 1094 540 689 N ATOM 3044 N HIS B 65 -29.521 43.065 18.576 1.00 39.70 N ANISOU 3044 N HIS B 65 4583 5855 4647 817 360 407 N ATOM 3045 CA HIS B 65 -28.947 42.522 17.348 1.00 47.12 C ANISOU 3045 CA HIS B 65 5524 6854 5525 837 341 407 C ATOM 3046 C HIS B 65 -29.472 41.109 17.136 1.00 43.02 C ANISOU 3046 C HIS B 65 4966 6409 4969 788 286 319 C ATOM 3047 O HIS B 65 -29.069 40.182 17.845 1.00 46.37 O ANISOU 3047 O HIS B 65 5407 6785 5429 706 277 261 O ATOM 3048 CB HIS B 65 -27.418 42.526 17.402 1.00 40.45 C ANISOU 3048 CB HIS B 65 4737 5921 4710 808 373 428 C ATOM 3049 CG HIS B 65 -26.817 43.891 17.539 1.00 48.80 C ANISOU 3049 CG HIS B 65 5832 6902 5809 852 431 511 C ATOM 3050 ND1 HIS B 65 -26.178 44.533 16.499 1.00 53.12 N ANISOU 3050 ND1 HIS B 65 6397 7458 6327 918 460 581 N ATOM 3051 CD2 HIS B 65 -26.752 44.734 18.598 1.00 42.49 C ANISOU 3051 CD2 HIS B 65 5054 6011 5080 839 468 533 C ATOM 3052 CE1 HIS B 65 -25.746 45.712 16.911 1.00 54.84 C ANISOU 3052 CE1 HIS B 65 6645 7591 6601 941 514 642 C ATOM 3053 NE2 HIS B 65 -26.079 45.857 18.182 1.00 52.75 N ANISOU 3053 NE2 HIS B 65 6383 7264 6397 894 519 612 N ATOM 3054 N LYS B 66 -30.354 40.941 16.148 1.00 43.68 N ANISOU 3054 N LYS B 66 5000 6613 4984 839 250 309 N ATOM 3055 CA LYS B 66 -30.898 39.623 15.842 1.00 43.76 C ANISOU 3055 CA LYS B 66 4968 6701 4959 795 197 221 C ATOM 3056 C LYS B 66 -29.858 38.677 15.255 1.00 43.41 C ANISOU 3056 C LYS B 66 4951 6653 4891 759 186 188 C ATOM 3057 O LYS B 66 -30.133 37.477 15.141 1.00 41.59 O ANISOU 3057 O LYS B 66 4694 6463 4644 707 148 107 O ATOM 3058 CB LYS B 66 -32.079 39.752 14.879 1.00 53.02 C ANISOU 3058 CB LYS B 66 6076 8009 6059 863 159 217 C ATOM 3059 N LYS B 67 -28.683 39.182 14.872 1.00 42.67 N ANISOU 3059 N LYS B 67 4908 6511 4796 786 220 247 N ATOM 3060 CA LYS B 67 -27.619 38.318 14.375 1.00 37.51 C ANISOU 3060 CA LYS B 67 4283 5846 4124 753 215 220 C ATOM 3061 C LYS B 67 -26.993 37.479 15.478 1.00 34.46 C ANISOU 3061 C LYS B 67 3927 5364 3803 655 222 169 C ATOM 3062 O LYS B 67 -26.317 36.488 15.179 1.00 44.10 O ANISOU 3062 O LYS B 67 5163 6583 5012 614 210 126 O ATOM 3063 CB LYS B 67 -26.534 39.156 13.699 1.00 43.50 C ANISOU 3063 CB LYS B 67 5085 6574 4868 810 255 304 C ATOM 3064 CG LYS B 67 -25.662 39.928 14.678 1.00 28.29 C ANISOU 3064 CG LYS B 67 3209 4518 3021 787 308 354 C ATOM 3065 CD LYS B 67 -24.701 40.847 13.952 1.00 48.31 C ANISOU 3065 CD LYS B 67 5781 7029 5546 849 351 440 C ATOM 3066 N LEU B 68 -27.193 37.855 16.740 1.00 45.79 N ANISOU 3066 N LEU B 68 5371 6722 5306 620 243 174 N ATOM 3067 CA LEU B 68 -26.573 37.170 17.872 1.00 37.02 C ANISOU 3067 CA LEU B 68 4291 5519 4257 535 254 134 C ATOM 3068 C LEU B 68 -27.574 36.164 18.433 1.00 40.70 C ANISOU 3068 C LEU B 68 4717 6015 4734 479 222 54 C ATOM 3069 O LEU B 68 -28.222 36.386 19.456 1.00 40.34 O ANISOU 3069 O LEU B 68 4660 5937 4732 457 229 47 O ATOM 3070 CB LEU B 68 -26.126 38.180 18.924 1.00 36.49 C ANISOU 3070 CB LEU B 68 4259 5350 4253 532 297 185 C ATOM 3071 CG LEU B 68 -25.087 39.215 18.485 1.00 37.91 C ANISOU 3071 CG LEU B 68 4480 5486 4438 580 337 262 C ATOM 3072 CD1 LEU B 68 -24.966 40.328 19.517 1.00 36.07 C ANISOU 3072 CD1 LEU B 68 4270 5166 4269 583 377 305 C ATOM 3073 CD2 LEU B 68 -23.742 38.555 18.245 1.00 38.46 C ANISOU 3073 CD2 LEU B 68 4588 5516 4510 544 344 253 C ATOM 3074 N ARG B 69 -27.694 35.027 17.737 1.00 33.58 N ANISOU 3074 N ARG B 69 3792 5174 3793 456 188 -7 N ATOM 3075 CA ARG B 69 -28.630 33.987 18.152 1.00 35.12 C ANISOU 3075 CA ARG B 69 3944 5399 4000 400 160 -87 C ATOM 3076 C ARG B 69 -28.010 32.593 18.105 1.00 39.36 C ANISOU 3076 C ARG B 69 4496 5917 4544 334 151 -152 C ATOM 3077 O ARG B 69 -28.742 31.601 18.000 1.00 25.54 O ANISOU 3077 O ARG B 69 2704 4212 2788 296 124 -226 O ATOM 3078 CB ARG B 69 -29.899 34.025 17.290 1.00 40.64 C ANISOU 3078 CB ARG B 69 4578 6219 4646 445 121 -111 C ATOM 3079 CG ARG B 69 -30.710 35.308 17.429 1.00 32.11 C ANISOU 3079 CG ARG B 69 3476 5162 3563 509 130 -53 C ATOM 3080 CD ARG B 69 -31.234 35.486 18.844 1.00 44.03 C ANISOU 3080 CD ARG B 69 4983 6605 5141 468 148 -58 C ATOM 3081 NE ARG B 69 -31.961 36.740 19.013 1.00 42.30 N ANISOU 3081 NE ARG B 69 4748 6402 4924 530 161 -1 N ATOM 3082 CZ ARG B 69 -31.394 37.899 19.320 1.00 40.72 C ANISOU 3082 CZ ARG B 69 4589 6137 4746 568 200 74 C ATOM 3083 NH1 ARG B 69 -30.085 38.009 19.474 1.00 23.89 N ANISOU 3083 NH1 ARG B 69 2516 3926 2636 552 228 102 N ATOM 3084 NH2 ARG B 69 -32.160 38.976 19.475 1.00 37.27 N ANISOU 3084 NH2 ARG B 69 4133 5716 4312 624 212 121 N ATOM 3085 N THR B 70 -26.684 32.490 18.179 1.00 33.59 N ANISOU 3085 N THR B 70 3819 5117 3826 318 176 -128 N ATOM 3086 CA THR B 70 -26.032 31.199 18.315 1.00 27.31 C ANISOU 3086 CA THR B 70 3043 4288 3046 254 175 -184 C ATOM 3087 C THR B 70 -26.203 30.683 19.741 1.00 34.85 C ANISOU 3087 C THR B 70 4004 5168 4069 186 192 -213 C ATOM 3088 O THR B 70 -26.596 31.435 20.636 1.00 38.06 O ANISOU 3088 O THR B 70 4410 5539 4510 192 207 -183 O ATOM 3089 CB THR B 70 -24.548 31.313 17.974 1.00 24.59 C ANISOU 3089 CB THR B 70 2753 3895 2696 263 198 -143 C ATOM 3090 OG1 THR B 70 -23.862 32.001 19.028 1.00 26.25 O ANISOU 3090 OG1 THR B 70 3003 4010 2959 252 234 -94 O ATOM 3091 CG2 THR B 70 -24.361 32.075 16.674 1.00 38.15 C ANISOU 3091 CG2 THR B 70 4468 5678 4350 341 192 -95 C ATOM 3092 N PRO B 71 -25.944 29.390 19.977 1.00 36.17 N ANISOU 3092 N PRO B 71 4177 5311 4256 124 191 -273 N ATOM 3093 CA PRO B 71 -25.988 28.890 21.362 1.00 37.78 C ANISOU 3093 CA PRO B 71 4392 5439 4524 64 213 -292 C ATOM 3094 C PRO B 71 -25.113 29.682 22.320 1.00 26.10 C ANISOU 3094 C PRO B 71 2962 3875 3082 68 246 -232 C ATOM 3095 O PRO B 71 -25.523 29.934 23.460 1.00 29.99 O ANISOU 3095 O PRO B 71 3453 4325 3616 50 261 -227 O ATOM 3096 CB PRO B 71 -25.504 27.442 21.216 1.00 21.66 C ANISOU 3096 CB PRO B 71 2360 3380 2489 10 213 -352 C ATOM 3097 CG PRO B 71 -25.949 27.050 19.864 1.00 25.72 C ANISOU 3097 CG PRO B 71 2838 3986 2948 30 179 -393 C ATOM 3098 CD PRO B 71 -25.836 28.286 19.004 1.00 24.55 C ANISOU 3098 CD PRO B 71 2692 3889 2749 107 169 -332 C ATOM 3099 N LEU B 72 -23.920 30.091 21.883 1.00 26.86 N ANISOU 3099 N LEU B 72 3099 3945 3163 92 259 -189 N ATOM 3100 CA LEU B 72 -23.053 30.893 22.740 1.00 28.86 C ANISOU 3100 CA LEU B 72 3393 4120 3451 96 289 -136 C ATOM 3101 C LEU B 72 -23.713 32.215 23.108 1.00 32.01 C ANISOU 3101 C LEU B 72 3781 4521 3861 137 295 -93 C ATOM 3102 O LEU B 72 -23.634 32.658 24.260 1.00 28.10 O ANISOU 3102 O LEU B 72 3301 3966 3408 122 316 -77 O ATOM 3103 CB LEU B 72 -21.712 31.137 22.047 1.00 33.14 C ANISOU 3103 CB LEU B 72 3974 4643 3975 118 301 -98 C ATOM 3104 CG LEU B 72 -20.657 31.947 22.803 1.00 34.92 C ANISOU 3104 CG LEU B 72 4241 4789 4238 120 332 -48 C ATOM 3105 CD1 LEU B 72 -20.202 31.207 24.049 1.00 33.30 C ANISOU 3105 CD1 LEU B 72 4057 4517 4077 62 346 -74 C ATOM 3106 CD2 LEU B 72 -19.469 32.260 21.893 1.00 25.91 C ANISOU 3106 CD2 LEU B 72 3127 3642 3074 149 343 -8 C ATOM 3107 N ASN B 73 -24.368 32.861 22.140 1.00 29.17 N ANISOU 3107 N ASN B 73 3392 4231 3460 192 279 -73 N ATOM 3108 CA ASN B 73 -25.034 34.129 22.418 1.00 20.99 C ANISOU 3108 CA ASN B 73 2343 3199 2433 236 288 -28 C ATOM 3109 C ASN B 73 -26.138 33.962 23.455 1.00 25.98 C ANISOU 3109 C ASN B 73 2946 3826 3097 208 284 -60 C ATOM 3110 O ASN B 73 -26.277 34.791 24.362 1.00 28.99 O ANISOU 3110 O ASN B 73 3340 4162 3515 215 305 -31 O ATOM 3111 CB ASN B 73 -25.596 34.719 21.124 1.00 27.53 C ANISOU 3111 CB ASN B 73 3142 4114 3205 304 270 -3 C ATOM 3112 CG ASN B 73 -24.541 34.872 20.045 1.00 30.02 C ANISOU 3112 CG ASN B 73 3484 4439 3483 338 275 32 C ATOM 3113 OD1 ASN B 73 -24.812 34.662 18.863 1.00 33.00 O ANISOU 3113 OD1 ASN B 73 3839 4897 3803 373 252 24 O ATOM 3114 ND2 ASN B 73 -23.328 35.228 20.449 1.00 21.87 N ANISOU 3114 ND2 ASN B 73 2500 3328 2484 327 306 67 N ATOM 3115 N TYR B 74 -26.935 32.895 23.337 1.00 25.75 N ANISOU 3115 N TYR B 74 2880 3844 3059 174 260 -122 N ATOM 3116 CA TYR B 74 -27.997 32.652 24.311 1.00 31.93 C ANISOU 3116 CA TYR B 74 3634 4623 3876 145 261 -153 C ATOM 3117 C TYR B 74 -27.429 32.397 25.701 1.00 30.92 C ANISOU 3117 C TYR B 74 3542 4405 3802 97 290 -155 C ATOM 3118 O TYR B 74 -27.941 32.923 26.695 1.00 22.76 O ANISOU 3118 O TYR B 74 2506 3342 2799 97 304 -143 O ATOM 3119 CB TYR B 74 -28.858 31.465 23.877 1.00 25.02 C ANISOU 3119 CB TYR B 74 2711 3810 2987 112 233 -223 C ATOM 3120 CG TYR B 74 -29.897 31.786 22.831 1.00 31.04 C ANISOU 3120 CG TYR B 74 3417 4673 3702 158 200 -231 C ATOM 3121 CD1 TYR B 74 -31.056 32.468 23.167 1.00 39.26 C ANISOU 3121 CD1 TYR B 74 4420 5747 4750 185 197 -220 C ATOM 3122 CD2 TYR B 74 -29.729 31.395 21.512 1.00 31.43 C ANISOU 3122 CD2 TYR B 74 3453 4791 3698 178 174 -251 C ATOM 3123 CE1 TYR B 74 -32.016 32.760 22.216 1.00 44.44 C ANISOU 3123 CE1 TYR B 74 5023 6502 5362 231 166 -226 C ATOM 3124 CE2 TYR B 74 -30.684 31.682 20.554 1.00 36.76 C ANISOU 3124 CE2 TYR B 74 4076 5568 4324 225 141 -259 C ATOM 3125 CZ TYR B 74 -31.825 32.364 20.912 1.00 37.92 C ANISOU 3125 CZ TYR B 74 4182 5747 4479 252 137 -246 C ATOM 3126 OH TYR B 74 -32.778 32.655 19.962 1.00 31.74 O ANISOU 3126 OH TYR B 74 3344 5071 3646 302 104 -254 O ATOM 3127 N ILE B 75 -26.370 31.588 25.788 1.00 20.25 N ANISOU 3127 N ILE B 75 2226 3011 2458 60 298 -170 N ATOM 3128 CA ILE B 75 -25.813 31.221 27.087 1.00 20.98 C ANISOU 3128 CA ILE B 75 2350 3026 2595 17 324 -175 C ATOM 3129 C ILE B 75 -25.210 32.439 27.779 1.00 19.82 C ANISOU 3129 C ILE B 75 2238 2824 2469 42 346 -122 C ATOM 3130 O ILE B 75 -25.324 32.597 29.002 1.00 23.54 O ANISOU 3130 O ILE B 75 2720 3250 2975 25 364 -121 O ATOM 3131 CB ILE B 75 -24.785 30.085 26.918 1.00 29.24 C ANISOU 3131 CB ILE B 75 3424 4045 3641 -22 328 -199 C ATOM 3132 CG1 ILE B 75 -25.476 28.797 26.459 1.00 29.70 C ANISOU 3132 CG1 ILE B 75 3447 4145 3691 -57 312 -262 C ATOM 3133 CG2 ILE B 75 -24.035 29.836 28.215 1.00 20.42 C ANISOU 3133 CG2 ILE B 75 2345 2850 2564 -56 356 -194 C ATOM 3134 CD1 ILE B 75 -26.433 28.220 27.479 1.00 33.57 C ANISOU 3134 CD1 ILE B 75 3913 4622 4220 -95 323 -296 C ATOM 3135 N LEU B 76 -24.569 33.324 27.012 1.00 21.12 N ANISOU 3135 N LEU B 76 2419 2992 2613 85 347 -78 N ATOM 3136 CA LEU B 76 -23.999 34.534 27.596 1.00 28.70 C ANISOU 3136 CA LEU B 76 3408 3898 3598 108 371 -31 C ATOM 3137 C LEU B 76 -25.077 35.542 27.978 1.00 26.85 C ANISOU 3137 C LEU B 76 3151 3677 3375 142 375 -12 C ATOM 3138 O LEU B 76 -24.915 36.271 28.963 1.00 30.83 O ANISOU 3138 O LEU B 76 3673 4127 3912 143 397 5 O ATOM 3139 CB LEU B 76 -22.996 35.162 26.629 1.00 21.61 C ANISOU 3139 CB LEU B 76 2534 2996 2682 143 377 12 C ATOM 3140 CG LEU B 76 -21.519 34.887 26.917 1.00 20.37 C ANISOU 3140 CG LEU B 76 2418 2779 2542 116 393 18 C ATOM 3141 CD1 LEU B 76 -21.086 35.603 28.188 1.00 20.71 C ANISOU 3141 CD1 LEU B 76 2486 2752 2631 105 416 32 C ATOM 3142 CD2 LEU B 76 -21.260 33.391 27.021 1.00 18.76 C ANISOU 3142 CD2 LEU B 76 2218 2578 2333 67 382 -30 C ATOM 3143 N LEU B 77 -26.169 35.610 27.209 1.00 34.36 N ANISOU 3143 N LEU B 77 4060 4699 4296 171 355 -17 N ATOM 3144 CA LEU B 77 -27.312 36.429 27.609 1.00 27.76 C ANISOU 3144 CA LEU B 77 3196 3881 3470 201 359 -3 C ATOM 3145 C LEU B 77 -27.921 35.912 28.904 1.00 24.05 C ANISOU 3145 C LEU B 77 2718 3386 3035 158 366 -39 C ATOM 3146 O LEU B 77 -28.299 36.697 29.783 1.00 20.09 O ANISOU 3146 O LEU B 77 2219 2853 2560 171 384 -22 O ATOM 3147 CB LEU B 77 -28.361 36.442 26.495 1.00 29.80 C ANISOU 3147 CB LEU B 77 3405 4232 3685 240 332 -6 C ATOM 3148 CG LEU B 77 -29.736 37.054 26.774 1.00 32.61 C ANISOU 3148 CG LEU B 77 3719 4625 4045 270 329 -1 C ATOM 3149 CD1 LEU B 77 -29.623 38.534 27.079 1.00 30.93 C ANISOU 3149 CD1 LEU B 77 3528 4374 3852 319 357 58 C ATOM 3150 CD2 LEU B 77 -30.646 36.833 25.577 1.00 25.55 C ANISOU 3150 CD2 LEU B 77 2773 3833 3102 303 296 -14 C ATOM 3151 N ASN B 78 -28.024 34.588 29.033 1.00 27.77 N ANISOU 3151 N ASN B 78 3177 3867 3507 109 355 -88 N ATOM 3152 CA ASN B 78 -28.521 33.987 30.264 1.00 19.85 C ANISOU 3152 CA ASN B 78 2168 2836 2537 68 367 -119 C ATOM 3153 C ASN B 78 -27.606 34.312 31.439 1.00 25.12 C ANISOU 3153 C ASN B 78 2883 3425 3236 53 394 -102 C ATOM 3154 O ASN B 78 -28.079 34.540 32.559 1.00 26.59 O ANISOU 3154 O ASN B 78 3070 3585 3449 46 410 -105 O ATOM 3155 CB ASN B 78 -28.650 32.473 30.074 1.00 25.84 C ANISOU 3155 CB ASN B 78 2911 3615 3294 18 356 -172 C ATOM 3156 CG ASN B 78 -29.219 31.769 31.292 1.00 19.77 C ANISOU 3156 CG ASN B 78 2132 2818 2560 -24 373 -202 C ATOM 3157 OD1 ASN B 78 -30.103 32.289 31.972 1.00 27.21 O ANISOU 3157 OD1 ASN B 78 3055 3763 3520 -11 382 -195 O ATOM 3158 ND2 ASN B 78 -28.714 30.570 31.569 1.00 24.81 N ANISOU 3158 ND2 ASN B 78 2786 3430 3213 -70 382 -232 N ATOM 3159 N LEU B 79 -26.292 34.334 31.204 1.00 19.10 N ANISOU 3159 N LEU B 79 2160 2627 2470 48 399 -87 N ATOM 3160 CA LEU B 79 -25.353 34.664 32.271 1.00 23.74 C ANISOU 3160 CA LEU B 79 2790 3146 3086 36 421 -75 C ATOM 3161 C LEU B 79 -25.472 36.123 32.688 1.00 20.86 C ANISOU 3161 C LEU B 79 2434 2756 2738 74 436 -40 C ATOM 3162 O LEU B 79 -25.420 36.436 33.882 1.00 18.62 O ANISOU 3162 O LEU B 79 2165 2430 2479 65 453 -43 O ATOM 3163 CB LEU B 79 -23.923 34.351 31.836 1.00 18.44 C ANISOU 3163 CB LEU B 79 2153 2447 2407 23 422 -67 C ATOM 3164 CG LEU B 79 -23.567 32.869 31.733 1.00 26.68 C ANISOU 3164 CG LEU B 79 3199 3494 3443 -20 416 -102 C ATOM 3165 CD1 LEU B 79 -22.103 32.694 31.357 1.00 33.24 C ANISOU 3165 CD1 LEU B 79 4065 4296 4268 -27 419 -88 C ATOM 3166 CD2 LEU B 79 -23.882 32.152 33.032 1.00 28.22 C ANISOU 3166 CD2 LEU B 79 3396 3663 3662 -55 430 -128 C ATOM 3167 N ALA B 80 -25.615 37.031 31.718 1.00 20.67 N ANISOU 3167 N ALA B 80 2400 2757 2698 119 432 -7 N ATOM 3168 CA ALA B 80 -25.798 38.441 32.045 1.00 19.22 C ANISOU 3168 CA ALA B 80 2223 2547 2534 158 451 28 C ATOM 3169 C ALA B 80 -27.016 38.641 32.935 1.00 19.37 C ANISOU 3169 C ALA B 80 2218 2574 2567 162 457 14 C ATOM 3170 O ALA B 80 -26.996 39.465 33.858 1.00 23.01 O ANISOU 3170 O ALA B 80 2696 2991 3056 171 478 24 O ATOM 3171 CB ALA B 80 -25.925 39.265 30.764 1.00 24.22 C ANISOU 3171 CB ALA B 80 2845 3214 3145 211 448 69 C ATOM 3172 N VAL B 81 -28.087 37.891 32.672 1.00 23.84 N ANISOU 3172 N VAL B 81 2745 3197 3117 154 439 -10 N ATOM 3173 CA VAL B 81 -29.295 37.992 33.486 1.00 19.74 C ANISOU 3173 CA VAL B 81 2198 2690 2612 156 445 -23 C ATOM 3174 C VAL B 81 -29.034 37.475 34.897 1.00 20.35 C ANISOU 3174 C VAL B 81 2297 2719 2716 115 462 -49 C ATOM 3175 O VAL B 81 -29.410 38.110 35.888 1.00 20.36 O ANISOU 3175 O VAL B 81 2305 2694 2739 126 481 -44 O ATOM 3176 CB VAL B 81 -30.454 37.238 32.809 1.00 30.04 C ANISOU 3176 CB VAL B 81 3449 4069 3894 154 422 -47 C ATOM 3177 CG1 VAL B 81 -31.677 37.231 33.709 1.00 22.01 C ANISOU 3177 CG1 VAL B 81 2402 3063 2897 150 431 -63 C ATOM 3178 CG2 VAL B 81 -30.785 37.865 31.452 1.00 32.08 C ANISOU 3178 CG2 VAL B 81 3684 4385 4120 204 404 -19 C ATOM 3179 N ALA B 82 -28.386 36.312 35.010 1.00 20.47 N ANISOU 3179 N ALA B 82 2326 2723 2728 72 457 -75 N ATOM 3180 CA ALA B 82 -28.103 35.749 36.327 1.00 26.47 C ANISOU 3180 CA ALA B 82 3108 3442 3509 38 475 -95 C ATOM 3181 C ALA B 82 -27.130 36.628 37.103 1.00 20.84 C ANISOU 3181 C ALA B 82 2436 2671 2811 47 491 -78 C ATOM 3182 O ALA B 82 -27.234 36.752 38.329 1.00 27.55 O ANISOU 3182 O ALA B 82 3299 3493 3677 41 508 -87 O ATOM 3183 CB ALA B 82 -27.555 34.331 36.194 1.00 19.86 C ANISOU 3183 CB ALA B 82 2277 2604 2665 -6 469 -122 C ATOM 3184 N ASP B 83 -26.168 37.235 36.405 1.00 22.07 N ANISOU 3184 N ASP B 83 2614 2810 2962 62 487 -56 N ATOM 3185 CA ASP B 83 -25.244 38.157 37.061 1.00 19.97 C ANISOU 3185 CA ASP B 83 2382 2489 2716 71 503 -44 C ATOM 3186 C ASP B 83 -25.977 39.367 37.631 1.00 28.36 C ANISOU 3186 C ASP B 83 3439 3538 3797 104 519 -32 C ATOM 3187 O ASP B 83 -25.674 39.820 38.740 1.00 18.96 O ANISOU 3187 O ASP B 83 2270 2308 2626 100 535 -41 O ATOM 3188 CB ASP B 83 -24.164 38.607 36.078 1.00 18.37 C ANISOU 3188 CB ASP B 83 2197 2272 2510 82 500 -19 C ATOM 3189 CG ASP B 83 -23.237 37.478 35.671 1.00 18.81 C ANISOU 3189 CG ASP B 83 2266 2331 2551 49 488 -31 C ATOM 3190 OD1 ASP B 83 -23.296 36.397 36.292 1.00 27.06 O ANISOU 3190 OD1 ASP B 83 3311 3379 3592 16 486 -59 O ATOM 3191 OD2 ASP B 83 -22.447 37.672 34.726 1.00 21.64 O ANISOU 3191 OD2 ASP B 83 2634 2687 2901 58 483 -11 O ATOM 3192 N LEU B 84 -26.943 39.908 36.882 1.00 23.63 N ANISOU 3192 N LEU B 84 2812 2976 3192 138 516 -11 N ATOM 3193 CA LEU B 84 -27.717 41.040 37.380 1.00 24.23 C ANISOU 3193 CA LEU B 84 2881 3041 3286 174 534 2 C ATOM 3194 C LEU B 84 -28.506 40.660 38.626 1.00 21.52 C ANISOU 3194 C LEU B 84 2529 2698 2951 159 543 -25 C ATOM 3195 O LEU B 84 -28.621 41.457 39.566 1.00 22.04 O ANISOU 3195 O LEU B 84 2607 2729 3036 173 563 -26 O ATOM 3196 CB LEU B 84 -28.651 41.564 36.289 1.00 27.24 C ANISOU 3196 CB LEU B 84 3228 3469 3653 217 528 32 C ATOM 3197 CG LEU B 84 -28.019 42.374 35.154 1.00 23.33 C ANISOU 3197 CG LEU B 84 2744 2968 3154 251 530 71 C ATOM 3198 CD1 LEU B 84 -29.042 42.663 34.070 1.00 31.22 C ANISOU 3198 CD1 LEU B 84 3703 4029 4128 296 520 98 C ATOM 3199 CD2 LEU B 84 -27.430 43.671 35.686 1.00 24.63 C ANISOU 3199 CD2 LEU B 84 2938 3066 3354 271 560 90 C ATOM 3200 N PHE B 85 -29.066 39.448 38.648 1.00 19.17 N ANISOU 3200 N PHE B 85 2207 2437 2639 131 531 -47 N ATOM 3201 CA PHE B 85 -29.710 38.960 39.863 1.00 27.66 C ANISOU 3201 CA PHE B 85 3276 3509 3723 114 544 -70 C ATOM 3202 C PHE B 85 -28.719 38.893 41.015 1.00 20.67 C ANISOU 3202 C PHE B 85 2432 2574 2847 95 558 -85 C ATOM 3203 O PHE B 85 -29.063 39.218 42.157 1.00 24.97 O ANISOU 3203 O PHE B 85 2984 3102 3402 101 576 -94 O ATOM 3204 CB PHE B 85 -30.337 37.588 39.621 1.00 22.94 C ANISOU 3204 CB PHE B 85 2648 2954 3115 83 533 -92 C ATOM 3205 CG PHE B 85 -31.688 37.644 38.976 1.00 29.50 C ANISOU 3205 CG PHE B 85 3428 3839 3940 102 524 -89 C ATOM 3206 CD1 PHE B 85 -32.786 38.101 39.685 1.00 26.30 C ANISOU 3206 CD1 PHE B 85 3002 3443 3548 122 540 -88 C ATOM 3207 CD2 PHE B 85 -31.866 37.225 37.669 1.00 30.67 C ANISOU 3207 CD2 PHE B 85 3549 4035 4070 102 500 -89 C ATOM 3208 CE1 PHE B 85 -34.035 38.152 39.098 1.00 35.82 C ANISOU 3208 CE1 PHE B 85 4157 4704 4750 141 531 -85 C ATOM 3209 CE2 PHE B 85 -33.116 37.269 37.077 1.00 31.31 C ANISOU 3209 CE2 PHE B 85 3579 4175 4144 121 488 -91 C ATOM 3210 CZ PHE B 85 -34.201 37.736 37.792 1.00 32.86 C ANISOU 3210 CZ PHE B 85 3751 4379 4354 140 504 -88 C ATOM 3211 N MET B 86 -27.485 38.462 40.738 1.00 18.56 N ANISOU 3211 N MET B 86 2191 2288 2574 72 548 -88 N ATOM 3212 CA MET B 86 -26.453 38.461 41.770 1.00 30.61 C ANISOU 3212 CA MET B 86 3753 3773 4106 57 558 -102 C ATOM 3213 C MET B 86 -26.168 39.873 42.265 1.00 25.80 C ANISOU 3213 C MET B 86 3162 3125 3515 84 571 -96 C ATOM 3214 O MET B 86 -26.093 40.116 43.475 1.00 25.29 O ANISOU 3214 O MET B 86 3113 3039 3457 84 584 -114 O ATOM 3215 CB MET B 86 -25.172 37.813 41.239 1.00 18.04 C ANISOU 3215 CB MET B 86 2180 2169 2504 32 545 -103 C ATOM 3216 CG MET B 86 -25.247 36.302 41.089 1.00 28.00 C ANISOU 3216 CG MET B 86 3433 3455 3752 0 539 -116 C ATOM 3217 SD MET B 86 -23.709 35.586 40.470 1.00 36.88 S ANISOU 3217 SD MET B 86 4582 4564 4865 -25 527 -115 S ATOM 3218 CE MET B 86 -22.590 35.929 41.826 1.00 25.97 C ANISOU 3218 CE MET B 86 3236 3140 3490 -29 538 -126 C ATOM 3219 N VAL B 87 -26.021 40.823 41.339 1.00 26.33 N ANISOU 3219 N VAL B 87 3227 3184 3592 108 570 -72 N ATOM 3220 CA VAL B 87 -25.622 42.178 41.710 1.00 23.69 C ANISOU 3220 CA VAL B 87 2912 2805 3283 130 586 -68 C ATOM 3221 C VAL B 87 -26.715 42.862 42.523 1.00 29.50 C ANISOU 3221 C VAL B 87 3638 3540 4030 156 604 -72 C ATOM 3222 O VAL B 87 -26.450 43.442 43.583 1.00 23.26 O ANISOU 3222 O VAL B 87 2867 2715 3255 158 618 -93 O ATOM 3223 CB VAL B 87 -25.261 42.992 40.454 1.00 23.75 C ANISOU 3223 CB VAL B 87 2918 2803 3301 153 587 -34 C ATOM 3224 CG1 VAL B 87 -25.128 44.467 40.798 1.00 19.18 C ANISOU 3224 CG1 VAL B 87 2354 2176 2757 181 611 -27 C ATOM 3225 CG2 VAL B 87 -23.972 42.468 39.838 1.00 22.79 C ANISOU 3225 CG2 VAL B 87 2814 2672 3174 128 574 -32 C ATOM 3226 N PHE B 88 -27.958 42.803 42.049 1.00 31.47 N ANISOU 3226 N PHE B 88 3856 3830 4273 176 603 -56 N ATOM 3227 CA PHE B 88 -29.026 43.538 42.715 1.00 20.64 C ANISOU 3227 CA PHE B 88 2472 2457 2913 206 622 -56 C ATOM 3228 C PHE B 88 -29.692 42.738 43.827 1.00 24.41 C ANISOU 3228 C PHE B 88 2942 2953 3380 190 627 -81 C ATOM 3229 O PHE B 88 -30.046 43.306 44.865 1.00 22.24 O ANISOU 3229 O PHE B 88 2676 2660 3115 205 647 -94 O ATOM 3230 CB PHE B 88 -30.070 43.991 41.694 1.00 19.88 C ANISOU 3230 CB PHE B 88 2342 2397 2814 242 621 -24 C ATOM 3231 CG PHE B 88 -29.578 45.064 40.775 1.00 31.92 C ANISOU 3231 CG PHE B 88 3876 3898 4353 272 628 8 C ATOM 3232 CD1 PHE B 88 -29.501 46.376 41.206 1.00 31.81 C ANISOU 3232 CD1 PHE B 88 3880 3836 4370 301 656 16 C ATOM 3233 CD2 PHE B 88 -29.184 44.762 39.483 1.00 27.72 C ANISOU 3233 CD2 PHE B 88 3337 3390 3805 273 611 31 C ATOM 3234 CE1 PHE B 88 -29.043 47.370 40.364 1.00 42.24 C ANISOU 3234 CE1 PHE B 88 5210 5128 5709 330 669 49 C ATOM 3235 CE2 PHE B 88 -28.728 45.753 38.634 1.00 34.00 C ANISOU 3235 CE2 PHE B 88 4142 4162 4614 304 622 66 C ATOM 3236 CZ PHE B 88 -28.658 47.058 39.076 1.00 35.98 C ANISOU 3236 CZ PHE B 88 4410 4362 4900 333 653 77 C ATOM 3237 N GLY B 89 -29.868 41.433 43.639 1.00 22.14 N ANISOU 3237 N GLY B 89 2638 2700 3074 161 614 -89 N ATOM 3238 CA GLY B 89 -30.487 40.616 44.664 1.00 24.87 C ANISOU 3238 CA GLY B 89 2975 3060 3413 146 624 -109 C ATOM 3239 C GLY B 89 -29.581 40.315 45.840 1.00 28.68 C ANISOU 3239 C GLY B 89 3493 3512 3890 128 632 -132 C ATOM 3240 O GLY B 89 -30.008 40.407 46.995 1.00 24.82 O ANISOU 3240 O GLY B 89 3010 3018 3401 137 651 -145 O ATOM 3241 N GLY B 90 -28.328 39.956 45.567 1.00 23.64 N ANISOU 3241 N GLY B 90 2879 2857 3247 105 619 -136 N ATOM 3242 CA GLY B 90 -27.413 39.591 46.633 1.00 31.27 C ANISOU 3242 CA GLY B 90 3875 3802 4204 90 623 -158 C ATOM 3243 C GLY B 90 -26.361 40.614 47.015 1.00 22.27 C ANISOU 3243 C GLY B 90 2765 2622 3074 98 623 -170 C ATOM 3244 O GLY B 90 -26.126 40.846 48.205 1.00 19.71 O ANISOU 3244 O GLY B 90 2458 2285 2745 104 633 -193 O ATOM 3245 N PHE B 91 -25.720 41.239 46.023 1.00 24.23 N ANISOU 3245 N PHE B 91 3018 2853 3337 100 613 -157 N ATOM 3246 CA PHE B 91 -24.566 42.087 46.313 1.00 20.01 C ANISOU 3246 CA PHE B 91 2509 2277 2818 99 613 -172 C ATOM 3247 C PHE B 91 -24.957 43.340 47.087 1.00 21.97 C ANISOU 3247 C PHE B 91 2763 2498 3086 126 632 -186 C ATOM 3248 O PHE B 91 -24.150 43.859 47.868 1.00 22.51 O ANISOU 3248 O PHE B 91 2852 2538 3163 123 635 -216 O ATOM 3249 CB PHE B 91 -23.845 42.473 45.022 1.00 20.97 C ANISOU 3249 CB PHE B 91 2631 2383 2954 96 604 -149 C ATOM 3250 CG PHE B 91 -23.011 41.371 44.432 1.00 19.57 C ANISOU 3250 CG PHE B 91 2457 2219 2759 68 586 -144 C ATOM 3251 CD1 PHE B 91 -23.047 40.088 44.953 1.00 18.03 C ANISOU 3251 CD1 PHE B 91 2261 2049 2538 47 580 -156 C ATOM 3252 CD2 PHE B 91 -22.180 41.628 43.357 1.00 18.16 C ANISOU 3252 CD2 PHE B 91 2283 2027 2592 64 578 -126 C ATOM 3253 CE1 PHE B 91 -22.272 39.082 44.411 1.00 18.30 C ANISOU 3253 CE1 PHE B 91 2300 2093 2559 22 566 -152 C ATOM 3254 CE2 PHE B 91 -21.404 40.626 42.807 1.00 23.41 C ANISOU 3254 CE2 PHE B 91 2951 2704 3239 39 563 -122 C ATOM 3255 CZ PHE B 91 -21.451 39.350 43.333 1.00 21.20 C ANISOU 3255 CZ PHE B 91 2672 2448 2935 18 557 -136 C ATOM 3256 N THR B 92 -26.176 43.844 46.883 1.00 20.45 N ANISOU 3256 N THR B 92 2552 2317 2902 153 645 -170 N ATOM 3257 CA THR B 92 -26.632 45.003 47.644 1.00 19.51 C ANISOU 3257 CA THR B 92 2439 2171 2802 181 667 -184 C ATOM 3258 C THR B 92 -26.665 44.700 49.138 1.00 19.53 C ANISOU 3258 C THR B 92 2455 2180 2787 178 674 -220 C ATOM 3259 O THR B 92 -26.330 45.559 49.963 1.00 21.45 O ANISOU 3259 O THR B 92 2716 2393 3043 188 685 -250 O ATOM 3260 CB THR B 92 -28.012 45.447 47.156 1.00 27.02 C ANISOU 3260 CB THR B 92 3365 3141 3762 213 680 -155 C ATOM 3261 OG1 THR B 92 -28.899 44.320 47.131 1.00 19.66 O ANISOU 3261 OG1 THR B 92 2408 2258 2805 205 673 -147 O ATOM 3262 CG2 THR B 92 -27.921 46.055 45.762 1.00 23.48 C ANISOU 3262 CG2 THR B 92 2907 2684 3332 228 678 -119 C ATOM 3263 N THR B 93 -27.074 43.482 49.506 1.00 19.36 N ANISOU 3263 N THR B 93 2424 2196 2737 166 669 -218 N ATOM 3264 CA THR B 93 -26.996 43.063 50.901 1.00 30.50 C ANISOU 3264 CA THR B 93 3849 3616 4124 165 677 -247 C ATOM 3265 C THR B 93 -25.547 42.962 51.367 1.00 24.61 C ANISOU 3265 C THR B 93 3129 2854 3369 147 663 -275 C ATOM 3266 O THR B 93 -25.220 43.379 52.484 1.00 23.33 O ANISOU 3266 O THR B 93 2983 2683 3198 156 669 -309 O ATOM 3267 CB THR B 93 -27.720 41.727 51.094 1.00 26.87 C ANISOU 3267 CB THR B 93 3373 3197 3640 156 681 -233 C ATOM 3268 OG1 THR B 93 -29.118 41.895 50.826 1.00 23.18 O ANISOU 3268 OG1 THR B 93 2878 2747 3183 174 695 -214 O ATOM 3269 CG2 THR B 93 -27.543 41.216 52.522 1.00 22.15 C ANISOU 3269 CG2 THR B 93 2792 2611 3015 159 692 -256 C ATOM 3270 N THR B 94 -24.663 42.425 50.517 1.00 20.15 N ANISOU 3270 N THR B 94 2565 2286 2804 121 644 -263 N ATOM 3271 CA THR B 94 -23.254 42.288 50.883 1.00 24.53 C ANISOU 3271 CA THR B 94 3139 2829 3351 103 630 -288 C ATOM 3272 C THR B 94 -22.635 43.638 51.213 1.00 22.54 C ANISOU 3272 C THR B 94 2900 2538 3125 111 632 -319 C ATOM 3273 O THR B 94 -21.911 43.774 52.206 1.00 19.54 O ANISOU 3273 O THR B 94 2534 2156 2734 110 628 -357 O ATOM 3274 CB THR B 94 -22.472 41.630 49.743 1.00 24.13 C ANISOU 3274 CB THR B 94 3087 2780 3303 78 612 -265 C ATOM 3275 OG1 THR B 94 -23.301 40.675 49.068 1.00 30.57 O ANISOU 3275 OG1 THR B 94 3884 3624 4108 72 612 -235 O ATOM 3276 CG2 THR B 94 -21.224 40.932 50.277 1.00 24.06 C ANISOU 3276 CG2 THR B 94 3092 2776 3272 59 598 -284 C ATOM 3277 N LEU B 95 -22.910 44.648 50.384 1.00 25.50 N ANISOU 3277 N LEU B 95 3268 2883 3537 121 641 -303 N ATOM 3278 CA LEU B 95 -22.350 45.978 50.599 1.00 25.74 C ANISOU 3278 CA LEU B 95 3310 2868 3604 127 650 -331 C ATOM 3279 C LEU B 95 -22.889 46.602 51.879 1.00 19.92 C ANISOU 3279 C LEU B 95 2579 2126 2862 149 665 -369 C ATOM 3280 O LEU B 95 -22.125 47.148 52.684 1.00 21.78 O ANISOU 3280 O LEU B 95 2828 2342 3104 145 664 -416 O ATOM 3281 CB LEU B 95 -22.660 46.867 49.395 1.00 23.87 C ANISOU 3281 CB LEU B 95 3064 2599 3407 139 663 -297 C ATOM 3282 CG LEU B 95 -22.326 48.353 49.519 1.00 29.73 C ANISOU 3282 CG LEU B 95 3815 3284 4197 150 683 -319 C ATOM 3283 CD1 LEU B 95 -20.823 48.562 49.616 1.00 35.66 C ANISOU 3283 CD1 LEU B 95 4576 4005 4966 121 672 -351 C ATOM 3284 CD2 LEU B 95 -22.899 49.107 48.342 1.00 37.11 C ANISOU 3284 CD2 LEU B 95 4740 4196 5165 172 702 -273 C ATOM 3285 N TYR B 96 -24.208 46.538 52.078 1.00 34.81 N ANISOU 3285 N TYR B 96 4456 4032 4739 173 681 -351 N ATOM 3286 CA TYR B 96 -24.803 47.064 53.302 1.00 22.00 C ANISOU 3286 CA TYR B 96 2841 2410 3109 198 698 -384 C ATOM 3287 C TYR B 96 -24.291 46.312 54.521 1.00 26.24 C ANISOU 3287 C TYR B 96 3389 2978 3602 191 687 -420 C ATOM 3288 O TYR B 96 -24.003 46.917 55.561 1.00 21.73 O ANISOU 3288 O TYR B 96 2831 2399 3026 202 692 -467 O ATOM 3289 CB TYR B 96 -26.328 46.983 53.220 1.00 25.61 C ANISOU 3289 CB TYR B 96 3281 2888 3560 224 717 -353 C ATOM 3290 CG TYR B 96 -27.049 47.826 54.249 1.00 38.77 C ANISOU 3290 CG TYR B 96 4954 4546 5231 256 741 -381 C ATOM 3291 CD1 TYR B 96 -27.210 49.193 54.064 1.00 32.11 C ANISOU 3291 CD1 TYR B 96 4114 3656 4429 274 761 -390 C ATOM 3292 CD2 TYR B 96 -27.571 47.255 55.405 1.00 43.95 C ANISOU 3292 CD2 TYR B 96 5612 5237 5848 269 749 -396 C ATOM 3293 CE1 TYR B 96 -27.869 49.968 55.003 1.00 45.18 C ANISOU 3293 CE1 TYR B 96 5777 5301 6089 304 785 -417 C ATOM 3294 CE2 TYR B 96 -28.232 48.021 56.350 1.00 39.67 C ANISOU 3294 CE2 TYR B 96 5078 4689 5307 300 772 -423 C ATOM 3295 CZ TYR B 96 -28.377 49.375 56.145 1.00 37.55 C ANISOU 3295 CZ TYR B 96 4813 4374 5081 317 789 -435 C ATOM 3296 OH TYR B 96 -29.036 50.133 57.086 1.00 43.23 O ANISOU 3296 OH TYR B 96 5540 5085 5801 349 814 -463 O ATOM 3297 N THR B 97 -24.170 44.987 54.408 1.00 23.91 N ANISOU 3297 N THR B 97 3090 2720 3274 176 674 -397 N ATOM 3298 CA THR B 97 -23.631 44.185 55.501 1.00 19.95 C ANISOU 3298 CA THR B 97 2600 2251 2728 175 666 -422 C ATOM 3299 C THR B 97 -22.194 44.580 55.818 1.00 26.17 C ANISOU 3299 C THR B 97 3400 3024 3518 160 646 -464 C ATOM 3300 O THR B 97 -21.828 44.755 56.986 1.00 28.57 O ANISOU 3300 O THR B 97 3715 3342 3797 172 644 -508 O ATOM 3301 CB THR B 97 -23.705 42.699 55.145 1.00 22.97 C ANISOU 3301 CB THR B 97 2975 2667 3084 160 660 -384 C ATOM 3302 OG1 THR B 97 -25.035 42.367 54.722 1.00 19.56 O ANISOU 3302 OG1 THR B 97 2525 2248 2658 168 677 -348 O ATOM 3303 CG2 THR B 97 -23.328 41.845 56.343 1.00 19.63 C ANISOU 3303 CG2 THR B 97 2564 2280 2613 167 660 -401 C ATOM 3304 N SER B 98 -21.363 44.727 54.783 1.00 19.98 N ANISOU 3304 N SER B 98 2613 2214 2764 134 632 -454 N ATOM 3305 CA SER B 98 -19.962 45.075 54.999 1.00 19.91 C ANISOU 3305 CA SER B 98 2612 2191 2763 116 614 -493 C ATOM 3306 C SER B 98 -19.811 46.469 55.593 1.00 20.40 C ANISOU 3306 C SER B 98 2679 2217 2854 126 622 -546 C ATOM 3307 O SER B 98 -18.893 46.707 56.386 1.00 20.67 O ANISOU 3307 O SER B 98 2718 2256 2880 120 608 -598 O ATOM 3308 CB SER B 98 -19.181 44.972 53.687 1.00 23.22 C ANISOU 3308 CB SER B 98 3024 2586 3211 89 602 -466 C ATOM 3309 OG SER B 98 -19.189 43.649 53.177 1.00 23.72 O ANISOU 3309 OG SER B 98 3084 2681 3247 78 593 -425 O ATOM 3310 N LEU B 99 -20.693 47.401 55.220 1.00 23.57 N ANISOU 3310 N LEU B 99 3078 2584 3292 141 646 -534 N ATOM 3311 CA LEU B 99 -20.595 48.765 55.729 1.00 21.07 C ANISOU 3311 CA LEU B 99 2767 2227 3012 150 660 -584 C ATOM 3312 C LEU B 99 -20.757 48.806 57.243 1.00 23.34 C ANISOU 3312 C LEU B 99 3064 2545 3261 170 659 -637 C ATOM 3313 O LEU B 99 -20.046 49.548 57.931 1.00 34.39 O ANISOU 3313 O LEU B 99 4468 3927 4671 165 654 -700 O ATOM 3314 CB LEU B 99 -21.640 49.656 55.058 1.00 22.81 C ANISOU 3314 CB LEU B 99 2984 2408 3274 169 689 -553 C ATOM 3315 CG LEU B 99 -21.335 50.091 53.625 1.00 27.40 C ANISOU 3315 CG LEU B 99 3558 2948 3905 156 695 -513 C ATOM 3316 CD1 LEU B 99 -22.573 50.673 52.962 1.00 36.98 C ANISOU 3316 CD1 LEU B 99 4764 4143 5142 185 723 -469 C ATOM 3317 CD2 LEU B 99 -20.201 51.099 53.615 1.00 29.13 C ANISOU 3317 CD2 LEU B 99 3782 3113 4174 136 698 -556 C ATOM 3318 N HIS B 100 -21.688 48.018 57.780 1.00 23.14 N ANISOU 3318 N HIS B 100 3039 2564 3189 192 666 -615 N ATOM 3319 CA HIS B 100 -21.939 47.984 59.214 1.00 25.85 C ANISOU 3319 CA HIS B 100 3392 2942 3488 218 670 -658 C ATOM 3320 C HIS B 100 -21.164 46.892 59.939 1.00 28.23 C ANISOU 3320 C HIS B 100 3697 3297 3731 215 646 -670 C ATOM 3321 O HIS B 100 -21.105 46.913 61.174 1.00 26.37 O ANISOU 3321 O HIS B 100 3470 3094 3454 238 645 -713 O ATOM 3322 CB HIS B 100 -23.435 47.804 59.480 1.00 27.92 C ANISOU 3322 CB HIS B 100 3653 3222 3734 250 696 -625 C ATOM 3323 CG HIS B 100 -24.279 48.907 58.930 1.00 26.48 C ANISOU 3323 CG HIS B 100 3466 2993 3603 262 722 -614 C ATOM 3324 ND1 HIS B 100 -24.632 50.014 59.671 1.00 29.84 N ANISOU 3324 ND1 HIS B 100 3901 3395 4043 286 741 -659 N ATOM 3325 CD2 HIS B 100 -24.833 49.081 57.707 1.00 21.67 C ANISOU 3325 CD2 HIS B 100 2844 2357 3031 258 732 -562 C ATOM 3326 CE1 HIS B 100 -25.372 50.820 58.930 1.00 29.39 C ANISOU 3326 CE1 HIS B 100 3838 3296 4033 296 765 -632 C ATOM 3327 NE2 HIS B 100 -25.511 50.276 57.735 1.00 39.40 N ANISOU 3327 NE2 HIS B 100 5092 4565 5314 281 759 -573 N ATOM 3328 N GLY B 101 -20.567 45.950 59.214 1.00 27.24 N ANISOU 3328 N GLY B 101 3566 3184 3599 191 629 -634 N ATOM 3329 CA GLY B 101 -19.820 44.885 59.848 1.00 20.97 C ANISOU 3329 CA GLY B 101 2776 2439 2752 192 610 -639 C ATOM 3330 C GLY B 101 -20.655 43.767 60.426 1.00 25.25 C ANISOU 3330 C GLY B 101 3322 3029 3244 216 626 -603 C ATOM 3331 O GLY B 101 -20.140 42.984 61.228 1.00 20.92 O ANISOU 3331 O GLY B 101 2779 2525 2644 228 617 -611 O ATOM 3332 N TYR B 102 -21.929 43.667 60.047 1.00 20.76 N ANISOU 3332 N TYR B 102 2748 2452 2689 226 650 -562 N ATOM 3333 CA TYR B 102 -22.792 42.574 60.483 1.00 31.66 C ANISOU 3333 CA TYR B 102 4128 3871 4032 245 671 -523 C ATOM 3334 C TYR B 102 -24.091 42.648 59.692 1.00 22.25 C ANISOU 3334 C TYR B 102 2922 2660 2873 244 693 -481 C ATOM 3335 O TYR B 102 -24.385 43.651 59.036 1.00 28.02 O ANISOU 3335 O TYR B 102 3646 3352 3647 240 695 -485 O ATOM 3336 CB TYR B 102 -23.056 42.616 61.993 1.00 25.86 C ANISOU 3336 CB TYR B 102 3404 3174 3247 284 683 -555 C ATOM 3337 CG TYR B 102 -24.119 43.595 62.434 1.00 32.49 C ANISOU 3337 CG TYR B 102 4245 4000 4100 310 707 -572 C ATOM 3338 CD1 TYR B 102 -23.871 44.963 62.460 1.00 22.70 C ANISOU 3338 CD1 TYR B 102 3008 2724 2892 310 701 -622 C ATOM 3339 CD2 TYR B 102 -25.366 43.145 62.844 1.00 24.80 C ANISOU 3339 CD2 TYR B 102 3266 3046 3109 336 739 -540 C ATOM 3340 CE1 TYR B 102 -24.846 45.857 62.871 1.00 35.12 C ANISOU 3340 CE1 TYR B 102 4583 4283 4478 336 725 -638 C ATOM 3341 CE2 TYR B 102 -26.342 44.024 63.255 1.00 29.55 C ANISOU 3341 CE2 TYR B 102 3869 3638 3722 362 762 -554 C ATOM 3342 CZ TYR B 102 -26.080 45.381 63.269 1.00 32.90 C ANISOU 3342 CZ TYR B 102 4298 4026 4176 363 755 -603 C ATOM 3343 OH TYR B 102 -27.057 46.261 63.680 1.00 35.01 O ANISOU 3343 OH TYR B 102 4566 4280 4455 392 780 -617 O ATOM 3344 N PHE B 103 -24.864 41.563 59.755 1.00 20.42 N ANISOU 3344 N PHE B 103 2683 2455 2622 250 711 -439 N ATOM 3345 CA PHE B 103 -26.086 41.430 58.963 1.00 25.76 C ANISOU 3345 CA PHE B 103 3339 3122 3327 246 729 -398 C ATOM 3346 C PHE B 103 -27.214 42.184 59.653 1.00 32.19 C ANISOU 3346 C PHE B 103 4150 3936 4142 280 756 -408 C ATOM 3347 O PHE B 103 -27.976 41.632 60.447 1.00 32.67 O ANISOU 3347 O PHE B 103 4209 4026 4176 302 781 -396 O ATOM 3348 CB PHE B 103 -26.431 39.962 58.747 1.00 24.78 C ANISOU 3348 CB PHE B 103 3205 3022 3188 235 740 -355 C ATOM 3349 CG PHE B 103 -25.777 39.375 57.536 1.00 21.10 C ANISOU 3349 CG PHE B 103 2732 2544 2740 198 719 -334 C ATOM 3350 CD1 PHE B 103 -26.354 39.526 56.287 1.00 23.11 C ANISOU 3350 CD1 PHE B 103 2967 2782 3033 181 716 -310 C ATOM 3351 CD2 PHE B 103 -24.576 38.693 57.637 1.00 20.26 C ANISOU 3351 CD2 PHE B 103 2639 2446 2611 185 703 -339 C ATOM 3352 CE1 PHE B 103 -25.755 39.001 55.161 1.00 24.31 C ANISOU 3352 CE1 PHE B 103 3114 2926 3198 150 697 -292 C ATOM 3353 CE2 PHE B 103 -23.969 38.164 56.514 1.00 24.92 C ANISOU 3353 CE2 PHE B 103 3224 3025 3219 153 685 -320 C ATOM 3354 CZ PHE B 103 -24.560 38.317 55.274 1.00 26.20 C ANISOU 3354 CZ PHE B 103 3368 3170 3418 135 682 -297 C ATOM 3355 N VAL B 104 -27.309 43.478 59.330 1.00 30.16 N ANISOU 3355 N VAL B 104 3894 3645 3919 284 753 -430 N ATOM 3356 CA VAL B 104 -28.371 44.322 59.869 1.00 23.54 C ANISOU 3356 CA VAL B 104 3053 2802 3089 317 779 -440 C ATOM 3357 C VAL B 104 -29.736 43.754 59.506 1.00 32.77 C ANISOU 3357 C VAL B 104 4198 3988 4266 324 802 -392 C ATOM 3358 O VAL B 104 -30.668 43.765 60.319 1.00 39.86 O ANISOU 3358 O VAL B 104 5093 4905 5149 353 830 -391 O ATOM 3359 CB VAL B 104 -28.205 45.765 59.358 1.00 33.49 C ANISOU 3359 CB VAL B 104 4316 4014 4394 318 775 -463 C ATOM 3360 CG1 VAL B 104 -29.199 46.696 60.035 1.00 33.25 C ANISOU 3360 CG1 VAL B 104 4286 3976 4370 355 804 -480 C ATOM 3361 CG2 VAL B 104 -26.778 46.240 59.574 1.00 28.61 C ANISOU 3361 CG2 VAL B 104 3716 3377 3777 302 751 -511 C ATOM 3362 N PHE B 105 -29.874 43.248 58.278 1.00 30.15 N ANISOU 3362 N PHE B 105 3846 3652 3958 298 792 -355 N ATOM 3363 CA PHE B 105 -31.113 42.637 57.811 1.00 37.65 C ANISOU 3363 CA PHE