HEADER MEMBRANE PROTEIN 23-MAR-22 7ZBE TITLE DARK STATE CRYSTAL STRUCTURE OF BOVINE RHODOPSIN IN LIPIDIC CUBIC TITLE 2 PHASE (SWISSFEL) 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, XFEL, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.GRUHL,T.WEINERT,M.J.RODRIGUES,C.MILNE,G.ORTOLANI,K.NASS,E.NANGO, AUTHOR 2 S.SEN,P.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.CASADEI,A.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 7ZBE 1 JRNL REVDAT 2 05-APR-23 7ZBE 1 JRNL REVDAT 1 29-MAR-23 7ZBE 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 1.19.2_4158 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) : 16.10 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 79098 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.450 REMARK 3 FREE R VALUE TEST SET COUNT : 1144 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 16.1000 - 3.5900 1.00 10114 150 0.2214 0.2474 REMARK 3 2 3.5900 - 2.8500 1.00 9841 145 0.2006 0.2262 REMARK 3 3 2.8500 - 2.4900 1.00 9754 142 0.1833 0.2183 REMARK 3 4 2.4900 - 2.2700 1.00 9711 142 0.1886 0.2240 REMARK 3 5 2.2700 - 2.1000 1.00 9690 142 0.1901 0.2119 REMARK 3 6 2.1000 - 1.9800 1.00 9644 141 0.2371 0.3330 REMARK 3 7 1.9800 - 1.8800 1.00 9646 141 0.2803 0.3154 REMARK 3 8 1.8800 - 1.8000 0.99 9554 141 0.3472 0.4015 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.246 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.959 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 30.05 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.69 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 5484 REMARK 3 ANGLE : 0.913 7443 REMARK 3 CHIRALITY : 0.056 831 REMARK 3 PLANARITY : 0.007 911 REMARK 3 DIHEDRAL : 13.203 1981 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): -5.4901 28.4182 37.7945 REMARK 3 T TENSOR REMARK 3 T11: 0.2504 T22: 0.2188 REMARK 3 T33: 0.2447 T12: -0.0196 REMARK 3 T13: -0.0237 T23: -0.0103 REMARK 3 L TENSOR REMARK 3 L11: 0.7269 L22: 0.3818 REMARK 3 L33: 0.3525 L12: -0.2216 REMARK 3 L13: -0.3172 L23: 0.0550 REMARK 3 S TENSOR REMARK 3 S11: -0.0097 S12: 0.0188 S13: 0.0022 REMARK 3 S21: -0.0054 S22: -0.0038 S23: -0.0122 REMARK 3 S31: 0.0260 S32: -0.0178 S33: 0.0005 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 7ZBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-APR-22. REMARK 100 THE DEPOSITION ID IS D_1292121578. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUL-20 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 : ESA REMARK 200 X-RAY GENERATOR MODEL : SWISSFEL ARAMIS BEAMLINE ESA REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.38 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI JUNGFRAU 1M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79305 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 16.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 830.6 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.6200 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 : 556.7 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.950 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 (%): 54.60 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 45.50500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.55500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.50500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 75.55500 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: 6070 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 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 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 GLN A 244 CG CD OE1 NE2 REMARK 470 LYS A 245 CE NZ REMARK 470 LYS A 311 CE NZ REMARK 470 LYS B 66 CG CD CE NZ REMARK 470 LYS B 67 CE NZ REMARK 470 LYS B 141 CD CE NZ REMARK 470 ARG B 147 CG 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 470 LYS B 311 CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 SG CYS A 322 O2 PLM A 410 2.06 REMARK 500 SG CYS B 322 O2 PLM B 407 2.15 REMARK 500 REMARK 500 REMARK: NULL 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 ASN A 8 31.40 -140.03 REMARK 500 GLN A 28 40.35 -94.21 REMARK 500 SER A 176 -166.05 61.36 REMARK 500 HIS A 195 67.06 34.23 REMARK 500 PHE A 212 -56.54 -133.51 REMARK 500 PHE A 212 -56.19 -133.51 REMARK 500 PHE A 228 57.83 -91.10 REMARK 500 GLN B 28 36.09 -93.64 REMARK 500 SER B 176 -167.30 59.72 REMARK 500 GLN B 184 22.91 80.11 REMARK 500 HIS B 195 69.04 32.03 REMARK 500 PHE B 212 -56.32 -138.66 REMARK 500 PHE B 228 55.18 -93.08 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 DAO A 404 REMARK 610 OLC A 406 REMARK 610 OLC A 407 REMARK 610 OLC A 408 REMARK 610 OLC A 409 REMARK 610 PLM A 410 REMARK 610 OLC A 411 REMARK 610 OLC A 413 REMARK 610 OLC A 414 REMARK 610 OLC B 404 REMARK 610 OLC B 405 REMARK 610 OLC B 406 REMARK 610 PLM B 407 REMARK 610 OLC B 408 DBREF 7ZBE A 1 348 UNP P02699 OPSD_BOVIN 1 348 DBREF 7ZBE 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 13 HET OLC A 405 25 HET OLC A 406 17 HET OLC A 407 7 HET OLC A 408 10 HET OLC A 409 12 HET PLM A 410 12 HET OLC A 411 10 HET OLC A 412 25 HET OLC A 413 10 HET OLC A 414 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 OLC B 406 17 HET PLM B 407 7 HET OLC B 408 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 *174(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 LYS A 245 THR A 277 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 GLY A 6 0 SHEET 2 AA1 2 PHE A 9 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 GLY B 6 0 SHEET 2 AA3 2 PHE B 9 VAL B 11 -1 O VAL B 11 N THR B 4 SHEET 1 AA4 2 TYR B 178 GLU B 181 0 SHEET 2 AA4 2 SER B 186 ILE B 189 -1 O GLY B 188 N ILE B 179 SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.05 SSBOND 2 CYS B 110 CYS B 187 1555 1555 2.05 LINK N MET A 1 C ACE A 401 1555 1555 1.34 LINK ND2 ASN A 2 C1 NAG A 403 1555 1555 1.46 LINK ND2 ASN A 15 C1 NAG C 1 1555 1555 1.44 LINK NZ LYS A 296 C15 RET A 402 1555 1555 1.33 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 1.45 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 407 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 61.510 91.010 151.110 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 0.016258 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010988 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006618 0.00000 ATOM 1 N MET A 1 16.279 34.502 5.181 1.00 69.54 N ANISOU 1 N MET A 1 9005 8910 8507 536 846 706 N ATOM 2 CA MET A 1 15.891 33.433 6.107 1.00 55.09 C ANISOU 2 CA MET A 1 7174 7076 6681 486 768 618 C ATOM 3 C MET A 1 16.637 32.132 5.825 1.00 57.04 C ANISOU 3 C MET A 1 7428 7336 6908 480 767 566 C ATOM 4 O MET A 1 16.688 31.625 4.697 1.00 58.73 O ANISOU 4 O MET A 1 7665 7610 7041 523 789 566 O ATOM 5 CB MET A 1 14.381 33.192 6.056 1.00 64.85 C ANISOU 5 CB MET A 1 8431 8372 7836 495 704 588 C ATOM 6 N ASN A 2 17.240 31.609 6.878 1.00 54.91 N ANISOU 6 N ASN A 2 7137 7011 6715 430 743 523 N ATOM 7 CA ASN A 2 18.072 30.425 6.807 1.00 43.10 C ANISOU 7 CA ASN A 2 5641 5512 5222 420 746 478 C ATOM 8 C ASN A 2 17.306 29.150 7.141 1.00 39.12 C ANISOU 8 C ASN A 2 5156 5036 4672 399 678 398 C ATOM 9 O ASN A 2 17.899 28.067 7.157 1.00 39.10 O ANISOU 9 O ASN A 2 5155 5028 4674 389 677 354 O ATOM 10 CB ASN A 2 19.260 30.626 7.745 1.00 44.37 C ANISOU 10 CB ASN A 2 5764 5598 5496 382 765 483 C ATOM 11 CG ASN A 2 20.264 31.647 7.197 1.00 44.96 C ANISOU 11 CG ASN A 2 5819 5645 5619 405 847 556 C ATOM 12 OD1 ASN A 2 21.084 31.294 6.358 1.00 42.61 O ANISOU 12 OD1 ASN A 2 5525 5362 5304 433 897 570 O ATOM 13 ND2 ASN A 2 20.201 32.909 7.668 1.00 45.73 N ANISOU 13 ND2 ASN A 2 5894 5701 5779 393 864 600 N ATOM 14 N GLY A 3 16.006 29.261 7.408 1.00 35.31 N ANISOU 14 N GLY A 3 4685 4581 4151 391 625 378 N ATOM 15 CA GLY A 3 15.187 28.137 7.824 1.00 29.57 C ANISOU 15 CA GLY A 3 3971 3873 3390 366 562 303 C ATOM 16 C GLY A 3 13.972 28.005 6.932 1.00 34.61 C ANISOU 16 C GLY A 3 4635 4591 3925 397 538 287 C ATOM 17 O GLY A 3 13.913 28.639 5.876 1.00 35.15 O ANISOU 17 O GLY A 3 4713 4704 3937 446 574 334 O ATOM 18 N THR A 4 12.995 27.196 7.326 1.00 27.39 N ANISOU 18 N THR A 4 3728 3695 2982 373 478 222 N ATOM 19 CA THR A 4 11.836 26.929 6.480 1.00 29.70 C ANISOU 19 CA THR A 4 4041 4068 3176 399 449 193 C ATOM 20 C THR A 4 10.563 27.180 7.272 1.00 30.42 C ANISOU 20 C THR A 4 4126 4162 3271 373 391 176 C ATOM 21 O THR A 4 10.224 26.408 8.171 1.00 26.93 O ANISOU 21 O THR A 4 3679 3690 2862 329 349 120 O ATOM 22 CB THR A 4 11.887 25.497 5.944 1.00 31.94 C ANISOU 22 CB THR A 4 4340 4382 3412 397 440 118 C ATOM 23 OG1 THR A 4 13.106 25.322 5.204 1.00 28.72 O ANISOU 23 OG1 THR A 4 3939 3972 3003 424 499 138 O ATOM 24 CG2 THR A 4 10.694 25.214 5.011 1.00 32.24 C ANISOU 24 CG2 THR A 4 4394 4513 3345 424 408 79 C ATOM 25 N GLU A 5 9.851 28.249 6.938 1.00 29.16 N ANISOU 25 N GLU A 5 3965 4038 3078 402 390 225 N ATOM 26 CA GLU A 5 8.615 28.574 7.626 1.00 29.57 C ANISOU 26 CA GLU A 5 4009 4095 3131 382 338 213 C ATOM 27 C GLU A 5 7.445 27.896 6.924 1.00 31.04 C ANISOU 27 C GLU A 5 4206 4364 3223 397 296 158 C ATOM 28 O GLU A 5 7.330 27.954 5.696 1.00 33.22 O ANISOU 28 O GLU A 5 4493 4713 3415 446 313 169 O ATOM 29 CB GLU A 5 8.389 30.090 7.674 1.00 30.79 C ANISOU 29 CB GLU A 5 4154 4242 3302 407 360 294 C ATOM 30 CG GLU A 5 7.168 30.467 8.500 1.00 32.79 C ANISOU 30 CG GLU A 5 4398 4492 3568 384 309 284 C ATOM 31 CD GLU A 5 6.939 31.965 8.624 1.00 36.81 C ANISOU 31 CD GLU A 5 4898 4985 4103 407 334 362 C ATOM 32 OE1 GLU A 5 7.785 32.745 8.149 1.00 38.55 O ANISOU 32 OE1 GLU A 5 5118 5188 4343 436 393 427 O ATOM 33 OE2 GLU A 5 5.913 32.357 9.220 1.00 38.82 O ANISOU 33 OE2 GLU A 5 5145 5241 4363 395 296 359 O ATOM 34 N GLY A 6 6.586 27.254 7.700 1.00 29.45 N ANISOU 34 N GLY A 6 3998 4155 3035 356 241 98 N ATOM 35 CA GLY A 6 5.345 26.735 7.180 1.00 30.41 C ANISOU 35 CA GLY A 6 4122 4352 3079 363 196 43 C ATOM 36 C GLY A 6 4.189 27.413 7.868 1.00 30.31 C ANISOU 36 C GLY A 6 4095 4342 3078 351 156 56 C ATOM 37 O GLY A 6 4.375 28.361 8.639 1.00 34.16 O ANISOU 37 O GLY A 6 4575 4776 3628 343 168 112 O ATOM 38 N PRO A 7 2.967 26.925 7.630 1.00 32.25 N ANISOU 38 N PRO A 7 4336 4648 3268 348 108 1 N ATOM 39 CA PRO A 7 1.794 27.574 8.243 1.00 31.05 C ANISOU 39 CA PRO A 7 4168 4504 3125 340 69 14 C ATOM 40 C PRO A 7 1.839 27.606 9.761 1.00 34.73 C ANISOU 40 C PRO A 7 4626 4882 3688 286 56 12 C ATOM 41 O PRO A 7 1.393 28.586 10.376 1.00 32.32 O ANISOU 41 O PRO A 7 4310 4556 3413 286 50 57 O ATOM 42 CB PRO A 7 0.620 26.719 7.739 1.00 36.34 C ANISOU 42 CB PRO A 7 4831 5252 3726 336 20 -64 C ATOM 43 CG PRO A 7 1.114 26.110 6.468 1.00 39.19 C ANISOU 43 CG PRO A 7 5206 5671 4014 368 40 -92 C ATOM 44 CD PRO A 7 2.586 25.868 6.671 1.00 35.98 C ANISOU 44 CD PRO A 7 4814 5193 3663 357 89 -73 C ATOM 45 N ASN A 8 2.372 26.551 10.383 1.00 30.28 N ANISOU 45 N ASN A 8 4067 4267 3173 243 53 -40 N ATOM 46 CA ASN A 8 2.369 26.429 11.836 1.00 28.48 C ANISOU 46 CA ASN A 8 3831 3963 3027 194 37 -48 C ATOM 47 C ASN A 8 3.689 25.855 12.339 1.00 27.97 C ANISOU 47 C ASN A 8 3773 3831 3024 172 66 -53 C ATOM 48 O ASN A 8 3.726 25.158 13.360 1.00 26.96 O ANISOU 48 O ASN A 8 3642 3653 2949 131 50 -87 O ATOM 49 CB ASN A 8 1.180 25.576 12.304 1.00 29.78 C ANISOU 49 CB ASN A 8 3987 4142 3186 159 -11 -118 C ATOM 50 CG ASN A 8 1.054 24.278 11.531 1.00 37.29 C ANISOU 50 CG ASN A 8 4945 5131 4093 154 -20 -193 C ATOM 51 OD1 ASN A 8 1.894 23.969 10.694 1.00 32.05 O ANISOU 51 OD1 ASN A 8 4294 4482 3402 176 11 -195 O ATOM 52 ND2 ASN A 8 0.017 23.498 11.830 1.00 37.14 N ANISOU 52 ND2 ASN A 8 4917 5125 4071 123 -58 -258 N ATOM 53 N PHE A 9 4.787 26.135 11.643 1.00 25.75 N ANISOU 53 N PHE A 9 3500 3549 2736 200 111 -16 N ATOM 54 CA PHE A 9 6.066 25.619 12.094 1.00 25.92 C ANISOU 54 CA PHE A 9 3523 3510 2816 182 139 -18 C ATOM 55 C PHE A 9 7.186 26.470 11.512 1.00 27.46 C ANISOU 55 C PHE A 9 3719 3697 3018 216 191 47 C ATOM 56 O PHE A 9 6.985 27.238 10.567 1.00 25.81 O ANISOU 56 O PHE A 9 3513 3536 2757 257 210 87 O ATOM 57 CB PHE A 9 6.230 24.140 11.709 1.00 24.59 C ANISOU 57 CB PHE A 9 3366 3350 2626 171 136 -88 C ATOM 58 CG PHE A 9 6.183 23.881 10.216 1.00 25.56 C ANISOU 58 CG PHE A 9 3501 3544 2665 210 152 -104 C ATOM 59 CD1 PHE A 9 7.325 24.010 9.440 1.00 25.74 C ANISOU 59 CD1 PHE A 9 3532 3570 2677 241 201 -73 C ATOM 60 CD2 PHE A 9 5.020 23.458 9.612 1.00 27.83 C ANISOU 60 CD2 PHE A 9 3790 3898 2885 214 118 -155 C ATOM 61 CE1 PHE A 9 7.304 23.762 8.081 1.00 30.48 C ANISOU 61 CE1 PHE A 9 4146 4240 3196 279 217 -88 C ATOM 62 CE2 PHE A 9 4.985 23.191 8.243 1.00 29.19 C ANISOU 62 CE2 PHE A 9 3973 4143 2974 252 130 -176 C ATOM 63 CZ PHE A 9 6.131 23.343 7.477 1.00 30.76 C ANISOU 63 CZ PHE A 9 4183 4345 3158 286 180 -142 C ATOM 64 N TYR A 10 8.373 26.333 12.105 1.00 25.24 N ANISOU 64 N TYR A 10 3430 3355 2803 199 217 59 N ATOM 65 CA TYR A 10 9.575 27.001 11.603 1.00 24.66 C ANISOU 65 CA TYR A 10 3354 3267 2750 225 271 114 C ATOM 66 C TYR A 10 10.714 26.015 11.814 1.00 28.02 C ANISOU 66 C TYR A 10 3778 3654 3213 210 290 87 C ATOM 67 O TYR A 10 11.203 25.858 12.939 1.00 25.47 O ANISOU 67 O TYR A 10 3442 3277 2960 178 281 82 O ATOM 68 CB TYR A 10 9.869 28.321 12.309 1.00 25.97 C ANISOU 68 CB TYR A 10 3501 3389 2978 219 286 173 C ATOM 69 CG TYR A 10 11.079 28.991 11.712 1.00 26.90 C ANISOU 69 CG TYR A 10 3612 3490 3118 245 346 228 C ATOM 70 CD1 TYR A 10 10.949 29.826 10.611 1.00 32.14 C ANISOU 70 CD1 TYR A 10 4284 4194 3735 290 382 280 C ATOM 71 CD2 TYR A 10 12.366 28.721 12.186 1.00 26.66 C ANISOU 71 CD2 TYR A 10 3568 3409 3154 227 371 228 C ATOM 72 CE1 TYR A 10 12.070 30.411 10.011 1.00 35.22 C ANISOU 72 CE1 TYR A 10 4668 4568 4147 316 445 333 C ATOM 73 CE2 TYR A 10 13.496 29.317 11.593 1.00 26.61 C ANISOU 73 CE2 TYR A 10 3551 3387 3171 250 431 278 C ATOM 74 CZ TYR A 10 13.329 30.161 10.512 1.00 34.52 C ANISOU 74 CZ TYR A 10 4563 4425 4130 293 469 330 C ATOM 75 OH TYR A 10 14.418 30.755 9.914 1.00 33.06 O ANISOU 75 OH TYR A 10 4368 4223 3970 317 534 382 O ATOM 76 N VAL A 11 11.135 25.362 10.739 1.00 25.05 N ANISOU 76 N VAL A 11 3416 3311 2789 235 316 70 N ATOM 77 CA VAL A 11 12.198 24.364 10.829 1.00 25.06 C ANISOU 77 CA VAL A 11 3418 3280 2822 226 338 44 C ATOM 78 C VAL A 11 13.537 25.071 10.663 1.00 25.21 C ANISOU 78 C VAL A 11 3423 3269 2885 243 392 102 C ATOM 79 O VAL A 11 13.728 25.799 9.683 1.00 25.74 O ANISOU 79 O VAL A 11 3495 3368 2916 280 428 145 O ATOM 80 CB VAL A 11 12.007 23.253 9.783 1.00 28.77 C ANISOU 80 CB VAL A 11 3911 3797 3225 243 343 -10 C ATOM 81 CG1 VAL A 11 13.200 22.316 9.789 1.00 29.89 C ANISOU 81 CG1 VAL A 11 4052 3902 3402 240 375 -30 C ATOM 82 CG2 VAL A 11 10.696 22.464 10.078 1.00 25.98 C ANISOU 82 CG2 VAL A 11 3565 3463 2843 217 290 -77 C ATOM 83 N PRO A 12 14.497 24.880 11.588 1.00 24.91 N ANISOU 83 N PRO A 12 3367 3174 2926 218 399 105 N ATOM 84 CA PRO A 12 15.821 25.531 11.480 1.00 25.09 C ANISOU 84 CA PRO A 12 3369 3166 2999 230 449 155 C ATOM 85 C PRO A 12 16.748 24.777 10.531 1.00 27.80 C ANISOU 85 C PRO A 12 3720 3521 3321 256 494 147 C ATOM 86 O PRO A 12 17.797 24.230 10.917 1.00 28.49 O ANISOU 86 O PRO A 12 3793 3572 3460 247 512 140 O ATOM 87 CB PRO A 12 16.308 25.524 12.938 1.00 29.10 C ANISOU 87 CB PRO A 12 3849 3616 3592 192 427 150 C ATOM 88 CG PRO A 12 15.650 24.310 13.545 1.00 28.43 C ANISOU 88 CG PRO A 12 3777 3529 3495 170 382 91 C ATOM 89 CD PRO A 12 14.305 24.177 12.880 1.00 24.41 C ANISOU 89 CD PRO A 12 3295 3071 2910 179 357 66 C ATOM 90 N PHE A 13 16.338 24.721 9.263 1.00 26.00 N ANISOU 90 N PHE A 13 3517 3351 3012 292 512 146 N ATOM 91 CA PHE A 13 17.018 23.933 8.243 1.00 26.49 C ANISOU 91 CA PHE A 13 3593 3435 3037 320 552 129 C ATOM 92 C PHE A 13 16.551 24.458 6.891 1.00 27.45 C ANISOU 92 C PHE A 13 3735 3625 3070 365 576 154 C ATOM 93 O PHE A 13 15.350 24.650 6.691 1.00 28.67 O ANISOU 93 O PHE A 13 3902 3824 3168 370 540 140 O ATOM 94 CB PHE A 13 16.683 22.437 8.411 1.00 28.28 C ANISOU 94 CB PHE A 13 3835 3662 3247 302 522 51 C ATOM 95 CG PHE A 13 17.595 21.512 7.651 1.00 29.26 C ANISOU 95 CG PHE A 13 3970 3791 3358 323 565 28 C ATOM 96 CD1 PHE A 13 18.712 20.979 8.258 1.00 28.56 C ANISOU 96 CD1 PHE A 13 3864 3648 3341 310 585 28 C ATOM 97 CD2 PHE A 13 17.340 21.189 6.324 1.00 30.46 C ANISOU 97 CD2 PHE A 13 4147 4004 3424 358 586 7 C ATOM 98 CE1 PHE A 13 19.566 20.120 7.558 1.00 28.95 C ANISOU 98 CE1 PHE A 13 3921 3697 3381 331 628 8 C ATOM 99 CE2 PHE A 13 18.193 20.336 5.617 1.00 36.95 C ANISOU 99 CE2 PHE A 13 4978 4828 4233 378 628 -17 C ATOM 100 CZ PHE A 13 19.304 19.805 6.239 1.00 38.08 C ANISOU 100 CZ PHE A 13 5104 4910 4452 365 651 -15 C ATOM 101 N SER A 14 17.486 24.722 5.984 1.00 27.56 N ANISOU 101 N SER A 14 3750 3650 3071 402 637 192 N ATOM 102 CA SER A 14 17.132 25.310 4.698 1.00 28.16 C ANISOU 102 CA SER A 14 3844 3793 3062 452 666 227 C ATOM 103 C SER A 14 16.465 24.281 3.790 1.00 28.54 C ANISOU 103 C SER A 14 3922 3910 3013 472 648 162 C ATOM 104 O SER A 14 16.889 23.125 3.734 1.00 31.53 O ANISOU 104 O SER A 14 4307 4279 3395 462 650 106 O ATOM 105 CB SER A 14 18.379 25.872 4.013 1.00 29.27 C ANISOU 105 CB SER A 14 3976 3923 3222 486 744 290 C ATOM 106 OG SER A 14 18.093 26.229 2.664 1.00 33.82 O ANISOU 106 OG SER A 14 4575 4571 3703 543 776 319 O ATOM 107 N ASN A 15 15.451 24.715 3.032 1.00 31.33 N ANISOU 107 N ASN A 15 4290 4336 3279 504 632 168 N ATOM 108 CA ASN A 15 14.801 23.838 2.058 1.00 30.06 C ANISOU 108 CA ASN A 15 4152 4252 3016 527 614 104 C ATOM 109 C ASN A 15 15.347 24.020 0.640 1.00 35.09 C ANISOU 109 C ASN A 15 4806 4950 3577 589 673 136 C ATOM 110 O ASN A 15 14.670 23.683 -0.335 1.00 32.87 O ANISOU 110 O ASN A 15 4543 4753 3192 622 660 100 O ATOM 111 CB ASN A 15 13.282 24.026 2.074 1.00 32.61 C ANISOU 111 CB ASN A 15 4480 4631 3281 524 553 78 C ATOM 112 CG ASN A 15 12.556 22.816 1.490 1.00 31.66 C ANISOU 112 CG ASN A 15 4375 4570 3085 523 518 -19 C ATOM 113 OD1 ASN A 15 13.102 21.723 1.485 1.00 30.63 O ANISOU 113 OD1 ASN A 15 4251 4415 2972 505 528 -76 O ATOM 114 ND2 ASN A 15 11.342 23.012 0.991 1.00 30.05 N ANISOU 114 ND2 ASN A 15 4174 4444 2798 541 478 -38 N ATOM 115 N LYS A 16 16.583 24.506 0.501 1.00 31.77 N ANISOU 115 N LYS A 16 4377 4490 3204 606 738 199 N ATOM 116 CA LYS A 16 17.139 24.693 -0.838 1.00 32.79 C ANISOU 116 CA LYS A 16 4522 4675 3262 667 800 234 C ATOM 117 C LYS A 16 17.237 23.373 -1.600 1.00 41.18 C ANISOU 117 C LYS A 16 5606 5783 4258 679 801 152 C ATOM 118 O LYS A 16 17.093 23.356 -2.831 1.00 38.60 O ANISOU 118 O LYS A 16 5299 5538 3829 733 825 152 O ATOM 119 CB LYS A 16 18.508 25.368 -0.750 1.00 43.08 C ANISOU 119 CB LYS A 16 5807 5918 4643 676 873 312 C ATOM 120 CG LYS A 16 19.545 24.572 0.035 1.00 47.45 C ANISOU 120 CG LYS A 16 6345 6394 5292 633 882 278 C ATOM 121 CD LYS A 16 20.761 25.418 0.418 1.00 60.60 C ANISOU 121 CD LYS A 16 7981 7990 7054 630 940 355 C ATOM 122 CE LYS A 16 21.574 24.751 1.529 1.00 66.59 C ANISOU 122 CE LYS A 16 8715 8670 7917 579 929 321 C ATOM 123 NZ LYS A 16 22.806 25.523 1.871 1.00 83.08 N ANISOU 123 NZ LYS A 16 10770 10698 10101 574 984 387 N ATOM 124 N THR A 17 17.477 22.260 -0.900 1.00 32.76 N ANISOU 124 N THR A 17 4536 4665 3248 632 778 81 N ATOM 125 CA THR A 17 17.543 20.953 -1.548 1.00 36.35 C ANISOU 125 CA THR A 17 5010 5152 3650 638 779 -5 C ATOM 126 C THR A 17 16.196 20.227 -1.596 1.00 35.55 C ANISOU 126 C THR A 17 4919 5100 3487 619 711 -95 C ATOM 127 O THR A 17 16.133 19.105 -2.109 1.00 35.37 O ANISOU 127 O THR A 17 4912 5104 3424 619 709 -178 O ATOM 128 CB THR A 17 18.565 20.062 -0.838 1.00 38.52 C ANISOU 128 CB THR A 17 5275 5343 4019 602 798 -34 C ATOM 129 OG1 THR A 17 18.138 19.830 0.509 1.00 35.21 O ANISOU 129 OG1 THR A 17 4840 4861 3679 545 745 -58 O ATOM 130 CG2 THR A 17 19.926 20.724 -0.818 1.00 49.12 C ANISOU 130 CG2 THR A 17 6601 6639 5424 620 866 48 C ATOM 131 N GLY A 18 15.131 20.813 -1.055 1.00 31.24 N ANISOU 131 N GLY A 18 4364 4566 2940 601 658 -85 N ATOM 132 CA GLY A 18 13.799 20.251 -1.215 1.00 32.99 C ANISOU 132 CA GLY A 18 4592 4846 3096 588 595 -165 C ATOM 133 C GLY A 18 13.417 19.143 -0.251 1.00 36.63 C ANISOU 133 C GLY A 18 5047 5249 3620 525 552 -249 C ATOM 134 O GLY A 18 12.362 18.523 -0.439 1.00 34.65 O ANISOU 134 O GLY A 18 4800 5045 3321 511 505 -327 O ATOM 135 N VAL A 19 14.209 18.902 0.797 1.00 31.10 N ANISOU 135 N VAL A 19 4336 4453 3027 488 565 -233 N ATOM 136 CA VAL A 19 14.013 17.736 1.663 1.00 33.71 C ANISOU 136 CA VAL A 19 4663 4725 3418 436 536 -307 C ATOM 137 C VAL A 19 13.195 18.026 2.920 1.00 32.84 C ANISOU 137 C VAL A 19 4537 4574 3365 390 482 -302 C ATOM 138 O VAL A 19 12.788 17.071 3.606 1.00 31.19 O ANISOU 138 O VAL A 19 4326 4326 3197 348 454 -365 O ATOM 139 CB VAL A 19 15.371 17.109 2.042 1.00 31.62 C ANISOU 139 CB VAL A 19 4397 4385 3233 427 583 -301 C ATOM 140 CG1 VAL A 19 16.150 16.727 0.775 1.00 31.72 C ANISOU 140 CG1 VAL A 19 4427 4438 3188 472 639 -314 C ATOM 141 CG2 VAL A 19 16.188 18.054 2.921 1.00 35.40 C ANISOU 141 CG2 VAL A 19 4855 4802 3795 420 601 -210 C ATOM 142 N VAL A 20 12.892 19.292 3.221 1.00 29.50 N ANISOU 142 N VAL A 20 4103 4160 2946 399 469 -229 N ATOM 143 CA VAL A 20 12.192 19.615 4.465 1.00 28.21 C ANISOU 143 CA VAL A 20 3923 3954 2841 357 422 -220 C ATOM 144 C VAL A 20 10.741 19.158 4.390 1.00 30.09 C ANISOU 144 C VAL A 20 4164 4239 3029 339 366 -290 C ATOM 145 O VAL A 20 10.048 19.376 3.387 1.00 31.88 O ANISOU 145 O VAL A 20 4397 4551 3164 370 355 -306 O ATOM 146 CB VAL A 20 12.276 21.119 4.768 1.00 28.99 C ANISOU 146 CB VAL A 20 4009 4046 2958 372 429 -126 C ATOM 147 CG1 VAL A 20 11.501 21.488 6.063 1.00 30.57 C ANISOU 147 CG1 VAL A 20 4193 4206 3215 330 380 -120 C ATOM 148 CG2 VAL A 20 13.733 21.543 4.874 1.00 28.14 C ANISOU 148 CG2 VAL A 20 3894 3889 2909 384 486 -64 C ATOM 149 N AARG A 21 10.278 18.509 5.456 0.54 30.50 N ANISOU 149 N AARG A 21 4208 4239 3142 290 332 -332 N ATOM 150 N BARG A 21 10.275 18.517 5.458 0.46 30.50 N ANISOU 150 N BARG A 21 4209 4240 3142 290 332 -332 N ATOM 151 CA AARG A 21 8.888 18.109 5.596 0.54 31.14 C ANISOU 151 CA AARG A 21 4285 4352 3195 264 279 -396 C ATOM 152 CA BARG A 21 8.886 18.115 5.591 0.46 31.14 C ANISOU 152 CA BARG A 21 4285 4352 3194 265 279 -395 C ATOM 153 C AARG A 21 8.359 18.616 6.929 0.54 28.81 C ANISOU 153 C AARG A 21 3974 4008 2965 229 244 -365 C ATOM 154 C BARG A 21 8.357 18.613 6.927 0.46 28.82 C ANISOU 154 C BARG A 21 3976 4009 2966 229 244 -365 C ATOM 155 O AARG A 21 9.112 18.773 7.897 0.54 29.59 O ANISOU 155 O AARG A 21 4066 4034 3142 212 259 -323 O ATOM 156 O BARG A 21 9.111 18.761 7.897 0.46 29.59 O ANISOU 156 O BARG A 21 4066 4034 3141 212 259 -324 O ATOM 157 CB AARG A 21 8.729 16.584 5.493 0.54 33.62 C ANISOU 157 CB AARG A 21 4607 4651 3516 237 276 -495 C ATOM 158 CB BARG A 21 8.733 16.591 5.479 0.46 33.63 C ANISOU 158 CB BARG A 21 4608 4653 3516 237 277 -494 C ATOM 159 CG AARG A 21 9.108 16.043 4.120 0.54 40.16 C ANISOU 159 CG AARG A 21 5452 5537 4271 271 307 -539 C ATOM 160 CG BARG A 21 9.251 16.039 4.156 0.46 40.13 C ANISOU 160 CG BARG A 21 5448 5526 4273 272 312 -534 C ATOM 161 CD AARG A 21 8.476 14.692 3.830 0.54 47.35 C ANISOU 161 CD AARG A 21 6367 6458 5168 244 291 -653 C ATOM 162 CD BARG A 21 9.314 14.522 4.147 0.46 45.08 C ANISOU 162 CD BARG A 21 6082 6119 4926 243 321 -629 C ATOM 163 NE AARG A 21 9.307 13.576 4.268 0.54 45.14 N ANISOU 163 NE AARG A 21 6095 6098 4960 221 326 -686 N ATOM 164 NE BARG A 21 8.023 13.918 3.839 0.46 49.06 N ANISOU 164 NE BARG A 21 6582 6671 5388 221 278 -719 N ATOM 165 CZ AARG A 21 8.986 12.300 4.108 0.54 48.92 C ANISOU 165 CZ AARG A 21 6578 6562 5448 195 326 -783 C ATOM 166 CZ BARG A 21 7.816 12.612 3.742 0.46 48.78 C ANISOU 166 CZ BARG A 21 6550 6614 5369 192 282 -815 C ATOM 167 NH1AARG A 21 7.851 11.941 3.531 0.54 49.64 N ANISOU 167 NH1AARG A 21 6664 6717 5482 184 291 -863 N ATOM 168 NH1BARG A 21 8.797 11.743 3.920 0.46 50.53 N ANISOU 168 NH1BARG A 21 6784 6768 5648 185 326 -830 N ATOM 169 NH2AARG A 21 9.824 11.360 4.538 0.54 49.60 N ANISOU 169 NH2AARG A 21 6671 6569 5605 180 364 -800 N ATOM 170 NH2BARG A 21 6.595 12.169 3.462 0.46 54.10 N ANISOU 170 NH2BARG A 21 7214 7334 6006 171 242 -897 N ATOM 171 N SER A 22 7.058 18.885 6.960 1.00 27.13 N ANISOU 171 N SER A 22 3753 3839 2716 221 198 -386 N ATOM 172 CA SER A 22 6.441 19.427 8.163 1.00 28.46 C ANISOU 172 CA SER A 22 3907 3970 2938 191 165 -357 C ATOM 173 C SER A 22 6.663 18.492 9.349 1.00 28.07 C ANISOU 173 C SER A 22 3854 3836 2973 144 162 -389 C ATOM 174 O SER A 22 6.588 17.266 9.198 1.00 26.29 O ANISOU 174 O SER A 22 3637 3601 2753 125 164 -460 O ATOM 175 CB SER A 22 4.943 19.630 7.960 1.00 27.86 C ANISOU 175 CB SER A 22 3821 3957 2810 187 116 -390 C ATOM 176 OG SER A 22 4.286 19.837 9.205 1.00 27.31 O ANISOU 176 OG SER A 22 3737 3841 2797 150 84 -381 O ATOM 177 N PRO A 23 6.952 19.033 10.537 1.00 25.90 N ANISOU 177 N PRO A 23 3571 3503 2768 126 158 -337 N ATOM 178 CA PRO A 23 7.086 18.180 11.724 1.00 26.18 C ANISOU 178 CA PRO A 23 3602 3466 2878 86 153 -361 C ATOM 179 C PRO A 23 5.760 17.619 12.216 1.00 29.11 C ANISOU 179 C PRO A 23 3968 3840 3253 52 112 -416 C ATOM 180 O PRO A 23 5.749 16.876 13.199 1.00 26.16 O ANISOU 180 O PRO A 23 3593 3408 2940 21 110 -436 O ATOM 181 CB PRO A 23 7.718 19.123 12.758 1.00 27.54 C ANISOU 181 CB PRO A 23 3764 3592 3110 84 157 -287 C ATOM 182 CG PRO A 23 7.177 20.481 12.391 1.00 26.96 C ANISOU 182 CG PRO A 23 3684 3565 2994 105 143 -241 C ATOM 183 CD PRO A 23 7.144 20.461 10.850 1.00 25.16 C ANISOU 183 CD PRO A 23 3467 3408 2685 142 160 -256 C ATOM 184 N PHE A 24 4.643 17.955 11.575 1.00 27.28 N ANISOU 184 N PHE A 24 3732 3675 2959 58 83 -440 N ATOM 185 CA PHE A 24 3.375 17.300 11.857 1.00 27.55 C ANISOU 185 CA PHE A 24 3757 3718 2994 26 47 -505 C ATOM 186 C PHE A 24 3.035 16.226 10.840 1.00 29.28 C ANISOU 186 C PHE A 24 3980 3976 3168 23 49 -592 C ATOM 187 O PHE A 24 1.979 15.590 10.957 1.00 33.81 O ANISOU 187 O PHE A 24 4543 4559 3742 -7 23 -656 O ATOM 188 CB PHE A 24 2.249 18.335 11.917 1.00 26.37 C ANISOU 188 CB PHE A 24 3592 3617 2809 31 8 -480 C ATOM 189 CG PHE A 24 2.481 19.401 12.954 1.00 28.82 C ANISOU 189 CG PHE A 24 3897 3888 3166 30 6 -403 C ATOM 190 CD1 PHE A 24 2.573 19.065 14.296 1.00 27.67 C ANISOU 190 CD1 PHE A 24 3748 3671 3094 -3 2 -398 C ATOM 191 CD2 PHE A 24 2.627 20.732 12.587 1.00 31.74 C ANISOU 191 CD2 PHE A 24 4265 4292 3505 65 9 -336 C ATOM 192 CE1 PHE A 24 2.793 20.039 15.268 1.00 30.01 C ANISOU 192 CE1 PHE A 24 4038 3934 3430 -4 -1 -334 C ATOM 193 CE2 PHE A 24 2.852 21.707 13.546 1.00 30.31 C ANISOU 193 CE2 PHE A 24 4076 4070 3370 62 9 -272 C ATOM 194 CZ PHE A 24 2.935 21.363 14.890 1.00 27.89 C ANISOU 194 CZ PHE A 24 3765 3696 3135 26 2 -274 C ATOM 195 N GLU A 25 3.909 15.989 9.860 1.00 27.61 N ANISOU 195 N GLU A 25 3783 3785 2921 52 82 -599 N ATOM 196 CA GLU A 25 3.601 15.066 8.782 1.00 27.08 C ANISOU 196 CA GLU A 25 3720 3765 2802 54 85 -685 C ATOM 197 C GLU A 25 4.552 13.887 8.669 1.00 32.20 C ANISOU 197 C GLU A 25 4385 4361 3489 46 127 -725 C ATOM 198 O GLU A 25 4.111 12.808 8.271 1.00 34.76 O ANISOU 198 O GLU A 25 4709 4691 3808 25 127 -814 O ATOM 199 CB GLU A 25 3.582 15.814 7.433 1.00 31.81 C ANISOU 199 CB GLU A 25 4323 4462 3302 104 84 -671 C ATOM 200 CG GLU A 25 2.544 16.924 7.402 1.00 41.22 C ANISOU 200 CG GLU A 25 5498 5714 4449 117 42 -636 C ATOM 201 CD GLU A 25 2.416 17.597 6.030 1.00 46.48 C ANISOU 201 CD GLU A 25 6167 6484 5010 172 41 -622 C ATOM 202 OE1 GLU A 25 3.187 17.259 5.096 1.00 45.40 O ANISOU 202 OE1 GLU A 25 6045 6373 4832 200 74 -637 O ATOM 203 OE2 GLU A 25 1.541 18.474 5.906 1.00 47.03 O ANISOU 203 OE2 GLU A 25 6222 6610 5037 189 8 -594 O ATOM 204 N ALA A 26 5.835 14.048 8.987 1.00 28.34 N ANISOU 204 N ALA A 26 3906 3821 3040 61 166 -666 N ATOM 205 CA ALA A 26 6.789 12.983 8.691 1.00 27.30 C ANISOU 205 CA ALA A 26 3789 3650 2934 63 210 -702 C ATOM 206 C ALA A 26 7.953 13.054 9.663 1.00 26.78 C ANISOU 206 C ALA A 26 3725 3505 2946 63 239 -635 C ATOM 207 O ALA A 26 8.263 14.135 10.180 1.00 26.85 O ANISOU 207 O ALA A 26 3726 3508 2968 74 232 -557 O ATOM 208 CB ALA A 26 7.309 13.081 7.248 1.00 32.52 C ANISOU 208 CB ALA A 26 4463 4377 3518 105 235 -715 C ATOM 209 N PRO A 27 8.614 11.928 9.926 1.00 28.97 N ANISOU 209 N PRO A 27 4010 3720 3277 52 273 -665 N ATOM 210 CA PRO A 27 9.800 11.942 10.799 1.00 26.49 C ANISOU 210 CA PRO A 27 3694 3338 3032 58 302 -603 C ATOM 211 C PRO A 27 10.853 12.901 10.269 1.00 28.61 C ANISOU 211 C PRO A 27 3962 3632 3276 97 325 -536 C ATOM 