B 105 4767 4621 4918 298 809 -315 C ATOM 3364 C PHE B 105 -31.431 41.319 58.505 1.00 29.47 C ANISOU 3364 C PHE B 105 3727 3620 3852 297 827 -298 C ATOM 3365 O PHE B 105 -32.443 40.697 58.166 1.00 29.33 O ANISOU 3365 O PHE B 105 3681 3618 3845 293 844 -268 O ATOM 3366 CB PHE B 105 -31.051 42.394 56.301 1.00 35.91 C ANISOU 3366 CB PHE B 105 4526 4392 4727 269 789 -286 C ATOM 3367 CG PHE B 105 -30.793 43.628 55.489 1.00 46.78 C ANISOU 3367 CG PHE B 105 5904 5734 6136 273 777 -292 C ATOM 3368 CD1 PHE B 105 -31.208 44.874 55.931 1.00 41.50 C ANISOU 3368 CD1 PHE B 105 5242 5044 5482 304 793 -310 C ATOM 3369 CD2 PHE B 105 -30.142 43.534 54.269 1.00 50.05 C ANISOU 3369 CD2 PHE B 105 6314 6136 6567 247 753 -277 C ATOM 3370 CE1 PHE B 105 -30.968 46.005 55.175 1.00 54.52 C ANISOU 3370 CE1 PHE B 105 6892 6656 7166 309 788 -310 C ATOM 3371 CE2 PHE B 105 -29.902 44.656 53.505 1.00 49.43 C ANISOU 3371 CE2 PHE B 105 6237 6024 6520 254 747 -276 C ATOM 3372 CZ PHE B 105 -30.317 45.895 53.956 1.00 48.02 C ANISOU 3372 CZ PHE B 105 6065 5821 6360 285 766 -291 C ATOM 3373 N GLY B 106 -30.602 40.869 59.444 1.00 30.14 N ANISOU 3373 N GLY B 106 3836 3717 3899 302 826 -317 N ATOM 3374 CA GLY B 106 -30.824 39.611 60.111 1.00 29.47 C ANISOU 3374 CA GLY B 106 3751 3662 3785 304 848 -296 C ATOM 3375 C GLY B 106 -30.693 38.439 59.161 1.00 25.58 C ANISOU 3375 C GLY B 106 3242 3171 3307 267 841 -264 C ATOM 3376 O GLY B 106 -30.071 38.538 58.098 1.00 21.73 O ANISOU 3376 O GLY B 106 2752 2666 2839 240 812 -264 O ATOM 3377 N PRO B 107 -31.280 37.298 59.531 1.00 23.16 N ANISOU 3377 N PRO B 107 2925 2884 2992 267 870 -237 N ATOM 3378 CA PRO B 107 -31.156 36.101 58.682 1.00 29.82 C ANISOU 3378 CA PRO B 107 3753 3726 3850 230 868 -211 C ATOM 3379 C PRO B 107 -31.750 36.260 57.289 1.00 25.35 C ANISOU 3379 C PRO B 107 3155 3150 3326 203 852 -201 C ATOM 3380 O PRO B 107 -31.357 35.516 56.382 1.00 22.22 O ANISOU 3380 O PRO B 107 2751 2750 2943 170 838 -190 O ATOM 3381 CB PRO B 107 -31.896 35.024 59.489 1.00 26.45 C ANISOU 3381 CB PRO B 107 3318 3318 3413 240 913 -186 C ATOM 3382 CG PRO B 107 -31.840 35.499 60.897 1.00 23.64 C ANISOU 3382 CG PRO B 107 2986 2978 3018 285 931 -200 C ATOM 3383 CD PRO B 107 -31.933 36.997 60.817 1.00 32.69 C ANISOU 3383 CD PRO B 107 4135 4113 4171 301 910 -230 C ATOM 3384 N THR B 108 -32.692 37.188 57.091 1.00 29.72 N ANISOU 3384 N THR B 108 3689 3703 3900 219 856 -203 N ATOM 3385 CA THR B 108 -33.270 37.380 55.763 1.00 20.91 C ANISOU 3385 CA THR B 108 2541 2586 2818 200 839 -192 C ATOM 3386 C THR B 108 -32.240 37.931 54.785 1.00 26.15 C ANISOU 3386 C THR B 108 3217 3229 3488 185 800 -201 C ATOM 3387 O THR B 108 -32.175 37.492 53.630 1.00 25.56 O ANISOU 3387 O THR B 108 3125 3157 3430 158 782 -190 O ATOM 3388 CB THR B 108 -34.487 38.303 55.844 1.00 23.02 C ANISOU 3388 CB THR B 108 2784 2859 3102 228 854 -189 C ATOM 3389 OG1 THR B 108 -35.514 37.671 56.619 1.00 20.97 O ANISOU 3389 OG1 THR B 108 2507 2620 2842 238 892 -176 O ATOM 3390 CG2 THR B 108 -35.024 38.607 54.452 1.00 40.54 C ANISOU 3390 CG2 THR B 108 4970 5082 5351 216 833 -177 C ATOM 3391 N GLY B 109 -31.422 38.889 55.226 1.00 30.45 N ANISOU 3391 N GLY B 109 3792 3755 4022 201 789 -224 N ATOM 3392 CA GLY B 109 -30.340 39.366 54.379 1.00 27.38 C ANISOU 3392 CA GLY B 109 3417 3344 3642 185 757 -232 C ATOM 3393 C GLY B 109 -29.329 38.279 54.070 1.00 27.96 C ANISOU 3393 C GLY B 109 3501 3419 3702 155 742 -228 C ATOM 3394 O GLY B 109 -28.790 38.211 52.962 1.00 19.17 O ANISOU 3394 O GLY B 109 2384 2298 2602 133 719 -221 O ATOM 3395 N CYS B 110 -29.052 37.419 55.053 1.00 19.77 N ANISOU 3395 N CYS B 110 2479 2396 2638 157 758 -230 N ATOM 3396 CA CYS B 110 -28.172 36.279 54.825 1.00 19.17 C ANISOU 3396 CA CYS B 110 2412 2322 2550 131 750 -222 C ATOM 3397 C CYS B 110 -28.749 35.342 53.775 1.00 24.34 C ANISOU 3397 C CYS B 110 3039 2983 3226 102 752 -199 C ATOM 3398 O CYS B 110 -28.017 34.827 52.922 1.00 18.79 O ANISOU 3398 O CYS B 110 2338 2274 2527 76 733 -194 O ATOM 3399 CB CYS B 110 -27.943 35.540 56.141 1.00 19.30 C ANISOU 3399 CB CYS B 110 2447 2355 2533 147 774 -222 C ATOM 3400 SG CYS B 110 -26.873 34.090 56.055 1.00 19.07 S ANISOU 3400 SG CYS B 110 2431 2329 2485 125 772 -208 S ATOM 3401 N ASN B 111 -30.062 35.100 53.828 1.00 19.26 N ANISOU 3401 N ASN B 111 2367 2354 2597 106 775 -187 N ATOM 3402 CA ASN B 111 -30.706 34.281 52.805 1.00 23.83 C ANISOU 3402 CA ASN B 111 2914 2942 3200 78 775 -173 C ATOM 3403 C ASN B 111 -30.579 34.922 51.430 1.00 21.16 C ANISOU 3403 C ASN B 111 2562 2601 2878 67 742 -174 C ATOM 3404 O ASN B 111 -30.303 34.235 50.441 1.00 23.28 O ANISOU 3404 O ASN B 111 2820 2872 3154 39 727 -170 O ATOM 3405 CB ASN B 111 -32.176 34.051 53.156 1.00 19.55 C ANISOU 3405 CB ASN B 111 2338 2417 2673 85 806 -164 C ATOM 3406 CG ASN B 111 -32.361 33.011 54.245 1.00 21.16 C ANISOU 3406 CG ASN B 111 2549 2625 2868 87 846 -154 C ATOM 3407 OD1 ASN B 111 -31.516 32.136 54.438 1.00 25.48 O ANISOU 3407 OD1 ASN B 111 3117 3164 3402 74 851 -150 O ATOM 3408 ND2 ASN B 111 -33.481 33.094 54.956 1.00 25.80 N ANISOU 3408 ND2 ASN B 111 3118 3224 3462 106 879 -147 N ATOM 3409 N LEU B 112 -30.773 36.240 51.348 1.00 27.09 N ANISOU 3409 N LEU B 112 3313 3345 3634 92 732 -179 N ATOM 3410 CA LEU B 112 -30.628 36.936 50.073 1.00 25.82 C ANISOU 3410 CA LEU B 112 3142 3181 3487 90 704 -175 C ATOM 3411 C LEU B 112 -29.203 36.826 49.546 1.00 23.70 C ANISOU 3411 C LEU B 112 2900 2894 3211 72 681 -178 C ATOM 3412 O LEU B 112 -28.984 36.474 48.381 1.00 21.21 O ANISOU 3412 O LEU B 112 2573 2585 2902 53 662 -170 O ATOM 3413 CB LEU B 112 -31.030 38.402 50.232 1.00 19.31 C ANISOU 3413 CB LEU B 112 2319 2346 2672 124 706 -176 C ATOM 3414 CG LEU B 112 -32.509 38.684 50.491 1.00 25.68 C ANISOU 3414 CG LEU B 112 3093 3173 3490 146 727 -169 C ATOM 3415 CD1 LEU B 112 -32.699 40.111 50.982 1.00 20.00 C ANISOU 3415 CD1 LEU B 112 2386 2435 2776 183 736 -174 C ATOM 3416 CD2 LEU B 112 -33.307 38.439 49.227 1.00 19.72 C ANISOU 3416 CD2 LEU B 112 2297 2446 2750 137 714 -154 C ATOM 3417 N GLU B 113 -28.217 37.115 50.400 1.00 21.63 N ANISOU 3417 N GLU B 113 2671 2612 2934 78 681 -192 N ATOM 3418 CA GLU B 113 -26.825 37.120 49.961 1.00 18.45 C ANISOU 3418 CA GLU B 113 2291 2192 2527 63 659 -198 C ATOM 3419 C GLU B 113 -26.377 35.737 49.502 1.00 23.07 C ANISOU 3419 C GLU B 113 2875 2787 3104 33 655 -189 C ATOM 3420 O GLU B 113 -25.739 35.601 48.452 1.00 18.04 O ANISOU 3420 O GLU B 113 2238 2144 2472 16 635 -183 O ATOM 3421 CB GLU B 113 -25.930 37.630 51.094 1.00 25.20 C ANISOU 3421 CB GLU B 113 3177 3032 3368 76 660 -220 C ATOM 3422 CG GLU B 113 -24.685 38.378 50.636 1.00 27.51 C ANISOU 3422 CG GLU B 113 3486 3298 3668 70 638 -231 C ATOM 3423 CD GLU B 113 -23.626 37.468 50.036 1.00 28.67 C ANISOU 3423 CD GLU B 113 3641 3447 3807 44 623 -224 C ATOM 3424 OE1 GLU B 113 -23.528 36.300 50.468 1.00 24.83 O ANISOU 3424 OE1 GLU B 113 3158 2976 3301 34 631 -219 O ATOM 3425 OE2 GLU B 113 -22.891 37.923 49.130 1.00 25.35 O ANISOU 3425 OE2 GLU B 113 3222 3008 3400 34 606 -220 O ATOM 3426 N GLY B 114 -26.705 34.697 50.271 1.00 20.75 N ANISOU 3426 N GLY B 114 2581 2505 2799 28 677 -187 N ATOM 3427 CA GLY B 114 -26.268 33.358 49.909 1.00 20.39 C ANISOU 3427 CA GLY B 114 2535 2462 2748 1 679 -179 C ATOM 3428 C GLY B 114 -27.007 32.782 48.714 1.00 18.13 C ANISOU 3428 C GLY B 114 2218 2188 2481 -22 674 -172 C ATOM 3429 O GLY B 114 -26.394 32.175 47.831 1.00 17.95 O ANISOU 3429 O GLY B 114 2196 2163 2460 -45 660 -170 O ATOM 3430 N PHE B 115 -28.330 32.958 48.671 1.00 23.08 N ANISOU 3430 N PHE B 115 2814 2832 3123 -15 686 -170 N ATOM 3431 CA PHE B 115 -29.139 32.305 47.644 1.00 23.30 C ANISOU 3431 CA PHE B 115 2805 2878 3168 -38 682 -169 C ATOM 3432 C PHE B 115 -28.813 32.831 46.251 1.00 18.36 C ANISOU 3432 C PHE B 115 2172 2260 2544 -41 648 -168 C ATOM 3433 O PHE B 115 -28.630 32.049 45.312 1.00 19.45 O ANISOU 3433 O PHE B 115 2299 2406 2684 -66 637 -172 O ATOM 3434 CB PHE B 115 -30.624 32.488 47.960 1.00 23.66 C ANISOU 3434 CB PHE B 115 2817 2945 3229 -26 701 -169 C ATOM 3435 CG PHE B 115 -31.540 32.156 46.816 1.00 23.41 C ANISOU 3435 CG PHE B 115 2740 2941 3215 -43 689 -173 C ATOM 3436 CD1 PHE B 115 -31.833 30.839 46.502 1.00 26.45 C ANISOU 3436 CD1 PHE B 115 3104 3332 3613 -78 700 -182 C ATOM 3437 CD2 PHE B 115 -32.124 33.165 46.066 1.00 21.57 C ANISOU 3437 CD2 PHE B 115 2483 2728 2985 -23 669 -170 C ATOM 3438 CE1 PHE B 115 -32.681 30.535 45.454 1.00 19.28 C ANISOU 3438 CE1 PHE B 115 2150 2454 2720 -94 687 -194 C ATOM 3439 CE2 PHE B 115 -32.971 32.865 45.018 1.00 20.22 C ANISOU 3439 CE2 PHE B 115 2268 2592 2825 -34 655 -176 C ATOM 3440 CZ PHE B 115 -33.251 31.549 44.714 1.00 19.41 C ANISOU 3440 CZ PHE B 115 2142 2499 2734 -72 662 -191 C ATOM 3441 N PHE B 116 -28.734 34.155 46.096 1.00 18.38 N ANISOU 3441 N PHE B 116 2180 2257 2545 -14 635 -163 N ATOM 3442 CA PHE B 116 -28.496 34.719 44.770 1.00 24.50 C ANISOU 3442 CA PHE B 116 2948 3041 3322 -10 608 -156 C ATOM 3443 C PHE B 116 -27.085 34.427 44.272 1.00 19.82 C ANISOU 3443 C PHE B 116 2382 2429 2719 -26 593 -155 C ATOM 3444 O PHE B 116 -26.884 34.253 43.064 1.00 19.75 O ANISOU 3444 O PHE B 116 2364 2434 2708 -35 574 -150 O ATOM 3445 CB PHE B 116 -28.767 36.224 44.778 1.00 31.55 C ANISOU 3445 CB PHE B 116 3841 3926 4221 26 606 -146 C ATOM 3446 CG PHE B 116 -30.223 36.575 44.649 1.00 27.10 C ANISOU 3446 CG PHE B 116 3239 3391 3666 44 612 -141 C ATOM 3447 CD1 PHE B 116 -30.878 36.420 43.438 1.00 24.98 C ANISOU 3447 CD1 PHE B 116 2935 3159 3399 44 596 -135 C ATOM 3448 CD2 PHE B 116 -30.935 37.057 45.736 1.00 28.69 C ANISOU 3448 CD2 PHE B 116 3439 3588 3874 65 635 -144 C ATOM 3449 CE1 PHE B 116 -32.215 36.738 43.310 1.00 26.24 C ANISOU 3449 CE1 PHE B 116 3054 3350 3566 63 600 -131 C ATOM 3450 CE2 PHE B 116 -32.275 37.378 45.616 1.00 25.31 C ANISOU 3450 CE2 PHE B 116 2974 3188 3456 83 642 -138 C ATOM 3451 CZ PHE B 116 -32.916 37.219 44.400 1.00 37.69 C ANISOU 3451 CZ PHE B 116 4503 4792 5025 82 624 -131 C ATOM 3452 N ALA B 117 -26.100 34.371 45.172 1.00 17.87 N ANISOU 3452 N ALA B 117 2168 2156 2465 -28 600 -160 N ATOM 3453 CA ALA B 117 -24.752 33.997 44.759 1.00 17.61 C ANISOU 3453 CA ALA B 117 2159 2108 2424 -44 587 -159 C ATOM 3454 C ALA B 117 -24.647 32.503 44.487 1.00 20.98 C ANISOU 3454 C ALA B 117 2582 2545 2846 -74 592 -162 C ATOM 3455 O ALA B 117 -23.905 32.087 43.589 1.00 22.81 O ANISOU 3455 O ALA B 117 2819 2774 3073 -88 578 -160 O ATOM 3456 CB ALA B 117 -23.737 34.417 45.820 1.00 21.21 C ANISOU 3456 CB ALA B 117 2647 2540 2872 -36 591 -167 C ATOM 3457 N THR B 118 -25.371 31.682 45.252 1.00 17.64 N ANISOU 3457 N THR B 118 2150 2128 2426 -81 615 -167 N ATOM 3458 CA THR B 118 -25.417 30.254 44.960 1.00 17.64 C ANISOU 3458 CA THR B 118 2142 2132 2429 -110 626 -171 C ATOM 3459 C THR B 118 -26.163 29.988 43.658 1.00 24.98 C ANISOU 3459 C THR B 118 3037 3085 3368 -125 612 -178 C ATOM 3460 O THR B 118 -25.769 29.115 42.876 1.00 17.71 O ANISOU 3460 O THR B 118 2116 2167 2448 -149 606 -185 O ATOM 3461 CB THR B 118 -26.072 29.496 46.115 1.00 17.81 C ANISOU 3461 CB THR B 118 2160 2151 2456 -112 662 -172 C ATOM 3462 OG1 THR B 118 -25.363 29.762 47.332 1.00 18.65 O ANISOU 3462 OG1 THR B 118 2298 2243 2545 -93 673 -166 O ATOM 3463 CG2 THR B 118 -26.057 28.003 45.850 1.00 17.85 C ANISOU 3463 CG2 THR B 118 2159 2151 2471 -143 680 -175 C ATOM 3464 N LEU B 119 -27.246 30.733 43.411 1.00 20.33 N ANISOU 3464 N LEU B 119 2419 2519 2787 -110 606 -179 N ATOM 3465 CA LEU B 119 -27.988 30.588 42.163 1.00 22.37 C ANISOU 3465 CA LEU B 119 2640 2810 3050 -118 588 -187 C ATOM 3466 C LEU B 119 -27.142 31.008 40.968 1.00 18.04 C ANISOU 3466 C LEU B 119 2102 2265 2486 -113 559 -180 C ATOM 3467 O LEU B 119 -27.018 30.262 39.989 1.00 21.51 O ANISOU 3467 O LEU B 119 2530 2721 2922 -133 547 -192 O ATOM 3468 CB LEU B 119 -29.274 31.415 42.219 1.00 23.92 C ANISOU 3468 CB LEU B 119 2803 3032 3254 -96 587 -185 C ATOM 3469 CG LEU B 119 -30.184 31.378 40.990 1.00 29.77 C ANISOU 3469 CG LEU B 119 3498 3817 3996 -97 566 -194 C ATOM 3470 CD1 LEU B 119 -30.940 30.058 40.928 1.00 25.01 C ANISOU 3470 CD1 LEU B 119 2863 3231 3410 -133 579 -220 C ATOM 3471 CD2 LEU B 119 -31.147 32.552 40.998 1.00 29.88 C ANISOU 3471 CD2 LEU B 119 3488 3854 4012 -61 562 -182 C ATOM 3472 N GLY B 120 -26.546 32.200 41.035 1.00 20.68 N ANISOU 3472 N GLY B 120 2458 2586 2815 -86 550 -163 N ATOM 3473 CA GLY B 120 -25.748 32.680 39.918 1.00 24.72 C ANISOU 3473 CA GLY B 120 2980 3099 3315 -77 528 -152 C ATOM 3474 C GLY B 120 -24.553 31.793 39.632 1.00 17.57 C ANISOU 3474 C GLY B 120 2098 2177 2401 -102 525 -156 C ATOM 3475 O GLY B 120 -24.206 31.558 38.473 1.00 25.83 O ANISOU 3475 O GLY B 120 3140 3238 3436 -106 508 -155 O ATOM 3476 N GLY B 121 -23.907 31.290 40.685 1.00 23.45 N ANISOU 3476 N GLY B 121 2868 2893 3148 -114 542 -159 N ATOM 3477 CA GLY B 121 -22.780 30.394 40.486 1.00 17.19 C ANISOU 3477 CA GLY B 121 2098 2085 2348 -134 542 -161 C ATOM 3478 C GLY B 121 -23.186 29.081 39.847 1.00 17.84 C ANISOU 3478 C GLY B 121 2163 2184 2432 -162 545 -178 C ATOM 3479 O GLY B 121 -22.474 28.548 38.992 1.00 29.27 O ANISOU 3479 O GLY B 121 3618 3631 3871 -174 536 -180 O ATOM 3480 N GLU B 122 -24.336 28.540 40.252 1.00 20.25 N ANISOU 3480 N GLU B 122 2442 2500 2750 -173 561 -191 N ATOM 3481 CA GLU B 122 -24.807 27.282 39.686 1.00 17.98 C ANISOU 3481 CA GLU B 122 2134 2226 2472 -204 567 -213 C ATOM 3482 C GLU B 122 -25.367 27.454 38.278 1.00 24.21 C ANISOU 3482 C GLU B 122 2890 3054 3253 -204 540 -226 C ATOM 3483 O GLU B 122 -25.270 26.528 37.464 1.00 17.97 O ANISOU 3483 O GLU B 122 2092 2275 2463 -227 535 -247 O ATOM 3484 CB GLU B 122 -25.855 26.652 40.607 1.00 17.90 C ANISOU 3484 CB GLU B 122 2104 2213 2484 -217 597 -224 C ATOM 3485 CG GLU B 122 -25.277 26.031 41.875 1.00 17.77 C ANISOU 3485 CG GLU B 122 2118 2162 2472 -220 630 -213 C ATOM 3486 CD GLU B 122 -24.374 24.844 41.589 1.00 22.76 C ANISOU 3486 CD GLU B 122 2770 2773 3105 -244 642 -217 C ATOM 3487 OE1 GLU B 122 -24.638 24.114 40.613 1.00 23.50 O ANISOU 3487 OE1 GLU B 122 2845 2877 3209 -268 637 -238 O ATOM 3488 OE2 GLU B 122 -23.397 24.638 42.340 1.00 29.69 O ANISOU 3488 OE2 GLU B 122 3681 3625 3973 -236 656 -200 O ATOM 3489 N ILE B 123 -25.951 28.615 37.968 1.00 18.00 N ANISOU 3489 N ILE B 123 2086 2292 2459 -175 522 -216 N ATOM 3490 CA ILE B 123 -26.347 28.888 36.589 1.00 23.32 C ANISOU 3490 CA ILE B 123 2732 3010 3118 -165 494 -222 C ATOM 3491 C ILE B 123 -25.124 28.884 35.682 1.00 24.25 C ANISOU 3491 C ILE B 123 2876 3123 3216 -162 479 -213 C ATOM 3492 O ILE B 123 -25.154 28.333 34.574 1.00 18.77 O ANISOU 3492 O ILE B 123 2167 2457 2508 -171 463 -230 O ATOM 3493 CB ILE B 123 -27.119 30.217 36.496 1.00 29.19 C ANISOU 3493 CB ILE B 123 3455 3777 3857 -127 482 -204 C ATOM 3494 CG1 ILE B 123 -28.468 30.093 37.199 1.00 18.65 C ANISOU 3494 CG1 ILE B 123 2087 2458 2542 -132 496 -218 C ATOM 3495 CG2 ILE B 123 -27.340 30.616 35.040 1.00 18.62 C ANISOU 3495 CG2 ILE B 123 2094 2487 2495 -107 453 -202 C ATOM 3496 CD1 ILE B 123 -29.372 31.284 36.996 1.00 28.09 C ANISOU 3496 CD1 ILE B 123 3255 3684 3732 -94 485 -202 C ATOM 3497 N ALA B 124 -24.028 29.493 36.141 1.00 17.72 N ANISOU 3497 N ALA B 124 2087 2259 2386 -149 484 -188 N ATOM 3498 CA ALA B 124 -22.800 29.500 35.356 1.00 18.41 C ANISOU 3498 CA ALA B 124 2200 2338 2458 -146 473 -176 C ATOM 3499 C ALA B 124 -22.244 28.092 35.176 1.00 19.47 C ANISOU 3499 C ALA B 124 2344 2462 2592 -179 481 -196 C ATOM 3500 O ALA B 124 -21.838 27.717 34.070 1.00 18.61 O ANISOU 3500 O ALA B 124 2235 2370 2467 -182 468 -202 O ATOM 3501 CB ALA B 124 -21.762 30.408 36.014 1.00 17.28 C ANISOU 3501 CB ALA B 124 2090 2156 2319 -129 480 -149 C ATOM 3502 N LEU B 125 -22.217 27.295 36.249 1.00 17.37 N ANISOU 3502 N LEU B 125 2089 2168 2343 -201 505 -206 N ATOM 3503 CA LEU B 125 -21.637 25.957 36.160 1.00 17.32 C ANISOU 3503 CA LEU B 125 2096 2145 2340 -230 519 -221 C ATOM 3504 C LEU B 125 -22.425 25.074 35.200 1.00 22.03 C ANISOU 3504 C LEU B 125 2660 2771 2938 -252 513 -255 C ATOM 3505 O LEU B 125 -21.845 24.382 34.355 1.00 21.05 O ANISOU 3505 O LEU B 125 2544 2651 2805 -265 508 -268 O ATOM 3506 CB LEU B 125 -21.571 25.310 37.542 1.00 24.83 C ANISOU 3506 CB LEU B 125 3062 3063 3310 -242 551 -219 C ATOM 3507 CG LEU B 125 -21.117 23.847 37.526 1.00 24.15 C ANISOU 3507 CG LEU B 125 2987 2955 3232 -271 574 -233 C ATOM 3508 CD1 LEU B 125 -19.783 23.687 36.813 1.00 27.54 C ANISOU 3508 CD1 LEU B 125 3443 3375 3644 -268 563 -224 C ATOM 3509 CD2 LEU B 125 -21.023 23.310 38.928 1.00 22.86 C ANISOU 3509 CD2 LEU B 125 2841 2761 3084 -274 608 -222 C ATOM 3510 N TRP B 126 -23.752 25.078 35.320 1.00 18.24 N ANISOU 3510 N TRP B 126 2143 2316 2471 -258 513 -274 N ATOM 3511 CA TRP B 126 -24.554 24.281 34.404 1.00 18.30 C ANISOU 3511 CA TRP B 126 2114 2357 2482 -280 504 -313 C ATOM 3512 C TRP B 126 -24.582 24.879 33.003 1.00 26.37 C ANISOU 3512 C TRP B 126 3120 3428 3472 -259 468 -316 C ATOM 3513 O TRP B 126 -24.812 24.145 32.037 1.00 24.55 O ANISOU 3513 O TRP B 126 2868 3226 3234 -276 456 -351 O ATOM 3514 CB TRP B 126 -25.965 24.103 34.969 1.00 22.51 C ANISOU 3514 CB TRP B 126 2608 2905 3041 -293 517 -333 C ATOM 3515 CG TRP B 126 -25.985 23.153 36.133 1.00 20.66 C ANISOU 3515 CG TRP B 126 2386 2625 2840 -320 558 -336 C ATOM 3516 CD1 TRP B 126 -26.061 23.474 37.458 1.00 18.43 C ANISOU 3516 CD1 TRP B 126 2119 2316 2570 -309 583 -311 C ATOM 3517 CD2 TRP B 126 -25.886 21.724 36.072 1.00 23.96 C ANISOU 3517 CD2 TRP B 126 2804 3020 3281 -358 584 -365 C ATOM 3518 NE1 TRP B 126 -26.033 22.332 38.224 1.00 19.62 N ANISOU 3518 NE1 TRP B 126 2278 2430 2747 -335 623 -318 N ATOM 3519 CE2 TRP B 126 -25.928 21.245 37.395 1.00 22.94 C ANISOU 3519 CE2 TRP B 126 2689 2848 3178 -366 627 -350 C ATOM 3520 CE3 TRP B 126 -25.778 20.804 35.024 1.00 24.19 C ANISOU 3520 CE3 TRP B 126 2821 3059 3312 -385 578 -402 C ATOM 3521 CZ2 TRP B 126 -25.862 19.887 37.697 1.00 25.23 C ANISOU 3521 CZ2 TRP B 126 2985 3104 3500 -399 666 -366 C ATOM 3522 CZ3 TRP B 126 -25.714 19.459 35.325 1.00 25.53 C ANISOU 3522 CZ3 TRP B 126 2996 3191 3515 -421 616 -424 C ATOM 3523 CH2 TRP B 126 -25.757 19.013 36.650 1.00 19.69 C ANISOU 3523 CH2 TRP B 126 2271 2406 2804 -427 661 -403 C ATOM 3524 N SER B 127 -24.332 26.185 32.868 1.00 22.81 N ANISOU 3524 N SER B 127 2678 2986 3002 -220 452 -281 N ATOM 3525 CA SER B 127 -24.160 26.768 31.540 1.00 21.89 C ANISOU 3525 CA SER B 127 2554 2912 2852 -193 423 -274 C ATOM 3526 C SER B 127 -22.942 26.192 30.834 1.00 27.07 C ANISOU 3526 C SER B 127 3239 3555 3492 -200 421 -274 C ATOM 3527 O SER B 127 -22.953 26.029 29.608 1.00 24.64 O ANISOU 3527 O SER B 127 2917 3288 3156 -193 401 -289 O ATOM 3528 CB SER B 127 -24.037 28.288 31.630 1.00 18.35 C ANISOU 3528 CB SER B 127 2115 2465 2394 -149 416 -230 C ATOM 3529 OG SER B 127 -25.300 28.890 31.842 1.00 21.58 O ANISOU 3529 OG SER B 127 2488 2904 2808 -133 410 -231 O ATOM 3530 N LEU B 128 -21.878 25.892 31.583 1.00 20.21 N ANISOU 3530 N LEU B 128 2410 2634 2636 -213 442 -259 N ATOM 3531 CA LEU B 128 -20.696 25.294 30.976 1.00 32.85 C ANISOU 3531 CA LEU B 128 4037 4220 4224 -220 444 -258 C ATOM 3532 C LEU B 128 -20.957 23.853 30.560 1.00 28.88 C ANISOU 3532 C LEU B 128 3523 3724 3727 -255 451 -304 C ATOM 3533 O LEU B 128 -20.365 23.370 29.588 1.00 27.28 O ANISOU 3533 O LEU B 128 3327 3532 3504 -258 443 -316 O ATOM 3534 CB LEU B 128 -19.513 25.373 31.940 1.00 19.80 C ANISOU 3534 CB LEU B 128 2425 2514 2584 -221 464 -229 C ATOM 3535 CG LEU B 128 -19.165 26.764 32.476 1.00 22.90 C ANISOU 3535 CG LEU B 128 2831 2892 2978 -191 461 -191 C ATOM 3536 CD1 LEU B 128 -18.120 26.668 33.572 1.00 19.53 C ANISOU 3536 CD1 LEU B 128 2438 2418 2566 -198 481 -175 C ATOM 3537 CD2 LEU B 128 -18.685 27.675 31.356 1.00 27.98 C ANISOU 3537 CD2 LEU B 128 3476 3556 3598 -160 443 -167 C ATOM 3538 N VAL B 129 -21.830 23.150 31.285 1.00 18.61 N ANISOU 3538 N VAL B 129 2202 2412 2455 -284 468 -330 N ATOM 3539 CA VAL B 129 -22.248 21.817 30.861 1.00 18.50 C ANISOU 3539 CA VAL B 129 2170 2404 2456 -320 477 -380 C ATOM 3540 C VAL B 129 -22.971 21.890 29.524 1.00 18.93 C ANISOU 3540 C VAL B 129 2185 2522 2483 -315 444 -414 C ATOM 3541 O VAL B 129 -22.743 21.067 28.629 1.00 27.62 O ANISOU 3541 O VAL B 129 3283 3637 3574 -331 439 -449 O ATOM 3542 CB VAL B 129 -23.126 21.166 31.944 1.00 18.63 C ANISOU 3542 CB VAL B 129 2170 2396 2514 -350 506 -398 C ATOM 3543 CG1 VAL B 129 -23.735 19.869 31.433 1.00 23.50 C ANISOU 3543 CG1 VAL B 129 2758 3019 3151 -390 517 -455 C ATOM 3544 CG2 VAL B 129 -22.308 20.919 33.199 1.00 18.28 C ANISOU 3544 CG2 VAL B 129 2165 2292 2487 -352 541 -365 C ATOM 3545 N VAL B 130 -23.851 22.880 29.369 1.00 24.42 N ANISOU 3545 N VAL B 130 2851 3261 3167 -289 421 -406 N ATOM 3546 CA VAL B 130 -24.577 23.052 28.115 1.00 20.74 C ANISOU 3546 CA VAL B 130 2345 2867 2670 -275 387 -434 C ATOM 3547 C VAL B 130 -23.620 23.435 26.991 1.00 25.90 C ANISOU 3547 C VAL B 130 3020 3542 3278 -244 367 -415 C ATOM 3548 O VAL B 130 -23.775 22.991 25.846 1.00 26.45 O ANISOU 3548 O VAL B 130 3070 3659 3320 -244 346 -451 O ATOM 3549 CB VAL B 130 -25.699 24.090 28.300 1.00 24.22 C ANISOU 3549 CB VAL B 130 2749 3346 3107 -248 371 -421 C ATOM 3550 CG1 VAL B 130 -26.272 24.511 26.957 1.00 27.33 C ANISOU 3550 CG1 VAL B 130 3106 3820 3457 -218 332 -436 C ATOM 3551 CG2 VAL B 130 -26.796 23.529 29.200 1.00 19.90 C ANISOU 3551 CG2 VAL B 130 2170 2788 2602 -283 389 -451 C ATOM 3552 N LEU B 131 -22.611 24.256 27.297 1.00 23.45 N ANISOU 3552 N LEU B 131 2749 3199 2961 -217 375 -360 N ATOM 3553 CA LEU B 131 -21.653 24.664 26.274 1.00 28.73 C ANISOU 3553 CA LEU B 131 3440 3883 3592 -186 362 -336 C ATOM 3554 C LEU B 131 -20.737 23.515 25.868 1.00 33.58 C ANISOU 3554 C LEU B 131 4079 4476 4204 -212 373 -360 C ATOM 3555 O LEU B 131 -20.402 23.374 24.685 1.00 26.91 O ANISOU 3555 O LEU B 131 3234 3669 3324 -197 357 -370 O ATOM 3556 CB LEU B 131 -20.834 25.856 26.767 1.00 24.00 C ANISOU 3556 CB LEU B 131 2874 3250 2996 -155 371 -274 C ATOM 3557 CG LEU B 131 -21.570 27.196 26.787 1.00 19.72 C ANISOU 3557 CG LEU B 131 2312 2736 2446 -116 359 -243 C ATOM 3558 CD1 LEU B 131 -20.695 28.276 27.382 1.00 29.79 C ANISOU 3558 CD1 LEU B 131 3621 3965 3734 -94 374 -189 C ATOM 3559 CD2 LEU B 131 -22.005 27.570 25.382 1.00 31.30 C ANISOU 3559 CD2 LEU B 131 3752 4274 3867 -80 332 -245 C ATOM 3560 N ALA B 132 -20.309 22.693 26.830 1.00 27.56 N ANISOU 3560 N ALA B 132 3338 3655 3478 -247 402 -367 N ATOM 3561 CA ALA B 132 -19.436 21.567 26.504 1.00 30.14 C ANISOU 3561 CA ALA B 132 3690 3957 3806 -270 417 -387 C ATOM 3562 C ALA B 132 -20.142 20.563 25.603 1.00 26.82 C ANISOU 3562 C ALA B 132 3238 3575 3378 -294 407 -452 C ATOM 3563 O ALA B 132 -19.558 20.070 24.631 1.00 29.77 O ANISOU 3563 O ALA B 132 3621 3964 3726 -292 401 -470 O ATOM 3564 CB ALA B 132 -18.950 20.888 27.785 1.00 23.74 C ANISOU 3564 CB ALA B 132 2905 3078 3036 -299 454 -379 C ATOM 3565 N ILE B 133 -21.402 20.252 25.912 1.00 21.09 N ANISOU 3565 N ILE B 133 2473 2866 2675 -318 405 -491 N ATOM 3566 CA ILE B 133 -22.178 19.345 25.075 1.00 26.18 C ANISOU 3566 CA ILE B 133 3079 3551 3316 -344 392 -560 C ATOM 3567 C ILE B 133 -22.359 19.935 23.684 1.00 30.94 C ANISOU 3567 C ILE B 133 3661 4233 3862 -307 351 -570 C ATOM 3568 O ILE B 133 -22.267 19.225 22.675 1.00 34.32 O ANISOU 3568 O ILE B 133 4080 4692 4268 -315 339 -616 O ATOM 3569 CB ILE B 133 -23.527 19.033 25.751 1.00 22.88 C ANISOU 3569 CB ILE B 133 2619 3137 2939 -375 399 -596 C ATOM 3570 CG1 ILE B 133 -23.293 18.217 27.026 1.00 29.46 C ANISOU 3570 CG1 ILE B 133 3475 3892 3828 -412 446 -590 C ATOM 3571 CG2 ILE B 133 -24.466 18.306 24.795 1.00 23.51 C ANISOU 3571 CG2 ILE B 133 2648 3272 3013 -399 378 -673 C ATOM 3572 CD1 ILE B 133 -24.471 18.200 27.977 1.00 26.04 C ANISOU 3572 CD1 ILE B 133 3008 3450 3434 -432 461 -601 C ATOM 3573 N GLU B 134 -22.607 21.244 23.606 1.00 30.07 N ANISOU 3573 N GLU B 134 3543 4157 3727 -262 330 -524 N ATOM 3574 CA GLU B 134 -22.767 21.899 22.310 1.00 31.82 C ANISOU 3574 CA GLU B 134 3745 4456 3890 -217 294 -522 C ATOM 3575 C GLU B 134 -21.490 21.802 21.482 1.00 35.40 C ANISOU 3575 C GLU B 134 4236 4904 4308 -197 296 -503 C ATOM 3576 O GLU B 134 -21.531 21.461 20.295 1.00 29.94 O ANISOU 3576 O GLU B 134 3531 4269 3575 -184 274 -538 O ATOM 3577 CB GLU B 134 -23.178 23.358 22.516 1.00 28.26 C ANISOU 3577 CB GLU B 134 3285 4028 3426 -171 282 -467 C ATOM 3578 CG GLU B 134 -23.515 24.113 21.235 1.00 27.16 C ANISOU 3578 CG GLU B 134 3120 3973 3225 -117 248 -458 C ATOM 3579 CD GLU B 134 -22.305 24.783 20.611 1.00 32.56 C ANISOU 3579 CD GLU B 134 3845 4651 3875 -74 252 -401 C ATOM 3580 OE1 GLU B 134 -21.266 24.891 21.296 1.00 31.57 O ANISOU 3580 OE1 GLU B 134 3764 4454 3777 -83 279 -363 O ATOM 3581 OE2 GLU B 134 -22.394 25.202 19.437 1.00 38.19 O ANISOU 3581 OE2 GLU B 134 4544 5433 4534 -28 229 -395 O ATOM 3582 N ARG B 135 -20.340 22.093 22.097 1.00 21.51 N ANISOU 3582 N ARG B 135 2525 3082 2565 -192 322 -450 N ATOM 3583 CA ARG B 135 -19.072 21.981 21.382 1.00 39.17 C ANISOU 3583 CA ARG B 135 4799 5310 4775 -174 327 -429 C ATOM 3584 C ARG B 135 -18.809 20.541 20.961 1.00 35.18 C ANISOU 3584 C ARG B 135 4297 4796 4273 -211 336 -489 C ATOM 3585 O ARG B 135 -18.256 20.288 19.884 1.00 36.99 O ANISOU 3585 O ARG B 135 4536 5056 4463 -194 328 -500 O ATOM 3586 CB ARG B 135 -17.929 22.505 22.248 1.00 31.79 C ANISOU 3586 CB ARG B 135 3908 4306 3864 -168 354 -367 C ATOM 3587 CG ARG B 135 -17.924 24.014 22.446 1.00 29.75 C ANISOU 3587 CG ARG B 135 3651 4053 3599 -126 348 -306 C ATOM 3588 CD ARG B 135 -17.548 24.752 21.166 1.00 24.28 C ANISOU 3588 CD ARG B 135 2960 3410 2856 -74 333 -276 C ATOM 3589 NE ARG B 135 -18.719 25.125 20.380 1.00 33.36 N ANISOU 3589 NE ARG B 135 4068 4638 3970 -47 303 -295 N ATOM 3590 CZ ARG B 135 -18.679 25.566 19.130 1.00 32.45 C ANISOU 3590 CZ ARG B 135 3944 4584 3800 0 286 -281 C ATOM 3591 NH1 ARG B 135 -17.536 25.696 18.477 1.00 37.42 N ANISOU 3591 NH1 ARG B 135 4605 5206 4408 24 297 -249 N ATOM 3592 NH2 ARG B 135 -19.817 25.882 18.518 1.00 29.33 N ANISOU 3592 NH2 ARG B 135 3506 4264 3372 26 258 -300 N ATOM 3593 N TYR B 136 -19.186 19.583 21.810 1.00 30.65 N ANISOU 3593 N TYR B 136 3719 4179 3748 -261 357 -526 N ATOM 3594 CA TYR B 136 -19.024 18.174 21.469 1.00 33.00 C ANISOU 3594 CA TYR B 136 4019 4461 4058 -299 371 -586 C ATOM 3595 C TYR B 136 -19.864 17.805 20.251 1.00 37.77 C ANISOU 3595 C TYR B 136 4581 5142 4627 -299 339 -654 C ATOM 3596 O TYR B 136 -19.360 17.213 19.290 1.00 33.10 O ANISOU 3596 O TYR B 136 4000 4571 4007 -296 335 -685 O ATOM 3597 CB TYR B 136 -19.396 17.308 22.673 1.00 34.15 C ANISOU 3597 CB TYR B 136 4164 4544 4267 -350 405 -608 C ATOM 3598 CG TYR B 136 -19.427 15.821 22.404 1.00 38.09 C ANISOU 3598 CG TYR B 136 4660 5021 4790 -394 426 -675 C ATOM 3599 CD1 TYR B 136 -18.329 15.168 21.856 1.00 39.22 C ANISOU 3599 CD1 TYR B 136 4839 5143 4921 -393 440 -679 C ATOM 3600 CD2 TYR B 136 -20.548 15.063 22.722 1.00 34.93 C ANISOU 3600 CD2 TYR B 136 4222 4619 4432 -438 434 -734 C ATOM 3601 CE1 TYR B 136 -18.354 13.802 21.616 1.00 33.90 C ANISOU 3601 CE1 TYR B 136 4163 4443 4273 -433 463 -742 C ATOM 3602 CE2 TYR B 136 -20.582 13.700 22.490 1.00 30.26 C ANISOU 3602 CE2 TYR B 136 3627 4000 3870 -481 458 -798 C ATOM 3603 CZ TYR B 136 -19.484 13.075 21.938 1.00 45.90 C ANISOU 3603 CZ TYR B 136 5646 5958 5837 -478 473 -802 C ATOM 3604 OH TYR B 136 -19.521 11.719 21.709 1.00 55.80 O ANISOU 3604 OH TYR B 136 6898 7180 7124 -520 501 -867 O ATOM 3605 N VAL B 137 -21.147 18.170 20.264 1.00 30.42 N ANISOU 3605 N VAL B 137 3601 4260 3696 -300 315 -678 N ATOM 3606 CA VAL B 137 -22.014 17.863 19.132 1.00 35.06 C ANISOU 3606 CA VAL B 137 4142 4930 4248 -298 280 -747 C ATOM 3607 C VAL B 137 -21.534 18.583 17.877 1.00 47.68 C ANISOU 3607 C VAL B 137 5748 6597 5772 -239 250 -722 C ATOM 3608 O VAL B 137 -21.507 18.005 16.784 1.00 43.02 O ANISOU 3608 O VAL B 137 5146 6056 5144 -235 233 -774 O ATOM 3609 CB VAL B 137 -23.475 18.218 19.463 1.00 38.74 C ANISOU 3609 CB VAL B 137 4552 5439 4730 -306 260 -771 C ATOM 3610 CG1 VAL B 137 -24.371 17.915 18.277 1.00 39.86 C ANISOU 3610 CG1 VAL B 137 4639 5674 4831 -302 220 -845 C ATOM 3611 CG2 VAL B 137 -23.939 17.451 20.688 1.00 40.82 C ANISOU 3611 CG2 VAL B 137 4809 5633 5067 -364 294 -794 C ATOM 3612 N VAL B 138 -21.152 19.854 18.012 1.00 44.23 N ANISOU 3612 N VAL B 138 5329 6162 5314 -190 247 -642 N ATOM 3613 CA VAL B 138 -20.762 20.647 16.850 1.00 41.80 C ANISOU 3613 CA VAL B 138 5025 5918 4937 -128 224 -609 C ATOM 3614 C VAL B 138 -19.456 20.132 16.254 1.00 45.36 C ANISOU 3614 C VAL B 138 5520 6345 5368 -122 241 -602 C ATOM 3615 O VAL B 138 -19.359 19.895 15.044 1.00 51.25 O ANISOU 3615 O VAL B 138 6259 7155 6060 -97 221 -632 O ATOM 3616 CB VAL B 138 -20.661 22.136 17.229 1.00 30.03 C ANISOU 3616 CB VAL B 138 3546 4424 3441 -80 226 -523 C ATOM 3617 CG1 VAL B 138 -19.865 22.905 16.184 1.00 51.10 C ANISOU 3617 CG1 VAL B 138 6236 7129 6051 -18 220 -471 C ATOM 3618 CG2 VAL B 138 -22.051 22.734 17.392 1.00 35.68 C ANISOU 3618 CG2 VAL B 138 4211 5192 4156 -68 201 -533 C ATOM 3619 N VAL B 139 -18.439 19.935 17.092 1.00 44.55 N ANISOU 3619 N VAL B 139 5463 6157 5307 -143 277 -565 N ATOM 3620 CA VAL B 139 -17.108 19.642 16.571 1.00 42.83 C ANISOU 3620 CA VAL B 139 5288 5916 5071 -130 294 -544 C ATOM 3621 C VAL B 139 -16.938 18.153 16.292 1.00 49.60 C ANISOU 3621 C VAL B 139 6149 6756 5939 -173 306 -617 C ATOM 3622 O VAL B 139 -16.416 17.767 15.241 1.00 63.54 O ANISOU 3622 O VAL B 139 7926 8554 7662 -155 301 -638 O ATOM 3623 CB VAL B 139 -16.035 20.169 17.540 1.00 46.67 C ANISOU 3623 CB VAL B 139 5818 6323 5593 -128 326 -470 C ATOM 3624 CG1 VAL B 139 -14.651 19.776 17.063 1.00 58.62 C ANISOU 3624 CG1 VAL B 139 7372 7810 7092 -118 347 -451 C ATOM 3625 CG2 VAL B 139 -16.140 21.677 17.661 1.00 46.99 C ANISOU 3625 CG2 VAL B 139 5854 6380 5620 -82 317 -402 C ATOM 3626 N CYS B 140 -17.364 17.292 17.218 1.00 42.22 N ANISOU 3626 N CYS B 140 5209 5770 5064 -229 325 -657 N ATOM 3627 CA CYS B 140 -17.198 15.857 17.016 1.00 39.51 C ANISOU 3627 CA CYS B 140 4872 5401 4741 -272 344 -725 C ATOM 3628 C CYS B 140 -18.238 15.267 16.077 1.00 54.09 C ANISOU 3628 C CYS B 140 6670 7318 6562 -286 314 -815 C ATOM 3629 O CYS B 140 -18.026 14.162 15.567 1.00 57.85 O ANISOU 3629 O CYS B 140 7152 7788 7042 -312 324 -877 O ATOM 3630 CB CYS B 140 -17.249 15.119 18.355 1.00 49.88 C ANISOU 3630 CB CYS B 140 6195 6628 6128 -324 382 -730 C ATOM 3631 SG CYS B 140 -15.792 15.380 19.398 1.00 46.61 S ANISOU 3631 SG CYS B 140 5840 6127 5743 -315 422 -643 S ATOM 3632 N ALYS B 141 -19.341 15.977 15.839 0.56 50.64 N ANISOU 3632 N ALYS B 141 6188 6952 6103 -268 278 -825 N ATOM 3633 N BLYS B 141 -19.343 15.973 15.843 0.44 50.69 N ANISOU 3633 N BLYS B 141 6193 6956 6108 -268 278 -825 N ATOM 3634 CA ALYS B 141 -20.440 15.550 14.977 0.56 51.18 C ANISOU 3634 CA ALYS B 141 6202 7101 6145 -277 242 -911 C ATOM 3635 CA BLYS B 141 -20.438 15.548 14.973 0.44 51.24 C ANISOU 3635 CA BLYS B 141 6209 7108 6152 -277 242 -911 C ATOM 3636 C ALYS B 141 -20.831 14.087 15.225 0.56 54.38 C ANISOU 3636 C ALYS B 141 6592 7465 6605 -347 263 -1001 C ATOM 3637 C BLYS B 141 -20.839 14.088 15.223 0.44 54.40 C ANISOU 3637 C BLYS B 141 6595 7469 6608 -347 263 -1001 C ATOM 3638 O ALYS B 141 -20.775 13.264 14.306 0.56 62.92 O ANISOU 3638 O ALYS B 141 7665 8577 7664 -358 255 -1072 O ATOM 3639 O BLYS B 141 -20.800 13.267 14.300 0.44 62.84 O ANISOU 3639 O BLYS B 141 7653 8568 7653 -358 255 -1073 O ATOM 3640 CB ALYS B 141 -20.098 15.781 13.509 0.56 55.48 C ANISOU 3640 CB ALYS B 141 6746 7729 6607 -226 212 -922 C ATOM 3641 CB BLYS B 141 -20.083 15.772 13.507 0.44 55.49 C ANISOU 3641 CB BLYS B 141 6747 7729 6607 -226 212 -922 C ATOM 3642 CG ALYS B 141 -19.854 17.243 13.163 0.56 58.28 C ANISOU 3642 CG ALYS B 141 7108 8129 6906 -154 193 -836 C ATOM 3643 CG BLYS B 141 -19.500 17.147 13.221 0.44 57.60 C ANISOU 3643 CG BLYS B 141 7037 8023 6825 -155 203 -827 C ATOM 3644 CD ALYS B 141 -19.322 17.408 11.749 0.56 57.44 C ANISOU 3644 CD ALYS B 141 7011 8096 6719 -99 173 -836 C ATOM 3645 CD BLYS B 141 -19.294 17.369 11.733 0.44 57.45 C ANISOU 3645 CD BLYS B 141 7012 8096 6720 -100 174 -838 C ATOM 3646 CE ALYS B 141 -18.986 18.865 11.457 0.56 60.15 C ANISOU 3646 CE ALYS B 141 7366 8472 7016 -26 166 -741 C ATOM 3647 CE BLYS B 141 -18.495 18.638 11.473 0.44 60.17 C ANISOU 3647 CE BLYS B 141 7388 8449 7024 -32 179 -735 C ATOM 3648 NZ ALYS B 141 -18.351 19.047 10.120 0.56 61.24 N ANISOU 3648 NZ ALYS B 141 7518 8675 7075 32 154 -729 N ATOM 3649 NZ BLYS B 141 -19.104 19.834 12.119 0.44 58.22 N ANISOU 3649 NZ BLYS B 141 7124 8206 6790 -9 171 -675 N ATOM 3650 N PRO B 142 -21.234 13.734 16.458 1.00 54.41 N ANISOU 3650 N PRO B 142 6592 7399 6682 -393 294 -1000 N ATOM 3651 CA PRO B 142 -21.594 12.344 16.737 1.00 54.69 C ANISOU 3651 CA PRO B 142 6614 7388 6779 -459 322 -1079 C ATOM 3652 C PRO B 142 -23.071 12.061 16.468 1.00 60.83 C ANISOU 3652 C PRO B 142 7321 8224 7568 -490 294 -1164 C ATOM 3653 O PRO B 142 -23.407 11.011 15.921 1.00 63.61 O ANISOU 3653 O PRO B 142 7649 8586 7935 -529 296 -1256 O ATOM 3654 CB PRO B 142 -21.273 12.208 18.223 1.00 58.00 C ANISOU 3654 CB PRO B 142 7064 7706 7266 -486 371 -1025 C ATOM 3655 CG PRO B 142 -21.622 13.557 18.775 1.00 53.57 C ANISOU 3655 CG PRO B 142 6495 7168 6690 -449 351 -954 C ATOM 3656 CD PRO B 142 -21.379 14.571 17.666 1.00 48.71 C ANISOU 3656 CD PRO B 142 5878 6637 5993 -387 307 -926 C ATOM 3657 N ARG B 147 -27.975 18.210 14.957 1.00 75.83 N ANISOU 3657 N ARG B 147 8978 10601 9234 -241 59 -1044 N ATOM 3658 CA ARG B 147 -27.455 19.572 15.008 1.00 70.26 C ANISOU 3658 CA ARG B 147 8307 9899 8490 -173 59 -939 C ATOM 3659 C ARG B 147 -28.010 20.344 16.209 1.00 70.24 C ANISOU 3659 C ARG B 147 8298 9856 8534 -174 75 -884 C ATOM 3660 O ARG B 147 -29.207 20.297 16.501 1.00 74.98 O ANISOU 3660 O ARG B 147 8842 10490 9158 -193 61 -922 O ATOM 3661 CB ARG B 147 -27.776 20.309 13.704 1.00 78.04 C ANISOU 3661 CB ARG B 147 9261 11006 9384 -100 12 -935 C ATOM 3662 CG ARG B 147 -27.148 21.690 13.591 1.00 76.58 C ANISOU 3662 CG ARG B 147 9114 10824 9158 -25 17 -826 C ATOM 3663 N PHE B 148 -27.117 21.052 16.901 1.00 49.88 N ANISOU 3663 N PHE B 148 5776 7205 5970 -154 105 -797 N ATOM 3664 CA PHE B 148 -27.457 21.850 18.077 1.00 51.09 C ANISOU 3664 CA PHE B 148 5934 7312 6166 -152 124 -739 C ATOM 3665 C PHE B 148 -27.892 23.227 17.588 1.00 54.34 C ANISOU 3665 C PHE B 148 6325 7795 6525 -78 98 -684 C ATOM 3666 O PHE B 148 -27.062 24.055 17.206 1.00 54.40 O ANISOU 3666 O PHE B 148 6372 7801 6497 -26 102 -617 O ATOM 3667 CB PHE B 148 -26.261 21.934 19.021 1.00 44.46 C ANISOU 3667 CB PHE B 148 5162 6367 5365 -165 167 -679 C ATOM 3668 CG PHE B 148 -26.617 22.253 20.449 1.00 39.13 C ANISOU 3668 CG PHE B 148 4491 5627 4749 -187 194 -648 C ATOM 3669 CD1 PHE B 148 -27.080 23.510 20.801 1.00 46.04 C ANISOU 3669 CD1 PHE B 148 5357 6520 5617 -145 188 -592 C ATOM 3670 CD2 PHE B 148 -26.458 21.301 21.445 1.00 28.07 C ANISOU 3670 CD2 PHE B 148 3106 4148 3409 -247 229 -671 C ATOM 3671 CE1 PHE B 148 -27.398 23.808 22.117 1.00 35.60 C ANISOU 3671 CE1 PHE B 148 4040 5140 4346 -163 213 -565 C ATOM 3672 CE2 PHE B 148 -26.770 21.593 22.762 1.00 44.85 C ANISOU 3672 CE2 PHE B 148 5238 6220 5585 -263 255 -641 C ATOM 3673 CZ PHE B 148 -27.242 22.848 23.098 1.00 36.85 C ANISOU 3673 CZ PHE B 148 4214 5226 4561 -222 245 -590 C ATOM 3674 N GLY B 149 -29.199 23.472 17.588 1.00 51.22 N ANISOU 3674 N GLY B 149 5870 7463 6128 -72 73 -711 N ATOM 