212 O PRO A 27 11.055 13.037 9.060 1.00 26.97 O ANISOU 212 O PRO A 27 3764 3478 3004 125 343 -551 O ATOM 213 CB PRO A 27 10.302 10.493 10.749 1.00 29.89 C ANISOU 213 CB PRO A 27 4136 3716 3505 50 341 -658 C ATOM 214 CG PRO A 27 9.067 9.674 10.391 1.00 34.84 C ANISOU 214 CG PRO A 27 4765 4359 4112 20 322 -750 C ATOM 215 CD PRO A 27 8.262 10.569 9.461 1.00 30.37 C ANISOU 215 CD PRO A 27 4196 3887 3456 33 287 -761 C ATOM 216 N GLN A 28 11.566 13.533 11.188 1.00 25.98 N ANISOU 216 N GLN A 28 3617 3260 2994 99 328 -465 N ATOM 217 CA GLN A 28 12.495 14.617 10.840 1.00 25.93 C ANISOU 217 CA GLN A 28 3605 3273 2976 131 348 -395 C ATOM 218 C GLN A 28 13.926 14.124 10.643 1.00 26.50 C ANISOU 218 C GLN A 28 3677 3310 3080 152 399 -380 C ATOM 219 O GLN A 28 14.898 14.767 11.060 1.00 26.84 O ANISOU 219 O GLN A 28 3706 3332 3162 164 415 -318 O ATOM 220 CB GLN A 28 12.427 15.697 11.917 1.00 25.33 C ANISOU 220 CB GLN A 28 3510 3178 2937 120 322 -331 C ATOM 221 CG GLN A 28 11.010 16.300 12.061 1.00 26.15 C ANISOU 221 CG GLN A 28 3612 3319 3006 104 274 -340 C ATOM 222 CD GLN A 28 10.622 17.172 10.867 1.00 26.35 C ANISOU 222 CD GLN A 28 3642 3418 2952 133 273 -328 C ATOM 223 OE1 GLN A 28 11.138 18.273 10.704 1.00 26.93 O ANISOU 223 OE1 GLN A 28 3708 3504 3021 155 287 -264 O ATOM 224 NE2 GLN A 28 9.731 16.662 10.015 1.00 25.93 N ANISOU 224 NE2 GLN A 28 3599 3416 2837 134 259 -389 N ATOM 225 N TYR A 29 14.091 12.972 10.005 1.00 26.61 N ANISOU 225 N TYR A 29 3707 3319 3084 156 426 -440 N ATOM 226 CA TYR A 29 15.408 12.365 9.849 1.00 26.84 C ANISOU 226 CA TYR A 29 3737 3312 3149 176 476 -431 C ATOM 227 C TYR A 29 16.309 13.097 8.860 1.00 30.20 C ANISOU 227 C TYR A 29 4162 3776 3537 215 512 -390 C ATOM 228 O TYR A 29 17.491 12.751 8.759 1.00 32.49 O ANISOU 228 O TYR A 29 4448 4037 3860 234 556 -372 O ATOM 229 CB TYR A 29 15.257 10.915 9.394 1.00 30.19 C ANISOU 229 CB TYR A 29 4180 3718 3574 170 499 -512 C ATOM 230 CG TYR A 29 14.491 10.020 10.337 1.00 27.14 C ANISOU 230 CG TYR A 29 3793 3282 3236 132 477 -553 C ATOM 231 CD1 TYR A 29 14.532 10.216 11.718 1.00 28.22 C ANISOU 231 CD1 TYR A 29 3915 3372 3436 115 457 -506 C ATOM 232 CD2 TYR A 29 13.754 8.936 9.844 1.00 36.29 C ANISOU 232 CD2 TYR A 29 4967 4441 4380 115 481 -641 C ATOM 233 CE1 TYR A 29 13.819 9.372 12.587 1.00 28.38 C ANISOU 233 CE1 TYR A 29 3938 3346 3501 85 443 -540 C ATOM 234 CE2 TYR A 29 13.054 8.083 10.695 1.00 36.83 C ANISOU 234 CE2 TYR A 29 5035 4458 4500 81 469 -678 C ATOM 235 CZ TYR A 29 13.097 8.307 12.065 1.00 35.77 C ANISOU 235 CZ TYR A 29 4888 4277 4426 67 452 -623 C ATOM 236 OH TYR A 29 12.401 7.464 12.902 1.00 34.99 O ANISOU 236 OH TYR A 29 4790 4128 4378 36 445 -654 O ATOM 237 N TYR A 30 15.782 14.059 8.100 1.00 31.89 N ANISOU 237 N TYR A 30 4380 4055 3683 230 499 -374 N ATOM 238 CA TYR A 30 16.633 14.842 7.206 1.00 33.34 C ANISOU 238 CA TYR A 30 4562 4272 3833 270 538 -324 C ATOM 239 C TYR A 30 17.495 15.839 7.971 1.00 30.29 C ANISOU 239 C TYR A 30 4150 3851 3507 272 548 -241 C ATOM 240 O TYR A 30 18.448 16.380 7.400 1.00 35.13 O ANISOU 240 O TYR A 30 4757 4474 4118 301 590 -196 O ATOM 241 CB TYR A 30 15.775 15.586 6.170 1.00 27.89 C ANISOU 241 CB TYR A 30 3884 3664 3050 291 524 -326 C ATOM 242 CG TYR A 30 14.836 16.577 6.818 1.00 28.13 C ANISOU 242 CG TYR A 30 3902 3706 3079 273 476 -293 C ATOM 243 CD1 TYR A 30 15.228 17.888 7.031 1.00 27.20 C ANISOU 243 CD1 TYR A 30 3769 3587 2978 286 484 -212 C ATOM 244 CD2 TYR A 30 13.567 16.190 7.234 1.00 27.98 C ANISOU 244 CD2 TYR A 30 3886 3695 3050 243 426 -344 C ATOM 245 CE1 TYR A 30 14.370 18.805 7.637 1.00 27.47 C ANISOU 245 CE1 TYR A 30 3794 3629 3016 271 443 -183 C ATOM 246 CE2 TYR A 30 12.709 17.087 7.849 1.00 26.84 C ANISOU 246 CE2 TYR A 30 3730 3560 2907 228 384 -314 C ATOM 247 CZ TYR A 30 13.114 18.399 8.043 1.00 28.56 C ANISOU 247 CZ TYR A 30 3936 3778 3139 243 393 -233 C ATOM 248 OH TYR A 30 12.266 19.295 8.658 1.00 29.11 O ANISOU 248 OH TYR A 30 3995 3853 3213 229 354 -204 O ATOM 249 N LEU A 31 17.178 16.111 9.239 1.00 27.29 N ANISOU 249 N LEU A 31 3754 3433 3182 241 510 -222 N ATOM 250 CA LEU A 31 17.939 17.081 10.010 1.00 29.99 C ANISOU 250 CA LEU A 31 4068 3745 3581 239 514 -153 C ATOM 251 C LEU A 31 18.710 16.481 11.177 1.00 28.32 C ANISOU 251 C LEU A 31 3838 3471 3452 222 515 -147 C ATOM 252 O LEU A 31 19.503 17.200 11.796 1.00 31.56 O ANISOU 252 O LEU A 31 4220 3858 3913 222 521 -96 O ATOM 253 CB LEU A 31 17.019 18.196 10.532 1.00 32.43 C ANISOU 253 CB LEU A 31 4369 4070 3883 223 472 -124 C ATOM 254 CG LEU A 31 15.775 17.874 11.364 1.00 27.52 C ANISOU 254 CG LEU A 31 3752 3440 3263 189 417 -161 C ATOM 255 CD1 LEU A 31 16.130 17.386 12.744 1.00 29.36 C ANISOU 255 CD1 LEU A 31 3970 3614 3572 164 402 -159 C ATOM 256 CD2 LEU A 31 14.893 19.143 11.478 1.00 33.76 C ANISOU 256 CD2 LEU A 31 4537 4261 4028 185 386 -128 C ATOM 257 N ALA A 32 18.474 15.217 11.517 1.00 25.93 N ANISOU 257 N ALA A 32 3547 3141 3166 209 509 -198 N ATOM 258 CA ALA A 32 19.274 14.537 12.528 1.00 26.70 C ANISOU 258 CA ALA A 32 3627 3181 3336 203 516 -190 C ATOM 259 C ALA A 32 19.165 13.034 12.305 1.00 31.34 C ANISOU 259 C ALA A 32 4236 3746 3925 203 534 -249 C ATOM 260 O ALA A 32 18.166 12.546 11.773 1.00 31.09 O ANISOU 260 O ALA A 32 4229 3736 3850 193 523 -304 O ATOM 261 CB ALA A 32 18.819 14.915 13.947 1.00 27.41 C ANISOU 261 CB ALA A 32 3700 3248 3468 176 469 -169 C ATOM 262 N GLU A 33 20.212 12.300 12.702 1.00 28.84 N ANISOU 262 N GLU A 33 3909 3386 3664 215 565 -240 N ATOM 263 CA GLU A 33 20.175 10.865 12.494 1.00 32.78 C ANISOU 263 CA GLU A 33 4427 3855 4172 217 590 -294 C ATOM 264 C GLU A 33 19.256 10.183 13.506 1.00 28.69 C ANISOU 264 C GLU A 33 3915 3302 3683 188 558 -321 C ATOM 265 O GLU A 33 19.089 10.673 14.619 1.00 29.46 O ANISOU 265 O GLU A 33 3995 3387 3811 174 523 -285 O ATOM 266 CB GLU A 33 21.576 10.284 12.619 1.00 39.25 C ANISOU 266 CB GLU A 33 5231 4637 5044 244 635 -271 C ATOM 267 CG GLU A 33 22.563 10.901 11.655 1.00 43.46 C ANISOU 267 CG GLU A 33 5756 5200 5557 273 674 -242 C ATOM 268 CD GLU A 33 23.672 9.952 11.352 1.00 59.04 C ANISOU 268 CD GLU A 33 7726 7142 7564 300 728 -249 C ATOM 269 OE1 GLU A 33 23.387 8.925 10.693 1.00 61.46 O ANISOU 269 OE1 GLU A 33 8061 7441 7851 305 753 -307 O ATOM 270 OE2 GLU A 33 24.810 10.209 11.804 1.00 65.11 O ANISOU 270 OE2 GLU A 33 8463 7893 8382 317 745 -199 O ATOM 271 N PRO A 34 18.675 9.031 13.145 1.00 29.58 N ANISOU 271 N PRO A 34 4052 3397 3790 179 572 -386 N ATOM 272 CA PRO A 34 17.732 8.358 14.064 1.00 28.71 C ANISOU 272 CA PRO A 34 3948 3251 3710 150 547 -413 C ATOM 273 C PRO A 34 18.290 8.123 15.459 1.00 32.28 C ANISOU 273 C PRO A 34 4381 3653 4231 154 544 -363 C ATOM 274 O PRO A 34 17.541 8.237 16.443 1.00 25.89 O ANISOU 274 O PRO A 34 3567 2831 3438 132 508 -354 O ATOM 275 CB PRO A 34 17.420 7.040 13.332 1.00 35.06 C ANISOU 275 CB PRO A 34 4777 4034 4511 147 582 -490 C ATOM 276 CG PRO A 34 17.598 7.386 11.846 1.00 32.18 C ANISOU 276 CG PRO A 34 4424 3726 4078 165 600 -517 C ATOM 277 CD PRO A 34 18.745 8.383 11.819 1.00 29.54 C ANISOU 277 CD PRO A 34 4069 3410 3745 193 610 -443 C ATOM 278 N TRP A 35 19.591 7.834 15.598 1.00 31.43 N ANISOU 278 N TRP A 35 4259 3521 4163 183 579 -329 N ATOM 279 CA TRP A 35 20.094 7.597 16.949 1.00 26.06 C ANISOU 279 CA TRP A 35 3557 2801 3542 190 573 -283 C ATOM 280 C TRP A 35 20.024 8.839 17.831 1.00 29.34 C ANISOU 280 C TRP A 35 3948 3243 3957 180 524 -231 C ATOM 281 O TRP A 35 19.998 8.703 19.059 1.00 25.27 O ANISOU 281 O TRP A 35 3420 2705 3478 178 504 -203 O ATOM 282 CB TRP A 35 21.527 7.064 16.922 1.00 28.86 C ANISOU 282 CB TRP A 35 3897 3130 3939 227 618 -255 C ATOM 283 CG TRP A 35 22.555 8.006 16.386 1.00 33.18 C ANISOU 283 CG TRP A 35 4422 3712 4474 247 628 -219 C ATOM 284 CD1 TRP A 35 23.019 8.061 15.107 1.00 39.24 C ANISOU 284 CD1 TRP A 35 5198 4501 5210 262 664 -237 C ATOM 285 CD2 TRP A 35 23.258 9.013 17.113 1.00 36.29 C ANISOU 285 CD2 TRP A 35 4778 4123 4888 253 604 -159 C ATOM 286 NE1 TRP A 35 23.967 9.047 14.991 1.00 40.77 N ANISOU 286 NE1 TRP A 35 5362 4720 5407 278 668 -188 N ATOM 287 CE2 TRP A 35 24.133 9.646 16.209 1.00 40.33 C ANISOU 287 CE2 TRP A 35 5276 4662 5386 270 630 -143 C ATOM 288 CE3 TRP A 35 23.228 9.453 18.442 1.00 37.39 C ANISOU 288 CE3 TRP A 35 4892 4259 5056 245 563 -121 C ATOM 289 CZ2 TRP A 35 24.975 10.687 16.590 1.00 46.06 C ANISOU 289 CZ2 TRP A 35 5963 5406 6133 277 619 -92 C ATOM 290 CZ3 TRP A 35 24.075 10.479 18.821 1.00 44.76 C ANISOU 290 CZ3 TRP A 35 5786 5214 6005 252 549 -75 C ATOM 291 CH2 TRP A 35 24.929 11.091 17.897 1.00 35.35 C ANISOU 291 CH2 TRP A 35 4580 4045 4806 266 577 -62 C ATOM 292 N GLN A 36 19.992 10.050 17.246 1.00 27.79 N ANISOU 292 N GLN A 36 3744 3094 3720 176 507 -218 N ATOM 293 CA GLN A 36 19.850 11.251 18.073 1.00 28.75 C ANISOU 293 CA GLN A 36 3842 3236 3844 164 463 -175 C ATOM 294 C GLN A 36 18.431 11.375 18.631 1.00 34.28 C ANISOU 294 C GLN A 36 4557 3940 4527 133 420 -196 C ATOM 295 O GLN A 36 18.235 11.778 19.792 1.00 24.18 O ANISOU 295 O GLN A 36 3262 2656 3270 123 387 -168 O ATOM 296 CB GLN A 36 20.223 12.500 17.264 1.00 31.35 C ANISOU 296 CB GLN A 36 4161 3608 4143 170 465 -153 C ATOM 297 CG GLN A 36 21.666 12.510 16.713 1.00 34.84 C ANISOU 297 CG GLN A 36 4585 4049 4606 200 510 -128 C ATOM 298 CD GLN A 36 21.901 13.625 15.688 1.00 37.77 C ANISOU 298 CD GLN A 36 4952 4459 4940 207 523 -111 C ATOM 299 OE1 GLN A 36 22.091 13.367 14.500 1.00 37.14 O ANISOU 299 OE1 GLN A 36 4889 4395 4827 224 559 -130 O ATOM 300 NE2 GLN A 36 21.884 14.866 16.147 1.00 49.72 N ANISOU 300 NE2 GLN A 36 6442 5988 6461 195 496 -74 N ATOM 301 N PHE A 37 17.417 11.071 17.805 1.00 27.04 N ANISOU 301 N PHE A 37 3668 3038 3569 118 420 -246 N ATOM 302 CA PHE A 37 16.051 11.033 18.332 1.00 24.80 C ANISOU 302 CA PHE A 37 3396 2755 3274 88 384 -270 C ATOM 303 C PHE A 37 15.922 9.986 19.429 1.00 24.43 C ANISOU 303 C PHE A 37 3349 2655 3277 83 388 -272 C ATOM 304 O PHE A 37 15.192 10.186 20.415 1.00 24.10 O ANISOU 304 O PHE A 37 3304 2608 3246 65 356 -261 O ATOM 305 CB PHE A 37 15.042 10.748 17.201 1.00 24.72 C ANISOU 305 CB PHE A 37 3409 2771 3213 74 385 -332 C ATOM 306 CG PHE A 37 14.926 11.884 16.217 1.00 24.73 C ANISOU 306 CG PHE A 37 3410 2831 3156 81 374 -324 C ATOM 307 CD1 PHE A 37 14.136 12.978 16.497 1.00 24.37 C ANISOU 307 CD1 PHE A 37 3357 2816 3085 67 333 -304 C ATOM 308 CD2 PHE A 37 15.672 11.875 15.029 1.00 28.55 C ANISOU 308 CD2 PHE A 37 3900 3337 3612 106 410 -331 C ATOM 309 CE1 PHE A 37 14.055 14.062 15.586 1.00 24.43 C ANISOU 309 CE1 PHE A 37 3364 2876 3041 78 329 -289 C ATOM 310 CE2 PHE A 37 15.614 12.959 14.134 1.00 25.19 C ANISOU 310 CE2 PHE A 37 3474 2966 3132 118 406 -314 C ATOM 311 CZ PHE A 37 14.810 14.031 14.408 1.00 24.85 C ANISOU 311 CZ PHE A 37 3424 2952 3066 105 366 -292 C ATOM 312 N ASER A 38 16.623 8.864 19.285 0.63 24.81 N ANISOU 312 N ASER A 38 3404 2665 3358 102 431 -283 N ATOM 313 N BSER A 38 16.613 8.855 19.282 0.38 24.81 N ANISOU 313 N BSER A 38 3404 2665 3358 101 431 -284 N ATOM 314 CA ASER A 38 16.518 7.829 20.308 0.63 24.87 C ANISOU 314 CA ASER A 38 3414 2620 3415 102 442 -279 C ATOM 315 CA BSER A 38 16.529 7.820 20.309 0.38 24.87 C ANISOU 315 CA BSER A 38 3414 2620 3416 102 443 -278 C ATOM 316 C ASER A 38 17.101 8.297 21.644 0.63 26.33 C ANISOU 316 C ASER A 38 3572 2801 3630 116 420 -215 C ATOM 317 C BSER A 38 17.081 8.320 21.644 0.38 26.24 C ANISOU 317 C BSER A 38 3561 2790 3618 116 419 -215 C ATOM 318 O ASER A 38 16.619 7.903 22.719 0.63 24.42 O ANISOU 318 O ASER A 38 3331 2534 3414 111 408 -202 O ATOM 319 O BSER A 38 16.566 7.969 22.716 0.38 24.40 O ANISOU 319 O BSER A 38 3328 2534 3408 109 406 -202 O ATOM 320 CB ASER A 38 17.211 6.557 19.819 0.63 25.41 C ANISOU 320 CB ASER A 38 3493 2646 3514 123 499 -301 C ATOM 321 CB BSER A 38 17.273 6.566 19.850 0.38 25.40 C ANISOU 321 CB BSER A 38 3492 2645 3516 125 500 -298 C ATOM 322 OG ASER A 38 16.877 5.455 20.635 0.63 26.44 O ANISOU 322 OG ASER A 38 3633 2722 3693 122 517 -306 O ATOM 323 OG BSER A 38 16.633 5.972 18.736 0.38 26.09 O ANISOU 323 OG BSER A 38 3603 2731 3578 109 520 -368 O ATOM 324 N MET A 39 18.131 9.137 21.597 1.00 24.44 N ANISOU 324 N MET A 39 3309 2589 3390 135 415 -176 N ATOM 325 CA MET A 39 18.702 9.675 22.822 1.00 26.48 C ANISOU 325 CA MET A 39 3536 2852 3672 146 389 -123 C ATOM 326 C MET A 39 17.723 10.589 23.545 1.00 27.18 C ANISOU 326 C MET A 39 3622 2964 3741 120 338 -116 C ATOM 327 O MET A 39 17.678 10.594 24.780 1.00 23.56 O ANISOU 327 O MET A 39 3150 2499 3302 123 317 -88 O ATOM 328 CB MET A 39 19.987 10.431 22.505 1.00 25.69 C ANISOU 328 CB MET A 39 3406 2776 3578 167 396 -92 C ATOM 329 CG MET A 39 21.168 9.500 22.310 1.00 33.90 C ANISOU 329 CG MET A 39 4438 3790 4653 201 441 -81 C ATOM 330 SD MET A 39 22.582 10.529 21.897 1.00 49.41 S ANISOU 330 SD MET A 39 6363 5787 6625 219 448 -47 S ATOM 331 CE MET A 39 23.028 11.174 23.510 1.00 37.99 C ANISOU 331 CE MET A 39 4873 4355 5208 224 402 0 C ATOM 332 N LEU A 40 16.963 11.404 22.795 1.00 23.56 N ANISOU 332 N LEU A 40 3173 2536 3241 96 320 -139 N ATOM 333 CA LEU A 40 15.903 12.202 23.415 1.00 23.16 C ANISOU 333 CA LEU A 40 3123 2505 3172 71 276 -137 C ATOM 334 C LEU A 40 14.849 11.319 24.071 1.00 23.14 C ANISOU 334 C LEU A 40 3139 2474 3180 56 271 -157 C ATOM 335 O LEU A 40 14.364 11.624 25.165 1.00 22.87 O ANISOU 335 O LEU A 40 3097 2440 3151 47 242 -138 O ATOM 336 CB LEU A 40 15.248 13.110 22.375 1.00 23.07 C ANISOU 336 CB LEU A 40 3121 2531 3114 54 263 -157 C ATOM 337 CG LEU A 40 16.159 14.083 21.629 1.00 23.12 C ANISOU 337 CG LEU A 40 3111 2566 3109 68 273 -135 C ATOM 338 CD1 LEU A 40 15.298 14.825 20.614 1.00 25.52 C ANISOU 338 CD1 LEU A 40 3429 2906 3362 55 263 -154 C ATOM 339 CD2 LEU A 40 16.804 15.058 22.549 1.00 26.94 C ANISOU 339 CD2 LEU A 40 3562 3056 3618 71 251 -91 C ATOM 340 N ALA A 41 14.460 10.232 23.416 1.00 23.47 N ANISOU 340 N ALA A 41 3204 2490 3223 51 302 -199 N ATOM 341 CA ALA A 41 13.425 9.367 23.991 1.00 23.52 C ANISOU 341 CA ALA A 41 3226 2463 3246 34 304 -221 C ATOM 342 C ALA A 41 13.912 8.677 25.259 1.00 23.57 C ANISOU 342 C ALA A 41 3225 2432 3298 55 316 -182 C ATOM 343 O ALA A 41 13.161 8.549 26.237 1.00 23.42 O ANISOU 343 O ALA A 41 3208 2401 3290 45 301 -171 O ATOM 344 CB ALA A 41 12.968 8.331 22.961 1.00 25.11 C ANISOU 344 CB ALA A 41 3451 2643 3447 23 338 -282 C ATOM 345 N ALA A 42 15.161 8.211 25.263 1.00 25.17 N ANISOU 345 N ALA A 42 3418 2619 3528 88 346 -157 N ATOM 346 CA ALA A 42 15.695 7.574 26.462 1.00 23.93 C ANISOU 346 CA ALA A 42 3251 2434 3409 116 357 -113 C ATOM 347 C ALA A 42 15.735 8.554 27.624 1.00 25.84 C ANISOU 347 C ALA A 42 3469 2709 3640 119 310 -70 C ATOM 348 O ALA A 42 15.406 8.201 28.761 1.00 23.54 O ANISOU 348 O ALA A 42 3177 2403 3363 127 304 -45 O ATOM 349 CB ALA A 42 17.093 7.040 26.182 1.00 26.51 C ANISOU 349 CB ALA A 42 3565 2746 3762 154 394 -93 C ATOM 350 N TYR A 43 16.179 9.781 27.356 1.00 23.30 N ANISOU 350 N TYR A 43 3127 2431 3295 115 281 -62 N ATOM 351 CA TYR A 43 16.183 10.821 28.373 1.00 22.97 C ANISOU 351 CA TYR A 43 3061 2422 3243 113 236 -32 C ATOM 352 C TYR A 43 14.777 11.081 28.912 1.00 24.84 C ANISOU 352 C TYR A 43 3314 2663 3463 84 208 -45 C ATOM 353 O TYR A 43 14.572 11.117 30.128 1.00 26.65 O ANISOU 353 O TYR A 43 3535 2894 3696 92 189 -19 O ATOM 354 CB TYR A 43 16.799 12.077 27.760 1.00 27.13 C ANISOU 354 CB TYR A 43 3567 2987 3754 107 218 -29 C ATOM 355 CG TYR A 43 16.784 13.332 28.581 1.00 23.36 C ANISOU 355 CG TYR A 43 3064 2544 3267 98 173 -10 C ATOM 356 CD1 TYR A 43 17.680 13.514 29.621 1.00 24.81 C ANISOU 356 CD1 TYR A 43 3215 2742 3469 121 157 22 C ATOM 357 CD2 TYR A 43 15.927 14.365 28.268 1.00 26.18 C ANISOU 357 CD2 TYR A 43 3428 2923 3598 68 148 -26 C ATOM 358 CE1 TYR A 43 17.671 14.716 30.348 1.00 32.07 C ANISOU 358 CE1 TYR A 43 4109 3694 4381 109 116 32 C ATOM 359 CE2 TYR A 43 15.913 15.554 29.000 1.00 21.94 C ANISOU 359 CE2 TYR A 43 2867 2413 3056 59 110 -12 C ATOM 360 CZ TYR A 43 16.796 15.719 30.021 1.00 28.12 C ANISOU 360 CZ TYR A 43 3618 3208 3859 78 95 14 C ATOM 361 OH TYR A 43 16.789 16.919 30.728 1.00 25.08 O ANISOU 361 OH TYR A 43 3208 2850 3471 66 59 19 O ATOM 362 N MET A 44 13.782 11.222 28.029 1.00 22.78 N ANISOU 362 N MET A 44 3074 2403 3179 54 207 -85 N ATOM 363 CA MET A 44 12.421 11.483 28.506 1.00 22.35 C ANISOU 363 CA MET A 44 3030 2352 3109 27 182 -98 C ATOM 364 C MET A 44 11.854 10.299 29.286 1.00 24.08 C ANISOU 364 C MET A 44 3265 2530 3355 30 203 -96 C ATOM 365 O MET A 44 11.069 10.484 30.220 1.00 22.36 O ANISOU 365 O MET A 44 3047 2314 3134 21 182 -84 O ATOM 366 CB MET A 44 11.482 11.819 27.346 1.00 23.05 C ANISOU 366 CB MET A 44 3134 2456 3167 -3 177 -143 C ATOM 367 CG MET A 44 11.746 13.212 26.691 1.00 22.55 C ANISOU 367 CG MET A 44 3058 2437 3073 -7 153 -138 C ATOM 368 SD MET A 44 12.019 14.554 27.869 1.00 22.21 S ANISOU 368 SD MET A 44 2988 2422 3030 -5 111 -96 S ATOM 369 CE MET A 44 10.463 14.662 28.778 1.00 23.53 C ANISOU 369 CE MET A 44 3165 2587 3186 -29 83 -105 C ATOM 370 N PHE A 45 12.167 9.078 28.880 1.00 22.93 N ANISOU 370 N PHE A 45 3132 2344 3237 42 248 -108 N ATOM 371 CA PHE A 45 11.678 7.940 29.653 1.00 24.40 C ANISOU 371 CA PHE A 45 3332 2484 3457 47 276 -100 C ATOM 372 C PHE A 45 12.229 7.969 31.082 1.00 24.54 C ANISOU 372 C PHE A 45 3334 2506 3485 81 266 -41 C ATOM 373 O PHE A 45 11.495 7.710 32.052 1.00 26.51 O ANISOU 373 O PHE A 45 3588 2742 3741 79 264 -24 O ATOM 374 CB PHE A 45 12.071 6.650 28.936 1.00 23.67 C ANISOU 374 CB PHE A 45 3253 2342 3397 58 331 -123 C ATOM 375 CG PHE A 45 11.481 5.419 29.536 1.00 24.00 C ANISOU 375 CG PHE A 45 3312 2327 3481 59 370 -122 C ATOM 376 CD1 PHE A 45 10.100 5.283 29.682 1.00 26.66 C ANISOU 376 CD1 PHE A 45 3659 2650 3819 24 366 -152 C ATOM 377 CD2 PHE A 45 12.308 4.363 29.909 1.00 25.82 C ANISOU 377 CD2 PHE A 45 3544 2513 3753 97 416 -90 C ATOM 378 CE1 PHE A 45 9.556 4.116 30.221 1.00 33.48 C ANISOU 378 CE1 PHE A 45 4537 3454 4730 23 409 -150 C ATOM 379 CE2 PHE A 45 11.771 3.210 30.464 1.00 32.07 C ANISOU 379 CE2 PHE A 45 4350 3245 4589 100 460 -84 C ATOM 380 CZ PHE A 45 10.400 3.075 30.612 1.00 29.59 C ANISOU 380 CZ PHE A 45 4048 2914 4280 62 459 -115 C ATOM 381 N LEU A 46 13.525 8.285 31.219 1.00 23.27 N ANISOU 381 N LEU A 46 3151 2367 3325 112 260 -9 N ATOM 382 CA LEU A 46 14.142 8.425 32.536 1.00 27.45 C ANISOU 382 CA LEU A 46 3658 2914 3856 147 243 44 C ATOM 383 C LEU A 46 13.435 9.499 33.356 1.00 25.41 C ANISOU 383 C LEU A 46 3392 2695 3568 129 194 50 C ATOM 384 O LEU A 46 13.152 9.297 34.540 1.00 25.39 O ANISOU 384 O LEU A 46 3388 2694 3565 145 187 81 O ATOM 385 CB LEU A 46 15.624 8.770 32.404 1.00 25.92 C ANISOU 385 CB LEU A 46 3436 2747 3666 177 238 66 C ATOM 386 CG LEU A 46 16.354 8.870 33.755 1.00 33.47 C ANISOU 386 CG LEU A 46 4364 3730 4622 216 218 117 C ATOM 387 CD1 LEU A 46 16.431 7.505 34.385 1.00 30.64 C ANISOU 387 CD1 LEU A 46 4018 3332 4292 254 260 150 C ATOM 388 CD2 LEU A 46 17.756 9.493 33.637 1.00 42.50 C ANISOU 388 CD2 LEU A 46 5469 4911 5767 238 202 132 C ATOM 389 N LEU A 47 13.148 10.656 32.746 1.00 26.02 N ANISOU 389 N LEU A 47 3463 2804 3619 98 162 23 N ATOM 390 CA LEU A 47 12.509 11.733 33.509 1.00 23.99 C ANISOU 390 CA LEU A 47 3198 2582 3337 82 117 27 C ATOM 391 C LEU A 47 11.129 11.316 33.998 1.00 24.93 C ANISOU 391 C LEU A 47 3339 2681 3454 64 121 19 C ATOM 392 O LEU A 47 10.727 11.698 35.103 1.00 25.77 O ANISOU 392 O LEU A 47 3440 2805 3548 68 97 40 O ATOM 393 CB LEU A 47 12.389 13.025 32.687 1.00 22.94 C ANISOU 393 CB LEU A 47 3056 2480 3180 54 89 2 C ATOM 394 CG LEU A 47 13.656 13.821 32.371 1.00 25.58 C ANISOU 394 CG LEU A 47 3361 2842 3516 66 78 12 C ATOM 395 CD1 LEU A 47 13.359 15.186 31.719 1.00 22.24 C ANISOU 395 CD1 LEU A 47 2932 2446 3074 38 54 -7 C ATOM 396 CD2 LEU A 47 14.498 14.006 33.576 1.00 29.53 C ANISOU 396 CD2 LEU A 47 3833 3365 4024 94 59 45 C ATOM 397 N ILE A 48 10.372 10.562 33.179 1.00 25.92 N ANISOU 397 N ILE A 48 3488 2770 3591 42 150 -14 N ATOM 398 CA ILE A 48 9.029 10.138 33.584 1.00 24.32 C ANISOU 398 CA ILE A 48 3302 2544 3393 21 157 -26 C ATOM 399 C ILE A 48 9.112 9.123 34.712 1.00 26.34 C ANISOU 399 C ILE A 48 3563 2769 3674 51 186 14 C ATOM 400 O ILE A 48 8.363 9.195 35.691 1.00 26.74 O ANISOU 400 O ILE A 48 3617 2822 3720 50 177 32 O ATOM 401 CB ILE A 48 8.242 9.565 32.386 1.00 25.70 C ANISOU 401 CB ILE A 48 3496 2692 3577 -11 181 -79 C ATOM 402 CG1 ILE A 48 7.922 10.663 31.361 1.00 26.90 C ANISOU 402 CG1 ILE A 48 3643 2883 3694 -38 149 -113 C ATOM 403 CG2 ILE A 48 6.964 8.873 32.862 1.00 28.85 C ANISOU 403 CG2 ILE A 48 3908 3057 3995 -31 199 -91 C ATOM 404 CD1 ILE A 48 7.475 10.086 29.990 1.00 26.25 C ANISOU 404 CD1 ILE A 48 3575 2786 3613 -61 172 -168 C ATOM 405 N MET A 49 10.016 8.149 34.574 1.00 24.97 N ANISOU 405 N MET A 49 3392 2565 3529 81 225 31 N ATOM 406 CA MET A 49 10.104 7.043 35.520 1.00 28.23 C ANISOU 406 CA MET A 49 3813 2942 3972 114 263 72 C ATOM 407 C MET A 49 10.700 7.487 36.851 1.00 25.14 C ANISOU 407 C MET A 49 3402 2590 3560 154 236 127 C ATOM 408 O MET A 49 10.422 6.874 37.886 1.00 31.00 O ANISOU 408 O MET A 49 4151 3317 4310 180 256 166 O ATOM 409 CB MET A 49 10.927 5.904 34.924 1.00 23.70 C ANISOU 409 CB MET A 49 3246 2322 3436 138 315 74 C ATOM 410 CG MET A 49 10.247 5.232 33.713 1.00 23.86 C ANISOU 410 CG MET A 49 3286 2296 3482 100 350 14 C ATOM 411 SD MET A 49 8.701 4.371 34.127 1.00 40.31 S ANISOU 411 SD MET A 49 5392 4326 5599 71 384 -2 S ATOM 412 CE MET A 49 9.378 3.070 35.134 1.00 42.98 C ANISOU 412 CE MET A 49 5735 4611 5983 127 443 64 C ATOM 413 N LEU A 50 11.536 8.514 36.844 1.00 24.57 N ANISOU 413 N LEU A 50 3306 2570 3461 162 194 131 N ATOM 414 CA LEU A 50 11.956 9.100 38.114 1.00 26.90 C ANISOU 414 CA LEU A 50 3578 2913 3729 192 159 170 C ATOM 415 C LEU A 50 10.945 10.115 38.607 1.00 26.40 C ANISOU 415 C LEU A 50 3516 2881 3635 162 119 155 C ATOM 416 O LEU A 50 10.693 10.211 39.814 1.00 28.06 O ANISOU 416 O LEU A 50 3722 3112 3827 183 106 185 O ATOM 417 CB LEU A 50 13.313 9.773 37.977 1.00 29.69 C ANISOU 417 CB LEU A 50 3899 3309 4073 212 131 177 C ATOM 418 CG LEU A 50 14.446 8.840 37.547 1.00 40.31 C ANISOU 418 CG LEU A 50 5239 4631 5448 247 169 196 C ATOM 419 CD1 LEU A 50 15.751 9.625 37.395 1.00 46.08 C ANISOU 419 CD1 LEU A 50 5931 5407 6170 261 139 198 C ATOM 420 CD2 LEU A 50 14.609 7.678 38.507 1.00 42.52 C ANISOU 420 CD2 LEU A 50 5524 4888 5743 296 204 247 C ATOM 421 N GLY A 51 10.396 10.901 37.681 1.00 23.77 N ANISOU 421 N GLY A 51 3186 2553 3293 118 100 111 N ATOM 422 CA GLY A 51 9.575 12.041 38.066 1.00 26.16 C ANISOU 422 CA GLY A 51 3484 2888 3566 92 59 96 C ATOM 423 C GLY A 51 8.256 11.640 38.693 1.00 29.59 C ANISOU 423 C GLY A 51 3939 3302 4001 80 71 99 C ATOM 424 O GLY A 51 7.782 12.282 39.639 1.00 26.65 O ANISOU 424 O GLY A 51 3562 2959 3605 81 44 110 O ATOM 425 N PHE A 52 7.625 10.598 38.166 1.00 25.47 N ANISOU 425 N PHE A 52 3440 2731 3508 67 113 86 N ATOM 426 CA PHE A 52 6.368 10.175 38.773 1.00 25.77 C ANISOU 426 CA PHE A 52 3494 2746 3554 54 130 89 C ATOM 427 C PHE A 52 6.551 9.700 40.215 1.00 26.16 C ANISOU 427 C PHE A 52 3542 2798 3599 98 142 145 C ATOM 428 O PHE A 52 5.884 10.258 41.103 1.00 26.58 O ANISOU 428 O PHE A 52 3594 2877 3628 96 121 156 O ATOM 429 CB PHE A 52 5.690 9.133 37.875 1.00 29.20 C ANISOU 429 CB PHE A 52 3947 3123 4026 28 175 57 C ATOM 430 CG PHE A 52 4.664 8.294 38.584 1.00 37.79 C ANISOU 430 CG PHE A 52 5048 4170 5138 25 211 71 C ATOM 431 CD1 PHE A 52 3.623 8.885 39.294 1.00 33.55 C ANISOU 431 CD1 PHE A 52 4511 3653 4583 9 190 73 C ATOM 432 CD2 PHE A 52 4.734 6.915 38.524 1.00 45.98 C ANISOU 432 CD2 PHE A 52 6099 5148 6222 37 270 81 C ATOM 433 CE1 PHE A 52 2.673 8.099 39.952 1.00 38.14 C ANISOU 433 CE1 PHE A 52 5104 4197 5191 7 229 88 C ATOM 434 CE2 PHE A 52 3.792 6.120 39.168 1.00 44.03 C ANISOU 434 CE2 PHE A 52 5865 4858 6006 33 311 96 C ATOM 435 CZ PHE A 52 2.761 6.710 39.882 1.00 37.12 C ANISOU 435 CZ PHE A 52 4988 4005 5111 18 290 100 C ATOM 436 N PRO A 53 7.436 8.749 40.537 1.00 23.57 N ANISOU 436 N PRO A 53 3214 2450 3290 140 175 183 N ATOM 437 CA PRO A 53 7.503 8.299 41.945 1.00 27.04 C ANISOU 437 CA PRO A 53 3656 2899 3721 187 189 241 C ATOM 438 C PRO A 53 7.969 9.377 42.915 1.00 29.80 C ANISOU 438 C PRO A 53 3982 3320 4020 210 135 260 C ATOM 439 O PRO A 53 7.421 9.485 44.020 1.00 30.51 O ANISOU 439 O PRO A 53 4075 3430 4087 226 130 286 O ATOM 440 CB PRO A 53 8.497 7.125 41.909 1.00 29.09 C ANISOU 440 CB PRO A 53 3916 3125 4011 231 234 278 C ATOM 441 CG PRO A 53 8.675 6.763 40.480 1.00 32.84 C ANISOU 441 CG PRO A 53 4398 3560 4520 200 255 233 C ATOM 442 CD PRO A 53 8.366 7.989 39.677 1.00 28.72 C ANISOU 442 CD PRO A 53 3868 3072 3973 153 206 180 C ATOM 443 N AILE A 54 8.965 10.185 42.545 0.53 24.18 N ANISOU 443 N AILE A 54 3247 2649 3292 211 96 244 N ATOM 444 N BILE A 54 8.970 10.172 42.534 0.48 24.19 N ANISOU 444 N BILE A 54 3248 2650 3294 211 97 244 N ATOM 445 CA AILE A 54 9.524 11.113 43.524 0.53 25.09 C ANISOU 445 CA AILE A 54 3336 2832 3365 236 48 258 C ATOM 446 CA BILE A 54 9.544 11.142 43.461 0.48 25.10 C ANISOU 446 CA BILE A 54 3337 2833 3368 234 47 256 C ATOM 447 C AILE A 54 8.529 12.230 43.845 0.53 24.36 C ANISOU 447 C AILE A 54 3244 2766 3245 201 12 230 C ATOM 448 C BILE A 54 8.517 12.204 43.834 0.48 24.37 C ANISOU 448 C BILE A 54 3246 2766 3247 200 13 230 C ATOM 449 O AILE A 54 8.433 12.677 44.994 0.53 25.79 O ANISOU 449 O AILE A 54 3417 2991 3392 222 -13 247 O ATOM 450 O BILE A 54 8.390 12.589 45.005 0.48 25.79 O ANISOU 450 O BILE A 54 3418 2988 3393 223 -9 249 O ATOM 451 CB AILE A 54 10.893 11.651 43.053 0.53 28.37 C ANISOU 451 CB AILE A 54 3721 3280 3779 245 20 247 C ATOM 452 CB BILE A 54 10.811 11.764 42.846 0.48 28.14 C ANISOU 452 CB BILE A 54 3693 3248 3753 235 19 238 C ATOM 453 CG1AILE A 54 11.673 12.230 44.243 0.53 26.15 C ANISOU 453 CG1AILE A 54 3408 3067 3461 284 -21 268 C ATOM 454 CG1BILE A 54 11.893 10.696 42.679 0.48 26.54 C ANISOU 454 CG1BILE A 54 3485 3026 3574 277 52 270 C ATOM 455 CG2AILE A 54 10.755 12.695 41.955 0.53 26.26 C ANISOU 455 CG2AILE A 54 3447 3014 3515 193 -5 194 C ATOM 456 CG2BILE A 54 11.319 12.932 43.697 0.48 26.96 C ANISOU 456 CG2BILE A 54 3511 3167 3564 246 -37 234 C ATOM 457 CD1AILE A 54 13.044 12.775 43.870 0.53 31.51 C ANISOU 457 CD1AILE A 54 4050 3780 4142 292 -48 256 C ATOM 458 CD1BILE A 54 13.160 11.222 42.039 0.48 32.90 C ANISOU 458 CD1BILE A 54 4259 3856 4384 280 30 255 C ATOM 459 N ASN A 55 7.759 12.687 42.850 1.00 22.03 N ANISOU 459 N ASN A 55 2959 2448 2962 149 8 186 N ATOM 460 CA ASN A 55 6.755 13.708 43.129 1.00 25.69 C ANISOU 460 CA ASN A 55 3425 2934 3404 119 -21 162 C ATOM 461 C ASN A 55 5.541 13.118 43.832 1.00 26.74 C ANISOU 461 C ASN A 55 3579 3044 3538 119 5 180 C ATOM 462 O ASN A 55 4.947 13.768 44.702 1.00 27.02 O ANISOU 462 O ASN A 55 3612 3109 3544 119 -16 182 O ATOM 463 CB ASN A 55 6.345 14.403 41.835 1.00 23.52 C ANISOU 463 CB ASN A 55 3150 2646 3139 70 -33 115 C ATOM 464 CG ASN A 55 7.401 15.356 41.365 1.00 26.28 C ANISOU 464 CG ASN A 55 3476 3027 3482 68 -65 98 C ATOM 465 OD1 ASN A 55 7.591 16.398 41.973 1.00 23.73 O ANISOU 465 OD1 ASN A 55 3134 2745 3137 68 -101 93 O ATOM 466 ND2 ASN A 55 8.122 14.996 40.299 1.00 24.27 N ANISOU 466 ND2 ASN A 55 3219 2753 3249 65 -49 90 N ATOM 467 N PHE A 56 5.131 11.905 43.447 1.00 24.32 N ANISOU 467 N PHE A 56 3293 2682 3266 117 55 189 N ATOM 468 CA PHE A 56 4.003 11.291 44.140 1.00 25.10 C ANISOU 468 CA PHE A 56 3410 2755 3373 117 87 209 C ATOM 469 C PHE A 56 4.336 11.023 45.609 1.00 28.08 C ANISOU 469 C PHE A 56 3785 3160 3724 171 92 264 C ATOM 470 O PHE A 56 3.492 11.234 46.494 1.00 27.03 O ANISOU 470 O PHE A 56 3658 3041 3571 174 92 278 O ATOM 471 CB PHE A 56 3.572 9.997 43.444 1.00 26.52 C ANISOU 471 CB PHE A 56 3608 2864 3604 104 145 205 C ATOM 472 CG PHE A 56 2.493 9.299 44.185 1.00 32.83 C ANISOU 472 CG PHE A 56 4423 3632 4421 105 185 228 C ATOM 473 CD1 PHE A 56 1.191 9.718 44.077 1.00 33.79 C ANISOU 473 CD1 PHE A 56 4547 3747 4543 64 179 198 C ATOM 474 CD2 PHE A 56 2.796 8.279 45.068 1.00 37.02 C ANISOU 474 CD2 PHE A 56 4962 4140 4963 153 230 286 C ATOM 475 CE1 PHE A 56 0.191 9.099 44.832 1.00 30.28 C ANISOU 475 CE1 PHE A 56 4114 3273 4116 66 219 222 C ATOM 476 CE2 PHE A 56 1.810 7.671 45.786 1.00 40.50 C ANISOU 476 CE2 PHE A 56 5417 4550 5421 156 272 313 C ATOM 477 CZ PHE A 56 0.511 8.082 45.663 1.00 30.90 C ANISOU 477 CZ PHE A 56 4204 3327 4210 111 