3675 CA GLY B 149 -29.764 24.703 17.088 1.00 33.64 C ANISOU 3675 CA GLY B 149 3617 5313 3853 0 48 -665 C ATOM 3676 C GLY B 149 -30.223 25.635 18.191 1.00 51.25 C ANISOU 3676 C GLY B 149 5848 7502 6123 11 67 -607 C ATOM 3677 O GLY B 149 -29.788 25.547 19.344 1.00 33.14 O ANISOU 3677 O GLY B 149 3592 5113 3887 -26 103 -583 O ATOM 3678 N GLU B 150 -31.117 26.557 17.819 1.00 48.42 N ANISOU 3678 N GLU B 150 5447 7220 5730 66 42 -584 N ATOM 3679 CA GLU B 150 -31.649 27.515 18.784 1.00 48.87 C ANISOU 3679 CA GLU B 150 5501 7247 5821 84 60 -531 C ATOM 3680 C GLU B 150 -32.547 26.837 19.812 1.00 46.48 C ANISOU 3680 C GLU B 150 5164 6915 5582 20 69 -581 C ATOM 3681 O GLU B 150 -32.536 27.210 20.991 1.00 45.89 O ANISOU 3681 O GLU B 150 5112 6767 5557 6 101 -544 O ATOM 3682 CB GLU B 150 -32.414 28.624 18.062 1.00 51.52 C ANISOU 3682 CB GLU B 150 5797 7677 6102 162 32 -494 C ATOM 3683 CG GLU B 150 -31.555 29.797 17.618 1.00 47.09 C ANISOU 3683 CG GLU B 150 5282 7107 5502 234 46 -404 C ATOM 3684 CD GLU B 150 -32.372 30.884 16.951 1.00 49.04 C ANISOU 3684 CD GLU B 150 5489 7444 5698 316 24 -364 C ATOM 3685 OE1 GLU B 150 -32.801 30.683 15.795 1.00 60.75 O ANISOU 3685 OE1 GLU B 150 6931 9033 7118 351 -13 -395 O ATOM 3686 OE2 GLU B 150 -32.603 31.932 17.589 1.00 51.10 O ANISOU 3686 OE2 GLU B 150 5760 7674 5982 348 46 -301 O ATOM 3687 N ASN B 151 -33.341 25.850 19.384 1.00 45.74 N ANISOU 3687 N ASN B 151 5013 6877 5489 -18 44 -667 N ATOM 3688 CA ASN B 151 -34.227 25.159 20.318 1.00 50.45 C ANISOU 3688 CA ASN B 151 5573 7445 6151 -80 58 -717 C ATOM 3689 C ASN B 151 -33.437 24.503 21.442 1.00 40.29 C ANISOU 3689 C ASN B 151 4341 6039 4928 -138 105 -710 C ATOM 3690 O ASN B 151 -33.835 24.564 22.611 1.00 36.32 O ANISOU 3690 O ASN B 151 3839 5483 4480 -163 134 -695 O ATOM 3691 CB ASN B 151 -35.064 24.116 19.577 1.00 48.41 C ANISOU 3691 CB ASN B 151 5247 7262 5887 -116 26 -818 C ATOM 3692 CG ASN B 151 -36.131 24.736 18.699 1.00 44.59 C ANISOU 3692 CG ASN B 151 4693 6903 5347 -62 -22 -831 C ATOM 3693 OD1 ASN B 151 -36.595 25.847 18.959 1.00 52.31 O ANISOU 3693 OD1 ASN B 151 5660 7901 6313 -10 -23 -771 O ATOM 3694 ND2 ASN B 151 -36.532 24.018 17.656 1.00 49.16 N ANISOU 3694 ND2 ASN B 151 5221 7566 5891 -72 -60 -912 N ATOM 3695 N HIS B 152 -32.313 23.871 21.104 1.00 40.10 N ANISOU 3695 N HIS B 152 4364 5977 4896 -157 115 -718 N ATOM 3696 CA HIS B 152 -31.493 23.222 22.120 1.00 47.32 C ANISOU 3696 CA HIS B 152 5330 6782 5865 -206 160 -709 C ATOM 3697 C HIS B 152 -30.770 24.238 22.995 1.00 41.30 C ANISOU 3697 C HIS B 152 4624 5954 5113 -176 187 -621 C ATOM 3698 O HIS B 152 -30.529 23.973 24.179 1.00 36.83 O ANISOU 3698 O HIS B 152 4086 5309 4600 -210 223 -606 O ATOM 3699 CB HIS B 152 -30.501 22.274 21.447 1.00 49.62 C ANISOU 3699 CB HIS B 152 5654 7056 6143 -230 162 -743 C ATOM 3700 CG HIS B 152 -31.108 21.457 20.349 1.00 48.39 C ANISOU 3700 CG HIS B 152 5444 6978 5962 -247 129 -829 C ATOM 3701 ND1 HIS B 152 -31.217 21.917 19.054 1.00 55.11 N ANISOU 3701 ND1 HIS B 152 6273 7926 6741 -195 86 -836 N ATOM 3702 CD2 HIS B 152 -31.656 20.219 20.355 1.00 46.98 C ANISOU 3702 CD2 HIS B 152 5230 6797 5823 -310 134 -915 C ATOM 3703 CE1 HIS B 152 -31.798 20.995 18.308 1.00 57.40 C ANISOU 3703 CE1 HIS B 152 6514 8274 7022 -225 61 -927 C ATOM 3704 NE2 HIS B 152 -32.073 19.953 19.073 1.00 57.33 N ANISOU 3704 NE2 HIS B 152 6495 8203 7084 -297 90 -978 N ATOM 3705 N ALA B 153 -30.406 25.394 22.435 1.00 40.22 N ANISOU 3705 N ALA B 153 4504 5849 4928 -112 172 -563 N ATOM 3706 CA ALA B 153 -29.803 26.451 23.241 1.00 35.45 C ANISOU 3706 CA ALA B 153 3947 5185 4338 -83 196 -484 C ATOM 3707 C ALA B 153 -30.791 26.981 24.273 1.00 29.98 C ANISOU 3707 C ALA B 153 3229 4481 3682 -83 208 -470 C ATOM 3708 O ALA B 153 -30.455 27.133 25.454 1.00 29.10 O ANISOU 3708 O ALA B 153 3151 4295 3612 -101 240 -442 O ATOM 3709 CB ALA B 153 -29.310 27.580 22.334 1.00 39.96 C ANISOU 3709 CB ALA B 153 4534 5795 4853 -12 181 -428 C ATOM 3710 N ILE B 154 -32.024 27.258 23.843 1.00 33.18 N ANISOU 3710 N ILE B 154 3572 4964 4069 -62 181 -492 N ATOM 3711 CA ILE B 154 -33.036 27.791 24.751 1.00 32.20 C ANISOU 3711 CA ILE B 154 3419 4837 3978 -58 192 -478 C ATOM 3712 C ILE B 154 -33.434 26.745 25.785 1.00 36.04 C ANISOU 3712 C ILE B 154 3895 5273 4526 -127 218 -523 C ATOM 3713 O ILE B 154 -33.669 27.068 26.956 1.00 33.31 O ANISOU 3713 O ILE B 154 3560 4877 4218 -134 246 -496 O ATOM 3714 CB ILE B 154 -34.248 28.296 23.947 1.00 30.82 C ANISOU 3714 CB ILE B 154 3177 4766 3767 -16 155 -491 C ATOM 3715 CG1 ILE B 154 -33.819 29.430 23.015 1.00 39.63 C ANISOU 3715 CG1 ILE B 154 4309 5925 4823 60 138 -434 C ATOM 3716 CG2 ILE B 154 -35.362 28.756 24.876 1.00 34.78 C ANISOU 3716 CG2 ILE B 154 3644 5267 4304 -15 167 -482 C ATOM 3717 CD1 ILE B 154 -34.869 29.822 22.017 1.00 47.14 C ANISOU 3717 CD1 ILE B 154 5196 6991 5726 108 99 -447 C ATOM 3718 N MET B 155 -33.514 25.477 25.375 1.00 35.02 N ANISOU 3718 N MET B 155 3745 5155 4407 -176 212 -591 N ATOM 3719 CA MET B 155 -33.791 24.411 26.333 1.00 36.74 C ANISOU 3719 CA MET B 155 3956 5315 4687 -241 245 -630 C ATOM 3720 C MET B 155 -32.667 24.286 27.353 1.00 36.36 C ANISOU 3720 C MET B 155 3979 5168 4667 -258 286 -588 C ATOM 3721 O MET B 155 -32.918 24.021 28.534 1.00 23.39 O ANISOU 3721 O MET B 155 2343 3471 3073 -286 320 -582 O ATOM 3722 CB MET B 155 -34.012 23.089 25.599 1.00 37.24 C ANISOU 3722 CB MET B 155 3986 5407 4758 -290 233 -712 C ATOM 3723 CG MET B 155 -34.427 21.934 26.502 1.00 38.41 C ANISOU 3723 CG MET B 155 4120 5498 4976 -359 271 -756 C ATOM 3724 SD MET B 155 -35.470 20.757 25.621 1.00 58.23 S ANISOU 3724 SD MET B 155 6549 8072 7502 -408 248 -864 S ATOM 3725 CE MET B 155 -34.557 20.598 24.087 1.00 26.24 C ANISOU 3725 CE MET B 155 2517 4071 3382 -385 209 -887 C ATOM 3726 N GLY B 156 -31.419 24.472 26.915 1.00 34.17 N ANISOU 3726 N GLY B 156 3754 4869 4360 -239 283 -558 N ATOM 3727 CA GLY B 156 -30.314 24.494 27.855 1.00 32.43 C ANISOU 3727 CA GLY B 156 3598 4563 4161 -247 318 -515 C ATOM 3728 C GLY B 156 -30.410 25.637 28.846 1.00 22.38 C ANISOU 3728 C GLY B 156 2343 3262 2899 -216 333 -458 C ATOM 3729 O GLY B 156 -30.027 25.487 30.008 1.00 26.74 O ANISOU 3729 O GLY B 156 2928 3748 3485 -234 366 -438 O ATOM 3730 N VAL B 157 -30.930 26.786 28.407 1.00 21.36 N ANISOU 3730 N VAL B 157 2192 3184 2741 -166 310 -430 N ATOM 3731 CA VAL B 157 -31.084 27.931 29.301 1.00 32.75 C ANISOU 3731 CA VAL B 157 3650 4600 4195 -134 324 -378 C ATOM 3732 C VAL B 157 -32.058 27.603 30.426 1.00 32.02 C ANISOU 3732 C VAL B 157 3531 4490 4147 -162 347 -396 C ATOM 3733 O VAL B 157 -31.771 27.833 31.607 1.00 20.79 O ANISOU 3733 O VAL B 157 2140 3007 2750 -167 377 -369 O ATOM 3734 CB VAL B 157 -31.537 29.173 28.511 1.00 27.95 C ANISOU 3734 CB VAL B 157 3019 4053 3548 -72 298 -347 C ATOM 3735 CG1 VAL B 157 -32.083 30.234 29.451 1.00 27.65 C ANISOU 3735 CG1 VAL B 157 2981 3996 3529 -44 314 -308 C ATOM 3736 CG2 VAL B 157 -30.384 29.726 27.696 1.00 32.37 C ANISOU 3736 CG2 VAL B 157 3619 4610 4071 -38 289 -310 C ATOM 3737 N ALA B 158 -33.224 27.054 30.077 1.00 25.08 N ANISOU 3737 N ALA B 158 2591 3662 3276 -181 334 -443 N ATOM 3738 CA ALA B 158 -34.189 26.668 31.102 1.00 22.14 C ANISOU 3738 CA ALA B 158 2188 3273 2950 -210 359 -461 C ATOM 3739 C ALA B 158 -33.627 25.569 31.994 1.00 21.34 C ANISOU 3739 C ALA B 158 2120 3099 2889 -261 398 -475 C ATOM 3740 O ALA B 158 -33.853 25.567 33.209 1.00 28.72 O ANISOU 3740 O ALA B 158 3066 3990 3857 -271 432 -459 O ATOM 3741 CB ALA B 158 -35.498 26.219 30.454 1.00 29.57 C ANISOU 3741 CB ALA B 158 3053 4288 3895 -224 337 -515 C ATOM 3742 N PHE B 159 -32.882 24.633 31.405 1.00 25.67 N ANISOU 3742 N PHE B 159 2685 3635 3433 -290 396 -504 N ATOM 3743 CA PHE B 159 -32.288 23.548 32.177 1.00 24.57 C ANISOU 3743 CA PHE B 159 2579 3426 3331 -335 435 -514 C ATOM 3744 C PHE B 159 -31.338 24.079 33.247 1.00 28.08 C ANISOU 3744 C PHE B 159 3085 3808 3777 -316 461 -458 C ATOM 3745 O PHE B 159 -31.307 23.560 34.370 1.00 24.30 O ANISOU 3745 O PHE B 159 2622 3278 3332 -338 500 -451 O ATOM 3746 CB PHE B 159 -31.573 22.583 31.227 1.00 25.60 C ANISOU 3746 CB PHE B 159 2720 3557 3450 -361 426 -551 C ATOM 3747 CG PHE B 159 -30.659 21.603 31.913 1.00 32.58 C ANISOU 3747 CG PHE B 159 3650 4366 4363 -395 466 -548 C ATOM 3748 CD1 PHE B 159 -31.166 20.468 32.531 1.00 25.67 C ANISOU 3748 CD1 PHE B 159 2757 3457 3540 -442 504 -582 C ATOM 3749 CD2 PHE B 159 -29.288 21.810 31.925 1.00 28.99 C ANISOU 3749 CD2 PHE B 159 3255 3876 3886 -377 469 -511 C ATOM 3750 CE1 PHE B 159 -30.323 19.566 33.151 1.00 20.86 C ANISOU 3750 CE1 PHE B 159 2191 2779 2956 -467 545 -574 C ATOM 3751 CE2 PHE B 159 -28.443 20.913 32.543 1.00 35.64 C ANISOU 3751 CE2 PHE B 159 4137 4655 4751 -403 505 -507 C ATOM 3752 CZ PHE B 159 -28.961 19.791 33.158 1.00 29.29 C ANISOU 3752 CZ PHE B 159 3317 3818 3996 -446 544 -536 C ATOM 3753 N THR B 160 -30.552 25.110 32.917 1.00 20.17 N ANISOU 3753 N THR B 160 2116 2810 2738 -274 441 -417 N ATOM 3754 CA THR B 160 -29.613 25.666 33.890 1.00 20.97 C ANISOU 3754 CA THR B 160 2272 2855 2840 -257 462 -370 C ATOM 3755 C THR B 160 -30.338 26.263 35.090 1.00 27.73 C ANISOU 3755 C THR B 160 3121 3697 3718 -245 483 -350 C ATOM 3756 O THR B 160 -29.886 26.114 36.231 1.00 19.36 O ANISOU 3756 O THR B 160 2094 2587 2675 -251 513 -331 O ATOM 3757 CB THR B 160 -28.722 26.725 33.238 1.00 20.60 C ANISOU 3757 CB THR B 160 2255 2817 2756 -216 438 -334 C ATOM 3758 OG1 THR B 160 -29.530 27.788 32.717 1.00 21.17 O ANISOU 3758 OG1 THR B 160 2294 2940 2809 -177 414 -322 O ATOM 3759 CG2 THR B 160 -27.889 26.118 32.117 1.00 27.23 C ANISOU 3759 CG2 THR B 160 3107 3667 3573 -226 422 -350 C ATOM 3760 N TRP B 161 -31.455 26.960 34.853 1.00 27.15 N ANISOU 3760 N TRP B 161 3004 3670 3641 -223 467 -351 N ATOM 3761 CA TRP B 161 -32.218 27.528 35.961 1.00 21.76 C ANISOU 3761 CA TRP B 161 2312 2977 2979 -209 488 -333 C ATOM 3762 C TRP B 161 -32.824 26.435 36.833 1.00 27.38 C ANISOU 3762 C TRP B 161 3007 3665 3731 -250 523 -358 C ATOM 3763 O TRP B 161 -32.881 26.575 38.061 1.00 20.58 O ANISOU 3763 O TRP B 161 2164 2768 2888 -246 554 -337 O ATOM 3764 CB TRP B 161 -33.310 28.460 35.434 1.00 26.74 C ANISOU 3764 CB TRP B 161 2896 3666 3597 -175 464 -330 C ATOM 3765 CG TRP B 161 -32.811 29.816 35.029 1.00 31.18 C ANISOU 3765 CG TRP B 161 3482 4237 4128 -124 445 -289 C ATOM 3766 CD1 TRP B 161 -32.349 30.185 33.800 1.00 20.25 C ANISOU 3766 CD1 TRP B 161 2099 2885 2709 -101 415 -282 C ATOM 3767 CD2 TRP B 161 -32.737 30.988 35.853 1.00 28.35 C ANISOU 3767 CD2 TRP B 161 3149 3852 3773 -88 458 -250 C ATOM 3768 NE1 TRP B 161 -31.984 31.511 33.808 1.00 27.42 N ANISOU 3768 NE1 TRP B 161 3032 3784 3603 -54 412 -237 N ATOM 3769 CE2 TRP B 161 -32.214 32.028 35.055 1.00 26.46 C ANISOU 3769 CE2 TRP B 161 2925 3625 3505 -47 438 -219 C ATOM 3770 CE3 TRP B 161 -33.059 31.258 37.188 1.00 19.92 C ANISOU 3770 CE3 TRP B 161 2091 2749 2728 -86 488 -238 C ATOM 3771 CZ2 TRP B 161 -32.004 33.317 35.548 1.00 27.13 C ANISOU 3771 CZ2 TRP B 161 3034 3684 3590 -8 448 -181 C ATOM 3772 CZ3 TRP B 161 -32.852 32.538 37.676 1.00 19.79 C ANISOU 3772 CZ3 TRP B 161 2100 2712 2707 -46 494 -203 C ATOM 3773 CH2 TRP B 161 -32.328 33.552 36.857 1.00 29.83 C ANISOU 3773 CH2 TRP B 161 3386 3992 3956 -9 475 -176 C ATOM 3774 N VAL B 162 -33.289 25.344 36.219 1.00 20.51 N ANISOU 3774 N VAL B 162 2100 2815 2878 -289 522 -403 N ATOM 3775 CA VAL B 162 -33.876 24.247 36.985 1.00 20.74 C ANISOU 3775 CA VAL B 162 2110 2816 2953 -330 561 -427 C ATOM 3776 C VAL B 162 -32.829 23.615 37.895 1.00 26.26 C ANISOU 3776 C VAL B 162 2866 3448 3664 -344 599 -407 C ATOM 3777 O VAL B 162 -33.082 23.359 39.079 1.00 20.35 O ANISOU 3777 O VAL B 162 2126 2665 2942 -350 639 -392 O ATOM 3778 CB VAL B 162 -34.505 23.208 36.040 1.00 26.88 C ANISOU 3778 CB VAL B 162 2837 3627 3750 -372 551 -486 C ATOM 3779 CG1 VAL B 162 -35.004 22.006 36.822 1.00 28.56 C ANISOU 3779 CG1 VAL B 162 3033 3800 4018 -419 600 -510 C ATOM 3780 CG2 VAL B 162 -35.638 23.831 35.250 1.00 29.67 C ANISOU 3780 CG2 VAL B 162 3128 4056 4090 -354 514 -506 C ATOM 3781 N MET B 163 -31.633 23.361 37.358 1.00 22.52 N ANISOU 3781 N MET B 163 2431 2957 3169 -347 587 -404 N ATOM 3782 CA MET B 163 -30.586 22.730 38.155 1.00 21.80 C ANISOU 3782 CA MET B 163 2391 2806 3085 -357 621 -384 C ATOM 3783 C MET B 163 -30.053 23.679 39.220 1.00 27.97 C ANISOU 3783 C MET B 163 3214 3564 3851 -320 629 -338 C ATOM 3784 O MET B 163 -29.779 23.259 40.351 1.00 21.96 O ANISOU 3784 O MET B 163 2477 2762 3103 -323 667 -320 O ATOM 3785 CB MET B 163 -29.452 22.245 37.253 1.00 23.85 C ANISOU 3785 CB MET B 163 2679 3058 3326 -367 605 -394 C ATOM 3786 CG MET B 163 -29.859 21.157 36.274 1.00 23.73 C ANISOU 3786 CG MET B 163 2628 3059 3328 -407 601 -446 C ATOM 3787 SD MET B 163 -30.587 19.705 37.067 1.00 27.33 S ANISOU 3787 SD MET B 163 3063 3475 3847 -456 659 -474 S ATOM 3788 CE MET B 163 -29.255 19.173 38.140 1.00 33.14 C ANISOU 3788 CE MET B 163 3867 4139 4586 -451 702 -432 C ATOM 3789 N ALA B 164 -29.896 24.959 38.879 1.00 19.19 N ANISOU 3789 N ALA B 164 2107 2476 2709 -284 596 -318 N ATOM 3790 CA ALA B 164 -29.421 25.929 39.859 1.00 28.64 C ANISOU 3790 CA ALA B 164 3339 3650 3892 -250 603 -281 C ATOM 3791 C ALA B 164 -30.415 26.088 41.003 1.00 28.80 C ANISOU 3791 C ALA B 164 3342 3666 3933 -244 632 -274 C ATOM 3792 O ALA B 164 -30.020 26.149 42.173 1.00 24.99 O ANISOU 3792 O ALA B 164 2891 3152 3452 -233 658 -254 O ATOM 3793 CB ALA B 164 -29.156 27.273 39.184 1.00 18.76 C ANISOU 3793 CB ALA B 164 2093 2423 2614 -214 567 -263 C ATOM 3794 N LEU B 165 -31.711 26.151 40.684 1.00 23.98 N ANISOU 3794 N LEU B 165 2681 3093 3340 -248 628 -293 N ATOM 3795 CA LEU B 165 -32.726 26.250 41.729 1.00 24.19 C ANISOU 3795 CA LEU B 165 2686 3117 3388 -243 658 -287 C ATOM 3796 C LEU B 165 -32.750 24.996 42.594 1.00 26.97 C ANISOU 3796 C LEU B 165 3046 3433 3771 -273 706 -292 C ATOM 3797 O LEU B 165 -32.957 25.077 43.809 1.00 22.83 O ANISOU 3797 O LEU B 165 2534 2888 3254 -260 739 -271 O ATOM 3798 CB LEU B 165 -34.099 26.507 41.110 1.00 25.69 C ANISOU 3798 CB LEU B 165 2814 3357 3591 -243 642 -308 C ATOM 3799 CG LEU B 165 -34.360 27.947 40.666 1.00 20.50 C ANISOU 3799 CG LEU B 165 2147 2734 2907 -199 609 -290 C ATOM 3800 CD1 LEU B 165 -35.575 28.022 39.754 1.00 27.49 C ANISOU 3800 CD1 LEU B 165 2968 3679 3798 -201 586 -315 C ATOM 3801 CD2 LEU B 165 -34.551 28.845 41.874 1.00 22.50 C ANISOU 3801 CD2 LEU B 165 2420 2968 3160 -166 630 -261 C ATOM 3802 N ALA B 166 -32.529 23.825 41.989 1.00 19.89 N ANISOU 3802 N ALA B 166 2142 2526 2891 -312 712 -317 N ATOM 3803 CA ALA B 166 -32.468 22.588 42.759 1.00 20.59 C ANISOU 3803 CA ALA B 166 2240 2573 3011 -339 763 -318 C ATOM 3804 C ALA B 166 -31.333 22.604 43.776 1.00 32.10 C ANISOU 3804 C ALA B 166 3757 3991 4448 -317 785 -281 C ATOM 3805 O ALA B 166 -31.351 21.810 44.723 1.00 24.94 O ANISOU 3805 O ALA B 166 2863 3052 3562 -324 833 -268 O ATOM 3806 CB ALA B 166 -32.313 21.389 41.821 1.00 26.58 C ANISOU 3806 CB ALA B 166 2983 3325 3790 -383 764 -354 C ATOM 3807 N CYS B 167 -30.349 23.485 43.595 1.00 30.27 N ANISOU 3807 N CYS B 167 3561 3763 4179 -290 752 -264 N ATOM 3808 CA CYS B 167 -29.239 23.664 44.522 1.00 21.28 C ANISOU 3808 CA CYS B 167 2474 2596 3016 -266 764 -234 C ATOM 3809 C CYS B 167 -29.416 24.864 45.444 1.00 33.25 C ANISOU 3809 C CYS B 167 4002 4119 4513 -226 761 -213 C ATOM 3810 O CYS B 167 -29.176 24.754 46.648 1.00 23.58 O ANISOU 3810 O CYS B 167 2802 2876 3282 -209 791 -193 O ATOM 3811 CB CYS B 167 -27.926 23.816 43.747 1.00 25.60 C ANISOU 3811 CB CYS B 167 3052 3137 3536 -264 731 -232 C ATOM 3812 SG CYS B 167 -26.471 24.067 44.791 1.00 24.59 S ANISOU 3812 SG CYS B 167 2982 2981 3378 -235 740 -201 S ATOM 3813 N ALA B 168 -29.836 26.013 44.904 1.00 31.28 N ANISOU 3813 N ALA B 168 3735 3898 4254 -209 726 -217 N ATOM 3814 CA ALA B 168 -29.928 27.232 45.700 1.00 25.95 C ANISOU 3814 CA ALA B 168 3072 3226 3561 -171 723 -200 C ATOM 3815 C ALA B 168 -31.157 27.265 46.604 1.00 27.76 C ANISOU 3815 C ALA B 168 3276 3462 3808 -162 754 -197 C ATOM 3816 O ALA B 168 -31.093 27.837 47.699 1.00 26.75 O ANISOU 3816 O ALA B 168 3169 3326 3668 -133 770 -182 O ATOM 3817 CB ALA B 168 -29.930 28.456 44.778 1.00 25.35 C ANISOU 3817 CB ALA B 168 2988 3173 3473 -152 680 -202 C ATOM 3818 N ALA B 169 -32.274 26.677 46.173 1.00 21.82 N ANISOU 3818 N ALA B 169 2478 2728 3087 -186 765 -213 N ATOM 3819 CA ALA B 169 -33.565 26.840 46.843 1.00 28.55 C ANISOU 3819 CA ALA B 169 3296 3592 3958 -177 792 -211 C ATOM 3820 C ALA B 169 -33.765 26.011 48.115 1.00 19.93 C ANISOU 3820 C ALA B 169 2215 2476 2882 -180 847 -197 C ATOM 3821 O ALA B 169 -34.353 26.528 49.073 1.00 20.08 O ANISOU 3821 O ALA B 169 2232 2498 2899 -153 869 -183 O ATOM 3822 CB ALA B 169 -34.706 26.536 45.868 1.00 22.03 C ANISOU 3822 CB ALA B 169 2410 2799 3160 -202 781 -237 C ATOM 3823 N PRO B 170 -33.345 24.744 48.175 1.00 26.45 N ANISOU 3823 N PRO B 170 3051 3276 3724 -208 875 -199 N ATOM 3824 CA PRO B 170 -33.627 23.923 49.377 1.00 20.21 C ANISOU 3824 CA PRO B 170 2268 2461 2951 -207 935 -180 C ATOM 3825 C PRO B 170 -33.142 24.562 50.671 1.00 26.62 C ANISOU 3825 C PRO B 170 3121 3266 3726 -161 949 -151 C ATOM 3826 O PRO B 170 -33.836 24.460 51.695 1.00 20.39 O ANISOU 3826 O PRO B 170 2326 2475 2945 -144 991 -135 O ATOM 3827 CB PRO B 170 -32.887 22.609 49.086 1.00 24.39 C ANISOU 3827 CB PRO B 170 2813 2959 3494 -238 955 -182 C ATOM 3828 CG PRO B 170 -32.932 22.503 47.615 1.00 34.15 C ANISOU 3828 CG PRO B 170 4022 4211 4742 -271 914 -216 C ATOM 3829 CD PRO B 170 -32.784 23.910 47.092 1.00 20.57 C ANISOU 3829 CD PRO B 170 2304 2523 2989 -244 859 -219 C ATOM 3830 N PRO B 171 -31.974 25.222 50.699 1.00 19.69 N ANISOU 3830 N PRO B 171 2285 2387 2809 -139 916 -146 N ATOM 3831 CA PRO B 171 -31.568 25.886 51.952 1.00 26.19 C ANISOU 3831 CA PRO B 171 3143 3210 3597 -96 927 -127 C ATOM 3832 C PRO B 171 -32.508 26.996 52.391 1.00 29.87 C ANISOU 3832 C PRO B 171 3591 3696 4060 -68 924 -128 C ATOM 3833 O PRO B 171 -32.464 27.398 53.560 1.00 27.57 O ANISOU 3833 O PRO B 171 3323 3408 3746 -32 944 -115 O ATOM 3834 CB PRO B 171 -30.170 26.429 51.628 1.00 26.17 C ANISOU 3834 CB PRO B 171 3179 3204 3561 -86 885 -130 C ATOM 3835 CG PRO B 171 -29.674 25.547 50.564 1.00 26.96 C ANISOU 3835 CG PRO B 171 3275 3292 3677 -123 874 -139 C ATOM 3836 CD PRO B 171 -30.869 25.251 49.720 1.00 27.01 C ANISOU 3836 CD PRO B 171 3232 3310 3721 -153 875 -156 C ATOM 3837 N LEU B 172 -33.348 27.512 51.493 1.00 22.15 N ANISOU 3837 N LEU B 172 2575 2738 3104 -80 900 -144 N ATOM 3838 CA LEU B 172 -34.356 28.480 51.900 1.00 35.54 C ANISOU 3838 CA LEU B 172 4250 4453 4801 -52 903 -143 C ATOM 3839 C LEU B 172 -35.517 27.833 52.644 1.00 20.52 C ANISOU 3839 C LEU B 172 2318 2553 2925 -54 955 -133 C ATOM 3840 O LEU B 172 -36.205 28.523 53.404 1.00 27.32 O ANISOU 3840 O LEU B 172 3173 3426 3781 -23 971 -125 O ATOM 3841 CB LEU B 172 -34.891 29.237 50.682 1.00 27.03 C ANISOU 3841 CB LEU B 172 3137 3398 3734 -59 862 -158 C ATOM 3842 CG LEU B 172 -33.937 30.154 49.917 1.00 23.81 C ANISOU 3842 CG LEU B 172 2753 2990 3303 -49 814 -164 C ATOM 3843 CD1 LEU B 172 -34.608 30.652 48.647 1.00 33.00 C ANISOU 3843 CD1 LEU B 172 3876 4182 4480 -55 781 -174 C ATOM 3844 CD2 LEU B 172 -33.514 31.322 50.778 1.00 21.90 C ANISOU 3844 CD2 LEU B 172 2545 2740 3035 -8 810 -157 C ATOM 3845 N VAL B 173 -35.753 26.534 52.450 1.00 24.28 N ANISOU 3845 N VAL B 173 2774 3016 3433 -90 985 -133 N ATOM 3846 CA VAL B 173 -37.012 25.935 52.885 1.00 30.41 C ANISOU 3846 CA VAL B 173 3511 3796 4249 -100 1033 -128 C ATOM 3847 C VAL B 173 -36.832 24.653 53.696 1.00 26.40 C ANISOU 3847 C VAL B 173 3017 3257 3755 -110 1093 -108 C ATOM 3848 O VAL B 173 -37.749 23.827 53.763 1.00 32.85 O ANISOU 3848 O VAL B 173 3796 4067 4618 -135 1136 -108 O ATOM 3849 CB VAL B 173 -37.922 25.675 51.669 1.00 28.35 C ANISOU 3849 CB VAL B 173 3190 3554 4029 -140 1015 -156 C ATOM 3850 CG1 VAL B 173 -38.387 26.990 51.055 1.00 22.70 C ANISOU 3850 CG1 VAL B 173 2452 2874 3300 -119 968 -167 C ATOM 3851 CG2 VAL B 173 -37.196 24.829 50.639 1.00 21.35 C ANISOU 3851 CG2 VAL B 173 2306 2655 3153 -181 994 -175 C ATOM 3852 N GLY B 174 -35.668 24.462 54.314 1.00 24.31 N ANISOU 3852 N GLY B 174 2806 2976 3455 -90 1099 -90 N ATOM 3853 CA GLY B 174 -35.519 23.417 55.322 1.00 37.04 C ANISOU 3853 CA GLY B 174 4438 4564 5072 -82 1162 -60 C ATOM 3854 C GLY B 174 -34.503 22.323 55.036 1.00 32.27 C ANISOU 3854 C GLY B 174 3859 3930 4471 -104 1172 -54 C ATOM 3855 O GLY B 174 -34.366 21.412 55.867 1.00 30.32 O ANISOU 3855 O GLY B 174 3629 3661 4229 -94 1229 -25 O ATOM 3856 N TRP B 175 -33.786 22.329 53.915 1.00 29.66 N ANISOU 3856 N TRP B 175 3534 3598 4139 -130 1124 -78 N ATOM 3857 CA TRP B 175 -32.715 21.366 53.668 1.00 30.14 C ANISOU 3857 CA TRP B 175 3622 3631 4197 -146 1132 -71 C ATOM 3858 C TRP B 175 -31.402 22.134 53.627 1.00 22.74 C ANISOU 3858 C TRP B 175 2729 2705 3206 -120 1083 -71 C ATOM 3859 O TRP B 175 -31.137 22.860 52.663 1.00 32.48 O ANISOU 3859 O TRP B 175 3956 3952 4431 -132 1027 -95 O ATOM 3860 CB TRP B 175 -32.939 20.593 52.372 1.00 23.17 C ANISOU 3860 CB TRP B 175 2708 2735 3360 -201 1123 -101 C ATOM 3861 CG TRP B 175 -32.112 19.347 52.291 1.00 24.08 C ANISOU 3861 CG TRP B 175 2847 2814 3488 -219 1154 -90 C ATOM 3862 CD1 TRP B 175 -31.502 18.701 53.327 1.00 23.89 C ANISOU 3862 CD1 TRP B 175 2861 2768 3449 -192 1202 -52 C ATOM 3863 CD2 TRP B 175 -31.800 18.598 51.113 1.00 30.52 C ANISOU 3863 CD2 TRP B 175 3652 3613 4331 -264 1140 -118 C ATOM 3864 NE1 TRP B 175 -30.832 17.593 52.866 1.00 25.88 N ANISOU 3864 NE1 TRP B 175 3126 2986 3720 -217 1222 -51 N ATOM 3865 CE2 TRP B 175 -31.001 17.507 51.509 1.00 24.14 C ANISOU 3865 CE2 TRP B 175 2878 2768 3528 -263 1184 -94 C ATOM 3866 CE3 TRP B 175 -32.123 18.742 49.761 1.00 22.29 C ANISOU 3866 CE3 TRP B 175 2575 2586 3307 -302 1096 -161 C ATOM 3867 CZ2 TRP B 175 -30.518 16.567 50.601 1.00 25.34 C ANISOU 3867 CZ2 TRP B 175 3030 2893 3706 -301 1186 -113 C ATOM 3868 CZ3 TRP B 175 -31.645 17.809 48.864 1.00 29.21 C ANISOU 3868 CZ3 TRP B 175 3452 3440 4207 -339 1095 -182 C ATOM 3869 CH2 TRP B 175 -30.852 16.735 49.286 1.00 21.56 C ANISOU 3869 CH2 TRP B 175 2518 2430 3246 -340 1141 -159 C ATOM 3870 N SER B 176 -30.581 21.949 54.665 1.00 28.14 N ANISOU 3870 N SER B 176 3454 3384 3853 -84 1105 -43 N ATOM 3871 CA SER B 176 -29.433 22.803 54.957 1.00 19.93 C ANISOU 3871 CA SER B 176 2452 2360 2759 -52 1064 -43 C ATOM 3872 C SER B 176 -29.914 24.226 55.220 1.00 26.99 C ANISOU 3872 C SER B 176 3340 3282 3635 -27 1033 -57 C ATOM 3873 O SER B 176 -31.110 24.447 55.442 1.00 27.04 O ANISOU 3873 O SER B 176 3316 3295 3662 -26 1053 -57 O ATOM 3874 CB SER B 176 -28.403 22.770 53.825 1.00 22.11 C ANISOU 3874 CB SER B 176 2740 2629 3032 -77 1017 -60 C ATOM 3875 OG SER B 176 -27.196 23.398 54.221 1.00 22.58 O ANISOU 3875 OG SER B 176 2836 2700 3044 -47 987 -57 O ATOM 3876 N ARG B 177 -29.001 25.193 55.209 1.00 26.56 N ANISOU 3876 N ARG B 177 3309 3239 3542 -7 987 -69 N ATOM 3877 CA ARG B 177 -29.359 26.571 55.515 1.00 19.56 C ANISOU 3877 CA ARG B 177 2421 2372 2638 18 961 -83 C ATOM 3878 C ARG B 177 -28.210 27.484 55.120 1.00 25.06 C ANISOU 3878 C ARG B 177 3141 3072 3308 24 908 -101 C ATOM 3879 O ARG B 177 -27.050 27.062 55.091 1.00 19.03 O ANISOU 3879 O ARG B 177 2402 2302 2526 23 898 -98 O ATOM 3880 CB ARG B 177 -29.680 26.745 57.004 1.00 24.06 C ANISOU 3880 CB ARG B 177 3004 2956 3180 63 998 -67 C ATOM 3881 CG ARG B 177 -28.551 26.318 57.920 1.00 26.62 C ANISOU 3881 CG ARG B 177 3369 3286 3462 92 1009 -52 C ATOM 3882 CD ARG B 177 -28.946 26.440 59.380 1.00 27.94 C ANISOU 3882 CD ARG B 177 3548 3472 3596 140 1047 -36 C ATOM 3883 NE ARG B 177 -27.886 25.961 60.256 1.00 33.29 N ANISOU 3883 NE ARG B 177 4260 4161 4228 173 1059 -19 N ATOM 3884 CZ ARG B 177 -27.886 26.105 61.573 1.00 24.03 C ANISOU 3884 CZ ARG B 177 3106 3014 3011 224 1084 -7 C ATOM 3885 NH1 ARG B 177 -28.877 26.718 62.200 1.00 21.72 N ANISOU 3885 NH1 ARG B 177 2802 2734 2715 246 1102 -10 N ATOM 3886 NH2 ARG B 177 -26.865 25.627 62.279 1.00 27.62 N ANISOU 3886 NH2 ARG B 177 3589 3485 3421 255 1091 8 N ATOM 3887 N TYR B 178 -28.546 28.737 54.818 1.00 24.70 N ANISOU 3887 N TYR B 178 3085 3035 3264 32 877 -120 N ATOM 3888 CA TYR B 178 -27.530 29.748 54.568 1.00 18.89 C ANISOU 3888 CA TYR B 178 2370 2299 2508 40 833 -138 C ATOM 3889 C TYR B 178 -27.051 30.330 55.889 1.00 20.24 C ANISOU 3889 C TYR B 178 2569 2482 2641 81 838 -144 C ATOM 3890 O TYR B 178 -27.838 30.531 56.819 1.00 20.87 O ANISOU 3890 O TYR B 178 2645 2572 2711 107 866 -140 O ATOM 3891 CB TYR B 178 -28.068 30.846 53.655 1.00 18.82 C ANISOU 3891 CB TYR B 178 2340 2290 2521 34 803 -153 C ATOM 3892 CG TYR B 178 -28.316 30.354 52.253 1.00 18.69 C ANISOU 3892 CG TYR B 178 2298 2270 2534 -3 789 -152 C ATOM 3893 CD1 TYR B 178 -27.258 30.076 51.400 1.00 25.40 C ANISOU 3893 CD1 TYR B 178 3161 3110 3381 -23 763 -155 C ATOM 3894 CD2 TYR B 178 -29.608 30.150 51.787 1.00 28.03 C ANISOU 3894 CD2 TYR B 178 3442 3463 3745 -15 801 -151 C ATOM 3895 CE1 TYR B 178 -27.478 29.618 50.119 1.00 18.33 C ANISOU 3895 CE1 TYR B 178 2242 2215 2507 -54 749 -157 C ATOM 3896 CE2 TYR B 178 -29.840 29.696 50.508 1.00 25.28 C ANISOU 3896 CE2 TYR B 178 3068 3118 3419 -47 785 -156 C ATOM 3897 CZ TYR B 178 -28.773 29.429 49.678 1.00 18.55 C ANISOU 3897 CZ TYR B 178 2232 2256 2561 -66 759 -159 C ATOM 3898 OH TYR B 178 -29.004 28.971 48.401 1.00 21.02 O ANISOU 3898 OH TYR B 178 2520 2576 2892 -95 743 -167 O ATOM 3899 N ILE B 179 -25.750 30.583 55.974 1.00 18.84 N ANISOU 3899 N ILE B 179 2417 2304 2439 86 811 -155 N ATOM 3900 CA ILE B 179 -25.125 30.879 57.259 1.00 19.01 C ANISOU 3900 CA ILE B 179 2464 2342 2418 123 815 -163 C ATOM 3901 C ILE B 179 -23.933 31.804 57.025 1.00 18.83 C ANISOU 3901 C ILE B 179 2456 2316 2383 123 771 -192 C ATOM 3902 O ILE B 179 -23.222 31.656 56.020 1.00 21.43 O ANISOU 3902 O ILE B 179 2784 2631 2728 95 747 -192 O ATOM 3903 CB ILE B 179 -24.736 29.571 57.974 1.00 19.14 C ANISOU 3903 CB ILE B 179 2494 2368 2409 135 848 -137 C ATOM 3904 CG1 ILE B 179 -24.480 29.793 59.466 1.00 19.45 C ANISOU 3904 CG1 ILE B 179 2554 2436 2399 183 862 -141 C ATOM 3905 CG2 ILE B 179 -23.538 28.913 57.306 1.00 22.75 C ANISOU 3905 CG2 ILE B 179 2963 2816 2865 114 829 -132 C ATOM 3906 CD1 ILE B 179 -24.449 28.506 60.263 1.00 19.68 C ANISOU 3906 CD1 ILE B 179 2595 2478 2406 204 908 -105 C ATOM 3907 N PRO B 180 -23.701 32.793 57.890 1.00 19.02 N ANISOU 3907 N PRO B 180 2492 2352 2383 151 761 -219 N ATOM 3908 CA PRO B 180 -22.570 33.706 57.677 1.00 18.91 C ANISOU 3908 CA PRO B 180 2488 2331 2366 147 721 -250 C ATOM 3909 C PRO B 180 -21.234 32.980 57.772 1.00 19.97 C ANISOU 3909 C PRO B 180 2637 2476 2476 144 709 -247 C ATOM 3910 O PRO B 180 -21.093 31.983 58.484 1.00 24.88 O ANISOU 3910 O PRO B 180 3268 3118 3067 161 732 -227 O ATOM 3911 CB PRO B 180 -22.732 34.738 58.798 1.00 26.50 C ANISOU 3911 CB PRO B 180 3458 3307 3305 182 721 -283 C ATOM 3912 CG PRO B 180 -24.179 34.660 59.179 1.00 20.30 C ANISOU 3912 CG PRO B 180 2661 2526 2525 197 756 -266 C ATOM 3913 CD PRO B 180 -24.568 33.232 58.997 1.00 19.38 C ANISOU 3913 CD PRO B 180 2537 2414 2411 186 785 -225 C ATOM 3914 N GLU B 181 -20.246 33.489 57.036 1.00 18.59 N ANISOU 3914 N GLU B 181 2463 2285 2314 123 675 -265 N ATOM 3915 CA GLU B 181 -18.934 32.857 56.969 1.00 19.08 C ANISOU 3915 CA GLU B 181 2536 2356 2359 117 660 -262 C ATOM 3916 C GLU B 181 -17.841 33.901 57.132 1.00 18.52 C ANISOU 3916 C GLU B 181 2469 2286 2284 119 625 -302 C ATOM 3917 O GLU B 181 -18.062 35.097 56.935 1.00 18.59 O ANISOU 3917 O GLU B 181 2471 2276 2315 114 612 -329 O ATOM 3918 CB GLU B 181 -18.707 32.124 55.643 1.00 25.62 C ANISOU 3918 CB GLU B 181 3357 3162 3215 82 656 -236 C ATOM 3919 CG GLU B 181 -19.882 31.320 55.138 1.00 18.06 C ANISOU 3919 CG GLU B 181 2388 2196 2279 69 684 -206 C ATOM 3920 CD GLU B 181 -19.501 30.464 53.955 1.00 17.79 C ANISOU 3920 CD GLU B 181 2349 2145 2264 37 681 -186 C ATOM 3921 OE1 GLU B 181 -18.840 29.427 54.166 1.00 19.55 O ANISOU 3921 OE1 GLU B 181 2584 2375 2470 39 692 -169 O ATOM 3922 OE2 GLU B 181 -19.833 30.845 52.813 1.00 26.92 O ANISOU 3922 OE2 GLU B 181 3492 3284 3451 13 666 -187 O ATOM 3923 N GLY B 182 -16.643 33.419 57.455 1.00 18.54 N ANISOU 3923 N GLY B 182 2478 2308 2258 124 612 -306 N ATOM 3924 CA GLY B 182 -15.495 34.306 57.552 1.00 18.62 C ANISOU 3924 CA GLY B 182 2487 2320 2268 121 578 -347 C ATOM 3925 C GLY B 182 -15.702 35.365 58.612 1.00 21.22 C ANISOU 3925 C GLY B 182 2817 2664 2581 146 572 -393 C ATOM 3926 O GLY B 182 -16.041 35.069 59.765 1.00 19.79 O ANISOU 3926 O GLY B 182 2644 2518 2357 181 587 -395 O ATOM 3927 N MET B 183 -15.498 36.625 58.221 1.00 23.71 N ANISOU 3927 N MET B 183 3126 2951 2932 129 553 -428 N ATOM 3928 CA MET B 183 -15.760 37.794 59.055 1.00 23.18 C ANISOU 3928 CA MET B 183 3059 2886 2862 147 549 -477 C ATOM 3929 C MET B 183 -17.264 38.073 59.227 1.00 23.79 C ANISOU 3929 C MET B 183 3138 2954 2948 161 577 -464 C ATOM 3930 O MET B 183 -17.598 39.128 59.783 1.00 21.48 O ANISOU 3930 O MET B 183 2846 2655 2661 175 577 -503 O ATOM 3931 CB MET B 183 -15.055 39.019 58.472 1.00 20.78 C ANISOU 3931 CB MET B 183 2746 2546 2604 121 526 -516 C ATOM 3932 CG MET B 183 -13.531 38.906 58.446 1.00 25.39 C ANISOU 3932 CG MET B 183 3324 3142 3181 108 497 -539 C ATOM 3933 SD MET B 183 -12.739 40.173 57.426 1.00 22.73 S ANISOU 3933 SD MET B 183 2974 2750 2913 69 479 -569 S ATOM 3934 CE MET B 183 -13.410 41.663 58.156 1.00 21.30 C ANISOU 3934 CE MET B 183 2793 2548 2752 82 487 -625 C ATOM 3935 N GLN B 184 -18.101 37.151 58.740 1.00 25.26 N ANISOU 3935 N GLN B 184 3323 3137 3138 157 600 -414 N ATOM 3936 CA GLN B 184 -19.553 37.126 58.937 1.00 29.63 C ANISOU 3936 CA GLN B 184 3873 3689 3695 172 630 -394 C ATOM 3937 C GLN B 184 -20.292 38.148 58.083 1.00 25.34 C ANISOU 3937 C GLN B 184 3319 3106 3201 157 630 -397 C ATOM 3938 O GLN B 184 -21.393 38.574 58.450 1.00 22.90 O ANISOU 3938 O GLN B 184 3007 2797 2897 175 650 -397 O ATOM 3939 CB GLN B 184 -19.936 37.329 60.408 1.00 20.84 C ANISOU 3939 CB GLN B 184 2769 2610 2539 213 644 -417 C ATOM 3940 CG GLN B 184 -19.286 36.342 61.373 1.00 25.53 C ANISOU 3940 CG GLN B 184 3374 3250 3076 239 648 -411 C ATOM 3941 CD GLN B 184 -19.669 34.903 61.089 1.00 19.71 C ANISOU 3941 CD GLN B 184 2636 2518 2332 236 676 -353 C ATOM 3942 OE1 GLN B 184 -20.814 34.504 61.291 1.00 21.83 O ANISOU 3942 OE1 GLN B 184 2903 2789 2604 247 709 -325 O ATOM 3943 NE2 GLN B 184 -18.707 34.115 60.623 1.00 19.48 N ANISOU 3943 NE2 GLN B 184 2610 2492 2300 220 664 -336 N ATOM 3944 N CYS B 185 -19.730 38.570 56.952 1.00 30.67 N ANISOU 3944 N CYS B 185 3989 3751 3915 128 611 -396 N ATOM 3945 CA CYS B 185 -20.376 39.570 56.109 1.00 32.08 C ANISOU 3945 CA CYS B 185 4157 3893 4139 120 613 -394 C ATOM 3946 C CYS B 185 -20.798 39.025 54.748 1.00 31.48 C ANISOU 3946 C CYS B 185 4068 3804 4087 97 615 -350 C ATOM 3947 O CYS B 185 -21.190 39.805 53.873 1.00 18.70 O ANISOU 3947 O CYS B 185 2440 2159 2505 92 614 -343 O ATOM 3948 CB CYS B 185 -19.464 40.787 55.939 1.00 19.18 C ANISOU 3948 CB CYS B 185 2526 2229 2533 111 594 -432 C ATOM 3949 SG CYS B 185 -19.329 41.780 57.443 1.00 29.26 S ANISOU 3949 SG CYS B 185 3812 3515 3791 138 595 -495 S ATOM 3950 N SER B 186 -20.721 37.713 54.546 1.00 18.49 N ANISOU 3950 N SER B 186 2423 2179 2425 87 619 -322 N ATOM 3951 CA SER B 186 -21.359 37.049 53.420 1.00 18.26 C ANISOU 3951 CA SER B 186 2379 2146 2414 68 624 -286 C ATOM 3952 C SER B 186 -21.844 35.692 53.907 1.00 18.24 C ANISOU 3952 C SER B 186 2376 2169 2387 71 646 -264 C ATOM 3953 O SER B 186 -21.463 35.227 54.984 1.00 28.58 O ANISOU 3953 O SER B 186 3699 3498 3664 87 654 -271 O ATOM 3954 CB SER B 186 -20.419 36.912 52.217 1.00 20.50 C ANISOU 3954 CB SER B 186 2662 2413 2715 42 603 -276 C ATOM 3955 OG SER B 186 -19.293 36.115 52.528 1.00 19.32 O ANISOU 3955 OG SER B 186 2525 2275 2542 34 595 -278 O ATOM 3956 N CYS B 187 -22.703 35.056 53.123 1.00 18.14 N ANISOU 3956 N CYS B 187 2346 2156 2391 56 657 -238 N ATOM 3957 CA CYS B 187 -23.320 33.817 53.565 1.00 21.05 C ANISOU 3957 CA CYS B 187 2710 2542 2747 57 684 -218 C ATOM 3958 C CYS B 187 -23.112 32.708 52.546 1.00 17.97 C ANISOU 3958 C CYS B 187 2312 2147 2367 26 683 -198 C ATOM 3959 O CYS B 187 -23.009 32.953 51.341 1.00 21.99 O ANISOU 3959 O CYS B 187 2812 2646 2898 7 663 -195 O ATOM 3960 CB CYS B 187 -24.809 34.014 53.848 1.00 18.43 C ANISOU 3960 CB CYS B 187 2358 2217 2425 70 708 -212 C ATOM 3961 SG CYS B 187 -25.087 34.819 55.430 1.00 22.91 S ANISOU 3961 SG CYS B 187 2940 2797 2967 111 724 -232 S ATOM 3962 N GLY B 188 -23.037 31.484 53.057 1.00 18.00 N ANISOU 3962 N GLY B 188 2323 2160 2357 25 706 -182 N ATOM 3963 CA GLY B 188 -22.931 30.301 52.228 1.00 30.12 C ANISOU 3963 CA GLY B 188 3851 3689 3904 -3 713 -166 C ATOM 3964 C GLY B 188 -23.707 29.145 52.822 1.00 24.15 C ANISOU 3964 C GLY B 188 3089 2938 3149 -2 755 -147 C ATOM 3965 O GLY B 188 -24.571 29.351 53.677 1.00 19.33 O ANISOU 3965 O GLY B 188 2473 2338 2535 18 778 -145 O ATOM 3966 N ILE B 189 -23.418 27.931 52.374 1.00 21.24 N ANISOU 3966 N ILE B 189 2722 2561 2789 -23 769 -133 N ATOM 3967 CA ILE B 189 -24.063 26.738 52.910 1.00 24.17 C ANISOU 3967 CA ILE B 189 3087 2929 3167 -25 815 -114 C ATOM 3968 C ILE B 189 -23.429 26.386 54.250 1.00 28.10 C ANISOU 3968 C ILE B 189 3611 3436 3628 10 838 -99 C ATOM 3969 O ILE B 189 -22.274 26.729 54.525 1.00 21.50 O ANISOU 3969 O ILE B 189 2797 2608 2763 25 815 -105 O ATOM 3970 CB ILE B 189 -23.967 25.584 51.889 1.00 25.73 C ANISOU 3970 CB ILE B 189 3276 3109 3391 -62 823 -108 C ATOM 3971 CG1 ILE B 189 -24.753 25.937 50.627 1.00 29.40 C ANISOU 3971 CG1 ILE B 189 3709 3575 3887 -90 801 -125 C ATOM 3972 CG2 ILE B 189 -24.490 24.274 52.458 1.00 18.42 C ANISOU 3972 CG2 ILE B 189 2347 2173 2479 -65 878 -87 C ATOM 3973 CD1 ILE B 189 -26.207 26.241 50.896 1.00 19.17 C ANISOU 3973 CD1 ILE B 189 2384 2290 2610 -87 819 -128 C ATOM 3974 N ASP B 190 -24.197 25.723 55.113 1.00 22.51 N ANISOU 3974 N ASP B 190 2900 2730 2920 24 885 -80 N ATOM 3975 CA ASP B 190 -23.721 25.359 56.446 1.00 28.26 C ANISOU 3975 CA ASP B 190 3653 3475 3610 65 913 -60 C ATOM 3976 C ASP B 190 -22.839 24.121 56.342 1.00 21.67 C ANISOU 3976 C ASP B 190 2835 2628 2771 60 932 -37 C ATOM 3977 O ASP B 190 -23.328 22.989 56.343 1.00 21.62 O ANISOU 3977 O ASP B 190 2824 2604 2789 49 978 -14 O ATOM 3978 CB ASP B 190 -24.896 25.125 57.391 1.00 29.84 C ANISOU 3978 CB ASP B 190 3844 3682 3813 86 961 -43 C ATOM 3979 CG ASP B 190 -24.471 25.033 58.851 1.00 23.36 C ANISOU 3979 CG ASP B 190 3048 2886 2941 138 985 -26 C ATOM 3980 OD1 ASP B 190 -23.252 25.043 59.130 1.00 19.48 O ANISOU 3980 OD1 ASP B 190 2580 2409 2413 157 964 -28 O ATOM 3981 OD2 ASP B 190 -25.366 24.955 59.722 1.00 27.35 O ANISOU 3981 OD2 ASP B 190 3550 3401 3442 163 1024 -11 O ATOM 3982 N TYR B 191 -21.529 24.338 56.253 1.00 32.40 N ANISOU 3982 N TYR B 191 4214 3996 4103 68 899 -44 N ATOM 3983 CA TYR B 191 -20.550 23.271 56.408 1.00 24.85 C ANISOU 3983 CA TYR B 191 3276 3036 3131 77 917 -20 C ATOM 3984 C TYR B 191 -20.016 23.181 57.829 1.00 27.84 C ANISOU 3984 C TYR B 191 3676 3446 3456 130 935 -2 C ATOM 3985 O TYR B 191 -19.131 22.362 58.096 1.00 25.40 O ANISOU 3985 O TYR B 191 3384 3141 3126 148 950 21 O ATOM 3986 CB TYR B 191 -19.375 23.477 55.449 1.00 30.40 C ANISOU 3986 CB TYR B 191 3984 3732 3833 55 873 -35 C ATOM 3987 CG TYR B 191 -19.711 24.295 54.225 1.00 26.31 C ANISOU 3987 CG TYR B 191 3448 3201 3348 