266 279 C ATOM 478 N ALEU A 57 5.554 10.551 45.893 0.42 27.13 N ANISOU 478 N ALEU A 57 3655 3053 3600 218 98 299 N ATOM 479 N BLEU A 57 5.554 10.546 45.887 0.58 27.11 N ANISOU 479 N BLEU A 57 3652 3050 3597 218 98 298 N ATOM 480 CA ALEU A 57 5.933 10.303 47.284 0.42 27.74 C ANISOU 480 CA ALEU A 57 3728 3168 3644 276 99 354 C ATOM 481 CA BLEU A 57 5.954 10.306 47.272 0.58 27.73 C ANISOU 481 CA BLEU A 57 3726 3166 3642 276 99 353 C ATOM 482 C ALEU A 57 5.953 11.594 48.096 0.42 29.29 C ANISOU 482 C ALEU A 57 3906 3437 3785 280 41 340 C ATOM 483 C BLEU A 57 5.939 11.595 48.086 0.58 29.30 C ANISOU 483 C BLEU A 57 3907 3437 3787 279 41 340 C ATOM 484 O ALEU A 57 5.603 11.593 49.285 0.42 28.99 O ANISOU 484 O ALEU A 57 3871 3430 3714 311 42 372 O ATOM 485 O BLEU A 57 5.556 11.591 49.266 0.58 28.98 O ANISOU 485 O BLEU A 57 3871 3426 3713 310 42 372 O ATOM 486 CB ALEU A 57 7.290 9.599 47.349 0.42 29.22 C ANISOU 486 CB ALEU A 57 3904 3361 3837 327 112 391 C ATOM 487 CB BLEU A 57 7.342 9.666 47.316 0.58 29.23 C ANISOU 487 CB BLEU A 57 3903 3365 3837 326 109 388 C ATOM 488 CG ALEU A 57 7.271 8.148 46.855 0.42 28.90 C ANISOU 488 CG ALEU A 57 3884 3246 3851 338 181 416 C ATOM 489 CG BLEU A 57 7.858 9.243 48.687 0.58 35.01 C ANISOU 489 CG BLEU A 57 4630 4139 4535 397 114 452 C ATOM 490 CD1ALEU A 57 8.677 7.583 46.747 0.42 33.71 C ANISOU 490 CD1ALEU A 57 4478 3860 4468 385 190 447 C ATOM 491 CD1BLEU A 57 6.902 8.246 49.328 0.58 32.12 C ANISOU 491 CD1BLEU A 57 4292 3729 4184 416 174 498 C ATOM 492 CD2ALEU A 57 6.420 7.283 47.778 0.42 34.71 C ANISOU 492 CD2ALEU A 57 4642 3952 4595 364 232 466 C ATOM 493 CD2BLEU A 57 9.251 8.656 48.569 0.58 34.79 C ANISOU 493 CD2BLEU A 57 4584 4120 4515 444 122 482 C ATOM 494 N THR A 58 6.365 12.708 47.478 1.00 25.44 N ANISOU 494 N THR A 58 3398 2977 3290 248 -6 293 N ATOM 495 CA THR A 58 6.353 13.989 48.185 1.00 25.22 C ANISOU 495 CA THR A 58 3353 3013 3218 245 -59 272 C ATOM 496 C THR A 58 4.930 14.408 48.539 1.00 30.65 C ANISOU 496 C THR A 58 4057 3693 3896 217 -57 259 C ATOM 497 O THR A 58 4.665 14.864 49.661 1.00 26.15 O ANISOU 497 O THR A 58 3484 3168 3285 238 -75 269 O ATOM 498 CB THR A 58 7.046 15.066 47.330 1.00 28.25 C ANISOU 498 CB THR A 58 3712 3414 3607 213 -100 224 C ATOM 499 OG1 THR A 58 8.409 14.680 47.123 1.00 28.10 O ANISOU 499 OG1 THR A 58 3673 3407 3596 243 -102 238 O ATOM 500 CG2 THR A 58 7.024 16.420 48.017 1.00 30.67 C ANISOU 500 CG2 THR A 58 3998 3778 3876 206 -150 195 C ATOM 501 N LEU A 59 4.005 14.260 47.584 1.00 26.92 N ANISOU 501 N LEU A 59 3602 3169 3458 172 -35 234 N ATOM 502 CA LEU A 59 2.592 14.532 47.839 1.00 29.52 C ANISOU 502 CA LEU A 59 3945 3486 3786 145 -27 223 C ATOM 503 C LEU A 59 2.055 13.650 48.959 1.00 28.58 C ANISOU 503 C LEU A 59 3842 3359 3657 181 12 273 C ATOM 504 O LEU A 59 1.380 14.124 49.881 1.00 34.81 O ANISOU 504 O LEU A 59 4633 4176 4415 188 3 279 O ATOM 505 CB LEU A 59 1.808 14.306 46.541 1.00 28.75 C ANISOU 505 CB LEU A 59 3859 3336 3731 94 -7 190 C ATOM 506 CG LEU A 59 0.306 14.528 46.496 1.00 41.48 C ANISOU 506 CG LEU A 59 5481 4929 5351 59 2 171 C ATOM 507 CD1 LEU A 59 -0.067 14.920 45.072 1.00 41.44 C ANISOU 507 CD1 LEU A 59 5473 4903 5369 10 -8 123 C ATOM 508 CD2 LEU A 59 -0.404 13.248 46.886 1.00 42.21 C ANISOU 508 CD2 LEU A 59 5592 4976 5471 69 59 203 C ATOM 509 N TYR A 60 2.361 12.359 48.899 1.00 26.15 N ANISOU 509 N TYR A 60 3546 3012 3378 207 59 311 N ATOM 510 CA TYR A 60 1.779 11.412 49.836 1.00 33.41 C ANISOU 510 CA TYR A 60 4483 3911 4300 240 108 363 C ATOM 511 C TYR A 60 2.290 11.656 51.247 1.00 34.48 C ANISOU 511 C TYR A 60 4611 4113 4376 299 90 405 C ATOM 512 O TYR A 60 1.511 11.684 52.209 1.00 31.65 O ANISOU 512 O TYR A 60 4262 3769 3994 314 103 428 O ATOM 513 CB TYR A 60 2.099 9.992 49.373 1.00 33.96 C ANISOU 513 CB TYR A 60 4565 3918 4419 254 167 393 C ATOM 514 CG TYR A 60 1.418 8.913 50.165 1.00 35.95 C ANISOU 514 CG TYR A 60 4837 4132 4690 283 231 448 C ATOM 515 CD1 TYR A 60 1.966 8.442 51.354 1.00 51.36 C ANISOU 515 CD1 TYR A 60 6792 6115 6610 352 248 515 C ATOM 516 CD2 TYR A 60 0.227 8.347 49.720 1.00 49.75 C ANISOU 516 CD2 TYR A 60 6599 5814 6489 242 277 433 C ATOM 517 CE1 TYR A 60 1.347 7.447 52.083 1.00 51.54 C ANISOU 517 CE1 TYR A 60 6833 6100 6651 382 314 571 C ATOM 518 CE2 TYR A 60 -0.397 7.342 50.440 1.00 47.12 C ANISOU 518 CE2 TYR A 60 6282 5439 6180 266 342 484 C ATOM 519 CZ TYR A 60 0.166 6.903 51.622 1.00 53.00 C ANISOU 519 CZ TYR A 60 7033 6213 6894 337 363 556 C ATOM 520 OH TYR A 60 -0.444 5.909 52.349 1.00 61.07 O ANISOU 520 OH TYR A 60 8072 7192 7941 366 434 614 O ATOM 521 N VAL A 61 3.601 11.853 51.387 1.00 28.37 N ANISOU 521 N VAL A 61 3818 3384 3578 332 58 411 N ATOM 522 CA VAL A 61 4.182 12.086 52.705 1.00 32.88 C ANISOU 522 CA VAL A 61 4376 4028 4088 392 34 445 C ATOM 523 C VAL A 61 3.616 13.358 53.319 1.00 29.45 C ANISOU 523 C VAL A 61 3934 3647 3609 374 -11 410 C ATOM 524 O VAL A 61 3.326 13.403 54.518 1.00 36.16 O ANISOU 524 O VAL A 61 4787 4539 4412 413 -10 439 O ATOM 525 CB VAL A 61 5.720 12.139 52.615 1.00 34.75 C ANISOU 525 CB VAL A 61 4587 4307 4312 425 3 449 C ATOM 526 CG1 VAL A 61 6.305 12.581 53.961 1.00 33.20 C ANISOU 526 CG1 VAL A 61 4370 4200 4044 481 -34 470 C ATOM 527 CG2 VAL A 61 6.288 10.773 52.239 1.00 34.73 C ANISOU 527 CG2 VAL A 61 4593 4255 4348 456 55 496 C ATOM 528 N THR A 62 3.465 14.416 52.514 1.00 29.87 N ANISOU 528 N THR A 62 3976 3698 3674 318 -49 347 N ATOM 529 CA THR A 62 2.998 15.690 53.055 1.00 33.12 C ANISOU 529 CA THR A 62 4379 4158 4049 301 -91 310 C ATOM 530 C THR A 62 1.562 15.586 53.568 1.00 36.40 C ANISOU 530 C THR A 62 4817 4553 4460 292 -61 322 C ATOM 531 O THR A 62 1.243 16.080 54.659 1.00 37.30 O ANISOU 531 O THR A 62 4930 4716 4526 315 -75 327 O ATOM 532 CB THR A 62 3.104 16.789 51.996 1.00 32.66 C ANISOU 532 CB THR A 62 4306 4092 4013 245 -128 246 C ATOM 533 OG1 THR A 62 4.461 16.897 51.542 1.00 31.75 O ANISOU 533 OG1 THR A 62 4166 3994 3903 254 -153 236 O ATOM 534 CG2 THR A 62 2.665 18.136 52.577 1.00 32.18 C ANISOU 534 CG2 THR A 62 4234 4076 3918 229 -169 207 C ATOM 535 N VAL A 63 0.684 14.942 52.795 1.00 36.57 N ANISOU 535 N VAL A 63 4857 4505 4532 258 -18 324 N ATOM 536 CA VAL A 63 -0.713 14.807 53.203 1.00 39.34 C ANISOU 536 CA VAL A 63 5227 4834 4889 244 14 334 C ATOM 537 C VAL A 63 -0.832 13.926 54.442 1.00 35.95 C ANISOU 537 C VAL A 63 4811 4416 4434 303 55 400 C ATOM 538 O VAL A 63 -1.672 14.172 55.317 1.00 44.04 O ANISOU 538 O VAL A 63 5844 5460 5430 313 65 412 O ATOM 539 CB VAL A 63 -1.541 14.268 52.022 1.00 39.36 C ANISOU 539 CB VAL A 63 5240 4761 4956 193 48 316 C ATOM 540 CG1 VAL A 63 -2.952 13.877 52.474 1.00 46.86 C ANISOU 540 CG1 VAL A 63 6204 5680 5919 183 92 333 C ATOM 541 CG2 VAL A 63 -1.600 15.320 50.919 1.00 41.26 C ANISOU 541 CG2 VAL A 63 5466 5001 5209 140 6 253 C ATOM 542 N GLN A 64 0.019 12.903 54.551 1.00 38.79 N ANISOU 542 N GLN A 64 5173 4765 4800 346 82 447 N ATOM 543 CA GLN A 64 -0.085 11.956 55.661 1.00 40.63 C ANISOU 543 CA GLN A 64 5422 5004 5013 407 130 519 C ATOM 544 C GLN A 64 0.307 12.580 56.995 1.00 47.51 C ANISOU 544 C GLN A 64 6283 5966 5802 461 95 536 C ATOM 545 O GLN A 64 -0.256 12.216 58.035 1.00 42.07 O ANISOU 545 O GLN A 64 5609 5293 5084 500 128 584 O ATOM 546 CB GLN A 64 0.778 10.717 55.397 1.00 37.51 C ANISOU 546 CB GLN A 64 5031 4574 4648 443 169 567 C ATOM 547 CG GLN A 64 1.273 10.061 56.678 1.00 52.71 C ANISOU 547 CG GLN A 64 6960 6541 6526 527 194 643 C ATOM 548 CD GLN A 64 1.323 8.552 56.600 1.00 58.21 C ANISOU 548 CD GLN A 64 7675 7170 7272 559 272 709 C ATOM 549 OE1 GLN A 64 1.524 7.979 55.530 1.00 59.99 O ANISOU 549 OE1 GLN A 64 7903 7330 7561 528 294 693 O ATOM 550 NE2 GLN A 64 1.132 7.895 57.740 1.00 70.47 N ANISOU 550 NE2 GLN A 64 9242 8738 8797 623 317 783 N ATOM 551 N HIS A 65 1.281 13.496 57.001 1.00 44.65 N ANISOU 551 N HIS A 65 5895 5666 5403 464 29 498 N ATOM 552 CA HIS A 65 1.862 14.004 58.244 1.00 41.09 C ANISOU 552 CA HIS A 65 5430 5309 4873 520 -8 508 C ATOM 553 C HIS A 65 1.370 15.423 58.524 1.00 43.68 C ANISOU 553 C HIS A 65 5748 5681 5168 486 -57 446 C ATOM 554 O HIS A 65 1.772 16.378 57.851 1.00 41.09 O ANISOU 554 O HIS A 65 5400 5361 4853 443 -105 384 O ATOM 555 CB HIS A 65 3.384 13.939 58.176 1.00 40.86 C ANISOU 555 CB HIS A 65 5375 5325 4827 554 -44 510 C ATOM 556 CG HIS A 65 3.913 12.541 58.114 1.00 43.05 C ANISOU 556 CG HIS A 65 5661 5568 5127 601 7 580 C ATOM 557 ND1 HIS A 65 4.144 11.784 59.242 1.00 50.46 N ANISOU 557 ND1 HIS A 65 6606 6546 6020 680 35 653 N ATOM 558 CD2 HIS A 65 4.243 11.757 57.060 1.00 38.84 C ANISOU 558 CD2 HIS A 65 5133 4965 4659 582 38 589 C ATOM 559 CE1 HIS A 65 4.605 10.596 58.885 1.00 55.31 C ANISOU 559 CE1 HIS A 65 7229 7112 6674 708 83 706 C ATOM 560 NE2 HIS A 65 4.668 10.552 57.565 1.00 38.50 N ANISOU 560 NE2 HIS A 65 5100 4916 4614 648 86 666 N ATOM 561 N LYS A 66 0.519 15.561 59.544 1.00 43.76 N ANISOU 561 N LYS A 66 5771 5718 5137 508 -42 464 N ATOM 562 CA LYS A 66 -0.097 16.847 59.857 1.00 40.29 C ANISOU 562 CA LYS A 66 5325 5312 4670 477 -79 407 C ATOM 563 C LYS A 66 0.905 17.869 60.372 1.00 36.90 C ANISOU 563 C LYS A 66 4865 4969 4185 494 -147 361 C ATOM 564 O LYS A 66 0.619 19.069 60.338 1.00 43.16 O ANISOU 564 O LYS A 66 5647 5780 4972 457 -184 298 O ATOM 565 CB LYS A 66 -1.215 16.661 60.889 1.00 51.66 C ANISOU 565 CB LYS A 66 6787 6763 6076 503 -41 442 C ATOM 566 N LYS A 67 2.077 17.433 60.827 1.00 38.97 N ANISOU 566 N LYS A 67 5111 5284 4412 549 -164 388 N ATOM 567 CA LYS A 67 3.100 18.380 61.250 1.00 42.85 C ANISOU 567 CA LYS A 67 5567 5858 4858 561 -231 337 C ATOM 568 C LYS A 67 3.690 19.171 60.085 1.00 46.35 C ANISOU 568 C LYS A 67 5986 6273 5353 500 -269 272 C ATOM 569 O LYS A 67 4.382 20.165 60.325 1.00 46.42 O ANISOU 569 O LYS A 67 5962 6338 5337 493 -323 215 O ATOM 570 CB LYS A 67 4.224 17.649 61.992 1.00 44.40 C ANISOU 570 CB LYS A 67 5746 6120 5003 638 -239 385 C ATOM 571 CG LYS A 67 4.893 16.542 61.193 1.00 45.91 C ANISOU 571 CG LYS A 67 5940 6260 5245 649 -208 432 C ATOM 572 N LEU A 68 3.437 18.762 58.837 1.00 40.19 N ANISOU 572 N LEU A 68 5218 5408 4644 455 -240 277 N ATOM 573 CA LEU A 68 4.080 19.390 57.674 1.00 39.29 C ANISOU 573 CA LEU A 68 5082 5267 4578 404 -270 225 C ATOM 574 C LEU A 68 3.152 20.453 57.081 1.00 40.27 C ANISOU 574 C LEU A 68 5213 5356 4733 340 -278 171 C ATOM 575 O LEU A 68 2.569 20.299 56.005 1.00 38.36 O ANISOU 575 O LEU A 68 4986 5044 4545 296 -253 168 O ATOM 576 CB LEU A 68 4.464 18.335 56.639 1.00 35.50 C ANISOU 576 CB LEU A 68 4612 4725 4153 400 -235 261 C ATOM 577 CG LEU A 68 5.439 17.228 57.074 1.00 36.56 C ANISOU 577 CG LEU A 68 4740 4884 4268 464 -221 319 C ATOM 578 CD1 LEU A 68 5.658 16.179 55.973 1.00 36.88 C ANISOU 578 CD1 LEU A 68 4793 4850 4370 454 -179 350 C ATOM 579 CD2 LEU A 68 6.767 17.817 57.478 1.00 45.77 C ANISOU 579 CD2 LEU A 68 5863 6128 5398 490 -277 291 C ATOM 580 N ARG A 69 3.037 21.573 57.807 1.00 36.41 N ANISOU 580 N ARG A 69 4709 4918 4207 336 -314 125 N ATOM 581 CA ARG A 69 2.122 22.638 57.408 1.00 38.10 C ANISOU 581 CA ARG A 69 4928 5103 4444 282 -320 76 C ATOM 582 C ARG A 69 2.756 24.032 57.495 1.00 37.08 C ANISOU 582 C ARG A 69 4766 5014 4310 259 -371 5 C ATOM 583 O ARG A 69 2.040 25.028 57.612 1.00 39.76 O ANISOU 583 O ARG A 69 5106 5348 4651 230 -380 -36 O ATOM 584 CB ARG A 69 0.834 22.558 58.240 1.00 43.24 C ANISOU 584 CB ARG A 69 5606 5758 5066 295 -293 96 C ATOM 585 CG ARG A 69 0.033 21.236 58.065 1.00 43.50 C ANISOU 585 CG ARG A 69 5670 5738 5119 307 -235 162 C ATOM 586 CD ARG A 69 -0.527 21.077 56.635 1.00 46.46 C ANISOU 586 CD ARG A 69 6056 6032 5565 251 -212 155 C ATOM 587 NE ARG A 69 -1.295 19.845 56.460 1.00 49.54 N ANISOU 587 NE ARG A 69 6473 6370 5982 257 -156 207 N ATOM 588 CZ ARG A 69 -0.770 18.668 56.142 1.00 46.93 C ANISOU 588 CZ ARG A 69 6148 6013 5671 278 -128 250 C ATOM 589 NH1 ARG A 69 0.527 18.527 55.914 1.00 43.00 N ANISOU 589 NH1 ARG A 69 5633 5536 5170 296 -151 250 N ATOM 590 NH2 ARG A 69 -1.563 17.604 56.061 1.00 39.39 N ANISOU 590 NH2 ARG A 69 5216 5008 4744 281 -73 294 N ATOM 591 N THR A 70 4.079 24.139 57.410 1.00 35.02 N ANISOU 591 N THR A 70 4473 4786 4048 270 -403 -13 N ATOM 592 CA THR A 70 4.704 25.443 57.235 1.00 32.63 C ANISOU 592 CA THR A 70 4136 4502 3760 238 -445 -84 C ATOM 593 C THR A 70 4.519 25.925 55.795 1.00 33.60 C ANISOU 593 C THR A 70 4260 4551 3954 179 -433 -103 C ATOM 594 O THR A 70 4.169 25.140 54.913 1.00 33.01 O ANISOU 594 O THR A 70 4209 4422 3912 169 -400 -64 O ATOM 595 CB THR A 70 6.193 25.366 57.564 1.00 40.08 C ANISOU 595 CB THR A 70 5039 5505 4686 267 -480 -96 C ATOM 596 OG1 THR A 70 6.857 24.609 56.547 1.00 37.45 O ANISOU 596 OG1 THR A 70 4704 5131 4395 263 -465 -64 O ATOM 597 CG2 THR A 70 6.417 24.700 58.909 1.00 41.29 C ANISOU 597 CG2 THR A 70 5191 5735 4764 334 -489 -64 C ATOM 598 N PRO A 71 4.728 27.223 55.529 1.00 34.12 N ANISOU 598 N PRO A 71 4303 4615 4045 141 -457 -164 N ATOM 599 CA PRO A 71 4.664 27.688 54.129 1.00 36.13 C ANISOU 599 CA PRO A 71 4558 4804 4365 92 -445 -177 C ATOM 600 C PRO A 71 5.584 26.922 53.184 1.00 32.00 C ANISOU 600 C PRO A 71 4028 4259 3872 94 -436 -149 C ATOM 601 O PRO A 71 5.180 26.630 52.055 1.00 30.34 O ANISOU 601 O PRO A 71 3837 3991 3700 69 -410 -129 O ATOM 602 CB PRO A 71 5.053 29.170 54.246 1.00 38.43 C ANISOU 602 CB PRO A 71 4818 5110 4674 62 -473 -246 C ATOM 603 CG PRO A 71 4.529 29.563 55.638 1.00 36.23 C ANISOU 603 CG PRO A 71 4540 4884 4341 84 -489 -270 C ATOM 604 CD PRO A 71 4.841 28.351 56.482 1.00 35.01 C ANISOU 604 CD PRO A 71 4393 4780 4131 140 -491 -224 C ATOM 605 N LEU A 72 6.795 26.559 53.616 1.00 30.39 N ANISOU 605 N LEU A 72 3796 4101 3651 124 -458 -148 N ATOM 606 CA LEU A 72 7.657 25.753 52.757 1.00 31.58 C ANISOU 606 CA LEU A 72 3941 4230 3830 131 -446 -118 C ATOM 607 C LEU A 72 6.991 24.427 52.401 1.00 33.77 C ANISOU 607 C LEU A 72 4258 4468 4107 147 -406 -56 C ATOM 608 O LEU A 72 7.050 23.986 51.245 1.00 30.33 O ANISOU 608 O LEU A 72 3832 3980 3710 128 -382 -40 O ATOM 609 CB LEU A 72 9.010 25.511 53.435 1.00 27.81 C ANISOU 609 CB LEU A 72 3424 3816 3327 169 -477 -122 C ATOM 610 CG LEU A 72 9.999 24.606 52.679 1.00 30.30 C ANISOU 610 CG LEU A 72 3729 4115 3668 184 -464 -88 C ATOM 611 CD1 LEU A 72 10.609 25.352 51.502 1.00 34.18 C ANISOU 611 CD1 LEU A 72 4198 4570 4219 139 -466 -122 C ATOM 612 CD2 LEU A 72 11.083 24.082 53.633 1.00 35.95 C ANISOU 612 CD2 LEU A 72 4413 4904 4343 239 -490 -75 C ATOM 613 N ASN A 73 6.354 23.770 53.380 1.00 32.14 N ANISOU 613 N ASN A 73 4072 4283 3855 183 -394 -23 N ATOM 614 CA ASN A 73 5.698 22.487 53.112 1.00 30.76 C ANISOU 614 CA ASN A 73 3933 4067 3687 198 -350 34 C ATOM 615 C ASN A 73 4.573 22.635 52.095 1.00 28.82 C ANISOU 615 C ASN A 73 3714 3756 3482 151 -323 28 C ATOM 616 O ASN A 73 4.396 21.772 51.225 1.00 28.58 O ANISOU 616 O ASN A 73 3701 3675 3482 143 -292 55 O ATOM 617 CB ASN A 73 5.131 21.873 54.405 1.00 30.84 C ANISOU 617 CB ASN A 73 3960 4112 3645 244 -338 71 C ATOM 618 CG ASN A 73 6.187 21.641 55.482 1.00 34.69 C ANISOU 618 CG ASN A 73 4422 4676 4082 300 -364 82 C ATOM 619 OD1 ASN A 73 5.933 21.893 56.664 1.00 32.04 O ANISOU 619 OD1 ASN A 73 4086 4396 3693 330 -379 80 O ATOM 620 ND2 ASN A 73 7.366 21.151 55.090 1.00 32.08 N ANISOU 620 ND2 ASN A 73 4071 4352 3766 318 -371 96 N ATOM 621 N TYR A 74 3.769 23.700 52.216 1.00 30.15 N ANISOU 621 N TYR A 74 3883 3923 3648 121 -335 -8 N ATOM 622 CA TYR A 74 2.698 23.938 51.251 1.00 29.10 C ANISOU 622 CA TYR A 74 3771 3735 3551 79 -314 -15 C ATOM 623 C TYR A 74 3.239 24.187 49.850 1.00 27.82 C ANISOU 623 C TYR A 74 3599 3537 3434 47 -314 -31 C ATOM 624 O TYR A 74 2.695 23.675 48.868 1.00 27.88 O ANISOU 624 O TYR A 74 3625 3499 3468 28 -288 -17 O ATOM 625 CB TYR A 74 1.858 25.136 51.685 1.00 30.08 C ANISOU 625 CB TYR A 74 3894 3870 3665 58 -328 -51 C ATOM 626 CG TYR A 74 0.806 24.793 52.704 1.00 35.99 C ANISOU 626 CG TYR A 74 4664 4632 4380 79 -312 -30 C ATOM 627 CD1 TYR A 74 -0.342 24.119 52.330 1.00 43.30 C ANISOU 627 CD1 TYR A 74 5616 5516 5321 68 -276 -3 C ATOM 628 CD2 TYR A 74 0.948 25.173 54.031 1.00 40.22 C ANISOU 628 CD2 TYR A 74 5190 5224 4867 108 -332 -42 C ATOM 629 CE1 TYR A 74 -1.320 23.814 53.260 1.00 51.00 C ANISOU 629 CE1 TYR A 74 6607 6500 6269 86 -257 18 C ATOM 630 CE2 TYR A 74 -0.022 24.873 54.964 1.00 46.53 C ANISOU 630 CE2 TYR A 74 6010 6038 5633 130 -313 -20 C ATOM 631 CZ TYR A 74 -1.152 24.197 54.574 1.00 45.65 C ANISOU 631 CZ TYR A 74 5924 5880 5542 118 -274 12 C ATOM 632 OH TYR A 74 -2.118 23.903 55.505 1.00 51.58 O ANISOU 632 OH TYR A 74 6693 6642 6264 139 -252 35 O ATOM 633 N AILE A 75 4.288 25.006 49.738 0.61 27.18 N ANISOU 633 N AILE A 75 3488 3477 3361 41 -342 -62 N ATOM 634 N BILE A 75 4.300 24.985 49.734 0.39 27.21 N ANISOU 634 N BILE A 75 3491 3481 3365 41 -342 -61 N ATOM 635 CA AILE A 75 4.852 25.330 48.429 0.61 27.05 C ANISOU 635 CA AILE A 75 3461 3429 3388 13 -339 -75 C ATOM 636 CA BILE A 75 4.820 25.325 48.414 0.39 27.05 C ANISOU 636 CA BILE A 75 3462 3428 3388 12 -339 -75 C ATOM 637 C AILE A 75 5.411 24.080 47.762 0.61 25.90 C ANISOU 637 C AILE A 75 3324 3262 3255 28 -317 -40 C ATOM 638 C BILE A 75 5.455 24.106 47.746 0.39 25.93 C ANISOU 638 C BILE A 75 3326 3266 3260 28 -318 -41 C ATOM 639 O AILE A 75 5.184 23.838 46.567 0.61 26.14 O ANISOU 639 O AILE A 75 3366 3251 3314 6 -297 -36 O ATOM 640 O BILE A 75 5.309 23.902 46.533 0.39 26.15 O ANISOU 640 O BILE A 75 3365 3254 3317 6 -299 -38 O ATOM 641 CB AILE A 75 5.925 26.426 48.571 0.61 27.77 C ANISOU 641 CB AILE A 75 3515 3548 3490 5 -370 -115 C ATOM 642 CB BILE A 75 5.787 26.518 48.531 0.39 27.85 C ANISOU 642 CB BILE A 75 3527 3555 3502 1 -369 -117 C ATOM 643 CG1AILE A 75 5.273 27.738 48.984 0.61 30.26 C ANISOU 643 CG1AILE A 75 3824 3869 3804 -18 -384 -154 C ATOM 644 CG1BILE A 75 4.969 27.802 48.692 0.39 30.14 C ANISOU 644 CG1BILE A 75 3816 3839 3796 -27 -377 -152 C ATOM 645 CG2AILE A 75 6.660 26.623 47.253 0.61 26.71 C ANISOU 645 CG2AILE A 75 3368 3382 3399 -18 -361 -120 C ATOM 646 CG2BILE A 75 6.687 26.615 47.306 0.39 26.74 C ANISOU 646 CG2BILE A 75 3370 3388 3401 -16 -362 -120 C ATOM 647 CD1AILE A 75 4.344 28.276 47.923 0.61 27.91 C ANISOU 647 CD1AILE A 75 3545 3523 3538 -53 -364 -157 C ATOM 648 CD1BILE A 75 5.471 28.747 49.760 0.39 27.34 C ANISOU 648 CD1BILE A 75 3432 3530 3426 -22 -408 -195 C ATOM 649 N LEU A 76 6.140 23.258 48.521 1.00 27.06 N ANISOU 649 N LEU A 76 3463 3439 3379 68 -320 -16 N ATOM 650 CA LEU A 76 6.684 22.030 47.947 1.00 28.39 C ANISOU 650 CA LEU A 76 3639 3584 3563 86 -295 19 C ATOM 651 C LEU A 76 5.581 21.047 47.569 1.00 29.17 C ANISOU 651 C LEU A 76 3775 3638 3671 81 -256 47 C ATOM 652 O LEU A 76 5.716 20.321 46.577 1.00 25.93 O ANISOU 652 O LEU A 76 3375 3188 3288 73 -231 58 O ATOM 653 CB LEU A 76 7.687 21.381 48.907 1.00 27.31 C ANISOU 653 CB LEU A 76 3484 3492 3399 136 -305 44 C ATOM 654 CG LEU A 76 9.158 21.766 48.681 1.00 29.00 C ANISOU 654 CG LEU A 76 3659 3733 3626 142 -330 26 C ATOM 655 CD1 LEU A 76 9.717 21.103 47.424 1.00 32.39 C ANISOU 655 CD1 LEU A 76 4092 4119 4094 135 -303 41 C ATOM 656 CD2 LEU A 76 9.325 23.278 48.573 1.00 28.09 C ANISOU 656 CD2 LEU A 76 3518 3633 3523 107 -361 -28 C ATOM 657 N LEU A 77 4.486 21.004 48.339 1.00 25.90 N ANISOU 657 N LEU A 77 3378 3227 3234 84 -249 55 N ATOM 658 CA LEU A 77 3.338 20.198 47.936 1.00 25.95 C ANISOU 658 CA LEU A 77 3415 3187 3256 72 -212 74 C ATOM 659 C LEU A 77 2.769 20.690 46.613 1.00 26.95 C ANISOU 659 C LEU A 77 3547 3278 3414 25 -208 45 C ATOM 660 O LEU A 77 2.463 19.892 45.719 1.00 26.64 O ANISOU 660 O LEU A 77 3523 3199 3400 13 -181 52 O ATOM 661 CB LEU A 77 2.257 20.227 49.027 1.00 26.48 C ANISOU 661 CB LEU A 77 3497 3269 3297 82 -205 85 C ATOM 662 CG LEU A 77 0.918 19.546 48.711 1.00 33.37 C ANISOU 662 CG LEU A 77 4395 4096 4188 63 -168 98 C ATOM 663 CD1 LEU A 77 1.097 18.081 48.336 1.00 33.75 C ANISOU 663 CD1 LEU A 77 4458 4105 4262 78 -127 132 C ATOM 664 CD2 LEU A 77 -0.015 19.664 49.929 1.00 34.35 C ANISOU 664 CD2 LEU A 77 4528 4240 4282 79 -162 112 C ATOM 665 N ASN A 78 2.649 22.009 46.461 1.00 25.08 N ANISOU 665 N ASN A 78 3298 3057 3176 2 -235 12 N ATOM 666 CA ASN A 78 2.168 22.574 45.207 1.00 26.55 C ANISOU 666 CA ASN A 78 3486 3215 3387 -36 -233 -11 C ATOM 667 C ASN A 78 3.105 22.235 44.044 1.00 24.09 C ANISOU 667 C ASN A 78 3168 2885 3098 -40 -226 -12 C ATOM 668 O ASN A 78 2.639 21.886 42.952 1.00 24.53 O ANISOU 668 O ASN A 78 3237 2910 3172 -60 -208 -16 O ATOM 669 CB ASN A 78 2.015 24.085 45.355 1.00 28.07 C ANISOU 669 CB ASN A 78 3664 3426 3576 -53 -260 -42 C ATOM 670 CG ASN A 78 1.322 24.715 44.161 1.00 27.68 C ANISOU 670 CG ASN A 78 3619 3352 3548 -86 -255 -58 C ATOM 671 OD1 ASN A 78 0.300 24.228 43.706 1.00 36.31 O ANISOU 671 OD1 ASN A 78 4729 4424 4644 -98 -237 -52 O ATOM 672 ND2 ASN A 78 1.892 25.789 43.649 1.00 31.59 N ANISOU 672 ND2 ASN A 78 4096 3850 4056 -99 -268 -78 N ATOM 673 N LEU A 79 4.428 22.295 44.264 1.00 25.14 N ANISOU 673 N LEU A 79 3281 3039 3232 -21 -238 -9 N ATOM 674 CA LEU A 79 5.376 21.930 43.204 1.00 24.03 C ANISOU 674 CA LEU A 79 3135 2882 3115 -22 -228 -8 C ATOM 675 C LEU A 79 5.247 20.461 42.809 1.00 22.80 C ANISOU 675 C LEU A 79 2999 2695 2968 -11 -194 16 C ATOM 676 O LEU A 79 5.394 20.112 41.629 1.00 24.12 O ANISOU 676 O LEU A 79 3174 2836 3156 -24 -177 11 O ATOM 677 CB LEU A 79 6.816 22.233 43.652 1.00 23.02 C ANISOU 677 CB LEU A 79 2975 2785 2986 -2 -248 -9 C ATOM 678 CG LEU A 79 7.118 23.730 43.777 1.00 27.56 C ANISOU 678 CG LEU A 79 3524 3381 3565 -20 -276 -41 C ATOM 679 CD1 LEU A 79 8.490 23.931 44.346 1.00 28.26 C ANISOU 679 CD1 LEU A 79 3578 3505 3655 0 -297 -47 C ATOM 680 CD2 LEU A 79 6.984 24.434 42.426 1.00 28.93 C ANISOU 680 CD2 LEU A 79 3699 3527 3766 -52 -267 -57 C ATOM 681 N ALA A 80 5.023 19.574 43.785 1.00 24.52 N ANISOU 681 N ALA A 80 3229 2916 3173 16 -182 43 N ATOM 682 CA ALA A 80 4.836 18.163 43.463 1.00 24.25 C ANISOU 682 CA ALA A 80 3214 2844 3155 26 -143 66 C ATOM 683 C ALA A 80 3.629 17.964 42.553 1.00 26.22 C ANISOU 683 C ALA A 80 3484 3058 3422 -9 -123 47 C ATOM 684 O ALA A 80 3.679 17.183 41.592 1.00 24.38 O ANISOU 684 O ALA A 80 3261 2792 3212 -18 -98 42 O ATOM 685 CB ALA A 80 4.697 17.345 44.754 1.00 24.26 C ANISOU 685 CB ALA A 80 3223 2854 3140 63 -128 103 C ATOM 686 N VAL A 81 2.535 18.677 42.825 1.00 21.90 N ANISOU 686 N VAL A 81 2939 2518 2862 -30 -136 33 N ATOM 687 CA VAL A 81 1.356 18.572 41.967 1.00 21.53 C ANISOU 687 CA VAL A 81 2906 2445 2829 -63 -123 12 C ATOM 688 C VAL A 81 1.652 19.111 40.568 1.00 20.31 C ANISOU 688 C VAL A 81 2745 2288 2683 -85 -132 -14 C ATOM 689 O VAL A 81 1.318 18.487 39.550 1.00 24.70 O ANISOU 689 O VAL A 81 3311 2819 3254 -101 -112 -28 O ATOM 690 CB VAL A 81 0.161 19.309 42.611 1.00 25.28 C ANISOU 690 CB VAL A 81 3382 2934 3289 -76 -136 5 C ATOM 691 CG1 VAL A 81 -1.013 19.359 41.636 1.00 27.20 C ANISOU 691 CG1 VAL A 81 3631 3158 3545 -110 -128 -20 C ATOM 692 CG2 VAL A 81 -0.233 18.624 43.932 1.00 23.41 C ANISOU 692 CG2 VAL A 81 3154 2697 3043 -52 -118 34 C ATOM 693 N ALA A 82 2.265 20.284 40.491 1.00 21.64 N ANISOU 693 N ALA A 82 2897 2482 2843 -86 -159 -22 N ATOM 694 CA ALA A 82 2.579 20.852 39.183 1.00 25.48 C ANISOU 694 CA ALA A 82 3378 2966 3336 -103 -162 -41 C ATOM 695 C ALA A 82 3.518 19.937 38.400 1.00 21.66 C ANISOU 695 C ALA A 82 2898 2466 2868 -93 -142 -36 C ATOM 696 O ALA A 82 3.348 19.749 37.190 1.00 23.86 O ANISOU 696 O ALA A 82 3183 2732 3152 -107 -130 -52 O ATOM 697 CB ALA A 82 3.205 22.235 39.348 1.00 21.95 C ANISOU 697 CB ALA A 82 2910 2543 2885 -104 -188 -47 C ATOM 698 N ASP A 83 4.515 19.369 39.081 1.00 21.72 N ANISOU 698 N ASP A 83 2899 2476 2880 -66 -137 -16 N ATOM 699 CA ASP A 83 5.434 18.419 38.450 1.00 22.39 C ANISOU 699 CA ASP A 83 2985 2541 2980 -52 -113 -8 C ATOM 700 C ASP A 83 4.686 17.213 37.894 1.00 24.88 C ANISOU 700 C ASP A 83 3323 2820 3309 -61 -80 -15 C ATOM 701 O ASP A 83 5.046 16.689 36.830 1.00 23.38 O ANISOU 701 O ASP A 83 3138 2612 3131 -65 -61 -27 O ATOM 702 CB ASP A 83 6.491 17.919 39.452 1.00 21.22 C ANISOU 702 CB ASP A 83 2826 2405 2834 -16 -113 20 C ATOM 703 CG ASP A 83 7.472 18.984 39.905 1.00 22.73 C ANISOU 703 CG ASP A 83 2988 2632 3017 -6 -144 20 C ATOM 704 OD1 ASP A 83 7.571 20.044 39.262 1.00 22.22 O ANISOU 704 OD1 ASP A 83 2912 2576 2956 -28 -158 -1 O ATOM 705 OD2 ASP A 83 8.166 18.740 40.950 1.00 22.23 O ANISOU 705 OD2 ASP A 83 2910 2591 2946 24 -153 40 O ATOM 706 N LEU A 84 3.668 16.719 38.617 1.00 22.35 N ANISOU 706 N LEU A 84 3015 2488 2989 -64 -71 -9 N ATOM 707 CA LEU A 84 2.943 15.558 38.111 1.00 23.05 C ANISOU 707 CA LEU A 84 3121 2538 3098 -77 -36 -20 C ATOM 708 C LEU A 84 2.126 15.917 36.879 1.00 23.92 C ANISOU 708 C LEU A 84 3234 2648 3205 -111 -42 -59 C ATOM 709 O LEU A 84 1.950 15.076 35.990 1.00 22.31 O ANISOU 709 O LEU A 84 3040 2420 3018 -122 -17 -82 O ATOM 710 CB LEU A 84 2.053 14.949 39.212 1.00 24.20 C ANISOU 710 CB LEU A 84 3277 2669 3250 -72 -20 -2 C ATOM 711 CG LEU A 84 2.787 14.180 40.334 1.00 27.00 C ANISOU 711 CG LEU A 84 3633 3016 3608 -31 -1 42 C ATOM 712 CD1 LEU A 84 1.885 13.978 41.583 1.00 32.46 C ANISOU 712 CD1 LEU A 84 4332 3708 4294 -22 8 66 C ATOM 713 CD2 LEU A 84 3.331 12.846 39.831 1.00 24.70 C ANISOU 713 CD2 LEU A 84 3352 2683 3350 -18 42 49 C ATOM 714 N PHE A 85 1.602 17.145 36.812 1.00 23.70 N ANISOU 714 N PHE A 85 3198 2650 3156 -125 -72 -70 N ATOM 715 CA PHE A 85 0.986 17.601 35.564 1.00 24.47 C ANISOU 715 CA PHE A 85 3296 2757 3246 -150 -80 -102 C ATOM 716 C PHE A 85 2.006 17.681 34.433 1.00 23.22 C ANISOU 716 C PHE A 85 3134 2603 3085 -144 -76 -109 C ATOM 717 O PHE A 85 1.690 17.363 33.278 1.00 24.31 O ANISOU 717 O PHE A 85 3278 2739 3220 -157 -67 -137 O ATOM 718 CB PHE A 85 0.313 18.962 35.770 1.00 25.49 C ANISOU 718 CB PHE A 85 3415 2916 3355 -160 -111 -103 C ATOM 719 CG PHE A 85 -1.083 18.850 36.317 1.00 28.41 C ANISOU 719 CG PHE A 85 3788 3282 3725 -175 -112 -110 C ATOM 720 CD1 PHE A 85 -2.137 18.525 35.478 1.00 34.70 C ANISOU 720 CD1 PHE A 85 4586 4076 4522 -198 -106 -140 C ATOM 721 CD2 PHE A 85 -1.330 19.017 37.670 1.00 32.87 C ANISOU 721 CD2 PHE A 85 4352 3849 4288 -166 -116 -89 C ATOM 722 CE1 PHE A 85 -3.433 18.404 35.977 1.00 43.77 C ANISOU 722 CE1 PHE A 85 5733 5221 5676 -214 -105 -148 C ATOM 723 CE2 PHE A 85 -2.634 18.898 38.178 1.00 38.00 C ANISOU 723 CE2 PHE A 85 5003 4494 4940 -179 -112 -94 C ATOM 724 CZ PHE A 85 -3.674 18.595 37.330 1.00 37.71 C ANISOU 724 CZ PHE A 85 4966 4453 4910 -204 -106 -123 C ATOM 725 N MET A 86 3.228 18.137 34.732 1.00 21.20 N ANISOU 725 N MET A 86 2869 2357 2830 -124 -84 -88 N ATOM 726 CA MET A 86 4.260 18.155 33.693 1.00 23.68 C ANISOU 726 CA MET A 86 3179 2673 3145 -117 -74 -92 C ATOM 727 C MET A 86 4.488 16.758 33.151 1.00 21.53 C ANISOU 727 C MET A 86 2921 2372 2890 -112 -41 -103 C ATOM 728 O MET A 86 4.530 16.544 31.935 1.00 25.03 O ANISOU 728 O MET A 86 3370 2814 3328 -120 -29 -126 O ATOM 729 CB MET A 86 5.574 18.721 34.240 1.00 20.06 C ANISOU 729 CB MET A 86 2703 2226 2692 -96 -84 -67 C ATOM 730 CG MET A 86 5.497 20.200 34.623 1.00 22.89 C ANISOU 730 CG MET A 86 3045 2611 3041 -102 -114 -63 C ATOM 731 SD MET A 86 7.105 20.802 35.249 1.00 27.54 S ANISOU 731 SD MET A 86 3606 3215 3643 -82 -125 -45 S ATOM 732 CE MET A 86 8.012 20.894 33.725 1.00 24.73 C ANISOU 732 CE MET A 86 3246 2854 3296 -81 -104 -49 C ATOM 733 N VAL A 87 4.596 15.782 34.047 1.00 22.27 N ANISOU 733 N VAL A 87 3019 2439 3001 -99 -23 -86 N ATOM 734 CA VAL A 87 4.997 14.434 33.653 1.00 21.06 C ANISOU 734 CA VAL A 87 2878 2252 2873 -91 14 -92 C ATOM 735 C VAL A 87 3.909 13.760 32.822 1.00 25.40 C ANISOU 735 C VAL A 87 3441 2782 3428 -118 32 -133 C ATOM 736 O VAL A 87 4.170 13.232 31.733 1.00 25.41 O ANISOU 736 O VAL A 87 3449 2773 3434 -122 51 -160 O ATOM 737 CB VAL A 87 5.341 13.616 34.911 1.00 22.11 C ANISOU 737 CB VAL A 87 3012 2362 3025 -65 32 -56 C ATOM 738 CG1 VAL A 87 5.397 12.137 34.593 1.00 27.31 C ANISOU 738 CG1 VAL A 87 3686 2974 3716 -60 78 -63 C ATOM 739 CG2 VAL A 87 6.663 14.127 35.506 1.00 23.51 C ANISOU 739 CG2 VAL A 87 3172 2564 3197 -34 16 -23 C ATOM 740 N PHE A 88 2.671 13.794 33.302 1.00 24.48 N ANISOU 740 N PHE A 88 3327 2663 3311 -137 24 -142 N ATOM 741 CA PHE A 88 1.607 13.065 32.619 1.00 25.03 C ANISOU 741 CA PHE A 88 3404 2715 3393 -165 42 -185 C ATOM 742 C PHE A 88 0.934 13.873 31.516 1.00 23.82 C ANISOU 742 C PHE A 88 3245 2598 3208 -187 15 -221 C ATOM 743 O PHE A 88 0.527 13.297 30.498 1.00 30.66 O ANISOU 743 O PHE