18 834 -64 C ATOM 3988 CD1 TYR B 191 -20.365 23.718 53.144 1.00 22.41 C ANISOU 3988 CD1 TYR B 191 2936 2683 2895 -21 843 -64 C ATOM 3989 CD2 TYR B 191 -19.365 25.642 54.143 1.00 17.92 C ANISOU 3989 CD2 TYR B 191 2384 2151 2273 23 789 -91 C ATOM 3990 CE1 TYR B 191 -20.674 24.454 52.021 1.00 24.15 C ANISOU 3990 CE1 TYR B 191 3138 2898 3139 -48 808 -87 C ATOM 3991 CE2 TYR B 191 -19.671 26.390 53.015 1.00 25.44 C ANISOU 3991 CE2 TYR B 191 3320 3092 3254 -5 758 -111 C ATOM 3992 CZ TYR B 191 -20.327 25.786 51.959 1.00 21.38 C ANISOU 3992 CZ TYR B 191 2789 2560 2775 -39 767 -107 C ATOM 3993 OH TYR B 191 -20.650 26.500 50.833 1.00 17.47 O ANISOU 3993 OH TYR B 191 2276 2059 2302 -61 737 -123 O ATOM 3994 N TYR B 192 -20.536 23.999 58.739 1.00 23.22 N ANISOU 3994 N TYR B 192 3090 2886 2847 160 933 -14 N ATOM 3995 CA TYR B 192 -19.939 24.219 60.047 1.00 19.73 C ANISOU 3995 CA TYR B 192 2666 2485 2345 214 935 -10 C ATOM 3996 C TYR B 192 -20.578 23.392 61.149 1.00 31.74 C ANISOU 3996 C TYR B 192 4195 4017 3848 254 997 30 C ATOM 3997 O TYR B 192 -19.874 22.928 62.049 1.00 24.20 O ANISOU 3997 O TYR B 192 3258 3091 2845 299 1014 52 O ATOM 3998 CB TYR B 192 -20.028 25.704 60.404 1.00 21.06 C ANISOU 3998 CB TYR B 192 2831 2676 2496 226 894 -53 C ATOM 3999 CG TYR B 192 -19.413 26.587 59.344 1.00 25.48 C ANISOU 3999 CG TYR B 192 3382 3221 3076 190 838 -89 C ATOM 4000 CD1 TYR B 192 -18.057 26.876 59.365 1.00 23.73 C ANISOU 4000 CD1 TYR B 192 3170 3016 2829 197 801 -106 C ATOM 4001 CD2 TYR B 192 -20.182 27.112 58.309 1.00 18.83 C ANISOU 4001 CD2 TYR B 192 2522 2351 2283 150 824 -103 C ATOM 4002 CE1 TYR B 192 -17.482 27.669 58.395 1.00 29.65 C ANISOU 4002 CE1 TYR B 192 3913 3751 3603 164 756 -136 C ATOM 4003 CE2 TYR B 192 -19.612 27.910 57.330 1.00 29.52 C ANISOU 4003 CE2 TYR B 192 3870 3691 3656 122 779 -130 C ATOM 4004 CZ TYR B 192 -18.261 28.184 57.382 1.00 18.44 C ANISOU 4004 CZ TYR B 192 2478 2299 2229 128 746 -146 C ATOM 4005 OH TYR B 192 -17.678 28.977 56.424 1.00 24.33 O ANISOU 4005 OH TYR B 192 3217 3029 2997 101 706 -170 O ATOM 4006 N THR B 193 -21.892 23.196 61.096 1.00 37.05 N ANISOU 4006 N THR B 193 4852 4669 4558 240 1034 41 N ATOM 4007 CA THR B 193 -22.614 22.531 62.164 1.00 29.56 C ANISOU 4007 CA THR B 193 3908 3728 3595 277 1098 80 C ATOM 4008 C THR B 193 -23.340 21.302 61.631 1.00 38.68 C ANISOU 4008 C THR B 193 5051 4839 4807 245 1154 112 C ATOM 4009 O THR B 193 -23.683 21.244 60.446 1.00 40.19 O ANISOU 4009 O THR B 193 5223 4998 5051 191 1138 94 O ATOM 4010 CB THR B 193 -23.635 23.477 62.810 1.00 28.42 C ANISOU 4010 CB THR B 193 3753 3603 3442 296 1100 62 C ATOM 4011 OG1 THR B 193 -24.697 23.738 61.885 1.00 30.35 O ANISOU 4011 OG1 THR B 193 3969 3816 3746 248 1097 47 O ATOM 4012 CG2 THR B 193 -22.974 24.792 63.191 1.00 23.43 C ANISOU 4012 CG2 THR B 193 3130 3008 2765 318 1043 19 C ATOM 4013 N PRO B 194 -23.568 20.294 62.474 1.00 42.47 N ANISOU 4013 N PRO B 194 5542 5318 5279 279 1221 160 N ATOM 4014 CA PRO B 194 -24.415 19.168 62.058 1.00 46.05 C ANISOU 4014 CA PRO B 194 5978 5723 5794 247 1282 187 C ATOM 4015 C PRO B 194 -25.857 19.600 61.859 1.00 43.54 C ANISOU 4015 C PRO B 194 5630 5393 5520 220 1293 171 C ATOM 4016 O PRO B 194 -26.442 19.341 60.801 1.00 52.26 O ANISOU 4016 O PRO B 194 6708 6463 6684 164 1291 154 O ATOM 4017 CB PRO B 194 -24.269 18.167 63.214 1.00 51.70 C ANISOU 4017 CB PRO B 194 6715 6445 6482 301 1353 245 C ATOM 4018 CG PRO B 194 -23.015 18.576 63.925 1.00 46.88 C ANISOU 4018 CG PRO B 194 6132 5884 5794 355 1318 246 C ATOM 4019 CD PRO B 194 -22.953 20.063 63.792 1.00 43.20 C ANISOU 4019 CD PRO B 194 5659 5450 5304 348 1245 191 C ATOM 4020 N HIS B 195 -26.429 20.244 62.881 1.00 48.77 N ANISOU 4020 N HIS B 195 6294 6088 6151 261 1305 175 N ATOM 4021 CA HIS B 195 -27.771 20.838 62.861 1.00 45.84 C ANISOU 4021 CA HIS B 195 5893 5714 5810 246 1313 160 C ATOM 4022 C HIS B 195 -28.764 19.950 62.114 1.00 47.11 C ANISOU 4022 C HIS B 195 6022 5829 6049 195 1356 169 C ATOM 4023 O HIS B 195 -29.324 20.312 61.077 1.00 41.31 O ANISOU 4023 O HIS B 195 5257 5080 5359 146 1325 135 O ATOM 4024 CB HIS B 195 -27.755 22.253 62.296 1.00 36.87 C ANISOU 4024 CB HIS B 195 4748 4596 4667 230 1239 108 C ATOM 4025 CG HIS B 195 -28.944 23.062 62.706 1.00 41.11 C ANISOU 4025 CG HIS B 195 5264 5146 5210 241 1247 97 C ATOM 4026 ND1 HIS B 195 -30.018 23.277 61.870 1.00 45.84 N ANISOU 4026 ND1 HIS B 195 5826 5726 5865 197 1243 79 N ATOM 4027 CD2 HIS B 195 -29.253 23.667 63.878 1.00 35.38 C ANISOU 4027 CD2 HIS B 195 4550 4454 4441 293 1261 102 C ATOM 4028 CE1 HIS B 195 -30.928 23.998 62.502 1.00 38.85 C ANISOU 4028 CE1 HIS B 195 4929 4859 4972 222 1255 76 C ATOM 4029 NE2 HIS B 195 -30.488 24.248 63.722 1.00 37.25 N ANISOU 4029 NE2 HIS B 195 4757 4687 4710 279 1267 89 N ATOM 4030 N GLU B 196 -28.964 18.757 62.664 1.00 36.20 N ANISOU 4030 N GLU B 196 4645 4425 4684 209 1431 215 N ATOM 4031 CA GLU B 196 -29.718 17.721 61.974 1.00 35.52 C ANISOU 4031 CA GLU B 196 4530 4289 4676 158 1479 222 C ATOM 4032 C GLU B 196 -31.188 18.070 61.758 1.00 29.38 C ANISOU 4032 C GLU B 196 3708 3505 3947 129 1492 204 C ATOM 4033 O GLU B 196 -31.849 17.375 60.981 1.00 32.62 O ANISOU 4033 O GLU B 196 4088 3880 4428 76 1516 195 O ATOM 4034 CB GLU B 196 -29.592 16.402 62.733 1.00 43.12 C ANISOU 4034 CB GLU B 196 5510 5226 5646 185 1565 280 C ATOM 4035 CG GLU B 196 -28.768 15.373 61.987 1.00 64.87 C ANISOU 4035 CG GLU B 196 8276 7942 8429 156 1573 286 C ATOM 4036 CD GLU B 196 -27.639 14.801 62.825 1.00 59.87 C ANISOU 4036 CD GLU B 196 7686 7320 7741 214 1601 334 C ATOM 4037 OE1 GLU B 196 -26.895 15.588 63.452 1.00 61.58 O ANISOU 4037 OE1 GLU B 196 7928 7588 7883 263 1559 332 O ATOM 4038 OE2 GLU B 196 -27.509 13.557 62.864 1.00 54.70 O ANISOU 4038 OE2 GLU B 196 7039 6624 7121 212 1667 372 O ATOM 4039 N GLU B 197 -31.719 19.115 62.409 1.00 25.55 N ANISOU 4039 N GLU B 197 3220 3057 3430 162 1477 197 N ATOM 4040 CA GLU B 197 -33.084 19.540 62.102 1.00 34.21 C ANISOU 4040 CA GLU B 197 4272 4152 4573 134 1482 177 C ATOM 4041 C GLU B 197 -33.232 19.921 60.635 1.00 33.97 C ANISOU 4041 C GLU B 197 4212 4113 4582 74 1420 128 C ATOM 4042 O GLU B 197 -34.321 19.790 60.065 1.00 28.38 O ANISOU 4042 O GLU B 197 3459 3393 3932 34 1432 112 O ATOM 4043 CB GLU B 197 -33.495 20.719 62.990 1.00 40.50 C ANISOU 4043 CB GLU B 197 5075 4991 5323 182 1468 174 C ATOM 4044 CG GLU B 197 -34.961 21.138 62.863 1.00 47.82 C ANISOU 4044 CG GLU B 197 5956 5920 6295 164 1483 162 C ATOM 4045 CD GLU B 197 -35.312 22.306 63.776 1.00 59.40 C ANISOU 4045 CD GLU B 197 7431 7425 7712 216 1472 158 C ATOM 4046 OE1 GLU B 197 -34.480 23.233 63.901 1.00 63.49 O ANISOU 4046 OE1 GLU B 197 7978 7970 8174 242 1416 136 O ATOM 4047 OE2 GLU B 197 -36.413 22.290 64.375 1.00 62.76 O ANISOU 4047 OE2 GLU B 197 7834 7855 8156 232 1521 176 O ATOM 4048 N THR B 198 -32.155 20.399 60.015 1.00 29.75 N ANISOU 4048 N THR B 198 3699 3588 4016 68 1355 104 N ATOM 4049 CA THR B 198 -32.143 20.747 58.602 1.00 27.53 C ANISOU 4049 CA THR B 198 3394 3302 3763 17 1297 61 C ATOM 4050 C THR B 198 -31.415 19.717 57.748 1.00 31.72 C ANISOU 4050 C THR B 198 3932 3802 4320 -21 1298 59 C ATOM 4051 O THR B 198 -31.259 19.933 56.541 1.00 27.39 O ANISOU 4051 O THR B 198 3368 3251 3789 -60 1249 24 O ATOM 4052 CB THR B 198 -31.514 22.128 58.403 1.00 28.13 C ANISOU 4052 CB THR B 198 3487 3409 3791 35 1224 34 C ATOM 4053 OG1 THR B 198 -30.340 22.242 59.219 1.00 22.12 O ANISOU 4053 OG1 THR B 198 2772 2661 2971 79 1218 50 O ATOM 4054 CG2 THR B 198 -32.501 23.227 58.778 1.00 24.77 C ANISOU 4054 CG2 THR B 198 3041 3008 3361 55 1215 23 C ATOM 4055 N ASN B 199 -30.973 18.608 58.346 1.00 28.74 N ANISOU 4055 N ASN B 199 3577 3400 3944 -7 1354 95 N ATOM 4056 CA ASN B 199 -30.265 17.539 57.637 1.00 34.95 C ANISOU 4056 CA ASN B 199 4372 4152 4756 -39 1365 97 C ATOM 4057 C ASN B 199 -29.093 18.092 56.832 1.00 31.03 C ANISOU 4057 C ASN B 199 3896 3668 4225 -46 1292 71 C ATOM 4058 O ASN B 199 -28.971 17.860 55.627 1.00 36.33 O ANISOU 4058 O ASN B 199 4552 4325 4927 -92 1263 41 O ATOM 4059 CB ASN B 199 -31.218 16.752 56.737 1.00 30.71 C ANISOU 4059 CB ASN B 199 3790 3581 4297 -100 1391 75 C ATOM 4060 CG ASN B 199 -32.214 15.934 57.524 1.00 35.30 C ANISOU 4060 CG ASN B 199 4354 4138 4923 -97 1477 106 C ATOM 4061 OD1 ASN B 199 -33.422 16.147 57.427 1.00 40.98 O ANISOU 4061 OD1 ASN B 199 5030 4861 5680 -118 1488 90 O ATOM 4062 ND2 ASN B 199 -31.714 14.989 58.311 1.00 41.35 N ANISOU 4062 ND2 ASN B 199 5149 4877 5683 -69 1540 152 N ATOM 4063 N ASN B 200 -28.220 18.832 57.522 1.00 30.20 N ANISOU 4063 N ASN B 200 3825 3594 4056 1 1262 80 N ATOM 4064 CA ASN B 200 -27.140 19.548 56.847 1.00 32.41 C ANISOU 4064 CA ASN B 200 4121 3889 4303 -2 1192 55 C ATOM 4065 C ASN B 200 -26.224 18.595 56.090 1.00 22.55 C ANISOU 4065 C ASN B 200 2886 2613 3069 -28 1193 58 C ATOM 4066 O ASN B 200 -25.844 18.860 54.944 1.00 27.47 O ANISOU 4066 O ASN B 200 3502 3234 3702 -61 1145 28 O ATOM 4067 CB ASN B 200 -26.329 20.357 57.861 1.00 33.56 C ANISOU 4067 CB ASN B 200 4300 4071 4382 53 1170 64 C ATOM 4068 CG ASN B 200 -27.057 21.594 58.345 1.00 34.58 C ANISOU 4068 CG ASN B 200 4417 4229 4493 73 1149 47 C ATOM 4069 OD1 ASN B 200 -28.222 21.824 58.013 1.00 29.56 O ANISOU 4069 OD1 ASN B 200 3749 3588 3895 51 1156 35 O ATOM 4070 ND2 ASN B 200 -26.366 22.403 59.142 1.00 27.68 N ANISOU 4070 ND2 ASN B 200 3568 3387 3563 117 1123 44 N ATOM 4071 N GLU B 201 -25.857 17.477 56.723 1.00 27.45 N ANISOU 4071 N GLU B 201 3526 3213 3689 -9 1251 96 N ATOM 4072 CA GLU B 201 -24.857 16.584 56.147 1.00 28.92 C ANISOU 4072 CA GLU B 201 3731 3375 3883 -23 1255 104 C ATOM 4073 C GLU B 201 -25.302 16.051 54.793 1.00 25.90 C ANISOU 4073 C GLU B 201 3321 2959 3561 -86 1250 72 C ATOM 4074 O GLU B 201 -24.510 16.007 53.844 1.00 24.71 O ANISOU 4074 O GLU B 201 3178 2804 3409 -108 1212 52 O ATOM 4075 CB GLU B 201 -24.570 15.432 57.110 1.00 24.43 C ANISOU 4075 CB GLU B 201 3186 2786 3310 11 1329 156 C ATOM 4076 CG GLU B 201 -23.649 14.361 56.552 1.00 43.15 C ANISOU 4076 CG GLU B 201 5575 5124 5697 -2 1347 168 C ATOM 4077 CD GLU B 201 -23.512 13.173 57.491 1.00 56.81 C ANISOU 4077 CD GLU B 201 7325 6829 7431 33 1431 224 C ATOM 4078 OE1 GLU B 201 -22.791 13.293 58.507 1.00 62.84 O ANISOU 4078 OE1 GLU B 201 8118 7624 8136 94 1438 260 O ATOM 4079 OE2 GLU B 201 -24.142 12.126 57.221 1.00 69.84 O ANISOU 4079 OE2 GLU B 201 8963 8430 9144 2 1492 233 O ATOM 4080 N SER B 202 -26.570 15.653 54.680 1.00 23.72 N ANISOU 4080 N SER B 202 3011 2664 3339 -116 1288 64 N ATOM 4081 CA SER B 202 -27.056 15.101 53.423 1.00 31.69 C ANISOU 4081 CA SER B 202 3989 3646 4405 -177 1285 27 C ATOM 4082 C SER B 202 -27.027 16.131 52.301 1.00 24.49 C ANISOU 4082 C SER B 202 3060 2764 3482 -201 1205 -18 C ATOM 4083 O SER B 202 -26.800 15.772 51.141 1.00 31.56 O ANISOU 4083 O SER B 202 3946 3647 4400 -239 1182 -48 O ATOM 4084 CB SER B 202 -28.468 14.546 53.604 1.00 21.24 C ANISOU 4084 CB SER B 202 2627 2301 3142 -203 1340 24 C ATOM 4085 OG SER B 202 -29.364 15.575 53.980 1.00 22.06 O ANISOU 4085 OG SER B 202 2708 2440 3235 -190 1320 16 O ATOM 4086 N PHE B 203 -27.250 17.410 52.615 1.00 22.00 N ANISOU 4086 N PHE B 203 2741 2486 3132 -176 1164 -24 N ATOM 4087 CA PHE B 203 -27.270 18.418 51.557 1.00 22.89 C ANISOU 4087 CA PHE B 203 2837 2625 3236 -194 1094 -61 C ATOM 4088 C PHE B 203 -25.874 18.683 51.006 1.00 26.42 C ANISOU 4088 C PHE B 203 3314 3076 3647 -188 1048 -65 C ATOM 4089 O PHE B 203 -25.702 18.828 49.789 1.00 19.64 O ANISOU 4089 O PHE B 203 2443 2220 2798 -217 1009 -94 O ATOM 4090 CB PHE B 203 -27.888 19.722 52.058 1.00 27.33 C ANISOU 4090 CB PHE B 203 3388 3221 3775 -168 1068 -65 C ATOM 4091 CG PHE B 203 -27.979 20.785 50.996 1.00 26.31 C ANISOU 4091 CG PHE B 203 3241 3116 3639 -182 1003 -97 C ATOM 4092 CD1 PHE B 203 -29.113 20.898 50.210 1.00 30.70 C ANISOU 4092 CD1 PHE B 203 3752 3682 4231 -212 993 -124 C ATOM 4093 CD2 PHE B 203 -26.922 21.655 50.768 1.00 27.35 C ANISOU 4093 CD2 PHE B 203 3399 3262 3731 -163 954 -100 C ATOM 4094 CE1 PHE B 203 -29.194 21.862 49.223 1.00 29.64 C ANISOU 4094 CE1 PHE B 203 3601 3573 4087 -218 936 -149 C ATOM 4095 CE2 PHE B 203 -26.998 22.618 49.782 1.00 23.53 C ANISOU 4095 CE2 PHE B 203 2899 2797 3243 -173 901 -125 C ATOM 4096 CZ PHE B 203 -28.136 22.723 49.010 1.00 27.89 C ANISOU 4096 CZ PHE B 203 3410 3362 3827 -198 892 -147 C ATOM 4097 N VAL B 204 -24.871 18.774 51.883 1.00 26.77 N ANISOU 4097 N VAL B 204 3396 3125 3649 -148 1053 -37 N ATOM 4098 CA VAL B 204 -23.518 19.092 51.430 1.00 25.16 C ANISOU 4098 CA VAL B 204 3218 2928 3412 -140 1010 -40 C ATOM 4099 C VAL B 204 -23.015 18.022 50.470 1.00 20.58 C ANISOU 4099 C VAL B 204 2641 2320 2858 -174 1019 -46 C ATOM 4100 O VAL B 204 -22.371 18.328 49.458 1.00 20.06 O ANISOU 4100 O VAL B 204 2578 2258 2786 -190 975 -66 O ATOM 4101 CB VAL B 204 -22.572 19.272 52.631 1.00 31.97 C ANISOU 4101 CB VAL B 204 4116 3805 4226 -91 1016 -10 C ATOM 4102 CG1 VAL B 204 -21.178 19.640 52.151 1.00 28.60 C ANISOU 4102 CG1 VAL B 204 3710 3387 3769 -85 971 -17 C ATOM 4103 CG2 VAL B 204 -23.101 20.340 53.569 1.00 22.38 C ANISOU 4103 CG2 VAL B 204 2898 2620 2986 -58 1007 -11 C ATOM 4104 N AILE B 205 -23.295 16.751 50.774 0.41 19.17 N ANISOU 4104 N AILE B 205 2464 2109 2712 -183 1081 -29 N ATOM 4105 N BILE B 205 -23.293 16.751 50.774 0.59 19.17 N ANISOU 4105 N BILE B 205 2464 2109 2712 -183 1080 -29 N ATOM 4106 CA AILE B 205 -22.948 15.668 49.857 0.41 21.88 C ANISOU 4106 CA AILE B 205 2808 2420 3087 -217 1096 -40 C ATOM 4107 CA BILE B 205 -22.944 15.672 49.853 0.59 21.81 C ANISOU 4107 CA BILE B 205 2799 2410 3078 -217 1096 -40 C ATOM 4108 C AILE B 205 -23.690 15.840 48.536 0.41 24.83 C ANISOU 4108 C AILE B 205 3144 2796 3493 -265 1064 -86 C ATOM 4109 C BILE B 205 -23.690 15.839 48.536 0.59 24.81 C ANISOU 4109 C BILE B 205 3142 2793 3490 -265 1064 -86 C ATOM 4110 O AILE B 205 -23.108 15.709 47.453 0.41 26.72 O ANISOU 4110 O AILE B 205 3387 3034 3734 -286 1034 -108 O ATOM 4111 O BILE B 205 -23.110 15.705 47.452 0.59 26.76 O ANISOU 4111 O BILE B 205 3391 3038 3738 -287 1034 -108 O ATOM 4112 CB AILE B 205 -23.254 14.301 50.496 0.41 24.91 C ANISOU 4112 CB AILE B 205 3196 2762 3507 -218 1177 -12 C ATOM 4113 CB BILE B 205 -23.238 14.303 50.495 0.59 24.90 C ANISOU 4113 CB BILE B 205 3196 2761 3506 -218 1176 -12 C ATOM 4114 CG1AILE B 205 -22.674 14.222 51.910 0.41 23.87 C ANISOU 4114 CG1AILE B 205 3097 2637 3336 -162 1210 38 C ATOM 4115 CG1BILE B 205 -22.473 14.141 51.811 0.59 23.69 C ANISOU 4115 CG1BILE B 205 3078 2612 3311 -162 1208 39 C ATOM 4116 CG2AILE B 205 -22.705 13.174 49.634 0.41 19.79 C ANISOU 4116 CG2AILE B 205 2554 2075 2888 -249 1196 -22 C ATOM 4117 CG2BILE B 205 -22.892 13.176 49.532 0.59 19.81 C ANISOU 4117 CG2BILE B 205 2552 2078 2898 -256 1196 -28 C ATOM 4118 CD1AILE B 205 -21.173 14.370 51.969 0.41 19.90 C ANISOU 4118 CD1AILE B 205 2629 2148 2785 -131 1181 55 C ATOM 4119 CD1BILE B 205 -22.717 12.808 52.495 0.59 26.44 C ANISOU 4119 CD1BILE B 205 3435 2919 3693 -155 1293 75 C ATOM 4120 N TYR B 206 -24.988 16.142 48.612 1.00 22.98 N ANISOU 4120 N TYR B 206 2874 2572 3284 -279 1070 -102 N ATOM 4121 CA TYR B 206 -25.792 16.303 47.404 1.00 23.88 C ANISOU 4121 CA TYR B 206 2948 2698 3427 -320 1040 -148 C ATOM 4122 C TYR B 206 -25.327 17.495 46.577 1.00 25.45 C ANISOU 4122 C TYR B 206 3148 2933 3589 -313 968 -165 C ATOM 4123 O TYR B 206 -25.299 17.428 45.341 1.00 22.88 O ANISOU 4123 O TYR B 206 2807 2615 3272 -341 936 -197 O ATOM 4124 CB TYR B 206 -27.265 16.439 47.791 1.00 21.82 C ANISOU 4124 CB TYR B 206 2647 2445 3198 -331 1062 -157 C ATOM 4125 CG TYR B 206 -28.111 17.246 46.834 1.00 28.11 C ANISOU 4125 CG TYR B 206 3402 3278 4001 -351 1013 -196 C ATOM 4126 CD1 TYR B 206 -28.582 16.692 45.651 1.00 25.23 C ANISOU 4126 CD1 TYR B 206 3002 2913 3670 -396 1002 -239 C ATOM 4127 CD2 TYR B 206 -28.461 18.557 47.128 1.00 24.81 C ANISOU 4127 CD2 TYR B 206 2978 2896 3554 -322 978 -190 C ATOM 4128 CE1 TYR B 206 -29.369 17.426 44.782 1.00 25.62 C ANISOU 4128 CE1 TYR B 206 3011 3003 3720 -408 956 -273 C ATOM 4129 CE2 TYR B 206 -29.242 19.297 46.265 1.00 31.45 C ANISOU 4129 CE2 TYR B 206 3780 3771 4398 -335 936 -221 C ATOM 4130 CZ TYR B 206 -29.693 18.730 45.095 1.00 20.63 C ANISOU 4130 CZ TYR B 206 2375 2406 3058 -376 924 -260 C ATOM 4131 OH TYR B 206 -30.474 19.472 44.241 1.00 26.76 O ANISOU 4131 OH TYR B 206 3110 3224 3833 -383 881 -289 O ATOM 4132 N MET B 207 -24.963 18.596 47.238 1.00 23.03 N ANISOU 4132 N MET B 207 2860 2649 3242 -275 942 -145 N ATOM 4133 CA MET B 207 -24.479 19.768 46.514 1.00 27.40 C ANISOU 4133 CA MET B 207 3416 3231 3765 -266 880 -158 C ATOM 4134 C MET B 207 -23.162 19.477 45.804 1.00 25.16 C ANISOU 4134 C MET B 207 3158 2937 3464 -270 860 -157 C ATOM 4135 O MET B 207 -22.958 19.900 44.660 1.00 21.62 O ANISOU 4135 O MET B 207 2702 2504 3010 -283 819 -178 O ATOM 4136 CB MET B 207 -24.320 20.949 47.472 1.00 18.28 C ANISOU 4136 CB MET B 207 2275 2094 2575 -225 864 -139 C ATOM 4137 CG MET B 207 -23.828 22.221 46.807 1.00 27.14 C ANISOU 4137 CG MET B 207 3401 3238 3672 -215 808 -149 C ATOM 4138 SD MET B 207 -23.381 23.485 48.004 1.00 26.63 S ANISOU 4138 SD MET B 207 3360 3188 3572 -169 794 -133 S ATOM 4139 CE MET B 207 -22.278 22.550 49.055 1.00 32.83 C ANISOU 4139 CE MET B 207 4182 3956 4335 -150 828 -106 C ATOM 4140 N PHE B 208 -22.254 18.758 46.467 1.00 27.70 N ANISOU 4140 N PHE B 208 3512 3236 3775 -256 890 -132 N ATOM 4141 CA PHE B 208 -20.937 18.512 45.895 1.00 31.33 C ANISOU 4141 CA PHE B 208 3998 3689 4218 -255 872 -128 C ATOM 4142 C PHE B 208 -20.926 17.397 44.859 1.00 23.75 C ANISOU 4142 C PHE B 208 3030 2706 3287 -291 887 -148 C ATOM 4143 O PHE B 208 -19.980 17.323 44.069 1.00 31.06 O ANISOU 4143 O PHE B 208 3970 3630 4200 -295 864 -152 O ATOM 4144 CB PHE B 208 -19.930 18.192 47.000 1.00 23.98 C ANISOU 4144 CB PHE B 208 3102 2748 3262 -221 897 -92 C ATOM 4145 CG PHE B 208 -19.225 19.400 47.540 1.00 26.21 C ANISOU 4145 CG PHE B 208 3399 3056 3503 -187 860 -83 C ATOM 4146 CD1 PHE B 208 -18.305 20.080 46.761 1.00 24.44 C ANISOU 4146 CD1 PHE B 208 3182 2843 3261 -188 814 -92 C ATOM 4147 CD2 PHE B 208 -19.477 19.855 48.822 1.00 26.73 C ANISOU 4147 CD2 PHE B 208 3470 3135 3549 -155 873 -67 C ATOM 4148 CE1 PHE B 208 -17.652 21.196 47.250 1.00 37.30 C ANISOU 4148 CE1 PHE B 208 4822 4492 4859 -161 782 -88 C ATOM 4149 CE2 PHE B 208 -18.824 20.968 49.319 1.00 25.52 C ANISOU 4149 CE2 PHE B 208 3329 3006 3361 -127 838 -66 C ATOM 4150 CZ PHE B 208 -17.910 21.638 48.532 1.00 25.58 C ANISOU 4150 CZ PHE B 208 3342 3020 3356 -132 793 -78 C ATOM 4151 N VAL B 209 -21.937 16.532 44.835 1.00 29.52 N ANISOU 4151 N VAL B 209 3738 3419 4060 -319 925 -162 N ATOM 4152 CA VAL B 209 -21.961 15.442 43.865 1.00 22.39 C ANISOU 4152 CA VAL B 209 2826 2493 3190 -356 942 -189 C ATOM 4153 C VAL B 209 -22.772 15.860 42.647 1.00 29.44 C ANISOU 4153 C VAL B 209 3680 3413 4093 -386 901 -234 C ATOM 4154 O VAL B 209 -22.257 15.892 41.524 1.00 30.48 O ANISOU 4154 O VAL B 209 3813 3555 4212 -397 869 -255 O ATOM 4155 CB VAL B 209 -22.522 14.148 44.482 1.00 27.20 C ANISOU 4155 CB VAL B 209 3431 3060 3844 -373 1012 -183 C ATOM 4156 CG1 VAL B 209 -22.839 13.134 43.390 1.00 19.40 C ANISOU 4156 CG1 VAL B 209 2423 2049 2898 -420 1026 -225 C ATOM 4157 CG2 VAL B 209 -21.536 13.565 45.476 1.00 19.08 C ANISOU 4157 CG2 VAL B 209 2443 2004 2801 -340 1053 -136 C ATOM 4158 N VAL B 210 -24.047 16.186 42.864 1.00 33.18 N ANISOU 4158 N VAL B 210 4118 3903 4586 -395 904 -249 N ATOM 4159 CA VAL B 210 -24.927 16.528 41.749 1.00 35.25 C ANISOU 4159 CA VAL B 210 4338 4198 4859 -420 868 -292 C ATOM 4160 C VAL B 210 -24.519 17.856 41.125 1.00 20.26 C ANISOU 4160 C VAL B 210 2443 2339 2915 -396 806 -289 C ATOM 4161 O VAL B 210 -24.498 18.000 39.898 1.00 35.46 O ANISOU 4161 O VAL B 210 4353 4289 4832 -408 770 -318 O ATOM 4162 CB VAL B 210 -26.393 16.549 42.216 1.00 19.45 C ANISOU 4162 CB VAL B 210 2294 2204 2890 -433 889 -305 C ATOM 4163 CG1 VAL B 210 -27.292 17.112 41.125 1.00 19.60 C ANISOU 4163 CG1 VAL B 210 2266 2269 2910 -449 844 -346 C ATOM 4164 CG2 VAL B 210 -26.839 15.154 42.600 1.00 19.90 C ANISOU 4164 CG2 VAL B 210 2342 2218 3001 -464 953 -314 C ATOM 4165 N HIS B 211 -24.191 18.846 41.952 1.00 26.04 N ANISOU 4165 N HIS B 211 3195 3080 3620 -360 795 -256 N ATOM 4166 CA HIS B 211 -23.951 20.195 41.465 1.00 19.19 C ANISOU 4166 CA HIS B 211 2327 2245 2718 -336 744 -252 C ATOM 4167 C HIS B 211 -22.482 20.590 41.481 1.00 20.72 C ANISOU 4167 C HIS B 211 2562 2430 2880 -314 726 -228 C ATOM 4168 O HIS B 211 -22.177 21.765 41.260 1.00 27.79 O ANISOU 4168 O HIS B 211 3462 3345 3751 -292 691 -220 O ATOM 4169 CB HIS B 211 -24.771 21.196 42.278 1.00 22.54 C ANISOU 4169 CB HIS B 211 2738 2687 3140 -314 740 -240 C ATOM 4170 CG HIS B 211 -26.241 20.923 42.255 1.00 30.44 C ANISOU 4170 CG HIS B 211 3693 3700 4172 -334 756 -263 C ATOM 4171 ND1 HIS B 211 -27.029 21.200 41.158 1.00 23.60 N ANISOU 4171 ND1 HIS B 211 2787 2869 3311 -348 725 -293 N ATOM 4172 CD2 HIS B 211 -27.066 20.387 43.185 1.00 23.33 C ANISOU 4172 CD2 HIS B 211 2780 2785 3301 -341 799 -259 C ATOM 4173 CE1 HIS B 211 -28.277 20.849 41.416 1.00 19.14 C ANISOU 4173 CE1 HIS B 211 2183 2311 2778 -365 746 -310 C ATOM 4174 NE2 HIS B 211 -28.326 20.355 42.639 1.00 19.62 N ANISOU 4174 NE2 HIS B 211 2259 2339 2856 -362 794 -289 N ATOM 4175 N PHE B 212 -21.569 19.678 41.817 1.00 20.27 N ANISOU 4175 N PHE B 212 2535 2344 2825 -316 753 -215 N ATOM 4176 CA PHE B 212 -20.165 19.975 41.554 1.00 28.51 C ANISOU 4176 CA PHE B 212 3610 3384 3840 -300 732 -198 C ATOM 4177 C PHE B 212 -19.445 18.917 40.719 1.00 29.04 C ANISOU 4177 C PHE B 212 3689 3434 3913 -320 741 -208 C ATOM 4178 O PHE B 212 -18.941 19.213 39.629 1.00 26.07 O ANISOU 4178 O PHE B 212 3313 3070 3521 -322 710 -219 O ATOM 4179 CB PHE B 212 -19.428 20.184 42.879 1.00 20.02 C ANISOU 4179 CB PHE B 212 2564 2297 2747 -270 748 -166 C ATOM 4180 CG PHE B 212 -17.974 20.517 42.718 1.00 32.38 C ANISOU 4180 CG PHE B 212 4157 3861 4286 -253 727 -150 C ATOM 4181 CD1 PHE B 212 -17.579 21.601 41.952 1.00 19.96 C ANISOU 4181 CD1 PHE B 212 2581 2305 2697 -247 684 -155 C ATOM 4182 CD2 PHE B 212 -17.001 19.753 43.338 1.00 29.96 C ANISOU 4182 CD2 PHE B 212 3878 3535 3972 -242 752 -130 C ATOM 4183 CE1 PHE B 212 -16.244 21.914 41.804 1.00 39.43 C ANISOU 4183 CE1 PHE B 212 5069 4769 5144 -233 667 -141 C ATOM 4184 CE2 PHE B 212 -15.664 20.060 43.192 1.00 37.64 C ANISOU 4184 CE2 PHE B 212 4871 4509 4921 -227 732 -117 C ATOM 4185 CZ PHE B 212 -15.285 21.143 42.426 1.00 26.31 C ANISOU 4185 CZ PHE B 212 3432 3091 3475 -225 690 -124 C ATOM 4186 N ILE B 213 -19.413 17.676 41.217 1.00 28.46 N ANISOU 4186 N ILE B 213 3624 3327 3860 -332 788 -205 N ATOM 4187 CA AILE B 213 -18.594 16.640 40.592 1.00 24.52 C ANISOU 4187 CA AILE B 213 3143 2805 3368 -346 803 -210 C ATOM 4188 CA BILE B 213 -18.594 16.640 40.591 0.00 24.60 C ANISOU 4188 CA BILE B 213 3153 2815 3378 -346 803 -210 C ATOM 4189 C ILE B 213 -19.200 16.190 39.268 1.00 22.01 C ANISOU 4189 C ILE B 213 2799 2496 3068 -380 792 -254 C ATOM 4190 O ILE B 213 -18.492 16.048 38.263 1.00 26.80 O ANISOU 4190 O ILE B 213 3414 3107 3661 -385 772 -265 O ATOM 4191 CB AILE B 213 -18.395 15.463 41.563 1.00 23.78 C ANISOU 4191 CB AILE B 213 3069 2672 3295 -344 863 -188 C ATOM 4192 CB BILE B 213 -18.397 15.461 41.561 0.00 23.88 C ANISOU 4192 CB BILE B 213 3081 2684 3307 -344 863 -188 C ATOM 4193 CG1AILE B 213 -17.444 15.874 42.691 1.00 25.86 C ANISOU 4193 CG1AILE B 213 3363 2937 3528 -304 866 -145 C ATOM 4194 CG1BILE B 213 -17.465 15.868 42.704 0.00 25.82 C ANISOU 4194 CG1BILE B 213 3356 2930 3522 -304 867 -145 C ATOM 4195 CG2AILE B 213 -17.863 14.242 40.829 1.00 20.98 C ANISOU 4195 CG2AILE B 213 2725 2287 2958 -365 887 -202 C ATOM 4196 CG2BILE B 213 -17.847 14.249 40.825 0.00 20.93 C ANISOU 4196 CG2BILE B 213 2720 2282 2952 -365 887 -202 C ATOM 4197 CD1AILE B 213 -17.207 14.795 43.718 1.00 20.35 C ANISOU 4197 CD1AILE B 213 2684 2205 2842 -291 925 -116 C ATOM 4198 CD1BILE B 213 -16.085 16.286 42.243 0.00 25.88 C ANISOU 4198 CD1BILE B 213 3386 2948 3498 -287 834 -134 C ATOM 4199 N ILE B 214 -20.511 15.953 39.244 1.00 24.07 N ANISOU 4199 N ILE B 214 3025 2762 3359 -404 803 -282 N ATOM 4200 CA ILE B 214 -21.158 15.517 38.006 1.00 22.52 C ANISOU 4200 CA ILE B 214 2797 2580 3178 -437 790 -331 C ATOM 4201 C ILE B 214 -20.994 16.536 36.884 1.00 18.98 C ANISOU 4201 C ILE B 214 2340 2179 2694 -425 731 -343 C ATOM 4202 O ILE B 214 -20.619 16.137 35.769 1.00 32.48 O ANISOU 4202 O ILE B 214 4050 3897 4396 -438 717 -368 O ATOM 4203 CB ILE B 214 -22.630 15.155 38.276 1.00 28.54 C ANISOU 4203 CB ILE B 214 3519 3344 3982 -464 812 -359 C ATOM 4204 CG1 ILE B 214 -22.726 13.842 39.059 1.00 24.05 C ANISOU 4204 CG1 ILE B 214 2959 2721 3457 -483 879 -354 C ATOM 4205 CG2 ILE B 214 -23.407 15.064 36.970 1.00 29.34 C ANISOU 4205 CG2 ILE B 214 3579 3480 4090 -493 782 -415 C ATOM 4206 CD1 ILE B 214 -24.144 13.438 39.404 1.00 20.48 C ANISOU 4206 CD1 ILE B 214 2466 2264 3053 -511 909 -380 C ATOM 4207 N PRO B 215 -21.253 17.839 37.086 1.00 24.95 N ANISOU 4207 N PRO B 215 3087 2965 3427 -400 699 -325 N ATOM 4208 CA PRO B 215 -21.023 18.792 35.985 1.00 18.09 C ANISOU 4208 CA PRO B 215 2212 2137 2525 -384 649 -329 C ATOM 4209 C PRO B 215 -19.596 18.787 35.460 1.00 25.19 C ANISOU 4209 C PRO B 215 3146 3026 3398 -371 639 -312 C ATOM 4210 O PRO B 215 -19.391 18.887 34.244 1.00 26.25 O ANISOU 4210 O PRO B 215 3273 3186 3513 -371 612 -329 O ATOM 4211 CB PRO B 215 -21.387 20.144 36.613 1.00 33.41 C ANISOU 4211 CB PRO B 215 4147 4096 4452 -355 630 -303 C ATOM 4212 CG PRO B 215 -22.333 19.816 37.688 1.00 20.95 C ANISOU 4212 CG PRO B 215 2553 2503 2902 -365 662 -304 C ATOM 4213 CD PRO B 215 -21.857 18.511 38.252 1.00 19.75 C ANISOU 4213 CD PRO B 215 2423 2307 2773 -383 708 -302 C ATOM 4214 N LEU B 216 -18.604 18.666 36.344 1.00 21.63 N ANISOU 4214 N LEU B 216 2730 2543 2944 -357 660 -278 N ATOM 4215 CA LEU B 216 -17.215 18.638 35.896 1.00 23.89 C ANISOU 4215 CA LEU B 216 3047 2821 3210 -345 652 -260 C ATOM 4216 C LEU B 216 -16.920 17.383 35.086 1.00 28.64 C ANISOU 4216 C LEU B 216 3653 3407 3821 -368 669 -287 C ATOM 4217 O LEU B 216 -16.178 17.438 34.099 1.00 26.75 O ANISOU 4217 O LEU B 216 3423 3179 3561 -363 650 -289 O ATOM 4218 CB LEU B 216 -16.269 18.741 37.090 1.00 26.57 C ANISOU 4218 CB LEU B 216 3417 3134 3545 -324 670 -222 C ATOM 4219 CG LEU B 216 -16.182 20.107 37.769 1.00 32.72 C ANISOU 4219 CG LEU B 216 4198 3927 4308 -297 648 -198 C ATOM 4220 CD1 LEU B 216 -15.053 20.112 38.801 1.00 33.03 C ANISOU 4220 CD1 LEU B 216 4266 3946 4338 -277 661 -167 C ATOM 4221 CD2 LEU B 216 -15.978 21.203 36.741 1.00 26.42 C ANISOU 4221 CD2 LEU B 216 3392 3156 3491 -285 607 -198 C ATOM 4222 N ILE B 217 -17.488 16.243 35.489 1.00 19.41 N ANISOU 4222 N ILE B 217 2478 2211 2686 -394 708 -306 N ATOM 4223 CA ILE B 217 -17.292 15.005 34.738 1.00 27.98 C ANISOU 4223 CA ILE B 217 3566 3277 3787 -420 729 -337 C ATOM 4224 C ILE B 217 -17.785 15.172 33.306 1.00 27.52 C ANISOU 4224 C ILE B 217 3481 3260 3715 -432 693 -381 C ATOM 4225 O ILE B 217 -17.107 14.787 32.347 1.00 23.36 O ANISOU 4225 O ILE B 217 2966 2737 3174 -434 685 -395 O ATOM 4226 CB ILE B 217 -18.000 13.831 35.440 1.00 36.30 C ANISOU 4226 CB ILE B 217 4612 4292 4888 -447 781 -353 C ATOM 4227 CG1 ILE B 217 -17.286 13.475 36.744 1.00 24.06 C ANISOU 4227 CG1 ILE B 217 3096 2703 3345 -428 822 -305 C ATOM 4228 CG2 ILE B 217 -18.084 12.623 34.511 1.00 28.98 C ANISOU 4228 CG2 ILE B 217 3678 3348 3984 -480 800 -400 C ATOM 4229 CD1 ILE B 217 -17.975 12.389 37.537 1.00 31.76 C ANISOU 4229 CD1 ILE B 217 4065 3637 4366 -448 880 -310 C ATOM 4230 N VAL B 218 -18.976 15.751 33.145 1.00 33.70 N ANISOU 4230 N VAL B 218 4226 4078 4500 -438 670 -402 N ATOM 4231 CA VAL B 218 -19.540 15.949 31.813 1.00 18.62 C ANISOU 4231 CA VAL B 218 2286 2217 2572 -445 633 -444 C ATOM 4232 C VAL B 218 -18.661 16.887 30.996 1.00 21.06 C ANISOU 4232 C VAL B 218 2610 2556 2834 -412 595 -420 C ATOM 4233 O VAL B 218 -18.378 16.635 29.818 1.00 19.72 O ANISOU 4233 O VAL B 218 2439 2410 2643 -413 578 -445 O ATOM 4234 CB VAL B 218 -20.983 16.476 31.915 1.00 23.44 C ANISOU 4234 CB VAL B 218 2850 2863 3192 -452 616 -465 C ATOM 4235 CG1 VAL B 218 -21.553 16.748 30.530 1.00 19.18 C ANISOU 4235 CG1 VAL B 218 2276 2384 2627 -452 574 -506 C ATOM 4236 CG2 VAL B 218 -21.857 15.490 32.678 1.00 26.90 C ANISOU 4236 CG2 VAL B 218 3269 3269 3682 -487 659 -490 C ATOM 4237 N ILE B 219 -18.214 17.984 31.612 1.00 23.55 N ANISOU 4237 N ILE B 219 2942 2871 3134 -381 584 -372 N ATOM 4238 CA ILE B 219 -17.416 18.977 30.894 1.00 24.36 C ANISOU 4238 CA ILE B 219 3058 2999 3199 -349 553 -345 C ATOM 4239 C ILE B 219 -16.116 18.358 30.397 1.00 32.03 C ANISOU 4239 C ILE B 219 4062 3949 4160 -348 564 -337 C ATOM 4240 O ILE B 219 -15.751 18.493 29.223 1.00 35.24 O ANISOU 4240 O ILE B 219 4468 4384 4538 -337 543 -346 O ATOM 4241 CB ILE B 219 -17.148 20.199 31.791 1.00 29.73 C ANISOU 4241 CB ILE B 219 3750 3672 3875 -322 546 -298 C ATOM 4242 CG1 ILE B 219 -18.437 20.979 32.045 1.00 21.73 C ANISOU 4242 CG1 ILE B 219 2704 2687 2867 -317 531 -305 C ATOM 4243 CG2 ILE B 219 -16.097 21.103 31.169 1.00 26.81 C ANISOU 4243 CG2 ILE B 219 3398 3312 3476 -292 525 -267 C ATOM 4244 CD1 ILE B 219 -18.304 22.032 33.121 1.00 20.89 C ANISOU 4244 CD1 ILE B 219 2608 2566 2763 -295 532 -267 C ATOM 4245 N PHE B 220 -15.398 17.663 31.282 1.00 36.52 N ANISOU 4245 N PHE B 220 4657 4471 4748 -355 597 -320 N ATOM 4246 CA PHE B 220 -14.106 17.111 30.893 1.00 31.06 C ANISOU 4246 CA PHE B 220 3996 3759 4046 -350 609 -308 C ATOM 4247 C PHE B 220 -14.257 15.879 30.006 1.00 35.84 C ANISOU 4247 C PHE B 220 4597 4360 4658 -375 623 -354 C ATOM 4248 O PHE B 220 -13.366 15.588 29.201 1.00 28.91 O ANISOU 4248 O PHE B 220 3738 3484 3763 -367 621 -354 O ATOM 4249 CB PHE B 220 -13.273 16.810 32.139 1.00 29.90 C ANISOU 4249 CB PHE B 220 3878 3569 3914 -343 640 -272 C ATOM 4250 CG PHE B 220 -12.690 18.043 32.777 1.00 47.31 C ANISOU 4250 CG PHE B 220 6092 5778 6104 -315 622 -230 C ATOM 4251 CD1 PHE B 220 -11.781 18.828 32.083 1.00 49.34 C ANISOU 4251 CD1 PHE B 220 6358 6051 6337 -294 599 -210 C ATOM 4252 CD2 PHE B 220 -13.054 18.425 34.058 1.00 42.97 C ANISOU 4252 CD2 PHE B 220 5541 5218 5567 -310 631 -213 C ATOM 4253 CE1 PHE B 220 -11.244 19.967 32.654 1.00 51.18 C ANISOU 4253 CE1 PHE B 220 6597 6285 6564 -272 585 -176 C ATOM 4254 CE2 PHE B 220 -12.517 19.565 34.636 1.00 47.73 C ANISOU 4254 CE2 PHE B 220 6151 5826 6159 -286 614 -182 C ATOM 4255 CZ PHE B 220 -11.612 20.336 33.932 1.00 40.75 C ANISOU 4255 CZ PHE B 220 5274 4953 5255 -269 592 -165 C ATOM 4256 N PHE B 221 -15.368 15.150 30.128 1.00 28.35 N ANISOU 4256 N PHE B 221 3624 3408 3738 -405 638 -396 N ATOM 4257 CA PHE B 221 -15.672 14.115 29.145 1.00 34.84 C ANISOU 4257 CA PHE B 221 4436 4235 4568 -432 644 -451 C ATOM 4258 C PHE B 221 -15.784 14.716 27.750 1.00 37.14 C ANISOU 4258 C PHE B 221 4710 4586 4816 -417 600 -473 C ATOM 4259 O PHE B 221 -15.147 14.243 26.801 1.00 27.01 O ANISOU 4259 O PHE B 221 3440 3309 3515 -415 598 -490 O ATOM 4260 CB PHE B 221 -16.964 13.386 29.522 1.00 31.02 C ANISOU 4260 CB PHE B 221 3920 3741 4126 -469 665 -495 C ATOM 4261 CG PHE B 221 -17.415 12.375 28.500 1.00 41.24 C ANISOU 4261 CG PHE B 221 5195 5042 5431 -501 669 -564 C ATOM 4262 CD1 PHE B 221 -16.927 11.078 28.525 1.00 47.46 C ANISOU 4262 CD1 PHE B 221 6004 5780 6250 -523 713 -583 C ATOM 4263 CD2 PHE B 221 -18.329 12.722 27.515 1.00 38.22 C ANISOU 4263 CD2 PHE B 221 4772 4721 5029 -507 629 -611 C ATOM 4264 CE1 PHE B 221 -17.340 10.149 27.590 1.00 32.93 C ANISOU 4264 CE1 PHE B 221 4145 3945 4423 -555 718 -652 C ATOM 4265 CE2 PHE B 221 -18.744 11.799 26.577 1.00 38.62 C ANISOU 4265 CE2 PHE B 221 4801 4783 5088 -537 630 -681 C ATOM 4266 CZ PHE B 221 -18.248 10.510 26.614 1.00 41.35 C ANISOU 4266 CZ PHE B 221 5170 5075 5469 -563 675 -704 C ATOM 4267 N CYS B 222 -16.583 15.777 27.613 1.00 26.26 N ANISOU 4267 N CYS B 222 3304 3253 3421 -403 566 -469 N ATOM 4268 CA CYS B 222 -16.777 16.398 26.306 1.00 35.81 C ANISOU 4268 CA CYS B 222 4495 4525 4588 -382 524 -485 C ATOM 4269 C CYS B 222 -15.486 17.019 25.789 1.00 37.37 C ANISOU 4269 C CYS B 222 4724 4727 4749 -347 514 -440 C ATOM 4270 O CYS B 222 -15.225 17.007 24.580 1.00 46.82 O ANISOU 4270 O CYS B 222 5919 5960 5910 -333 496 -457 O ATOM 4271 CB CYS B 222 -17.892 17.443 26.385 1.00 31.71 C ANISOU 4271 CB CYS B 222 3940 4050 4059 -369 495 -482 C ATOM 4272 SG CYS B 222 -19.555 16.742 26.577 1.00 32.35 S ANISOU 4272 SG CYS B 222 3969 4146 4174 -410 498 -546 S ATOM 4273 N TYR B 223 -14.671 17.580 26.687 1.00 35.63 N ANISOU 4273 N TYR B 223 4530 4471 4536 -331 526 -386 N ATOM 4274 CA TYR B 223 -13.383 18.141 26.288 1.00 38.18 C ANISOU 4274 CA TYR B 223 4881 4791 4833 -301 522 -343 C ATOM 4275 C TYR B 223 -12.440 17.054 25.785 1.00 38.77 C ANISOU 4275 C TYR B 223 4981 4844 4906 -309 543 -356 C ATOM 4276 O TYR B 223 -11.788 17.215 24.747 1.00 37.82 O ANISOU 4276 O TYR B 223 4870 4747 4753 -289 531 -351 O ATOM 4277 CB TYR B 223 -12.777 18.911 27.465 1.00 44.65 C ANISOU 4277 CB TYR B 223 5719 5578 5668 -287 530 -290 C ATOM 4278 CG TYR B 223 -11.270 18.843 27.621 1.00 57.69 C ANISOU 4278 CG TYR B 223 7404 7199 7317 -274 546 -254 C ATOM 4279 CD1 TYR B 223 -10.431 19.683 26.891 1.00 57.68 C ANISOU 4279 CD1 TYR B 223 7412 7214 7290 -246 531 -223 C ATOM 4280 CD2 TYR B 223 -10.691 17.971 28.540 1.00 58.70 C ANISOU 4280 CD2 TYR B 223 7552 7281 7469 -288 577 -248 C ATOM 4281 CE1 TYR B 223 -9.055 19.636 27.053 1.00 56.57 C ANISOU 4281 CE1 TYR B 223 7297 7047 7151 -235 545 -191 C ATOM 4282 CE2 TYR B 223 -9.321 17.916 28.710 1.00 57.42 C ANISOU 4282 CE2 TYR B 223 7417 7096 7304 -275 590 -215 C ATOM 4283 CZ TYR B 223 -8.508 18.749 27.965 1.00 64.75 C ANISOU 4283 CZ TYR B 223 8351 8042 8209 -250 573 -188 C ATOM 4284 OH TYR B 223 -7.144 18.685 28.142 1.00 72.62 O ANISOU 4284 OH TYR B 223 9370 9017 9206 -238 586 -157 O ATOM 4285 N GLY B 224 -12.373 15.928 26.499 1.00 28.14 N ANISOU 4285 N GLY B 224 3646 3453 3594 -337 577 -372 N ATOM 4286 CA GLY B 224 -11.510 14.837 26.071 1.00 43.07 C ANISOU 4286 CA GLY B 224 5562 5318 5487 -345 602 -385 C ATOM 4287 C GLY B 224 -11.892 14.287 24.711 1.00 41.32 C ANISOU 4287 C GLY B 224 5325 5131 5243 -354 590 -440 C ATOM 4288 O GLY B 224 -11.025 13.981 23.887 1.00 44.59 O ANISOU 4288 O GLY B 224 5758 5548 5634 -341 592 -440 O ATOM 4289 N GLN B 225 -13.196 14.148 24.459 1.00 33.22 N ANISOU 4289 N GLN B 225 4264 4134 4224 -374 575 -490 N ATOM 4290 CA GLN B 225 -13.654 13.732 23.139 1.00 33.50 C ANISOU 4290 CA GLN B 225 4280 4216 4234 -380 555 -548 C ATOM 4291 C GLN B 225 -13.184 14.704 22.067 1.00 45.34 C ANISOU 4291 C GLN B 225 5781 5769 5675 -337 521 -524 C ATOM 4292 O GLN B 225 -12.846 14.292 20.952 1.00 42.51 O ANISOU 4292 O GLN B 225 5427 5438 5286 -329 514 -552 O ATOM 4293 CB GLN B 225 -15.178 13.617 23.123 1.00 36.09 C ANISOU 4293 CB GLN B 225 4562 4574 4576 -406 540 -602 C ATOM 4294 CG GLN B 225 -15.721 12.529 24.026 1.00 37.91 C ANISOU 4294 CG GLN B 225 4787 4750 4867 -452 579 -634 C ATOM 4295 CD GLN B 225 -15.288 11.147 23.583 1.00 42.34 C ANISOU 4295 CD GLN B 225 5364 5276 5447 -478 612 -680 C ATOM 4296 OE1 GLN B 225 -14.511 10.479 24.265 1.00 55.13 O ANISOU 4296 OE1 GLN B 225 7017 6833 7096 -484 654 -654 O ATOM 4297 NE2 GLN B 225 -15.788 10.711 22.431 1.00 45.52 N ANISOU 4297 NE2 GLN B 225 5742 5722 5832 -491 592 -748 N ATOM 4298 N LEU B 226 -13.170 16.001 22.382 1.00 51.90 N ANISOU 4298 N LEU B 226 6610 6618 6493 -308 501 -472 N ATOM 4299 CA LEU B 226 -12.671 16.988 21.432 1.00 52.24 C ANISOU 4299 CA LEU B 226 6656 6706 6487 -264 476 -438 C ATOM 4300 C LEU B 226 -11.179 16.813 21.173 1.00 54.44 C ANISOU 4300 C LEU B 226 6973 6956 6756 -247 496 -403 C ATOM 4301 O LEU B 226 -10.727 16.926 20.028 1.00 59.35 O ANISOU 4301 O LEU B 226 7600 7614 7336 -221 485 -403 O ATOM 4302 CB LEU B 226 -12.961 18.400 21.940 1.00 56.29 C ANISOU 4302 CB LEU B 226 7159 7231 6998 -239 459 -388 C ATOM 4303 CG LEU B 226 -14.432 18.803 22.034 1.00 51.66 C ANISOU 4303 CG LEU B 226 6531 6684 6412 -244 435 -415 C ATOM 4304 CD1 LEU B 226 -14.572 20.226 22.555 1.00 54.88 C ANISOU 4304 CD1 LEU B 226 6935 7096 6821 -216 424 -360 C ATOM 4305 CD2 LEU B 226 -15.101 18.662 20.681 1.00 54.84 C ANISOU 4305 CD2 LEU B 226 6907 7159 6772 -232 406 -461 C ATOM 4306 N VAL B 227 -10.398 16.538 22.219 1.00 46.21 N ANISOU 4306 N VAL B 227 5956 5854 5748 -259 525 -372 N ATOM 4307 CA VAL B 227 -8.943 16.531 22.082 1.00 42.49 C ANISOU 4307 CA VAL B 227 5518 5358 5270 -240 542 -332 C ATOM 4308 C VAL B 227 -8.481 15.316 21.284 1.00 55.26 C ANISOU 4308 C VAL B 227 7150 6970 6877 -249 560 -369 C ATOM 4309 O VAL B 227 -7.803 15.448 20.258 1.00 57.32 O ANISOU 4309 O VAL B 227 7422 7256 7102 -223 555 -361 O ATOM 4310 CB VAL B 227 -8.270 16.587 23.464 1.00 55.64 C ANISOU 4310 CB VAL B 227 7202 6968 6972 -247 566 -290 C ATOM 4311 CG1 VAL B 227 -6.799 16.217 23.354 1.00 58.34 C ANISOU 4311 CG1 VAL B 227 7574 7281 7312 -234 588 -260 C ATOM 4312 CG2 VAL B 227 -8.421 17.975 24.061 1.00 45.66 C ANISOU 4312 CG2 VAL B 227 5928 5711 5710 -229 547 -248 C ATOM 4313 N PHE B 228 -8.844 14.119 21.736 1.00 47.90 N ANISOU 4313 N PHE B 228 6219 6003 5977 -284 584 -412 N ATOM 4314 CA PHE B 228 -8.393 12.889 21.086 1.00 52.97 C ANISOU 4314 CA PHE B 228 6878 6630 6619 -296 607 -450 C ATOM 4315 C PHE B 228 -9.334 12.462 19.963 1.00 50.78 C ANISOU 4315 C PHE B 228 6576 6402 6318 -307 587 -522 C ATOM 4316 O PHE B 228 -9.735 11.302 19.868 1.00 60.17 O ANISOU 4316 O PHE B 228 7762 7571 7531 -340 606 -581 O ATOM 4317 CB PHE B 228 -8.245 11.784 22.126 1.00 52.90 C ANISOU 4317 CB PHE B 228 6885 6554 6661 -326 651 -458 C ATOM 4318 N THR B 229 -9.666 13.410 19.086 1.00 58.99 N ANISOU 4318 N THR B 229 7597 7506 7310 -278 549 -518 N ATOM 4319 CA THR B 229 -10.513 13.170 17.917 1.00 55.84 C ANISOU 4319 CA THR B 229 7171 7171 6876 -278 522 -583 C ATOM 4320 C THR B 229 -10.604 14.425 17.054 1.00 58.69 C ANISOU 4320 C THR B 229 7518 7602 7179 -231 484 -553 C ATOM 4321 O THR B 229 -11.336 15.363 17.378 1.00 58.58 O ANISOU 4321 O THR B 229 7481 7614 7164 -221 461 -532 O ATOM 4322 CB THR B 229 -11.939 12.740 18.304 1.00 48.46 C ANISOU 4322 CB THR B 229 6198 6242 5971 -319 513 -644 C ATOM 4323 N GLN B 244 -15.424 26.695 10.530 1.00 59.92 N ANISOU 4323 N GLN B 244 7470 8419 6879 334 257 -156 N ATOM 4324 CA GLN B 244 -14.104 26.144 10.824 1.00 58.31 C ANISOU 4324 CA GLN B 244 7308 8139 6708 301 288 -146 C ATOM 4325 C GLN B 244 -13.316 27.102 11.715 1.00 57.55 C ANISOU 4325 C GLN B 244 7240 7957 6670 300 323 -69 C ATOM 4326 O GLN B 244 -13.061 26.807 12.884 1.00 49.72 O ANISOU 4326 O GLN B 244 6261 6889 5741 245 336 -79 O ATOM 4327 CB GLN B 244 -13.335 25.861 9.530 1.00 60.99 C ANISOU 4327 CB GLN B 244 7665 8525 6984 343 293 -140 C ATOM 4328 N LYS B 245 -12.927 28.248 11.151 1.00 64.06 N ANISOU 4328 N LYS B 245 8073 8794 7472 362 342 8 N ATOM 4329 CA LYS B 245 -12.310 29.294 11.961 1.00 66.10 C ANISOU 4329 CA LYS B 245 8351 8975 7789 363 375 78 C ATOM 4330 C LYS B 245 -13.321 29.940 12.899 1.00 62.38 C ANISOU 4330 C LYS B 245 7858 8490 7355 350 365 79 C ATOM 4331 O LYS B 245 -12.970 30.316 14.023 1.00 63.38 O ANISOU 4331 O LYS B 245 7998 8538 7545 317 384 99 O ATOM 4332 CB LYS B 245 -11.665 30.350 11.061 1.00 72.83 C ANISOU 4332 CB LYS B 245 9217 9843 8613 433 403 160 C ATOM 4333 CG LYS B 245 -10.769 31.331 11.803 1.00 72.35 C ANISOU 4333 CG LYS B 245 9179 9694 8618 429 444 228 C ATOM 4334 CD LYS B 245 -10.125 32.324 10.846 1.00 76.24 C ANISOU 4334 CD LYS B 245 9684 10199 9086 498 478 309 C ATOM 4335 N ALA B 246 -14.574 30.079 12.456 1.00 49.42 N ANISOU 4335 N ALA B 246 6180 6924 5672 378 335 57 N ATOM 4336 CA ALA B 246 -15.619 30.602 13.328 1.00 49.49 C ANISOU 4336 CA ALA B 246 6165 6925 5714 366 324 53 C ATOM 4337 C ALA B 246 -15.882 29.663 14.498 1.00 40.09 C ANISOU 4337 C ALA B 246 4972 5686 4575 288 314 -10 C ATOM 4338 O ALA B 246 -16.079 30.116 15.631 1.00 38.12 O ANISOU 4338 O ALA B 246 4724 5381 4380 263 325 3 O ATOM 4339 CB ALA B 246 -16.900 30.839 12.528 1.00 50.76 C ANISOU 4339 CB ALA B 246 6283 7188 5816 414 291 38 C ATOM 4340 N GLU B 247 -15.902 28.352 14.243 1.00 32.08 N ANISOU 4340 N GLU B 247 3953 4691 3544 252 298 -79 N ATOM 4341 CA GLU B 247 -16.096 27.399 15.331 1.00 48.13 C ANISOU 4341 CA GLU B 247 5985 6674 5627 180 296 -134 C ATOM 4342 C GLU B 247 -14.890 27.366 16.258 1.00 42.36 C ANISOU 4342 C GLU B 247 5295 5848 4952 147 329 -105 C ATOM 4343 O GLU B 247 -15.040 27.190 17.473 1.00 31.63 O ANISOU 4343 O GLU B 247 3939 4435 3645 103 336 -118 O ATOM 4344 CB GLU B 247 -16.379 26.004 14.772 1.00 42.52 C ANISOU 4344 CB GLU B 247 5261 6004 4890 150 275 -215 C ATOM 4345 CG GLU B 247 -17.592 25.927 13.851 1.00 44.53 C ANISOU 4345 CG GLU B 247 5470 6360 5089 178 237 -258 C ATOM 4346 CD GLU B 247 -18.927 26.052 14.580 1.00 45.75 C ANISOU 4346 CD GLU B 247 5584 6528 5270 156 219 -287 C ATOM 4347 OE1 GLU B 247 -18.949 26.426 15.775 1.00 52.77 O ANISOU 4347 OE1 GLU B 247 6484 7351 6217 131 237 -262 O ATOM 4348 OE2 GLU B 247 -19.965 25.764 13.946 1.00 45.18 O ANISOU 4348 OE2 GLU B 247 5469 6538 5160 166 186 -337 O ATOM 4349 N LYS B 248 -13.687 27.531 15.704 1.00 35.05 N ANISOU 4349 N LYS B 248 4399 4906 4014 170 350 -65 N ATOM 4350 CA LYS B 248 -12.482 27.511 16.525 1.00 39.49 C ANISOU 4350 CA LYS B 248 4995 5384 4625 141 380 -37 C ATOM 4351 C LYS B 248 -12.491 28.643 17.546 1.00 44.41 C ANISOU 4351 C LYS B 248 5622 5957 5297 142 394 8 C ATOM 4352 O LYS B 248 -12.036 28.469 18.683 1.00 22.57 O ANISOU 4352 O LYS B 248 2870 3126 2581 102 408 5 O ATOM 4353 CB LYS B 248 -11.245 27.599 15.632 1.00 27.18 C ANISOU 4353 CB LYS B 248 3461 3824 3041 172 400 1 C ATOM 4354 CG LYS B 248 -9.938 27.300 16.340 1.00 30.37 C ANISOU 4354 CG LYS B 248 3897 4152 3490 140 427 17 C ATOM 4355 CD LYS B 248 -8.752 27.610 15.438 1.00 44.47 C ANISOU 4355 CD LYS B 248 5704 5937 5254 176 450 65 C ATOM 4356 CE LYS B 248 -8.774 29.066 14.977 1.00 44.27 C ANISOU 4356 CE LYS B 248 5674 5924 5222 231 463 133 C ATOM 4357 NZ LYS B 248 -7.603 29.399 14.113 1.00 59.01 N ANISOU 4357 NZ LYS B 248 7561 7788 7073 267 492 184 N ATOM 4358 N GLU B 249 -13.003 29.814 17.156 1.00 35.71 N ANISOU 4358 N GLU B 249 4505 4884 4180 190 393 51 N ATOM 4359 CA GLU B 249 -13.074 30.935 18.086 1.00 37.31 C ANISOU 4359 CA GLU B 249 4710 5037 4430 193 409 91 C ATOM 4360 C GLU B 249 -13.977 30.613 19.269 1.00 36.71 C ANISOU 4360 C GLU B 249 4618 4943 4388 150 395 48 C ATOM 4361 O GLU B 249 -13.639 30.917 20.419 1.00 27.62 O ANISOU 4361 O GLU B 249 3480 3729 3287 123 410 58 O ATOM 4362 CB GLU B 249 -13.568 32.190 17.365 1.00 35.33 C ANISOU 4362 CB GLU B 249 4445 4825 4155 257 413 143 C ATOM 4363 CG GLU B 249 -13.486 33.455 18.207 1.00 40.45 C ANISOU 4363 CG GLU B 249 5098 5415 4854 264 437 190 C ATOM 4364 CD GLU B 249 -14.178 34.643 17.564 1.00 46.65 C ANISOU 4364 CD GLU B 249 5868 6239 5619 328 442 239 C ATOM 4365 OE1 GLU B 249 -15.206 34.439 16.884 1.00 43.32 O ANISOU 4365 OE1 GLU B 249 5419 5894 5147 356 416 220 O ATOM 4366 OE2 GLU B 249 -13.693 35.782 17.744 1.00 33.50 O ANISOU 4366 OE2 GLU B 249 4215 4527 3988 352 474 295 O ATOM 4367 N VAL B 250 -15.129 29.991 19.008 1.00 37.71 N ANISOU 4367 N VAL B 250 4715 5126 4486 144 368 0 N ATOM 4368 CA VAL B 250 -16.043 29.639 20.090 1.00 26.10 C ANISOU 4368 CA VAL B 250 3228 3641 3048 104 357 -40 C ATOM 4369 C VAL B 250 -15.429 28.572 20.988 1.00 29.38 C ANISOU 4369 C VAL B 250 3664 4001 3499 46 368 -74 C ATOM 4370 O VAL B 250 -15.512 28.657 22.219 1.00 32.43 O ANISOU 4370 O VAL B 250 4055 4339 3929 18 378 -76 O ATOM 4371 CB VAL B 250 -17.399 29.190 19.516 1.00 33.10 C ANISOU 4371 CB VAL B 250 4073 4604 3899 110 326 -87 C ATOM 4372 CG1 VAL B 250 -18.333 28.753 20.636 1.00 20.71 C ANISOU 4372 CG1 VAL B 250 2484 3017 2366 66 320 -128 C ATOM 4373 CG2 VAL B 250 -18.023 30.317 18.709 1.00 31.09 C ANISOU 4373 CG2 VAL B 250 3798 4408 3608 174 317 -47 C ATOM 4374 N THR B 251 -14.809 27.552 20.389 1.00 28.75 N ANISOU 4374 N THR B 251 3596 3928 3400 32 368 -100 N ATOM 4375 CA THR B 251 -14.186 26.496 21.181 1.00 24.16 C ANISOU 4375 CA THR B 251 3035 3294 2850 -17 383 -127 C ATOM 4376 C THR B 251 -13.102 27.060 22.092 1.00 26.72 C ANISOU 4376 C THR B 251 3389 3551 3214 -23 407 -84 C ATOM 4377 O THR B 251 -12.955 26.622 23.239 1.00 32.72 O ANISOU 4377 O THR B 251 4157 4265 4010 -59 417 -97 O ATOM 4378 CB THR B 251 -13.607 25.419 20.260 1.00 37.26 C ANISOU 4378 CB THR B 251 4706 4972 4480 -24 382 -156 C ATOM 4379 OG1 THR B 251 -14.661 24.820 19.497 1.00 33.17 O ANISOU 4379 OG1 THR B 251 4157 4518 3929 -25 358 -209 O ATOM 4380 CG2 THR B 251 -12.896 24.338 21.064 1.00 21.55 C ANISOU 4380 CG2 THR B 251 2738 2925 2524 -70 402 -178 C ATOM 4381 N ARG B 252 -12.338 28.037 21.600 1.00 25.16 N ANISOU 4381 N ARG B 252 3204 3348 3010 13 417 -32 N ATOM 4382 CA ARG B 252 -11.300 28.651 22.423 1.00 27.52 C ANISOU 4382 CA ARG B 252 3524 3585 3348 7 439 6 C ATOM 4383 C ARG B 252 -11.890 29.411 23.605 1.00 32.88 C ANISOU 4383 C ARG B 252 4194 4234 4063 -2 440 12 C ATOM 4384 O ARG B 252 -11.375 29.318 24.725 1.00 23.42 O ANISOU 4384 O ARG B 252 3010 2988 2901 -29 451 10 O ATOM 4385 CB ARG B 252 -10.438 29.576 21.565 1.00 36.35 C ANISOU 4385 CB ARG B 252 4653 4703 4456 48 454 60 C ATOM 4386 CG ARG B 252 -9.504 28.836 20.629 1.00 28.00 C ANISOU 4386 CG ARG B 252 3611 3657 3370 53 461 60 C ATOM 4387 CD ARG B 252 -8.823 29.781 19.664 1.00 34.24 C ANISOU 4387 CD ARG B 252 4408 4456 4145 99 477 116 C ATOM 4388 NE ARG B 252 -7.748 29.120 18.935 1.00 32.63 N ANISOU 4388 NE ARG B 252 4222 4253 3922 102 489 121 N ATOM 4389 CZ ARG B 252 -7.051 29.684 17.960 1.00 30.92 C ANISOU 4389 CZ ARG B 252 4014 4048 3687 142 507 166 C ATOM 4390 NH1 ARG B 252 -7.294 30.922 17.563 1.00 34.44 N ANISOU 4390 NH1 ARG B 252 4452 4503 4132 184 517 214 N ATOM 4391 NH2 ARG B 252 -6.090 28.986 17.361 1.00 54.97 N ANISOU 4391 NH2 ARG B 252 7076 7094 6716 143 518 167 N ATOM 4392 N MET B 253 -12.967 30.168 23.382 1.00 24.09 N ANISOU 4392 N MET B 253 3058 3154 2940 24 429 19 N ATOM 4393 CA MET B 253 -13.566 30.922 24.479 1.00 28.32 C ANISOU 4393 CA MET B 253 3587 3664 3510 18 432 24 C ATOM 4394 C MET B 253 -14.167 29.994 25.529 1.00 26.45 C ANISOU 4394 C MET B 253 3343 3415 3290 -24 426 -22 C ATOM 4395 O MET B 253 -14.094 30.281 26.730 1.00 18.24 O ANISOU 4395 O MET B 253 2311 2335 2284 -41 435 -21 O ATOM 4396 CB MET B 253 -14.620 31.892 23.945 1.00 25.56 C ANISOU 4396 CB MET B 253 3214 3356 3144 59 423 44 C ATOM 4397 CG MET B 253 -15.390 32.611 25.048 1.00 23.06 C ANISOU 4397 CG MET B 253 2887 3016 2860 55 426 44 C ATOM 4398 SD MET B 253 -16.675 33.726 24.461 1.00 32.20 S ANISOU 4398 SD MET B 253 4015 4222 3998 107 418 69 S ATOM 4399 CE MET B 253 -17.637 33.917 25.959 1.00 28.78 C ANISOU 4399 CE MET B 253 3569 3762 3602 82 417 45 C ATOM 4400 N VAL B 254 -14.759 28.876 25.100 1.00 21.04 N ANISOU 4400 N VAL B 254 2645 2766 2582 -41 412 -64 N ATOM 4401 CA VAL B 254 -15.346 27.933 26.051 1.00 32.05 C ANISOU 4401 CA VAL B 254 4033 4148 3998 -82 413 -106 C ATOM 4402 C VAL B 254 -14.272 27.364 26.972 1.00 24.30 C ANISOU 4402 C VAL B 254 3080 3110 3043 -110 432 -104 C ATOM 4403 O VAL B 254 -14.509 27.153 28.168 1.00 24.39 O ANISOU 4403 O VAL B 254 3093 3092 3080 -132 441 -115 O ATOM 4404 CB VAL B 254 -16.114 26.824 25.304 1.00 22.69 C ANISOU 4404 CB VAL B 254 2826 3008 2788 -96 398 -154 C ATOM 4405 CG1 VAL B 254 -16.623 25.771 26.278 1.00 24.11 C ANISOU 4405 CG1 VAL B 254 3001 3165 2996 -141 407 -195 C ATOM 4406 CG2 VAL B 254 -17.278 27.420 24.532 1.00 19.44 C ANISOU 4406 CG2 VAL B 254 2379 2658 2348 -67 375 -158 C ATOM 4407 N ILE B 255 -13.073 27.118 26.437 1.00 26.74 N ANISOU 4407 N ILE B 255 3411 3406 3342 -106 440 -89 N ATOM 4408 CA ILE B 255 -11.972 26.633 27.269 1.00 28.52 C ANISOU 4408 CA ILE B 255 3661 3584 3590 -127 458 -84 C ATOM 4409 C ILE B 255 -11.618 27.659 28.338 1.00 19.08 C ANISOU 4409 C ILE B 255 2473 2353 2424 -122 465 -58 C ATOM 4410 O ILE B 255 -11.440 27.319 29.514 1.00 30.84 O ANISOU 4410 O ILE B 255 3971 3813 3935 -142 474 -67 O ATOM 4411 CB ILE B 255 -10.751 26.286 26.395 1.00 26.71 C ANISOU 4411 CB ILE B 255 3451 3352 3345 -119 465 -70 C ATOM 4412 CG1 ILE B 255 -11.101 25.196 25.381 1.00 27.46 C ANISOU 4412 CG1 ILE B 255 3541 3483 3411 -126 458 -104 C ATOM 4413 CG2 ILE B 255 -9.585 25.836 27.262 1.00 20.05 C ANISOU 4413 CG2 ILE B 255 2630 2463 2524 -137 483 -62 C ATOM 4414 CD1 ILE B 255 -10.028 24.972 24.337 1.00 36.33 C ANISOU 4414 CD1 ILE B 255 4681 4612 4511 -110 465 -88 C ATOM 4415 N ILE B 256 -11.518 28.932 27.949 1.00 27.25 N ANISOU 4415 N ILE B 256 3504 3390 3460 -94 463 -25 N ATOM 4416 CA ILE B 256 -11.168 29.977 28.905 1.00 27.89 C ANISOU 4416 CA ILE B 256 3589 3435 3572 -90 471 -5 C ATOM 4417 C ILE B 256 -12.283 30.179 29.927 1.00 20.71 C ANISOU 4417 C ILE B 256 2667 2524 2677 -98 467 -24 C ATOM 4418 O ILE B 256 -12.012 30.476 31.097 1.00 26.57 O ANISOU 4418 O ILE B 256 3417 3235 3443 -108 474 -25 O ATOM 4419 CB ILE B 256 -10.821 31.278 28.157 1.00 20.29 C ANISOU 4419 CB ILE B 256 2626 2471 2613 -56 476 34 C ATOM 4420 CG1 ILE B 256 -9.566 31.075 27.304 1.00 34.71 C ANISOU 4420 CG1 ILE B 256 4467 4292 4431 -50 486 56 C ATOM 4421 CG2 ILE B 256 -10.603 32.427 29.127 1.00 22.69 C ANISOU 4421 CG2 ILE B 256 2931 2735 2953 -54 486 48 C ATOM 4422 CD1 ILE B 256 -8.329 30.722 28.112 1.00 28.48 C ANISOU 4422 CD1 ILE B 256 3694 3464 3665 -73 496 54 C ATOM 4423 N MET B 257 -13.544 30.020 29.518 1.00 22.21 N ANISOU 4423 N MET B 257 2836 2751 2850 -93 455 -39 N ATOM 4424 CA MET B 257 -14.643 30.117 30.476 1.00 20.45 C ANISOU 4424 CA MET B 257 2600 2530 2642 -101 454 -57 C ATOM 4425 C MET B 257 -14.531 29.051 31.559 1.00 16.93 C ANISOU 4425 C MET B 257 2162 2061 2208 -134 463 -83 C ATOM 4426 O MET B 257 -14.740 29.335 32.745 1.00 32.65 O ANISOU 4426 O MET B 257 4156 4032 4218 -139 470 -86 O ATOM 4427 CB MET B 257 -15.985 29.996 29.758 1.00 19.04 C ANISOU 4427 CB MET B 257 2392 2399 2443 -91 439 -73 C ATOM 4428 CG MET B 257 -16.299 31.149 28.826 1.00 27.04 C ANISOU 4428 CG MET B 257 3393 3440 3442 -51 432 -43 C ATOM 4429 SD MET B 257 -17.976 31.065 28.174 1.00 27.49 S ANISOU 4429 SD MET B 257 3410 3562 3475 -36 411 -64 S ATOM 4430 CE MET B 257 -18.927 31.155 29.689 1.00 20.92 C ANISOU 4430 CE MET B 257 2566 2708 2675 -55 418 -82 C ATOM 4431 N VAL B 258 -14.217 27.815 31.167 1.00 19.34 N ANISOU 4431 N VAL B 258 2474 2372 2502 -153 466 -101 N ATOM 4432 CA VAL B 258 -14.057 26.741 32.143 1.00 17.92 C ANISOU 4432 CA VAL B 258 2305 2170 2335 -180 481 -120 C ATOM 4433 C VAL B 258 -12.884 27.036 33.070 1.00 24.44 C ANISOU 4433 C VAL B 258 3154 2960 3174 -179 491 -101 C ATOM 4434 O VAL B 258 -12.979 26.860 34.291 1.00 18.22 O ANISOU 4434 O VAL B 258 2370 2154 2399 -187 501 -106 O ATOM 4435 CB VAL B 258 -13.887 25.388 31.429 1.00 16.49 C ANISOU 4435 CB VAL B 258 2127 1997 2142 -198 486 -142 C ATOM 4436 CG1 VAL B 258 -13.645 24.281 32.440 1.00 19.24 C ANISOU 4436 CG1 VAL B 258 2489 2316 2506 -222 508 -154 C ATOM 4437 CG2 VAL B 258 -15.111 25.075 30.595 1.00 20.83 C ANISOU 4437 CG2 VAL B 258 2648 2586 2679 -202 473 -170 C ATOM 4438 N ILE B 259 -11.761 27.486 32.506 1.00 22.80 N ANISOU 4438 N ILE B 259 2958 2743 2963 -167 489 -79 N ATOM 4439 CA ILE B 259 -10.587 27.796 33.316 1.00 17.26 C ANISOU 4439 CA ILE B 259 2273 2011 2274 -167 496 -65 C ATOM 4440 C ILE B 259 -10.894 28.929 34.286 1.00 23.97 C ANISOU 4440 C ILE B 259 3118 2849 3143 -158 494 -61 C ATOM 4441 O ILE B 259 -10.477 28.901 35.451 1.00 15.79 O ANISOU 4441 O ILE B 259 2088 1795 2115 -163 500 -66 O ATOM 4442 CB ILE B 259 -9.390 28.135 32.410 1.00 22.06 C ANISOU 4442 CB ILE B 259 2889 2613 2878 -156 496 -42 C ATOM 4443 CG1 ILE B 259 -8.973 26.906 31.601 1.00 30.71 C ANISOU 4443 CG1 ILE B 259 3994 3719 3956 -165 501 -48 C ATOM 4444 CG2 ILE B 259 -8.225 28.664 33.230 1.00 19.56 C ANISOU 4444 CG2 ILE B 259 2582 2269 2581 -155 501 -30 C ATOM 4445 CD1 ILE B 259 -7.830 27.162 30.653 1.00 25.09 C ANISOU 4445 CD1 ILE B 259 3291 3005 3239 -152 504 -25 C ATOM 4446 N ALA B 260 -11.626 29.944 33.822 1.00 20.74 N ANISOU 4446 N ALA B 260 2694 2450 2736 -142 486 -53 N ATOM 4447 CA ALA B 260 -11.989 31.056 34.693 1.00 21.92 C ANISOU 4447 CA ALA B 260 2839 2585 2905 -132 487 -52 C ATOM 4448 C ALA B 260 -12.915 30.600 35.814 1.00 24.31 C ANISOU 4448 C ALA B 260 3136 2892 3208 -142 490 -74 C ATOM 4449 O ALA B 260 -12.820 31.090 36.946 1.00 20.01 O ANISOU 4449 O ALA B 260 2596 2331 2676 -140 494 -79 O ATOM 4450 CB ALA B 260 -12.639 32.171 33.874 1.00 23.28 C ANISOU 4450 CB ALA B 260 2998 2768 3080 -108 482 -35 C ATOM 4451 N PHE B 261 -13.823 29.669 35.516 1.00 22.32 N ANISOU 4451 N PHE B 261 2874 2662 2943 -152 490 -88 N ATOM 4452 CA PHE B 261 -14.720 29.146 36.542 1.00 16.32 C ANISOU 4452 CA PHE B 261 2108 1904 2188 -162 499 -106 C ATOM 4453 C PHE B 261 -13.939 28.438 37.644 1.00 23.74 C ANISOU 4453 C PHE B 261 3067 2825 3129 -172 512 -110 C ATOM 4454 O PHE B 261 -14.210 28.629 38.836 1.00 22.73 O ANISOU 4454 O PHE B 261 2941 2690 3006 -168 520 -115 O ATOM 4455 CB PHE B 261 -15.739 28.197 35.910 1.00 17.63 C ANISOU 4455 CB PHE B 261 2257 2096 2346 -175 499 -123 C ATOM 4456 CG PHE B 261 -16.742 27.644 36.885 1.00 31.59 C ANISOU 4456 CG PHE B 261 4015 3864 4123 -186 513 -140 C ATOM 4457 CD1 PHE B 261 -17.896 28.349 37.182 1.00 23.20 C ANISOU 4457 CD1 PHE B 261 2933 2816 3068 -176 510 -143 C ATOM 4458 CD2 PHE B 261 -16.528 26.424 37.508 1.00 23.32 C ANISOU 4458 CD2 PHE B 261 2978 2803 3078 -205 533 -149 C ATOM 4459 CE1 PHE B 261 -18.820 27.848 38.077 1.00 25.32 C ANISOU 4459 CE1 PHE B 261 3191 3085 3346 -185 525 -157 C ATOM 4460 CE2 PHE B 261 -17.446 25.921 38.409 1.00 28.04 C ANISOU 4460 CE2 PHE B 261 3566 3399 3687 -213 551 -160 C ATOM 4461 CZ PHE B 261 -18.593 26.634 38.691 1.00 24.15 C ANISOU 4461 CZ PHE B 261 3053 2922 3202 -204 547 -165 C ATOM 4462 N LEU B 262 -12.966 27.610 37.261 1.00 23.54 N ANISOU 4462 N LEU B 262 3055 2793 3096 -181 517 -106 N ATOM 4463 CA LEU B 262 -12.194 26.865 38.249 1.00 22.84 C ANISOU 4463 CA LEU B 262 2984 2690 3006 -186 531 -106 C ATOM 4464 C LEU B 262 -11.358 27.795 39.120 1.00 18.24 C ANISOU 4464 C LEU B 262 2408 2096 2428 -173 525 -100 C ATOM 4465 O LEU B 262 -11.280 27.610 40.338 1.00 23.40 O ANISOU 4465 O LEU B 262 3068 2746 3078 -169 533 -105 O ATOM 4466 CB LEU B 262 -11.315 25.833 37.545 1.00 20.87 C ANISOU 4466 CB LEU B 262 2745 2435 2748 -196 537 -101 C ATOM 4467 CG LEU B 262 -12.125 24.812 36.741 1.00 27.17 C ANISOU 4467 CG LEU B 262 3535 3244 3543 -212 545 -115 C ATOM 4468 CD1 LEU B 262 -11.227 23.983 35.836 1.00 18.10 C ANISOU 4468 CD1 LEU B 262 2400 2092 2387 -218 549 -112 C ATOM 4469 CD2 LEU B 262 -12.921 23.915 37.673 1.00 20.16 C ANISOU 4469 CD2 LEU B 262 2646 2350 2663 -222 567 -127 C ATOM 4470 N ILE B 263 -10.730 28.806 38.516 1.00 20.31 N ANISOU 4470 N ILE B 263 2668 2351 2697 -166 512 -90 N ATOM 4471 CA ILE B 263 -9.969 29.778 39.298 1.00 22.19 C ANISOU 4471 CA ILE B 263 2909 2577 2946 -157 506 -92 C ATOM 4472 C ILE B 263 -10.875 30.467 40.309 1.00 22.90 C ANISOU 4472 C ILE B 263 2993 2667 3042 -149 506 -106 C ATOM 4473 O ILE B 263 -10.512 30.643 41.479 1.00 26.32 O ANISOU 4473 O ILE B 263 3430 3097 3472 -144 507 -117 O ATOM 4474 CB ILE B 263 -9.288 30.800 38.367 1.00 18.92 C ANISOU 4474 CB ILE B 263 2491 2150 2547 -153 498 -78 C ATOM 4475 CG1 ILE B 263 -8.219 30.121 37.508 1.00 28.38 C ANISOU 4475 CG1 ILE B 263 3696 3348 3738 -158 500 -64 C ATOM 4476 CG2 ILE B 263 -8.694 31.950 39.173 1.00 23.65 C ANISOU 4476 CG2 ILE B 263 3087 2732 3166 -147 494 -87 C ATOM 4477 CD1 ILE B 263 -7.544 31.057 36.514 1.00 15.73 C ANISOU 4477 CD1 ILE B 263 2091 1734 2152 -152 497 -46 C ATOM 4478 N CYS B 264 -12.072 30.854 39.874 1.00 23.61 N ANISOU 4478 N CYS B 264 3071 2765 3136 -146 506 -105 N ATOM 4479 CA CYS B 264 -12.985 31.586 40.741 1.00 16.02 C ANISOU 4479 CA CYS B 264 2103 1803 2182 -135 508 -117 C ATOM 4480 C CYS B 264 -13.535 30.708 41.863 1.00 23.79 C ANISOU 4480 C CYS B 264 3089 2796 3152 -138 520 -128 C ATOM 4481 O CYS B 264 -13.634 31.157 43.010 1.00 16.11 O ANISOU 4481 O CYS B 264 2120 1823 2179 -127 523 -139 O ATOM 4482 CB CYS B 264 -14.122 32.171 39.906 1.00 21.28 C ANISOU 4482 CB CYS B 264 2752 2477 2854 -128 504 -110 C ATOM 4483 SG CYS B 264 -15.347 33.087 40.852 1.00 23.82 S ANISOU 4483 SG CYS B 264 3064 2801 3187 -112 510 -121 S ATOM 4484 N TRP B 265 -13.888 29.451 41.562 1.00 16.00 N ANISOU 4484 N TRP B 265 2103 1820 2157 -150 530 -125 N ATOM 4485 CA TRP B 265 -14.700 28.651 42.472 1.00 20.88 C ANISOU 4485 CA TRP B 265 2720 2445 2769 -151 549 -131 C ATOM 4486 C TRP B 265 -13.978 27.492 43.150 1.00 27.36 C ANISOU 4486 C TRP B 265 3557 3263 3577 -154 566 -127 C ATOM 4487 O TRP B 265 -14.457 27.023 44.188 1.00 18.97 O ANISOU 4487 O TRP B 265 2496 2203 2508 -147 584 -128 O ATOM 4488 CB TRP B 265 -15.934 28.103 41.736 1.00 24.02 C ANISOU 4488 CB TRP B 265 3100 2854 3173 -163 555 -135 C ATOM 4489 CG TRP B 265 -17.005 29.139 41.534 1.00 22.59 C ANISOU 4489 CG TRP B 265 2899 2682 3000 -153 546 -139 C ATOM 4490 CD1 TRP B 265 -17.288 29.821 40.382 1.00 16.37 C ANISOU 4490 CD1 TRP B 265 2099 1905 2218 -149 530 -134 C ATOM 4491 CD2 TRP B 265 -17.923 29.624 42.523 1.00 16.43 C ANISOU 4491 CD2 TRP B 265 2112 1906 2225 -142 555 -145 C ATOM 4492 NE1 TRP B 265 -18.331 30.694 40.594 1.00 16.87 N ANISOU 4492 NE1 TRP B 265 2146 1976 2289 -135 528 -136 N ATOM 4493 CE2 TRP B 265 -18.736 30.593 41.899 1.00 16.54 C ANISOU 4493 CE2 TRP B 265 2107 1930 2249 -132 543 -144 C ATOM 4494 CE3 TRP B 265 -18.132 29.336 43.878 1.00 25.46 C ANISOU 4494 CE3 TRP B 265 3262 3047 3363 -135 573 -149 C ATOM 4495 CZ2 TRP B 265 -19.747 31.267 42.581 1.00 16.70 C ANISOU 4495 CZ2 TRP B 265 2116 1956 2276 -117 550 -148 C ATOM 4496 CZ3 TRP B 265 -19.132 30.008 44.553 1.00 16.65 C ANISOU 4496 CZ3 TRP B 265 2136 1938 2253 -120 579 -154 C ATOM 4497 CH2 TRP B 265 -19.929 30.961 43.904 1.00 16.75 C ANISOU 4497 CH2 TRP B 265 2129 1958 2277 -113 568 -155 C ATOM 4498 N LEU B 266 -12.857 27.011 42.604 1.00 20.87 N ANISOU 4498 N LEU B 266 2746 2435 2750 -160 562 -119 N ATOM 4499 CA LEU B 266 -12.134 25.921 43.264 1.00 23.06 C ANISOU 4499 CA LEU B 266 3038 2709 3014 -157 580 -111 C ATOM 4500 C LEU B 266 -11.641 26.282 44.660 1.00 23.70 C ANISOU 4500 C LEU B 266 3126 2798 3080 -136 580 -112 C ATOM 4501 O LEU B 266 -11.840 25.472 45.583 1.00 25.81 O ANISOU 4501 O LEU B 266 3401 3070 3335 -126 604 -106 O ATOM 4502 CB LEU B 266 -10.972 25.439 42.389 1.00 28.40 C ANISOU 4502 CB LEU B 266 3723 3380 3689 -164 575 -101 C ATOM 4503 CG LEU B 266 -11.289 24.475 41.244 1.00 37.70 C ANISOU 4503 CG LEU B 266 4900 4552 4872 -183 585 -100 C ATOM 4504 CD1 LEU B 266 -10.003 23.888 40.692 1.00 32.00 C ANISOU 4504 CD1 LEU B 266 4191 3824 4144 -184 586 -89 C ATOM 4505 CD2 LEU B 266 -12.217 23.371 41.718 1.00 34.07 C ANISOU 4505 CD2 LEU B 266 4439 4088 4417 -191 614 -104 C ATOM 4506 N PRO B 267 -10.992 27.435 44.898 1.00 21.58 N ANISOU 4506 N PRO B 267 2856 2531 2812 -127 558 -122 N ATOM 4507 CA PRO B 267 -10.540 27.723 46.271 1.00 23.05 C ANISOU 4507 CA PRO B 267 3047 2731 2980 -106 557 -130 C ATOM 4508 C PRO B 267 -11.670 27.739 47.281 1.00 23.38 C ANISOU 4508 C PRO B 267 3088 2782 3014 -93 572 -136 C ATOM 4509 O PRO B 267 -11.493 27.278 48.416 1.00 20.78 O ANISOU 4509 O PRO B 267 2766 2469 2662 -73 585 -134 O ATOM 4510 CB PRO B 267 -9.880 29.104 46.142 1.00 25.80 C ANISOU 4510 CB PRO B 267 3388 3074 3342 -106 530 -147 C ATOM 4511 CG PRO B 267 -9.511 29.218 44.718 1.00 22.80 C ANISOU 4511 CG PRO B 267 3004 2678 2980 -123 522 -137 C ATOM 4512 CD PRO B 267 -10.602 28.515 43.973 1.00 19.67 C ANISOU 4512 CD PRO B 267 2606 2280 2588 -134 536 -126 C ATOM 4513 N TYR B 268 -12.835 28.260 46.899 1.00 24.51 N ANISOU 4513 N TYR B 268 3219 2918 3174 -100 572 -142 N ATOM 4514 CA TYR B 268 -13.961 28.291 47.823 1.00 22.45 C ANISOU 4514 CA TYR B 268 2955 2666 2908 -88 589 -146 C ATOM 4515 C TYR B 268 -14.474 26.886 48.110 1.00 21.92 C ANISOU 4515 C TYR B 268 2892 2601 2834 -89 622 -129 C ATOM 4516 O TYR B 268 -14.747 26.536 49.264 1.00 20.78 O ANISOU 4516 O TYR B 268 2754 2468 2672 -69 643 -124 O ATOM 4517 CB TYR B 268 -15.082 29.163 47.264 1.00 19.18 C ANISOU 4517 CB TYR B 268 2525 2246 2515 -94 583 -154 C ATOM 4518 CG TYR B 268 -16.301 29.182 48.152 1.00 19.10 C ANISOU 4518 CG TYR B 268 2509 2246 2502 -82 602 -157 C ATOM 4519 CD1 TYR B 268 -16.344 29.984 49.284 1.00 16.80 C ANISOU 4519 CD1 TYR B 268 2222 1964 2199 -59 600 -172 C ATOM 4520 CD2 TYR B 268 -17.404 28.386 47.866 1.00 20.76 C ANISOU 4520 CD2 TYR B 268 2709 2457 2724 -93 623 -148 C ATOM 4521 CE1 TYR B 268 -17.453 29.998 50.104 1.00 17.00 C ANISOU 4521 CE1 TYR B 268 2242 1997 2219 -45 620 -173 C ATOM 4522 CE2 TYR B 268 -18.517 28.394 48.677 1.00 18.00 C ANISOU 4522 CE2 TYR B 268 2351 2115 2374 -82 644 -149 C ATOM 4523 CZ TYR B 268 -18.538 29.201 49.794 1.00 17.04 C ANISOU 4523 CZ TYR B 268 2235 2002 2237 -56 643 -159 C ATOM 4524 OH TYR B 268 -19.652 29.205 50.600 1.00 18.49 O ANISOU 4524 OH TYR B 268 2412 2195 2420 -42 666 -158 O ATOM 4525 N ALA B 269 -14.631 26.073 47.065 1.00 18.66 N ANISOU 4525 N ALA B 269 2477 2177 2438 -112 630 -120 N ATOM 4526 CA ALA B 269 -15.109 24.709 47.256 1.00 22.85 C ANISOU 4526 CA ALA B 269 3010 2702 2971 -118 666 -106 C ATOM 4527 C ALA B 269 -14.123 23.891 48.079 1.00 19.17 C ANISOU 4527 C ALA B 269 2563 2238 2482 -99 684 -89 C ATOM 4528 O ALA B 269 -14.527 23.086 48.927 1.00 18.13 O ANISOU 4528 O ALA B 269 2438 2108 2344 -86 719 -75 O ATOM 4529 CB ALA B 269 -15.363 24.046 45.903 1.00 24.08 C ANISOU 4529 CB ALA B 269 3157 2844 3147 -147 667 -108 C ATOM 4530 N GLY B 270 -12.823 24.073 47.832 1.00 18.35 N ANISOU 4530 N GLY B 270 2468 2137 2366 -94 663 -88 N ATOM 4531 CA GLY B 270 -11.826 23.331 48.588 1.00 19.32 C ANISOU 4531 CA GLY B 270 2607 2269 2465 -72 677 -71 C ATOM 4532 C GLY B 270 -11.830 23.688 50.062 1.00 31.31 C ANISOU 4532 C GLY B 270 4130 3812 3954 -38 681 -71 C ATOM 4533 O GLY B 270 -11.796 22.811 50.929 1.00 25.90 O ANISOU 4533 O GLY B 270 3456 3136 3250 -14 713 -50 O ATOM 4534 N VAL B 271 -11.869 24.987 50.366 1.00 20.51 N ANISOU 4534 N VAL B 271 2754 2458 2582 -32 652 -95 N ATOM 4535 CA VAL B 271 -11.938 25.418 51.757 1.00 23.80 C ANISOU 4535 CA VAL B 271 3173 2901 2968 1 653 -103 C ATOM 4536 C VAL B 271 -13.246 24.964 52.389 1.00 26.53 C ANISOU 4536 C VAL B 271 3520 3247 3315 10 689 -91 C ATOM 4537 O VAL B 271 -13.272 24.501 53.537 1.00 29.29 O ANISOU 4537 O VAL B 271 3878 3617 3635 43 713 -77 O ATOM 4538 CB VAL B 271 -11.759 26.944 51.857 1.00 25.42 C ANISOU 4538 CB VAL B 271 3368 3113 3176 0 616 -137 C ATOM 4539 CG1 VAL B 271 -12.099 27.422 53.254 1.00 26.37 C ANISOU 4539 CG1 VAL B 271 3491 3262 3268 33 620 -151 C ATOM 4540 CG2 VAL B 271 -10.332 27.319 51.500 1.00 27.49 C ANISOU 4540 CG2 VAL B 271 3629 3380 3436 -4 586 -148 C ATOM 4541 N ALA B 272 -14.351 25.083 51.650 1.00 28.07 N ANISOU 4541 N ALA B 272 3702 3420 3542 -16 695 -95 N ATOM 4542 CA ALA B 272 -15.643 24.661 52.177 1.00 26.38 C ANISOU 4542 CA ALA B 272 3484 3205 3335 -10 731 -85 C ATOM 4543 C ALA B 272 -15.648 23.173 52.497 1.00 22.26 C ANISOU 4543 C ALA B 272 2973 2675 2811 -4 776 -53 C ATOM 4544 O ALA B 272 -16.151 22.760 53.549 1.00 24.50 O ANISOU 4544 O ALA B 272 3262 2968 3080 22 811 -37 O ATOM 4545 CB ALA B 272 -16.756 24.999 51.186 1.00 18.43 C ANISOU 4545 CB ALA B 272 2458 2180 2365 -42 726 -96 C ATOM 4546 N PHE B 273 -15.084 22.352 51.609 1.00 17.33 N ANISOU 4546 N PHE B 273 2353 2031 2202 -24 781 -43 N ATOM 4547 CA PHE B 273 -15.074 20.916 51.861 1.00 23.20 C ANISOU 4547 CA PHE B 273 3107 2759 2948 -19 829 -13 C ATOM 4548 C PHE B 273 -14.110 20.544 52.980 1.00 20.30 C ANISOU 4548 C PHE B 273 2759 2415 2539 26 843 10 C ATOM 4549 O PHE B 273 -14.354 19.571 53.703 1.00 18.00 O ANISOU 4549 O PHE B 273 2478 2120 2243 47 891 41 O ATOM 4550 CB PHE B 273 -14.727 20.146 50.589 1.00 27.11 C ANISOU 4550 CB PHE B 273 3602 3226 3472 -53 831 -13 C ATOM 4551 CG PHE B 273 -14.808 18.656 50.753 1.00 21.96 C ANISOU 4551 CG PHE B 273 2960 2550 2834 -52 887 15 C ATOM 4552 CD1 PHE B 273 -16.025 18.001 50.645 1.00 21.11 C ANISOU 4552 CD1 PHE B 273 2841 2418 2763 -73 926 16 C ATOM 4553 CD2 PHE B 273 -13.673 17.911 51.032 1.00 35.01 C ANISOU 4553 CD2 PHE B 273 4633 4202 4467 -28 902 40 C ATOM 4554 CE1 PHE B 273 -16.105 16.632 50.803 1.00 32.31 C ANISOU 4554 CE1 PHE B 273 4269 3808 4201 -73 983 40 C ATOM 4555 CE2 PHE B 273 -13.747 16.543 51.194 1.00 35.30 C ANISOU 4555 CE2 PHE B 273 4682 4212 4520 -25 959 69 C ATOM 4556 CZ PHE B 273 -14.964 15.902 51.078 1.00 25.42 C ANISOU 4556 CZ PHE B 273 3419 2930 3308 -48 1001 68 C ATOM 4557 N TYR B 274 -13.010 21.284 53.134 1.00 20.65 N ANISOU 4557 N TYR B 274 2807 2485 2555 41 802 -2 N ATOM 4558 CA TYR B 274 -12.128 21.038 54.269 1.00 25.36 C ANISOU 4558 CA TYR B 274 3416 3114 3105 88 809 15 C ATOM 4559 C TYR B 274 -12.848 21.296 55.584 1.00 20.35 C ANISOU 4559 C TYR B 274 2783 2506 2443 124 828 20 C ATOM 4560 O TYR B 274 -12.686 20.542 56.551 1.00 23.82 O ANISOU 4560 O TYR B 274 3236 2963 2852 164 864 51 O ATOM 4561 CB TYR B 274 -10.874 21.908 54.174 1.00 34.26 C ANISOU 4561 CB TYR B 274 4540 4267 4211 93 757 -8 C ATOM 4562 CG TYR B 274 -10.046 21.885 55.441 1.00 25.95 C ANISOU 4562 CG TYR B 274 3495 3261 3106 144 755 -1 C ATOM 4563 CD1 TYR B 274 -9.100 20.891 55.656 1.00 33.24 C ANISOU 4563 CD1 TYR B 274 4428 4195 4006 170 774 31 C ATOM 4564 CD2 TYR B 274 -10.220 22.850 56.429 1.00 33.73 C ANISOU 4564 CD2 TYR B 274 4474 4282 4060 169 735 -26 C ATOM 4565 CE1 TYR B 274 -8.350 20.860 56.815 1.00 36.36 C ANISOU 4565 CE1 TYR B 274 4827 4642 4348 221 770 38 C ATOM 4566 CE2 TYR B 274 -9.477 22.825 57.589 1.00 21.86 C ANISOU 4566 CE2 TYR B 274 2974 2828 2503 218 730 -24 C ATOM 4567 CZ TYR B 274 -8.543 21.832 57.775 1.00 30.63 C ANISOU 4567 CZ TYR B 274 4094 3955 3590 245 747 10 C ATOM 4568 OH TYR B 274 -7.799 21.814 58.930 1.00 54.39 O ANISOU 4568 OH TYR B 274 7104 7022 6540 298 740 12 O ATOM 4569 N ILE B 275 -13.632 22.374 55.643 1.00 19.93 N ANISOU 4569 N ILE B 275 2718 2457 2398 113 806 -10 N ATOM 4570 CA ILE B 275 -14.372 22.705 56.856 1.00 18.64 C ANISOU 4570 CA ILE B 275 2556 2318 2209 147 824 -9 C ATOM 4571 C ILE B 275 -15.428 21.646 57.144 1.00 21.30 C ANISOU 4571 C ILE B 275 2896 2635 2564 151 885 26 C ATOM 4572 O ILE B 275 -15.618 21.235 58.296 1.00 22.91 O ANISOU 4572 O ILE B 275 3110 2861 2736 194 921 51 O ATOM 4573 CB ILE B 275 -14.986 24.109 56.727 1.00 18.28 C ANISOU 4573 CB ILE B 275 2496 2275 2175 132 789 -49 C ATOM 4574 CG1 ILE B 275 -13.882 25.164 56.638 1.00 20.57 C ANISOU 4574 CG1 ILE B 275 2783 2584 2448 133 735 -84 C ATOM 4575 CG2 ILE B 275 -15.906 24.402 57.898 1.00 25.71 C ANISOU 4575 CG2 ILE B 275 3438 3238 3094 165 812 -48 C ATOM 4576 CD1 ILE B 275 -14.377 26.530 56.216 1.00 28.16 C ANISOU 4576 CD1 ILE B 275 3732 3535 3433 111 703 -122 C ATOM 4577 N PHE B 276 -16.128 21.188 56.104 1.00 19.94 N ANISOU 4577 N PHE B 276 2712 2421 2441 107 900 28 N ATOM 4578 CA PHE B 276 -17.144 20.153 56.273 1.00 23.67 C ANISOU 4578 CA PHE B 276 3184 2869 2942 103 960 56 C ATOM 4579 C PHE B 276 -16.555 18.899 56.908 1.00 29.33 C ANISOU 4579 C PHE B 276 3919 3583 3640 136 1009 100 C ATOM 4580 O PHE B 276 -17.210 18.238 57.723 1.00 25.81 O ANISOU 4580 O PHE B 276 3479 3135 3194 160 1064 132 O ATOM 4581 CB PHE B 276 -17.774 19.836 54.916 1.00 27.68 C ANISOU 4581 CB PHE B 276 3674 3337 3507 47 961 42 C ATOM 4582 CG PHE B 276 -18.814 18.753 54.957 1.00 24.47 C ANISOU 4582 CG PHE B 276 3260 2899 3139 33 1022 63 C ATOM 4583 CD1 PHE B 276 -19.963 18.901 55.715 1.00 23.90 C ANISOU 4583 CD1 PHE B 276 3177 2832 3072 45 1052 70 C ATOM 4584 CD2 PHE B 276 -18.653 17.595 54.216 1.00 31.22 C ANISOU 4584 CD2 PHE B 276 4116 3717 4028 6 1051 74 C ATOM 4585 CE1 PHE B 276 -20.925 17.908 55.741 1.00 21.07 C ANISOU 4585 CE1 PHE B 276 2808 2442 2757 29 1112 88 C ATOM 4586 CE2 PHE B 276 -19.611 16.601 54.240 1.00 26.14 C ANISOU 4586 CE2 PHE B 276 3463 3040 3428 -12 1110 89 C ATOM 4587 CZ PHE B 276 -20.747 16.757 55.005 1.00 19.45 C ANISOU 4587 CZ PHE B 276 2602 2197 2589 -1 1141 97 C ATOM 4588 N THR B 277 -15.312 18.568 56.561 1.00 24.97 N ANISOU 4588 N THR B 277 3380 3035 3074 140 992 106 N ATOM 4589 CA THR B 277 -14.635 17.391 57.083 1.00 24.53 C ANISOU 4589 CA THR B 277 3343 2978 3000 175 1037 151 C ATOM 4590 C THR B 277 -13.816 17.673 58.338 1.00 31.17 C ANISOU 4590 C THR B 277 4196 3874 3772 238 1028 165 C ATOM 4591 O THR B 277 -13.306 16.728 58.949 1.00 26.01 O ANISOU 4591 O THR B 277 3558 3228 3095 278 1068 208 O ATOM 4592 CB THR B 277 -13.725 16.798 56.002 1.00 31.01 C ANISOU 4592 CB THR B 277 4169 3773 3841 148 1026 152 C ATOM 4593 OG1 THR B 277 -12.778 17.787 55.579 1.00 21.78 O ANISOU 4593 OG1 THR B 277 2995 2629 2651 141 960 120 O ATOM 4594 CG2 THR B 277 -14.546 16.349 54.799 1.00 33.57 C ANISOU 4594 CG2 THR B 277 4481 4046 4229 90 1041 137 C ATOM 4595 N HIS B 278 -13.679 18.935 58.738 1.00 26.52 N ANISOU 4595 N HIS B 278 3599 3324 3152 248 977 129 N ATOM 4596 CA HIS B 278 -12.916 19.334 59.919 1.00 27.98 C ANISOU 4596 CA HIS B 278 3792 3570 3270 306 960 130 C ATOM 4597 C HIS B 278 -13.702 20.352 60.738 1.00 25.97 C ANISOU 4597 C HIS B 278 3530 3344 2993 323 947 105 C ATOM 4598 O HIS B 278 -13.200 21.412 61.112 1.00 28.54 O ANISOU 4598 O HIS B 278 3850 3709 3286 336 898 66 O ATOM 4599 CB HIS B 278 -11.547 19.892 59.529 1.00 30.31 C ANISOU 4599 CB HIS B 278 4083 3889 3546 302 901 103 C ATOM 4600 CG HIS B 278 -10.677 18.915 58.798 1.00 34.53 C ANISOU 4600 CG HIS B 278 4624 4401 4096 292 913 129 C ATOM 4601 ND1 HIS B 278 -10.857 18.608 57.466 1.00 28.06 N ANISOU 4601 ND1 HIS B 278 3802 3529 3332 237 914 124 N ATOM 4602 CD2 HIS B 278 -9.619 18.179 59.214 1.00 28.77 C ANISOU 4602 CD2 HIS B 278 3905 3696 3331 333 926 160 C ATOM 4603 CE1 HIS B 278 -9.948 17.724 57.094 1.00 32.87 C ANISOU 4603 CE1 HIS B 278 4420 4128 3942 243 927 149 C ATOM 4604 NE2 HIS B 278 -9.187 17.444 58.136 1.00 29.22 N ANISOU 4604 NE2 HIS B 278 3965 3711 3425 301 936 174 N ATOM 4605 N GLN B 279 -14.969 20.042 61.011 1.00 22.00 N ANISOU 4605 N GLN B 279 3027 2820 2513 322 993 123 N ATOM 4606 CA GLN B 279 -15.823 20.969 61.742 1.00 28.32 C ANISOU 4606 CA GLN B 279 3821 3644 3296 338 987 101 C ATOM 4607 C GLN B 279 -15.299 21.193 63.155 1.00 25.62 C ANISOU 4607 C GLN B 279 3490 3366 2880 406 985 106 C ATOM 4608 O GLN B 279 -14.905 20.253 63.850 1.00 20.85 O ANISOU 4608 O GLN B 279 2900 2782 2241 453 1025 151 O ATOM 4609 CB GLN B 279 -17.256 20.444 61.801 1.00 28.00 C ANISOU 4609 CB GLN B 279 3775 3570 3294 326 1044 126 C ATOM 4610 CG GLN B 279 -17.920 20.283 60.451 1.00 19.88 C ANISOU 4610 CG GLN B 279 2730 2486 2338 259 1044 114 C ATOM 4611 CD GLN B 279 -19.379 19.900 60.575 1.00 34.53 C ANISOU 4611 CD GLN B 279 4575 4315 4232 248 1096 131 C ATOM 4612 OE1 GLN B 279 -19.824 19.444 61.628 1.00 33.99 O ANISOU 4612 OE1 GLN B 279 4514 4260 4143 289 1147 165 O ATOM 4613 NE2 GLN B 279 -20.134 20.087 59.501 1.00 