A 88 4114 3459 4075 -204 28 -265 O ATOM 744 CB PHE A 88 0.590 12.584 33.659 1.00 26.12 C ANISOU 744 CB PHE A 88 3545 2829 3551 -174 53 -177 C ATOM 745 CG PHE A 88 1.119 11.460 34.496 1.00 26.76 C ANISOU 745 CG PHE A 88 3634 2866 3666 -152 92 -146 C ATOM 746 CD1 PHE A 88 1.480 10.265 33.906 1.00 38.40 C ANISOU 746 CD1 PHE A 88 5118 4298 5173 -152 132 -164 C ATOM 747 CD2 PHE A 88 1.311 11.617 35.850 1.00 36.14 C ANISOU 747 CD2 PHE A 88 4822 4057 4853 -128 88 -98 C ATOM 748 CE1 PHE A 88 2.002 9.226 34.663 1.00 39.43 C ANISOU 748 CE1 PHE A 88 5257 4386 5338 -126 173 -130 C ATOM 749 CE2 PHE A 88 1.836 10.588 36.607 1.00 36.61 C ANISOU 749 CE2 PHE A 88 4890 4081 4940 -100 126 -63 C ATOM 750 CZ PHE A 88 2.175 9.393 36.013 1.00 35.25 C ANISOU 750 CZ PHE A 88 4727 3862 4804 -99 169 -77 C ATOM 751 N GLY A 89 0.829 15.181 31.677 1.00 25.36 N ANISOU 751 N GLY A 89 3429 2830 3375 -184 -19 -204 N ATOM 752 CA GLY A 89 0.243 16.018 30.652 1.00 26.31 C ANISOU 752 CA GLY A 89 3544 2989 3464 -198 -42 -229 C ATOM 753 C GLY A 89 1.175 16.367 29.508 1.00 27.74 C ANISOU 753 C GLY A 89 3726 3189 3626 -185 -41 -233 C ATOM 754 O GLY A 89 0.736 16.417 28.349 1.00 26.57 O ANISOU 754 O GLY A 89 3578 3064 3454 -194 -44 -266 O ATOM 755 N GLY A 90 2.445 16.670 29.803 1.00 23.48 N ANISOU 755 N GLY A 90 3184 2645 3092 -163 -37 -200 N ATOM 756 CA GLY A 90 3.341 17.045 28.714 1.00 22.53 C ANISOU 756 CA GLY A 90 3062 2542 2955 -150 -32 -201 C ATOM 757 C GLY A 90 4.378 16.005 28.325 1.00 25.58 C ANISOU 757 C GLY A 90 3456 2904 3360 -137 0 -206 C ATOM 758 O GLY A 90 4.536 15.704 27.145 1.00 24.19 O ANISOU 758 O GLY A 90 3286 2735 3169 -136 14 -232 O ATOM 759 N PHE A 91 5.068 15.409 29.304 1.00 22.98 N ANISOU 759 N PHE A 91 3126 2544 3060 -123 14 -181 N ATOM 760 CA PHE A 91 6.207 14.548 28.964 1.00 21.18 C ANISOU 760 CA PHE A 91 2902 2294 2852 -104 45 -178 C ATOM 761 C PHE A 91 5.776 13.279 28.255 1.00 23.43 C ANISOU 761 C PHE A 91 3203 2551 3148 -115 76 -219 C ATOM 762 O PHE A 91 6.567 12.711 27.494 1.00 21.95 O ANISOU 762 O PHE A 91 3020 2353 2967 -103 102 -230 O ATOM 763 CB PHE A 91 7.013 14.163 30.214 1.00 21.18 C ANISOU 763 CB PHE A 91 2896 2272 2880 -82 52 -139 C ATOM 764 CG PHE A 91 7.801 15.273 30.808 1.00 22.07 C ANISOU 764 CG PHE A 91 2988 2411 2986 -68 27 -105 C ATOM 765 CD1 PHE A 91 7.710 16.577 30.322 1.00 23.13 C ANISOU 765 CD1 PHE A 91 3113 2578 3098 -77 4 -107 C ATOM 766 CD2 PHE A 91 8.638 15.016 31.885 1.00 25.98 C ANISOU 766 CD2 PHE A 91 3472 2899 3500 -44 29 -72 C ATOM 767 CE1 PHE A 91 8.457 17.604 30.883 1.00 24.84 C ANISOU 767 CE1 PHE A 91 3309 2813 3317 -68 -16 -81 C ATOM 768 CE2 PHE A 91 9.391 16.034 32.451 1.00 21.89 C ANISOU 768 CE2 PHE A 91 2931 2408 2979 -33 4 -49 C ATOM 769 CZ PHE A 91 9.290 17.326 31.963 1.00 26.20 C ANISOU 769 CZ PHE A 91 3467 2980 3508 -48 -18 -56 C ATOM 770 N THR A 92 4.558 12.785 28.518 1.00 21.60 N ANISOU 770 N THR A 92 2977 2306 2924 -138 76 -244 N ATOM 771 CA THR A 92 4.101 11.625 27.772 1.00 22.68 C ANISOU 771 CA THR A 92 3125 2417 3076 -153 105 -293 C ATOM 772 C THR A 92 4.030 11.934 26.273 1.00 24.80 C ANISOU 772 C THR A 92 3395 2722 3308 -160 99 -334 C ATOM 773 O THR A 92 4.342 11.069 25.450 1.00 24.18 O ANISOU 773 O THR A 92 3325 2626 3236 -159 128 -370 O ATOM 774 CB THR A 92 2.739 11.149 28.311 1.00 25.48 C ANISOU 774 CB THR A 92 3480 2752 3448 -180 105 -316 C ATOM 775 OG1 THR A 92 1.851 12.261 28.380 1.00 26.52 O ANISOU 775 OG1 THR A 92 3602 2927 3548 -194 66 -315 O ATOM 776 CG2 THR A 92 2.892 10.524 29.723 1.00 29.99 C ANISOU 776 CG2 THR A 92 4054 3280 4059 -168 126 -275 C ATOM 777 N THR A 93 3.676 13.169 25.901 1.00 24.57 N ANISOU 777 N THR A 93 3357 2742 3238 -162 64 -328 N ATOM 778 CA THR A 93 3.745 13.545 24.484 1.00 23.65 C ANISOU 778 CA THR A 93 3242 2666 3080 -159 60 -356 C ATOM 779 C THR A 93 5.201 13.743 24.019 1.00 23.12 C ANISOU 779 C THR A 93 3176 2599 3008 -131 78 -330 C ATOM 780 O THR A 93 5.542 13.357 22.898 1.00 23.07 O ANISOU 780 O THR A 93 3177 2604 2984 -124 97 -360 O ATOM 781 CB THR A 93 2.894 14.813 24.238 1.00 29.80 C ANISOU 781 CB THR A 93 4011 3495 3817 -165 22 -351 C ATOM 782 OG1 THR A 93 1.499 14.459 24.250 1.00 28.28 O ANISOU 782 OG1 THR A 93 3815 3309 3622 -192 9 -392 O ATOM 783 CG2 THR A 93 3.218 15.479 22.911 1.00 24.46 C ANISOU 783 CG2 THR A 93 3334 2866 3093 -150 19 -357 C ATOM 784 N THR A 94 6.082 14.335 24.854 1.00 23.96 N ANISOU 784 N THR A 94 3274 2698 3132 -114 74 -277 N ATOM 785 CA THR A 94 7.495 14.440 24.453 1.00 21.90 C ANISOU 785 CA THR A 94 3010 2436 2875 -89 94 -254 C ATOM 786 C THR A 94 8.074 13.065 24.140 1.00 22.27 C ANISOU 786 C THR A 94 3068 2446 2948 -80 134 -276 C ATOM 787 O THR A 94 8.813 12.886 23.163 1.00 24.28 O ANISOU 787 O THR A 94 3326 2707 3190 -66 156 -287 O ATOM 788 CB THR A 94 8.363 15.094 25.545 1.00 21.98 C ANISOU 788 CB THR A 94 3004 2439 2908 -74 84 -201 C ATOM 789 OG1 THR A 94 7.653 16.126 26.206 1.00 21.36 O ANISOU 789 OG1 THR A 94 2917 2380 2820 -86 50 -185 O ATOM 790 CG2 THR A 94 9.646 15.671 24.908 1.00 21.69 C ANISOU 790 CG2 THR A 94 2956 2416 2867 -53 97 -179 C ATOM 791 N LEU A 95 7.726 12.067 24.936 1.00 22.36 N ANISOU 791 N LEU A 95 3085 2416 2994 -88 147 -284 N ATOM 792 CA LEU A 95 8.296 10.739 24.720 1.00 22.75 C ANISOU 792 CA LEU A 95 3146 2423 3076 -78 190 -301 C ATOM 793 C LEU A 95 7.784 10.119 23.423 1.00 23.40 C ANISOU 793 C LEU A 95 3241 2511 3140 -93 207 -366 C ATOM 794 O LEU A 95 8.568 9.608 22.609 1.00 23.69 O ANISOU 794 O LEU A 95 3283 2539 3177 -79 238 -383 O ATOM 795 CB LEU A 95 7.968 9.842 25.923 1.00 22.80 C ANISOU 795 CB LEU A 95 3155 2380 3127 -81 205 -288 C ATOM 796 CG LEU A 95 8.292 8.348 25.776 1.00 27.54 C ANISOU 796 CG LEU A 95 3768 2925 3770 -75 256 -310 C ATOM 797 CD1 LEU A 95 9.783 8.112 25.500 1.00 27.24 C ANISOU 797 CD1 LEU A 95 3727 2878 3744 -40 282 -285 C ATOM 798 CD2 LEU A 95 7.862 7.575 27.023 1.00 30.31 C ANISOU 798 CD2 LEU A 95 4122 3229 4164 -75 272 -288 C ATOM 799 N TYR A 96 6.463 10.165 23.213 1.00 23.17 N ANISOU 799 N TYR A 96 3213 2497 3093 -122 188 -406 N ATOM 800 CA TYR A 96 5.870 9.589 22.010 1.00 23.60 C ANISOU 800 CA TYR A 96 3275 2565 3127 -139 198 -477 C ATOM 801 C TYR A 96 6.411 10.260 20.758 1.00 24.33 C ANISOU 801 C TYR A 96 3368 2709 3167 -121 193 -484 C ATOM 802 O TYR A 96 6.698 9.596 19.756 1.00 25.51 O ANISOU 802 O TYR A 96 3527 2860 3306 -117 220 -528 O ATOM 803 CB TYR A 96 4.354 9.749 22.069 1.00 24.35 C ANISOU 803 CB TYR A 96 3363 2680 3208 -171 169 -513 C ATOM 804 CG TYR A 96 3.641 8.901 21.070 1.00 38.34 C ANISOU 804 CG TYR A 96 5139 4456 4972 -193 182 -595 C ATOM 805 CD1 TYR A 96 3.544 7.522 21.242 1.00 32.06 C ANISOU 805 CD1 TYR A 96 4351 3601 4231 -209 222 -635 C ATOM 806 CD2 TYR A 96 3.073 9.469 19.945 1.00 38.51 C ANISOU 806 CD2 TYR A 96 5155 4544 4934 -198 155 -634 C ATOM 807 CE1 TYR A 96 2.893 6.737 20.317 1.00 39.39 C ANISOU 807 CE1 TYR A 96 5278 4532 5155 -233 234 -719 C ATOM 808 CE2 TYR A 96 2.411 8.696 19.012 1.00 44.01 C ANISOU 808 CE2 TYR A 96 5850 5252 5618 -218 162 -717 C ATOM 809 CZ TYR A 96 2.317 7.337 19.202 1.00 48.55 C ANISOU 809 CZ TYR A 96 6432 5766 6250 -238 201 -763 C ATOM 810 OH TYR A 96 1.654 6.583 18.261 1.00 51.89 O ANISOU 810 OH TYR A 96 6850 6201 6664 -262 209 -854 O ATOM 811 N THR A 97 6.524 11.589 20.803 1.00 23.33 N ANISOU 811 N THR A 97 3232 2625 3007 -110 163 -440 N ATOM 812 CA THR A 97 7.053 12.362 19.689 1.00 24.93 C ANISOU 812 CA THR A 97 3436 2877 3161 -89 162 -434 C ATOM 813 C THR A 97 8.502 11.988 19.389 1.00 23.59 C ANISOU 813 C THR A 97 3270 2685 3009 -63 200 -414 C ATOM 814 O THR A 97 8.861 11.737 18.237 1.00 26.85 O ANISOU 814 O THR A 97 3691 3118 3392 -50 221 -444 O ATOM 815 CB THR A 97 6.926 13.853 20.034 1.00 24.74 C ANISOU 815 CB THR A 97 3399 2887 3115 -83 128 -382 C ATOM 816 OG1 THR A 97 5.537 14.184 20.212 1.00 25.85 O ANISOU 816 OG1 THR A 97 3535 3051 3237 -106 94 -402 O ATOM 817 CG2 THR A 97 7.517 14.734 18.945 1.00 23.22 C ANISOU 817 CG2 THR A 97 3205 2740 2877 -58 133 -364 C ATOM 818 N ASER A 98 9.353 11.953 20.424 0.79 23.35 N ANISOU 818 N ASER A 98 3232 2617 3024 -51 208 -366 N ATOM 819 N BSER A 98 9.350 11.947 20.418 0.21 23.36 N ANISOU 819 N BSER A 98 3232 2617 3024 -51 209 -366 N ATOM 820 CA ASER A 98 10.763 11.618 20.217 0.79 24.33 C ANISOU 820 CA ASER A 98 3354 2720 3169 -24 244 -344 C ATOM 821 CA BSER A 98 10.755 11.619 20.196 0.21 24.11 C ANISOU 821 CA BSER A 98 3326 2693 3140 -24 244 -345 C ATOM 822 C ASER A 98 10.933 10.188 19.715 0.79 24.01 C ANISOU 822 C ASER A 98 3330 2645 3148 -23 285 -392 C ATOM 823 C BSER A 98 10.931 10.185 19.709 0.21 24.01 C ANISOU 823 C BSER A 98 3330 2645 3148 -23 285 -392 C ATOM 824 O ASER A 98 11.867 9.906 18.962 0.79 24.30 O ANISOU 824 O ASER A 98 3371 2681 3182 -2 316 -396 O ATOM 825 O BSER A 98 11.882 9.897 18.974 0.21 24.30 O ANISOU 825 O BSER A 98 3371 2681 3183 -1 317 -395 O ATOM 826 CB ASER A 98 11.557 11.824 21.512 0.79 23.22 C ANISOU 826 CB ASER A 98 3198 2552 3073 -12 240 -286 C ATOM 827 CB BSER A 98 11.553 11.847 21.476 0.21 23.22 C ANISOU 827 CB BSER A 98 3199 2554 3071 -12 240 -287 C ATOM 828 OG ASER A 98 11.407 13.142 22.018 0.79 22.81 O ANISOU 828 OG ASER A 98 3131 2530 3008 -16 204 -249 O ATOM 829 OG BSER A 98 11.035 11.049 22.520 0.21 23.18 O ANISOU 829 OG BSER A 98 3196 2508 3102 -24 239 -290 O ATOM 830 N LEU A 99 10.034 9.276 20.104 1.00 24.14 N ANISOU 830 N LEU A 99 3355 2629 3189 -46 288 -430 N ATOM 831 CA LEU A 99 10.123 7.886 19.630 1.00 24.67 C ANISOU 831 CA LEU A 99 3436 2655 3282 -49 331 -482 C ATOM 832 C LEU A 99 9.918 7.806 18.112 1.00 26.40 C ANISOU 832 C LEU A 99 3665 2915 3452 -51 339 -544 C ATOM 833 O LEU A 99 10.584 7.025 17.408 1.00 25.53 O ANISOU 833 O LEU A 99 3565 2787 3349 -37 380 -573 O ATOM 834 CB LEU A 99 9.073 7.022 20.353 1.00 24.76 C ANISOU 834 CB LEU A 99 3451 2623 3332 -78 334 -512 C ATOM 835 CG LEU A 99 9.347 6.592 21.802 1.00 30.37 C ANISOU 835 CG LEU A 99 4158 3280 4102 -70 346 -461 C ATOM 836 CD1 LEU A 99 8.098 5.985 22.469 1.00 33.74 C ANISOU 836 CD1 LEU A 99 4588 3674 4558 -101 344 -487 C ATOM 837 CD2 LEU A 99 10.491 5.597 21.855 1.00 28.68 C ANISOU 837 CD2 LEU A 99 3951 3016 3933 -42 397 -448 C ATOM 838 N HIS A 100 8.997 8.606 17.599 1.00 24.99 N ANISOU 838 N HIS A 100 3483 2794 3219 -65 301 -563 N ATOM 839 CA HIS A 100 8.623 8.610 16.190 1.00 25.43 C ANISOU 839 CA HIS A 100 3545 2901 3215 -65 300 -623 C ATOM 840 C HIS A 100 9.388 9.635 15.360 1.00 29.19 C ANISOU 840 C HIS A 100 4021 3432 3639 -34 299 -586 C ATOM 841 O HIS A 100 9.333 9.581 14.129 1.00 28.91 O ANISOU 841 O HIS A 100 3994 3441 3551 -24 307 -629 O ATOM 842 CB HIS A 100 7.110 8.839 16.091 1.00 25.43 C ANISOU 842 CB HIS A 100 3539 2938 3186 -96 261 -666 C ATOM 843 CG HIS A 100 6.316 7.641 16.502 1.00 27.81 C ANISOU 843 CG HIS A 100 3842 3189 3535 -129 273 -724 C ATOM 844 ND1 HIS A 100 6.103 6.566 15.660 1.00 30.68 N ANISOU 844 ND1 HIS A 100 4212 3543 3900 -142 300 -807 N ATOM 845 CD2 HIS A 100 5.730 7.321 17.678 1.00 30.37 C ANISOU 845 CD2 HIS A 100 4160 3467 3912 -152 268 -711 C ATOM 846 CE1 HIS A 100 5.410 5.642 16.300 1.00 33.72 C ANISOU 846 CE1 HIS A 100 4596 3875 4343 -173 313 -843 C ATOM 847 NE2 HIS A 100 5.167 6.077 17.524 1.00 35.08 N ANISOU 847 NE2 HIS A 100 4760 4023 4544 -179 295 -783 N ATOM 848 N GLY A 101 10.102 10.559 15.984 1.00 24.94 N ANISOU 848 N GLY A 101 3472 2892 3113 -17 290 -511 N ATOM 849 CA GLY A 101 10.814 11.572 15.211 1.00 26.02 C ANISOU 849 CA GLY A 101 3606 3075 3207 12 294 -474 C ATOM 850 C GLY A 101 9.983 12.746 14.722 1.00 24.98 C ANISOU 850 C GLY A 101 3469 3008 3014 12 258 -465 C ATOM 851 O GLY A 101 10.490 13.563 13.937 1.00 27.31 O ANISOU 851 O GLY A 101 3764 3344 3269 38 267 -436 O ATOM 852 N TYR A 102 8.722 12.846 15.130 1.00 24.68 N ANISOU 852 N TYR A 102 3427 2981 2969 -14 221 -487 N ATOM 853 CA TYR A 102 7.863 13.964 14.739 1.00 26.66 C ANISOU 853 CA TYR A 102 3672 3293 3165 -12 186 -475 C ATOM 854 C TYR A 102 6.593 13.935 15.579 1.00 26.20 C ANISOU 854 C TYR A 102 3606 3227 3123 -44 149 -493 C ATOM 855 O TYR A 102 6.284 12.947 16.253 1.00 25.42 O ANISOU 855 O TYR A 102 3508 3082 3069 -69 153 -524 O ATOM 856 CB TYR A 102 7.505 13.939 13.248 1.00 25.61 C ANISOU 856 CB TYR A 102 3547 3227 2957 4 188 -520 C ATOM 857 CG TYR A 102 6.463 12.918 12.836 1.00 29.72 C ANISOU 857 CG TYR A 102 4071 3760 3460 -20 177 -609 C ATOM 858 CD1 TYR A 102 6.774 11.554 12.770 1.00 28.38 C ANISOU 858 CD1 TYR A 102 3911 3546 3326 -33 208 -665 C ATOM 859 CD2 TYR A 102 5.169 13.322 12.467 1.00 26.81 C ANISOU 859 CD2 TYR A 102 3694 3452 3043 -30 137 -639 C ATOM 860 CE1 TYR A 102 5.813 10.610 12.366 1.00 27.88 C ANISOU 860 CE1 TYR A 102 3847 3492 3254 -60 201 -754 C ATOM 861 CE2 TYR A 102 4.218 12.394 12.052 1.00 30.16 C ANISOU 861 CE2 TYR A 102 4115 3892 3454 -55 126 -727 C ATOM 862 CZ TYR A 102 4.545 11.045 11.999 1.00 36.40 C ANISOU 862 CZ TYR A 102 4914 4633 4283 -71 159 -786 C ATOM 863 OH TYR A 102 3.591 10.117 11.606 1.00 34.94 O ANISOU 863 OH TYR A 102 4724 4459 4093 -100 150 -880 O ATOM 864 N PHE A 103 5.856 15.043 15.525 1.00 24.15 N ANISOU 864 N PHE A 103 3336 3012 2826 -42 116 -468 N ATOM 865 CA PHE A 103 4.631 15.198 16.307 1.00 23.89 C ANISOU 865 CA PHE A 103 3294 2978 2805 -69 80 -478 C ATOM 866 C PHE A 103 3.507 14.407 15.632 1.00 27.88 C ANISOU 866 C PHE A 103 3798 3514 3280 -88 66 -558 C ATOM 867 O PHE A 103 2.681 14.938 14.885 1.00 28.13 O ANISOU 867 O PHE A 103 3823 3612 3254 -82 40 -576 O ATOM 868 CB PHE A 103 4.288 16.679 16.471 1.00 25.76 C ANISOU 868 CB PHE A 103 3520 3250 3017 -57 53 -423 C ATOM 869 CG PHE A 103 4.907 17.304 17.709 1.00 24.73 C ANISOU 869 CG PHE A 103 3383 3075 2940 -59 53 -361 C ATOM 870 CD1 PHE A 103 4.327 17.118 18.939 1.00 23.71 C ANISOU 870 CD1 PHE A 103 3248 2911 2852 -84 34 -360 C ATOM 871 CD2 PHE A 103 6.100 18.022 17.627 1.00 22.97 C ANISOU 871 CD2 PHE A 103 3158 2845 2724 -34 74 -307 C ATOM 872 CE1 PHE A 103 4.880 17.679 20.098 1.00 27.98 C ANISOU 872 CE1 PHE A 103 3781 3416 3435 -84 32 -308 C ATOM 873 CE2 PHE A 103 6.672 18.568 18.756 1.00 23.72 C ANISOU 873 CE2 PHE A 103 3242 2902 2867 -38 71 -260 C ATOM 874 CZ PHE A 103 6.068 18.388 20.011 1.00 27.68 C ANISOU 874 CZ PHE A 103 3738 3374 3404 -62 49 -261 C ATOM 875 N VAL A 104 3.472 13.101 15.930 1.00 30.64 N ANISOU 875 N VAL A 104 4153 3815 3674 -112 86 -608 N ATOM 876 CA VAL A 104 2.424 12.232 15.390 1.00 30.40 C ANISOU 876 CA VAL A 104 4118 3804 3630 -137 77 -694 C ATOM 877 C VAL A 104 1.048 12.798 15.721 1.00 37.37 C ANISOU 877 C VAL A 104 4982 4720 4497 -156 33 -701 C ATOM 878 O VAL A 104 0.138 12.796 14.881 1.00 37.97 O ANISOU 878 O VAL A 104 5048 4857 4524 -161 10 -755 O ATOM 879 CB VAL A 104 2.576 10.797 15.937 1.00 34.32 C ANISOU 879 CB VAL A 104 4621 4225 4195 -163 110 -736 C ATOM 880 CG1 VAL A 104 1.481 9.882 15.360 1.00 43.13 C ANISOU 880 CG1 VAL A 104 5728 5356 5304 -195 104 -833 C ATOM 881 CG2 VAL A 104 3.930 10.229 15.606 1.00 35.38 C ANISOU 881 CG2 VAL A 104 4772 4325 4346 -142 154 -728 C ATOM 882 N PHE A 105 0.888 13.324 16.940 1.00 32.97 N ANISOU 882 N PHE A 105 4419 4129 3978 -165 21 -647 N ATOM 883 CA PHE A 105 -0.387 13.859 17.421 1.00 32.81 C ANISOU 883 CA PHE A 105 4382 4133 3953 -183 -17 -647 C ATOM 884 C PHE A 105 -0.728 15.216 16.837 1.00 37.77 C ANISOU 884 C PHE A 105 5000 4832 4517 -157 -47 -613 C ATOM 885 O PHE A 105 -1.732 15.797 17.258 1.00 37.73 O ANISOU 885 O PHE A 105 4981 4848 4507 -167 -78 -604 O ATOM 886 CB PHE A 105 -0.399 14.038 18.937 1.00 30.84 C ANISOU 886 CB PHE A 105 4131 3826 3763 -197 -18 -597 C ATOM 887 CG PHE A 105 -0.111 12.807 19.730 1.00 45.67 C ANISOU 887 CG PHE A 105 6016 5630 5708 -217 14 -614 C ATOM 888 CD1 PHE A 105 -0.497 11.550 19.291 1.00 49.40 C ANISOU 888 CD1 PHE A 105 6488 6083 6198 -240 33 -688 C ATOM 889 CD2 PHE A 105 0.528 12.927 20.968 1.00 43.36 C ANISOU 889 CD2 PHE A 105 5729 5284 5461 -212 25 -554 C ATOM 890 CE1 PHE A 105 -0.224 10.425 20.063 1.00 50.62 C ANISOU 890 CE1 PHE A 105 6651 6162 6421 -256 69 -696 C ATOM 891 CE2 PHE A 105 0.802 11.823 21.731 1.00 47.71 C ANISOU 891 CE2 PHE A 105 6287 5769 6072 -224 57 -560 C ATOM 892 CZ PHE A 105 0.417 10.571 21.292 1.00 55.20 C ANISOU 892 CZ PHE A 105 7237 6693 7043 -246 81 -628 C ATOM 893 N GLY A 106 0.088 15.773 15.951 1.00 34.17 N ANISOU 893 N GLY A 106 4555 4412 4017 -122 -36 -586 N ATOM 894 CA GLY A 106 -0.228 17.037 15.327 1.00 29.28 C ANISOU 894 CA GLY A 106 3928 3860 3337 -93 -58 -550 C ATOM 895 C GLY A 106 -0.116 18.221 16.271 1.00 30.92 C ANISOU 895 C GLY A 106 4131 4047 3569 -86 -67 -472 C ATOM 896 O GLY A 106 0.522 18.158 17.332 1.00 30.66 O ANISOU 896 O GLY A 106 4104 3952 3595 -96 -54 -440 O ATOM 897 N PRO A 107 -0.712 19.346 15.873 1.00 29.49 N ANISOU 897 N PRO A 107 3940 3921 3343 -64 -89 -442 N ATOM 898 CA PRO A 107 -0.653 20.546 16.720 1.00 25.26 C ANISOU 898 CA PRO A 107 3400 3366 2832 -57 -96 -372 C ATOM 899 C PRO A 107 -1.252 20.336 18.085 1.00 25.18 C ANISOU 899 C PRO A 107 3382 3308 2877 -91 -111 -376 C ATOM 900 O PRO A 107 -0.819 20.983 19.044 1.00 25.60 O ANISOU 900 O PRO A 107 3435 3322 2969 -92 -107 -326 O ATOM 901 CB PRO A 107 -1.450 21.583 15.913 1.00 35.38 C ANISOU 901 CB PRO A 107 4671 4720 4051 -28 -116 -353 C ATOM 902 CG PRO A 107 -1.316 21.132 14.503 1.00 30.74 C ANISOU 902 CG PRO A 107 4088 4191 3399 -5 -109 -390 C ATOM 903 CD PRO A 107 -1.276 19.631 14.535 1.00 32.13 C ANISOU 903 CD PRO A 107 4270 4341 3598 -37 -104 -464 C ATOM 904 N THR A 108 -2.243 19.452 18.218 1.00 26.01 N ANISOU 904 N THR A 108 3478 3416 2987 -120 -128 -435 N ATOM 905 CA THR A 108 -2.758 19.185 19.556 1.00 24.78 C ANISOU 905 CA THR A 108 3317 3212 2888 -151 -136 -435 C ATOM 906 C THR A 108 -1.656 18.651 20.461 1.00 24.10 C ANISOU 906 C THR A 108 3244 3054 2857 -159 -108 -414 C ATOM 907 O THR A 108 -1.533 19.075 21.616 1.00 26.20 O ANISOU 907 O THR A 108 3510 3286 3161 -164 -110 -374 O ATOM 908 CB THR A 108 -3.916 18.191 19.493 1.00 31.58 C ANISOU 908 CB THR A 108 4165 4082 3753 -182 -150 -505 C ATOM 909 OG1 THR A 108 -4.972 18.771 18.722 1.00 30.78 O ANISOU 909 OG1 THR A 108 4045 4053 3598 -172 -180 -522 O ATOM 910 CG2 THR A 108 -4.411 17.875 20.911 1.00 31.49 C ANISOU 910 CG2 THR A 108 4148 4015 3801 -212 -151 -499 C ATOM 911 N GLY A 109 -0.840 17.726 19.947 1.00 26.03 N ANISOU 911 N GLY A 109 3502 3282 3108 -157 -81 -440 N ATOM 912 CA GLY A 109 0.303 17.257 20.716 1.00 28.44 C ANISOU 912 CA GLY A 109 3817 3526 3461 -157 -54 -414 C ATOM 913 C GLY A 109 1.268 18.375 21.056 1.00 22.60 C ANISOU 913 C GLY A 109 3079 2782 2727 -133 -50 -348 C ATOM 914 O GLY A 109 1.759 18.464 22.180 1.00 23.29 O ANISOU 914 O GLY A 109 3166 2827 2857 -137 -46 -315 O ATOM 915 N CYS A 110 1.551 19.245 20.085 1.00 24.90 N ANISOU 915 N CYS A 110 3370 3116 2975 -108 -50 -327 N ATOM 916 CA CYS A 110 2.442 20.376 20.334 1.00 23.82 C ANISOU 916 CA CYS A 110 3230 2972 2848 -88 -42 -266 C ATOM 917 C CYS A 110 1.893 21.296 21.428 1.00 24.99 C ANISOU 917 C CYS A 110 3368 3110 3019 -97 -64 -233 C ATOM 918 O CYS A 110 2.639 21.741 22.313 1.00 23.79 O ANISOU 918 O CYS A 110 3211 2924 2904 -97 -59 -198 O ATOM 919 CB CYS A 110 2.642 21.127 19.013 1.00 22.75 C ANISOU 919 CB CYS A 110 3097 2888 2660 -58 -33 -250 C ATOM 920 SG CYS A 110 3.707 22.574 19.065 1.00 23.77 S ANISOU 920 SG CYS A 110 3220 3009 2803 -32 -14 -176 S ATOM 921 N ASN A 111 0.579 21.572 21.402 1.00 23.41 N ANISOU 921 N ASN A 111 3160 2938 2796 -106 -90 -249 N ATOM 922 CA ASN A 111 -0.043 22.377 22.454 1.00 22.99 C ANISOU 922 CA ASN A 111 3098 2875 2764 -115 -110 -223 C ATOM 923 C ASN A 111 0.094 21.722 23.823 1.00 23.18 C ANISOU 923 C ASN A 111 3122 2848 2838 -138 -110 -227 C ATOM 924 O ASN A 111 0.388 22.406 24.809 1.00 23.80 O ANISOU 924 O ASN A 111 3195 2904 2943 -138 -114 -194 O ATOM 925 CB ASN A 111 -1.529 22.611 22.145 1.00 24.69 C ANISOU 925 CB ASN A 111 3302 3131 2946 -121 -137 -244 C ATOM 926 CG ASN A 111 -1.749 23.640 21.061 1.00 29.00 C ANISOU 926 CG ASN A 111 3844 3730 3444 -91 -141 -221 C ATOM 927 OD1 ASN A 111 -0.866 24.448 20.773 1.00 27.14 O ANISOU 927 OD1 ASN A 111 3612 3493 3207 -68 -122 -178 O ATOM 928 ND2 ASN A 111 -2.945 23.628 20.457 1.00 29.62 N ANISOU 928 ND2 ASN A 111 3913 3860 3482 -89 -163 -248 N ATOM 929 N LEU A 112 -0.106 20.403 23.910 1.00 22.59 N ANISOU 929 N LEU A 112 3054 2755 2776 -155 -103 -267 N ATOM 930 CA LEU A 112 0.037 19.728 25.207 1.00 22.32 C ANISOU 930 CA LEU A 112 3021 2672 2787 -170 -98 -264 C ATOM 931 C LEU A 112 1.462 19.844 25.735 1.00 24.48 C ANISOU 931 C LEU A 112 3297 2915 3088 -156 -81 -229 C ATOM 932 O LEU A 112 1.681 20.132 26.917 1.00 22.52 O ANISOU 932 O LEU A 112 3044 2645 2866 -157 -87 -203 O ATOM 933 CB LEU A 112 -0.326 18.243 25.090 1.00 24.81 C ANISOU 933 CB LEU A 112 3343 2966 3117 -188 -84 -312 C ATOM 934 CG LEU A 112 -1.785 17.865 24.852 1.00 33.83 C ANISOU 934 CG LEU A 112 4478 4128 4249 -210 -99 -356 C ATOM 935 CD1 LEU A 112 -1.868 16.391 24.473 1.00 30.28 C ANISOU 935 CD1 LEU A 112 4034 3655 3818 -227 -76 -409 C ATOM 936 CD2 LEU A 112 -2.567 18.148 26.112 1.00 37.48 C ANISOU 936 CD2 LEU A 112 4931 4573 4735 -224 -112 -339 C ATOM 937 N GLU A 113 2.440 19.573 24.869 1.00 22.10 N ANISOU 937 N GLU A 113 3001 2616 2778 -141 -60 -230 N ATOM 938 CA GLU A 113 3.839 19.561 25.286 1.00 21.63 C ANISOU 938 CA GLU A 113 2941 2531 2748 -127 -43 -201 C ATOM 939 C GLU A 113 4.273 20.942 25.756 1.00 22.32 C ANISOU 939 C GLU A 113 3015 2625 2841 -118 -54 -159 C ATOM 940 O GLU A 113 4.877 21.088 26.831 1.00 24.73 O ANISOU 940 O GLU A 113 3312 2908 3177 -117 -57 -138 O ATOM 941 CB GLU A 113 4.713 19.066 24.118 1.00 22.83 C ANISOU 941 CB GLU A 113 3101 2689 2887 -111 -16 -212 C ATOM 942 CG GLU A 113 5.966 18.253 24.524 1.00 22.35 C ANISOU 942 CG GLU A 113 3041 2591 2861 -101 9 -203 C ATOM 943 CD GLU A 113 7.142 19.123 24.972 1.00 23.66 C ANISOU 943 CD GLU A 113 3192 2752 3048 -86 12 -159 C ATOM 944 OE1 GLU A 113 7.263 20.281 24.517 1.00 20.97 O ANISOU 944 OE1 GLU A 113 2843 2434 2691 -80 7 -138 O ATOM 945 OE2 GLU A 113 7.958 18.635 25.791 1.00 21.22 O ANISOU 945 OE2 GLU A 113 2876 2415 2771 -80 20 -145 O ATOM 946 N GLY A 114 3.968 21.976 24.964 1.00 20.61 N ANISOU 946 N GLY A 114 2795 2440 2596 -110 -59 -148 N ATOM 947 CA GLY A 114 4.366 23.327 25.336 1.00 20.87 C ANISOU 947 CA GLY A 114 2814 2473 2641 -103 -64 -111 C ATOM 948 C GLY A 114 3.603 23.861 26.539 1.00 21.80 C ANISOU 948 C GLY A 114 2926 2584 2775 -117 -88 -105 C ATOM 949 O GLY A 114 4.176 24.515 27.412 1.00 20.96 O ANISOU 949 O GLY A 114 2807 2461 2696 -118 -92 -84 O ATOM 950 N PHE A 115 2.307 23.588 26.604 1.00 21.86 N ANISOU 950 N PHE A 115 2938 2604 2765 -129 -105 -126 N ATOM 951 CA PHE A 115 1.492 24.162 27.671 1.00 21.18 C ANISOU 951 CA PHE A 115 2845 2514 2689 -141 -126 -120 C ATOM 952 C PHE A 115 1.923 23.636 29.037 1.00 21.79 C ANISOU 952 C PHE A 115 2920 2560 2798 -148 -129 -117 C ATOM 953 O PHE A 115 2.136 24.417 29.980 1.00 21.19 O ANISOU 953 O PHE A 115 2834 2477 2740 -148 -138 -100 O ATOM 954 CB PHE A 115 0.006 23.865 27.431 1.00 24.41 C ANISOU 954 CB PHE A 115 3256 2942 3074 -152 -141 -145 C ATOM 955 CG PHE A 115 -0.875 24.261 28.591 1.00 22.87 C ANISOU 955 CG PHE A 115 3056 2741 2893 -164 -159 -141 C ATOM 956 CD1 PHE A 115 -1.245 25.584 28.774 1.00 25.86 C ANISOU 956 CD1 PHE A 115 3425 3131 3269 -158 -169 -119 C ATOM 957 CD2 PHE A 115 -1.317 23.303 29.503 1.00 26.89 C ANISOU 957 CD2 PHE A 115 3569 3230 3419 -179 -161 -157 C ATOM 958 CE1 PHE A 115 -2.070 25.953 29.857 1.00 27.14 C ANISOU 958 CE1 PHE A 115 3583 3287 3444 -168 -184 -117 C ATOM 959 CE2 PHE A 115 -2.125 23.663 30.588 1.00 28.62 C ANISOU 959 CE2 PHE A 115 3783 3444 3648 -188 -175 -152 C ATOM 960 CZ PHE A 115 -2.492 24.989 30.764 1.00 28.50 C ANISOU 960 CZ PHE A 115 3758 3442 3628 -183 -187 -134 C ATOM 961 N PHE A 116 2.069 22.315 29.171 1.00 19.85 N ANISOU 961 N PHE A 116 2684 2298 2561 -152 -118 -135 N ATOM 962 CA PHE A 116 2.350 21.800 30.514 1.00 20.92 C ANISOU 962 CA PHE A 116 2818 2409 2722 -153 -120 -127 C ATOM 963 C PHE A 116 3.772 22.105 30.975 1.00 22.64 C ANISOU 963 C PHE A 116 3025 2617 2959 -139 -115 -104 C ATOM 964 O PHE A 116 4.013 22.227 32.187 1.00 22.88 O ANISOU 964 O PHE A 116 3048 2641 3004 -136 -125 -92 O ATOM 965 CB PHE A 116 2.040 20.308 30.578 1.00 23.71 C ANISOU 965 CB PHE A 116 3184 2741 3083 -160 -105 -148 C ATOM 966 CG PHE A 116 0.558 20.033 30.744 1.00 25.06 C ANISOU 966 CG PHE A 116 3358 2915 3247 -178 -113 -169 C ATOM 967 CD1 PHE A 116 -0.079 20.339 31.945 1.00 27.36 C ANISOU 967 CD1 PHE A 116 3646 3203 3547 -184 -126 -157 C ATOM 968 CD2 PHE A 116 -0.197 19.527 29.695 1.00 25.35 C ANISOU 968 CD2 PHE A 116 3399 2963 3269 -190 -109 -203 C ATOM 969 CE1 PHE A 116 -1.446 20.124 32.109 1.00 26.07 C ANISOU 969 CE1 PHE A 116 3482 3042 3381 -201 -132 -176 C ATOM 970 CE2 PHE A 116 -1.567 19.303 29.850 1.00 29.44 C ANISOU 970 CE2 PHE A 116 3915 3487 3785 -209 -118 -226 C ATOM 971 CZ PHE A 116 -2.190 19.598 31.064 1.00 28.61 C ANISOU 971 CZ PHE A 116 3805 3373 3692 -215 -128 -210 C ATOM 972 N ALA A 117 4.724 22.228 30.047 1.00 20.93 N ANISOU 972 N ALA A 117 2805 2404 2742 -128 -100 -99 N ATOM 973 CA ALA A 117 6.079 22.633 30.436 1.00 20.82 C ANISOU 973 CA ALA A 117 2776 2385 2752 -116 -96 -79 C ATOM 974 C ALA A 117 6.116 24.097 30.866 1.00 22.41 C ANISOU 974 C ALA A 117 2959 2594 2960 -120 -111 -66 C ATOM 975 O ALA A 117 6.771 24.451 31.855 1.00 22.39 O ANISOU 975 O ALA A 117 2940 2589 2978 -118 -121 -58 O ATOM 976 CB ALA A 117 7.048 22.383 29.268 1.00 22.11 C ANISOU 976 CB ALA A 117 2939 2548 2915 -104 -70 -77 C ATOM 977 N THR A 118 5.449 24.969 30.108 1.00 21.34 N ANISOU 977 N THR A 118 2827 2472 2810 -125 -111 -64 N ATOM 978 CA THR A 118 5.389 26.382 30.470 1.00 22.26 C ANISOU 978 CA THR A 118 2929 2591 2939 -128 -120 -52 C ATOM 979 C THR A 118 4.676 26.564 31.797 1.00 21.98 C ANISOU 979 C THR A 118 2891 2554 2908 -138 -144 -59 C ATOM 980 O THR A 118 5.139 27.306 32.670 1.00 20.84 O ANISOU 980 O THR A 118 2728 2405 2784 -141 -153 -56 O ATOM 981 CB THR A 118 4.650 27.158 29.376 1.00 23.35 C ANISOU 981 CB THR A 118 3072 2744 3055 -126 -113 -44 C ATOM 982 OG1 THR A 118 5.309 26.933 28.126 1.00 21.50 O ANISOU 982 OG1 THR A 118 2842 2515 2810 -113 -89 -37 O ATOM 983 CG2 THR A 118 4.609 28.669 29.684 1.00 22.12 C ANISOU 983 CG2 THR A 118 2902 2583 2920 -128 -114 -29 C ATOM 984 N LEU A 119 3.540 25.884 31.963 1.00 20.79 N ANISOU 984 N LEU A 119 2756 2408 2738 -145 -152 -71 N ATOM 985 CA LEU A 119 2.796 25.973 33.217 1.00 22.04 C ANISOU 985 CA LEU A 119 2912 2564 2896 -152 -171 -76 C ATOM 986 C LEU A 119 3.653 25.520 34.393 1.00 20.89 C ANISOU 986 C LEU A 119 2758 2412 2766 -146 -176 -73 C ATOM 987 O LEU A 119 3.725 26.195 35.430 1.00 23.68 O ANISOU 987 O LEU A 119 3100 2770 3128 -147 -191 -73 O ATOM 988 CB LEU A 119 1.521 25.131 33.121 1.00 24.68 C ANISOU 988 CB LEU A 119 3262 2902 3212 -160 -173 -89 C ATOM 989 CG LEU A 119 0.700 25.066 34.419 1.00 30.23 C ANISOU 989 CG LEU A 119 3967 3603 3917 -167 -186 -92 C ATOM 990 CD1 LEU A 119 -0.063 26.381 34.604 1.00 31.72 C ANISOU 990 CD1 LEU A 119 4148 3802 4103 -172 -199 -90 C ATOM 991 CD2 LEU A 119 -0.252 23.875 34.345 1.00 30.49 C ANISOU 991 CD2 LEU A 119 4013 3630 3942 -175 -180 -105 C ATOM 992 N GLY A 120 4.331 24.383 34.250 1.00 20.79 N ANISOU 992 N GLY A 120 2751 2391 2757 -136 -164 -72 N ATOM 993 CA GLY A 120 5.111 23.874 35.366 1.00 21.87 C ANISOU 993 CA GLY A 120 2879 2527 2904 -124 -169 -65 C ATOM 994 C GLY A 120 6.281 24.774 35.716 1.00 23.09 C ANISOU 994 C GLY A 120 3007 2690 3076 -119 -178 -61 C ATOM 995 O GLY A 120 6.575 25.007 36.893 1.00 22.28 O ANISOU 995 O GLY A 120 2890 2598 2976 -113 -195 -62 O ATOM 996 N GLY A 121 6.979 25.282 34.703 1.00 22.48 N ANISOU 996 N GLY A 121 2921 2609 3011 -120 -165 -59 N ATOM 997 CA GLY A 121 8.099 26.160 34.983 1.00 20.47 C ANISOU 997 CA GLY A 121 2637 2359 2782 -119 -169 -58 C ATOM 998 C GLY A 121 7.669 27.476 35.606 1.00 23.85 C ANISOU 998 C GLY A 121 3052 2792 3218 -132 -185 -68 C ATOM 999 O GLY A 121 8.343 27.999 36.500 1.00 23.12 O ANISOU 999 O GLY A 121 2935 2708 3143 -132 -200 -78 O ATOM 1000 N GLU A 122 6.531 28.019 35.161 1.00 20.19 N ANISOU 1000 N GLU A 122 2604 2324 2743 -142 -183 -68 N ATOM 1001 CA GLU A 122 6.053 29.273 35.743 1.00 21.34 C ANISOU 1001 CA GLU A 122 2740 2470 2900 -153 -194 -77 C ATOM 1002 C GLU A 122 5.464 29.086 37.139 1.00 20.20 C ANISOU 1002 C GLU A 122 2597 2338 2741 -154 -218 -89 C ATOM 1003 O GLU A 122 5.541 30.009 37.951 1.00 22.40 O ANISOU 1003 O GLU A 122 2859 2620 3033 -160 -230 -104 O ATOM 1004 CB GLU A 122 5.033 29.935 34.815 1.00 21.00 C ANISOU 1004 CB GLU A 122 2711 2421 2849 -159 -182 -68 C ATOM 1005 CG GLU A 122 5.709 30.646 33.613 1.00 19.57 C ANISOU 1005 CG GLU A 122 2520 2229 2687 -157 -157 -54 C ATOM 1006 CD GLU A 122 6.516 31.883 34.017 1.00 25.74 C ANISOU 1006 CD GLU A 122 3273 2997 3511 -165 -152 -59 C ATOM 1007 OE1 GLU A 122 6.154 32.530 35.011 1.00 27.93 O ANISOU 1007 OE1 GLU A 122 3542 3273 3798 -174 -167 -76 O ATOM 1008 OE2 GLU A 122 7.515 32.229 33.335 1.00 25.06 O ANISOU 1008 OE2 GLU A 122 3172 2900 3450 -163 -129 -50 O ATOM 1009 N ILE A 123 4.869 27.928 37.444 1.00 19.35 N ANISOU 1009 N ILE A 123 2509 2235 2609 -146 -221 -85 N ATOM 1010 CA ILE A 123 4.483 27.686 38.835 1.00 20.96 C ANISOU 1010 CA ILE A 123 2713 2451 2798 -141 -239 -91 C ATOM 1011 C ILE A 123 5.719 27.669 39.718 1.00 25.73 C ANISOU 1011 C ILE A 123 3294 3072 3411 -129 -252 -97 C ATOM 1012 O ILE A 123 5.717 28.212 40.833 1.00 24.98 O ANISOU 1012 O ILE A 123 3185 2994 3312 -128 -272 -112 O ATOM 1013 CB ILE A 123 3.670 26.388 38.969 1.00 19.93 C ANISOU 1013 CB ILE A 123 2607 2318 2646 -135 -233 -81 C ATOM 1014 CG1 ILE A 123 2.285 26.602 38.347 1.00 26.47 C ANISOU 1014 CG1 ILE A 123 3452 3139 3466 -149 -227 -83 C ATOM 1015 CG2 ILE A 123 3.576 25.957 40.465 1.00 26.64 C ANISOU 1015 CG2 ILE A 123 3456 3184 3481 -121 -246 -79 C ATOM 1016 CD1 ILE A 123 1.506 25.313 38.108 1.00 27.94 C ANISOU 1016 CD1 ILE A 123 3659 3316 3640 -149 -215 -79 C ATOM 1017 N ALA A 124 6.807 27.065 39.229 1.00 20.03 N ANISOU 1017 N ALA A 124 2562 2348 2700 -119 -243 -88 N ATOM 1018 CA ALA A 124 8.035 27.061 40.018 1.00 23.71 C ANISOU 1018 CA ALA A 124 2999 2834 3174 -106 -258 -94 C ATOM 1019 C ALA A 124 8.555 28.483 40.236 1.00 22.92 C ANISOU 1019 C ALA A 124 2869 2740 3101 -121 -269 -119 C ATOM 1020 O ALA A 124 8.920 28.850 41.357 1.00 24.26 O ANISOU 1020 O ALA A 124 3016 2935 3267 -117 -292 -139 O ATOM 1021 CB ALA A 124 9.089 26.175 39.335 1.00 24.05 C ANISOU 1021 CB ALA A 124 3038 2872 3229 -92 -242 -79 C ATOM 1022 N LEU A 125 8.600 29.301 39.177 1.00 20.00 N ANISOU 1022 N LEU A 125 2496 2347 2757 -138 -251 -120 N ATOM 1023 CA LEU A 125 9.151 30.654 39.318 1.00 21.27 C ANISOU 1023 CA LEU A 125 2626 2504 2953 -154 -253 -143 C ATOM 1024 C LEU A 125 8.294 31.497 40.254 1.00 25.95 C ANISOU 1024 C LEU A 125 3218 3102 3539 -165 -270 -165 C ATOM 1025 O LEU A 125 8.810 32.188 41.130 1.00 24.57 O ANISOU 1025 O LEU A 125 3014 2941 3380 -171 -287 -196 O ATOM 1026 CB LEU A 125 9.249 31.345 37.947 1.00 23.13 C ANISOU 1026 CB LEU A 125 2862 2710 3218 -167 -223 -130 C ATOM 1027 CG LEU A 125 9.665 32.817 37.933 1.00 25.17 C ANISOU 1027 CG LEU A 125 3092 2952 3522 -186 -214 -149 C ATOM 1028 CD1 LEU A 125 11.037 33.097 38.657 1.00 24.72 C ANISOU 1028 CD1 LEU A 125 2988 2907 3496 -190 -227 -178 C ATOM 1029 CD2 LEU A 125 9.706 33.344 36.473 1.00 25.41 C ANISOU 1029 CD2 LEU A 125 3128 2952 3575 -190 -176 -124 C ATOM 1030 N TRP A 126 6.970 31.456 40.085 1.00 25.05 N ANISOU 1030 N TRP A 126 3135 2979 3404 -167 -265 -154 N ATOM 1031 CA TRP A 126 6.144 32.269 40.980 1.00 28.97 C ANISOU 1031 CA TRP A 126 3632 3480 3895 -175 -278 -175 C ATOM 1032 C TRP A 126 6.119 31.709 42.408 1.00 25.38 C ANISOU 1032 C TRP A 126 3174 3059 3409 -161 -305 -189 C ATOM 1033 O TRP A 126 5.943 32.476 43.369 1.00 23.85 O ANISOU 1033 O TRP A 126 2968 2878 3215 -166 -320 -218 O ATOM 1034 CB TRP A 126 4.738 32.431 40.388 1.00 22.82 C ANISOU 1034 CB TRP A 126 2882 2684 3104 -180 -264 -158 C ATOM 1035 CG TRP A 126 4.719 33.403 39.236 1.00 23.94 C ANISOU 1035 CG TRP A 126 3021 2799 3277 -191 -240 -149 C ATOM 1036 CD1 TRP A 126 4.628 33.094 37.900 1.00 25.34 C ANISOU 1036 CD1 TRP A 126 3212 2965 3453 -187 -219 -122 C ATOM 1037 CD2 TRP A 126 4.819 34.837 39.308 1.00 25.89 C ANISOU 1037 CD2 TRP A 126 3249 3026 3562 -204 -230 -166 C ATOM 1038 NE1 TRP A 126 4.657 34.247 37.144 1.00 23.85 N ANISOU 1038 NE1 TRP A 126 3016 2754 3294 -194 -197 -115 N ATOM 1039 CE2 TRP A 126 4.766 35.327 37.984 1.00 24.42 C ANISOU 1039 CE2 TRP A 126 3067 2816 3395 -205 -201 -140 C ATOM 1040 CE3 TRP A 126 4.939 35.754 40.367 1.00 26.99 C ANISOU 1040 CE3 TRP A 126 3367 3166 3721 -215 -241 -201 C ATOM 1041 CZ2 TRP A 126 4.831 36.688 37.688 1.00 26.90 C ANISOU 1041 CZ2 TRP A 126 3368 3102 3752 -215 -178 -143 C ATOM 1042 CZ3 TRP A 126 4.999 37.108 40.068 1.00 27.57 C ANISOU 1042 CZ3 TRP A 126 3426 3208 3840 -229 -220 -210 C ATOM 1043 CH2 TRP A 126 4.944 37.564 38.742 1.00 24.07 C ANISOU 1043 CH2 TRP A 126 2988 2737 3420 -228 -187 -179 C ATOM 1044 N SER A 127 6.344 30.396 42.580 1.00 23.87 N ANISOU 1044 N SER A 127 2994 2884 3192 -141 -308 -168 N ATOM 1045 CA SER A 127 6.549 29.845 43.921 1.00 23.05 C ANISOU 1045 CA SER A 127 2884 2816 3057 -120 -331 -175 C ATOM 1046 C SER A 127 7.788 30.423 44.596 1.00 25.57 C ANISOU 1046 C SER A 127 3161 3163 3390 -118 -353 -206 C ATOM 1047 O SER A 127 7.791 30.642 45.814 1.00 25.05 O ANISOU 1047 O SER A 127 3084 3132 3302 -108 -377 -229 O ATOM 1048 CB SER A 127 6.655 28.319 43.871 1.00 25.02 C ANISOU 1048 CB SER A 127 3151 3071 3283 -96 -324 -141 C ATOM 1049 OG SER A 127 5.413 27.742 43.531 1.00 23.53 O ANISOU 1049 OG SER A 127 2998 2863 3081 -99 -307 -121 O ATOM 1050 N LEU A 128 8.859 30.662 43.837 1.00 24.22 N ANISOU 1050 N LEU A 128 2967 2981 3255 -126 -345 -209 N ATOM 1051 CA LEU A 128 10.041 31.269 44.444 1.00 23.59 C ANISOU 1051 CA LEU A 128 2842 2927 3196 -129 -366 -245 C ATOM 1052 C LEU A 128 9.768 32.707 44.873 1.00 26.96 C ANISOU 1052 C LEU A 128 3250 3348 3646 -154 -372 -288 C ATOM 1053 O LEU A 128 10.373 33.191 45.843 1.00 28.11 O ANISOU 1053 O LEU A 128 3361 3526 3792 -154 -398 -330 O ATOM 1054 CB LEU A 128 11.235 31.217 43.478 1.00 25.47 C ANISOU 1054 CB LEU A 128 3054 3149 3472 -134 -350 -238 C ATOM 1055 CG LEU A 128 11.661 29.813 43.016 1.00 26.72 C ANISOU 1055 CG LEU A 128 3227 3312 3614 -108 -341 -198 C ATOM 1056 CD1 LEU A 128 12.791 29.926 41.978 1.00 29.26 C ANISOU 1056 CD1 LEU A 128 3525 3615 3978 -115 -321 -193 C ATOM 1057 CD2 LEU A 128 12.133 28.979 44.216 1.00 31.09 C ANISOU 1057 CD2 LEU A 128 3768 3915 4132 -75 -368 -197 C ATOM 1058 N VAL A 129 8.869 33.399 44.172 1.00 23.35 N ANISOU 1058 N VAL A 129 2814 2850 3207 -174 -349 -282 N ATOM 1059 CA VAL A 129 8.487 34.750 44.593 1.00 33.84 C ANISOU 1059 CA VAL A 129 4130 4167 4560 -196 -350 -321 C ATOM 1060 C VAL A 129 7.789 34.695 45.948 1.00 26.34 C ANISOU 1060 C VAL A 129 3189 3253 3568 -184 -376 -342 C ATOM 1061 O VAL A 129 8.092 35.475 46.853 1.00 28.86 O ANISOU 1061 O VAL A 129 3480 3592 3894 -192 -394 -391 O ATOM 1062 CB VAL A 129 7.600 35.416 43.521 1.00 29.93 C ANISOU 1062 CB VAL A 129 3658 3623 4091 -212 -317 -300 C ATOM 1063 CG1 VAL A 129 7.005 36.754 44.031 1.00 27.85 C ANISOU 1063 CG1 VAL A 129 3388 3343 3851 -230 -313 -335 C ATOM 1064 CG2 VAL A 129 8.409 35.638 42.216 1.00 25.67 C ANISOU 1064 CG2 VAL A 129 3106 3051 3595 -221 -288 -281 C ATOM 1065 N VAL A 130 6.859 33.752 46.108 1.00 23.69 N ANISOU 1065 N VAL A 130 2890 2926 3187 -165 -375 -309 N ATOM 1066 CA VAL A 130 6.162 33.578 47.385 1.00 27.52 C ANISOU 1066 CA VAL A 130 3385 3446 3626 -149 -395 -321 C ATOM 1067 C VAL A 130 7.153 33.263 48.501 1.00 28.43 C ANISOU 1067 C VAL A 130 3470 3616 3714 -129 -427 -346 C ATOM 1068 O VAL A 130 7.092 33.848 49.589 1.00 28.71 O ANISOU 1068 O VAL A 130 3491 3685 3733 -127 -448 -387 O ATOM 1069 CB VAL A 130 5.083 32.483 47.269 1.00 25.85 C ANISOU 1069 CB VAL A 130 3215 3230 3376 -132 -383 -275 C ATOM 1070 CG1 VAL A 130 4.422 32.246 48.634 1.00 30.24 C ANISOU 1070 CG1 VAL A 130 3782 3824 3885 -112 -399 -283 C ATOM 1071 CG2 VAL A 130 4.033 32.849 46.232 1.00 34.09 C ANISOU 1071 CG2 VAL A 130 4283 4228 4441 -150 -356 -256 C ATOM 1072 N LEU A 131 8.092 32.340 48.254 1.00 28.84 N ANISOU 1072 N LEU A 131 3512 3684 3762 -111 -431 -323 N ATOM 1073 CA LEU A 131 9.056 31.991 49.298 1.00 27.96 C ANISOU 1073 CA LEU A 131 3370 3632 3622 -86 -464 -342 C ATOM 1074 C LEU A 131 9.996 33.147 49.615 1.00 32.50 C ANISOU 1074 C LEU A 131 3894 4223 4231 -107 -483 -404 C ATOM 1075 O LEU A 131 10.411 33.307 50.769 1.00 29.81 O ANISOU 1075 O LEU A 131 3526 3939 3861 -92 -516 -442 O ATOM 1076 CB LEU A 131 9.863 30.750 48.902 1.00 25.14 C ANISOU 1076 CB LEU A 131 3011 3285 3257 -60 -460 -300 C ATOM 1077 CG LEU A 131 9.107 29.420 48.977 1.00 31.02 C ANISOU 1077 CG LEU A 131 3798 4027 3961 -30 -445 -245 C ATOM 1078 CD1 LEU A 131 9.912 28.310 48.297 1.00 34.57 C ANISOU 1078 CD1 LEU A 131 4247 4469 4419 -12 -432 -206 C ATOM 1079 CD2 LEU A 131 8.835 29.041 50.414 1.00 35.19 C ANISOU 1079 CD2 LEU A 131 4329 4611 4431 4 -466 -245 C ATOM 1080 N ALA A 132 10.377 33.944 48.615 1.00 28.25 N ANISOU 1080 N ALA A 132 3340 3639 3756 -140 -463 -417 N ATOM 1081 CA ALA A 132 11.269 35.069 48.908 1.00 31.12 C ANISOU 1081 CA ALA A 132 3652 4010 4161 -165 -477 -480 C ATOM 1082 C ALA A 132 10.579 36.090 49.807 1.00 30.92 C ANISOU 1082 C ALA A 132 3625 3993 4131 -179 -488 -531 C ATOM 1083 O ALA A 132 11.197 36.648 50.726 1.00 30.87 O ANISOU 1083 O ALA A 132 3578 4028 4125 -183 -516 -592 O ATOM 1084 CB ALA A 132 11.733 35.737 47.612 1.00 30.27 C ANISOU 1084 CB ALA A 132 3532 3844 4127 -197 -443 -476 C ATOM 1085 N ILE A 133 9.300 36.351 49.531 1.00 29.57 N ANISOU 1085 N ILE A 133 3495 3784 3957 -186 -464 -511 N ATOM 1086 CA ILE A 133 8.493 37.239 50.369 1.00 31.11 C ANISOU 1086 CA ILE A 133 3694 3983 4143 -196 -470 -553 C ATOM 1087 C ILE A 133 8.349 36.664 51.772 1.00 32.60 C ANISOU 1087 C ILE A 133 3884 4243 4259 -163 -505 -568 C ATOM 1088 O ILE A 133 8.541 37.368 52.772 1.00 36.68 O ANISOU 1088 O ILE A 133 4374 4796 4767 -167 -528 -630 O ATOM 1089 CB ILE A 133 7.125 37.475 49.704 1.00 34.31 C ANISOU 1089 CB ILE A 133 4145 4336 4557 -205 -436 -518 C ATOM 1090 CG1 ILE A 133 7.310 38.271 48.409 1.00 34.14 C ANISOU 1090 CG1 ILE A 133 4116 4249 4606 -234 -401 -509 C ATOM 1091 CG2 ILE A 133 6.141 38.143 50.667 1.00 31.98 C ANISOU 1091 CG2 ILE A 133 3861 4050 4240 -206 -441 -552 C ATOM 1092 CD1 ILE A 133 6.022 38.341 47.566 1.00 37.40 C ANISOU 1092 CD1 ILE A 133 4572 4617 5022 -236 -369 -463 C ATOM 1093 N GLU A 134 8.031 35.369 51.868 1.00 30.96 N ANISOU 1093 N GLU A 134 3707 4058 3999 -129 -507 -512 N ATOM 1094 CA GLU A 134 7.899 34.733 53.181 1.00 34.53 C ANISOU 1094 CA GLU A 134 4163 4579 4379 -90 -535 -514 C ATOM 1095 C GLU A 134 9.186 34.845 53.996 1.00 32.85 C ANISOU 1095 C GLU A 134 3898 4431 4152 -78 -575 -563 C ATOM 1096 O GLU A 134 9.156 35.206 55.178 1.00 36.19 O ANISOU 1096 O GLU A 134 4306 4910 4535 -65 -602 -609 O ATOM 1097 CB GLU A 134 7.485 33.266 53.010 1.00 33.70 C ANISOU 1097 CB GLU A 134 4094 4477 4232 -56 -523 -440 C ATOM 1098 CG GLU A 134 7.183 32.513 54.321 1.00 33.90 C ANISOU 1098 CG GLU A 134 4132 4568 4182 -11 -541 -426 C ATOM 1099 CD GLU A 134 8.379 31.733 54.852 1.00 37.92 C ANISOU 1099 CD GLU A 134 4612 5138 4657 27 -568 -419 C ATOM 1100 OE1 GLU A 134 9.467 31.836 54.253 1.00 41.00 O ANISOU 1100 OE1 GLU A 134 4969 5522 5087 14 -576 -431 O ATOM 1101 OE2 GLU A 134 8.241 31.020 55.875 1.00 40.83 O ANISOU 1101 OE2 GLU A 134 4989 5562 4961 71 -581 -398 O ATOM 1102 N ARG A 135 10.334 34.547 53.380 1.00 30.18 N ANISOU 1102 N ARG A 135 3531 4093 3845 -80 -579 -555 N ATOM 1103 CA ARG A 135 11.606 34.642 54.100 1.00 32.98 C ANISOU 1103 CA ARG A 135 3829 4512 4189 -69 -618 -602 C ATOM 1104 C ARG A 135 11.884 36.071 54.536 1.00 40.70 C ANISOU 1104 C ARG A 135 4765 5494 5204 -105 -633 -691 C ATOM 1105 O ARG A 135 12.368 36.313 55.653 1.00 42.17 O ANISOU 1105 O ARG A 135 4916 5752 5354 -91 -672 -748 O ATOM 1106 CB ARG A 135 12.751 34.138 53.221 1.00 38.30 C ANISOU 1106 CB ARG A 135 4477 5174 4900 -69 -613 -577 C ATOM 1107 CG ARG A 135 12.767 32.638 52.979 1.00 37.95 C ANISOU 1107 CG ARG A 135 4462 5139 4818 -27 -605 -500 C ATOM 1108 CD ARG A 135 13.150 31.869 54.230 1.00 36.00 C ANISOU 1108 CD ARG A 135 4202 4980 4498 26 -640 -495 C ATOM 1109 NE ARG A 135 11.990 31.544 55.052 1.00 37.25 N ANISOU 1109 NE ARG A 135 4402 5157 4594 51 -638 -474 N ATOM 1110 CZ ARG A 135 12.059 31.185 56.328 1.00 39.04 C ANISOU 1110 CZ ARG A 135 4619 5463 4749 96 -668 -480 C ATOM 1111 NH1 ARG A 135 13.214 31.137 56.969 1.00 37.82 N ANISOU 1111 NH1 ARG A 135 4414 5383 4574 120 -708 -511 N ATOM 1112 NH2 ARG A 135 10.940 30.870 56.974 1.00 43.15 N ANISOU 1112 NH2 ARG A 135 5182 5993 5219 118 -658 -454 N ATOM 1113 N TYR A 136 11.587 37.032 53.661 1.00 32.89 N ANISOU 1113 N TYR A 136 3780 4430 4285 -150 -600 -706 N ATOM 1114 CA TYR A 136 11.833 38.433 53.973 1.00 38.55 C ANISOU 1114 CA TYR A 136 4459 5137 5052 -189 -605 -790 C ATOM 1115 C TYR A 136 10.955 38.902 55.129 1.00 51.57 C ANISOU 1115 C TYR A 136 6122 6819 6655 -181 -620 -833 C ATOM 1116 O TYR A 136 11.414 39.648 56.002 1.00 47.99 O ANISOU 1116 O TYR A 136 5626 6406 6201 -192 -648 -914 O ATOM 1117 CB TYR A 136 11.594 39.282 52.727 1.00 40.26 C ANISOU 1117 CB TYR A 136 4683 5259 5354 -232 -558 -782 C ATOM 1118 CG TYR A 136 11.402 40.744 53.017 1.00 44.28 C ANISOU 1118 CG TYR A 136 5171 5738 5915 -271 -547 -856 C ATOM 1119 CD1 TYR A 136 12.484 41.550 53.345 1.00 49.45 C ANISOU 1119 CD1 TYR A 136 5762 6407 6619 -299 -563 -935 C ATOM 1120 CD2 TYR A 136 10.143 41.319 52.970 1.00 50.61 C ANISOU 1120 CD2 TYR A 136 6012 6496 6721 -280 -520 -849 C ATOM 1121 CE1 TYR A 136 12.319 42.887 53.615 1.00 47.76 C ANISOU 1121 CE1 TYR A 136 5527 6159 6459 -336 -549 -1008 C ATOM 1122 CE2 TYR A 136 9.965 42.667 53.238 1.00 58.41 C ANISOU 1122 CE2 TYR A 136 6980 7450 7761 -314 -506 -917 C ATOM 1123 CZ TYR A 136 11.063 43.442 53.556 1.00 55.94 C ANISOU 1123 CZ TYR A 136 6607 7148 7500 -343 -519 -997 C ATOM 1124 OH TYR A 136 10.913 44.780 53.827 1.00 65.51 O ANISOU 1124 OH TYR A 136 7798 8323 8772 -379 -501 -1069 O ATOM 1125 N VAL A 137 9.687 38.476 55.150 1.00 42.92 N ANISOU 1125 N VAL A 137 5082 5706 5519 -163 -601 -782 N ATOM 1126 CA VAL A 137 8.812 38.788 56.279 1.00 45.34 C ANISOU 1126 CA VAL A 137 5406 6048 5774 -150 -613 -814 C ATOM 1127 C VAL A 137 9.339 38.156 57.565 1.00 50.95 C ANISOU 1127 C VAL A 137 6095 6860 6403 -106 -660 -835 C ATOM 1128 O VAL A 137 9.486 38.831 58.593 1.00 53.46 O ANISOU 1128 O VAL A 137 6386 7229 6699 -107 -687 -910 O ATOM 1129 CB VAL A 137 7.376 38.324 55.982 1.00 48.58 C ANISOU 1129 CB VAL A 137 5878 6420 6159 -137 -581 -747 C ATOM 1130 CG1 VAL A 137 6.566 38.266 57.273 1.00 51.70 C ANISOU 1130 CG1 VAL A 137 6292 6869 6483 -108 -596 -764 C ATOM 1131 CG2 VAL A 137 6.719 39.239 54.963 1.00 41.79 C ANISOU 1131 CG2 VAL A 137 5033 5472 5372 -177 -540 -743 C ATOM 1132 N VAL A 138 9.633 36.852 57.528 1.00 47.65 N ANISOU 1132 N VAL A 138 5690 6476 5940 -66 -668 -769 N ATOM 1133 CA VAL A 138 9.986 36.126 58.749 1.00 41.87 C ANISOU 1133 CA VAL A 138 4945 5842 5120 -14 -707 -771 C ATOM 1134 C VAL A 138 11.301 36.639 59.327 1.00 55.23 C ANISOU 1134 C VAL A 138 6570 7600 6817 -18 -752 -851 C ATOM 1135 O VAL A 138 11.407 36.905 60.529 1.00 55.99 O ANISOU 1135 O VAL A 138 6643 7774 6856 3 -787 -906 O ATOM 1136 CB VAL A 138 10.049 34.609 58.480 1.00 53.49 C ANISOU 1136 CB VAL A 138 6445 7325 6554 30 -698 -678 C ATOM 1137 CG1 VAL A 138 10.679 33.875 59.667 1.00 51.55 C ANISOU 1137 CG1 VAL A 138 6177 7184 6225 89 -739 -677 C ATOM 1138 CG2 VAL A 138 8.666 34.055 58.197 1.00 49.64 C ANISOU 1138 CG2 VAL A 138 6022 6790 6050 39 -659 -610 C ATOM 1139 N VAL A 139 12.324 36.778 58.485 1.00 50.79 N ANISOU 1139 N VAL A 139 5969 7009 6319 -44 -751 -859 N ATOM 1140 CA VAL A 139 13.650 37.116 58.992 1.00 53.58 C ANISOU 1140 CA VAL A 139 6252 7428 6678 -46 -795 -930 C ATOM 1141 C VAL A 139 13.728 38.592 59.375 1.00 63.05 C ANISOU 1141 C VAL A 139 7413 8620 7922 -94 -804 -1037 C ATOM 1142 O VAL A 139 14.280 38.947 60.424 1.00 65.66 O ANISOU 1142 O VAL A 139 7697 9033 8217 -84 -848 -1114 O ATOM 1143 CB VAL A 139 14.726 36.741 57.959 1.00 53.52 C ANISOU 1143 CB VAL A 139 6215 7391 6728 -58 -787 -901 C ATOM 1144 CG1 VAL A 139 16.113 37.139 58.459 1.00 56.15 C ANISOU 1144 CG1 VAL A 139 6468 7792 7075 -63 -832 -978 C ATOM 1145 CG2 VAL A 139 14.665 35.248 57.644 1.00 51.19 C ANISOU 1145 CG2 VAL A 139 5957 7105 6389 -9 -776 -799 C ATOM 1146 N CYS A 140 13.194 39.479 58.525 1.00 63.79 N ANISOU 1146 N CYS A 140 7524 8617 8096 -144 -761 -1046 N ATOM 1147 CA CYS A 140 13.323 40.916 58.758 1.00 61.95 C ANISOU 1147 CA CYS A 140 7254 8362 7923 -193 -760 -1146 C ATOM 1148 C CYS A 140 12.233 41.486 59.656 1.00 73.20 C ANISOU 1148 C CYS A 140 8707 9799 9308 -190 -759 -1186 C ATOM 1149 O CYS A 140 12.404 42.596 60.173 1.00 81.37 O ANISOU 1149 O CYS A 140 9706 10838 10374 -222 -768 -1283 O ATOM 1150 CB CYS A 140 13.325 41.674 57.431 1.00 57.42 C ANISOU 1150 CB CYS A 140 6681 7676 7459 -247 -708 -1137 C ATOM 1151 SG CYS A 140 14.824 41.432 56.447 1.00 66.60 S ANISOU 1151 SG CYS A 140 7792 8822 8691 -265 -707 -1124 S ATOM 1152 N LYS A 141 11.132 40.764 59.850 1.00 71.62 N ANISOU 1152 N LYS A 141 8568 9603 9042 -154 -747 -1116 N ATOM 1153 CA LYS A 141 10.044 41.178 60.729 1.00 75.80 C ANISOU 1153 CA LYS A 141 9127 10148 9525 -143 -744 -1144 C ATOM 1154 C LYS A 141 9.629 42.636 60.505 1.00 85.84 C ANISOU 1154 C LYS A 141 10391 11347 10876 -197 -714 -1213 C ATOM 1155 O LYS A 141 9.631 43.437 61.444 1.00 90.54 O ANISOU 1155 O LYS A 141 10962 11980 11460 -206 -733 -1303 O ATOM 1156 CB LYS A 141 10.421 40.949 62.186 1.00 78.99 C ANISOU 1156 CB LYS A 141 9504 10671 9837 -103 -797 -1197 C ATOM 1157 CG LYS A 141 10.665 39.498 62.555 1.00 78.14 C ANISOU 1157 CG LYS A 141 9410 10637 9641 -40 -821 -1122 C ATOM 1158 CD LYS A 141 11.290 39.388 63.938 1.00 87.33 C ANISOU 1158 CD LYS A 141 10534 11927 10720 1 -878 -1183 C ATOM 1159 CE LYS A 141 11.451 37.937 64.365 1.00 92.65 C ANISOU 1159 CE LYS A 141 11226 12675 11303 72 -896 -1099 C ATOM 1160 NZ LYS A 141 12.235 37.146 63.375 1.00 85.59 N ANISOU 1160 NZ LYS A 141 10321 11750 10449 73 -888 -1034 N ATOM 1161 N PRO A 142 9.268 43.015 59.265 1.00 85.08 N ANISOU 1161 N PRO A 142 10316 11149 10862 -232 -666 -1172 N ATOM 1162 CA PRO A 142 8.917 44.419 59.026 1.00 88.68 C ANISOU 1162 CA PRO A 142 10764 11532 11400 -280 -632 -1232 C ATOM 1163 C PRO A 142 7.543 44.787 59.585 1.00 90.14 C ANISOU 1163 C PRO A 142 10992 11705 11551 -270 -614 -1235 C ATOM 1164 O PRO A 142 7.415 45.821 60.243 1.00 94.35 O ANISOU 1164 O PRO A 142 11506 12237 12104 -290 -613 -1322 O ATOM 1165 CB PRO A 142 8.929 44.519 57.500 1.00 85.94 C ANISOU 1165 CB PRO A 142 10429 11087 11135 -307 -586 -1168 C ATOM 1166 CG PRO A 142 8.506 43.169 57.054 1.00 76.57 C ANISOU 1166 CG PRO A 142 9289 9913 9891 -268 -585 -1064 C ATOM 1167 CD PRO A 142 9.080 42.193 58.055 1.00 76.89 C ANISOU 1167 CD PRO A 142 9314 10058 9843 -225 -637 -1069 C ATOM 1168 N ARG A 147 2.459 37.994 60.669 1.00 74.57 N ANISOU 1168 N ARG A 147 9304 9864 9164 -17 -575 -749 N ATOM 1169 CA ARG A 147 3.334 36.853 60.424 1.00 78.60 C ANISOU 1169 CA ARG A 147 9807 10403 9653 8 -591 -700 C ATOM 1170 C ARG A 147 2.768 35.954 59.331 1.00 77.47 C ANISOU 1170 C ARG A 147 9700 10199 9536 6 -557 -613 C ATOM 1171 O ARG A 147 1.560 35.708 59.273 1.00 80.68 O ANISOU 1171 O ARG A 147 10145 10578 9934 11 -527 -573 O ATOM 1172 CB ARG A 147 3.546 36.051 61.710 1.00 75.92 C ANISOU 1172 CB ARG A 147 9468 10159 9220 65 -617 -691 C ATOM 1173 N PHE A 148 3.657 35.461 58.472 1.00 73.45 N ANISOU 1173 N PHE A 148 9177 9673 9060 -1 -560 -587 N ATOM 1174 CA PHE A 148 3.292 34.624 57.330 1.00 60.82 C ANISOU 1174 CA PHE A 148 7605 8015 7487 -6 -530 -514 C ATOM 1175 C PHE A 148 2.860 33.254 57.838 1.00 60.93 C ANISOU 1175 C PHE A 148 7649 8060 7441 40 -522 -448 C ATOM 1176 O PHE A 148 3.694 32.402 58.154 1.00 61.39 O ANISOU 1176 O PHE A 148 7696 8163 7466 72 -538 -426 O ATOM 1177 CB PHE A 148 4.472 34.524 56.371 1.00 57.29 C ANISOU 1177 CB PHE A 148 7131 7547 7088 -24 -537 -512 C ATOM 1178 CG PHE A 148 4.087 34.242 54.950 1.00 48.63 C ANISOU 1178 CG PHE A 148 6057 6377 6042 -47 -504 -463 C ATOM 1179 CD1 PHE A 148 3.651 32.985 54.572 1.00 50.23 C ANISOU 1179 CD1 PHE A 148 6291 6567 6225 -26 -485 -395 C ATOM 1180 CD2 PHE A 148 4.177 35.231 53.986 1.00 51.33 C ANISOU 1180 CD2 PHE A 148 6387 6664 6452 -89 -491 -487 C ATOM 1181 CE1 PHE A 148 3.298 32.721 53.253 1.00 45.23 C ANISOU 1181 CE1 PHE A 148 5676 5873 5635 -48 -458 -357 C ATOM 1182 CE2 PHE A 148 3.819 34.972 52.668 1.00 50.26 C ANISOU 1182 CE2 PHE A 148 6273 6470 6356 -106 -461 -442 C ATOM 1183 CZ PHE A 148 3.380 33.712 52.309 1.00 43.52 C ANISOU 1183 CZ PHE A 148 5449 5609 5476 -86 -448 -380 C ATOM 1184 N GLY A 149 1.548 33.033 57.921 1.00 61.78 N ANISOU 1184 N GLY A 149 7793 8143 7535 43 -493 -416 N ATOM 1185 CA GLY A 149 0.994 31.786 58.415 1.00 55.03 C ANISOU 1185 CA GLY A 149 6969 7309 6632 84 -476 -353 C ATOM 1186 C GLY A 149 0.439 30.910 57.309 1.00 52.63 C ANISOU 1186 C GLY A 149 6692 6943 6363 72 -442 -291 C ATOM 1187 O GLY A 149 0.718 31.106 56.120 1.00 49.97 O ANISOU 1187 O GLY A 149 6349 6557 6081 39 -437 -291 O ATOM 1188 N GLU A 150 -0.367 29.923 57.714 1.00 48.65 N ANISOU 1188 N GLU A 150 6217 6441 5826 100 -416 -238 N ATOM 1189 CA GLU A 150 -0.938 28.988 56.750 1.00 53.26 C ANISOU 1189 CA GLU A 150 6825 6968 6442 90 -382 -183 C ATOM 1190 C GLU A 150 -1.837 29.704 55.756 1.00 45.78 C ANISOU 1190 C GLU A 150 5886 5962 5547 44 -366 -197 C ATOM 1191 O GLU A 150 -1.853 29.363 54.566 1.00 48.21 O ANISOU 1191 O GLU A 150 6198 6222 5896 22 -353 -177 O ATOM 1192 CB GLU A 150 -1.729 27.884 57.457 1.00 52.13 C ANISOU 1192 CB GLU A 150 6709 6835 6261 125 -352 -128 C ATOM 1193 CG GLU A 150 -0.879 26.906 58.244 1.00 57.38 C ANISOU 1193 CG GLU A 150 7372 7551 6880 176 -358 -94 C ATOM 1194 CD GLU A 150 -1.662 25.682 58.697 1.00 58.93 C ANISOU 1194 CD GLU A 150 7598 7739 7054 209 -316 -28 C ATOM 1195 OE1 GLU A 150 -2.243 24.988 57.836 1.00 52.25 O ANISOU 1195 OE1 GLU A 150 6770 6833 6251 189 -282 5 O ATOM 1196 OE2 GLU A 150 -1.691 25.416 59.919 1.00 67.65 O ANISOU 1196 OE2 GLU A 150 8706 8898 8098 255 -314 -11 O ATOM 1197 N ASN A 151 -2.600 30.694 56.228 1.00 43.90 N ANISOU 1197 N ASN A 151 5648 5728 5304 34 -367 -231 N ATOM 1198 CA ASN A 151 -3.522 31.403 55.344 1.00 45.47 C ANISOU 1198 CA ASN A 151 5854 5874 5550 -3 -350 -240 C ATOM 1199 C ASN A 151 -2.776 32.098 54.219 1.00 39.62 C ANISOU 1199 C ASN A 151 5093 5101 4859 -35 -362 -264 C ATOM 1200 O ASN A 151 -3.244 32.118 53.076 1.00 40.97 O ANISOU 1200 O ASN A 151 5271 5226 5069 -59 -346 -248 O ATOM 1201 CB ASN A 151 -4.340 32.426 56.136 1.00 51.85 C ANISOU 1201 CB ASN A 151 6663 6695 6344 -5 -349 -276 C ATOM 1202 CG ASN A 151 -5.534 31.807 56.847 1.00 54.46 C ANISOU 1202 CG ASN A 151 7017 7033 6641 16 -323 -242 C ATOM 1203 OD1 ASN A 151 -5.995 30.722 56.491 1.00 54.62 O ANISOU 1203 OD1 ASN A 151 7054 7034 6666 22 -300 -192 O ATOM 1204 ND2 ASN A 151 -6.043 32.505 57.859 1.00 52.43 N ANISOU 1204 ND2 ASN A 151 6761 6804 6355 28 -323 -271 N ATOM 1205 N HIS A 152 -1.626 32.704 54.535 1.00 36.55 N ANISOU 1205 N HIS A 152 4678 4740 4470 -35 -389 -305 N ATOM 1206 CA HIS A 152 -0.828 33.373 53.512 1.00 49.65 C ANISOU 1206 CA HIS A 152 6316 6368 6180 -64 -396 -327 C ATOM 1207 C HIS A 152 -0.200 32.374 52.554 1.00 40.25 C ANISOU 1207 C HIS A 152 5128 5159 5005 -64 -391 -287 C ATOM 1208 O HIS A 152 -0.067 32.656 51.356 1.00 38.46 O ANISOU 1208 O HIS A 152 4898 4891 4822 -88 -381 -282 O ATOM 1209 CB HIS A 152 0.267 34.216 54.157 1.00 49.56 C ANISOU 1209 CB HIS A 152 6270 6390 6168 -66 -425 -385 C ATOM 1210 CG HIS A 152 -0.241 35.209 55.149 1.00 57.84 C ANISOU 1210 CG HIS A 152 7315 7460 7202 -67 -431 -434 C ATOM 1211 ND1 HIS A 152 -0.460 34.891 56.472 1.00 55.14 N ANISOU 1211 ND1 HIS A 152 6978 7174 6798 -35 -443 -441 N ATOM 1212 CD2 HIS A 152 -0.567 36.516 55.015 1.00 60.40 C ANISOU 1212 CD2 HIS A 152 7630 7755 7564 -94 -424 -477 C ATOM 1213 CE1 HIS A 152 -0.902 35.960 57.109 1.00 67.52 C ANISOU 1213 CE1 HIS A 152 8540 8748 8364 -43 -445 -492 C ATOM 1214 NE2 HIS A 152 -0.977 36.959 56.248 1.00 68.79 N ANISOU 1214 NE2 HIS A 152 8692 8855 8588 -80 -433 -515 N ATOM 1215 N ALA A 153 0.235 31.224 53.077 1.00 37.99 N ANISOU 1215 N ALA A 153 4847 4906 4682 -32 -396 -258 N ATOM 1216 CA ALA A 153 0.841 30.201 52.230 1.00 39.95 C ANISOU 1216 CA ALA A 153 5098 5136 4944 -28 -388 -220 C ATOM 1217 C ALA A 153 -0.160 29.671 51.211 1.00 41.49 C ANISOU 1217 C ALA A 153 5320 5282 5164 -44 -357 -185 C ATOM 1218 O ALA A 153 0.166 29.523 50.023 1.00 36.08 O ANISOU 1218 O ALA A 153 4633 4564 4511 -62 -349 -175 O ATOM 1219 CB ALA A 153 1.378 29.063 53.105 1.00 39.77 C ANISOU 1219 CB ALA A 153 5078 5157 4877 14 -394 -191 C ATOM 1220 N ILE A 154 -1.391 29.396 51.654 1.00 35.32 N ANISOU 1220 N ILE A 154 4560 4497 4364 -38 -340 -168 N ATOM 1221 CA ILE A 154 -2.407 28.869 50.750 1.00 33.13 C ANISOU 1221 CA ILE A 154 4303 4178 4108 -55 -313 -140 C ATOM 1222 C ILE A 154 -2.792 29.912 49.714 1.00 36.39 C ANISOU 1222 C ILE A 154 4710 4559 4559 -87 -312 -161 C ATOM 1223 O ILE A 154 -2.978 29.592 48.535 1.00 30.89 O ANISOU 1223 O ILE A 154 4019 3831 3887 -103 -300 -146 O ATOM 1224 CB ILE A 154 -3.625 28.371 51.548 1.00 35.65 C ANISOU 1224 CB ILE A 154 4642 4502 4402 -41 -294 -120 C ATOM 1225 CG1 ILE A 154 -3.215 27.188 52.437 1.00 40.21 C ANISOU 1225 CG1 ILE A 154 5227 5106 4944 -4 -287 -87 C ATOM 1226 CG2 ILE A 154 -4.769 27.982 50.603 1.00 41.11 C ANISOU 1226 CG2 ILE A 154 5347 5152 5121 -63 -269 -101 C ATOM 1227 CD1 ILE A 154 -4.252 26.793 53.486 1.00 51.20 C ANISOU 1227 CD1 ILE A 154 6637 6512 6306 17 -266 -66 C ATOM 1228 N MET A 155 -2.930 31.172 50.136 1.00 32.46 N ANISOU 1228 N MET A 155 4201 4069 4065 -96 -323 -196 N ATOM 1229 CA MET A 155 -3.160 32.244 49.173 1.00 34.92 C ANISOU 1229 CA MET A 155 4504 4348 4415 -122 -319 -212 C ATOM 1230 C MET A 155 -2.002 32.348 48.190 1.00 31.71 C ANISOU 1230 C MET A 155 4084 3928 4038 -133 -324 -214 C ATOM 1231 O MET A 155 -2.210 32.619 47.001 1.00 31.29 O ANISOU 1231 O MET A 155 4032 3845 4013 -149 -312 -204 O ATOM 1232 CB MET A 155 -3.360 33.575 49.904 1.00 37.28 C ANISOU 1232 CB MET A 155 4792 4655 4718 -127 -326 -252 C ATOM 1233 CG MET A 155 -3.940 34.659 49.030 1.00 44.39 C ANISOU 1233 CG MET A 155 5689 5519 5658 -148 -313 -259 C ATOM 1234 SD MET A 155 -4.232 36.201 49.912 1.00 56.09 S ANISOU 1234 SD MET A 155 7159 7002 7151 -154 -314 -308 S ATOM 1235 CE MET A 155 -4.184 35.642 51.611 1.00 43.46 C ANISOU 1235 CE MET A 155 5562 5455 5494 -128 -331 -324 C ATOM 1236 N GLY A 156 -0.771 32.150 48.673 1.00 33.33 N ANISOU 1236 N GLY A 156 4272 4156 4234 -122 -342 -226 N ATOM 1237 CA GLY A 156 0.372 32.155 47.774 1.00 32.46 C ANISOU 1237 CA GLY A 156 4147 4034 4152 -130 -344 -226 C ATOM 1238 C GLY A 156 0.289 31.062 46.727 1.00 28.57 C ANISOU 1238 C GLY A 156 3671 3522 3664 -129 -328 -188 C ATOM 1239 O GLY A 156 0.595 31.297 45.557 1.00 31.28 O ANISOU 1239 O GLY A 156 4010 3839 4035 -144 -319 -183 O ATOM 1240 N VAL A 157 -0.130 29.859 47.135 1.00 28.42 N ANISOU 1240 N VAL A 157 3670 3512 3617 -112 -322 -162 N ATOM 1241 CA VAL A 157 -0.301 28.745 46.199 1.00 30.28 C ANISOU 1241 CA VAL A 157 3922 3726 3858 -112 -304 -132 C ATOM 1242 C VAL A 157 -1.296 29.111 45.099 1.00 30.52 C ANISOU 1242 C VAL A 157 3961 3727 3907 -134 -290 -129 C ATOM 1243 O VAL A 157 -1.033 28.913 43.906 1.00 28.17 O ANISOU 1243 O VAL A 157 3664 3411 3626 -144 -281 -121 O ATOM 1244 CB VAL A 157 -0.755 27.478 46.947 1.00 30.94 C ANISOU 1244 CB VAL A 157 4023 3819 3915 -91 -293 -105 C ATOM 1245 CG1 VAL A 157 -1.236 26.399 45.937 1.00 33.75 C ANISOU 1245 CG1 VAL A 157 4396 4144 4284 -99 -269 -82 C ATOM 1246 CG2 VAL A 157 0.355 26.926 47.825 1.00 29.00 C ANISOU 1246 CG2 VAL A 157 3767 3603 3647 -62 -304 -98 C ATOM 1247 N ALA A 158 -2.469 29.627 45.481 1.00 32.03 N ANISOU 1247 N ALA A 158 4159 3918 4092 -140 -287 -135 N ATOM 1248 CA ALA A 158 -3.467 29.962 44.466 1.00 28.50 C ANISOU 1248 CA ALA A 158 3718 3451 3661 -156 -275 -130 C ATOM 1249 C ALA A 158 -2.937 31.032 43.525 1.00 26.37 C ANISOU 1249 C ALA A 158 3435 3168 3416 -168 -277 -140 C ATOM 1250 O ALA A 158 -3.199 30.999 42.316 1.00 28.11 O ANISOU 1250 O ALA A 158 3659 3375 3647 -175 -267 -129 O ATOM 1251 CB ALA A 158 -4.768 30.437 45.116 1.00 31.22 C ANISOU 1251 CB ALA A 158 4067 3799 3996 -158 -272 -135 C ATOM 1252 N PHE A 159 -2.191 31.985 44.071 1.00 25.60 N ANISOU 1252 N PHE A 159 3321 3075 3329 -168 -287 -161 N ATOM 1253 CA PHE A 159 -1.566 33.032 43.269 1.00 28.49 C ANISOU 1253 CA PHE A 