26.98 N ANISOU 4613 NE2 GLN B 279 3597 3323 3332 192 1084 107 N ATOM 4614 N GLY B 280 -15.312 22.454 63.580 1.00 25.66 N ANISOU 4614 N GLY B 280 3487 3404 2858 415 940 58 N ATOM 4615 CA GLY B 280 -14.805 22.830 64.880 1.00 29.72 C ANISOU 4615 CA GLY B 280 4008 3985 3298 478 929 49 C ATOM 4616 C GLY B 280 -13.303 22.981 64.963 1.00 28.71 C ANISOU 4616 C GLY B 280 3880 3898 3131 495 883 30 C ATOM 4617 O GLY B 280 -12.786 23.254 66.055 1.00 36.74 O ANISOU 4617 O GLY B 280 4899 4979 4082 550 870 18 O ATOM 4618 N SER B 281 -12.588 22.823 63.853 1.00 20.56 N ANISOU 4618 N SER B 281 2842 2834 2136 451 858 24 N ATOM 4619 CA SER B 281 -11.136 22.877 63.857 1.00 32.00 C ANISOU 4619 CA SER B 281 4287 4319 3554 465 818 10 C ATOM 4620 C SER B 281 -10.650 24.324 63.924 1.00 36.58 C ANISOU 4620 C SER B 281 4851 4925 4123 452 752 -61 C ATOM 4621 O SER B 281 -11.426 25.282 63.876 1.00 34.17 O ANISOU 4621 O SER B 281 4540 4605 3839 430 739 -97 O ATOM 4622 CB SER B 281 -10.574 22.164 62.630 1.00 22.65 C ANISOU 4622 CB SER B 281 3103 3088 2414 424 820 31 C ATOM 4623 OG SER B 281 -11.031 22.772 61.436 1.00 29.00 O ANISOU 4623 OG SER B 281 3897 3840 3281 358 798 2 O ATOM 4624 N ASP B 282 -9.330 24.473 64.005 1.00 33.70 N ANISOU 4624 N ASP B 282 4477 4597 3729 464 713 -81 N ATOM 4625 CA ASP B 282 -8.693 25.727 64.406 1.00 40.28 C ANISOU 4625 CA ASP B 282 5293 5471 4539 466 656 -149 C ATOM 4626 C ASP B 282 -8.456 26.604 63.177 1.00 32.15 C ANISOU 4626 C ASP B 282 4250 4392 3574 398 616 -190 C ATOM 4627 O ASP B 282 -7.374 26.628 62.589 1.00 38.24 O ANISOU 4627 O ASP B 282 5009 5162 4357 379 587 -201 O ATOM 4628 CB ASP B 282 -7.396 25.418 65.146 1.00 37.40 C ANISOU 4628 CB ASP B 282 4921 5177 4112 514 634 -152 C ATOM 4629 CG ASP B 282 -6.825 26.618 65.872 1.00 48.23 C ANISOU 4629 CG ASP B 282 6273 6604 5447 528 580 -226 C ATOM 4630 OD1 ASP B 282 -7.491 27.677 65.906 1.00 48.07 O ANISOU 4630 OD1 ASP B 282 6250 6567 5450 505 565 -272 O ATOM 4631 OD2 ASP B 282 -5.702 26.492 66.409 1.00 50.91 O ANISOU 4631 OD2 ASP B 282 6600 7006 5738 563 554 -239 O ATOM 4632 N PHE B 283 -9.493 27.352 62.792 1.00 32.26 N ANISOU 4632 N PHE B 283 4263 4364 3629 365 618 -210 N ATOM 4633 CA PHE B 283 -9.375 28.315 61.704 1.00 27.14 C ANISOU 4633 CA PHE B 283 3601 3670 3039 308 584 -247 C ATOM 4634 C PHE B 283 -10.036 29.629 62.100 1.00 28.22 C ANISOU 4634 C PHE B 283 3733 3806 3184 303 567 -299 C ATOM 4635 O PHE B 283 -10.977 29.656 62.898 1.00 30.72 O ANISOU 4635 O PHE B 283 4057 4137 3477 332 592 -294 O ATOM 4636 CB PHE B 283 -9.980 27.786 60.391 1.00 30.59 C ANISOU 4636 CB PHE B 283 4044 4044 3535 263 608 -210 C ATOM 4637 CG PHE B 283 -11.433 27.413 60.485 1.00 24.45 C ANISOU 4637 CG PHE B 283 3277 3243 2771 265 651 -181 C ATOM 4638 CD1 PHE B 283 -12.422 28.373 60.334 1.00 27.10 C ANISOU 4638 CD1 PHE B 283 3606 3555 3134 246 646 -207 C ATOM 4639 CD2 PHE B 283 -11.810 26.098 60.694 1.00 24.59 C ANISOU 4639 CD2 PHE B 283 3307 3259 2777 284 699 -127 C ATOM 4640 CE1 PHE B 283 -13.758 28.030 60.411 1.00 28.97 C ANISOU 4640 CE1 PHE B 283 3848 3774 3386 247 686 -182 C ATOM 4641 CE2 PHE B 283 -13.144 25.749 60.771 1.00 19.31 C ANISOU 4641 CE2 PHE B 283 2643 2568 2127 283 740 -102 C ATOM 4642 CZ PHE B 283 -14.120 26.717 60.629 1.00 21.73 C ANISOU 4642 CZ PHE B 283 2942 2856 2459 264 732 -130 C ATOM 4643 N GLY B 284 -9.531 30.721 61.526 1.00 26.02 N ANISOU 4643 N GLY B 284 3439 3507 2941 267 528 -347 N ATOM 4644 CA GLY B 284 -9.991 32.050 61.855 1.00 19.91 C ANISOU 4644 CA GLY B 284 2658 2727 2179 261 511 -401 C ATOM 4645 C GLY B 284 -10.897 32.659 60.803 1.00 28.03 C ANISOU 4645 C GLY B 284 3687 3692 3273 218 519 -398 C ATOM 4646 O GLY B 284 -11.227 32.032 59.791 1.00 25.92 O ANISOU 4646 O GLY B 284 3423 3387 3039 192 536 -355 O ATOM 4647 N PRO B 285 -11.324 33.906 61.033 1.00 25.65 N ANISOU 4647 N PRO B 285 3379 3377 2988 212 507 -445 N ATOM 4648 CA PRO B 285 -12.240 34.561 60.080 1.00 33.29 C ANISOU 4648 CA PRO B 285 4346 4288 4015 179 516 -440 C ATOM 4649 C PRO B 285 -11.655 34.754 58.688 1.00 26.03 C ANISOU 4649 C PRO B 285 3418 3325 3149 134 500 -432 C ATOM 4650 O PRO B 285 -12.396 34.701 57.698 1.00 29.36 O ANISOU 4650 O PRO B 285 3840 3707 3609 110 515 -403 O ATOM 4651 CB PRO B 285 -12.537 35.911 60.753 1.00 24.93 C ANISOU 4651 CB PRO B 285 3283 3230 2960 187 504 -499 C ATOM 4652 CG PRO B 285 -12.104 35.759 62.180 1.00 33.85 C ANISOU 4652 CG PRO B 285 4415 4423 4024 232 496 -528 C ATOM 4653 CD PRO B 285 -10.970 34.786 62.157 1.00 33.20 C ANISOU 4653 CD PRO B 285 4330 4372 3912 238 484 -507 C ATOM 4654 N ILE B 286 -10.346 34.989 58.580 1.00 32.69 N ANISOU 4654 N ILE B 286 4250 4176 3993 123 471 -459 N ATOM 4655 CA ILE B 286 -9.736 35.241 57.279 1.00 20.86 C ANISOU 4655 CA ILE B 286 2743 2637 2545 83 459 -451 C ATOM 4656 C ILE B 286 -9.759 33.995 56.400 1.00 30.74 C ANISOU 4656 C ILE B 286 4002 3878 3799 72 475 -393 C ATOM 4657 O ILE B 286 -9.709 34.104 55.167 1.00 25.86 O ANISOU 4657 O ILE B 286 3380 3221 3223 41 474 -375 O ATOM 4658 CB ILE B 286 -8.301 35.772 57.481 1.00 26.71 C ANISOU 4658 CB ILE B 286 3468 3394 3288 76 426 -496 C ATOM 4659 CG1 ILE B 286 -8.313 37.002 58.394 1.00 39.39 C ANISOU 4659 CG1 ILE B 286 5064 5008 4893 84 411 -562 C ATOM 4660 CG2 ILE B 286 -7.648 36.126 56.156 1.00 28.71 C ANISOU 4660 CG2 ILE B 286 3711 3602 3596 35 417 -488 C ATOM 4661 CD1 ILE B 286 -9.266 38.090 57.942 1.00 35.49 C ANISOU 4661 CD1 ILE B 286 4574 4464 4449 67 423 -574 C ATOM 4662 N PHE B 287 -9.877 32.812 57.007 1.00 31.53 N ANISOU 4662 N PHE B 287 4113 4012 3856 100 494 -362 N ATOM 4663 CA PHE B 287 -9.721 31.559 56.275 1.00 29.52 C ANISOU 4663 CA PHE B 287 3865 3748 3602 91 510 -312 C ATOM 4664 C PHE B 287 -10.760 31.412 55.168 1.00 24.69 C ANISOU 4664 C PHE B 287 3256 3094 3032 63 529 -283 C ATOM 4665 O PHE B 287 -10.435 30.975 54.058 1.00 23.96 O ANISOU 4665 O PHE B 287 3162 2977 2963 38 529 -260 O ATOM 4666 CB PHE B 287 -9.793 30.388 57.256 1.00 21.64 C ANISOU 4666 CB PHE B 287 2879 2791 2553 130 534 -283 C ATOM 4667 CG PHE B 287 -9.554 29.045 56.630 1.00 29.59 C ANISOU 4667 CG PHE B 287 3894 3788 3561 124 556 -234 C ATOM 4668 CD1 PHE B 287 -8.451 28.822 55.821 1.00 17.96 C ANISOU 4668 CD1 PHE B 287 2416 2306 2103 105 539 -229 C ATOM 4669 CD2 PHE B 287 -10.424 27.995 56.876 1.00 31.69 C ANISOU 4669 CD2 PHE B 287 4172 4052 3816 139 597 -194 C ATOM 4670 CE1 PHE B 287 -8.233 27.580 55.253 1.00 26.02 C ANISOU 4670 CE1 PHE B 287 3445 3315 3125 101 561 -186 C ATOM 4671 CE2 PHE B 287 -10.213 26.752 56.314 1.00 33.11 C ANISOU 4671 CE2 PHE B 287 4360 4218 4002 132 621 -152 C ATOM 4672 CZ PHE B 287 -9.115 26.543 55.502 1.00 33.44 C ANISOU 4672 CZ PHE B 287 4399 4251 4056 114 603 -149 C ATOM 4673 N MET B 288 -12.016 31.765 55.443 1.00 25.82 N ANISOU 4673 N MET B 288 3401 3229 3180 69 546 -285 N ATOM 4674 CA MET B 288 -13.056 31.682 54.425 1.00 22.14 C ANISOU 4674 CA MET B 288 2933 2730 2752 46 561 -262 C ATOM 4675 C MET B 288 -13.375 33.025 53.780 1.00 27.20 C ANISOU 4675 C MET B 288 3563 3340 3431 28 545 -285 C ATOM 4676 O MET B 288 -13.929 33.045 52.677 1.00 23.56 O ANISOU 4676 O MET B 288 3097 2854 3002 6 549 -267 O ATOM 4677 CB MET B 288 -14.338 31.076 55.019 1.00 22.72 C ANISOU 4677 CB MET B 288 3010 2811 2811 63 595 -241 C ATOM 4678 CG MET B 288 -15.455 30.794 54.010 1.00 27.48 C ANISOU 4678 CG MET B 288 3606 3387 3450 39 611 -218 C ATOM 4679 SD MET B 288 -14.932 29.810 52.587 1.00 18.31 S ANISOU 4679 SD MET B 288 2443 2205 2310 6 610 -190 S ATOM 4680 CE MET B 288 -15.761 28.258 52.916 1.00 17.33 C ANISOU 4680 CE MET B 288 2323 2084 2177 12 655 -156 C ATOM 4681 N THR B 289 -13.016 34.140 54.422 1.00 23.30 N ANISOU 4681 N THR B 289 3066 2851 2936 37 527 -326 N ATOM 4682 CA THR B 289 -13.364 35.451 53.880 1.00 18.93 C ANISOU 4682 CA THR B 289 2504 2264 2423 23 519 -347 C ATOM 4683 C THR B 289 -12.791 35.647 52.482 1.00 24.63 C ANISOU 4683 C THR B 289 3220 2954 3183 -6 508 -333 C ATOM 4684 O THR B 289 -13.509 36.039 51.554 1.00 19.99 O ANISOU 4684 O THR B 289 2628 2341 2627 -18 515 -317 O ATOM 4685 CB THR B 289 -12.861 36.554 54.812 1.00 22.51 C ANISOU 4685 CB THR B 289 2955 2725 2873 35 503 -399 C ATOM 4686 OG1 THR B 289 -13.594 36.523 56.042 1.00 18.51 O ANISOU 4686 OG1 THR B 289 2455 2246 2332 66 516 -412 O ATOM 4687 CG2 THR B 289 -13.020 37.923 54.161 1.00 18.30 C ANISOU 4687 CG2 THR B 289 2414 2149 2391 19 498 -419 C ATOM 4688 N AILE B 290 -11.490 35.386 52.322 0.12 22.85 N ANISOU 4688 N AILE B 290 2993 2735 2954 -16 492 -337 N ATOM 4689 N BILE B 290 -11.505 35.368 52.307 0.88 22.51 N ANISOU 4689 N BILE B 290 2951 2692 2912 -16 492 -336 N ATOM 4690 CA AILE B 290 -10.837 35.620 51.033 0.12 22.86 C ANISOU 4690 CA AILE B 290 2989 2707 2991 -41 483 -324 C ATOM 4691 CA BILE B 290 -10.834 35.621 51.033 0.88 22.86 C ANISOU 4691 CA BILE B 290 2988 2706 2990 -41 483 -324 C ATOM 4692 C AILE B 290 -11.415 34.743 49.927 0.12 25.76 C ANISOU 4692 C AILE B 290 3358 3066 3363 -53 496 -280 C ATOM 4693 C BILE B 290 -11.394 34.741 49.914 0.88 25.87 C ANISOU 4693 C BILE B 290 3372 3080 3377 -53 496 -280 C ATOM 4694 O AILE B 290 -11.766 35.282 48.864 0.12 21.36 O ANISOU 4694 O AILE B 290 2796 2482 2837 -65 497 -268 O ATOM 4695 O BILE B 290 -11.705 35.271 48.837 0.88 21.12 O ANISOU 4695 O BILE B 290 2765 2451 2807 -66 496 -268 O ATOM 4696 CB AILE B 290 -9.312 35.467 51.178 0.12 26.16 C ANISOU 4696 CB AILE B 290 3402 3137 3402 -47 465 -339 C ATOM 4697 CB BILE B 290 -9.312 35.472 51.183 0.88 26.19 C ANISOU 4697 CB BILE B 290 3405 3140 3406 -47 465 -339 C ATOM 4698 CG1AILE B 290 -8.800 36.295 52.359 0.12 19.34 C ANISOU 4698 CG1AILE B 290 2530 2288 2529 -36 450 -390 C ATOM 4699 CG1BILE B 290 -8.824 36.359 52.330 0.88 18.93 C ANISOU 4699 CG1BILE B 290 2479 2235 2480 -36 450 -391 C ATOM 4700 CG2AILE B 290 -8.610 35.882 49.895 0.12 27.21 C ANISOU 4700 CG2AILE B 290 3527 3237 3575 -72 458 -328 C ATOM 4701 CG2BILE B 290 -8.611 35.858 49.891 0.88 27.21 C ANISOU 4701 CG2BILE B 290 3527 3237 3575 -72 458 -327 C ATOM 4702 CD1AILE B 290 -9.010 37.783 52.194 0.12 24.72 C ANISOU 4702 CD1AILE B 290 3204 2934 3255 -46 448 -422 C ATOM 4703 CD1BILE B 290 -7.341 36.340 52.534 0.88 26.50 C ANISOU 4703 CD1BILE B 290 3426 3209 3434 -42 429 -414 C ATOM 4704 N PRO B 291 -11.537 33.416 50.087 1.00 17.46 N ANISOU 4704 N PRO B 291 2315 2035 2284 -48 508 -257 N ATOM 4705 CA PRO B 291 -12.197 32.633 49.024 1.00 27.02 C ANISOU 4705 CA PRO B 291 3525 3237 3504 -62 520 -224 C ATOM 4706 C PRO B 291 -13.640 33.041 48.786 1.00 18.32 C ANISOU 4706 C PRO B 291 2418 2128 2417 -60 532 -220 C ATOM 4707 O PRO B 291 -14.097 33.040 47.636 1.00 29.58 O ANISOU 4707 O PRO B 291 3837 3541 3863 -73 532 -203 O ATOM 4708 CB PRO B 291 -12.095 31.187 49.533 1.00 20.37 C ANISOU 4708 CB PRO B 291 2694 2416 2631 -54 537 -206 C ATOM 4709 CG PRO B 291 -10.964 31.198 50.479 1.00 37.81 C ANISOU 4709 CG PRO B 291 4906 4645 4815 -38 526 -222 C ATOM 4710 CD PRO B 291 -11.056 32.525 51.161 1.00 17.07 C ANISOU 4710 CD PRO B 291 2274 2019 2194 -29 512 -258 C ATOM 4711 N ALA B 292 -14.366 33.403 49.846 1.00 19.40 N ANISOU 4711 N ALA B 292 2554 2274 2542 -42 540 -235 N ATOM 4712 CA ALA B 292 -15.780 33.738 49.699 1.00 22.62 C ANISOU 4712 CA ALA B 292 2953 2678 2963 -38 553 -230 C ATOM 4713 C ALA B 292 -15.970 35.002 48.874 1.00 20.35 C ANISOU 4713 C ALA B 292 2657 2367 2709 -42 542 -235 C ATOM 4714 O ALA B 292 -16.849 35.057 48.008 1.00 20.10 O ANISOU 4714 O ALA B 292 2615 2331 2693 -47 547 -218 O ATOM 4715 CB ALA B 292 -16.434 33.893 51.071 1.00 17.28 C ANISOU 4715 CB ALA B 292 2280 2018 2266 -13 566 -245 C ATOM 4716 N PHE B 293 -15.162 36.032 49.131 1.00 19.72 N ANISOU 4716 N PHE B 293 2580 2272 2641 -40 530 -259 N ATOM 4717 CA PHE B 293 -15.324 37.284 48.402 1.00 21.64 C ANISOU 4717 CA PHE B 293 2816 2486 2920 -41 527 -261 C ATOM 4718 C PHE B 293 -14.653 37.248 47.037 1.00 20.28 C ANISOU 4718 C PHE B 293 2640 2298 2766 -58 519 -239 C ATOM 4719 O PHE B 293 -15.109 37.930 46.112 1.00 23.63 O ANISOU 4719 O PHE B 293 3057 2705 3215 -56 522 -223 O ATOM 4720 CB PHE B 293 -14.797 38.450 49.240 1.00 17.53 C ANISOU 4720 CB PHE B 293 2298 1950 2413 -33 522 -299 C ATOM 4721 CG PHE B 293 -15.812 38.992 50.204 1.00 19.95 C ANISOU 4721 CG PHE B 293 2605 2262 2714 -12 534 -318 C ATOM 4722 CD1 PHE B 293 -16.088 38.324 51.388 1.00 17.85 C ANISOU 4722 CD1 PHE B 293 2345 2027 2410 2 539 -329 C ATOM 4723 CD2 PHE B 293 -16.511 40.152 49.913 1.00 17.95 C ANISOU 4723 CD2 PHE B 293 2347 1983 2493 -4 543 -321 C ATOM 4724 CE1 PHE B 293 -17.029 38.812 52.273 1.00 19.77 C ANISOU 4724 CE1 PHE B 293 2589 2276 2646 24 552 -346 C ATOM 4725 CE2 PHE B 293 -17.455 40.646 50.791 1.00 28.95 C ANISOU 4725 CE2 PHE B 293 3740 3380 3880 18 556 -338 C ATOM 4726 CZ PHE B 293 -17.714 39.976 51.975 1.00 20.07 C ANISOU 4726 CZ PHE B 293 2621 2287 2716 31 560 -351 C ATOM 4727 N PHE B 294 -13.585 36.463 46.883 1.00 24.01 N ANISOU 4727 N PHE B 294 3118 2778 3226 -71 510 -234 N ATOM 4728 CA PHE B 294 -13.004 36.273 45.559 1.00 21.26 C ANISOU 4728 CA PHE B 294 2767 2419 2892 -85 505 -210 C ATOM 4729 C PHE B 294 -14.000 35.603 44.621 1.00 23.65 C ANISOU 4729 C PHE B 294 3065 2734 3188 -86 512 -183 C ATOM 4730 O PHE B 294 -14.072 35.942 43.433 1.00 23.36 O ANISOU 4730 O PHE B 294 3022 2688 3167 -88 510 -164 O ATOM 4731 CB PHE B 294 -11.718 35.453 45.663 1.00 19.59 C ANISOU 4731 CB PHE B 294 2562 2215 2664 -96 497 -211 C ATOM 4732 CG PHE B 294 -11.038 35.220 44.346 1.00 16.48 C ANISOU 4732 CG PHE B 294 2167 1812 2282 -109 493 -187 C ATOM 4733 CD1 PHE B 294 -10.512 36.281 43.625 1.00 21.98 C ANISOU 4733 CD1 PHE B 294 2858 2481 3011 -112 492 -184 C ATOM 4734 CD2 PHE B 294 -10.910 33.939 43.836 1.00 17.68 C ANISOU 4734 CD2 PHE B 294 2324 1980 2414 -116 495 -168 C ATOM 4735 CE1 PHE B 294 -9.883 36.068 42.413 1.00 31.11 C ANISOU 4735 CE1 PHE B 294 4014 3630 4175 -120 491 -159 C ATOM 4736 CE2 PHE B 294 -10.280 33.719 42.623 1.00 24.43 C ANISOU 4736 CE2 PHE B 294 3178 2827 3276 -126 493 -148 C ATOM 4737 CZ PHE B 294 -9.765 34.786 41.912 1.00 28.30 C ANISOU 4737 CZ PHE B 294 3664 3295 3795 -126 490 -142 C ATOM 4738 N ALA B 295 -14.783 34.653 45.139 1.00 16.59 N ANISOU 4738 N ALA B 295 2171 1862 2272 -85 520 -182 N ATOM 4739 CA ALA B 295 -15.794 33.983 44.331 1.00 16.54 C ANISOU 4739 CA ALA B 295 2154 1868 2262 -90 526 -165 C ATOM 4740 C ALA B 295 -16.886 34.934 43.856 1.00 16.69 C ANISOU 4740 C ALA B 295 2158 1885 2298 -77 527 -159 C ATOM 4741 O ALA B 295 -17.588 34.620 42.889 1.00 18.13 O ANISOU 4741 O ALA B 295 2327 2080 2480 -80 526 -145 O ATOM 4742 CB ALA B 295 -16.414 32.827 45.117 1.00 16.54 C ANISOU 4742 CB ALA B 295 2155 1887 2243 -92 540 -167 C ATOM 4743 N LYS B 296 -17.045 36.088 44.509 1.00 20.94 N ANISOU 4743 N LYS B 296 2698 2409 2850 -62 530 -172 N ATOM 4744 CA LYS B 296 -18.054 37.050 44.086 1.00 24.75 C ANISOU 4744 CA LYS B 296 3167 2888 3350 -46 534 -164 C ATOM 4745 C LYS B 296 -17.674 37.774 42.800 1.00 22.44 C ANISOU 4745 C LYS B 296 2870 2580 3076 -42 529 -144 C ATOM 4746 O LYS B 296 -18.505 38.509 42.257 1.00 17.41 O ANISOU 4746 O LYS B 296 2222 1943 2451 -24 534 -130 O ATOM 4747 CB LYS B 296 -18.321 38.058 45.205 1.00 17.26 C ANISOU 4747 CB LYS B 296 2222 1924 2412 -29 543 -186 C ATOM 4748 CG LYS B 296 -18.943 37.434 46.442 1.00 24.15 C ANISOU 4748 CG LYS B 296 3097 2817 3263 -25 552 -201 C ATOM 4749 CD LYS B 296 -19.297 38.486 47.477 1.00 22.93 C ANISOU 4749 CD LYS B 296 2946 2649 3116 -5 561 -224 C ATOM 4750 CE LYS B 296 -19.532 37.862 48.847 1.00 21.85 C ANISOU 4750 CE LYS B 296 2816 2533 2953 2 570 -241 C ATOM 4751 NZ LYS B 296 -20.535 36.811 48.804 1.00 28.07 N ANISOU 4751 NZ LYS B 296 3592 3345 3726 0 581 -223 N ATOM 4752 N THR B 297 -16.453 37.579 42.294 1.00 23.40 N ANISOU 4752 N THR B 297 3002 2691 3200 -55 522 -138 N ATOM 4753 CA THR B 297 -16.118 38.047 40.953 1.00 16.97 C ANISOU 4753 CA THR B 297 2183 1867 2399 -50 521 -112 C ATOM 4754 C THR B 297 -16.860 37.276 39.871 1.00 22.56 C ANISOU 4754 C THR B 297 2879 2608 3087 -49 515 -93 C ATOM 4755 O THR B 297 -16.794 37.665 38.699 1.00 19.03 O ANISOU 4755 O THR B 297 2426 2163 2643 -37 514 -69 O ATOM 4756 CB THR B 297 -14.613 37.937 40.695 1.00 16.86 C ANISOU 4756 CB THR B 297 2180 1834 2390 -65 516 -112 C ATOM 4757 OG1 THR B 297 -14.206 36.567 40.797 1.00 16.63 O ANISOU 4757 OG1 THR B 297 2156 1826 2335 -83 508 -116 O ATOM 4758 CG2 THR B 297 -13.835 38.770 41.688 1.00 23.61 C ANISOU 4758 CG2 THR B 297 3043 2660 3269 -68 519 -136 C ATOM 4759 N SER B 298 -17.552 36.194 40.238 1.00 16.84 N ANISOU 4759 N SER B 298 2148 1910 2341 -59 513 -104 N ATOM 4760 CA SER B 298 -18.305 35.407 39.268 1.00 23.86 C ANISOU 4760 CA SER B 298 3021 2832 3214 -62 507 -95 C ATOM 4761 C SER B 298 -19.350 36.246 38.546 1.00 17.41 C ANISOU 4761 C SER B 298 2183 2030 2401 -37 506 -79 C ATOM 4762 O SER B 298 -19.753 35.909 37.429 1.00 26.67 O ANISOU 4762 O SER B 298 3340 3232 3560 -33 497 -68 O ATOM 4763 CB SER B 298 -18.970 34.223 39.967 1.00 16.80 C ANISOU 4763 CB SER B 298 2120 1956 2307 -79 511 -113 C ATOM 4764 OG SER B 298 -19.744 34.661 41.071 1.00 27.08 O ANISOU 4764 OG SER B 298 3418 3254 3616 -69 522 -124 O ATOM 4765 N ALA B 299 -19.795 37.340 39.159 1.00 19.81 N ANISOU 4765 N ALA B 299 2486 2318 2724 -17 516 -79 N ATOM 4766 CA ALA B 299 -20.818 38.185 38.563 1.00 24.12 C ANISOU 4766 CA ALA B 299 3012 2878 3274 12 518 -61 C ATOM 4767 C ALA B 299 -20.295 39.088 37.449 1.00 22.71 C ANISOU 4767 C ALA B 299 2836 2687 3104 34 520 -30 C ATOM 4768 O ALA B 299 -21.104 39.751 36.791 1.00 25.11 O ANISOU 4768 O ALA B 299 3124 3009 3409 64 523 -8 O ATOM 4769 CB ALA B 299 -21.475 39.045 39.647 1.00 17.71 C ANISOU 4769 CB ALA B 299 2199 2049 2480 28 532 -70 C ATOM 4770 N VAL B 300 -18.980 39.143 37.220 1.00 24.05 N ANISOU 4770 N VAL B 300 3026 2831 3283 23 521 -25 N ATOM 4771 CA VAL B 300 -18.376 40.156 36.363 1.00 25.23 C ANISOU 4771 CA VAL B 300 3180 2957 3449 44 532 6 C ATOM 4772 C VAL B 300 -17.609 39.554 35.189 1.00 18.71 C ANISOU 4772 C VAL B 300 2358 2147 2606 39 523 24 C ATOM 4773 O VAL B 300 -17.682 40.074 34.070 1.00 24.48 O ANISOU 4773 O VAL B 300 3082 2888 3332 66 528 57 O ATOM 4774 CB VAL B 300 -17.465 41.098 37.183 1.00 22.79 C ANISOU 4774 CB VAL B 300 2888 2592 3178 39 548 -4 C ATOM 4775 CG1 VAL B 300 -16.662 42.020 36.269 1.00 38.35 C ANISOU 4775 CG1 VAL B 300 4866 4533 5174 55 563 28 C ATOM 4776 CG2 VAL B 300 -18.301 41.912 38.165 1.00 22.35 C ANISOU 4776 CG2 VAL B 300 2829 2521 3141 52 559 -18 C ATOM 4777 N TYR B 301 -16.862 38.468 35.412 1.00 18.60 N ANISOU 4777 N TYR B 301 2353 2135 2578 8 513 4 N ATOM 4778 CA TYR B 301 -15.787 38.122 34.482 1.00 21.34 C ANISOU 4778 CA TYR B 301 2709 2481 2917 2 511 21 C ATOM 4779 C TYR B 301 -16.290 37.569 33.148 1.00 23.12 C ANISOU 4779 C TYR B 301 2922 2754 3110 16 500 37 C ATOM 4780 O TYR B 301 -15.630 37.766 32.122 1.00 18.62 O ANISOU 4780 O TYR B 301 2356 2185 2534 30 504 63 O ATOM 4781 CB TYR B 301 -14.813 37.131 35.136 1.00 24.15 C ANISOU 4781 CB TYR B 301 3080 2826 3269 -32 505 -4 C ATOM 4782 CG TYR B 301 -15.323 35.714 35.301 1.00 26.41 C ANISOU 4782 CG TYR B 301 3362 3146 3528 -52 493 -25 C ATOM 4783 CD1 TYR B 301 -15.323 34.821 34.232 1.00 22.43 C ANISOU 4783 CD1 TYR B 301 2853 2672 2998 -56 484 -20 C ATOM 4784 CD2 TYR B 301 -15.766 35.255 36.535 1.00 23.96 C ANISOU 4784 CD2 TYR B 301 3052 2834 3218 -67 493 -52 C ATOM 4785 CE1 TYR B 301 -15.786 33.531 34.378 1.00 34.56 C ANISOU 4785 CE1 TYR B 301 4384 4232 4515 -76 477 -44 C ATOM 4786 CE2 TYR B 301 -16.222 33.960 36.694 1.00 34.12 C ANISOU 4786 CE2 TYR B 301 4335 4145 4486 -85 489 -69 C ATOM 4787 CZ TYR B 301 -16.229 33.103 35.611 1.00 20.48 C ANISOU 4787 CZ TYR B 301 2602 2442 2738 -92 482 -66 C ATOM 4788 OH TYR B 301 -16.684 31.814 35.760 1.00 21.32 O ANISOU 4788 OH TYR B 301 2702 2566 2832 -113 481 -86 O ATOM 4789 N ASN B 302 -17.419 36.856 33.132 1.00 24.43 N ANISOU 4789 N ASN B 302 3069 2960 3252 13 487 20 N ATOM 4790 CA ASN B 302 -17.846 36.201 31.895 1.00 22.23 C ANISOU 4790 CA ASN B 302 2776 2732 2940 22 472 25 C ATOM 4791 C ASN B 302 -18.059 37.180 30.745 1.00 26.16 C ANISOU 4791 C ASN B 302 3264 3248 3429 66 476 64 C ATOM 4792 O ASN B 302 -17.573 36.902 29.634 1.00 25.11 O ANISOU 4792 O ASN B 302 3133 3135 3272 77 472 79 O ATOM 4793 CB ASN B 302 -19.098 35.356 32.150 1.00 19.60 C ANISOU 4793 CB ASN B 302 2419 2437 2590 10 459 -5 C ATOM 4794 CG ASN B 302 -18.772 33.975 32.682 1.00 21.14 C ANISOU 4794 CG ASN B 302 2622 2628 2781 -31 456 -38 C ATOM 4795 OD1 ASN B 302 -17.938 33.262 32.127 1.00 33.25 O ANISOU 4795 OD1 ASN B 302 4169 4163 4304 -45 453 -40 O ATOM 4796 ND2 ASN B 302 -19.428 33.593 33.768 1.00 17.26 N ANISOU 4796 ND2 ASN B 302 2125 2131 2301 -49 460 -61 N ATOM 4797 N PRO B 303 -18.749 38.314 30.915 1.00 30.37 N ANISOU 4797 N PRO B 303 3788 3774 3978 97 487 83 N ATOM 4798 CA PRO B 303 -18.822 39.281 29.809 1.00 29.88 C ANISOU 4798 CA PRO B 303 3720 3724 3908 145 497 128 C ATOM 4799 C PRO B 303 -17.471 39.852 29.410 1.00 20.61 C ANISOU 4799 C PRO B 303 2569 2507 2753 150 518 159 C ATOM 4800 O PRO B 303 -17.330 40.325 28.277 1.00 23.17 O ANISOU 4800 O PRO B 303 2891 2848 3063 188 526 198 O ATOM 4801 CB PRO B 303 -19.753 40.373 30.355 1.00 27.95 C ANISOU 4801 CB PRO B 303 3465 3468 3686 172 511 140 C ATOM 4802 CG PRO B 303 -20.548 39.697 31.411 1.00 25.44 C ANISOU 4802 CG PRO B 303 3137 3161 3370 143 498 98 C ATOM 4803 CD PRO B 303 -19.607 38.725 32.041 1.00 21.30 C ANISOU 4803 CD PRO B 303 2632 2612 2850 95 492 67 C ATOM 4804 N VAL B 304 -16.481 39.836 30.304 1.00 34.10 N ANISOU 4804 N VAL B 304 4298 4163 4494 117 527 142 N ATOM 4805 CA VAL B 304 -15.153 40.328 29.943 1.00 28.38 C ANISOU 4805 CA VAL B 304 3592 3398 3794 118 546 167 C ATOM 4806 C VAL B 304 -14.475 39.371 28.969 1.00 26.32 C ANISOU 4806 C VAL B 304 3335 3166 3499 112 536 172 C ATOM 4807 O VAL B 304 -13.838 39.800 28.000 1.00 22.14 O ANISOU 4807 O VAL B 304 2811 2632 2968 136 551 210 O ATOM 4808 CB VAL B 304 -14.302 40.553 31.206 1.00 31.10 C ANISOU 4808 CB VAL B 304 3952 3686 4181 84 556 142 C ATOM 4809 CG1 VAL B 304 -12.953 41.145 30.831 1.00 26.67 C ANISOU 4809 CG1 VAL B 304 3404 3080 3650 83 578 166 C ATOM 4810 CG2 VAL B 304 -15.032 41.464 32.184 1.00 18.80 C ANISOU 4810 CG2 VAL B 304 2389 2101 2652 91 566 131 C ATOM 4811 N ILE B 305 -14.586 38.063 29.219 1.00 26.62 N ANISOU 4811 N ILE B 305 3372 3231 3511 80 513 136 N ATOM 4812 CA ILE B 305 -14.073 37.067 28.280 1.00 21.29 C ANISOU 4812 CA ILE B 305 2700 2587 2802 74 502 135 C ATOM 4813 C ILE B 305 -14.814 37.164 26.952 1.00 19.65 C ANISOU 4813 C ILE B 305 2477 2436 2555 115 494 158 C ATOM 4814 O ILE B 305 -14.215 37.057 25.874 1.00 18.24 O ANISOU 4814 O ILE B 305 2304 2274 2354 133 498 181 O ATOM 4815 CB ILE B 305 -14.189 35.656 28.891 1.00 26.25 C ANISOU 4815 CB ILE B 305 3329 3229 3416 33 483 89 C ATOM 4816 CG1 ILE B 305 -13.434 35.570 30.220 1.00 31.64 C ANISOU 4816 CG1 ILE B 305 4027 3862 4132 0 490 69 C ATOM 4817 CG2 ILE B 305 -13.675 34.598 27.922 1.00 23.18 C ANISOU 4817 CG2 ILE B 305 2945 2869 2994 27 474 84 C ATOM 4818 CD1 ILE B 305 -13.701 34.284 30.981 1.00 28.11 C ANISOU 4818 CD1 ILE B 305 3581 3426 3674 -34 478 30 C ATOM 4819 N TYR B 306 -16.131 37.370 27.018 1.00 22.74 N ANISOU 4819 N TYR B 306 2846 2861 2934 132 484 151 N ATOM 4820 CA TYR B 306 -16.964 37.508 25.828 1.00 30.24 C ANISOU 4820 CA TYR B 306 3774 3873 3842 175 473 169 C ATOM 4821 C TYR B 306 -16.449 38.620 24.919 1.00 23.33 C ANISOU 4821 C TYR B 306 2906 2989 2967 224 498 228 C ATOM 4822 O TYR B 306 -16.286 38.426 23.708 1.00 19.40 O ANISOU 4822 O TYR B 306 2406 2534 2430 253 494 249 O ATOM 4823 CB TYR B 306 -18.395 37.795 26.282 1.00 20.40 C ANISOU 4823 CB TYR B 306 2502 2653 2594 186 463 156 C ATOM 4824 CG TYR B 306 -19.511 37.528 25.301 1.00 19.27 C ANISOU 4824 CG TYR B 306 2328 2591 2404 218 440 153 C ATOM 4825 CD1 TYR B 306 -19.323 36.755 24.159 1.00 25.29 C ANISOU 4825 CD1 TYR B 306 3083 3405 3120 225 423 146 C ATOM 4826 CD2 TYR B 306 -20.772 38.061 25.531 1.00 19.53 C ANISOU 4826 CD2 TYR B 306 2334 2651 2437 242 436 155 C ATOM 4827 CE1 TYR B 306 -20.374 36.523 23.277 1.00 27.01 C ANISOU 4827 CE1 TYR B 306 3267 3703 3291 254 399 136 C ATOM 4828 CE2 TYR B 306 -21.814 37.838 24.668 1.00 19.94 C ANISOU 4828 CE2 TYR B 306 2351 2782 2444 271 412 149 C ATOM 4829 CZ TYR B 306 -21.617 37.071 23.545 1.00 23.58 C ANISOU 4829 CZ TYR B 306 2804 3297 2859 277 393 138 C ATOM 4830 OH TYR B 306 -22.680 36.863 22.700 1.00 32.30 O ANISOU 4830 OH TYR B 306 3870 4486 3916 307 367 126 O ATOM 4831 N ILE B 307 -16.186 39.795 25.494 1.00 23.08 N ANISOU 4831 N ILE B 307 2886 2902 2983 234 526 256 N ATOM 4832 CA ILE B 307 -15.687 40.929 24.720 1.00 23.36 C ANISOU 4832 CA ILE B 307 2928 2916 3030 280 558 315 C ATOM 4833 C ILE B 307 -14.310 40.622 24.144 1.00 28.93 C ANISOU 4833 C ILE B 307 3653 3602 3736 270 570 331 C ATOM 4834 O ILE B 307 -14.022 40.931 22.980 1.00 24.01 O ANISOU 4834 O ILE B 307 3032 3002 3090 312 585 375 O ATOM 4835 CB ILE B 307 -15.664 42.197 25.595 1.00 32.72 C ANISOU 4835 CB ILE B 307 4121 4036 4275 285 589 332 C ATOM 4836 CG1 ILE B 307 -17.075 42.556 26.060 1.00 19.66 C ANISOU 4836 CG1 ILE B 307 2447 2405 2618 303 580 322 C ATOM 4837 CG2 ILE B 307 -15.051 43.366 24.847 1.00 20.95 C ANISOU 4837 CG2 ILE B 307 2639 2511 2808 328 630 394 C ATOM 4838 CD1 ILE B 307 -17.110 43.667 27.082 1.00 35.47 C ANISOU 4838 CD1 ILE B 307 4457 4340 4678 301 607 326 C ATOM 4839 N AMET B 308 -13.439 40.011 24.950 0.53 26.14 N ANISOU 4839 N AMET B 308 3314 3210 3407 218 566 297 N ATOM 4840 N BMET B 308 -13.437 40.014 24.947 0.47 26.14 N ANISOU 4840 N BMET B 308 3314 3210 3407 218 566 297 N ATOM 4841 CA AMET B 308 -12.062 39.776 24.527 0.53 28.78 C ANISOU 4841 CA AMET B 308 3666 3520 3749 207 580 311 C ATOM 4842 CA BMET B 308 -12.061 39.786 24.529 0.47 28.77 C ANISOU 4842 CA BMET B 308 3665 3518 3748 207 580 312 C ATOM 4843 C AMET B 308 -11.956 38.670 23.485 0.53 26.59 C ANISOU 4843 C AMET B 308 3388 3301 3415 213 560 305 C ATOM 4844 C BMET B 308 -11.903 38.614 23.569 0.47 26.58 C ANISOU 4844 C BMET B 308 3387 3296 3416 208 560 302 C ATOM 4845 O AMET B 308 -11.019 38.676 22.677 0.53 32.44 O ANISOU 4845 O AMET B 308 4140 4038 4149 226 577 335 O ATOM 4846 O BMET B 308 -10.868 38.522 22.900 0.47 32.40 O ANISOU 4846 O BMET B 308 4137 4025 4150 214 575 325 O ATOM 4847 CB AMET B 308 -11.194 39.428 25.736 0.53 32.20 C ANISOU 4847 CB AMET B 308 4111 3900 4222 153 579 276 C ATOM 4848 CB BMET B 308 -11.170 39.564 25.753 0.47 32.22 C ANISOU 4848 CB BMET B 308 4115 3899 4230 155 582 279 C ATOM 4849 CG AMET B 308 -10.969 40.573 26.708 0.53 35.26 C ANISOU 4849 CG AMET B 308 4502 4224 4671 145 602 279 C ATOM 4850 CG BMET B 308 -10.942 40.819 26.584 0.47 35.12 C ANISOU 4850 CG BMET B 308 4484 4202 4658 153 609 289 C ATOM 4851 SD AMET B 308 -10.058 40.032 28.167 0.53 44.40 S ANISOU 4851 SD AMET B 308 5669 5339 5863 85 593 229 S ATOM 4852 SD BMET B 308 -10.113 42.118 25.643 0.47 41.05 S ANISOU 4852 SD BMET B 308 5240 4912 5444 192 657 355 S ATOM 4853 CE AMET B 308 -8.728 39.108 27.401 0.53 38.36 C ANISOU 4853 CE AMET B 308 4914 4581 5079 72 593 237 C ATOM 4854 CE BMET B 308 -8.586 41.289 25.205 0.47 33.11 C ANISOU 4854 CE BMET B 308 4247 3900 4433 167 658 355 C ATOM 4855 N MET B 309 -12.888 37.716 23.483 1.00 24.48 N ANISOU 4855 N MET B 309 3106 3086 3108 201 528 265 N ATOM 4856 CA MET B 309 -12.730 36.500 22.692 1.00 25.98 C ANISOU 4856 CA MET B 309 3296 3324 3250 194 508 243 C ATOM 4857 C MET B 309 -13.840 36.233 21.679 1.00 32.54 C ANISOU 4857 C MET B 309 4104 4235 4023 230 485 239 C ATOM 4858 O MET B 309 -13.855 35.153 21.078 1.00 22.77 O ANISOU 4858 O MET B 309 2864 3041 2746 220 465 209 O ATOM 4859 CB MET B 309 -12.596 35.286 23.618 1.00 30.59 C ANISOU 4859 CB MET B 309 3885 3895 3842 137 490 187 C ATOM 4860 CG MET B 309 -11.431 35.370 24.592 1.00 24.99 C ANISOU 4860 CG MET B 309 3196 3118 3181 103 506 186 C ATOM 4861 SD MET B 309 -11.110 33.798 25.407 1.00 23.73 S ANISOU 4861 SD MET B 309 3045 2953 3019 48 490 131 S ATOM 4862 CE MET B 309 -10.405 32.863 24.054 1.00 17.63 C ANISOU 4862 CE MET B 309 2281 2214 2203 56 488 135 C ATOM 4863 N ASN B 310 -14.764 37.165 21.461 1.00 28.32 N ANISOU 4863 N ASN B 310 3553 3724 3484 272 488 266 N ATOM 4864 CA ASN B 310 -15.748 37.020 20.391 1.00 27.82 C ANISOU 4864 CA ASN B 310 3465 3744 3361 315 467 267 C ATOM 4865 C ASN B 310 -15.707 38.276 19.533 1.00 31.30 C ANISOU 4865 C ASN B 310 3905 4194 3791 383 494 337 C ATOM 4866 O ASN B 310 -16.169 39.341 19.958 1.00 23.21 O ANISOU 4866 O ASN B 310 2876 3146 2798 406 512 367 O ATOM 4867 CB ASN B 310 -17.155 36.770 20.936 1.00 19.94 C ANISOU 4867 CB ASN B 310 2437 2781 2357 304 440 227 C ATOM 4868 CG ASN B 310 -18.090 36.189 19.884 1.00 30.50 C ANISOU 4868 CG ASN B 310 3744 4214 3630 331 408 205 C ATOM 4869 OD1 ASN B 310 -18.703 36.922 19.105 1.00 30.99 O ANISOU 4869 OD1 ASN B 310 3788 4326 3660 390 408 241 O ATOM 4870 ND2 ASN B 310 -18.192 34.864 19.850 1.00 32.88 N ANISOU 4870 ND2 ASN B 310 4039 4542 3912 289 383 146 N ATOM 4871 N LYS B 311 -15.152 38.144 18.326 1.00 25.58 N ANISOU 4871 N LYS B 311 3188 3506 3026 418 500 365 N ATOM 4872 CA LYS B 311 -15.030 39.287 17.430 1.00 33.79 C ANISOU 4872 CA LYS B 311 4230 4556 4053 488 531 438 C ATOM 4873 C LYS B 311 -16.397 39.828 17.031 1.00 23.84 C ANISOU 4873 C LYS B 311 2939 3360 2757 542 518 454 C ATOM 4874 O LYS B 311 -16.588 41.047 16.947 1.00 30.73 O ANISOU 4874 O LYS B 311 3812 4214 3650 589 550 512 O ATOM 4875 CB LYS B 311 -14.227 38.894 16.191 1.00 26.90 C ANISOU 4875 CB LYS B 311 3368 3719 3133 516 538 461 C ATOM 4876 CG LYS B 311 -14.141 39.971 15.126 1.00 44.00 C ANISOU 4876 CG LYS B 311 5535 5907 5276 597 571 541 C ATOM 4877 CD LYS B 311 -13.503 39.422 13.860 1.00 33.15 C ANISOU 4877 CD LYS B 311 4169 4584 3842 628 572 555 C ATOM 4878 CE LYS B 311 -13.351 40.498 12.798 1.00 52.67 C ANISOU 4878 CE LYS B 311 6644 7077 6291 712 612 642 C ATOM 4879 NZ LYS B 311 -12.691 39.972 11.566 1.00 60.94 N ANISOU 4879 NZ LYS B 311 7701 8176 7277 746 614 658 N ATOM 4880 N GLN B 312 -17.360 38.939 16.773 1.00 24.77 N ANISOU 4880 N GLN B 312 3029 3556 2825 535 473 402 N ATOM 4881 CA GLN B 312 -18.680 39.391 16.344 1.00 26.86 C ANISOU 4881 CA GLN B 312 3260 3894 3052 588 457 412 C ATOM 4882 C GLN B 312 -19.375 40.187 17.440 1.00 33.02 C ANISOU 4882 C GLN B 312 4032 4628 3884 580 468 419 C ATOM 4883 O GLN B 312 -19.901 41.278 17.188 1.00 38.19 O ANISOU 4883 O GLN B 312 4678 5295 4539 640 488 472 O ATOM 4884 CB GLN B 312 -19.546 38.204 15.922 1.00 28.35 C ANISOU 4884 CB GLN B 312 3416 4173 3183 574 405 344 C ATOM 4885 CG GLN B 312 -20.919 38.621 15.418 1.00 36.53 C ANISOU 4885 CG GLN B 312 4410 5295 4174 630 383 351 C ATOM 4886 CD GLN B 312 -21.790 37.446 15.025 1.00 38.43 C ANISOU 4886 CD GLN B 312 4613 5626 4364 611 331 276 C ATOM 4887 OE1 GLN B 312 -21.990 36.514 15.803 1.00 47.99 O ANISOU 4887 OE1 GLN B 312 5818 6815 5601 541 311 209 O ATOM 4888 NE2 GLN B 312 -22.315 37.486 13.809 1.00 45.89 N ANISOU 4888 NE2 GLN B 312 5531 6672 5234 674 311 286 N ATOM 4889 N PHE B 313 -19.389 39.658 18.666 1.00 28.80 N ANISOU 4889 N PHE B 313 3502 4044 3396 511 458 367 N ATOM 4890 CA PHE B 313 -20.048 40.360 19.764 1.00 24.04 C ANISOU 4890 CA PHE B 313 2893 3399 2842 502 468 367 C ATOM 4891 C PHE B 313 -19.348 41.676 20.076 1.00 24.74 C ANISOU 4891 C PHE B 313 3008 3408 2984 524 518 428 C ATOM 4892 O PHE B 313 -20.004 42.678 20.384 1.00 21.75 O ANISOU 4892 O PHE B 313 2621 3015 2628 557 536 458 O ATOM 4893 CB PHE B 313 -20.098 39.475 21.009 1.00 22.45 C ANISOU 4893 CB PHE B 313 2694 3160 2675 425 450 301 C ATOM 4894 CG PHE B 313 -20.684 40.163 22.212 1.00 29.85 C ANISOU 4894 CG PHE B 313 3628 4051 3662 413 463 299 C ATOM 4895 CD1 PHE B 313 -22.051 40.362 22.312 1.00 30.97 C ANISOU 4895 CD1 PHE B 313 3736 4242 3789 436 446 291 C ATOM 4896 CD2 PHE B 313 -19.868 40.624 23.235 1.00 28.82 C ANISOU 4896 CD2 PHE B 313 3527 3831 3592 381 490 305 C ATOM 4897 CE1 PHE B 313 -22.596 40.998 23.410 1.00 34.99 C ANISOU 4897 CE1 PHE B 313 4243 4709 4343 428 460 289 C ATOM 4898 CE2 PHE B 313 -20.407 41.263 24.335 1.00 26.37 C ANISOU 4898 CE2 PHE B 313 3214 3480 3324 373 502 300 C ATOM 4899 CZ PHE B 313 -21.774 41.450 24.422 1.00 27.51 C ANISOU 4899 CZ PHE B 313 3328 3671 3453 397 488 293 C ATOM 4900 N ARG B 314 -18.014 41.688 20.008 1.00 24.00 N ANISOU 4900 N ARG B 314 2945 3259 2915 506 542 445 N ATOM 4901 CA ARG B 314 -17.263 42.905 20.300 1.00 30.46 C ANISOU 4901 CA ARG B 314 3786 3995 3791 520 592 497 C ATOM 4902 C ARG B 314 -17.629 44.031 19.340 1.00 32.44 C ANISOU 4902 C ARG B 314 4030 4270 4025 603 622 571 C ATOM 4903 O ARG B 314 -17.814 45.179 19.760 1.00 31.59 O ANISOU 4903 O ARG B 314 3927 4113 3964 626 658 607 O ATOM 4904 CB ARG B 314 -15.763 42.613 20.243 1.00 28.06 C ANISOU 4904 CB ARG B 314 3510 3640 3511 488 609 501 C ATOM 4905 CG ARG B 314 -14.887 43.852 20.244 1.00 31.26 C ANISOU 4905 CG ARG B 314 3935 3969 3973 508 664 559 C ATOM 4906 CD ARG B 314 -13.451 43.522 20.611 1.00 24.75 C ANISOU 4906 CD ARG B 314 3133 3083 3188 458 678 545 C ATOM 4907 NE ARG B 314 -12.739 42.803 19.562 1.00 23.84 N ANISOU 4907 NE ARG B 314 3025 3006 3028 468 673 557 N ATOM 4908 CZ ARG B 314 -12.456 41.507 19.598 1.00 33.93 C ANISOU 4908 CZ ARG B 314 4304 4312 4275 427 638 507 C ATOM 4909 NH1 ARG B 314 -12.829 40.746 20.613 1.00 29.55 N ANISOU 4909 NH1 ARG B 314 3745 3753 3728 373 606 445 N ATOM 4910 NH2 ARG B 314 -11.779 40.963 18.591 1.00 31.18 N ANISOU 4910 NH2 ARG B 314 3964 3995 3888 442 639 522 N ATOM 4911 N ASN B 315 -17.747 43.719 18.048 1.00 32.27 N ANISOU 4911 N ASN B 315 3999 4327 3936 651 611 595 N ATOM 4912 CA ASN B 315 -18.094 44.744 17.070 1.00 30.94 C ANISOU 4912 CA ASN B 315 3823 4190 3742 738 641 670 C ATOM 4913 C ASN B 315 -19.559 45.150 17.174 1.00 35.62 C ANISOU 4913 C ASN B 315 4385 4836 4314 778 625 672 C ATOM 4914 O ASN B 315 -19.896 46.313 16.922 1.00 31.40 O ANISOU 4914 O ASN B 315 3848 4290 3792 840 663 736 O ATOM 4915 CB ASN B 315 -17.760 44.246 15.665 1.00 23.41 C ANISOU 4915 CB ASN B 315 2868 3312 2716 781 632 693 C ATOM 4916 CG ASN B 315 -16.328 43.753 15.548 1.00 35.52 C ANISOU 4916 CG ASN B 315 4430 4798 4267 742 647 688 C ATOM 4917 OD1 ASN B 315 -15.455 44.162 16.316 1.00 32.62 O ANISOU 4917 OD1 ASN B 315 4086 4337 3972 702 678 694 O ATOM 4918 ND2 ASN B 315 -16.080 42.862 14.590 1.00 45.71 N ANISOU 4918 ND2 ASN B 315 5719 6157 5492 752 623 675 N ATOM 4919 N CYS B 316 -20.442 44.214 17.541 1.00 33.57 N ANISOU 4919 N CYS B 316 4099 4631 4026 743 573 605 N ATOM 4920 CA CYS B 316 -21.832 44.575 17.799 1.00 32.21 C ANISOU 4920 CA CYS B 316 3894 4502 3842 772 558 600 C ATOM 4921 C CYS B 316 -21.935 45.539 18.973 1.00 36.79 C ANISOU 4921 C CYS B 316 4487 4993 4499 758 592 614 C ATOM 4922 O CYS B 316 -22.773 46.448 18.967 1.00 35.12 O ANISOU 4922 O CYS B 316 4259 4792 4291 811 610 652 O ATOM 4923 CB CYS B 316 -22.669 43.321 18.061 1.00 38.96 C ANISOU 4923 CB CYS B 316 4718 5423 4662 727 499 519 C ATOM 4924 SG CYS B 316 -22.962 42.290 16.595 1.00 44.00 S ANISOU 4924 SG CYS B 316 5328 6189 5202 757 453 496 S ATOM 4925 N MET B 317 -21.099 45.346 19.995 1.00 34.89 N ANISOU 4925 N MET B 317 4273 4666 4318 688 602 581 N ATOM 4926 CA MET B 317 -21.097 46.256 21.135 1.00 34.33 C ANISOU 4926 CA MET B 317 4216 4508 4321 672 635 587 C ATOM 4927 C MET B 317 -20.565 47.633 20.750 1.00 38.77 C ANISOU 4927 C MET B 317 4797 5013 4921 725 696 664 C ATOM 4928 O MET B 317 -21.134 48.655 21.149 1.00 39.00 O ANISOU 4928 O MET B 317 4824 5010 4985 756 