159 3672 3424 3728 -178 -282 -169 C ATOM 1254 C PHE A 159 -0.629 32.460 42.204 1.00 28.46 C ANISOU 1254 C PHE A 159 3667 3413 3735 -179 -276 -154 C ATOM 1255 O PHE A 159 -0.599 32.960 41.076 1.00 25.73 O ANISOU 1255 O PHE A 159 3319 3050 3407 -185 -263 -144 O ATOM 1256 CB PHE A 159 -0.808 33.970 44.202 1.00 29.61 C ANISOU 1256 CB PHE A 159 3794 3573 3883 -181 -293 -201 C ATOM 1257 CG PHE A 159 0.050 34.982 43.504 1.00 32.31 C ANISOU 1257 CG PHE A 159 4116 3894 4266 -193 -285 -212 C ATOM 1258 CD1 PHE A 159 -0.513 36.087 42.901 1.00 33.78 C ANISOU 1258 CD1 PHE A 159 4301 4054 4480 -202 -267 -210 C ATOM 1259 CD2 PHE A 159 1.427 34.847 43.497 1.00 33.22 C ANISOU 1259 CD2 PHE A 159 4212 4015 4396 -194 -292 -222 C ATOM 1260 CE1 PHE A 159 0.281 37.034 42.282 1.00 35.61 C ANISOU 1260 CE1 PHE A 159 4515 4261 4756 -212 -252 -216 C ATOM 1261 CE2 PHE A 159 2.218 35.795 42.882 1.00 34.66 C ANISOU 1261 CE2 PHE A 159 4373 4174 4622 -206 -279 -232 C ATOM 1262 CZ PHE A 159 1.638 36.886 42.274 1.00 32.34 C ANISOU 1262 CZ PHE A 159 4081 3850 4357 -216 -257 -228 C ATOM 1263 N THR A 160 0.177 31.444 42.548 1.00 26.94 N ANISOU 1263 N THR A 160 3474 3234 3529 -169 -283 -150 N ATOM 1264 CA THR A 160 1.108 30.897 41.550 1.00 23.97 C ANISOU 1264 CA THR A 160 3095 2850 3164 -168 -275 -137 C ATOM 1265 C THR A 160 0.377 30.263 40.373 1.00 24.96 C ANISOU 1265 C THR A 160 3239 2963 3282 -170 -260 -118 C ATOM 1266 O THR A 160 0.857 30.332 39.234 1.00 24.82 O ANISOU 1266 O THR A 160 3219 2935 3276 -173 -249 -109 O ATOM 1267 CB THR A 160 2.070 29.859 42.155 1.00 21.55 C ANISOU 1267 CB THR A 160 2784 2559 2845 -152 -284 -134 C ATOM 1268 OG1 THR A 160 1.370 28.673 42.568 1.00 25.76 O ANISOU 1268 OG1 THR A 160 3337 3097 3352 -142 -280 -118 O ATOM 1269 CG2 THR A 160 2.863 30.443 43.294 1.00 21.94 C ANISOU 1269 CG2 THR A 160 2810 2631 2896 -147 -303 -157 C ATOM 1270 N TRP A 161 -0.753 29.594 40.624 1.00 25.17 N ANISOU 1270 N TRP A 161 3282 2993 3289 -170 -259 -112 N ATOM 1271 CA TRP A 161 -1.535 29.052 39.508 1.00 23.86 C ANISOU 1271 CA TRP A 161 3129 2820 3117 -175 -247 -102 C ATOM 1272 C TRP A 161 -2.113 30.153 38.628 1.00 27.56 C ANISOU 1272 C TRP A 161 3594 3285 3594 -181 -243 -100 C ATOM 1273 O TRP A 161 -2.129 30.028 37.394 1.00 25.90 O ANISOU 1273 O TRP A 161 3386 3073 3381 -182 -234 -93 O ATOM 1274 CB TRP A 161 -2.658 28.150 40.021 1.00 26.48 C ANISOU 1274 CB TRP A 161 3474 3154 3434 -176 -245 -100 C ATOM 1275 CG TRP A 161 -2.150 26.828 40.426 1.00 28.36 C ANISOU 1275 CG TRP A 161 3720 3389 3666 -167 -239 -93 C ATOM 1276 CD1 TRP A 161 -1.614 26.490 41.640 1.00 27.89 C ANISOU 1276 CD1 TRP A 161 3659 3338 3599 -153 -244 -88 C ATOM 1277 CD2 TRP A 161 -2.079 25.659 39.610 1.00 27.69 C ANISOU 1277 CD2 TRP A 161 3644 3292 3582 -169 -224 -89 C ATOM 1278 NE1 TRP A 161 -1.233 25.167 41.630 1.00 31.09 N ANISOU 1278 NE1 TRP A 161 4074 3736 4004 -143 -231 -76 N ATOM 1279 CE2 TRP A 161 -1.509 24.636 40.395 1.00 30.29 C ANISOU 1279 CE2 TRP A 161 3980 3619 3911 -155 -217 -78 C ATOM 1280 CE3 TRP A 161 -2.442 25.379 38.287 1.00 28.85 C ANISOU 1280 CE3 TRP A 161 3797 3435 3732 -180 -216 -95 C ATOM 1281 CZ2 TRP A 161 -1.295 23.346 39.903 1.00 31.30 C ANISOU 1281 CZ2 TRP A 161 4118 3730 4046 -153 -199 -73 C ATOM 1282 CZ3 TRP A 161 -2.246 24.094 37.803 1.00 28.81 C ANISOU 1282 CZ3 TRP A 161 3801 3417 3730 -180 -201 -96 C ATOM 1283 CH2 TRP A 161 -1.667 23.099 38.607 1.00 29.19 C ANISOU 1283 CH2 TRP A 161 3855 3454 3783 -168 -190 -85 C ATOM 1284 N VAL A 162 -2.621 31.232 39.228 1.00 25.45 N ANISOU 1284 N VAL A 162 3320 3017 3334 -184 -247 -107 N ATOM 1285 CA VAL A 162 -3.190 32.302 38.411 1.00 23.78 C ANISOU 1285 CA VAL A 162 3104 2800 3132 -184 -239 -100 C ATOM 1286 C VAL A 162 -2.116 32.962 37.548 1.00 27.97 C ANISOU 1286 C VAL A 162 3625 3319 3684 -182 -227 -92 C ATOM 1287 O VAL A 162 -2.320 33.204 36.350 1.00 25.85 O ANISOU 1287 O VAL A 162 3359 3051 3413 -177 -216 -76 O ATOM 1288 CB VAL A 162 -3.921 33.338 39.283 1.00 30.11 C ANISOU 1288 CB VAL A 162 3900 3599 3942 -186 -242 -109 C ATOM 1289 CG1 VAL A 162 -4.459 34.423 38.395 1.00 28.46 C ANISOU 1289 CG1 VAL A 162 3687 3382 3746 -182 -229 -95 C ATOM 1290 CG2 VAL A 162 -5.061 32.669 40.028 1.00 32.15 C ANISOU 1290 CG2 VAL A 162 4168 3869 4179 -186 -248 -112 C ATOM 1291 N MET A 163 -0.956 33.265 38.129 1.00 24.61 N ANISOU 1291 N MET A 163 3187 2886 3278 -185 -230 -103 N ATOM 1292 CA MET A 163 0.099 33.857 37.305 1.00 23.88 C ANISOU 1292 CA MET A 163 3082 2779 3211 -185 -214 -95 C ATOM 1293 C MET A 163 0.579 32.873 36.238 1.00 27.08 C ANISOU 1293 C MET A 163 3496 3191 3603 -179 -207 -80 C ATOM 1294 O MET A 163 0.787 33.255 35.083 1.00 27.48 O ANISOU 1294 O MET A 163 3547 3236 3659 -173 -188 -63 O ATOM 1295 CB MET A 163 1.273 34.326 38.178 1.00 23.54 C ANISOU 1295 CB MET A 163 3018 2730 3196 -191 -219 -117 C ATOM 1296 CG MET A 163 0.887 35.420 39.181 1.00 29.27 C ANISOU 1296 CG MET A 163 3733 3448 3939 -199 -224 -139 C ATOM 1297 SD MET A 163 0.053 36.816 38.375 1.00 34.20 S ANISOU 1297 SD MET A 163 4359 4048 4589 -198 -198 -122 S ATOM 1298 CE MET A 163 1.433 37.571 37.567 1.00 32.97 C ANISOU 1298 CE MET A 163 4182 3866 4480 -203 -172 -116 C ATOM 1299 N ALA A 164 0.742 31.599 36.595 1.00 24.14 N ANISOU 1299 N ALA A 164 3133 2830 3212 -177 -217 -86 N ATOM 1300 CA ALA A 164 1.251 30.644 35.617 1.00 24.07 C ANISOU 1300 CA ALA A 164 3131 2823 3192 -172 -207 -76 C ATOM 1301 C ALA A 164 0.278 30.473 34.450 1.00 25.56 C ANISOU 1301 C ALA A 164 3333 3019 3358 -169 -200 -67 C ATOM 1302 O ALA A 164 0.698 30.382 33.286 1.00 23.04 O ANISOU 1302 O ALA A 164 3016 2702 3034 -162 -185 -56 O ATOM 1303 CB ALA A 164 1.530 29.307 36.298 1.00 24.84 C ANISOU 1303 CB ALA A 164 3236 2925 3278 -169 -216 -83 C ATOM 1304 N LEU A 165 -1.031 30.428 34.741 1.00 24.47 N ANISOU 1304 N LEU A 165 3203 2890 3205 -173 -209 -71 N ATOM 1305 CA LEU A 165 -2.033 30.332 33.674 1.00 24.11 C ANISOU 1305 CA LEU A 165 3164 2860 3137 -169 -206 -66 C ATOM 1306 C LEU A 165 -2.052 31.585 32.803 1.00 25.64 C ANISOU 1306 C LEU A 165 3351 3055 3336 -158 -194 -47 C ATOM 1307 O LEU A 165 -2.266 31.509 31.581 1.00 25.01 O ANISOU 1307 O LEU A 165 3275 2993 3236 -148 -186 -36 O ATOM 1308 CB LEU A 165 -3.418 30.059 34.283 1.00 26.88 C ANISOU 1308 CB LEU A 165 3518 3220 3476 -176 -219 -77 C ATOM 1309 CG LEU A 165 -3.610 28.627 34.789 1.00 28.19 C ANISOU 1309 CG LEU A 165 3693 3384 3635 -185 -222 -92 C ATOM 1310 CD1 LEU A 165 -4.851 28.490 35.680 1.00 31.97 C ANISOU 1310 CD1 LEU A 165 4172 3865 4109 -192 -230 -99 C ATOM 1311 CD2 LEU A 165 -3.706 27.657 33.610 1.00 30.50 C ANISOU 1311 CD2 LEU A 165 3992 3686 3910 -186 -216 -100 C ATOM 1312 N ALA A 166 -1.828 32.754 33.401 1.00 22.48 N ANISOU 1312 N ALA A 166 2940 2638 2962 -159 -189 -41 N ATOM 1313 CA ALA A 166 -1.791 33.967 32.599 1.00 26.23 C ANISOU 1313 CA ALA A 166 3409 3108 3450 -147 -170 -17 C ATOM 1314 C ALA A 166 -0.616 33.974 31.624 1.00 27.10 C ANISOU 1314 C ALA A 166 3516 3212 3567 -139 -149 -2 C ATOM 1315 O ALA A 166 -0.650 34.723 30.646 1.00 26.42 O ANISOU 1315 O ALA A 166 3429 3128 3480 -123 -128 24 O ATOM 1316 CB ALA A 166 -1.735 35.195 33.509 1.00 27.75 C ANISOU 1316 CB ALA A 166 3590 3277 3679 -152 -165 -20 C ATOM 1317 N CYS A 167 0.419 33.166 31.876 1.00 24.35 N ANISOU 1317 N CYS A 167 3167 2859 3225 -146 -152 -15 N ATOM 1318 CA CYS A 167 1.520 32.997 30.928 1.00 25.38 C ANISOU 1318 CA CYS A 167 3296 2987 3360 -138 -131 -2 C ATOM 1319 C CYS A 167 1.238 31.875 29.933 1.00 23.97 C ANISOU 1319 C CYS A 167 3133 2833 3140 -129 -133 -3 C ATOM 1320 O CYS A 167 1.426 32.039 28.716 1.00 27.82 O ANISOU 1320 O CYS A 167 3625 3333 3613 -113 -114 16 O ATOM 1321 CB CYS A 167 2.831 32.707 31.693 1.00 24.33 C ANISOU 1321 CB CYS A 167 3150 2837 3256 -148 -133 -16 C ATOM 1322 SG CYS A 167 4.276 32.655 30.586 1.00 28.49 S ANISOU 1322 SG CYS A 167 3670 3358 3799 -138 -103 2 S ATOM 1323 N ALA A 168 0.759 30.736 30.425 1.00 21.70 N ANISOU 1323 N ALA A 168 2855 2554 2835 -138 -152 -26 N ATOM 1324 CA ALA A 168 0.740 29.523 29.621 1.00 21.38 C ANISOU 1324 CA ALA A 168 2826 2529 2766 -135 -150 -37 C ATOM 1325 C ALA A 168 -0.511 29.383 28.768 1.00 27.27 C ANISOU 1325 C ALA A 168 3580 3306 3475 -129 -157 -41 C ATOM 1326 O ALA A 168 -0.474 28.682 27.746 1.00 24.39 O ANISOU 1326 O ALA A 168 3223 2960 3084 -122 -151 -49 O ATOM 1327 CB ALA A 168 0.851 28.281 30.515 1.00 23.61 C ANISOU 1327 CB ALA A 168 3115 2803 3054 -147 -162 -59 C ATOM 1328 N ALA A 169 -1.625 30.008 29.174 1.00 22.43 N ANISOU 1328 N ALA A 169 2964 2701 2860 -131 -170 -39 N ATOM 1329 CA ALA A 169 -2.908 29.813 28.491 1.00 24.15 C ANISOU 1329 CA ALA A 169 3182 2952 3042 -127 -181 -47 C ATOM 1330 C ALA A 169 -3.115 30.640 27.214 1.00 21.33 C ANISOU 1330 C ALA A 169 2823 2624 2659 -101 -170 -22 C ATOM 1331 O ALA A 169 -3.715 30.114 26.273 1.00 25.01 O ANISOU 1331 O ALA A 169 3291 3127 3086 -93 -177 -34 O ATOM 1332 CB ALA A 169 -4.067 30.085 29.472 1.00 23.61 C ANISOU 1332 CB ALA A 169 3107 2881 2980 -138 -198 -54 C ATOM 1333 N PRO A 170 -2.684 31.906 27.129 1.00 22.63 N ANISOU 1333 N PRO A 170 2982 2775 2843 -86 -152 12 N ATOM 1334 CA PRO A 170 -2.966 32.716 25.918 1.00 23.31 C ANISOU 1334 CA PRO A 170 3066 2890 2902 -56 -138 44 C ATOM 1335 C PRO A 170 -2.519 32.062 24.616 1.00 26.49 C ANISOU 1335 C PRO A 170 3476 3323 3265 -40 -128 43 C ATOM 1336 O PRO A 170 -3.256 32.142 23.616 1.00 23.51 O ANISOU 1336 O PRO A 170 3098 2991 2842 -17 -132 50 O ATOM 1337 CB PRO A 170 -2.214 34.030 26.184 1.00 25.03 C ANISOU 1337 CB PRO A 170 3277 3070 3162 -48 -110 80 C ATOM 1338 CG PRO A 170 -2.331 34.180 27.695 1.00 27.69 C ANISOU 1338 CG PRO A 170 3608 3373 3538 -74 -124 60 C ATOM 1339 CD PRO A 170 -2.126 32.754 28.214 1.00 25.37 C ANISOU 1339 CD PRO A 170 3322 3081 3237 -96 -145 22 C ATOM 1340 N PRO A 171 -1.354 31.396 24.558 1.00 24.65 N ANISOU 1340 N PRO A 171 3251 3072 3045 -48 -116 33 N ATOM 1341 CA PRO A 171 -0.959 30.753 23.282 1.00 25.06 C ANISOU 1341 CA PRO A 171 3311 3155 3056 -31 -105 29 C ATOM 1342 C PRO A 171 -1.841 29.593 22.875 1.00 23.38 C ANISOU 1342 C PRO A 171 3102 2980 2802 -38 -129 -14 C ATOM 1343 O PRO A 171 -1.716 29.117 21.742 1.00 23.78 O ANISOU 1343 O PRO A 171 3158 3065 2811 -22 -123 -23 O ATOM 1344 CB PRO A 171 0.487 30.274 23.541 1.00 25.70 C ANISOU 1344 CB PRO A 171 3395 3201 3170 -42 -86 26 C ATOM 1345 CG PRO A 171 0.972 31.140 24.641 1.00 29.41 C ANISOU 1345 CG PRO A 171 3853 3626 3693 -54 -81 43 C ATOM 1346 CD PRO A 171 -0.233 31.372 25.525 1.00 23.75 C ANISOU 1346 CD PRO A 171 3133 2911 2980 -67 -107 31 C ATOM 1347 N LEU A 172 -2.695 29.080 23.761 1.00 22.52 N ANISOU 1347 N LEU A 172 2989 2864 2704 -63 -154 -44 N ATOM 1348 CA LEU A 172 -3.699 28.112 23.329 1.00 24.90 C ANISOU 1348 CA LEU A 172 3289 3202 2971 -71 -176 -86 C ATOM 1349 C LEU A 172 -4.849 28.749 22.565 1.00 25.97 C ANISOU 1349 C LEU A 172 3414 3392 3063 -48 -190 -77 C ATOM 1350 O LEU A 172 -5.569 28.028 21.862 1.00 27.85 O ANISOU 1350 O LEU A 172 3646 3673 3262 -49 -207 -114 O ATOM 1351 CB LEU A 172 -4.304 27.367 24.527 1.00 25.57 C ANISOU 1351 CB LEU A 172 3370 3259 3084 -104 -194 -118 C ATOM 1352 CG LEU A 172 -3.376 26.531 25.397 1.00 26.69 C ANISOU 1352 CG LEU A 172 3522 3353 3264 -124 -184 -130 C ATOM 1353 CD1 LEU A 172 -4.182 25.909 26.511 1.00 31.16 C ANISOU 1353 CD1 LEU A 172 4086 3902 3854 -150 -198 -153 C ATOM 1354 CD2 LEU A 172 -2.694 25.459 24.543 1.00 26.12 C ANISOU 1354 CD2 LEU A 172 3461 3288 3178 -123 -170 -155 C ATOM 1355 N VAL A 173 -5.078 30.060 22.721 1.00 23.46 N ANISOU 1355 N VAL A 173 3089 3072 2753 -29 -184 -33 N ATOM 1356 CA VAL A 173 -6.340 30.640 22.249 1.00 27.15 C ANISOU 1356 CA VAL A 173 3543 3589 3186 -8 -201 -24 C ATOM 1357 C VAL A 173 -6.159 31.905 21.413 1.00 32.70 C ANISOU 1357 C VAL A 173 4244 4312 3868 35 -180 33 C ATOM 1358 O VAL A 173 -7.094 32.706 21.280 1.00 29.66 O ANISOU 1358 O VAL A 173 3847 3954 3467 57 -187 57 O ATOM 1359 CB VAL A 173 -7.290 30.919 23.436 1.00 32.56 C ANISOU 1359 CB VAL A 173 4217 4253 3902 -28 -219 -29 C ATOM 1360 CG1 VAL A 173 -7.745 29.610 24.077 1.00 28.40 C ANISOU 1360 CG1 VAL A 173 3687 3716 3386 -66 -239 -84 C ATOM 1361 CG2 VAL A 173 -6.629 31.840 24.471 1.00 26.69 C ANISOU 1361 CG2 VAL A 173 3478 3452 3212 -34 -200 4 C ATOM 1362 N GLY A 174 -4.979 32.102 20.831 1.00 27.55 N ANISOU 1362 N GLY A 174 3603 3648 3215 51 -150 59 N ATOM 1363 CA GLY A 174 -4.823 33.119 19.796 1.00 30.31 C ANISOU 1363 CA GLY A 174 3953 4026 3536 98 -124 113 C ATOM 1364 C GLY A 174 -3.860 34.248 20.099 1.00 28.18 C ANISOU 1364 C GLY A 174 3687 3702 3317 107 -84 166 C ATOM 1365 O GLY A 174 -3.724 35.146 19.262 1.00 28.63 O ANISOU 1365 O GLY A 174 3745 3776 3356 148 -55 217 O ATOM 1366 N TRP A 175 -3.187 34.288 21.244 1.00 25.84 N ANISOU 1366 N TRP A 175 3392 3343 3084 73 -78 156 N ATOM 1367 CA TRP A 175 -2.149 35.285 21.502 1.00 25.96 C ANISOU 1367 CA TRP A 175 3406 3306 3152 77 -39 196 C ATOM 1368 C TRP A 175 -0.831 34.528 21.580 1.00 25.77 C ANISOU 1368 C TRP A 175 3388 3255 3147 57 -27 176 C ATOM 1369 O TRP A 175 -0.585 33.826 22.562 1.00 25.29 O ANISOU 1369 O TRP A 175 3326 3167 3114 22 -47 138 O ATOM 1370 CB TRP A 175 -2.401 36.046 22.799 1.00 27.82 C ANISOU 1370 CB TRP A 175 3633 3494 3445 55 -42 197 C ATOM 1371 CG TRP A 175 -1.506 37.258 22.964 1.00 23.50 C ANISOU 1371 CG TRP A 175 3079 2895 2954 61 1 237 C ATOM 1372 CD1 TRP A 175 -0.847 37.943 21.985 1.00 24.64 C ANISOU 1372 CD1 TRP A 175 3225 3037 3099 92 45 284 C ATOM 1373 CD2 TRP A 175 -1.226 37.926 24.182 1.00 28.71 C ANISOU 1373 CD2 TRP A 175 3731 3500 3679 35 6 229 C ATOM 1374 NE1 TRP A 175 -0.157 38.996 22.528 1.00 27.21 N ANISOU 1374 NE1 TRP A 175 3541 3304 3494 84 79 306 N ATOM 1375 CE2 TRP A 175 -0.376 39.005 23.881 1.00 24.15 C ANISOU 1375 CE2 TRP A 175 3146 2884 3145 48 54 269 C ATOM 1376 CE3 TRP A 175 -1.597 37.704 25.511 1.00 26.09 C ANISOU 1376 CE3 TRP A 175 3393 3147 3372 3 -23 191 C ATOM 1377 CZ2 TRP A 175 0.113 39.859 24.860 1.00 27.50 C ANISOU 1377 CZ2 TRP A 175 3558 3251 3641 26 71 265 C ATOM 1378 CZ3 TRP A 175 -1.117 38.569 26.482 1.00 28.87 C ANISOU 1378 CZ3 TRP A 175 3735 3447 3787 -15 -8 189 C ATOM 1379 CH2 TRP A 175 -0.274 39.618 26.160 1.00 28.30 C ANISOU 1379 CH2 TRP A 175 3654 3338 3760 -6 37 222 C ATOM 1380 N SER A 176 0.021 34.713 20.573 1.00 24.91 N ANISOU 1380 N SER A 176 3285 3154 3026 82 7 206 N ATOM 1381 CA SER A 176 1.144 33.813 20.304 1.00 23.78 C ANISOU 1381 CA SER A 176 3147 3003 2884 72 17 186 C ATOM 1382 C SER A 176 0.631 32.407 19.995 1.00 26.80 C ANISOU 1382 C SER A 176 3539 3427 3216 64 -15 136 C ATOM 1383 O SER A 176 -0.557 32.218 19.711 1.00 25.14 O ANISOU 1383 O SER A 176 3328 3260 2962 71 -42 121 O ATOM 1384 CB SER A 176 2.139 33.795 21.481 1.00 26.40 C ANISOU 1384 CB SER A 176 3471 3274 3285 38 22 172 C ATOM 1385 OG SER A 176 3.297 33.038 21.146 1.00 27.59 O ANISOU 1385 OG SER A 176 3626 3418 3441 34 38 161 O ATOM 1386 N ARG A 177 1.522 31.414 20.009 1.00 22.73 N ANISOU 1386 N ARG A 177 3030 2898 2708 48 -11 108 N ATOM 1387 CA ARG A 177 1.148 30.033 19.723 1.00 22.00 C ANISOU 1387 CA ARG A 177 2946 2834 2578 37 -35 57 C ATOM 1388 C ARG A 177 2.303 29.142 20.159 1.00 24.33 C ANISOU 1388 C ARG A 177 3245 3092 2908 16 -25 34 C ATOM 1389 O ARG A 177 3.436 29.608 20.293 1.00 23.90 O ANISOU 1389 O ARG A 177 3185 3004 2890 19 3 62 O ATOM 1390 CB ARG A 177 0.860 29.818 18.232 1.00 22.24 C ANISOU 1390 CB ARG A 177 2984 2928 2538 71 -29 57 C ATOM 1391 CG ARG A 177 2.043 30.254 17.341 1.00 26.61 C ANISOU 1391 CG ARG A 177 3544 3480 3088 100 16 97 C ATOM 1392 CD ARG A 177 1.698 30.193 15.863 1.00 27.28 C ANISOU 1392 CD ARG A 177 3637 3635 3095 141 24 104 C ATOM 1393 NE ARG A 177 2.799 30.618 15.002 1.00 24.28 N ANISOU 1393 NE ARG A 177 3263 3255 2709 173 72 147 N ATOM 1394 CZ ARG A 177 2.824 30.422 13.690 1.00 30.11 C ANISOU 1394 CZ ARG A 177 4010 4051 3378 210 86 152 C ATOM 1395 NH1 ARG A 177 1.809 29.850 13.062 1.00 30.56 N ANISOU 1395 NH1 ARG A 177 4070 4175 3367 221 54 114 N ATOM 1396 NH2 ARG A 177 3.894 30.796 12.991 1.00 29.11 N ANISOU 1396 NH2 ARG A 177 3890 3919 3253 237 135 194 N ATOM 1397 N TYR A 178 2.013 27.858 20.350 1.00 22.01 N ANISOU 1397 N TYR A 178 2957 2802 2603 -3 -45 -15 N ATOM 1398 CA TYR A 178 3.064 26.869 20.583 1.00 24.62 C ANISOU 1398 CA TYR A 178 3293 3103 2959 -16 -33 -35 C ATOM 1399 C TYR A 178 3.521 26.313 19.239 1.00 23.91 C ANISOU 1399 C TYR A 178 3214 3045 2827 6 -11 -45 C ATOM 1400 O TYR A 178 2.707 26.082 18.342 1.00 23.96 O ANISOU 1400 O TYR A 178 3226 3100 2777 19 -22 -65 O ATOM 1401 CB TYR A 178 2.581 25.738 21.509 1.00 21.49 C ANISOU 1401 CB TYR A 178 2898 2686 2580 -47 -57 -80 C ATOM 1402 CG TYR A 178 2.362 26.222 22.931 1.00 22.22 C ANISOU 1402 CG TYR A 178 2981 2745 2716 -66 -74 -68 C ATOM 1403 CD1 TYR A 178 3.440 26.570 23.736 1.00 22.11 C ANISOU 1403 CD1 TYR A 178 2959 2693 2748 -71 -62 -47 C ATOM 1404 CD2 TYR A 178 1.075 26.327 23.470 1.00 23.47 C ANISOU 1404 CD2 TYR A 178 3136 2914 2868 -79 -101 -82 C ATOM 1405 CE1 TYR A 178 3.242 27.036 25.047 1.00 20.34 C ANISOU 1405 CE1 TYR A 178 2726 2444 2560 -87 -79 -42 C ATOM 1406 CE2 TYR A 178 0.868 26.787 24.788 1.00 25.19 C ANISOU 1406 CE2 TYR A 178 3346 3102 3122 -95 -114 -73 C ATOM 1407 CZ TYR A 178 1.960 27.152 25.562 1.00 23.55 C ANISOU 1407 CZ TYR A 178 3132 2861 2956 -98 -103 -53 C ATOM 1408 OH TYR A 178 1.786 27.620 26.861 1.00 23.63 O ANISOU 1408 OH TYR A 178 3133 2847 2997 -112 -117 -49 O ATOM 1409 N ILE A 179 4.830 26.135 19.100 1.00 22.11 N ANISOU 1409 N ILE A 179 2987 2791 2622 12 18 -32 N ATOM 1410 CA ILE A 179 5.440 25.761 17.825 1.00 22.28 C ANISOU 1410 CA ILE A 179 3019 2841 2607 37 47 -34 C ATOM 1411 C ILE A 179 6.634 24.849 18.111 1.00 22.23 C ANISOU 1411 C ILE A 179 3014 2797 2636 28 66 -48 C ATOM 1412 O ILE A 179 7.314 25.039 19.135 1.00 21.95 O ANISOU 1412 O ILE A 179 2966 2717 2656 13 68 -33 O ATOM 1413 CB ILE A 179 5.842 27.033 17.058 1.00 27.16 C ANISOU 1413 CB ILE A 179 3633 3475 3212 69 77 23 C ATOM 1414 CG1 ILE A 179 6.188 26.759 15.598 1.00 26.11 C ANISOU 1414 CG1 ILE A 179 3512 3386 3022 103 104 24 C ATOM 1415 CG2 ILE A 179 6.984 27.750 17.768 1.00 24.61 C ANISOU 1415 CG2 ILE A 179 3295 3099 2955 62 101 61 C ATOM 1416 CD1 ILE A 179 6.367 28.045 14.791 1.00 28.52 C ANISOU 1416 CD1 ILE A 179 3816 3714 3308 140 136 86 C ATOM 1417 N PRO A 180 6.926 23.848 17.267 1.00 22.54 N ANISOU 1417 N PRO A 180 3065 2852 2645 37 81 -80 N ATOM 1418 CA PRO A 180 8.050 22.945 17.559 1.00 22.51 C ANISOU 1418 CA PRO A 180 3063 2811 2680 30 102 -92 C ATOM 1419 C PRO A 180 9.390 23.667 17.561 1.00 23.21 C ANISOU 1419 C PRO A 180 3139 2877 2804 44 135 -45 C ATOM 1420 O PRO A 180 9.619 24.603 16.786 1.00 22.77 O ANISOU 1420 O PRO A 180 3080 2841 2728 68 157 -8 O ATOM 1421 CB PRO A 180 7.978 21.909 16.425 1.00 24.41 C ANISOU 1421 CB PRO A 180 3320 3081 2872 42 115 -135 C ATOM 1422 CG PRO A 180 6.533 21.875 16.051 1.00 26.07 C ANISOU 1422 CG PRO A 180 3536 3337 3033 38 83 -167 C ATOM 1423 CD PRO A 180 6.112 23.336 16.145 1.00 23.85 C ANISOU 1423 CD PRO A 180 3245 3074 2745 50 74 -116 C ATOM 1424 N GLU A 181 10.311 23.175 18.401 1.00 22.36 N ANISOU 1424 N GLU A 181 3021 2726 2750 32 141 -46 N ATOM 1425 CA GLU A 181 11.654 23.755 18.507 1.00 22.48 C ANISOU 1425 CA GLU A 181 3017 2718 2807 42 171 -8 C ATOM 1426 C GLU A 181 12.745 22.723 18.278 1.00 24.94 C ANISOU 1426 C GLU A 181 3329 3012 3135 50 198 -21 C ATOM 1427 O GLU A 181 12.548 21.512 18.477 1.00 22.59 O ANISOU 1427 O GLU A 181 3044 2706 2834 42 190 -59 O ATOM 1428 CB GLU A 181 11.891 24.391 19.896 1.00 22.06 C ANISOU 1428 CB GLU A 181 2940 2630 2810 21 151 10 C ATOM 1429 CG GLU A 181 10.764 25.306 20.368 1.00 22.92 C ANISOU 1429 CG GLU A 181 3049 2749 2912 9 122 18 C ATOM 1430 CD GLU A 181 11.260 26.219 21.457 1.00 22.45 C ANISOU 1430 CD GLU A 181 2962 2659 2908 -5 115 40 C ATOM 1431 OE1 GLU A 181 11.030 25.895 22.637 1.00 25.42 O ANISOU 1431 OE1 GLU A 181 3333 3020 3307 -24 86 23 O ATOM 1432 OE2 GLU A 181 11.948 27.196 21.109 1.00 23.88 O ANISOU 1432 OE2 GLU A 181 3128 2833 3111 4 142 72 O ATOM 1433 N GLY A 182 13.924 23.239 17.878 1.00 22.81 N ANISOU 1433 N GLY A 182 3044 2734 2888 66 234 12 N ATOM 1434 CA GLY A 182 15.109 22.386 17.804 1.00 23.80 C ANISOU 1434 CA GLY A 182 3163 2840 3040 75 261 6 C ATOM 1435 C GLY A 182 14.934 21.267 16.792 1.00 23.29 C ANISOU 1435 C GLY A 182 3126 2795 2930 90 278 -29 C ATOM 1436 O GLY A 182 14.598 21.497 15.620 1.00 23.60 O ANISOU 1436 O GLY A 182 3180 2871 2915 109 295 -30 O ATOM 1437 N MET A 183 15.159 20.028 17.249 1.00 23.27 N ANISOU 1437 N MET A 183 3127 2768 2946 83 276 -60 N ATOM 1438 CA MET A 183 14.957 18.863 16.374 1.00 23.60 C ANISOU 1438 CA MET A 183 3194 2821 2951 93 293 -104 C ATOM 1439 C MET A 183 13.429 18.537 16.142 1.00 23.57 C ANISOU 1439 C MET A 183 3213 2844 2900 78 262 -147 C ATOM 1440 O MET A 183 13.113 17.502 15.517 1.00 23.86 O ANISOU 1440 O MET A 183 3268 2889 2910 80 271 -195 O ATOM 1441 CB MET A 183 15.674 17.632 16.957 1.00 23.63 C ANISOU 1441 CB MET A 183 3196 2784 2999 92 306 -122 C ATOM 1442 CG MET A 183 17.200 17.627 16.768 1.00 23.85 C ANISOU 1442 CG MET A 183 3204 2795 3061 114 346 -92 C ATOM 1443 SD MET A 183 17.995 16.370 17.807 1.00 27.67 S ANISOU 1443 SD MET A 183 3678 3231 3606 114 353 -100 S ATOM 1444 CE MET A 183 17.144 14.882 17.289 1.00 24.07 C ANISOU 1444 CE MET A 183 3258 2767 3121 110 361 -163 C ATOM 1445 N GLN A 184 12.569 19.434 16.637 1.00 23.27 N ANISOU 1445 N GLN A 184 3169 2818 2856 65 228 -131 N ATOM 1446 CA GLN A 184 11.128 19.450 16.413 1.00 23.26 C ANISOU 1446 CA GLN A 184 3179 2848 2809 53 197 -162 C ATOM 1447 C GLN A 184 10.375 18.440 17.269 1.00 23.07 C ANISOU 1447 C GLN A 184 3161 2798 2806 25 172 -203 C ATOM 1448 O GLN A 184 9.254 18.059 16.904 1.00 25.57 O ANISOU 1448 O GLN A 184 3489 3140 3087 15 154 -245 O ATOM 1449 CB GLN A 184 10.787 19.225 14.927 1.00 23.74 C ANISOU 1449 CB GLN A 184 3259 2960 2802 74 212 -190 C ATOM 1450 CG GLN A 184 11.557 20.181 13.979 1.00 24.53 C ANISOU 1450 CG GLN A 184 3355 3087 2877 107 245 -143 C ATOM 1451 CD GLN A 184 11.151 21.644 14.173 1.00 25.55 C ANISOU 1451 CD GLN A 184 3473 3232 3002 111 231 -93 C ATOM 1452 OE1 GLN A 184 10.070 22.064 13.747 1.00 24.03 O ANISOU 1452 OE1 GLN A 184 3286 3082 2761 116 209 -99 O ATOM 1453 NE2 GLN A 184 12.034 22.434 14.793 1.00 23.62 N ANISOU 1453 NE2 GLN A 184 3209 2953 2812 110 246 -44 N ATOM 1454 N CYS A 185 10.943 18.000 18.401 1.00 22.83 N ANISOU 1454 N CYS A 185 3121 2720 2832 15 172 -193 N ATOM 1455 CA CYS A 185 10.264 17.052 19.282 1.00 25.29 C ANISOU 1455 CA CYS A 185 3438 3003 3168 -8 155 -224 C ATOM 1456 C CYS A 185 9.836 17.671 20.606 1.00 23.49 C ANISOU 1456 C CYS A 185 3197 2761 2968 -24 123 -197 C ATOM 1457 O CYS A 185 9.378 16.944 21.489 1.00 24.26 O ANISOU 1457 O CYS A 185 3297 2831 3090 -40 112 -213 O ATOM 1458 CB CYS A 185 11.146 15.824 19.540 1.00 27.28 C ANISOU 1458 CB CYS A 185 3694 3214 3459 -2 185 -236 C ATOM 1459 SG CYS A 185 11.431 14.868 18.035 1.00 30.88 S ANISOU 1459 SG CYS A 185 4168 3682 3882 13 223 -283 S ATOM 1460 N SER A 186 9.969 18.990 20.766 1.00 22.05 N ANISOU 1460 N SER A 186 3000 2594 2784 -20 111 -158 N ATOM 1461 CA SER A 186 9.342 19.701 21.875 1.00 22.01 C ANISOU 1461 CA SER A 186 2984 2583 2794 -36 79 -141 C ATOM 1462 C SER A 186 8.745 20.977 21.310 1.00 21.65 C ANISOU 1462 C SER A 186 2937 2574 2717 -32 68 -123 C ATOM 1463 O SER A 186 9.093 21.390 20.203 1.00 23.18 O ANISOU 1463 O SER A 186 3133 2791 2882 -14 88 -113 O ATOM 1464 CB SER A 186 10.335 20.013 23.014 1.00 22.91 C ANISOU 1464 CB SER A 186 3078 2670 2958 -35 78 -108 C ATOM 1465 OG SER A 186 11.299 20.977 22.576 1.00 23.82 O ANISOU 1465 OG SER A 186 3178 2793 3081 -21 95 -76 O ATOM 1466 N CYS A 187 7.803 21.582 22.043 1.00 21.39 N ANISOU 1466 N CYS A 187 2898 2544 2684 -48 38 -119 N ATOM 1467 CA CYS A 187 7.200 22.833 21.595 1.00 21.38 C ANISOU 1467 CA CYS A 187 2894 2573 2657 -41 28 -97 C ATOM 1468 C CYS A 187 7.439 23.953 22.597 1.00 21.71 C ANISOU 1468 C CYS A 187 2917 2596 2736 -48 18 -63 C ATOM 1469 O CYS A 187 7.520 23.719 23.808 1.00 22.75 O ANISOU 1469 O CYS A 187 3041 2702 2901 -63 2 -66 O ATOM 1470 CB CYS A 187 5.705 22.667 21.336 1.00 21.41 C ANISOU 1470 CB CYS A 187 2906 2605 2622 -51 4 -126 C ATOM 1471 SG CYS A 187 5.490 21.843 19.763 1.00 21.90 S ANISOU 1471 SG CYS A 187 2984 2707 2629 -36 18 -164 S ATOM 1472 N GLY A 188 7.567 25.171 22.077 1.00 21.19 N ANISOU 1472 N GLY A 188 2845 2544 2664 -35 29 -31 N ATOM 1473 CA GLY A 188 7.690 26.329 22.931 1.00 21.99 C ANISOU 1473 CA GLY A 188 2927 2626 2801 -42 22 -4 C ATOM 1474 C GLY A 188 6.888 27.498 22.398 1.00 22.44 C ANISOU 1474 C GLY A 188 2985 2706 2835 -32 22 19 C ATOM 1475 O GLY A 188 6.102 27.350 21.460 1.00 21.60 O ANISOU 1475 O GLY A 188 2892 2634 2679 -19 20 13 O ATOM 1476 N ILE A 189 7.080 28.666 23.001 1.00 22.84 N ANISOU 1476 N ILE A 189 3019 2736 2922 -37 25 45 N ATOM 1477 CA ILE A 189 6.489 29.898 22.489 1.00 21.13 C ANISOU 1477 CA ILE A 189 2802 2533 2695 -23 34 76 C ATOM 1478 C ILE A 189 7.126 30.268 21.148 1.00 23.40 C ANISOU 1478 C ILE A 189 3093 2836 2964 6 75 108 C ATOM 1479 O ILE A 189 8.313 30.025 20.909 1.00 25.95 O ANISOU 1479 O ILE A 189 3409 3143 3308 10 101 114 O ATOM 1480 CB ILE A 189 6.680 31.011 23.531 1.00 20.99 C ANISOU 1480 CB ILE A 189 2764 2480 2730 -38 33 91 C ATOM 1481 CG1 ILE A 189 5.968 30.619 24.814 1.00 24.62 C ANISOU 1481 CG1 ILE A 189 3223 2933 3199 -62 -6 61 C ATOM 1482 CG2 ILE A 189 6.180 32.365 22.999 1.00 29.24 C ANISOU 1482 CG2 ILE A 189 3806 3530 3774 -21 53 129 C ATOM 1483 CD1 ILE A 189 4.477 30.501 24.638 1.00 30.23 C ANISOU 1483 CD1 ILE A 189 3947 3671 3866 -59 -29 51 C ATOM 1484 N ASP A 190 6.336 30.856 20.253 1.00 23.97 N ANISOU 1484 N ASP A 190 3174 2941 2994 30 82 130 N ATOM 1485 CA ASP A 190 6.860 31.198 18.923 1.00 24.08 C ANISOU 1485 CA ASP A 190 3193 2976 2981 64 123 165 C ATOM 1486 C ASP A 190 7.733 32.456 19.029 1.00 26.04 C ANISOU 1486 C ASP A 190 3424 3186 3286 69 164 211 C ATOM 1487 O ASP A 190 7.232 33.576 18.926 1.00 24.18 O ANISOU 1487 O ASP A 190 3183 2947 3056 82 176 246 O ATOM 1488 CB ASP A 190 5.703 31.404 17.943 1.00 23.53 C ANISOU 1488 CB ASP A 190 3137 2962 2842 93 116 176 C ATOM 1489 CG ASP A 190 6.173 31.599 16.515 1.00 28.16 C ANISOU 1489 CG ASP A 190 3733 3582 3387 134 157 209 C ATOM 1490 OD1 ASP A 190 7.405 31.660 16.290 1.00 25.92 O ANISOU 1490 OD1 ASP A 190 3443 3271 3133 138 195 228 O ATOM 1491 OD2 ASP A 190 5.314 31.668 15.609 1.00 27.19 O ANISOU 1491 OD2 ASP A 190 3620 3514 3197 164 151 216 O ATOM 1492 N TYR A 191 9.055 32.266 19.224 1.00 24.30 N ANISOU 1492 N TYR A 191 3189 2932 3110 59 187 211 N ATOM 1493 CA TYR A 191 10.087 33.304 19.078 1.00 22.64 C ANISOU 1493 CA TYR A 191 2959 2687 2955 64 234 252 C ATOM 1494 C TYR A 191 10.553 33.467 17.642 1.00 24.62 C ANISOU 1494 C TYR A 191 3220 2962 3174 103 284 291 C ATOM 1495 O TYR A 191 11.378 34.347 17.372 1.00 28.51 O ANISOU 1495 O TYR A 191 3696 3424 3710 111 332 331 O ATOM 1496 CB TYR A 191 11.351 32.979 19.938 1.00 24.08 C ANISOU 1496 CB TYR A 191 3117 2831 3202 37 236 231 C ATOM 1497 CG TYR A 191 11.036 32.185 21.182 1.00 22.85 C ANISOU 1497 CG TYR A 191 2959 2669 3054 7 184 183 C ATOM 1498 CD1 TYR A 191 10.367 32.773 22.237 1.00 22.65 C ANISOU 1498 CD1 TYR A 191 2925 2628 3052 -14 156 172 C ATOM 1499 CD2 TYR A 191 11.361 30.826 21.277 1.00 24.75 C ANISOU 1499 CD2 TYR A 191 3208 2921 3276 3 167 151 C ATOM 1500 CE1 TYR A 191 10.044 32.046 23.382 1.00 23.66 C ANISOU 1500 CE1 TYR A 191 3053 2754 3183 -37 112 133 C ATOM 1501 CE2 TYR A 191 11.042 30.093 22.414 1.00 22.21 C ANISOU 1501 CE2 TYR A 191 2885 2594 2961 -20 125 114 C ATOM 1502 CZ TYR A 191 10.369 30.718 23.459 1.00 26.53 C ANISOU 1502 CZ TYR A 191 3424 3128 3528 -39 97 106 C ATOM 1503 OH TYR A 191 10.007 30.015 24.589 1.00 24.87 O ANISOU 1503 OH TYR A 191 3214 2915 3320 -58 58 74 O ATOM 1504 N TYR A 192 10.069 32.628 16.723 1.00 27.64 N ANISOU 1504 N TYR A 192 3626 3395 3481 126 275 279 N ATOM 1505 CA TYR A 192 10.707 32.435 15.418 1.00 26.19 C ANISOU 1505 CA TYR A 192 3453 3238 3261 161 318 304 C ATOM 1506 C TYR A 192 10.131 33.308 14.314 1.00 26.51 C ANISOU 1506 C TYR A 192 3505 3316 3253 205 348 356 C ATOM 1507 O TYR A 192 10.852 33.663 13.376 1.00 27.79 O ANISOU 1507 O TYR A 192 3668 3482 3407 236 401 398 O ATOM 1508 CB TYR A 192 10.575 30.974 14.986 1.00 23.69 C ANISOU 1508 CB TYR A 192 3156 2959 2887 163 295 256 C ATOM 1509 CG TYR A 192 11.201 30.063 16.002 1.00 26.43 C ANISOU 1509 CG TYR A 192 3492 3270 3281 127 273 212 C ATOM 1510 CD1 TYR A 192 10.460 29.578 17.061 1.00 25.44 C ANISOU 1510 CD1 TYR A 192 3367 3136 3164 96 223 172 C ATOM 1511 CD2 TYR A 192 12.550 29.749 15.927 1.00 24.74 C ANISOU 1511 CD2 TYR A 192 3266 3031 3104 126 305 217 C ATOM 1512 CE1 TYR A 192 11.056 28.766 18.040 1.00 25.04 C ANISOU 1512 CE1 TYR A 192 3306 3053 3156 68 205 140 C ATOM 1513 CE2 TYR A 192 13.149 28.957 16.876 1.00 23.15 C ANISOU 1513 CE2 TYR A 192 3052 2798 2945 98 286 183 C ATOM 1514 CZ TYR A 192 12.394 28.465 17.920 1.00 22.82 C ANISOU 1514 CZ TYR A 192 3012 2750 2908 72 236 146 C ATOM 1515 OH TYR A 192 13.003 27.679 18.859 1.00 23.85 O ANISOU 1515 OH TYR A 192 3131 2854 3077 50 220 118 O ATOM 1516 N THR A 193 8.839 33.599 14.369 1.00 24.41 N ANISOU 1516 N THR A 193 3248 3079 2949 212 316 355 N ATOM 1517 CA THR A 193 8.166 34.222 13.245 1.00 30.63 C ANISOU 1517 CA THR A 193 4048 3917 3673 262 337 400 C ATOM 1518 C THR A 193 7.332 35.387 13.745 1.00 31.39 C ANISOU 1518 C THR A 193 4135 3996 3794 263 332 432 C ATOM 1519 O THR A 193 6.882 35.380 14.890 1.00 30.14 O ANISOU 1519 O THR A 193 3968 3808 3674 226 294 401 O ATOM 1520 CB THR A 193 7.239 33.232 12.513 1.00 33.93 C ANISOU 1520 CB THR A 193 4486 4411 3996 280 298 361 C ATOM 1521 OG1 THR A 193 6.025 33.076 13.263 1.00 29.59 O ANISOU 1521 OG1 THR A 193 3934 3871 3438 257 243 326 O ATOM 1522 CG2 THR A 193 7.910 31.866 12.326 1.00 30.88 C ANISOU 1522 CG2 THR A 193 4107 4031 3594 265 291 308 C ATOM 1523 N PRO A 194 7.103 36.395 12.906 1.00 33.33 N ANISOU 1523 N PRO A 194 4385 4261 4019 309 372 498 N ATOM 1524 CA PRO A 194 6.296 37.532 13.366 1.00 31.37 C ANISOU 1524 CA PRO A 194 4129 3993 3798 314 373 532 C ATOM 1525 C PRO A 194 4.817 37.208 13.501 1.00 34.78 C ANISOU 1525 C PRO A 194 4567 4476 4170 318 314 502 C ATOM 1526 O PRO A 194 4.154 37.775 14.378 1.00 38.97 O ANISOU 1526 O PRO A 194 5089 4980 4739 299 294 500 O ATOM 1527 CB PRO A 194 6.545 38.599 12.289 1.00 38.88 C ANISOU 1527 CB PRO A 194 5083 4952 4738 370 440 615 C ATOM 1528 CG PRO A 194 7.679 38.095 11.445 1.00 42.92 C ANISOU 1528 CG PRO A 194 5601 5474 5233 386 480 625 C ATOM 1529 CD PRO A 194 7.669 36.615 11.565 1.00 33.80 C ANISOU 1529 CD PRO A 194 4455 4352 4036 360 428 549 C ATOM 1530 N HIS A 195 4.267 36.406 12.583 1.00 34.78 N ANISOU 1530 N HIS A 195 4581 4554 4079 345 290 482 N ATOM 1531 CA HIS A 195 2.897 35.887 12.606 1.00 36.42 C ANISOU 1531 CA HIS A 195 4792 4821 4226 346 231 443 C ATOM 1532 C HIS A 195 1.871 36.845 13.202 1.00 34.95 C ANISOU 1532 C HIS A 195 4595 4624 4061 349 218 468 C ATOM 1533 O HIS A 195 1.339 36.587 14.292 1.00 33.03 O ANISOU 1533 O HIS A 195 4344 4354 3851 307 176 425 O ATOM 1534 CB HIS A 195 2.794 34.533 13.306 1.00 34.41 C ANISOU 1534 CB HIS A 195 4538 4562 3973 296 180 359 C ATOM 1535 CG HIS A 195 1.651 33.717 12.786 1.00 33.97 C ANISOU 1535 CG HIS A 195 4487 4584 3835 306 132 314 C ATOM 1536 ND1 HIS A 195 0.532 33.425 13.537 1.00 34.29 N ANISOU 1536 ND1 HIS A 195 4519 4632 3877 279 81 273 N ATOM 1537 CD2 HIS A 195 1.412 33.217 11.549 1.00 38.59 C ANISOU 1537 CD2 HIS A 195 5081 5247 4334 344 130 304 C ATOM 1538 CE1 HIS A 195 -0.321 32.731 12.800 1.00 37.89 C ANISOU 1538 CE1 HIS A 195 4977 5164 4256 295 48 236 C ATOM 1539 NE2 HIS A 195 0.188 32.595 11.589 1.00 36.77 N ANISOU 1539 NE2 HIS A 195 4846 5069 4058 334 75 252 N ATOM 1540 N GLU A 196 1.625 37.964 12.512 1.00 36.40 N ANISOU 1540 N GLU A 196 4779 4824 4228 401 256 541 N ATOM 1541 CA GLU A 196 0.769 39.035 13.035 1.00 35.01 C ANISOU 1541 CA GLU A 196 4593 4628 4082 410 256 576 C ATOM 1542 C GLU A 196 -0.620 38.553 13.439 1.00 30.34 C ANISOU 1542 C GLU A 196 3995 4081 3450 398 190 529 C ATOM 1543 O GLU A 196 -1.252 39.163 14.311 1.00 35.34 O ANISOU 1543 O GLU A 196 4618 4681 4128 382 179 532 O ATOM 1544 CB GLU A 196 0.624 40.152 12.000 1.00 47.09 C ANISOU 1544 CB GLU A 196 6126 6184 5583 479 309 664 C ATOM 1545 CG GLU A 196 1.762 41.151 11.983 1.00 56.56 C ANISOU 1545 CG GLU A 196 7323 7309 6858 486 385 726 C ATOM 1546 CD GLU A 196 2.861 40.763 11.016 1.00 61.77 C ANISOU 1546 CD GLU A 196 7994 7985 7492 508 426 744 C ATOM 1547 OE1 GLU A 196 2.751 39.677 10.401 1.00 62.49 O ANISOU 1547 OE1 GLU A 196 8096 8145 7505 515 392 703 O ATOM 1548 OE2 GLU A 196 3.827 41.546 10.867 1.00 70.08 O ANISOU 1548 OE2 GLU A 196 9042 8980 8604 516 493 797 O ATOM 1549 N GLU A 197 -1.137 37.500 12.801 1.00 34.06 N ANISOU 1549 N GLU A 197 4471 4629 3841 406 150 484 N ATOM 1550 CA GLU A 197 -2.465 37.015 13.168 1.00 34.51 C ANISOU 1550 CA GLU A 197 4518 4730 3866 392 89 436 C ATOM 1551 C GLU A 197 -2.559 36.687 14.654 1.00 38.97 C ANISOU 1551 C GLU A 197 5076 5229 4503 328 60 386 C ATOM 1552 O GLU A 197 -3.621 36.864 15.267 1.00 34.44 O ANISOU 1552 O GLU A 197 4490 4660 3934 318 28 372 O ATOM 1553 CB GLU A 197 -2.830 35.787 12.337 1.00 38.72 C ANISOU 1553 CB GLU A 197 5054 5344 4312 399 51 379 C ATOM 1554 CG GLU A 197 -4.248 35.292 12.589 1.00 58.05 C ANISOU 1554 CG GLU A 197 7488 7844 6726 386 -10 329 C ATOM 1555 CD GLU A 197 -4.567 34.008 11.844 1.00 68.56 C ANISOU 1555 CD GLU A 197 8818 9249 7983 384 -47 260 C ATOM 1556 OE1 GLU A 197 -3.908 32.979 12.113 1.00 69.86 O ANISOU 1556 OE1 GLU A 197 8992 9384 8168 342 -52 205 O ATOM 1557 OE2 GLU A 197 -5.479 34.030 10.990 1.00 72.04 O ANISOU 1557 OE2 GLU A 197 9248 9779 8346 424 -70 258 O ATOM 1558 N THR A 198 -1.468 36.227 15.264 1.00 33.19 N ANISOU 1558 N THR A 198 4350 4437 3825 287 72 360 N ATOM 1559 CA THR A 198 -1.492 35.914 16.689 1.00 29.80 C ANISOU 1559 CA THR A 198 3914 3949 3460 231 46 317 C ATOM 1560 C THR A 198 -0.717 36.925 17.533 1.00 30.79 C ANISOU 1560 C THR A 198 4034 3994 3671 215 82 350 C ATOM 1561 O THR A 198 -0.471 36.668 18.714 1.00 29.02 O ANISOU 1561 O THR A 198 3806 3721 3501 170 65 315 O ATOM 1562 CB THR A 198 -0.970 34.490 16.940 1.00 27.84 C ANISOU 1562 CB THR A 198 3672 3696 3209 192 22 252 C ATOM 1563 OG1 THR A 198 0.237 34.280 16.211 1.00 31.89 O ANISOU 1563 OG1 THR A 198 4195 4204 3717 206 59 267 O ATOM 1564 CG2 THR A 198 -2.005 33.459 16.496 1.00 29.53 C ANISOU 1564 CG2 THR A 198 3886 3977 3356 192 -22 200 C ATOM 1565 N ASN A 199 -0.338 38.067 16.957 1.00 29.70 N ANISOU 1565 N ASN A 199 3895 3842 3547 252 132 417 N ATOM 1566 CA ASN A 199 0.299 39.157 17.695 1.00 33.08 C ANISOU 1566 CA ASN A 199 4314 4193 4061 238 171 448 C ATOM 1567 C ASN A 199 1.513 38.666 18.487 1.00 34.41 C ANISOU 1567 C ASN A 199 4478 4306 4289 190 174 410 C ATOM 1568 O ASN A 199 1.664 38.929 19.688 1.00 28.94 O ANISOU 1568 O ASN A 199 3775 3562 3659 153 164 387 O ATOM 1569 CB ASN A 199 -0.723 39.856 18.585 1.00 32.56 C ANISOU 1569 CB ASN A 199 4239 4109 4025 228 152 448 C ATOM 1570 CG ASN A 199 -1.786 40.569 17.768 1.00 43.22 C ANISOU 1570 CG ASN A 199 5589 5507 5326 283 161 498 C ATOM 1571 OD1 ASN A 199 -1.485 41.514 17.050 1.00 40.21 O ANISOU 1571 OD1 ASN A 199 5209 5118 4952 324 212 564 O ATOM 1572 ND2 ASN A 199 -3.026 40.105 17.856 1.00 43.10 N ANISOU 1572 ND2 ASN A 199 5570 5543 5262 285 112 470 N ATOM 1573 N ASN A 200 2.399 37.951 17.775 1.00 30.01 N ANISOU 1573 N ASN A 200 3928 3765 3708 196 187 405 N ATOM 1574 CA ASN A 200 3.487 37.217 18.420 1.00 28.09 C ANISOU 1574 CA ASN A 200 3681 3485 3507 156 182 365 C ATOM 1575 C ASN A 200 4.418 38.139 19.187 1.00 28.43 C ANISOU 1575 C ASN A 200 3706 3455 3640 134 217 381 C ATOM 1576 O ASN A 200 4.849 37.806 20.296 1.00 28.24 O ANISOU 1576 O ASN A 200 3671 3396 3662 92 195 339 O ATOM 1577 CB ASN A 200 4.315 36.448 17.380 1.00 30.70 C ANISOU 1577 CB ASN A 200 4022 3844 3799 174 202 366 C ATOM 1578 CG ASN A 200 3.738 35.086 17.028 1.00 32.42 C ANISOU 1578 CG ASN A 200 4253 4118 3946 172 159 316 C ATOM 1579 OD1 ASN A 200 2.640 34.741 17.439 1.00 27.77 O ANISOU 1579 OD1 ASN A 200 3665 3552 3333 160 115 286 O ATOM 1580 ND2 ASN A 200 4.481 34.315 16.211 1.00 27.81 N ANISOU 1580 ND2 ASN A 200 3679 3557 3332 183 174 308 N ATOM 1581 N GLU A 201 4.788 39.279 18.588 1.00 29.47 N ANISOU 1581 N GLU A 201 3833 3564 3799 162 273 440 N ATOM 1582 CA GLU A 201 5.802 40.137 19.196 1.00 27.83 C ANISOU 1582 CA GLU A 201 3604 3285 3683 139 312 451 C ATOM 1583 C GLU A 201 5.364 40.631 20.565 1.00 30.50 C ANISOU 1583 C GLU A 201 3929 3583 4075 103 286 420 C ATOM 1584 O GLU A 201 6.138 40.586 21.530 1.00 29.70 O ANISOU 1584 O GLU A 201 3810 3441 4034 64 280 384 O ATOM 1585 CB GLU A 201 6.129 41.338 18.293 1.00 35.62 C ANISOU 1585 CB GLU A 201 4589 4252 4694 177 383 524 C ATOM 1586 CG GLU A 201 7.184 42.265 18.912 1.00 41.18 C ANISOU 1586 CG GLU A 201 5267 4877 5504 149 429 531 C ATOM 1587 CD GLU A 201 7.514 43.498 18.071 1.00 52.97 C ANISOU 1587 CD GLU A 201 6755 6338 7033 186 508 607 C ATOM 1588 OE1 GLU A 201 6.579 44.177 17.602 1.00 48.45 O ANISOU 1588 OE1 GLU A 201 6194 5782 6434 224 524 653 O ATOM 1589 OE2 GLU A 201 8.716 43.789 17.897 1.00 51.93 O ANISOU 1589 OE2 GLU A 201 6606 6165 6959 176 557 620 O ATOM 1590 N SER A 202 4.117 41.072 20.688 1.00 28.70 N ANISOU 1590 N SER A 202 3707 3371 3824 118 270 431 N ATOM 1591 CA SER A 202 3.712 41.602 21.981 1.00 27.77 C ANISOU 1591 CA SER A 202 3578 3215 3760 86 250 402 C ATOM 1592 C SER A 202 3.623 40.508 23.040 1.00 28.38 C ANISOU 1592 C SER A 202 3655 3303 3827 46 190 335 C ATOM 1593 O SER A 202 3.866 40.775 24.218 1.00 28.15 O ANISOU 1593 O SER A 202 3611 3234 3850 12 179 301 O ATOM 1594 CB SER A 202 2.392 42.366 21.856 1.00 28.13 C ANISOU 1594 CB SER A 202 3630 3274 3786 114 250 432 C ATOM 1595 OG SER A 202 1.325 41.534 21.463 1.00 31.55 O ANISOU 1595 OG SER A 202 4077 3773 4136 131 206 422 O ATOM 1596 N PHE A 203 3.292 39.270 22.668 1.00 25.73 N ANISOU 1596 N PHE A 203 3334 3018 3424 50 155 312 N ATOM 1597 CA PHE A 203 3.271 38.246 23.706 1.00 25.74 C ANISOU 1597 CA PHE A 203 3334 3022 3423 14 106 254 C ATOM 1598 C PHE A 203 4.673 37.986 24.260 1.00 25.21 C ANISOU 1598 C PHE A 203 3252 2920 3406 -13 115 232 C ATOM 1599 O PHE A 203 4.840 37.814 25.473 1.00 25.93 O ANISOU 1599 O PHE A 203 3333 2991 3530 -44 89 194 O ATOM 1600 CB PHE A 203 2.650 36.924 23.210 1.00 23.63 C ANISOU 1600 CB PHE A 203 3085 2810 3082 21 71 231 C ATOM 1601 CG PHE A 203 2.655 35.854 24.271 1.00 26.27 C ANISOU 1601 CG PHE A 203 3420 3142 3421 -13 29 178 C ATOM 1602 CD1 PHE A 203 1.616 35.771 25.194 1.00 24.39 C ANISOU 1602 CD1 PHE A 203 3182 2906 3178 -29 -6 154 C ATOM 1603 CD2 PHE A 203 3.735 34.977 24.407 1.00 27.20 C ANISOU 1603 CD2 PHE A 203 3535 3250 3549 -28 28 156 C ATOM 1604 CE1 PHE A 203 1.626 34.827 26.209 1.00 27.95 C ANISOU 1604 CE1 PHE A 203 3633 3353 3634 -56 -38 111 C ATOM 1605 CE2 PHE A 203 3.743 34.039 25.417 1.00 32.27 C ANISOU 1605 CE2 PHE A 203 4178 3888 4195 -54 -6 114 C ATOM 1606 CZ PHE A 203 2.691 33.959 26.323 1.00 27.04 C ANISOU 1606 CZ PHE A 203 3518 3230 3528 -68 -38 93 C ATOM 1607 N VAL A 204 5.688 37.926 23.393 1.00 26.32 N ANISOU 1607 N VAL A 204 3391 3058 3552 0 150 255 N ATOM 1608 CA VAL A 204 7.038 37.613 23.859 1.00 26.88 C ANISOU 1608 CA VAL A 204 3443 3100 3669 -23 158 234 C ATOM 1609 C VAL A 204 7.561 38.698 24.808 1.00 27.64 C ANISOU 1609 C VAL A 204 3513 3144 3846 -48 173 226 C ATOM 1610 O VAL A 204 8.207 38.397 25.818 1.00 29.27 O ANISOU 1610 O VAL A 204 3700 3335 4086 -78 152 187 O ATOM 1611 CB VAL A 204 7.977 37.380 22.663 1.00 28.52 C ANISOU 1611 CB VAL A 204 3653 3316 3866 -1 198 263 C ATOM 1612 CG1 VAL A 204 9.390 37.122 23.157 1.00 27.98 C ANISOU 1612 CG1 VAL A 204 3561 3218 3852 -25 207 242 C ATOM 1613 CG2 VAL A 204 7.473 36.156 21.857 1.00 28.11 C ANISOU 1613 CG2 VAL A 204 3628 3319 3734 18 176 254 C ATOM 1614 N AILE A 205 7.300 39.970 24.492 0.40 26.37 N ANISOU 1614 N AILE A 205 3347 2957 3717 -35 212 263 N ATOM 1615 N BILE A 205 7.302 39.969 24.500 0.60 26.31 N ANISOU 1615 N BILE A 205 3339 2949 3710 -36 212 263 N ATOM 1616 CA AILE A 205 7.688 41.058 25.391 0.40 30.69 C ANISOU 1616 CA AILE A 205 3867 3450 4344 -61 229 250 C ATOM 1617 CA BILE A 205 7.716 41.033 25.416 0.60 30.75 C ANISOU 1617 CA BILE A 205 3873 3457 4352 -62 228 248 C ATOM 1618 C AILE A 205 6.958 40.933 26.720 0.40 26.79 C ANISOU 1618 C AILE A 205 3372 2959 3850 -86 179 203 C ATOM 1619 C BILE A 205 6.961 40.925 26.733 0.60 26.77 C ANISOU 1619 C BILE A 205 3368 2955 3846 -86 178 202 C ATOM 1620 O AILE A 205 7.555 41.087 27.794 0.40 28.95 O ANISOU 1620 O AILE A 205 3622 3208 4171 -118 165 162 O ATOM 1621 O BILE A 205 7.544 41.085 27.814 0.60 28.98 O ANISOU 1621 O BILE A 205 3625 3211 4174 -118 165 161 O ATOM 1622 CB AILE A 205 7.421 42.424 24.730 0.40 33.40 C ANISOU 1622 CB AILE A 205 4208 3761 4721 -38 286 303 C ATOM 1623 CB BILE A 205 7.526 42.414 24.765 0.60 33.48 C ANISOU 1623 CB BILE A 205 4216 3768 4735 -41 286 300 C ATOM 1624 CG1AILE A 205 8.199 42.542 23.418 0.40 30.78 C ANISOU 1624 CG1AILE A 205 3877 3428 4388 -10 340 354 C ATOM 1625 CG1BILE A 205 8.303 42.486 23.454 0.60 30.76 C ANISOU 1625 CG1BILE A 205 3874 3425 4389 -13 340 351 C ATOM 1626 CG2AILE A 205 7.775 43.569 25.691 0.40 29.66 C ANISOU 1626 CG2AILE A 205 3706 3226 4337 -68 306 282 C ATOM 1627 CG2BILE A 205 7.959 43.532 25.725 0.60 29.60 C ANISOU 1627 CG2BILE A 205 3695 3216 4335 -72 307 278 C ATOM 1628 CD1AILE A 205 9.686 42.643 23.612 0.40 33.21 C ANISOU 1628 CD1AILE A 205 4155 3698 4764 -35 368 339 C ATOM 1629 CD1BILE A 205 8.200 43.823 22.791 0.60 37.45 C ANISOU 1629 CD1BILE A 205 4718 4236 5276 12 405 409 C ATOM 1630 N TYR A 206 5.656 40.655 26.664 1.00 27.96 N ANISOU 1630 N TYR A 206 3543 3138 3942 -71 152 207 N ATOM 1631 CA TYR A 206 4.876 40.413 27.876 1.00 27.74 C ANISOU 1631 CA TYR A 206 3517 3118 3906 -92 105 166 C ATOM 1632 C TYR A 206 5.468 39.278 28.699 1.00 30.44 C ANISOU 1632 C TYR A 206 3854 3474 4238 -116 65 120 C ATOM 1633 O TYR A 206 5.628 39.393 29.925 1.00 28.73 O ANISOU 1633 O TYR A 206 3622 3244 4050 -140 43 81 O ATOM 1634 CB TYR A 206 3.442 40.085 27.466 1.00 25.52 C ANISOU 1634 CB TYR A 206 3260 2876 3561 -69 84 181 C ATOM 1635 CG TYR A 206 2.599 39.346 28.474 1.00 26.18 C ANISOU 1635 CG TYR A 206 3352 2982 3615 -86 33 140 C ATOM 1636 CD1 TYR A 206 2.133 39.982 29.633 1.00 27.66 C ANISOU 1636 CD1 TYR A 206 3529 3146 3833 -103 21 117 C ATOM 1637 CD2 TYR A 206 2.256 38.008 28.273 1.00 24.12 C ANISOU 1637 CD2 TYR A 206 3106 2762 3297 -84 0 125 C ATOM 1638 CE1 TYR A 206 1.340 39.293 30.554 1.00 27.48 C ANISOU 1638 CE1 TYR A 206 3515 3146 3782 -116 -22 84 C ATOM 1639 CE2 TYR A 206 1.452 37.316 29.187 1.00 26.95 C ANISOU 1639 CE2 TYR A 206 3471 3137 3632 -98 -40 92 C ATOM 1640 CZ TYR A 206 0.998 37.965 30.316 1.00 30.47 C ANISOU 1640 CZ TYR A 206 3908 3562 4106 -113 -50 74 C ATOM 1641 OH TYR A 206 0.187 37.281 31.204 1.00 30.78 O ANISOU 1641 OH TYR A 206 3955 3620 4122 -124 -86 46 O ATOM 1642 N MET A 207 5.818 38.171 28.044 1.00 25.05 N ANISOU 1642 N MET A 207 3182 2820 3514 -106 58 123 N ATOM 1643 CA MET A 207 6.322 37.028 28.798 1.00 30.87 C ANISOU 1643 CA MET A 207 3916 3571 4241 -123 23 85 C ATOM 1644 C MET A 207 7.645 37.354 29.475 1.00 25.57 C ANISOU 1644 C MET A 207 3213 2872 3629 -143 31 65 C ATOM 1645 O MET A 207 7.848 37.029 30.653 1.00 31.30 O ANISOU 1645 O MET A 207 3928 3601 4365 -162 -1 27 O ATOM 1646 CB MET A 207 6.492 35.804 27.896 1.00 28.36 C ANISOU 1646 CB MET A 207 3617 3285 3875 -107 20 93 C ATOM 1647 CG MET A 207 6.963 34.557 28.672 1.00 28.89 C ANISOU 1647 CG MET A 207 3682 3363 3932 -121 -12 58 C ATOM 1648 SD MET A 207 7.095 33.088 27.616 1.00 30.56 S ANISOU 1648 SD MET A 207 3916 3604 4091 -104 -10 62 S ATOM 1649 CE MET A 207 8.442 33.572 26.604 1.00 23.46 C ANISOU 1649 CE MET A 207 3002 2690 3222 -92 37 91 C ATOM 1650 N PHE A 208 8.570 37.974 28.751 1.00 23.85 N ANISOU 1650 N PHE A 208 2980 2632 3451 -139 74 88 N ATOM 1651 CA PHE A 208 9.870 38.221 29.361 1.00 25.16 C ANISOU 1651 CA PHE A 208 3110 2774 3675 -160 80 64 C ATOM 1652 C PHE A 208 9.797 39.288 30.446 1.00 29.41 C ANISOU 1652 C PHE A 208 3624 3283 4266 -184 76 34 C ATOM 1653 O PHE A 208 10.562 39.228 31.415 1.00 31.73 O ANISOU 1653 O PHE A 208 3889 3575 4591 -206 56 -6 O ATOM 1654 CB PHE A 208 10.901 38.611 28.305 1.00 24.88 C ANISOU 1654 CB PHE A 208 3060 2718 3674 -151 132 96 C ATOM 1655 CG PHE A 208 11.581 37.435 27.681 1.00 35.40 C ANISOU 1655 CG PHE A 208 4399 4076 4974 -138 131 102 C ATOM 1656 CD1 PHE A 208 12.538 36.706 28.399 1.00 42.41 C ANISOU 1656 CD1 PHE A 208 5265 4971 5878 -152 107 70 C ATOM 1657 CD2 PHE A 208 11.245 37.019 26.401 1.00 30.57 C ANISOU 1657 CD2 PHE A 208 3817 3485 4314 -110 152 139 C ATOM 1658 CE1 PHE A 208 13.161 35.592 27.832 1.00 31.18 C ANISOU 1658 CE1 PHE A 208 3849 3569 4428 -138 109 76 C ATOM 1659 CE2 PHE A 208 11.873 35.917 25.825 1.00 36.40 C ANISOU 1659 CE2 PHE A 208 4562 4245 5024 -98 153 141 C ATOM 1660 CZ PHE A 208 12.828 35.199 26.546 1.00 33.03 C ANISOU 1660 CZ PHE A 208 4113 3818 4617 -113 133 110 C ATOM 1661 N VAL A 209 8.901 40.271 30.306 1.00 28.53 N ANISOU 1661 N VAL A 209 3523 3153 4166 -180 94 51 N ATOM 1662 CA VAL A 209 8.819 41.329 31.316 1.00 26.33 C ANISOU 1662 CA VAL A 209 3222 2842 3941 -203 94 20 C ATOM 1663 C VAL A 209 8.054 40.844 32.535 1.00 27.24 C ANISOU 1663 C VAL A 209 3346 2984 4021 -213 41 -20 C ATOM 1664 O VAL A 209 8.543 40.908 33.669 1.00 28.73 O ANISOU 1664 O VAL A 209 3510 3172 4234 -235 17 -68 O ATOM 1665 CB VAL A 209 8.165 42.592 30.725 1.00 30.17 C ANISOU 1665 CB VAL A 209 3715 3293 4457 -191 140 56 C ATOM 1666 CG1 VAL A 209 7.871 43.578 31.839 1.00 31.08 C ANISOU 1666 CG1 VAL A 209 3812 3376 4620 -214 136 17 C ATOM 1667 CG2 VAL A 209 9.068 43.195 29.703 1.00 28.01 C ANISOU 1667 CG2 VAL A 209 3426 2987 4231 -184 199 93 C ATOM 1668 N VAL A 210 6.846 40.334 32.320 1.00 24.87 N ANISOU 1668 N VAL A 210 3078 2709 3661 -195 22 -3 N ATOM 1669 CA VAL A 210 5.961 40.026 33.439 1.00 26.28 C ANISOU 1669 CA VAL A 210 3266 2908 3810 -202 -19 -34 C ATOM 1670 C VAL A 210 6.302 38.689 34.082 1.00 28.21 C ANISOU 1670 C VAL A 210 3513 3188 4017 -206 -61 -59 C ATOM 1671 O VAL A 210 6.178 38.522 35.302 1.00 27.06 O ANISOU 1671 O VAL A 210 3361 3055 3867 -217 -92 -96 O ATOM 1672 CB VAL A 210 4.503 40.069 32.956 1.00 29.75 C ANISOU 1672 CB VAL A 210 3735 3360 4208 -183 -20 -5 C ATOM 1673 CG1 VAL A 210 3.580 39.475 33.992 1.00 30.59 C ANISOU 1673 CG1 VAL A 210 3854 3492 4277 -188 -62 -33 C ATOM 1674 CG2 VAL A 210 4.132 41.499 32.622 1.00 29.83 C ANISOU 1674 CG2 VAL A 210 3740 3332 4262 -177 20 17 C ATOM 1675 N HIS A 211 6.699 37.705 33.281 1.00 25.54 N ANISOU 1675 N HIS A 211 3187 2869 3650 -193 -59 -39 N ATOM 1676 CA HIS A 211 6.872 36.348 33.781 1.00 22.32 C ANISOU 1676 CA HIS A 211 2786 2492 3204 -192 -92 -55 C ATOM 1677 C HIS A 211 8.325 35.915 33.784 1.00 25.44 C ANISOU 1677 C HIS A 211 3157 2887 3622 -195 -89 -64 C ATOM 1678 O HIS A 211 8.605 34.707 33.752 1.00 25.53 O ANISOU 1678 O HIS A 211 3177 2920 3602 -186 -104 -63 O ATOM 1679 CB HIS A 211 6.006 35.384 32.968 1.00 22.52 C ANISOU 1679 CB HIS A 211 2844 2539 3174 -175 -96 -32 C ATOM 1680 CG HIS A 211 4.541 35.670 33.096 1.00 29.68 C ANISOU 1680 CG HIS A 211 3770 3452 4056 -171 -106 -28 C ATOM 1681 ND1 HIS A 211 3.823 35.353 34.232 1.00 24.17 N ANISOU 1681 ND1 HIS A 211 3077 2766 3341 -179 -136 -51 N ATOM 1682 CD2 HIS A 211 3.667 36.284 32.251 1.00 31.07 C ANISOU 1682 CD2 HIS A 211 3958 3626 4221 -159 -88 -1 C ATOM 1683 CE1 HIS A 211 2.564 35.740 34.076 1.00 31.60 C ANISOU 1683 CE1 HIS A 211 4032 3710 4265 -174 -136 -41 C ATOM 1684 NE2 HIS A 211 2.440 36.297 32.879 1.00 29.29 N ANISOU 1684 NE2 HIS A 211 3743 3411 3975 -161 -109 -11 N ATOM 1685 N PHE A 212 9.257 36.852 33.614 1.00 25.03 N ANISOU 1685 N PHE A 212 3075 2809 3626 -206 -63 -67 N ATOM 1686 CA PHE A 212 10.649 36.558 33.943 1.00 28.60 C ANISOU 1686 CA PHE A 212 3496 3265 4108 -213 -67 -86 C ATOM 1687 C PHE A 212 11.337 37.649 34.764 1.00 27.03 C ANISOU 1687 C PHE A 212 3254 3047 3970 -237 -65 -122 C ATOM 1688 O PHE A 212 11.806 37.421 35.887 1.00 29.44 O ANISOU 1688 O PHE A 212 3536 3372 4278 -246 -99 -161 O ATOM 1689 CB PHE A 212 11.386 36.310 32.621 1.00 24.79 C ANISOU 1689 CB PHE A 212 3012 2773 3632 -201 -30 -52 C ATOM 1690 CG PHE A 212 12.855 36.015 32.757 1.00 30.17 C ANISOU 1690 CG PHE A 212 3659 3456 4348 -206 -27 -65 C ATOM 1691 CD1 PHE A 212 13.294 34.845 33.372 1.00 29.98 C ANISOU 1691 CD1 PHE A 212 3631 3463 4297 -199 -60 -81 C ATOM 1692 CD2 PHE A 212 13.800 36.886 32.235 1.00 34.31 C ANISOU 1692 CD2 PHE A 212 4152 3952 4933 -215 12 -59 C ATOM 1693 CE1 PHE A 212 14.645 34.570 33.484 1.00 29.03 C ANISOU 1693 CE1 PHE A 212 3475 3348 4207 -200 -58 -91 C ATOM 1694 CE2 PHE A 212 15.155 36.618 32.347 1.00 34.79 C ANISOU 1694 CE2 PHE A 212 4176 4016 5028 -220 15 -72 C ATOM 1695 CZ PHE A 212 15.576 35.456 32.957 1.00 31.97 C ANISOU 1695 CZ PHE A 212 3814 3694 4641 -212 -21 -88 C ATOM 1696 N AILE A 213 11.331 38.865 34.222 0.72 25.44 N ANISOU 1696 N AILE A 213 3043 2806 3817 -245 -26 -111 N ATOM 1697 N BILE A 213 11.325 38.869 34.224 0.29 25.63 N ANISOU 1697 N BILE A 213 3068 2830 3841 -245 -26 -111 N ATOM 1698 CA AILE A 213 12.109 39.954 34.804 0.72 29.19 C ANISOU 1698 CA AILE A 213 3474 3254 4364 -271 -14 -148 C ATOM 1699 CA BILE A 213 12.121 39.953 34.792 0.29 29.18 C ANISOU 1699 CA BILE A 213 3473 3253 4363 -271 -13 -147 C ATOM 1700 C AILE A 213 11.493 40.417 36.119 0.72 28.93 C ANISOU 1700 C AILE A 213 3435 3227 4330 -286 -46 -194 C ATOM 1701 C BILE A 213 11.511 40.437 36.103 0.29 28.96 C ANISOU 1701 C BILE A 213 3439 3230 4336 -286 -45 -194 C ATOM 1702 O AILE A 213 12.200 40.603 37.116 0.72 29.70 O ANISOU 1702 O AILE A 213 3496 3335 4453 -304 -69 -244 O ATOM 1703 O BILE A 213 12.219 40.628 37.099 0.29 29.70 O ANISOU 1703 O BILE A 213 3495 3334 4455 -304 -68 -244 O ATOM 1704 CB AILE A 213 12.235 41.107 33.792 0.72 33.35 C ANISOU 1704 CB AILE A 213 3994 3730 4947 -274 47 -116 C ATOM 1705 CB BILE A 213 12.268 41.099 33.770 0.29 33.26 C ANISOU 1705 CB BILE A 213 3982 3718 4936 -274 48 -116 C ATOM 1706 CG1AILE A 213 13.292 40.756 32.739 0.72 33.05 C ANISOU 1706 CG1AILE A 213 3946 3687 4926 -265 80 -85 C ATOM 1707 CG1BILE A 213 13.171 40.673 32.603 0.29 32.96 C ANISOU 1707 CG1BILE A 213 3941 3677 4906 -261 81 -78 C ATOM 1708 CG2AILE A 213 12.522 42.430 34.483 0.72 33.25 C ANISOU 1708 CG2AILE A 213 3945 3679 5010 -303 63 -157 C ATOM 1709 CG2BILE A 213 12.799 42.359 34.430 0.29 33.44 C ANISOU 1709 CG2BILE A 213 3962 3703 5040 -305 65 -158 C ATOM 1710 CD1AILE A 213 13.490 41.821 31.714 0.72 36.55 C ANISOU 1710 CD1AILE A 213 4383 4082 5424 -264 145 -48 C ATOM 1711 CD1BILE A 213 14.557 40.204 33.015 0.29 30.55 C ANISOU 1711 CD1BILE A 213 3594 3385 4628 -274 68 -109 C ATOM 1712 N AILE A 214 10.176 40.660 36.133 0.72 28.40 N ANISOU 1712 N AILE A 214 3401 3156 4233 -278 -47 -179 N ATOM 1713 N BILE A 214 10.193 40.658 36.119 0.29 28.46 N ANISOU 1713 N BILE A 214 3408 3163 4241 -278 -47 -179 N ATOM 1714 CA AILE A 214 9.529 41.143 37.360 0.72 29.19 C ANISOU 1714 CA AILE A 214 3498 3260 4332 -290 -74 -222 C ATOM 1715 CA BILE A 214 9.535 41.132 37.341 0.29 29.21 C ANISOU 1715 CA BILE A 214 3501 3264 4335 -290 -73 -221 C ATOM 1716 C AILE A 214 9.684 40.148 38.507 0.72 31.43 C ANISOU 1716 C AILE A 214 3778 3595 4569 -287 -127 -256 C ATOM 1717 C BILE A 214 9.691 40.146 38.495 0.29 31.28 C ANISOU 1717 C BILE A 214 3759 3576 4550 -287 -127 -256 C ATOM 1718 O AILE A 214 10.067 40.569 39.613 0.72 28.42 O ANISOU 1718 O AILE A 214 3367 3224 4208 -304 -149 -309 O ATOM 1719 O BILE A 214 10.068 40.576 39.599 0.29 28.51 O ANISOU 1719 O BILE A 214 3379 3235 4220 -304 -148 -308 O ATOM 1720 CB AILE A 214 8.059 41.504 37.081 0.72 30.72 C ANISOU 1720 CB AILE A 214 3728 3443 4500 -278 -63 -194 C ATOM 1721 CB BILE A 214 8.065 41.484 37.048 0.29 30.66 C ANISOU 1721 CB BILE A 214 3722 3436 4493 -277 -62 -193 C ATOM 1722 CG1AILE A 214 7.954 42.912 36.490 0.72 31.02 C ANISOU 1722 CG1AILE A 214 3758 3427 4602 -284 -11 -180 C ATOM 1723 CG1BILE A 214 7.982 42.775 36.230 0.29 30.95 C ANISOU 1723 CG1BILE A 214 3753 3419 4588 -280 -8 -168 C ATOM 1724 CG2AILE A 214 7.211 41.361 38.362 0.72 30.72 C ANISOU 1724 CG2AILE A 214 3738 3468 4466 -280 -102 -230 C ATOM 1725 CG2BILE A 214 7.258 41.577 38.345 0.29 30.72 C ANISOU 1725 CG2BILE A 214 3734 3461 4477 -283 -97 -232 C ATOM 1726 CD1AILE A 214 6.518 43.378 36.267 0.72 30.90 C ANISOU 1726 CD1AILE A 214 3774 3400 4567 -269 0 -152 C ATOM 1727 CD1BILE A 214 8.638 43.962 36.892 0.29 31.72 C ANISOU 1727 CD1BILE A 214 3811 3479 4763 -309 10 -216 C ATOM 1728 N PRO A 215 9.433 38.838 38.327 1.00 28.91 N ANISOU 1728 N PRO A 215 3485 3309 4189 -266 -148 -230 N ATOM 1729 CA PRO A 215 9.717 37.900 39.441 1.00 27.54 C ANISOU 1729 CA PRO A 215 3304 3181 3976 -260 -193 -257 C ATOM 1730 C PRO A 215 11.157 37.921 39.930 1.00 28.38 C ANISOU 1730 C PRO A 215 3364 3302 4116 -270 -206 -291 C ATOM 1731 O PRO A 215 11.397 37.879 41.145 1.00 28.23 O ANISOU 1731 O PRO A 215 3325 3317 4086 -272 -240 -333 O ATOM 1732 CB PRO A 215 9.369 36.522 38.848 1.00 27.25 C ANISOU 1732 CB PRO A 215 3303 3165 3886 -237 -198 -215 C ATOM 1733 CG PRO A 215 8.461 36.796 37.730 1.00 29.19 C ANISOU 1733 CG PRO A 215 3579 3385 4128 -232 -169 -178 C ATOM 1734 CD PRO A 215 8.831 38.143 37.173 1.00 25.83 C ANISOU 1734 CD PRO A 215 3132 2919 3762 -247 -132 -178 C ATOM 1735 N LEU A 216 12.137 37.995 39.027 1.00 29.55 N ANISOU 1735 N LEU A 216 3493 3432 4303 -273 -178 -275 N ATOM 1736 CA LEU A 216 13.526 38.025 39.493 1.00 26.60 C ANISOU 1736 CA LEU A 216 3068 3074 3964 -283 -190 -310 C ATOM 1737 C LEU A 216 13.840 39.305 40.262 1.00 30.51 C ANISOU 1737 C LEU A 216 3522 3556 4515 -312 -192 -368 C ATOM 1738 O LEU A 216 14.638 39.275 41.208 1.00 32.23 O ANISOU 1738 O LEU A 216 3699 3807 4740 -319 -223 -416 O ATOM 1739 CB LEU A 216 14.492 37.862 38.318 1.00 28.51 C ANISOU 1739 CB LEU A 216 3296 3295 4240 -281 -155 -280 C ATOM 1740 CG LEU A 216 14.564 36.461 37.710 1.00 34.20 C ANISOU 1740 CG LEU A 216 4046 4038 4912 -253 -158 -237 C ATOM 1741 CD1 LEU A 216 15.604 36.435 36.598 1.00 44.32 C ANISOU 1741 CD1 LEU A 216 5308 5299 6232 -253 -121 -213 C ATOM 1742 CD2 LEU A 216 14.904 35.452 38.787 1.00 31.31 C ANISOU 1742 CD2 LEU A 216 3670 3723 4505 -238 -205 -257 C ATOM 1743 N ILE A 217 13.208 40.428 39.901 1.00 34.53 N ANISOU 1743 N ILE A 217 4040 4018 5062 -328 -158 -367 N ATOM 1744 CA ILE A 217 13.429 41.664 40.655 1.00 28.26 C ANISOU 1744 CA ILE A 217 3208 3204 4325 -358 -156 -427 C ATOM 1745 C ILE A 217 12.959 41.495 42.092 1.00 29.15 C ANISOU 1745 C ILE A 217 3320 3362 4392 -355 -206 -475 C ATOM 1746 O ILE A 217 13.636 41.907 43.046 1.00 37.50 O ANISOU 1746 O ILE A 217 4334 4442 5474 -372 -230 -539 O ATOM 1747 CB ILE A 217 12.715 42.847 39.984 1.00 33.96 C ANISOU 1747 CB ILE A 217 3946 3863 5095 -369 -105 -408 C ATOM 1748 CG1 ILE A 217 13.372 43.186 38.650 1.00 32.99 C ANISOU 1748 CG1 ILE A 217 3814 3695 5025 -372 -51 -366 C ATOM 1749 CG2 ILE A 217 12.753 44.063 40.921 1.00 37.98 C ANISOU 1749 CG2 ILE A 217 4422 4352 5658 -399 -105 -477 C ATOM 1750 CD1 ILE A 217 12.618 44.258 37.878 1.00 38.15 C ANISOU 1750 CD1 ILE A 217 4487 4289 5718 -374 4 -333 C ATOM 1751 N VAL A 218 11.782 40.907 42.267 1.00 26.94 N ANISOU 1751 N VAL A 218 3088 3100 4047 -334 -221 -446 N ATOM 1752 CA VAL A 218 11.238 40.716 43.609 1.00 32.51 C ANISOU 1752 CA VAL A 218 3798 3849 4704 -327 -264 -484 C ATOM 1753 C VAL A 218 12.137 39.788 44.424 1.00 34.16 C ANISOU 1753 C VAL A 218 3982 4121 4877 -313 -309 -507 C ATOM 1754 O VAL A 218 12.443 40.051 45.595 1.00 33.91 O ANISOU 1754 O VAL A 218 3920 4127 4838 -318 -342 -565 O ATOM 1755 CB VAL A 218 9.805 40.158 43.529 1.00 32.15 C ANISOU 1755 CB VAL A 218 3809 3808 4599 -306 -266 -442 C ATOM 1756 CG1 VAL A 218 9.257 39.911 44.932 1.00 31.15 C ANISOU 1756 CG1 VAL A 218 3687 3727 4420 -296 -306 -477 C ATOM 1757 CG2 VAL A 218 8.892 41.102 42.749 1.00 31.08 C ANISOU 1757 CG2 VAL A 218 3696 3617 4497 -315 -224 -418 C ATOM 1758 N ILE A 219 12.556 38.677 43.817 1.00 30.47 N ANISOU 1758 N ILE A 219 3525 3668 4384 -292 -310 -461 N ATOM 1759 CA ILE A 219 13.367 37.694 44.535 1.00 31.39 C ANISOU 1759 CA ILE A 219 3620 3844 4464 -271 -349 -472 C ATOM 1760 C ILE A 219 14.665 38.330 45.013 1.00 32.05 C ANISOU 1760 C ILE A 219 3638 3945 4596 -291 -362 -531 C ATOM 1761 O ILE A 219 15.035 38.214 46.189 1.00 32.73 O ANISOU 1761 O ILE A 219 3695 4086 4654 -283 -404 -576 O ATOM 1762 CB ILE A 219 13.615 36.463 43.636 1.00 31.63 C ANISOU 1762 CB ILE A 219 3673 3874 4469 -247 -337 -411 C ATOM 1763 CG1 ILE A 219 12.316 35.675 43.480 