725 693 O ATOM 4929 CB MET B 317 -20.274 45.658 22.273 1.00 37.21 C ANISOU 4929 CB MET B 317 4602 4804 4732 588 628 530 C ATOM 4930 CG MET B 317 -20.565 46.268 23.631 1.00 32.07 C ANISOU 4930 CG MET B 317 3957 4085 4143 561 644 510 C ATOM 4931 SD MET B 317 -19.589 45.489 24.922 1.00 49.24 S ANISOU 4931 SD MET B 317 6154 6194 6361 469 632 444 S ATOM 4932 CE MET B 317 -17.955 45.666 24.216 1.00 44.51 C ANISOU 4932 CE MET B 317 5582 5549 5778 467 662 479 C ATOM 4933 N VAL B 318 -19.476 47.678 19.977 1.00 43.83 N ANISOU 4933 N VAL B 318 5458 5637 5559 736 719 700 N ATOM 4934 CA VAL B 318 -18.936 48.957 19.519 1.00 42.03 C ANISOU 4934 CA VAL B 318 5247 5353 5369 788 783 778 C ATOM 4935 C VAL B 318 -19.956 49.681 18.650 1.00 49.36 C ANISOU 4935 C VAL B 318 6155 6343 6256 881 797 840 C ATOM 4936 O VAL B 318 -20.118 50.903 18.744 1.00 51.57 O ANISOU 4936 O VAL B 318 6442 6573 6580 925 849 895 O ATOM 4937 CB VAL B 318 -17.603 48.742 18.778 1.00 25.77 C ANISOU 4937 CB VAL B 318 3209 3273 3308 784 803 804 C ATOM 4938 CG1 VAL B 318 -17.194 49.999 18.028 1.00 44.72 C ANISOU 4938 CG1 VAL B 318 5622 5635 5735 853 871 895 C ATOM 4939 CG2 VAL B 318 -16.517 48.344 19.756 1.00 28.60 C ANISOU 4939 CG2 VAL B 318 3589 3554 3726 699 802 753 C ATOM 4940 N THR B 319 -20.659 48.938 17.790 1.00 38.92 N ANISOU 4940 N THR B 319 4806 5133 4848 914 753 833 N ATOM 4941 CA THR B 319 -21.743 49.529 17.009 1.00 41.77 C ANISOU 4941 CA THR B 319 5141 5569 5160 1003 758 885 C ATOM 4942 C THR B 319 -22.812 50.120 17.921 1.00 45.64 C ANISOU 4942 C THR B 319 5616 6042 5684 1007 760 874 C ATOM 4943 O THR B 319 -23.239 51.267 17.741 1.00 47.00 O ANISOU 4943 O THR B 319 5787 6197 5875 1074 804 939 O ATOM 4944 CB THR B 319 -22.355 48.477 16.077 1.00 37.29 C ANISOU 4944 CB THR B 319 4544 5132 4495 1025 699 857 C ATOM 4945 OG1 THR B 319 -21.389 48.080 15.095 1.00 51.62 O ANISOU 4945 OG1 THR B 319 6374 6967 6273 1037 704 879 O ATOM 4946 CG2 THR B 319 -23.595 49.026 15.373 1.00 36.11 C ANISOU 4946 CG2 THR B 319 4359 5072 4290 1116 695 902 C ATOM 4947 N THR B 320 -23.247 49.349 18.920 1.00 44.21 N ANISOU 4947 N THR B 320 5423 5861 5514 938 716 795 N ATOM 4948 CA THR B 320 -24.260 49.838 19.849 1.00 47.65 C ANISOU 4948 CA THR B 320 5844 6281 5981 938 718 780 C ATOM 4949 C THR B 320 -23.748 51.024 20.656 1.00 52.02 C ANISOU 4949 C THR B 320 6428 6715 6624 932 779 810 C ATOM 4950 O THR B 320 -24.464 52.016 20.840 1.00 54.63 O ANISOU 4950 O THR B 320 6752 7030 6977 982 810 848 O ATOM 4951 CB THR B 320 -24.702 48.706 20.777 1.00 40.03 C ANISOU 4951 CB THR B 320 4863 5334 5012 860 664 690 C ATOM 4952 OG1 THR B 320 -25.512 47.778 20.046 1.00 37.62 O ANISOU 4952 OG1 THR B 320 4520 5146 4630 876 611 663 O ATOM 4953 CG2 THR B 320 -25.492 49.250 21.961 1.00 44.85 C ANISOU 4953 CG2 THR B 320 5467 5903 5671 848 674 672 C ATOM 4954 N LEU B 321 -22.507 50.945 21.139 1.00 46.86 N ANISOU 4954 N LEU B 321 5806 5977 6022 874 797 791 N ATOM 4955 CA LEU B 321 -21.970 51.988 22.004 1.00 50.61 C ANISOU 4955 CA LEU B 321 6307 6336 6585 857 850 803 C ATOM 4956 C LEU B 321 -21.657 53.276 21.252 1.00 53.88 C ANISOU 4956 C LEU B 321 6734 6708 7028 929 919 893 C ATOM 4957 O LEU B 321 -21.591 54.340 21.877 1.00 55.24 O ANISOU 4957 O LEU B 321 6921 6794 7272 935 969 911 O ATOM 4958 CB LEU B 321 -20.710 51.480 22.706 1.00 56.80 C ANISOU 4958 CB LEU B 321 7117 7051 7413 773 846 753 C ATOM 4959 CG LEU B 321 -20.716 51.467 24.234 1.00 48.69 C ANISOU 4959 CG LEU B 321 6098 5960 6442 707 839 688 C ATOM 4960 CD1 LEU B 321 -22.070 51.022 24.741 1.00 46.20 C ANISOU 4960 CD1 LEU B 321 5756 5706 6092 707 798 651 C ATOM 4961 CD2 LEU B 321 -19.630 50.541 24.748 1.00 35.30 C ANISOU 4961 CD2 LEU B 321 4418 4238 4758 629 814 632 C ATOM 4962 N CYS B 322 -21.468 53.209 19.938 1.00 54.27 N ANISOU 4962 N CYS B 322 6781 6816 7025 986 926 949 N ATOM 4963 CA CYS B 322 -21.036 54.373 19.168 1.00 57.38 C ANISOU 4963 CA CYS B 322 7190 7166 7446 1056 997 1040 C ATOM 4964 C CYS B 322 -21.978 54.671 18.002 1.00 59.80 C ANISOU 4964 C CYS B 322 7473 7570 7680 1159 1000 1109 C ATOM 4965 O CYS B 322 -21.553 54.747 16.847 1.00 56.21 O ANISOU 4965 O CYS B 322 7022 7150 7185 1213 1020 1168 O ATOM 4966 CB CYS B 322 -19.610 54.161 18.650 1.00 53.39 C ANISOU 4966 CB CYS B 322 6708 6623 6956 1032 1019 1056 C ATOM 4967 SG CYS B 322 -18.439 53.585 19.911 1.00 75.49 S ANISOU 4967 SG CYS B 322 9529 9331 9824 912 1003 970 S TER 4968 CYS B 322 HETATM 4969 C1 NAG C 1 10.504 21.775 0.449 1.00 31.14 C ANISOU 4969 C1 NAG C 1 4348 4372 3112 692 980 498 C HETATM 4970 C2 NAG C 1 9.023 21.861 0.817 1.00 23.37 C ANISOU 4970 C2 NAG C 1 3351 3416 2112 670 927 444 C HETATM 4971 C3 NAG C 1 8.228 20.792 0.069 1.00 29.16 C ANISOU 4971 C3 NAG C 1 4096 4219 2766 681 894 358 C HETATM 4972 C4 NAG C 1 8.469 20.889 -1.432 1.00 33.45 C ANISOU 4972 C4 NAG C 1 4651 4837 3221 760 916 384 C HETATM 4973 C5 NAG C 1 9.969 20.833 -1.720 1.00 36.32 C ANISOU 4973 C5 NAG C 1 5031 5165 3605 781 972 443 C HETATM 4974 C6 NAG C 1 10.308 21.064 -3.176 1.00 37.45 C ANISOU 4974 C6 NAG C 1 5186 5378 3665 865 1002 483 C HETATM 4975 C7 NAG C 1 8.286 22.682 3.011 1.00 41.30 C ANISOU 4975 C7 NAG C 1 5591 5596 4504 578 891 440 C HETATM 4976 C8 NAG C 1 8.167 22.373 4.473 1.00 34.37 C ANISOU 4976 C8 NAG C 1 4705 4654 3700 506 871 406 C HETATM 4977 N2 NAG C 1 8.833 21.727 2.252 1.00 38.15 N ANISOU 4977 N2 NAG C 1 5212 5221 4062 598 906 416 N HETATM 4978 O3 NAG C 1 6.841 20.944 0.352 1.00 28.76 O ANISOU 4978 O3 NAG C 1 4028 4199 2701 664 846 311 O HETATM 4979 O4 NAG C 1 7.811 19.808 -2.085 1.00 37.12 O ANISOU 4979 O4 NAG C 1 5126 5364 3615 766 885 294 O HETATM 4980 O5 NAG C 1 10.653 21.856 -0.977 1.00 31.25 O ANISOU 4980 O5 NAG C 1 4375 4456 3044 766 1002 523 O HETATM 4981 O6 NAG C 1 9.840 22.329 -3.624 1.00 26.84 O ANISOU 4981 O6 NAG C 1 3829 4073 2298 916 1008 548 O HETATM 4982 O7 NAG C 1 7.904 23.748 2.537 1.00 35.08 O ANISOU 4982 O7 NAG C 1 4793 4837 3697 620 897 489 O HETATM 4983 C1 NAG C 2 6.942 20.236 -3.160 1.00 40.88 C ANISOU 4983 C1 NAG C 2 5595 5938 4001 829 865 289 C HETATM 4984 C2 NAG C 2 6.700 19.020 -4.054 1.00 46.35 C ANISOU 4984 C2 NAG C 2 6302 6694 4616 844 847 201 C HETATM 4985 C3 NAG C 2 5.771 19.385 -5.208 1.00 42.94 C ANISOU 4985 C3 NAG C 2 5858 6376 4080 913 820 187 C HETATM 4986 C4 NAG C 2 4.490 20.015 -4.681 1.00 42.44 C ANISOU 4986 C4 NAG C 2 5766 6332 4028 894 775 173 C HETATM 4987 C5 NAG C 2 4.816 21.187 -3.758 1.00 46.18 C ANISOU 4987 C5 NAG C 2 6231 6731 4585 878 799 266 C HETATM 4988 C6 NAG C 2 3.590 21.771 -3.098 1.00 58.65 C ANISOU 4988 C6 NAG C 2 7781 8317 6185 853 758 251 C HETATM 4989 C7 NAG C 2 8.511 17.365 -4.102 1.00 46.31 C ANISOU 4989 C7 NAG C 2 6339 6618 4640 818 902 172 C HETATM 4990 C8 NAG C 2 9.806 16.973 -4.740 1.00 45.87 C ANISOU 4990 C8 NAG C 2 6307 6552 4568 853 953 206 C HETATM 4991 N2 NAG C 2 7.953 18.489 -4.560 1.00 38.75 N ANISOU 4991 N2 NAG C 2 5364 5714 3644 866 893 222 N HETATM 4992 O3 NAG C 2 5.462 18.215 -5.959 1.00 42.20 O ANISOU 4992 O3 NAG C 2 5774 6342 3916 920 798 90 O HETATM 4993 O4 NAG C 2 3.693 20.470 -5.770 1.00 54.13 O ANISOU 4993 O4 NAG C 2 7233 7922 5410 967 754 173 O HETATM 4994 O5 NAG C 2 5.689 20.757 -2.702 1.00 46.71 O ANISOU 4994 O5 NAG C 2 6308 6695 4744 812 821 269 O HETATM 4995 O6 NAG C 2 2.905 20.794 -2.326 1.00 59.66 O ANISOU 4995 O6 NAG C 2 7902 8423 6344 780 717 153 O HETATM 4996 O7 NAG C 2 7.991 16.693 -3.216 1.00 40.49 O ANISOU 4996 O7 NAG C 2 5597 5840 3949 751 874 105 O HETATM 4997 C1 NAG D 1 -19.971 34.615 74.790 1.00 36.31 C ANISOU 4997 C1 NAG D 1 4847 5192 3757 809 800 -486 C HETATM 4998 C2 NAG D 1 -21.473 34.531 74.458 1.00 32.36 C ANISOU 4998 C2 NAG D 1 4348 4639 3307 796 852 -440 C HETATM 4999 C3 NAG D 1 -22.256 35.630 75.190 1.00 35.23 C ANISOU 4999 C3 NAG D 1 4717 5016 3656 823 857 -490 C HETATM 5000 C4 NAG D 1 -21.910 35.668 76.674 1.00 30.87 C ANISOU 5000 C4 NAG D 1 4176 4551 3002 900 858 -518 C HETATM 5001 C5 NAG D 1 -20.400 35.757 76.849 1.00 39.74 C ANISOU 5001 C5 NAG D 1 5296 5722 4084 904 801 -567 C HETATM 5002 C6 NAG D 1 -19.955 35.752 78.295 1.00 37.28 C ANISOU 5002 C6 NAG D 1 4992 5507 3665 984 795 -598 C HETATM 5003 C7 NAG D 1 -22.298 33.693 72.294 1.00 39.26 C ANISOU 5003 C7 NAG D 1 5206 5395 4317 697 880 -357 C HETATM 5004 C8 NAG D 1 -22.419 33.976 70.825 1.00 39.34 C ANISOU 5004 C8 NAG D 1 5201 5334 4414 624 860 -358 C HETATM 5005 N2 NAG D 1 -21.683 34.632 73.022 1.00 33.77 N ANISOU 5005 N2 NAG D 1 4515 4741 3577 723 842 -427 N HETATM 5006 O3 NAG D 1 -23.651 35.398 75.033 1.00 39.54 O ANISOU 5006 O3 NAG D 1 5262 5525 4237 822 911 -440 O HETATM 5007 O4 NAG D 1 -22.508 36.806 77.285 1.00 29.80 O ANISOU 5007 O4 NAG D 1 4044 4423 2854 921 856 -578 O HETATM 5008 O5 NAG D 1 -19.789 34.627 76.214 1.00 25.78 O ANISOU 5008 O5 NAG D 1 3524 3942 2328 885 804 -507 O HETATM 5009 O6 NAG D 1 -20.469 34.636 79.009 1.00 32.31 O ANISOU 5009 O6 NAG D 1 4377 4918 2981 1045 853 -518 O HETATM 5010 O7 NAG D 1 -22.737 32.664 72.796 1.00 54.91 O ANISOU 5010 O7 NAG D 1 7195 7396 6273 732 929 -297 O HETATM 5011 C1 NAG D 2 -23.486 36.418 78.271 1.00 46.46 C ANISOU 5011 C1 NAG D 2 6167 6570 4915 984 912 -538 C HETATM 5012 C2 NAG D 2 -23.864 37.670 79.074 1.00 39.25 C ANISOU 5012 C2 NAG D 2 5259 5680 3972 1014 902 -615 C HETATM 5013 C3 NAG D 2 -24.992 37.368 80.061 1.00 47.30 C ANISOU 5013 C3 NAG D 2 6292 6734 4946 1079 964 -573 C HETATM 5014 C4 NAG D 2 -26.150 36.658 79.373 1.00 53.57 C ANISOU 5014 C4 NAG D 2 7081 7468 5806 1053 1022 -486 C HETATM 5015 C5 NAG D 2 -25.645 35.452 78.591 1.00 46.15 C ANISOU 5015 C5 NAG D 2 6135 6506 4895 1020 1026 -420 C HETATM 5016 C6 NAG D 2 -26.729 34.783 77.781 1.00 56.47 C ANISOU 5016 C6 NAG D 2 7431 7750 6277 983 1077 -345 C HETATM 5017 C7 NAG D 2 -22.038 39.287 79.373 1.00 48.38 C ANISOU 5017 C7 NAG D 2 6407 6877 5099 996 794 -781 C HETATM 5018 C8 NAG D 2 -20.873 39.695 80.225 1.00 46.49 C ANISOU 5018 C8 NAG D 2 6164 6714 4786 1029 744 -864 C HETATM 5019 N2 NAG D 2 -22.707 38.203 79.777 1.00 46.47 N ANISOU 5019 N2 NAG D 2 6175 6659 4822 1040 849 -696 N HETATM 5020 O3 NAG D 2 -25.457 38.599 80.602 1.00 39.41 O ANISOU 5020 O3 NAG D 2 5297 5740 3936 1097 957 -645 O HETATM 5021 O4 NAG D 2 -27.101 36.225 80.341 1.00 48.31 O ANISOU 5021 O4 NAG D 2 6425 6838 5094 1118 1085 -440 O HETATM 5022 O5 NAG D 2 -24.643 35.876 77.657 1.00 53.88 O ANISOU 5022 O5 NAG D 2 7104 7454 5916 960 964 -465 O HETATM 5023 O6 NAG D 2 -26.907 35.439 76.533 1.00 60.13 O ANISOU 5023 O6 NAG D 2 7877 8142 6828 910 1047 -370 O HETATM 5024 O7 NAG D 2 -22.357 39.910 78.365 1.00 60.07 O ANISOU 5024 O7 NAG D 2 7879 8278 6667 935 786 -792 O HETATM 5025 C ACE A 401 17.301 34.909 5.033 1.00 56.54 C ANISOU 5025 C ACE A 401 7315 6944 7224 598 1408 1210 C HETATM 5026 O ACE A 401 18.249 34.504 5.707 1.00 54.99 O ANISOU 5026 O ACE A 401 7100 6715 7080 551 1406 1186 O HETATM 5027 CH3 ACE A 401 17.462 35.971 3.986 1.00 50.48 C ANISOU 5027 CH3 ACE A 401 6546 6170 6463 660 1479 1301 C HETATM 5028 C1 RET A 402 10.565 31.853 30.839 1.00 25.52 C ANISOU 5028 C1 RET A 402 3216 2862 3621 -173 622 163 C HETATM 5029 C2 RET A 402 11.380 32.290 32.059 1.00 31.04 C ANISOU 5029 C2 RET A 402 3879 3561 4353 -192 605 127 C HETATM 5030 C3 RET A 402 11.928 31.151 32.834 1.00 34.64 C ANISOU 5030 C3 RET A 402 4333 4053 4776 -187 588 113 C HETATM 5031 C4 RET A 402 10.775 30.304 33.352 1.00 16.79 C ANISOU 5031 C4 RET A 402 2103 1813 2464 -177 571 100 C HETATM 5032 C5 RET A 402 9.783 29.952 32.281 1.00 20.59 C ANISOU 5032 C5 RET A 402 2618 2287 2919 -166 585 126 C HETATM 5033 C6 RET A 402 9.832 30.541 31.063 1.00 24.56 C ANISOU 5033 C6 RET A 402 3123 2769 3440 -161 607 156 C HETATM 5034 C7 RET A 402 9.174 30.007 29.881 1.00 16.57 C ANISOU 5034 C7 RET A 402 2140 1762 2395 -144 620 182 C HETATM 5035 C8 RET A 402 8.874 28.704 29.604 1.00 17.03 C ANISOU 5035 C8 RET A 402 2223 1841 2406 -133 619 185 C HETATM 5036 C9 RET A 402 8.692 28.068 28.375 1.00 20.55 C ANISOU 5036 C9 RET A 402 2691 2295 2823 -116 635 208 C HETATM 5037 C10 RET A 402 8.555 26.661 28.330 1.00 26.52 C ANISOU 5037 C10 RET A 402 3468 3069 3539 -110 635 201 C HETATM 5038 C11 RET A 402 9.095 25.754 27.443 1.00 16.25 C ANISOU 5038 C11 RET A 402 2181 1776 2215 -96 652 219 C HETATM 5039 C12 RET A 402 8.982 24.387 27.464 1.00 16.15 C ANISOU 5039 C12 RET A 402 2190 1775 2170 -90 656 209 C HETATM 5040 C13 RET A 402 9.842 23.449 26.877 1.00 16.22 C ANISOU 5040 C13 RET A 402 2209 1789 2165 -77 675 225 C HETATM 5041 C14 RET A 402 9.596 22.095 26.884 1.00 16.16 C ANISOU 5041 C14 RET A 402 2224 1787 2128 -72 683 213 C HETATM 5042 C15 RET A 402 10.451 21.150 26.346 1.00 16.25 C ANISOU 5042 C15 RET A 402 2247 1801 2128 -58 705 227 C HETATM 5043 C16 RET A 402 9.566 32.969 30.500 1.00 21.79 C ANISOU 5043 C16 RET A 402 2748 2363 3169 -173 629 167 C HETATM 5044 C17 RET A 402 11.534 31.704 29.655 1.00 32.62 C ANISOU 5044 C17 RET A 402 4111 3755 4529 -162 650 203 C HETATM 5045 C18 RET A 402 8.785 28.920 32.731 1.00 19.21 C ANISOU 5045 C18 RET A 402 2471 2132 2697 -158 573 114 C HETATM 5046 C19 RET A 402 8.601 28.831 27.099 1.00 27.19 C ANISOU 5046 C19 RET A 402 3533 3126 3671 -103 654 238 C HETATM 5047 C20 RET A 402 11.094 23.940 26.258 1.00 16.41 C ANISOU 5047 C20 RET A 402 2216 1809 2209 -67 693 255 C HETATM 5048 C1 NAG A 403 20.980 33.848 7.284 1.00 47.25 C ANISOU 5048 C1 NAG A 403 6056 5650 6249 445 1422 1151 C HETATM 5049 C2 NAG A 403 20.652 35.221 7.869 1.00 49.29 C ANISOU 5049 C2 NAG A 403 6289 5852 6586 420 1436 1165 C HETATM 5050 C3 NAG A 403 21.638 36.263 7.346 1.00 50.70 C ANISOU 5050 C3 NAG A 403 6439 5983 6840 435 1515 1239 C HETATM 5051 C4 NAG A 403 23.073 35.818 7.596 1.00 55.87 C ANISOU 5051 C4 NAG A 403 7064 6620 7544 407 1534 1237 C HETATM 5052 C5 NAG A 403 23.301 34.411 7.050 1.00 67.98 C ANISOU 5052 C5 NAG A 403 8626 8214 8990 434 1514 1222 C HETATM 5053 C6 NAG A 403 24.656 33.850 7.411 1.00 61.86 C ANISOU 5053 C6 NAG A 403 7821 7426 8257 406 1525 1214 C HETATM 5054 C7 NAG A 403 18.524 36.319 8.400 1.00 50.47 C ANISOU 5054 C7 NAG A 403 6455 5996 6726 419 1394 1142 C HETATM 5055 C8 NAG A 403 17.140 36.641 7.924 1.00 52.49 C ANISOU 5055 C8 NAG A 403 6738 6285 6920 460 1379 1151 C HETATM 5056 N2 NAG A 403 19.286 35.612 7.559 1.00 46.40 N ANISOU 5056 N2 NAG A 403 5949 5510 6171 450 1418 1168 N HETATM 5057 O3 NAG A 403 21.398 37.513 7.983 1.00 67.30 O ANISOU 5057 O3 NAG A 403 8517 8027 9028 405 1530 1245 O HETATM 5058 O4 NAG A 403 23.973 36.711 6.950 1.00 60.03 O ANISOU 5058 O4 NAG A 403 7565 7107 8134 427 1612 1309 O HETATM 5059 O5 NAG A 403 22.328 33.507 7.595 1.00 54.66 O ANISOU 5059 O5 NAG A 403 6966 6564 7237 418 1441 1152 O HETATM 5060 O6 NAG A 403 24.892 33.922 8.810 1.00 65.02 O ANISOU 5060 O6 NAG A 403 8187 7793 8724 338 1486 1157 O HETATM 5061 O7 NAG A 403 18.934 36.679 9.499 1.00 60.11 O ANISOU 5061 O7 NAG A 403 7646 7168 8026 362 1384 1111 O HETATM 5062 O1 DAO A 404 22.761 24.710 22.240 1.00 42.59 O ANISOU 5062 O1 DAO A 404 5343 5118 5721 22 906 515 O HETATM 5063 O2 DAO A 404 22.968 26.840 22.854 1.00 52.44 O ANISOU 5063 O2 DAO A 404 6530 6332 7061 -20 900 506 O HETATM 5064 C1 DAO A 404 23.149 25.613 23.009 1.00 45.90 C ANISOU 5064 C1 DAO A 404 5720 5528 6190 -3 894 502 C HETATM 5065 C2 DAO A 404 23.924 25.201 24.274 1.00 44.87 C ANISOU 5065 C2 DAO A 404 5555 5420 6074 -13 870 477 C HETATM 5066 C3 DAO A 404 23.292 25.563 25.610 1.00 38.85 C ANISOU 5066 C3 DAO A 404 4781 4662 5318 -38 828 432 C HETATM 5067 C4 DAO A 404 23.617 24.554 26.705 1.00 38.50 C ANISOU 5067 C4 DAO A 404 4730 4651 5246 -29 804 411 C HETATM 5068 C5 DAO A 404 22.536 24.451 27.773 1.00 37.34 C ANISOU 5068 C5 DAO A 404 4600 4511 5076 -40 768 373 C HETATM 5069 C6 DAO A 404 22.626 23.172 28.595 1.00 35.79 C ANISOU 5069 C6 DAO A 404 4416 4345 4836 -20 755 365 C HETATM 5070 C7 DAO A 404 23.699 23.208 29.677 1.00 42.28 C ANISOU 5070 C7 DAO A 404 5187 5200 5677 -19 736 351 C HETATM 5071 C8 DAO A 404 24.236 21.825 30.023 1.00 46.18 C ANISOU 5071 C8 DAO A 404 5691 5724 6132 15 743 366 C HETATM 5072 C9 DAO A 404 25.008 21.775 31.335 1.00 48.78 C ANISOU 5072 C9 DAO A 404 5974 6096 6464 22 716 347 C HETATM 5073 C10 DAO A 404 25.503 20.378 31.686 1.00 46.94 C ANISOU 5073 C10 DAO A 404 5752 5892 6190 63 726 368 C HETATM 5074 C11 DAO A 404 25.612 20.139 33.187 1.00 50.11 C ANISOU 5074 C11 DAO A 404 6130 6339 6570 76 694 345 C HETATM 5075 C12 DAO A 404 26.330 18.839 33.524 1.00 55.17 C ANISOU 5075 C12 DAO A 404 6774 7012 7176 122 708 373 C HETATM 5076 C18 OLC A 405 23.713 31.720 38.259 1.00 48.18 C ANISOU 5076 C18 OLC A 405 5593 6022 6692 -245 473 -89 C HETATM 5077 C10 OLC A 405 24.618 30.457 29.204 1.00 53.46 C ANISOU 5077 C10 OLC A 405 6418 6476 7417 -180 754 287 C HETATM 5078 C9 OLC A 405 23.562 31.126 28.817 1.00 59.15 C ANISOU 5078 C9 OLC A 405 7169 7161 8144 -187 763 290 C HETATM 5079 C17 OLC A 405 23.905 30.408 37.541 1.00 48.29 C ANISOU 5079 C17 OLC A 405 5641 6048 6657 -208 495 -26 C HETATM 5080 C11 OLC A 405 25.116 30.418 30.614 1.00 50.20 C ANISOU 5080 C11 OLC A 405 5961 6101 7010 -193 714 235 C HETATM 5081 C8 OLC A 405 22.914 31.030 27.473 1.00 51.00 C ANISOU 5081 C8 OLC A 405 6184 6103 7089 -166 797 339 C HETATM 5082 C24 OLC A 405 23.975 30.182 16.681 1.00 51.77 C ANISOU 5082 C24 OLC A 405 6458 6160 7052 79 1128 749 C HETATM 5083 C16 OLC A 405 23.744 30.495 36.046 1.00 47.88 C ANISOU 5083 C16 OLC A 405 5620 5940 6631 -213 540 28 C HETATM 5084 C12 OLC A 405 24.099 29.848 31.552 1.00 53.75 C ANISOU 5084 C12 OLC A 405 6445 6576 7401 -183 676 206 C HETATM 5085 C7 OLC A 405 23.142 32.238 26.624 1.00 55.36 C ANISOU 5085 C7 OLC A 405 6720 6610 7705 -177 837 366 C HETATM 5086 C15 OLC A 405 23.856 29.149 35.376 1.00 56.37 C ANISOU 5086 C15 OLC A 405 6733 7029 7655 -176 560 83 C HETATM 5087 C13 OLC A 405 24.499 29.851 33.017 1.00 53.85 C ANISOU 5087 C13 OLC A 405 6416 6633 7411 -191 633 154 C HETATM 5088 C6 OLC A 405 22.622 32.086 25.202 1.00 51.51 C ANISOU 5088 C6 OLC A 405 6277 6107 7188 -148 873 420 C HETATM 5089 C14 OLC A 405 23.508 29.144 33.909 1.00 49.76 C ANISOU 5089 C14 OLC A 405 5936 6143 6829 -174 602 134 C HETATM 5090 C5 OLC A 405 23.256 33.019 24.205 1.00 56.53 C ANISOU 5090 C5 OLC A 405 6891 6705 7882 -148 925 463 C HETATM 5091 C4 OLC A 405 22.983 32.632 22.779 1.00 52.62 C ANISOU 5091 C4 OLC A 405 6438 6209 7346 -109 960 519 C HETATM 5092 C3 OLC A 405 23.954 33.210 21.768 1.00 49.18 C ANISOU 5092 C3 OLC A 405 5979 5749 6960 -100 1017 570 C HETATM 5093 C2 OLC A 405 24.222 32.239 20.666 1.00 50.99 C ANISOU 5093 C2 OLC A 405 6239 6003 7133 -60 1040 614 C HETATM 5094 C21 OLC A 405 25.135 32.371 17.175 1.00 60.19 C ANISOU 5094 C21 OLC A 405 7438 7155 8276 31 1173 770 C HETATM 5095 C1 OLC A 405 24.961 32.814 19.496 1.00 56.25 C ANISOU 5095 C1 OLC A 405 6892 6645 7837 -42 1101 673 C HETATM 5096 C22 OLC A 405 25.058 31.158 16.274 1.00 61.51 C ANISOU 5096 C22 OLC A 405 7649 7362 8361 75 1178 791 C HETATM 5097 O19 OLC A 405 25.392 33.935 19.412 1.00 52.90 O ANISOU 5097 O19 OLC A 405 6433 6181 7486 -59 1133 688 O HETATM 5098 O25 OLC A 405 24.042 28.974 15.927 1.00 55.11 O ANISOU 5098 O25 OLC A 405 6916 6617 7405 114 1133 761 O HETATM 5099 O23 OLC A 405 24.850 31.586 14.928 1.00 60.48 O ANISOU 5099 O23 OLC A 405 7541 7226 8213 115 1225 848 O HETATM 5100 O20 OLC A 405 25.091 31.900 18.540 1.00 63.69 O ANISOU 5100 O20 OLC A 405 7866 7613 8720 -2 1119 708 O HETATM 5101 C10 OLC A 406 -3.027 22.422 43.435 1.00 58.33 C ANISOU 5101 C10 OLC A 406 7564 7190 7408 -100 591 -24 C HETATM 5102 C9 OLC A 406 -2.977 22.015 44.678 1.00 57.72 C ANISOU 5102 C9 OLC A 406 7491 7130 7310 -76 602 -18 C HETATM 5103 C11 OLC A 406 -3.776 21.713 42.348 1.00 55.43 C ANISOU 5103 C11 OLC A 406 7206 6800 7056 -121 609 -20 C HETATM 5104 C8 OLC A 406 -1.943 22.371 45.701 1.00 57.43 C ANISOU 5104 C8 OLC A 406 7445 7125 7250 -51 586 -20 C HETATM 5105 C24 OLC A 406 -6.438 17.854 54.796 1.00 73.12 C ANISOU 5105 C24 OLC A 406 9508 9228 9047 203 831 123 C HETATM 5106 C12 OLC A 406 -4.754 22.561 41.595 1.00 52.32 C ANISOU 5106 C12 OLC A 406 6802 6398 6678 -141 594 -37 C HETATM 5107 C7 OLC A 406 -2.512 22.955 46.957 1.00 61.08 C ANISOU 5107 C7 OLC A 406 7901 7609 7696 -34 578 -37 C HETATM 5108 C15 OLC A 406 -6.987 21.879 38.465 1.00 64.19 C ANISOU 5108 C15 OLC A 406 8299 7880 8209 -192 601 -60 C HETATM 5109 C13 OLC A 406 -5.442 21.810 40.466 1.00 55.01 C ANISOU 5109 C13 OLC A 406 7148 6723 7028 -160 608 -39 C HETATM 5110 C6 OLC A 406 -3.801 22.289 47.417 1.00 72.45 C ANISOU 5110 C6 OLC A 406 9355 9040 9132 -30 609 -27 C HETATM 5111 C14 OLC A 406 -6.349 22.646 39.599 1.00 57.97 C ANISOU 5111 C14 OLC A 406 7511 7099 7416 -175 590 -53 C HETATM 5112 C5 OLC A 406 -4.158 22.527 48.864 1.00 65.18 C ANISOU 5112 C5 OLC A 406 8433 8148 8183 -1 610 -33 C HETATM 5113 C4 OLC A 406 -3.417 21.643 49.838 1.00 65.80 C ANISOU 5113 C4 OLC A 406 8519 8256 8226 39 628 -10 C HETATM 5114 C3 OLC A 406 -3.897 21.762 51.276 1.00 70.35 C ANISOU 5114 C3 OLC A 406 9097 8865 8769 73 635 -12 C HETATM 5115 C2 OLC A 406 -3.376 20.668 52.159 1.00 68.13 C ANISOU 5115 C2 OLC A 406 8826 8610 8450 118 664 22 C HETATM 5116 C21 OLC A 406 -4.744 19.598 54.086 1.00 71.53 C ANISOU 5116 C21 OLC A 406 9278 9063 8837 179 731 63 C HETATM 5117 C1 OLC A 406 -3.968 19.312 51.859 1.00 75.25 C ANISOU 5117 C1 OLC A 406 9748 9477 9366 117 717 60 C HETATM 5118 C22 OLC A 406 -5.285 18.744 55.212 1.00 72.32 C ANISOU 5118 C22 OLC A 406 9394 9178 8908 224 779 99 C HETATM 5119 O19 OLC A 406 -3.940 18.772 50.784 1.00 78.66 O ANISOU 5119 O19 OLC A 406 10186 9873 9829 90 730 69 O HETATM 5120 O25 OLC A 406 -6.921 17.075 55.887 1.00 68.86 O ANISOU 5120 O25 OLC A 406 8981 8699 8483 247 882 161 O HETATM 5121 O23 OLC A 406 -4.228 17.964 55.769 1.00 70.61 O ANISOU 5121 O23 OLC A 406 9182 8993 8654 270 793 132 O HETATM 5122 O20 OLC A 406 -4.530 18.755 52.932 1.00 66.84 O ANISOU 5122 O20 OLC A 406 8693 8427 8278 152 751 82 O HETATM 5123 C10 OLC A 407 15.802 39.412 28.053 1.00 44.37 C ANISOU 5123 C10 OLC A 407 5404 4977 6476 -252 840 264 C HETATM 5124 C9 OLC A 407 14.785 40.140 28.435 1.00 43.90 C ANISOU 5124 C9 OLC A 407 5357 4896 6428 -255 835 246 C HETATM 5125 C11 OLC A 407 16.686 38.588 28.937 1.00 38.88 C ANISOU 5125 C11 OLC A 407 4683 4322 5767 -270 804 224 C HETATM 5126 C8 OLC A 407 13.942 40.969 27.515 1.00 42.25 C ANISOU 5126 C8 OLC A 407 5171 4650 6232 -231 873 293 C HETATM 5127 C12 OLC A 407 16.754 37.150 28.529 1.00 35.63 C ANISOU 5127 C12 OLC A 407 4299 3960 5279 -243 789 248 C HETATM 5128 C7 OLC A 407 12.872 41.743 28.217 1.00 38.19 C ANISOU 5128 C7 OLC A 407 4665 4114 5733 -239 862 261 C HETATM 5129 C13 OLC A 407 17.713 36.313 29.358 1.00 45.99 C ANISOU 5129 C13 OLC A 407 5584 5312 6577 -254 759 215 C HETATM 5130 C10 OLC A 408 19.707 15.280 25.315 1.00 48.52 C ANISOU 5130 C10 OLC A 408 6322 5912 6203 102 888 397 C HETATM 5131 C9 OLC A 408 20.566 14.728 24.499 1.00 45.48 C ANISOU 5131 C9 OLC A 408 5943 5526 5812 125 919 419 C HETATM 5132 C11 OLC A 408 19.969 15.610 26.751 1.00 47.16 C ANISOU 5132 C11 OLC A 408 6117 5754 6046 97 863 394 C HETATM 5133 C8 OLC A 408 20.324 14.379 23.064 1.00 54.44 C ANISOU 5133 C8 OLC A 408 7110 6650 6926 134 944 419 C HETATM 5134 C12 OLC A 408 19.765 17.057 27.073 1.00 40.47 C ANISOU 5134 C12 OLC A 408 5238 4914 5224 71 831 383 C HETATM 5135 C7 OLC A 408 21.304 15.009 22.124 1.00 55.23 C ANISOU 5135 C7 OLC A 408 7190 6758 7037 146 959 450 C HETATM 5136 C13 OLC A 408 20.126 17.436 28.498 1.00 39.90 C ANISOU 5136 C13 OLC A 408 5131 4863 5166 67 804 374 C HETATM 5137 C6 OLC A 408 21.098 14.630 20.663 1.00 54.11 C ANISOU 5137 C6 OLC A 408 7081 6612 6867 161 985 451 C HETATM 5138 C14 OLC A 408 21.571 17.189 28.855 1.00 43.35 C ANISOU 5138 C14 OLC A 408 5533 5323 5613 89 812 397 C HETATM 5139 C5 OLC A 408 22.116 15.221 19.719 1.00 52.02 C ANISOU 5139 C5 OLC A 408 6797 6356 6611 179 1007 487 C HETATM 5140 C10 OLC A 409 24.292 22.414 45.896 1.00 66.68 C ANISOU 5140 C10 OLC A 409 8005 8894 8437 170 348 4 C HETATM 5141 C9 OLC A 409 24.067 21.528 46.834 1.00 70.49 C ANISOU 5141 C9 OLC A 409 8504 9425 8854 224 348 24 C HETATM 5142 C11 OLC A 409 24.255 22.221 44.412 1.00 67.88 C ANISOU 5142 C11 OLC A 409 8188 8972 8631 144 389 45 C HETATM 5143 C8 OLC A 409 24.173 21.847 48.293 1.00 58.53 C ANISOU 5143 C8 OLC A 409 6953 7991 7296 251 304 -22 C HETATM 5144 C12 OLC A 409 24.591 23.470 43.654 1.00 52.23 C ANISOU 5144 C12 OLC A 409 6173 6951 6721 87 382 13 C HETATM 5145 C7 OLC A 409 23.837 20.712 49.206 1.00 53.00 C ANISOU 5145 C7 OLC A 409 6281 7337 6519 319 316 16 C HETATM 5146 C13 OLC A 409 24.581 23.313 42.143 1.00 46.43 C ANISOU 5146 C13 OLC A 409 5469 6148 6025 66 423 56 C HETATM 5147 C6 OLC A 409 23.861 21.109 50.675 1.00 50.66 C ANISOU 5147 C6 OLC A 409 5950 7126 6174 348 271 -32 C HETATM 5148 C5 OLC A 409 23.310 20.076 51.621 1.00 52.49 C ANISOU 5148 C5 OLC A 409 6218 7397 6329 416 287 7 C HETATM 5149 C4 OLC A 409 23.160 20.577 53.034 1.00 48.51 C ANISOU 5149 C4 OLC A 409 5684 6973 5775 443 243 -44 C HETATM 5150 C3 OLC A 409 22.553 19.572 53.993 1.00 58.09 C ANISOU 5150 C3 OLC A 409 6935 8224 6911 514 264 0 C HETATM 5151 C2 OLC A 409 22.414 20.120 55.378 1.00 61.10 C ANISOU 5151 C2 OLC A 409 7286 8689 7238 542 220 -54 C HETATM 5152 C1 PLM A 410 12.613 2.013 53.832 1.00 49.12 C ANISOU 5152 C1 PLM A 410 6567 6327 5767 940 1302 883 C HETATM 5153 O2 PLM A 410 12.452 1.037 54.612 1.00 66.02 O ANISOU 5153 O2 PLM A 410 8732 8463 7891 1008 1372 949 O HETATM 5154 C2 PLM A 410 13.989 2.111 53.103 1.00 47.73 C ANISOU 5154 C2 PLM A 410 6368 6179 5591 943 1269 878 C HETATM 5155 C3 PLM A 410 13.918 2.637 51.682 1.00 52.81 C ANISOU 5155 C3 PLM A 410 7009 6767 6290 853 1235 819 C HETATM 5156 C4 PLM A 410 15.278 2.815 50.993 1.00 45.79 C ANISOU 5156 C4 PLM A 410 6092 5908 5398 856 1202 813 C HETATM 5157 C5 PLM A 410 15.153 3.433 49.591 1.00 43.12 C ANISOU 5157 C5 PLM A 410 5752 5520 5112 769 1168 755 C HETATM 5158 C6 PLM A 410 16.483 3.687 48.871 1.00 57.13 C ANISOU 5158 C6 PLM A 410 7497 7323 6887 768 1135 748 C HETATM 5159 C7 PLM A 410 16.479 3.194 47.410 1.00 52.31 C ANISOU 5159 C7 PLM A 410 6914 6630 6333 721 1166 739 C HETATM 5160 C8 PLM A 410 17.355 4.017 46.453 1.00 54.75 C ANISOU 5160 C8 PLM A 410 7190 6958 6654 683 1112 703 C HETATM 5161 C9 PLM A 410 17.813 3.229 45.227 1.00 40.41 C ANISOU 5161 C9 PLM A 410 5397 5082 4874 673 1154 717 C HETATM 5162 CA PLM A 410 18.585 4.068 44.198 1.00 46.67 C ANISOU 5162 CA PLM A 410 6161 5889 5684 632 1105 681 C HETATM 5163 CB PLM A 410 17.680 4.830 43.231 1.00 56.12 C ANISOU 5163 CB PLM A 410 7368 7039 6917 551 1078 624 C HETATM 5164 CC PLM A 410 18.428 5.462 42.047 1.00 52.19 C ANISOU 5164 CC PLM A 410 6849 6540 6440 515 1047 599 C HETATM 5165 CD PLM A 410 17.507 6.216 41.072 1.00 50.54 C ANISOU 5165 CD PLM A 410 6651 6290 6264 441 1022 547 C HETATM 5166 CE PLM A 410 18.149 7.461 40.441 1.00 43.42 C ANISOU 5166 CE PLM A 410 5711 5417 5370 407 966 516 C HETATM 5167 CF PLM A 410 19.105 7.144 39.278 1.00 49.06 C ANISOU 5167 CF PLM A 410 6425 6115 6101 408 983 529 C HETATM 5168 CG PLM A 410 19.582 8.393 38.520 1.00 35.88 C ANISOU 5168 CG PLM A 410 4722 4464 4448 369 935 498 C HETATM 5169 C8 OLC A 411 24.834 35.012 44.538 1.00 68.75 C ANISOU 5169 C8 OLC A 411 7957 8822 9341 -322 268 -483 C HETATM 5170 C7 OLC A 411 24.840 35.185 46.025 1.00 64.62 C ANISOU 5170 C7 OLC A 411 7402 8371 8780 -312 216 -560 C HETATM 5171 C6 OLC A 411 25.423 34.001 46.784 1.00 62.93 C ANISOU 5171 C6 OLC A 411 7173 8256 8483 -259 185 -550 C HETATM 5172 C5 OLC A 411 25.363 34.126 48.287 1.00 68.03 C ANISOU 5172 C5 OLC A 411 7791 8981 9078 -240 133 -623 C HETATM 5173 C4 OLC A 411 26.155 35.276 48.858 1.00 69.30 C ANISOU 5173 C4 OLC A 411 7871 9161 9299 -283 103 -719 C HETATM 5174 C3 OLC A 411 26.226 35.270 50.375 1.00 62.39 C ANISOU 5174 C3 OLC A 411 6962 8381 8361 -256 47 -793 C HETATM 5175 C2 OLC A 411 24.878 35.384 51.014 1.00 67.66 C ANISOU 5175 C2 OLC A 411 7686 9040 8983 -242 40 -806 C HETATM 5176 C1 OLC A 411 24.863 34.937 52.447 1.00 68.41 C ANISOU 5176 C1 OLC A 411 7765 9242 8986 -192 -8 -848 C HETATM 5177 O19 OLC A 411 23.909 34.037 52.664 1.00 77.57 O ANISOU 5177 O19 OLC A 411 8992 10412 10068 -144 2 -791 O HETATM 5178 O20 OLC A 411 25.606 35.331 53.308 1.00 68.81 O ANISOU 5178 O20 OLC A 411 7749 9363 9031 -194 -51 -926 O HETATM 5179 C18 OLC A 412 -7.379 25.193 37.222 1.00 51.96 C ANISOU 5179 C18 OLC A 412 6720 6348 6674 -186 542 -64 C HETATM 5180 C10 OLC A 412 -6.160 26.183 46.418 1.00 55.89 C ANISOU 5180 C10 OLC A 412 7223 6912 7100 -87 544 -104 C HETATM 5181 C9 OLC A 412 -6.781 25.324 47.189 1.00 62.39 C ANISOU 5181 C9 OLC A 412 8056 7745 7906 -72 569 -93 C HETATM 5182 C17 OLC A 412 -6.704 26.286 38.013 1.00 53.99 C ANISOU 5182 C17 OLC A 412 6974 6601 6940 -176 530 -61 C HETATM 5183 C11 OLC A 412 -5.787 25.952 44.985 1.00 56.71 C ANISOU 5183 C11 OLC A 412 7327 6996 7223 -107 543 -91 C HETATM 5184 C8 OLC A 412 -7.128 25.487 48.638 1.00 60.37 C ANISOU 5184 C8 OLC A 412 7801 7512 7624 -46 573 -101 C HETATM 5185 C24 OLC A 412 -5.867 27.180 58.297 1.00 61.85 C ANISOU 5185 C24 OLC A 412 7975 8004 7523 213 531 -212 C HETATM 5186 C16 OLC A 412 -7.040 26.302 39.483 1.00 49.33 C ANISOU 5186 C16 OLC A 412 6383 6013 6346 -170 534 -71 C HETATM 5187 C12 OLC A 412 -6.465 26.896 44.038 1.00 58.78 C ANISOU 5187 C12 OLC A 412 7581 7242 7510 -125 531 -100 C HETATM 5188 C7 OLC A 412 -7.856 24.302 49.203 1.00 52.65 C ANISOU 5188 C7 OLC A 412 6836 6536 6633 -32 611 -79 C HETATM 5189 C15 OLC A 412 -6.462 27.507 40.183 1.00 54.82 C ANISOU 5189 C15 OLC A 412 7072 6708 7051 -161 519 -77 C HETATM 5190 C13 OLC A 412 -6.163 26.655 42.567 1.00 56.48 C ANISOU 5190 C13 OLC A 412 7290 6936 7232 -141 531 -87 C HETATM 5191 C6 OLC A 412 -8.182 24.386 50.690 1.00 52.06 C ANISOU 5191 C6 OLC A 412 6763 6490 6528 1 620 -81 C HETATM 5192 C14 OLC A 412 -6.835 27.640 41.640 1.00 53.94 C ANISOU 5192 C14 OLC A 412 6960 6604 6931 -151 520 -91 C HETATM 5193 C5 OLC A 412 -7.109 23.849 51.612 1.00 58.72 C ANISOU 5193 C5 OLC A 412 7612 7366 7333 36 623 -69 C HETATM 5194 C4 OLC A 412 -7.438 23.967 53.085 1.00 52.45 C ANISOU 5194 C4 OLC A 412 6821 6606 6502 74 632 -72 C HETATM 5195 C3 OLC A 412 -6.341 23.469 54.012 1.00 53.86 C ANISOU 5195 C3 OLC A 412 7002 6827 6636 116 632 -60 C HETATM 5196 C2 OLC A 412 -6.595 23.795 55.455 1.00 51.86 C ANISOU 5196 C2 OLC A 412 6749 6617 6340 157 632 -71 C HETATM 5197 C21 OLC A 412 -6.539 24.760 57.985 1.00 53.90 C ANISOU 5197 C21 OLC A 412 6999 6969 6510 233 612 -110 C HETATM 5198 C1 OLC A 412 -5.428 23.456 56.345 1.00 59.01 C ANISOU 5198 C1 OLC A 412 7651 7573 7195 201 624 -64 C HETATM 5199 C22 OLC A 412 -6.203 25.862 58.965 1.00 53.39 C ANISOU 5199 C22 OLC A 412 6921 6952 6412 255 575 -160 C HETATM 5200 O19 OLC A 412 -4.683 22.529 56.162 1.00 70.29 O ANISOU 5200 O19 OLC A 412 9086 9006 8616 214 639 -33 O HETATM 5201 O25 OLC A 412 -5.650 28.216 59.251 1.00 58.30 O ANISOU 5201 O25 OLC A 412 7512 7594 7047 231 501 -265 O HETATM 5202 O23 OLC A 412 -7.278 26.032 59.888 1.00 53.23 O ANISOU 5202 O23 OLC A 412 6909 6946 6369 281 595 -162 O HETATM 5203 O20 OLC A 412 -5.315 24.287 57.380 1.00 60.31 O ANISOU 5203 O20 OLC A 412 7806 7782 7326 227 600 -98 O HETATM 5204 C8 OLC A 413 -5.988 22.431 30.773 1.00 55.36 C ANISOU 5204 C8 OLC A 413 7173 6809 7051 -197 554 -61 C HETATM 5205 C7 OLC A 413 -5.831 22.865 29.350 1.00 45.76 C ANISOU 5205 C7 OLC A 413 5954 5614 5817 -184 544 -54 C HETATM 5206 C6 OLC A 413 -5.214 21.810 28.441 1.00 47.01 C ANISOU 5206 C6 OLC A 413 6126 5775 5961 -185 557 -60 C HETATM 5207 C5 OLC A 413 -5.173 22.204 26.986 1.00 57.25 C ANISOU 5207 C5 OLC A 413 7419 7099 7233 -168 547 -55 C HETATM 5208 C4 OLC A 413 -4.633 21.136 26.066 1.00 53.69 C ANISOU 5208 C4 OLC A 413 6982 6653 6764 -168 560 -67 C HETATM 5209 C3 OLC A 413 -4.618 21.533 24.600 1.00 52.18 C ANISOU 5209 C3 OLC A 413 6787 6496 6542 -145 550 -61 C HETATM 5210 C2 OLC A 413 -5.989 21.806 24.068 1.00 60.44 C ANISOU 5210 C2 OLC A 413 7814 7580 7570 -143 530 -87 C HETATM 5211 C1 OLC A 413 -5.986 22.395 22.686 1.00 61.26 C ANISOU 5211 C1 OLC A 413 7912 7724 7639 -112 519 -74 C HETATM 5212 O19 OLC A 413 -5.344 21.614 21.825 1.00 61.98 O ANISOU 5212 O19 OLC A 413 8017 7824 7709 -107 529 -82 O HETATM 5213 O20 OLC A 413 -6.490 23.445 22.377 1.00 60.13 O ANISOU 5213 O20 OLC A 413 7756 7605 7488 -91 505 -56 O HETATM 5214 C18 OLC A 414 -8.714 40.445 42.390 1.00 46.02 C ANISOU 5214 C18 OLC A 414 5883 5406 6198 -118 514 -194 C HETATM 5215 C10 OLC A 414 -10.172 41.718 50.288 1.00 56.51 C ANISOU 5215 C10 OLC A 414 7217 6812 7444 -75 480 -442 C HETATM 5216 C9 OLC A 414 -10.298 42.312 51.448 1.00 48.49 C ANISOU 5216 C9 OLC A 414 6200 5802 6421 -64 477 -491 C HETATM 5217 C17 OLC A 414 -9.317 39.944 43.681 1.00 53.32 C ANISOU 5217 C17 OLC A 414 6811 6359 7089 -114 503 -224 C HETATM 5218 C11 OLC A 414 -11.110 41.820 49.125 1.00 39.20 C ANISOU 5218 C11 OLC A 414 5028 4596 5271 -72 497 -394 C HETATM 5219 C8 OLC A 414 -9.379 42.088 52.607 1.00 42.06 C ANISOU 5219 C8 OLC A 414 5380 5024 5577 -62 455 -539 C HETATM 5220 C24 OLC A 414 -3.517 35.841 60.266 1.00 68.91 C ANISOU 5220 C24 OLC A 414 8740 8930 8511 128 313 -648 C HETATM 5221 C16 OLC A 414 -8.327 39.818 44.810 1.00 36.38 C ANISOU 5221 C16 OLC A 414 4663 4223 4937 -124 489 -264 C HETATM 5222 C12 OLC A 414 -11.604 40.491 48.642 1.00 35.06 C ANISOU 5222 C12 OLC A 414 4509 4102 4710 -68 497 -351 C HETATM 5223 C7 OLC A 414 -10.084 41.708 53.870 1.00 36.20 C ANISOU 5223 C7 OLC A 414 4646 4324 4783 -34 454 -558 C HETATM 5224 C15 OLC A 414 -8.903 39.281 46.098 1.00 45.76 C ANISOU 5224 C15 OLC A 414 5856 5443 6086 -113 481 -289 C HETATM 5225 C13 OLC A 414 -10.534 39.613 48.013 1.00 37.32 C ANISOU 5225 C13 OLC A 414 4794 4399 4987 -85 486 -331 C HETATM 5226 C6 OLC A 414 -9.188 41.018 54.890 1.00 42.40 C ANISOU 5226 C6 OLC A 414 5428 5164 5519 -24 432 -586 C HETATM 5227 C14 OLC A 414 -9.964 40.155 46.723 1.00 40.62 C ANISOU 5227 C14 OLC A 414 5206 4782 5445 -99 491 -309 C HETATM 5228 C5 OLC A 414 -7.827 41.648 55.044 1.00 55.82 C ANISOU 5228 C5 OLC A 414 7108 6859 7242 -43 411 -636 C HETATM 5229 C4 OLC A 414 -6.951 40.988 56.078 1.00 43.26 C ANISOU 5229 C4 OLC A 414 5509 5330 5598 -28 386 -665 C HETATM 5230 C3 OLC A 414 -5.535 41.537 56.134 1.00 60.44 C ANISOU 5230 C3 OLC A 414 7659 7505 7799 -50 363 -715 C HETATM 5231 C2 OLC A 414 -4.760 41.015 57.305 1.00 65.70 C ANISOU 5231 C2 OLC A 414 8314 8242 8407 -28 336 -752 C HETATM 5232 C21 OLC A 414 -3.951 37.643 58.538 1.00 61.31 C ANISOU 5232 C21 OLC A 414 7772 7842 7682 48 320 -671 C HETATM 5233 C1 OLC A 414 -4.501 39.536 57.245 1.00 72.77 C ANISOU 5233 C1 OLC A 414 9218 9182 9250 -9 334 -698 C HETATM 5234 C22 OLC A 414 -3.461 37.318 59.931 1.00 65.34 C ANISOU 5234 C22 OLC A 414 8273 8431 8122 89 300 -707 C HETATM 5235 O19 OLC A 414 -4.691 38.834 56.288 1.00 69.20 O ANISOU 5235 O19 OLC A 414 8776 8708 8807 -18 349 -637 O HETATM 5236 O25 OLC A 414 -2.723 35.064 59.373 1.00 76.17 O ANISOU 5236 O25 OLC A 414 9655 9840 9445 112 313 -605 O HETATM 5237 O23 OLC A 414 -2.133 37.814 60.093 1.00 64.22 O ANISOU 5237 O23 OLC A 414 8099 8311 7992 75 266 -762 O HETATM 5238 O20 OLC A 414 -4.035 39.079 58.404 1.00 73.71 O ANISOU 5238 O20 OLC A 414 9330 9368 9308 21 315 -726 O HETATM 5239 C10 OLC A 415 -6.507 34.602 29.022 1.00 53.74 C ANISOU 5239 C10 OLC A 415 6890 6554 6976 -46 538 126 C HETATM 5240 C9 OLC A 415 -6.347 34.548 27.725 1.00 51.66 C ANISOU 5240 C9 OLC A 415 6628 6311 6690 -24 545 154 C HETATM 5241 C11 OLC A 415 -6.124 33.538 30.004 1.00 47.68 C ANISOU 5241 C11 OLC A 415 6129 5784 6204 -77 527 92 C HETATM 5242 C8 OLC A 415 -6.824 35.573 26.742 1.00 40.63 C ANISOU 5242 C8 OLC A 415 5224 4922 5290 14 558 192 C HETATM 5243 C12 OLC A 415 -6.372 33.939 31.425 1.00 48.82 C ANISOU 5243 C12 OLC A 415 6269 5908 6373 -92 522 68 C HETATM 5244 C7 OLC A 415 -6.484 35.233 25.325 1.00 38.80 C ANISOU 5244 C7 OLC A 415 4997 4721 5025 40 564 220 C HETATM 5245 C13 OLC A 415 -6.040 32.866 32.448 1.00 43.42 C ANISOU 5245 C13 OLC A 415 5592 5226 5681 -116 514 39 C HETATM 5246 C6 OLC A 415 -7.166 36.109 24.283 1.00 39.93 C ANISOU 5246 C6 OLC A 415 5132 4888 5151 86 574 258 C HETATM 5247 C14 OLC A 415 -6.233 33.295 33.881 1.00 38.17 C ANISOU 5247 C14 OLC A 415 4923 4545 5034 -126 509 14 C HETATM 5248 C5 OLC A 415 -6.898 35.683 22.862 1.00 35.48 C ANISOU 5248 C5 OLC A 415 4572 4364 4543 116 578 283 C HETATM 5249 C4 OLC A 415 -7.676 36.455 21.827 1.00 51.72 C ANISOU 5249 C4 OLC A 415 6621 6458 6574 168 586 321 C HETATM 5250 C3 OLC A 415 -7.413 36.013 20.398 1.00 42.34 C ANISOU 5250 C3 OLC A 415 5436 5317 5333 202 589 344 C HETATM 5251 C2 OLC A 415 -8.204 36.797 19.397 1.00 59.21 C ANISOU 5251 C2 OLC A 415 7563 7496 7438 261 596 384 C HETATM 5252 C ACE B 401 -13.332 21.999 70.887 1.00 26.65 C ANISOU 5252 C ACE B 401 3663 3912 2551 825 993 122 C HETATM 5253 O ACE B 401 -12.321 22.201 70.216 1.00 31.71 O ANISOU 5253 O ACE B 401 4293 4551 3204 794 944 93 O HETATM 5254 CH3 ACE B 401 -13.303 21.158 72.128 1.00 38.96 C ANISOU 5254 CH3 ACE B 401 5238 5530 4037 915 1047 182 C HETATM 5255 C1 RET B 402 -19.982 24.736 44.668 1.00 26.75 C ANISOU 5255 C1 RET B 402 3409 3204 3549 -187 673 -149 C HETATM 5256 C2 RET B 402 -19.283 24.113 43.458 1.00 35.25 C ANISOU 5256 C2 RET B 402 4490 4275 4628 -208 662 -154 C HETATM 5257 C3 RET B 402 -18.727 25.124 42.527 1.00 37.44 C ANISOU 5257 C3 RET B 402 4767 4562 4895 -202 624 -155 C HETATM 5258 C4 RET B 402 -19.863 25.973 41.977 1.00 29.81 C ANISOU 5258 C4 RET B 402 3772 3615 3937 -200 607 -165 C HETATM 5259 C5 RET B 402 -20.825 26.441 43.032 1.00 16.90 C ANISOU 5259 C5 RET B 402 2128 1986 2308 -186 620 -165 C HETATM 5260 C6 RET B 402 -20.752 25.994 44.307 1.00 28.17 C ANISOU 5260 C6 RET B 402 3569 3402 3732 -179 648 -158 C HETATM 5261 C7 RET B 402 -21.422 26.640 45.420 1.00 21.29 C ANISOU 5261 C7 RET B 402 2694 2535 2859 -158 658 -156 C HETATM 5262 C8 RET B 402 -21.663 27.970 45.599 1.00 26.64 C ANISOU 5262 C8 RET B 402 3368 3220 3533 -138 640 -158 C HETATM 5263 C9 RET B 402 -21.915 28.631 46.799 1.00 17.16 C ANISOU 5263 C9 RET B 402 2174 2021 2324 -114 650 -157 C HETATM 5264 C10 RET B 402 -22.027 30.029 46.839 1.00 17.16 C ANISOU 5264 C10 RET B 402 2172 2024 2325 -95 631 -163 C HETATM 5265 C11 RET B 402 -21.636 30.894 47.840 1.00 17.20 C ANISOU 5265 C11 RET B 402 2192 2024 2317 -71 629 -168 C HETATM 5266 C12 RET B 402 -21.707 32.272 47.819 1.00 17.24 C ANISOU 5266 C12 RET B 402 2197 2026 2329 -55 613 -176 C HETATM 5267 C13 RET B 402 -20.881 33.192 48.482 1.00 17.25 C ANISOU 5267 C13 RET B 402 2215 2016 2322 -39 604 -188 C HETATM 5268 C14 RET B 402 -21.114 34.566 48.454 1.00 24.13 C ANISOU 5268 C14 RET B 402 3083 2877 3207 -24 595 -198 C HETATM 5269 C15 RET B 402 -20.272 35.516 49.016 1.00 25.76 C ANISOU 5269 C15 RET B 402 3305 3070 3413 -12 585 -216 C HETATM 5270 C16 RET B 402 -20.926 23.685 45.271 1.00 28.65 C ANISOU 5270 C16 RET B 402 3639 3438 3808 -198 714 -149 C HETATM 5271 C17 RET B 402 -18.904 25.071 45.712 1.00 28.28 C ANISOU 5271 C17 RET B 402 3632 3394 3720 -162 673 -136 C HETATM 5272 C18 RET B 402 -21.835 27.420 42.497 1.00 21.89 C ANISOU 5272 C18 RET B 402 2733 2638 2946 -178 602 -171 C HETATM 5273 C19 RET B 402 -22.079 27.892 48.076 1.00 23.25 C ANISOU 5273 C19 RET B 402 2955 2791 3087 -104 683 -150 C HETATM 5274 C20 RET B 402 -19.705 32.644 49.200 1.00 19.36 C ANISOU 5274 C20 RET B 402 2504 2283 2568 -38 603 -193 C HETATM 5275 C1 NAG B 403 -9.390 22.856 68.224 1.00 35.33 C ANISOU 5275 C1 NAG B 403 4716 5002 3706 703 806 10 C HETATM 5276 C2 NAG B 403 -9.705 21.454 67.729 1.00 24.05 C ANISOU 5276 C2 NAG B 403 3304 3522 2311 700 871 88 C HETATM 5277 C3 NAG B 403 -8.751 20.457 68.373 1.00 32.00 C ANISOU 5277 C3 NAG B 403 4319 4582 3260 767 892 138 C HETATM 5278 C4 NAG B 403 -7.309 20.848 68.074 1.00 37.96 C ANISOU 5278 C4 NAG B 403 5054 5373 3996 760 828 98 C HETATM 5279 C5 NAG B 403 -7.047 22.294 68.498 1.00 38.71 C ANISOU 5279 C5 NAG B 403 5128 5516 4063 754 759 14 C HETATM 5280 C6 NAG B 403 -5.691 22.797 68.060 1.00 36.80 C ANISOU 5280 C6 NAG B 403 4862 5299 3820 733 695 -33 C HETATM 5281 C7 NAG B 403 -11.905 20.590 67.065 1.00 40.58 C ANISOU 5281 C7 NAG B 403 5415 5504 4499 652 968 150 C HETATM 5282 C8 NAG B 403 -13.301 20.275 67.513 1.00 28.47 C ANISOU 5282 C8 NAG B 403 3890 3947 2981 663 1029 182 C HETATM 5283 N2 NAG B 403 -11.088 21.093 67.997 1.00 34.41 N ANISOU 5283 N2 NAG B 403 4630 4801 3644 704 931 124 N HETATM 5284 O3 NAG B 403 -9.019 19.148 67.885 1.00 26.75 O ANISOU 5284 O3 NAG B 403 3670 3862 2633 762 957 209 O HETATM 5285 O4 NAG B 403 -6.418 19.987 68.775 1.00 43.87 O ANISOU 5285 O4 NAG B 403 5806 6182 4680 831 845 143 O HETATM 5286 O5 NAG B 403 -8.020 23.180 67.916 1.00 33.73 O ANISOU 5286 O5 NAG B 403 4496 4829 3492 693 749 -26 O HETATM 5287 O6 NAG B 403 -5.394 22.401 66.727 1.00 35.26 O ANISOU 5287 O6 NAG B 403 4667 5036 3694 675 697 -15 O HETATM 5288 O7 NAG B 403 -11.534 20.397 65.910 1.00 33.96 O ANISOU 5288 O7 NAG B 403 4572 4619 3714 598 953 145 O HETATM 5289 C10 OLC B 404 -34.293 33.981 30.798 1.00 52.28 C ANISOU 5289 C10 OLC B 404 6061 7140 6664 95 337 -192 C HETATM 5290 C9 OLC B 404 -33.185 34.282 30.176 1.00 44.98 C ANISOU 5290 C9 OLC B 404 5175 6198 5717 111 333 -167 C HETATM 5291 C11 OLC B 404 -34.466 33.616 32.240 1.00 42.07 C ANISOU 5291 C11 OLC B 404 4780 5790 5415 57 367 -204 C HETATM 5292 C8 OLC B 404 -33.152 34.931 28.828 1.00 58.20 C ANISOU 5292 C8 OLC B 404 6837 7932 7346 165 310 -141 C HETATM 5293 C12 OLC B 404 -35.336 34.594 32.968 1.00 47.19 C ANISOU 5293 C12 OLC B 404 5413 6437 6078 91 383 -179 C HETATM 5294 C7 OLC B 404 -33.683 34.074 27.718 1.00 64.99 C ANISOU 5294 C7 OLC B 404 7649 8873 8173 157 274 -184 C HETATM 5295 C15 OLC B 404 -37.127 34.738 36.421 1.00 41.62 C ANISOU 5295 C15 OLC B 404 4693 5658 5462 66 460 -185 C HETATM 5296 C13 OLC B 404 -35.735 34.181 34.374 1.00 41.17 C ANISOU 5296 C13 OLC B 404 4654 5633 5356 58 413 -194 C HETATM 5297 C6 OLC B 404 -34.046 34.849 26.457 1.00 57.39 C ANISOU 5297 C6 OLC B 404 6657 7988 7159 224 250 -156 C HETATM 5298 C14 OLC B 404 -36.649 35.169 35.058 1.00 48.77 C ANISOU 5298 C14 OLC B 404 5599 6599 6332 95 429 -170 C HETATM 5299 C5 OLC B 404 -34.102 34.018 25.198 1.00 54.42 C ANISOU 5299 C5 OLC B 404 6250 7688 6739 219 214 -197 C HETATM 5300 C4 OLC B 404 -34.742 34.716 24.021 1.00 55.22 C ANISOU 5300 C4 OLC B 404 6311 7885 6786 289 187 -174 C HETATM 5301 C3 OLC B 404 -34.282 36.149 23.813 1.00 55.41 C ANISOU 5301 C3 OLC B 404 6368 7889 6795 360 207 -93 C HETATM 5302 C2 OLC B 404 -34.953 36.814 22.646 1.00 59.16 C ANISOU 5302 C2 OLC B 404 6802 8463 7214 436 183 -66 C HETATM 5303 C21 OLC B 404 -35.993 38.047 20.608 1.00 54.00 C ANISOU 5303 C21 OLC B 404 6081 7984 6453 582 146 -7 C HETATM 5304 C1 OLC B 404 -34.698 38.299 22.584 1.00 61.74 C ANISOU 5304 C1 OLC B 404 7157 8765 7537 508 212 18 C HETATM 5305 C22 OLC B 404 -36.469 38.898 19.453 1.00 46.58 C ANISOU 5305 C22 OLC B 404 5110 7140 5449 678 132 41 C HETATM 5306 O19 OLC B 404 -34.108 38.918 23.430 1.00 68.66 O ANISOU 5306 O19 OLC B 404 8080 9551 8456 502 248 53 O HETATM 5307 O20 OLC B 404 -35.198 38.870 21.488 1.00 63.91 O ANISOU 5307 O20 OLC B 404 7398 9127 7756 582 194 48 O HETATM 5308 C10 OLC B 405 -4.556 38.255 41.262 1.00 61.68 C ANISOU 5308 C10 OLC B 405 7857 7414 8164 -163 490 -171 C HETATM 5309 C9 OLC B 405 -4.567 36.960 41.450 1.00 56.09 C ANISOU 5309 C9 OLC B 405 7158 6740 7414 -162 480 -165 C HETATM 5310 C11 OLC B 405 -4.583 38.949 39.936 1.00 62.78 C ANISOU 5310 C11 OLC B 405 7996 7524 8336 -160 509 -136 C HETATM 5311 C8 OLC B 405 -4.495 36.276 42.781 1.00 57.96 C ANISOU 5311 C8 OLC B 405 7396 7008 7618 -159 467 -194 C HETATM 5312 C24 OLC B 405 -7.758 31.780 52.745 1.00 45.98 C ANISOU 5312 C24 OLC B 405 5931 5749 5790 0 476 -288 C HETATM 5313 C7 OLC B 405 -5.685 35.417 43.076 1.00 57.67 C ANISOU 5313 C7 OLC B 405 7373 6995 7544 -148 468 -185 C HETATM 5314 C6 OLC B 405 -5.658 34.774 44.456 1.00 57.46 C ANISOU 5314 C6 OLC B 405 7349 6998 7484 -140 460 -209 C HETATM 5315 C5 OLC B 405 -6.900 33.991 44.809 1.00 47.87 C ANISOU 5315 C5 OLC B 405 6146 5802 6240 -129 469 -200 C HETATM 5316 C4 OLC B 405 -6.930 33.508 46.239 1.00 47.94 C ANISOU 5316 C4 OLC B 405 6158 5839 6216 -115 466 -221 C HETATM 5317 C3 OLC B 405 -8.252 32.895 46.669 1.00 44.15 C ANISOU 5317 C3 OLC B 405 5687 5373 5714 -104 479 -212 C HETATM 5318 C2 OLC B 405 -8.352 32.733 48.157 1.00 48.90 C ANISOU 5318 C2 OLC B 405 6291 6000 6286 -85 479 -234 C HETATM 5319 C21 OLC B 405 -7.129 30.410 50.700 1.00 45.41 C ANISOU 5319 C21 OLC B 405 5865 5644 5745 -33 488 -228 C HETATM 5320 C1 OLC B 405 -7.520 31.608 48.709 1.00 45.91 C ANISOU 5320 C1 OLC B 405 5919 5649 5875 -75 480 -225 C HETATM 5321 C22 OLC B 405 -6.917 30.657 52.179 1.00 47.69 C ANISOU 5321 C22 OLC B 405 6152 5971 5998 -4 480 -255 C HETATM 5322 O19 OLC B 405 -6.954 30.778 48.047 1.00 48.82 O ANISOU 5322 O19 OLC B 405 6292 6017 6242 -82 484 -202 O HETATM 5323 O25 OLC B 405 -7.229 33.056 52.396 1.00 51.39 O ANISOU 5323 O25 OLC B 405 6602 6414 6509 -18 454 -322 O HETATM 5324 O23 OLC B 405 -7.177 29.450 52.895 1.00 50.09 O ANISOU 5324 O23 OLC B 405 6468 6300 6263 23 503 -229 O HETATM 5325 O20 OLC B 405 -7.456 31.652 50.038 1.00 45.58 O ANISOU 5325 O20 OLC B 405 5878 5636 5805 -53 477 -246 O HETATM 5326 C1 PLM B 406 -17.498 53.766 21.395 1.00 56.78 C ANISOU 5326 C1 PLM B 406 7180 6841 7554 817 1017 905 C HETATM 5327 O2 PLM B 406 -17.366 55.019 21.480 1.00 54.03 O ANISOU 5327 O2 PLM B 406 6842 6416 7273 847 1082 952 O HETATM 5328 C2 PLM B 406 -16.987 52.933 22.612 1.00 51.22 C ANISOU 5328 C2 PLM B 406 6481 6106 6875 720 975 813 C HETATM 5329 C3 PLM B 406 -16.111 53.709 23.594 1.00 47.27 C ANISOU 5329 C3 PLM B 406 5998 5489 6472 673 1016 791 C HETATM 5330 C4 PLM B 406 -15.693 52.919 24.846 1.00 51.60 C ANISOU 5330 C4 PLM B 406 6550 6018 7038 586 973 701 C HETATM 5331 C5 PLM B 406 -14.886 53.763 25.845 1.00 51.81 C ANISOU 5331 C5 PLM B 406 6591 5936 7161 542 1012 674 C HETATM 5332 C6 PLM B 406 -14.112 52.948 26.896 1.00 48.03 C ANISOU 5332 C6 PLM B 406 6116 5440 6696 460 973 594 C HETATM 5333 C10 OLC B 407 -14.672 17.961 46.711 1.00 31.94 C ANISOU 5333 C10 OLC B 407 4202 3760 4174 -160 844 -40 C HETATM 5334 C9 OLC B 407 -15.192 16.822 46.333 1.00 43.02 C ANISOU 5334 C9 OLC B 407 5603 5135 5609 -183 883 -42 C HETATM 5335 C11 OLC B 407 -13.837 18.848 45.843 1.00 35.76 C ANISOU 5335 C11 OLC B 407 4685 4258 4644 -164 794 -53 C HETATM 5336 C8 OLC B 407 -15.895 15.838 47.214 1.00 31.46 C ANISOU 5336 C8 OLC B 407 4140 3649 4164 -177 943 -23 C HETATM 5337 C12 OLC B 407 -13.355 20.081 46.538 1.00 31.70 C ANISOU 5337 C12 OLC B 407 4173 3770 4101 -138 761 -52 C HETATM 5338 C7 OLC B 407 -15.245 14.489 47.216 1.00 40.14 C ANISOU 5338 C7 OLC B 407 5260 4716 5276 -174 990 -1 C HETATM 5339 C13 OLC B 407 -12.383 20.915 45.720 1.00 31.73 C ANISOU 5339 C13 OLC B 407 4177 3782 4095 -142 717 -62 C HETATM 5340 O HOH A 501 16.468 30.038 10.758 1.00 31.29 O ANISOU 5340 O HOH A 501 4116 3742 4033 316 1113 815 O HETATM 5341 O HOH A 502 0.667 14.193 26.455 1.00 31.73 O ANISOU 5341 O HOH A 502 4320 3730 4008 -174 729 -60 O HETATM 5342 O HOH A 503 17.698 21.501 1.862 1.00 31.45 O ANISOU 5342 O HOH A 503 4374 4150 3427 649 1199 726 O HETATM 5343 O HOH A 504 13.010 14.900 62.300 1.00 41.18 O ANISOU 5343 O HOH A 504 5167 6177 4303 943 540 274 O HETATM 5344 O HOH A 505 -8.357 24.099 60.659 1.00 44.04 O ANISOU 5344 O HOH A 505 5775 5784 5174 332 683 -74 O HETATM 5345 O HOH A 506 10.898 23.038 23.158 1.00 27.42 O ANISOU 5345 O HOH A 506 3655 3223 3539 -25 733 287 O HETATM 5346 O HOH A 507 14.353 23.197 54.515 1.00 33.42 O ANISOU 5346 O HOH A 507 4026 4797 3876 308 286 -152 O HETATM 5347 O HOH A 508 5.087 34.467 20.007 1.00 20.83 O ANISOU 5347 O HOH A 508 2752 2326 2837 81 776 468 O HETATM 5348 O HOH A 509 -7.443 29.842 59.677 1.00 40.83 O ANISOU 5348 O HOH A 509 5301 5353 4860 217 501 -316 O HETATM 5349 O HOH A 510 10.943 19.874 40.163 1.00 20.92 O ANISOU 5349 O HOH A 510 2736 2551 2662 6 588 131 O HETATM 5350 O HOH A 511 5.425 17.845 4.348 1.00 31.61 O ANISOU 5350 O HOH A 511 4382 4384 3243 409 763 74 O HETATM 5351 O HOH A 512 4.134 30.343 9.955 1.00 24.46 O ANISOU 5351 O HOH A 512 3317 3197 2780 407 814 574 O HETATM 5352 O HOH A 513 2.439 26.140 15.370 1.00 31.37 O ANISOU 5352 O HOH A 513 4191 3975 3752 146 670 280 O HETATM 5353 O HOH A 514 10.163 25.001 0.586 1.00 40.79 O ANISOU 5353 O HOH A 514 5531 5574 4394 743 1014 663 O HETATM 5354 O HOH A 515 12.440 7.183 15.383 1.00 28.46 O ANISOU 5354 O HOH A 515 4112 3303 3397 99 1040 23 O HETATM 5355 O HOH A 516 19.862 24.718 6.591 1.00 27.83 O ANISOU 5355 O HOH A 516 3775 3450 3348 467 1212 834 O HETATM 5356 O HOH A 517 13.560 20.224 58.267 1.00 33.56 O ANISOU 5356 O HOH A 517 4098 5012 3644 552 343 -34 O HETATM 5357 O HOH A 518 4.913 34.356 10.059 1.00 32.76 O ANISOU 5357 O HOH A 518 4337 4132 3977 463 924 759 O HETATM 5358 O HOH A 519 -2.786 30.232 19.627 1.00 26.38 O ANISOU 5358 O HOH A 519 3482 3294 3248 90 584 244 O HETATM 5359 O HOH A 520 5.925 18.696 27.920 1.00 22.77 O ANISOU 5359 O HOH A 520 3129 2619 2904 -101 685 118 O HETATM 5360 O HOH A 521 5.485 19.315 51.314 1.00 25.94 O ANISOU 5360 O HOH A 521 3403 3423 3030 217 576 75 O HETATM 5361 O HOH A 522 14.123 25.609 16.984 1.00 21.48 O ANISOU 5361 O HOH A 522 2892 2492 2778 108 879 495 O HETATM 5362 O HOH A 523 13.450 20.332 20.780 1.00 21.77 O ANISOU 5362 O HOH A 523 2980 2525 2766 35 811 330 O HETATM 5363 O HOH A 524 17.359 25.032 17.013 1.00 18.48 O ANISOU 5363 O HOH A 524 2476 2088 2457 114 936 548 O HETATM 5364 O HOH A 525 20.952 12.574 8.611 1.00 31.32 O ANISOU 5364 O HOH A 525 4406 3858 3637 396 1183 443 O HETATM 5365 O HOH A 526 11.959 25.647 15.457 1.00 19.31 O ANISOU 5365 O HOH A 526 2655 2272 2411 148 861 480 O HETATM 5366 O HOH A 527 1.053 23.666 18.478 1.00 30.00 O ANISOU 5366 O HOH A 527 4020 3750 3629 25 620 138 O HETATM 5367 O HOH A 528 7.428 22.628 38.553 1.00 32.77 O ANISOU 5367 O HOH A 528 4258 3970 4222 -85 559 70 O HETATM 5368 O HOH A 529 1.765 20.442 9.046 1.00 31.34 O ANISOU 5368 O HOH A 529 4258 4245 3405 256 654 70 O HETATM 5369 O HOH A 530 18.558 23.532 54.302 1.00 29.59 O ANISOU 5369 O HOH A 530 3383 4451 3408 323 209 -198 O HETATM 5370 O HOH A 531 -0.777 26.957 20.218 1.00 18.39 O ANISOU 5370 O HOH A 531 2505 2253 2230 23 590 178 O HETATM 5371 O HOH A 532 17.178 3.237 19.082 1.00 25.44 O ANISOU 5371 O HOH A 532 3768 2757 3142 190 1230 191 O HETATM 5372 O HOH A 533 8.614 24.247 14.322 1.00 18.42 O ANISOU 5372 O HOH A 533 2588 2254 2158 167 798 381 O HETATM 5373 O HOH A 534 -3.683 40.492 14.080 1.00 43.06 O ANISOU 5373 O HOH A 534 5560 5392 5410 500 835 746 O HETATM 5374 O HOH A 535 9.442 20.576 56.925 1.00 32.83 O ANISOU 5374 O HOH A 535 4130 4685 3657 435 429 -15 O HETATM 5375 O HOH A 536 16.631 28.930 4.023 1.00 38.65 O ANISOU 5375 O HOH A 536 5152 4897 4634 610 1247 978 O HETATM 5376 O HOH A 537 13.139 25.698 41.849 1.00 28.75 O ANISOU 5376 O HOH A 537 3555 3603 3765 -68 452 -16 O HETATM 5377 O HOH A 538 11.929 24.684 37.320 1.00 26.34 O ANISOU 5377 O HOH A 538 3342 3173 3492 -97 538 84 O HETATM 5378 O HOH A 539 2.753 13.099 18.947 1.00 36.83 O ANISOU 5378 O HOH A 539 5012 4487 4494 -90 748 -113 O HETATM 5379 O HOH A 540 13.183 14.351 4.610 1.00 28.87 O ANISOU 5379 O HOH A 540 4135 3804 3029 425 999 210 O HETATM 5380 O HOH A 541 22.193 32.375 14.603 1.00 29.43 O ANISOU 5380 O HOH A 541 3671 3295 4216 135 1194 837 O HETATM 5381 O HOH A 542 17.656 25.181 29.548 1.00 17.30 O ANISOU 5381 O HOH A 542 2151 1947 2475 -83 688 276 O HETATM 5382 O HOH A 543 -3.843 17.781 16.338 1.00 32.86 O ANISOU 5382 O HOH A 543 4377 4254 3853 -56 556 -199 O HETATM 5383 O HOH A 544 9.715 23.195 38.088 1.00 26.64 O ANISOU 5383 O HOH A 544 3440 3209 3472 -81 550 83 O HETATM 5384 O HOH A 545 7.981 35.915 17.265 1.00 21.83 O ANISOU 5384 O HOH A 545 2866 2409 3020 155 908 628 O HETATM 5385 O HOH A 546 3.587 39.750 16.150 1.00 32.73 O ANISOU 5385 O HOH A 546 4253 3799 4384 287 943 729 O HETATM 5386 O HOH A 547 19.453 15.653 4.825 1.00 23.93 O ANISOU 5386 O HOH A 547 3472 3067 2554 502 1178 508 O HETATM 5387 O HOH A 548 9.855 17.563 1.115 1.00 38.84 O ANISOU 5387 O HOH A 548 5365 5332 4060 579 919 236 O HETATM 5388 O HOH A 549 20.954 6.224 13.536 1.00 30.13 O ANISOU 5388 O HOH A 549 4328 3510 3608 313 1237 303 O HETATM 5389 O HOH A 550 17.425 32.817 57.833 1.00 38.06 O ANISOU 5389 O HOH A 550 4242 5550 4668 69 -32 -810 O HETATM 5390 O HOH A 551 14.835 6.522 16.297 1.00 26.99 O ANISOU 5390 O HOH A 551 3930 3076 3249 140 1099 113 O HETATM 5391 O HOH A 552 19.580 10.509 8.604 1.00 36.93 O ANISOU 5391 O HOH A 552 5170 4556 4307 374 1172 327 O HETATM 5392 O HOH A 553 17.727 28.242 10.409 1.00 30.02 O ANISOU 5392 O HOH A 553 3969 3605 3832 322 1121 798 O HETATM 5393 O HOH A 554 -9.274 33.372 19.746 1.00 40.63 O ANISOU 5393 O HOH A 554 5202 5231 5004 181 513 237 O HETATM 5394 O HOH A 555 13.719 7.608 18.240 1.00 23.02 O ANISOU 5394 O HOH A 555 3392 2570 2785 97 1045 122 O HETATM 5395 O HOH A 556 14.539 27.315 3.544 1.00 34.79 O ANISOU 5395 O HOH A 556 4708 4515 3998 624 1156 860 O HETATM 5396 O HOH A 557 14.410 39.225 14.995 1.00 31.20 O ANISOU 5396 O HOH A 557 3954 3389 4510 177 1191 873 O HETATM 5397 O HOH A 558 10.602 30.028 4.976 1.00 41.50 O ANISOU 5397 O HOH A 558 5523 5368 4876 601 1064 841 O HETATM 5398 O HOH A 559 -1.697 24.635 14.213 1.00 30.12 O ANISOU 5398 O HOH A 559 4013 3970 3461 151 579 130 O HETATM 5399 O HOH A 560 22.610 22.240 15.015 1.00 34.72 O ANISOU 5399 O HOH A 560 4518 4167 4507 201 1071 654 O HETATM 5400 O HOH A 561 15.482 4.239 16.408 1.00 25.32 O ANISOU 5400 O HOH A 561 3762 2800 3057 158 1176 91 O HETATM 5401 O HOH A 562 21.815 16.824 13.608 1.00 45.21 O ANISOU 5401 O HOH A 562 5994 5541 5641 268 1091 553 O HETATM 5402 O HOH A 563 13.476 32.384 13.276 1.00 27.16 O ANISOU 5402 O HOH A 563 3566 3158 3594 240 1031 748 O HETATM 5403 O HOH A 564 6.791 30.848 58.256 1.00 49.00 O ANISOU 5403 O HOH A 564 6052 6652 5913 160 197 -532 O HETATM 5404 O HOH A 565 20.397 24.515 9.587 1.00 37.15 O ANISOU 5404 O HOH A 565 4907 4551 4659 351 1158 772 O HETATM 5405 O HOH A 566 -0.799 28.384 14.240 1.00 48.24 O ANISOU 5405 O HOH A 566 6292 6214 5823 222 629 301 O HETATM 5406 O HOH A 567 -3.750 20.494 58.311 1.00 48.21 O ANISOU 5406 O HOH A 567 6310 6299 5711 338 698 47 O HETATM 5407 O HOH A 568 8.016 27.988 55.786 1.00 36.16 O ANISOU 5407 O HOH A 568 4459 4971 4310 164 263 -352 O HETATM 5408 O HOH A 569 2.087 41.643 18.274 1.00 30.26 O ANISOU 5408 O HOH A 569 3920 3401 4177 246 933 688 O HETATM 5409 O HOH A 570 2.155 14.367 61.771 1.00 46.01 O ANISOU 5409 O HOH A 570 6051 6283 5147 728 843 346 O HETATM 5410 O HOH A 571 13.814 18.213 19.704 1.00 27.94 O ANISOU 5410 O HOH A 571 3806 3314 3496 61 846 316 O HETATM 5411 O HOH A 572 -1.041 20.364 10.460 1.00 33.38 O ANISOU 5411 O HOH A 572 4474 4518 3691 188 583 -28 O HETATM 5412 O HOH A 573 21.216 9.277 6.001 1.00 44.74 O ANISOU 5412 O HOH A 573 6207 5583 5209 472 1260 340 O HETATM 5413 O HOH A 574 21.499 22.370 10.290 1.00 30.32 O ANISOU 5413 O HOH A 574 4053 3684 3784 334 1152 725 O HETATM 5414 O HOH A 575 9.611 25.106 -2.469 1.00 38.33 O ANISOU 5414 O HOH A 575 5243 5447 3875 912 1036 698 O HETATM 5415 O HOH B 501 -11.948 34.303 72.898 1.00 41.50 O ANISOU 5415 O HOH B 501 5426 5955 4386 701 523 -646 O HETATM 5416 O HOH B 502 -13.402 26.451 64.052 1.00 23.32 O ANISOU 5416 O HOH B 502 3162 3199 2498 410 752 -128 O HETATM 5417 O HOH B 503 -29.846 42.307 48.464 1.00 35.10 O ANISOU 5417 O HOH B 503 4346 4270 4720 179 678 -166 O HETATM 5418 O HOH B 504 -12.191 33.289 21.073 1.00 34.88 O ANISOU 5418 O HOH B 504 4428 4548 4275 158 464 166 O HETATM 5419 O HOH B 505 -26.701 25.905 64.777 1.00 32.70 O ANISOU 5419 O HOH B 505 4268 4194 3962 362 1132 27 O HETATM 5420 O HOH B 506 -25.977 11.933 55.492 1.00 44.04 O ANISOU 5420 O HOH B 506 5623 5117 5994 -112 1486 155 O HETATM 5421 O HOH B 507 -22.754 28.766 20.068 1.00 40.84 O ANISOU 5421 O HOH B 507 4886 5763 4868 90 241 -228 O HETATM 5422 O HOH B 508 -12.664 31.230 45.375 1.00 16.23 O ANISOU 5422 O HOH B 508 2150 1842 2172 -109 526 -162 O HETATM 5423 O HOH B 509 -20.513 33.560 36.741 1.00 43.63 O ANISOU 5423 O HOH B 509 5466 5436 5677 -70 484 -95 O HETATM 5424 O HOH B 510 -28.416 30.420 59.323 1.00 22.62 O ANISOU 5424 O HOH B 510 2888 2827 2879 178 928 -125 O HETATM 5425 O HOH B 511 -25.354 21.852 55.212 1.00 24.37 O ANISOU 5425 O HOH B 511 3119 2910 3230 -16 1030 -13 O HETATM 5426 O HOH B 512 -19.909 36.595 34.941 1.00 18.44 O ANISOU 5426 O HOH B 512 2278 2228 2499 6 484 -24 O HETATM 5427 O HOH B 513 -16.100 33.714 20.846 1.00 36.68 O ANISOU 5427 O HOH B 513 4576 4914 4448 204 406 120 O HETATM 5428 O HOH B 514 -11.474 38.574 73.021 1.00 34.73 O ANISOU 5428 O HOH B 514 4528 5048 3621 614 416 -928 O HETATM 5429 O HOH B 515 -24.802 36.979 24.219 1.00 23.36 O ANISOU 5429 O HOH B 515 2688 3369 2820 287 354 84 O HETATM 5430 O HOH B 516 -17.290 30.623 33.504 1.00 22.17 O ANISOU 5430 O HOH B 516 2786 2734 2904 -117 463 -95 O HETATM 5431 O HOH B 517 -17.221 36.041 16.339 1.00 37.63 O ANISOU 5431 O HOH B 517 4648 5260 4388 450 405 268 O HETATM 5432 O HOH B 518 -20.160 38.926 73.902 1.00 25.05 O ANISOU 5432 O HOH B 518 3398 3658 2461 708 702 -716 O HETATM 5433 O HOH B 519 -18.677 31.025 59.720 1.00 19.08 O ANISOU 5433 O HOH B 519 2563 2434 2251 198 714 -230 O HETATM 5434 O HOH B 520 -33.314 25.824 56.004 1.00 24.87 O ANISOU 5434 O HOH B 520 2990 3053 3407 0 1066 -65 O HETATM 5435 O HOH B 521 -21.922 32.091 61.109 1.00 19.67 O ANISOU 5435 O HOH B 521 2624 2516 2332 244 778 -233 O HETATM 5436 O HOH B 522 -21.113 49.401 62.128 1.00 27.65 O ANISOU 5436 O HOH B 522 3641 3195 3670 254 662 -828 O HETATM 5437 O HOH B 523 -20.038 33.448 52.243 1.00 27.30 O ANISOU 5437 O HOH B 523 3529 3312 3531 18 627 -225 O HETATM 5438 O HOH B 524 -24.368 37.451 46.948 1.00 20.09 O ANISOU 5438 O HOH B 524 2512 2368 2753 24 600 -179 O HETATM 5439 O HOH B 525 -31.215 29.610 55.308 1.00 31.47 O ANISOU 5439 O HOH B 525 3886 3913 4156 52 914 -120 O HETATM 5440 O HOH B 526 -17.201 36.258 54.215 1.00 26.67 O ANISOU 5440 O HOH B 526 3478 3228 3426 51 572 -328 O HETATM 5441 O HOH B 527 -20.123 31.021 73.853 1.00 32.53 O ANISOU 5441 O HOH B 527 4379 4678 3305 808 903 -268 O HETATM 5442 O HOH B 528 -12.637 28.764 64.872 1.00 31.25 O ANISOU 5442 O HOH B 528 4150 4258 3467 420 667 -244 O HETATM 5443 O HOH B 529 -21.293 36.195 18.546 1.00 31.79 O ANISOU 5443 O HOH B 529 3809 4581 3689 412 342 171 O HETATM 5444 O HOH B 530 -23.212 33.601 36.889 1.00 27.11 O ANISOU 5444 O HOH B 530 3316 3399 3585 -56 483 -111 O HETATM 5445 O HOH B 531 -10.475 32.648 68.771 1.00 31.46 O ANISOU 5445 O HOH B 531 4138 4506 3310 534 515 -519 O HETATM 5446 O HOH B 532 -13.005 24.065 17.364 1.00 35.29 O ANISOU 5446 O HOH B 532 4458 4827 4123 14 365 -205 O HETATM 5447 O HOH B 533 -34.418 38.428 59.088 1.00 44.34 O ANISOU 5447 O HOH B 533 5539 5574 5736 296 914 -213 O HETATM 5448 O HOH B 534 -17.030 24.140 62.138 1.00 19.92 O ANISOU 5448 O HOH B 534 2731 2612 2226 322 901 -7 O HETATM 5449 O HOH B 535 -10.343 32.894 65.520 1.00 32.14 O ANISOU 5449 O HOH B 535 4212 4425 3574 388 504 -487 O HETATM 5450 O HOH B 536 -18.003 42.228 71.164 1.00 33.51 O ANISOU 5450 O HOH B 536 4427 4559 3746 526 576 -899 O HETATM 5451 O HOH B 537 -25.198 37.536 70.632 1.00 33.37 O ANISOU 5451 O HOH B 537 4428 4495 3757 605 865 -463 O HETATM 5452 O HOH B 538 -13.336 31.379 58.023 1.00 24.36 O ANISOU 5452 O HOH B 538 3230 3108 2918 144 586 -287 O HETATM 5453 O HOH B 539 -16.780 30.794 58.501 1.00 21.25 O ANISOU 5453 O HOH B 539 2838 2694 2540 161 669 -236 O HETATM 5454 O HOH B 540 -16.931 16.990 60.247 1.00 23.34 O ANISOU 5454 O HOH B 540 3199 2865 2802 277 1161 220 O HETATM 5455 O HOH B 541 -30.133 33.069 57.141 1.00 34.07 O ANISOU 5455 O HOH B 541 4280 4258 4409 148 866 -166 O HETATM 5456 O HOH B 542 -7.393 22.053 64.721 1.00 26.70 O ANISOU 5456 O HOH B 542 3606 3781 2759 559 758 20 O HETATM 5457 O HOH B 543 -18.834 31.701 37.958 1.00 17.12 O ANISOU 5457 O HOH B 543 2148 2039 2316 -118 498 -117 O HETATM 5458 O HOH B 544 -33.978 18.483 55.855 1.00 30.47 O ANISOU 5458 O HOH B 544 3654 3600 4322 -144 1339 6 O HETATM 5459 O HOH B 545 -17.245 38.453 55.514 1.00 30.73 O ANISOU 5459 O HOH B 545 3995 3733 3949 78 564 -402 O HETATM 5460 O HOH B 546 -12.434 18.752 63.718 1.00 36.42 O ANISOU 5460 O HOH B 546 4890 4782 4167 497 1024 202 O HETATM 5461 O HOH B 547 -28.107 14.841 57.044 1.00 39.58 O ANISOU 5461 O HOH B 547 5015 4658 5368 -59 1429 139 O HETATM 5462 O HOH B 548 -17.933 43.954 68.690 1.00 29.34 O ANISOU 5462 O HOH B 548 3880 3866 3402 412 561 -919 O HETATM 5463 O HOH B 549 -10.632 45.266 66.139 1.00 35.52 O ANISOU 5463 O HOH B 549 4558 4592 4346 208 373 -1115 O HETATM 5464 O HOH B 550 -28.880 35.393 66.907 1.00 38.77 O ANISOU 5464 O HOH B 550 5035 5031 4665 473 965 -267 O HETATM 5465 O HOH B 551 -32.805 32.150 61.701 1.00 41.63 O ANISOU 5465 O HOH B 551 5242 5275 5299 272 1034 -115 O HETATM 5466 O HOH B 552 -10.833 40.635 70.564 1.00 43.77 O ANISOU 5466 O HOH B 552 5642 6014 4976 456 375 -1006 O HETATM 5467 O HOH B 553 -19.849 27.094 71.014 1.00 38.13 O ANISOU 5467 O HOH B 553 5084 5242 4163 702 996 -61 O HETATM 5468 O HOH B 554 -27.687 42.962 56.201 1.00 32.08 O ANISOU 5468 O HOH B 554 4096 3860 4234 231 732 -347 O HETATM 5469 O HOH B 555 -31.234 20.422 65.106 1.00 54.62 O ANISOU 5469 O HOH B 555 6961 6829 6964 306 1487 232 O HETATM 5470 O HOH B 556 -25.231 37.186 44.392 1.00 25.72 O ANISOU 5470 O HOH B 556 3182 3114 3475 17 578 -145 O HETATM 5471 O HOH B 557 -8.053 34.859 60.719 1.00 35.50 O ANISOU 5471 O HOH B 557 4588 4652 4249 179 420 -533 O HETATM 5472 O HOH B 558 -16.730 29.162 72.230 1.00 28.05 O ANISOU 5472 O HOH B 558 3801 4112 2746 756 833 -227 O HETATM 5473 O HOH B 559 -31.346 35.825 64.610 1.00 40.28 O ANISOU 5473 O HOH B 559 5158 5150 4995 402 983 -228 O HETATM 5474 O HOH B 560 -9.871 30.116 67.749 1.00 44.75 O ANISOU 5474 O HOH B 560 5835 6169 4999 535 563 -379 O HETATM 5475 O HOH B 561 -11.353 37.541 19.465 1.00 36.53 O ANISOU 5475 O HOH B 561 4647 4712 4521 312 555 368 O HETATM 5476 O HOH B 562 -18.968 28.685 73.244 1.00 28.35 O ANISOU 5476 O HOH B 562 3855 4143 2773 809 937 -158 O HETATM 5477 O HOH B 563 -34.221 26.436 58.033 1.00 42.50 O ANISOU 5477 O HOH B 563 5233 5306 5609 68 1123 -39 O HETATM 5478 O HOH B 564 -12.441 43.005 71.573 1.00 42.78 O ANISOU 5478 O HOH B 564 5530 5845 4881 467 395 -1127 O HETATM 5479 O HOH B 565 -8.678 34.338 64.850 1.00 37.48 O ANISOU 5479 O HOH B 565 4855 5087 4298 334 432 -579 O CONECT 1 5025 CONECT 13 5048 CONECT 114 4969 CONECT 921 1472 CONECT 1472 921 CONECT 2270 5042 CONECT 2485 5152 CONECT 2487 5252 CONECT 2499 5275 CONECT 2600 4997 CONECT 3400 3961 CONECT 3961 3400 CONECT 4751 5269 CONECT 4967 5326 CONECT 4969 114 4970 4980 CONECT 4970 4969 4971 4977 CONECT 4971 4970 4972 4978 CONECT 4972 4971 4973 4979 CONECT 4973 4972 4974 4980 CONECT 4974 4973 4981 CONECT 4975 4976 4977 4982 CONECT 4976 4975 CONECT 4977 4970 4975 CONECT 4978 4971 CONECT 4979 4972 4983 CONECT 4980 4969 4973 CONECT 4981 4974 CONECT 4982 4975 CONECT 4983 4979 4984 4994 CONECT 4984 4983 4985 4991 CONECT 4985 4984 4986 4992 CONECT 4986 4985 4987 4993 CONECT 4987 4986 4988 4994 CONECT 4988 4987 4995 CONECT 4989 4990 4991 4996 CONECT 4990 4989 CONECT 4991 4984 4989 CONECT 4992 4985 CONECT 4993 4986 CONECT 4994 4983 4987 CONECT 4995 4988 CONECT 4996 4989 CONECT 4997 2600 4998 5008 CONECT 4998 4997 4999 5005 CONECT 4999 4998 5000 5006 CONECT 5000 4999 5001 5007 CONECT 5001 5000 5002 5008 CONECT 5002 5001 5009 CONECT 5003 5004 5005 5010 CONECT 5004 5003 CONECT 5005 4998 5003 CONECT 5006 4999 CONECT 5007 5000 5011 CONECT 5008 4997 5001 CONECT 5009 5002 CONECT 5010 5003 CONECT 5011 5007 5012 5022 CONECT 5012 5011 5013 5019 CONECT 5013 5012 5014 5020 CONECT 5014 5013 5015 5021 CONECT 5015 5014 5016 5022 CONECT 5016 5015 5023 CONECT 5017 5018 5019 5024 CONECT 5018 5017 CONECT 5019 5012 5017 CONECT 5020 5013 CONECT 5021 5014 CONECT 5022 5011 5015 CONECT 5023 5016 CONECT 5024 5017 CONECT 5025 1 5026 5027 CONECT 5026 5025 CONECT 5027 5025 CONECT 5028 5029 5033 5043 5044 CONECT 5029 5028 5030 CONECT 5030 5029 5031 CONECT 5031 5030 5032 CONECT 5032 5031 5033 5045 CONECT 5033 5028 5032 5034 CONECT 5034 5033 5035 CONECT 5035 5034 5036 CONECT 5036 5035 5037 5046 CONECT 5037 5036 5038 CONECT 5038 5037 5039 CONECT 5039 5038 5040 CONECT 5040 5039 5041 5047 CONECT 5041 5040 5042 CONECT 5042 2270 5041 CONECT 5043 5028 CONECT 5044 5028 CONECT 5045 5032 CONECT 5046 5036 CONECT 5047 5040 CONECT 5048 13 5049 5059 CONECT 5049 5048 5050 5056 CONECT 5050 5049 5051 5057 CONECT 5051 5050 5052 5058 CONECT 5052 5051 5053 5059 CONECT 5053 5052 5060 CONECT 5054 5055 5056 5061 CONECT 5055 5054 CONECT 5056 5049 5054 CONECT 5057 5050 CONECT 5058 5051 CONECT 5059 5048 5052 CONECT 5060 5053 CONECT 5061 5054 CONECT 5062 5064 CONECT 5063 5064 CONECT 5064 5062 5063 5065 CONECT 5065 5064 5066 CONECT 5066 5065 5067 CONECT 5067 5066 5068 CONECT 5068 5067 5069 CONECT 5069 5068 5070 CONECT 5070 5069 5071 CONECT 5071 5070 5072 CONECT 5072 5071 5073 CONECT 5073 5072 5074 CONECT 5074 5073 5075 CONECT 5075 5074 CONECT 5076 5079 CONECT 5077 5078 5080 CONECT 5078 5077 5081 CONECT 5079 5076 5083 CONECT 5080 5077 5084 CONECT 5081 5078 5085 CONECT 5082 5096 5098 CONECT 5083 5079 5086 CONECT 5084 5080 5087 CONECT 5085 5081 5088 CONECT 5086 5083 5089 CONECT 5087 5084 5089 CONECT 5088 5085 5090 CONECT 5089 5086 5087 CONECT 5090 5088 5091 CONECT 5091 5090 5092 CONECT 5092 5091 5093 CONECT 5093 5092 5095 CONECT 5094 5096 5100 CONECT 5095 5093 5097 5100 CONECT 5096 5082 5094 5099 CONECT 5097 5095 CONECT 5098 5082 CONECT 5099 5096 CONECT 5100 5094 5095 CONECT 5101 5102 5103 CONECT 5102 5101 5104 CONECT 5103 5101 5106 CONECT 5104 5102 5107 CONECT 5105 5118 5120 CONECT 5106 5103 5109 CONECT 5107 5104 5110 CONECT 5108 5111 CONECT 5109 5106 5111 CONECT 5110 5107 5112 CONECT 5111 5108 5109 CONECT 5112 5110 5113 CONECT 5113 5112 5114 CONECT 5114 5113 5115 CONECT 5115 5114 5117 CONECT 5116 5118 5122 CONECT 5117 5115 5119 5122 CONECT 5118 5105 5116 5121 CONECT 5119 5117 CONECT 5120 5105 CONECT 5121 5118 CONECT 5122 5116 5117 CONECT 5123 5124 5125 CONECT 5124 5123 5126 CONECT 5125 5123 5127 CONECT 5126 5124 5128 CONECT 5127 5125 5129 CONECT 5128 5126 CONECT 5129 5127 CONECT 5130 5131 5132 CONECT 5131 5130 5133 CONECT 5132 5130 5134 CONECT 5133 5131 5135 CONECT 5134 5132 5136 CONECT 5135 5133 5137 CONECT 5136 5134 5138 CONECT 5137 5135 5139 CONECT 5138 5136 CONECT 5139 5137 CONECT 5140 5141 5142 CONECT 5141 5140 5143 CONECT 5142 5140 5144 CONECT 5143 5141 5145 CONECT 5144 5142 5146 CONECT 5145 5143 5147 CONECT 5146 5144 CONECT 5147 5145 5148 CONECT 5148 5147 5149 CONECT 5149 5148 5150 CONECT 5150 5149 5151 CONECT 5151 5150 CONECT 5152 2485 5153 5154 CONECT 5153 5152 CONECT 5154 5152 5155 CONECT 5155 5154 5156 CONECT 5156 5155 5157 CONECT 5157 5156 5158 CONECT 5158 5157 5159 CONECT 5159 5158 5160 CONECT 5160 5159 5161 CONECT 5161 5160 5162 CONECT 5162 5161 5163 CONECT 5163 5162 5164 CONECT 5164 5163 5165 CONECT 5165 5164 5166 CONECT 5166 5165 5167 CONECT 5167 5166 5168 CONECT 5168 5167 CONECT 5169 5170 CONECT 5170 5169 5171 CONECT 5171 5170 5172 CONECT 5172 5171 5173 CONECT 5173 5172 5174 CONECT 5174 5173 5175 CONECT 5175 5174 5176 CONECT 5176 5175 5177 5178 CONECT 5177 5176 CONECT 5178 5176 CONECT 5179 5182 CONECT 5180 5181 5183 CONECT 5181 5180 5184 CONECT 5182 5179 5186 CONECT 5183 5180 5187 CONECT 5184 5181 5188 CONECT 5185 5199 5201 CONECT 5186 5182 5189 CONECT 5187 5183 5190 CONECT 5188 5184 5191 CONECT 5189 5186 5192 CONECT 5190 5187 5192 CONECT 5191 5188 5193 CONECT 5192 5189 5190 CONECT 5193 5191 5194 CONECT 5194 5193 5195 CONECT 5195 5194 5196 CONECT 5196 5195 5198 CONECT 5197 5199 5203 CONECT 5198 5196 5200 5203 CONECT 5199 5185 5197 5202 CONECT 5200 5198 CONECT 5201 5185 CONECT 5202 5199 CONECT 5203 5197 5198 CONECT 5204 5205 CONECT 5205 5204 5206 CONECT 5206 5205 5207 CONECT 5207 5206 5208 CONECT 5208 5207 5209 CONECT 5209 5208 5210 CONECT 5210 5209 5211 CONECT 5211 5210 5212 5213 CONECT 5212 5211 CONECT 5213 5211 CONECT 5214 5217 CONECT 5215 5216 5218 CONECT 5216 5215 5219 CONECT 5217 5214 5221 CONECT 5218 5215 5222 CONECT 5219 5216 5223 CONECT 5220 5234 5236 CONECT 5221 5217 5224 CONECT 5222 5218 5225 CONECT 5223 5219 5226 CONECT 5224 5221 5227 CONECT 5225 5222 5227 CONECT 5226 5223 5228 CONECT 5227 5224 5225 CONECT 5228 5226 5229 CONECT 5229 5228 5230 CONECT 5230 5229 5231 CONECT 5231 5230 5233 CONECT 5232 5234 5238 CONECT 5233 5231 5235 5238 CONECT 5234 5220 5232 5237 CONECT 5235 5233 CONECT 5236 5220 CONECT 5237 5234 CONECT 5238 5232 5233 CONECT 5239 5240 5241 CONECT 5240 5239 5242 CONECT 5241 5239 5243 CONECT 5242 5240 5244 CONECT 5243 5241 5245 CONECT 5244 5242 5246 CONECT 5245 5243 5247 CONECT 5246 5244 5248 CONECT 5247 5245 CONECT 5248 5246 5249 CONECT 5249 5248 5250 CONECT 5250 5249 5251 CONECT 5251 5250 CONECT 5252 2487 5253 5254 CONECT 5253 5252 CONECT 5254 5252 CONECT 5255 5256 5260 5270 5271 CONECT 5256 5255 5257 CONECT 5257 5256 5258 CONECT 5258 5257 5259 CONECT 5259 5258 5260 5272 CONECT 5260 5255 5259 5261 CONECT 5261 5260 5262 CONECT 5262 5261 5263 CONECT 5263 5262 5264 5273 CONECT 5264 5263 5265 CONECT 5265 5264 5266 CONECT 5266 5265 5267 CONECT 5267 5266 5268 5274 CONECT 5268 5267 5269 CONECT 5269 4751 5268 CONECT 5270 5255 CONECT 5271 5255 CONECT 5272 5259 CONECT 5273 5263 CONECT 5274 5267 CONECT 5275 2499 5276 5286 CONECT 5276 5275 5277 5283 CONECT 5277 5276 5278 5284 CONECT 5278 5277 5279 5285 CONECT 5279 5278 5280 5286 CONECT 5280 5279 5287 CONECT 5281 5282 5283 5288 CONECT 5282 5281 CONECT 5283 5276 5281 CONECT 5284 5277 CONECT 5285 5278 CONECT 5286 5275 5279 CONECT 5287 5280 CONECT 5288 5281 CONECT 5289 5290 5291 CONECT 5290 5289 5292 CONECT 5291 5289 5293 CONECT 5292 5290 5294 CONECT 5293 5291 5296 CONECT 5294 5292 5297 CONECT 5295 5298 CONECT 5296 5293 5298 CONECT 5297 5294 5299 CONECT 5298 5295 5296 CONECT 5299 5297 5300 CONECT 5300 5299 5301 CONECT 5301 5300 5302 CONECT 5302 5301 5304 CONECT 5303 5305 5307 CONECT 5304 5302 5306 5307 CONECT 5305 5303 CONECT 5306 5304 CONECT 5307 5303 5304 CONECT 5308 5309 5310 CONECT 5309 5308 5311 CONECT 5310 5308 CONECT 5311 5309 5313 CONECT 5312 5321 5323 CONECT 5313 5311 5314 CONECT 5314 5313 5315 CONECT 5315 5314 5316 CONECT 5316 5315 5317 CONECT 5317 5316 5318 CONECT 5318 5317 5320 CONECT 5319 5321 5325 CONECT 5320 5318 5322 5325 CONECT 5321 5312 5319 5324 CONECT 5322 5320 CONECT 5323 5312 CONECT 5324 5321 CONECT 5325 5319 5320 CONECT 5326 4967 5327 5328 CONECT 5327 5326 CONECT 5328 5326 5329 CONECT 5329 5328 5330 CONECT 5330 5329 5331 CONECT 5331 5330 5332 CONECT 5332 5331 CONECT 5333 5334 5335 CONECT 5334 5333 5336 CONECT 5335 5333 5337 CONECT 5336 5334 5338 CONECT 5337 5335 5339 CONECT 5338 5336 CONECT 5339 5337 MASTER 402 0 26 28 8 0 0 6 5312 2 385 54 END