1.00 28.63 C ANISOU 1763 CG1 ILE A 219 3353 3494 4033 -227 -335 -366 C ATOM 1764 CG2 ILE A 219 14.754 35.593 44.193 1.00 31.85 C ANISOU 1764 CG2 ILE A 219 3668 3956 4479 -227 -368 -419 C ATOM 1765 CD1 ILE A 219 12.306 34.712 42.287 1.00 29.29 C ANISOU 1765 CD1 ILE A 219 3465 3558 4105 -212 -310 -309 C ATOM 1766 N PHE A 220 15.339 39.081 44.128 1.00 28.65 N ANISOU 1766 N PHE A 220 3180 3466 4239 -317 -326 -534 N ATOM 1767 CA PHE A 220 16.623 39.663 44.489 1.00 34.59 C ANISOU 1767 CA PHE A 220 3865 4231 5047 -339 -335 -591 C ATOM 1768 C PHE A 220 16.484 40.907 45.351 1.00 40.42 C ANISOU 1768 C PHE A 220 4573 4963 5822 -370 -343 -666 C ATOM 1769 O PHE A 220 17.407 41.211 46.119 1.00 35.75 O ANISOU 1769 O PHE A 220 3924 4408 5253 -383 -371 -731 O ATOM 1770 CB PHE A 220 17.448 39.944 43.234 1.00 36.72 C ANISOU 1770 CB PHE A 220 4114 4451 5385 -354 -288 -565 C ATOM 1771 CG PHE A 220 18.097 38.696 42.665 1.00 41.16 C ANISOU 1771 CG PHE A 220 4682 5038 5919 -326 -291 -516 C ATOM 1772 CD1 PHE A 220 19.285 38.213 43.199 1.00 45.63 C ANISOU 1772 CD1 PHE A 220 5197 5655 6487 -318 -323 -544 C ATOM 1773 CD2 PHE A 220 17.495 37.989 41.641 1.00 41.05 C ANISOU 1773 CD2 PHE A 220 4722 5000 5874 -305 -264 -446 C ATOM 1774 CE1 PHE A 220 19.872 37.051 42.698 1.00 51.94 C ANISOU 1774 CE1 PHE A 220 6000 6473 7260 -288 -323 -498 C ATOM 1775 CE2 PHE A 220 18.074 36.834 41.129 1.00 50.60 C ANISOU 1775 CE2 PHE A 220 5936 6229 7059 -279 -264 -406 C ATOM 1776 CZ PHE A 220 19.262 36.361 41.657 1.00 50.43 C ANISOU 1776 CZ PHE A 220 5866 6252 7043 -270 -292 -429 C ATOM 1777 N PHE A 221 15.353 41.609 45.281 1.00 32.75 N ANISOU 1777 N PHE A 221 3638 3951 4856 -380 -320 -663 N ATOM 1778 CA PHE A 221 15.091 42.654 46.265 1.00 33.36 C ANISOU 1778 CA PHE A 221 3692 4028 4954 -403 -332 -737 C ATOM 1779 C PHE A 221 14.968 42.060 47.656 1.00 36.67 C ANISOU 1779 C PHE A 221 4106 4528 5297 -381 -393 -775 C ATOM 1780 O PHE A 221 15.543 42.584 48.622 1.00 36.00 O ANISOU 1780 O PHE A 221 3974 4480 5226 -397 -422 -853 O ATOM 1781 CB PHE A 221 13.817 43.426 45.918 1.00 37.14 C ANISOU 1781 CB PHE A 221 4214 4449 5448 -412 -295 -717 C ATOM 1782 CG PHE A 221 13.376 44.364 47.007 1.00 41.58 C ANISOU 1782 CG PHE A 221 4762 5015 6020 -430 -308 -791 C ATOM 1783 CD1 PHE A 221 13.964 45.604 47.143 1.00 50.18 C ANISOU 1783 CD1 PHE A 221 5804 6067 7197 -470 -287 -857 C ATOM 1784 CD2 PHE A 221 12.388 43.992 47.900 1.00 47.26 C ANISOU 1784 CD2 PHE A 221 5516 5776 6666 -408 -340 -795 C ATOM 1785 CE1 PHE A 221 13.570 46.465 48.154 1.00 53.48 C ANISOU 1785 CE1 PHE A 221 6208 6487 7625 -488 -298 -931 C ATOM 1786 CE2 PHE A 221 11.987 44.846 48.907 1.00 54.62 C ANISOU 1786 CE2 PHE A 221 6436 6714 7604 -423 -351 -865 C ATOM 1787 CZ PHE A 221 12.580 46.083 49.035 1.00 51.61 C ANISOU 1787 CZ PHE A 221 6008 6295 7308 -463 -331 -935 C ATOM 1788 N CYS A 222 14.210 40.958 47.774 1.00 35.87 N ANISOU 1788 N CYS A 222 4056 4459 5115 -344 -410 -720 N ATOM 1789 CA CYS A 222 14.033 40.300 49.064 1.00 35.40 C ANISOU 1789 CA CYS A 222 3997 4476 4975 -315 -462 -743 C ATOM 1790 C CYS A 222 15.357 39.761 49.594 1.00 43.83 C ANISOU 1790 C CYS A 222 5012 5611 6032 -302 -501 -772 C ATOM 1791 O CYS A 222 15.651 39.874 50.793 1.00 36.57 O ANISOU 1791 O CYS A 222 4060 4754 5080 -295 -544 -831 O ATOM 1792 CB CYS A 222 12.997 39.180 48.946 1.00 31.65 C ANISOU 1792 CB CYS A 222 3585 4012 4427 -279 -462 -671 C ATOM 1793 SG CYS A 222 11.313 39.777 48.757 1.00 39.08 S ANISOU 1793 SG CYS A 222 4582 4903 5364 -287 -432 -652 S ATOM 1794 N TYR A 223 16.165 39.167 48.712 1.00 40.09 N ANISOU 1794 N TYR A 223 4526 5124 5580 -297 -487 -730 N ATOM 1795 CA TYR A 223 17.471 38.650 49.106 1.00 41.31 C ANISOU 1795 CA TYR A 223 4628 5339 5730 -283 -520 -752 C ATOM 1796 C TYR A 223 18.399 39.773 49.546 1.00 45.50 C ANISOU 1796 C TYR A 223 5086 5878 6326 -321 -532 -841 C ATOM 1797 O TYR A 223 19.132 39.630 50.533 1.00 52.71 O ANISOU 1797 O TYR A 223 5950 6865 7213 -309 -580 -894 O ATOM 1798 CB TYR A 223 18.082 37.847 47.949 1.00 48.84 C ANISOU 1798 CB TYR A 223 5587 6268 6702 -271 -494 -687 C ATOM 1799 CG TYR A 223 19.606 37.815 47.894 1.00 60.98 C ANISOU 1799 CG TYR A 223 7055 7833 8281 -276 -507 -715 C ATOM 1800 CD1 TYR A 223 20.336 36.867 48.609 1.00 65.66 C ANISOU 1800 CD1 TYR A 223 7620 8504 8823 -239 -551 -715 C ATOM 1801 CD2 TYR A 223 20.313 38.719 47.100 1.00 61.91 C ANISOU 1801 CD2 TYR A 223 7135 7898 8492 -317 -471 -738 C ATOM 1802 CE1 TYR A 223 21.728 36.831 48.552 1.00 67.37 C ANISOU 1802 CE1 TYR A 223 7770 8749 9079 -242 -563 -741 C ATOM 1803 CE2 TYR A 223 21.703 38.692 47.037 1.00 72.36 C ANISOU 1803 CE2 TYR A 223 8391 9245 9858 -323 -480 -765 C ATOM 1804 CZ TYR A 223 22.404 37.748 47.767 1.00 77.81 C ANISOU 1804 CZ TYR A 223 9052 10017 10496 -286 -528 -768 C ATOM 1805 OH TYR A 223 23.782 37.726 47.705 1.00 77.96 O ANISOU 1805 OH TYR A 223 9000 10063 10558 -291 -538 -795 O ATOM 1806 N GLY A 224 18.383 40.897 48.828 1.00 44.21 N ANISOU 1806 N GLY A 224 4912 5638 6247 -365 -487 -861 N ATOM 1807 CA GLY A 224 19.218 42.023 49.212 1.00 53.95 C ANISOU 1807 CA GLY A 224 6076 6868 7554 -406 -491 -950 C ATOM 1808 C GLY A 224 18.913 42.517 50.612 1.00 48.61 C ANISOU 1808 C GLY A 224 5380 6245 6843 -409 -534 -1032 C ATOM 1809 O GLY A 224 19.819 42.906 51.353 1.00 53.31 O ANISOU 1809 O GLY A 224 5909 6889 7459 -424 -568 -1113 O ATOM 1810 N GLN A 225 17.631 42.501 50.995 1.00 43.97 N ANISOU 1810 N GLN A 225 4850 5654 6202 -395 -534 -1014 N ATOM 1811 CA GLN A 225 17.253 42.831 52.369 1.00 47.90 C ANISOU 1811 CA GLN A 225 5337 6210 6651 -389 -576 -1085 C ATOM 1812 C GLN A 225 17.825 41.823 53.363 1.00 58.28 C ANISOU 1812 C GLN A 225 6629 7635 7879 -346 -639 -1095 C ATOM 1813 O GLN A 225 18.430 42.208 54.368 1.00 56.80 O ANISOU 1813 O GLN A 225 6386 7512 7682 -351 -682 -1181 O ATOM 1814 CB GLN A 225 15.731 42.903 52.492 1.00 53.13 C ANISOU 1814 CB GLN A 225 6071 6846 7272 -378 -559 -1052 C ATOM 1815 CG GLN A 225 15.104 43.951 51.610 1.00 46.13 C ANISOU 1815 CG GLN A 225 5205 5857 6464 -415 -499 -1043 C ATOM 1816 CD GLN A 225 15.544 45.355 51.980 1.00 55.86 C ANISOU 1816 CD GLN A 225 6384 7061 7779 -463 -488 -1142 C ATOM 1817 OE1 GLN A 225 16.462 45.911 51.376 1.00 62.17 O ANISOU 1817 OE1 GLN A 225 7137 7820 8664 -496 -463 -1164 O ATOM 1818 NE2 GLN A 225 14.885 45.939 52.975 1.00 54.39 N ANISOU 1818 NE2 GLN A 225 6202 6894 7569 -467 -504 -1202 N ATOM 1819 N LEU A 226 17.642 40.522 53.100 1.00 50.25 N ANISOU 1819 N LEU A 226 5652 6641 6798 -300 -645 -1009 N ATOM 1820 CA LEU A 226 18.171 39.497 53.998 1.00 56.19 C ANISOU 1820 CA LEU A 226 6386 7495 7469 -251 -698 -1005 C ATOM 1821 C LEU A 226 19.663 39.686 54.232 1.00 59.91 C ANISOU 1821 C LEU A 226 6773 8015 7976 -262 -729 -1066 C ATOM 1822 O LEU A 226 20.132 39.683 55.374 1.00 65.80 O ANISOU 1822 O LEU A 226 7474 8851 8675 -244 -782 -1127 O ATOM 1823 CB LEU A 226 17.904 38.097 53.439 1.00 53.86 C ANISOU 1823 CB LEU A 226 6142 7199 7124 -207 -687 -900 C ATOM 1824 CG LEU A 226 16.508 37.495 53.639 1.00 62.60 C ANISOU 1824 CG LEU A 226 7324 8298 8162 -177 -676 -841 C ATOM 1825 CD1 LEU A 226 16.568 35.967 53.604 1.00 57.88 C ANISOU 1825 CD1 LEU A 226 6756 7736 7502 -124 -683 -760 C ATOM 1826 CD2 LEU A 226 15.887 37.992 54.924 1.00 57.52 C ANISOU 1826 CD2 LEU A 226 6682 7704 7468 -171 -706 -899 C ATOM 1827 N VAL A 227 20.420 39.879 53.157 1.00 56.27 N ANISOU 1827 N VAL A 227 6286 7498 7596 -290 -697 -1052 N ATOM 1828 CA VAL A 227 21.868 39.990 53.277 1.00 59.48 C ANISOU 1828 CA VAL A 227 6609 7947 8043 -301 -722 -1103 C ATOM 1829 C VAL A 227 22.265 41.351 53.828 1.00 68.14 C ANISOU 1829 C VAL A 227 7643 9045 9203 -352 -733 -1219 C ATOM 1830 O VAL A 227 22.964 41.446 54.844 1.00 68.41 O ANISOU 1830 O VAL A 227 7614 9166 9211 -344 -787 -1294 O ATOM 1831 CB VAL A 227 22.538 39.719 51.919 1.00 63.26 C ANISOU 1831 CB VAL A 227 7082 8364 8590 -313 -678 -1046 C ATOM 1832 CG1 VAL A 227 23.967 40.241 51.923 1.00 64.14 C ANISOU 1832 CG1 VAL A 227 7100 8495 8774 -342 -690 -1114 C ATOM 1833 CG2 VAL A 227 22.501 38.233 51.617 1.00 66.53 C ANISOU 1833 CG2 VAL A 227 7537 8805 8937 -257 -682 -950 C ATOM 1834 N PHE A 228 21.826 42.424 53.172 1.00 61.59 N ANISOU 1834 N PHE A 228 6826 8119 8457 -402 -681 -1236 N ATOM 1835 CA PHE A 228 22.320 43.768 53.475 1.00 69.88 C ANISOU 1835 CA PHE A 228 7811 9149 9592 -458 -677 -1345 C ATOM 1836 C PHE A 228 21.454 44.454 54.535 1.00 72.90 C ANISOU 1836 C PHE A 228 8208 9552 9939 -466 -697 -1414 C ATOM 1837 O PHE A 228 20.887 45.525 54.320 1.00 82.26 O ANISOU 1837 O PHE A 228 9405 10661 11189 -507 -656 -1447 O ATOM 1838 CB PHE A 228 22.403 44.598 52.198 1.00 61.84 C ANISOU 1838 CB PHE A 228 6794 8012 8691 -507 -603 -1325 C ATOM 1839 N THR A 229 21.352 43.803 55.693 1.00 85.51 N ANISOU 1839 N THR A 229 9804 11254 11431 -421 -759 -1433 N ATOM 1840 CA THR A 229 20.830 44.436 56.908 1.00 91.72 C ANISOU 1840 CA THR A 229 10583 12088 12177 -425 -791 -1520 C ATOM 1841 C THR A 229 21.695 44.044 58.096 1.00100.65 C ANISOU 1841 C THR A 229 11651 13352 13240 -396 -866 -1587 C ATOM 1842 O THR A 229 21.553 42.944 58.632 1.00101.58 O ANISOU 1842 O THR A 229 11794 13550 13252 -334 -904 -1535 O ATOM 1843 CB THR A 229 19.364 44.045 57.235 1.00 93.73 C ANISOU 1843 CB THR A 229 10924 12340 12347 -390 -784 -1462 C ATOM 1844 OG1 THR A 229 19.248 42.620 57.352 1.00 93.13 O ANISOU 1844 OG1 THR A 229 10885 12325 12174 -326 -809 -1373 O ATOM 1845 CG2 THR A 229 18.390 44.584 56.188 1.00 81.16 C ANISOU 1845 CG2 THR A 229 9392 10626 10819 -419 -713 -1409 C ATOM 1846 N GLN A 244 15.247 29.933 65.123 1.00 71.51 N ANISOU 1846 N GLN A 244 8529 10325 8318 456 -961 -623 N ATOM 1847 CA GLN A 244 16.528 30.481 64.681 1.00 74.92 C ANISOU 1847 CA GLN A 244 8890 10770 8806 422 -996 -688 C ATOM 1848 C GLN A 244 17.295 29.461 63.846 1.00 68.05 C ANISOU 1848 C GLN A 244 8014 9871 7970 443 -979 -612 C ATOM 1849 O GLN A 244 17.561 29.689 62.667 1.00 61.07 O ANISOU 1849 O GLN A 244 7126 8901 7177 390 -955 -614 O ATOM 1850 CB GLN A 244 17.374 30.920 65.878 1.00 77.55 C ANISOU 1850 CB GLN A 244 9155 11238 9072 455 -1064 -769 C ATOM 1851 N LYS A 245 17.662 28.342 64.477 1.00 69.79 N ANISOU 1851 N LYS A 245 8234 10167 8118 524 -989 -544 N ATOM 1852 CA LYS A 245 18.312 27.255 63.751 1.00 67.98 C ANISOU 1852 CA LYS A 245 8004 9908 7915 552 -966 -464 C ATOM 1853 C LYS A 245 17.354 26.619 62.752 1.00 63.13 C ANISOU 1853 C LYS A 245 7464 9173 7350 531 -898 -383 C ATOM 1854 O LYS A 245 17.758 26.234 61.646 1.00 54.43 O ANISOU 1854 O LYS A 245 6364 8001 6316 509 -870 -350 O ATOM 1855 CB LYS A 245 18.837 26.215 64.741 1.00 72.64 C ANISOU 1855 CB LYS A 245 8579 10608 8412 650 -989 -406 C ATOM 1856 CG LYS A 245 19.242 24.893 64.123 1.00 71.59 C ANISOU 1856 CG LYS A 245 8463 10439 8297 692 -952 -303 C ATOM 1857 CD LYS A 245 19.712 23.920 65.191 1.00 77.29 C ANISOU 1857 CD LYS A 245 9171 11274 8924 795 -972 -243 C ATOM 1858 N ALA A 246 16.080 26.499 63.132 1.00 62.60 N ANISOU 1858 N ALA A 246 7457 9083 7247 538 -869 -354 N ATOM 1859 CA ALA A 246 15.075 25.986 62.211 1.00 58.26 C ANISOU 1859 CA ALA A 246 6973 8419 6743 512 -806 -289 C ATOM 1860 C ALA A 246 14.857 26.939 61.043 1.00 46.31 C ANISOU 1860 C ALA A 246 5461 6810 5323 425 -791 -339 C ATOM 1861 O ALA A 246 14.706 26.501 59.897 1.00 48.91 O ANISOU 1861 O ALA A 246 5818 7053 5714 399 -751 -296 O ATOM 1862 CB ALA A 246 13.763 25.738 62.956 1.00 64.29 C ANISOU 1862 CB ALA A 246 7793 9186 7450 538 -781 -254 C ATOM 1863 N GLU A 247 14.819 28.244 61.311 1.00 46.02 N ANISOU 1863 N GLU A 247 5397 6790 5299 381 -820 -431 N ATOM 1864 CA GLU A 247 14.606 29.186 60.220 1.00 48.99 C ANISOU 1864 CA GLU A 247 5775 7075 5765 302 -801 -474 C ATOM 1865 C GLU A 247 15.800 29.216 59.281 1.00 41.59 C ANISOU 1865 C GLU A 247 4794 6114 4895 278 -806 -484 C ATOM 1866 O GLU A 247 15.625 29.362 58.068 1.00 38.77 O ANISOU 1866 O GLU A 247 4455 5667 4611 233 -770 -470 O ATOM 1867 CB GLU A 247 14.319 30.586 60.763 1.00 53.17 C ANISOU 1867 CB GLU A 247 6282 7623 6297 262 -827 -570 C ATOM 1868 CG GLU A 247 13.036 30.701 61.587 1.00 53.20 C ANISOU 1868 CG GLU A 247 6332 7640 6243 277 -816 -565 C ATOM 1869 CD GLU A 247 11.751 30.585 60.766 1.00 58.10 C ANISOU 1869 CD GLU A 247 7016 8158 6902 247 -762 -516 C ATOM 1870 OE1 GLU A 247 11.791 30.212 59.566 1.00 51.91 O ANISOU 1870 OE1 GLU A 247 6248 7296 6178 222 -730 -474 O ATOM 1871 OE2 GLU A 247 10.680 30.870 61.341 1.00 65.37 O ANISOU 1871 OE2 GLU A 247 7970 9079 7790 249 -751 -522 O ATOM 1872 N LYS A 248 17.012 29.065 59.825 1.00 38.88 N ANISOU 1872 N LYS A 248 4391 5855 4527 312 -848 -507 N ATOM 1873 CA LYS A 248 18.212 29.044 58.996 1.00 43.84 C ANISOU 1873 CA LYS A 248 4973 6468 5218 294 -853 -515 C ATOM 1874 C LYS A 248 18.164 27.912 57.973 1.00 40.31 C ANISOU 1874 C LYS A 248 4565 5952 4800 308 -805 -423 C ATOM 1875 O LYS A 248 18.514 28.111 56.802 1.00 37.35 O ANISOU 1875 O LYS A 248 4184 5506 4500 265 -781 -424 O ATOM 1876 CB LYS A 248 19.445 28.923 59.892 1.00 47.62 C ANISOU 1876 CB LYS A 248 5380 7061 5652 339 -908 -548 C ATOM 1877 CG LYS A 248 20.767 29.062 59.172 1.00 47.04 C ANISOU 1877 CG LYS A 248 5245 6983 5645 318 -919 -572 C ATOM 1878 CD LYS A 248 21.932 29.064 60.165 1.00 50.76 C ANISOU 1878 CD LYS A 248 5639 7578 6069 361 -981 -616 C ATOM 1879 CE LYS A 248 22.145 27.690 60.795 1.00 56.56 C ANISOU 1879 CE LYS A 248 6385 8382 6722 452 -988 -532 C ATOM 1880 NZ LYS A 248 23.375 27.636 61.642 1.00 63.94 N ANISOU 1880 NZ LYS A 248 7238 9441 7613 498 -1048 -569 N ATOM 1881 N GLU A 249 17.724 26.717 58.390 1.00 36.47 N ANISOU 1881 N GLU A 249 4120 5483 4256 368 -788 -344 N ATOM 1882 CA GLU A 249 17.609 25.598 57.454 1.00 39.50 C ANISOU 1882 CA GLU A 249 4543 5797 4668 380 -740 -261 C ATOM 1883 C GLU A 249 16.707 25.943 56.269 1.00 36.93 C ANISOU 1883 C GLU A 249 4265 5362 4406 318 -695 -257 C ATOM 1884 O GLU A 249 17.030 25.614 55.117 1.00 32.78 O ANISOU 1884 O GLU A 249 3744 4772 3937 298 -665 -231 O ATOM 1885 CB GLU A 249 17.086 24.359 58.183 1.00 40.25 C ANISOU 1885 CB GLU A 249 4679 5920 4694 451 -721 -181 C ATOM 1886 CG GLU A 249 17.127 23.066 57.355 1.00 39.43 C ANISOU 1886 CG GLU A 249 4610 5755 4618 473 -672 -96 C ATOM 1887 CD GLU A 249 16.356 21.918 58.010 1.00 45.00 C ANISOU 1887 CD GLU A 249 5364 6466 5267 533 -641 -16 C ATOM 1888 OE1 GLU A 249 15.200 22.144 58.429 1.00 51.31 O ANISOU 1888 OE1 GLU A 249 6203 7253 6041 523 -629 -17 O ATOM 1889 OE2 GLU A 249 16.902 20.798 58.110 1.00 40.95 O ANISOU 1889 OE2 GLU A 249 4851 5970 4740 590 -625 48 O ATOM 1890 N VAL A 250 15.568 26.592 56.536 1.00 32.56 N ANISOU 1890 N VAL A 250 3744 4787 3842 290 -689 -281 N ATOM 1891 CA VAL A 250 14.644 26.982 55.474 1.00 31.68 C ANISOU 1891 CA VAL A 250 3674 4579 3785 235 -649 -278 C ATOM 1892 C VAL A 250 15.274 28.028 54.562 1.00 32.37 C ANISOU 1892 C VAL A 250 3725 4628 3946 177 -653 -333 C ATOM 1893 O VAL A 250 15.167 27.947 53.334 1.00 29.84 O ANISOU 1893 O VAL A 250 3424 4234 3680 146 -618 -311 O ATOM 1894 CB VAL A 250 13.318 27.494 56.071 1.00 35.70 C ANISOU 1894 CB VAL A 250 4219 5082 4262 223 -645 -294 C ATOM 1895 CG1 VAL A 250 12.389 27.964 54.976 1.00 33.57 C ANISOU 1895 CG1 VAL A 250 3987 4721 4049 168 -608 -293 C ATOM 1896 CG2 VAL A 250 12.652 26.412 56.911 1.00 39.58 C ANISOU 1896 CG2 VAL A 250 4749 5604 4686 280 -632 -232 C ATOM 1897 N THR A 251 15.910 29.046 55.143 1.00 30.01 N ANISOU 1897 N THR A 251 3373 4378 3651 161 -693 -408 N ATOM 1898 CA THR A 251 16.527 30.079 54.314 1.00 33.10 C ANISOU 1898 CA THR A 251 3727 4730 4119 105 -691 -461 C ATOM 1899 C THR A 251 17.593 29.478 53.394 1.00 30.81 C ANISOU 1899 C THR A 251 3414 4420 3871 110 -677 -429 C ATOM 1900 O THR A 251 17.677 29.832 52.212 1.00 31.62 O ANISOU 1900 O THR A 251 3522 4453 4040 69 -646 -427 O ATOM 1901 CB THR A 251 17.130 31.168 55.210 1.00 40.37 C ANISOU 1901 CB THR A 251 4588 5714 5038 91 -736 -551 C ATOM 1902 OG1 THR A 251 16.099 31.726 56.039 1.00 33.86 O ANISOU 1902 OG1 THR A 251 3788 4904 4174 86 -745 -581 O ATOM 1903 CG2 THR A 251 17.773 32.281 54.371 1.00 37.38 C ANISOU 1903 CG2 THR A 251 4168 5287 4749 30 -728 -606 C ATOM 1904 N ARG A 252 18.400 28.552 53.918 1.00 25.95 N ANISOU 1904 N ARG A 252 2774 3868 3217 164 -698 -401 N ATOM 1905 CA ARG A 252 19.438 27.922 53.106 1.00 29.46 C ANISOU 1905 CA ARG A 252 3195 4298 3700 174 -684 -369 C ATOM 1906 C ARG A 252 18.844 27.140 51.948 1.00 30.76 C ANISOU 1906 C ARG A 252 3419 4380 3890 168 -631 -301 C ATOM 1907 O ARG A 252 19.374 27.173 50.833 1.00 30.37 O ANISOU 1907 O ARG A 252 3360 4281 3897 144 -606 -294 O ATOM 1908 CB ARG A 252 20.286 26.998 53.966 1.00 28.73 C ANISOU 1908 CB ARG A 252 3070 4291 3554 241 -715 -343 C ATOM 1909 CG ARG A 252 21.140 27.745 54.941 1.00 27.35 C ANISOU 1909 CG ARG A 252 2824 4206 3361 245 -771 -416 C ATOM 1910 CD ARG A 252 21.740 26.808 55.965 1.00 30.32 C ANISOU 1910 CD ARG A 252 3175 4679 3665 322 -804 -385 C ATOM 1911 NE ARG A 252 22.875 27.447 56.616 1.00 35.78 N ANISOU 1911 NE ARG A 252 3784 5457 4355 325 -858 -456 N ATOM 1912 CZ ARG A 252 23.705 26.826 57.445 1.00 44.96 C ANISOU 1912 CZ ARG A 252 4902 6716 5463 388 -896 -444 C ATOM 1913 NH1 ARG A 252 23.524 25.559 57.786 1.00 44.03 N ANISOU 1913 NH1 ARG A 252 4820 6622 5288 458 -882 -359 N ATOM 1914 NH2 ARG A 252 24.743 27.492 57.940 1.00 50.19 N ANISOU 1914 NH2 ARG A 252 5483 7456 6132 383 -947 -519 N ATOM 1915 N MET A 253 17.757 26.413 52.198 1.00 25.02 N ANISOU 1915 N MET A 253 2750 3637 3119 192 -611 -253 N ATOM 1916 CA MET A 253 17.119 25.670 51.122 1.00 26.37 C ANISOU 1916 CA MET A 253 2976 3731 3314 184 -562 -197 C ATOM 1917 C MET A 253 16.567 26.595 50.038 1.00 30.47 C ANISOU 1917 C MET A 253 3512 4177 3887 122 -537 -223 C ATOM 1918 O MET A 253 16.675 26.298 48.843 1.00 25.42 O ANISOU 1918 O MET A 253 2889 3482 3289 106 -503 -198 O ATOM 1919 CB MET A 253 16.017 24.772 51.685 1.00 24.29 C ANISOU 1919 CB MET A 253 2766 3465 2997 218 -545 -147 C ATOM 1920 CG MET A 253 15.252 24.049 50.577 1.00 27.89 C ANISOU 1920 CG MET A 253 3276 3840 3480 203 -494 -100 C ATOM 1921 SD MET A 253 14.175 22.760 51.214 1.00 30.80 S ANISOU 1921 SD MET A 253 3700 4204 3798 248 -467 -35 S ATOM 1922 CE MET A 253 13.017 22.607 49.838 1.00 32.00 C ANISOU 1922 CE MET A 253 3906 4259 3993 200 -419 -20 C ATOM 1923 N VAL A 254 15.951 27.714 50.422 1.00 28.26 N ANISOU 1923 N VAL A 254 3231 3898 3608 90 -552 -271 N ATOM 1924 CA VAL A 254 15.397 28.599 49.402 1.00 30.28 C ANISOU 1924 CA VAL A 254 3504 4086 3916 36 -525 -289 C ATOM 1925 C VAL A 254 16.511 29.159 48.514 1.00 28.14 C ANISOU 1925 C VAL A 254 3190 3793 3708 9 -518 -312 C ATOM 1926 O VAL A 254 16.329 29.338 47.300 1.00 27.62 O ANISOU 1926 O VAL A 254 3144 3666 3686 -19 -483 -297 O ATOM 1927 CB VAL A 254 14.556 29.706 50.065 1.00 32.47 C ANISOU 1927 CB VAL A 254 3785 4368 4184 11 -540 -337 C ATOM 1928 CG1 VAL A 254 14.105 30.757 49.037 1.00 30.11 C ANISOU 1928 CG1 VAL A 254 3495 4001 3942 -41 -513 -356 C ATOM 1929 CG2 VAL A 254 13.358 29.070 50.779 1.00 30.39 C ANISOU 1929 CG2 VAL A 254 3569 4116 3860 38 -537 -305 C ATOM 1930 N ILE A 255 17.675 29.445 49.101 1.00 26.11 N ANISOU 1930 N ILE A 255 2873 3590 3458 17 -551 -350 N ATOM 1931 CA ILE A 255 18.814 29.917 48.315 1.00 30.54 C ANISOU 1931 CA ILE A 255 3387 4133 4083 -7 -542 -371 C ATOM 1932 C ILE A 255 19.156 28.906 47.226 1.00 27.96 C ANISOU 1932 C ILE A 255 3081 3769 3773 8 -507 -312 C ATOM 1933 O ILE A 255 19.381 29.263 46.065 1.00 24.94 O ANISOU 1933 O ILE A 255 2699 3334 3443 -21 -474 -307 O ATOM 1934 CB ILE A 255 20.036 30.174 49.221 1.00 29.36 C ANISOU 1934 CB ILE A 255 3165 4058 3932 6 -586 -419 C ATOM 1935 CG1 ILE A 255 19.833 31.403 50.090 1.00 30.79 C ANISOU 1935 CG1 ILE A 255 3317 4266 4114 -22 -617 -494 C ATOM 1936 CG2 ILE A 255 21.292 30.343 48.364 1.00 32.04 C ANISOU 1936 CG2 ILE A 255 3456 4380 4337 -10 -573 -426 C ATOM 1937 CD1 ILE A 255 20.868 31.526 51.230 1.00 38.11 C ANISOU 1937 CD1 ILE A 255 4176 5286 5020 0 -670 -546 C ATOM 1938 N ILE A 256 19.225 27.627 47.593 1.00 25.14 N ANISOU 1938 N ILE A 256 2741 3441 3370 57 -510 -265 N ATOM 1939 CA ILE A 256 19.597 26.606 46.617 1.00 24.98 C ANISOU 1939 CA ILE A 256 2738 3386 3365 75 -476 -213 C ATOM 1940 C ILE A 256 18.494 26.422 45.582 1.00 26.30 C ANISOU 1940 C ILE A 256 2969 3483 3542 53 -434 -182 C ATOM 1941 O ILE A 256 18.776 26.179 44.402 1.00 25.07 O ANISOU 1941 O ILE A 256 2822 3283 3420 43 -400 -162 O ATOM 1942 CB ILE A 256 19.953 25.286 47.330 1.00 28.46 C ANISOU 1942 CB ILE A 256 3181 3874 3760 136 -486 -170 C ATOM 1943 CG1 ILE A 256 21.164 25.500 48.226 1.00 29.63 C ANISOU 1943 CG1 ILE A 256 3259 4098 3901 159 -530 -201 C ATOM 1944 CG2 ILE A 256 20.239 24.182 46.323 1.00 24.02 C ANISOU 1944 CG2 ILE A 256 2642 3269 3216 154 -445 -117 C ATOM 1945 CD1 ILE A 256 22.428 25.916 47.456 1.00 31.41 C ANISOU 1945 CD1 ILE A 256 3430 4316 4188 139 -524 -223 C ATOM 1946 N MET A 257 17.225 26.549 45.989 1.00 25.80 N ANISOU 1946 N MET A 257 2946 3410 3446 46 -435 -181 N ATOM 1947 CA MET A 257 16.142 26.461 45.011 1.00 24.81 C ANISOU 1947 CA MET A 257 2873 3222 3329 24 -399 -159 C ATOM 1948 C MET A 257 16.257 27.558 43.958 1.00 26.13 C ANISOU 1948 C MET A 257 3031 3348 3549 -21 -381 -183 C ATOM 1949 O MET A 257 15.972 27.326 42.782 1.00 23.55 O ANISOU 1949 O MET A 257 2732 2975 3240 -32 -346 -159 O ATOM 1950 CB MET A 257 14.772 26.540 45.689 1.00 25.41 C ANISOU 1950 CB MET A 257 2989 3300 3367 22 -406 -159 C ATOM 1951 CG MET A 257 14.415 25.346 46.563 1.00 27.34 C ANISOU 1951 CG MET A 257 3255 3572 3560 66 -410 -122 C ATOM 1952 SD MET A 257 12.876 25.621 47.482 1.00 30.65 S ANISOU 1952 SD MET A 257 3711 3998 3937 63 -419 -128 S ATOM 1953 CE MET A 257 11.682 25.478 46.168 1.00 26.12 C ANISOU 1953 CE MET A 257 3187 3350 3385 31 -377 -108 C ATOM 1954 N VAL A 258 16.648 28.766 44.358 1.00 22.91 N ANISOU 1954 N VAL A 258 2582 2955 3167 -45 -400 -231 N ATOM 1955 CA VAL A 258 16.769 29.837 43.366 1.00 23.40 C ANISOU 1955 CA VAL A 258 2635 2973 3285 -85 -376 -248 C ATOM 1956 C VAL A 258 17.955 29.589 42.438 1.00 23.81 C ANISOU 1956 C VAL A 258 2660 3011 3377 -84 -354 -235 C ATOM 1957 O VAL A 258 17.855 29.780 41.218 1.00 24.63 O ANISOU 1957 O VAL A 258 2781 3068 3510 -100 -317 -216 O ATOM 1958 CB VAL A 258 16.859 31.203 44.064 1.00 24.93 C ANISOU 1958 CB VAL A 258 2791 3179 3502 -114 -397 -306 C ATOM 1959 CG1 VAL A 258 17.217 32.289 43.050 1.00 29.59 C ANISOU 1959 CG1 VAL A 258 3362 3721 4160 -151 -366 -321 C ATOM 1960 CG2 VAL A 258 15.519 31.511 44.754 1.00 29.50 C ANISOU 1960 CG2 VAL A 258 3405 3760 4044 -118 -409 -316 C ATOM 1961 N ILE A 259 19.091 29.149 42.991 1.00 23.16 N ANISOU 1961 N ILE A 259 2533 2972 3295 -60 -375 -242 N ATOM 1962 CA ILE A 259 20.238 28.820 42.147 1.00 25.21 C ANISOU 1962 CA ILE A 259 2766 3222 3593 -55 -353 -226 C ATOM 1963 C ILE A 259 19.884 27.705 41.164 1.00 24.90 C ANISOU 1963 C ILE A 259 2775 3148 3537 -36 -318 -173 C ATOM 1964 O ILE A 259 20.225 27.775 39.975 1.00 23.78 O ANISOU 1964 O ILE A 259 2638 2970 3429 -48 -281 -158 O ATOM 1965 CB ILE A 259 21.452 28.434 43.011 1.00 24.70 C ANISOU 1965 CB ILE A 259 2644 3217 3525 -27 -386 -241 C ATOM 1966 CG1 ILE A 259 21.971 29.660 43.763 1.00 26.85 C ANISOU 1966 CG1 ILE A 259 2857 3520 3826 -54 -417 -305 C ATOM 1967 CG2 ILE A 259 22.559 27.876 42.121 1.00 27.63 C ANISOU 1967 CG2 ILE A 259 2992 3575 3929 -15 -359 -216 C ATOM 1968 CD1 ILE A 259 23.062 29.354 44.739 1.00 26.40 C ANISOU 1968 CD1 ILE A 259 2739 3533 3757 -26 -458 -328 C ATOM 1969 N ALA A 260 19.202 26.656 41.640 1.00 22.70 N ANISOU 1969 N ALA A 260 2535 2881 3208 -7 -325 -145 N ATOM 1970 CA ALA A 260 18.868 25.536 40.759 1.00 22.43 C ANISOU 1970 CA ALA A 260 2546 2814 3162 10 -290 -102 C ATOM 1971 C ALA A 260 17.938 25.979 39.640 1.00 24.37 C ANISOU 1971 C ALA A 260 2833 3010 3418 -20 -260 -98 C ATOM 1972 O ALA A 260 18.030 25.488 38.507 1.00 21.90 O ANISOU 1972 O ALA A 260 2540 2665 3114 -19 -226 -75 O ATOM 1973 CB ALA A 260 18.235 24.398 41.564 1.00 25.03 C ANISOU 1973 CB ALA A 260 2907 3160 3442 44 -300 -76 C ATOM 1974 N PHE A 261 17.008 26.878 39.953 1.00 21.83 N ANISOU 1974 N PHE A 261 2523 2682 3088 -45 -272 -118 N ATOM 1975 CA PHE A 261 16.086 27.379 38.944 1.00 21.96 C ANISOU 1975 CA PHE A 261 2575 2658 3112 -70 -246 -113 C ATOM 1976 C PHE A 261 16.840 28.111 37.844 1.00 22.30 C ANISOU 1976 C PHE A 261 2595 2676 3201 -88 -217 -115 C ATOM 1977 O PHE A 261 16.570 27.914 36.649 1.00 23.27 O ANISOU 1977 O PHE A 261 2746 2770 3326 -91 -184 -93 O ATOM 1978 CB PHE A 261 15.048 28.314 39.588 1.00 22.23 C ANISOU 1978 CB PHE A 261 2619 2694 3135 -91 -264 -136 C ATOM 1979 CG PHE A 261 14.021 28.824 38.597 1.00 23.04 C ANISOU 1979 CG PHE A 261 2755 2758 3240 -112 -239 -126 C ATOM 1980 CD1 PHE A 261 14.287 29.937 37.820 1.00 25.79 C ANISOU 1980 CD1 PHE A 261 3088 3082 3628 -134 -218 -134 C ATOM 1981 CD2 PHE A 261 12.828 28.154 38.419 1.00 25.36 C ANISOU 1981 CD2 PHE A 261 3095 3043 3498 -106 -234 -108 C ATOM 1982 CE1 PHE A 261 13.365 30.380 36.871 1.00 26.07 C ANISOU 1982 CE1 PHE A 261 3155 3089 3662 -146 -194 -119 C ATOM 1983 CE2 PHE A 261 11.892 28.605 37.484 1.00 25.10 C ANISOU 1983 CE2 PHE A 261 3090 2984 3464 -122 -214 -100 C ATOM 1984 CZ PHE A 261 12.182 29.697 36.708 1.00 23.02 C ANISOU 1984 CZ PHE A 261 2812 2701 3234 -139 -194 -104 C ATOM 1985 N LEU A 262 17.800 28.952 38.224 1.00 21.94 N ANISOU 1985 N LEU A 262 2499 2643 3195 -100 -227 -142 N ATOM 1986 CA LEU A 262 18.541 29.713 37.221 1.00 22.11 C ANISOU 1986 CA LEU A 262 2496 2637 3267 -119 -195 -142 C ATOM 1987 C LEU A 262 19.401 28.800 36.362 1.00 23.61 C ANISOU 1987 C LEU A 262 2684 2822 3465 -98 -168 -114 C ATOM 1988 O LEU A 262 19.510 29.007 35.149 1.00 24.42 O ANISOU 1988 O LEU A 262 2798 2895 3587 -104 -129 -96 O ATOM 1989 CB LEU A 262 19.408 30.766 37.898 1.00 22.53 C ANISOU 1989 CB LEU A 262 2488 2704 3367 -139 -211 -183 C ATOM 1990 CG LEU A 262 18.591 31.838 38.613 1.00 26.01 C ANISOU 1990 CG LEU A 262 2930 3143 3810 -163 -230 -216 C ATOM 1991 CD1 LEU A 262 19.528 32.738 39.407 1.00 28.49 C ANISOU 1991 CD1 LEU A 262 3179 3475 4169 -182 -250 -266 C ATOM 1992 CD2 LEU A 262 17.799 32.641 37.600 1.00 30.24 C ANISOU 1992 CD2 LEU A 262 3496 3630 4363 -183 -192 -200 C ATOM 1993 N ILE A 263 20.023 27.784 36.965 1.00 22.37 N ANISOU 1993 N ILE A 263 2512 2695 3291 -70 -187 -109 N ATOM 1994 CA ILE A 263 20.778 26.822 36.161 1.00 22.46 C ANISOU 1994 CA ILE A 263 2526 2700 3309 -47 -159 -81 C ATOM 1995 C ILE A 263 19.859 26.173 35.133 1.00 23.42 C ANISOU 1995 C ILE A 263 2708 2791 3402 -42 -128 -54 C ATOM 1996 O ILE A 263 20.204 26.025 33.950 1.00 23.19 O ANISOU 1996 O ILE A 263 2687 2739 3385 -41 -91 -37 O ATOM 1997 CB ILE A 263 21.425 25.763 37.069 1.00 22.70 C ANISOU 1997 CB ILE A 263 2537 2768 3321 -11 -183 -74 C ATOM 1998 CG1 ILE A 263 22.566 26.380 37.878 1.00 24.93 C ANISOU 1998 CG1 ILE A 263 2749 3086 3635 -13 -210 -103 C ATOM 1999 CG2 ILE A 263 21.876 24.586 36.272 1.00 26.15 C ANISOU 1999 CG2 ILE A 263 2991 3190 3755 16 -151 -42 C ATOM 2000 CD1 ILE A 263 23.215 25.400 38.827 1.00 29.24 C ANISOU 2000 CD1 ILE A 263 3272 3679 4159 27 -238 -95 C ATOM 2001 N CYS A 264 18.674 25.773 35.588 1.00 21.81 N ANISOU 2001 N CYS A 264 2543 2588 3156 -40 -145 -51 N ATOM 2002 CA CYS A 264 17.739 25.033 34.762 1.00 22.65 C ANISOU 2002 CA CYS A 264 2703 2671 3233 -36 -122 -33 C ATOM 2003 C CYS A 264 17.232 25.867 33.592 1.00 26.35 C ANISOU 2003 C CYS A 264 3189 3114 3708 -58 -96 -32 C ATOM 2004 O CYS A 264 17.190 25.383 32.454 1.00 26.15 O ANISOU 2004 O CYS A 264 3188 3073 3675 -51 -65 -17 O ATOM 2005 CB CYS A 264 16.581 24.546 35.637 1.00 24.92 C ANISOU 2005 CB CYS A 264 3020 2966 3481 -32 -146 -34 C ATOM 2006 SG CYS A 264 15.379 23.505 34.789 1.00 25.65 S ANISOU 2006 SG CYS A 264 3173 3033 3541 -29 -122 -20 S ATOM 2007 N TRP A 265 16.850 27.125 33.839 1.00 21.33 N ANISOU 2007 N TRP A 265 2541 2476 3086 -81 -106 -46 N ATOM 2008 CA TRP A 265 16.066 27.875 32.869 1.00 21.90 C ANISOU 2008 CA TRP A 265 2639 2527 3156 -97 -84 -39 C ATOM 2009 C TRP A 265 16.823 28.980 32.141 1.00 24.50 C ANISOU 2009 C TRP A 265 2940 2840 3530 -109 -55 -36 C ATOM 2010 O TRP A 265 16.377 29.406 31.069 1.00 23.26 O ANISOU 2010 O TRP A 265 2803 2666 3368 -112 -26 -19 O ATOM 2011 CB TRP A 265 14.839 28.492 33.569 1.00 20.94 C ANISOU 2011 CB TRP A 265 2532 2407 3016 -112 -109 -52 C ATOM 2012 CG TRP A 265 13.819 27.463 33.903 1.00 20.68 C ANISOU 2012 CG TRP A 265 2537 2383 2939 -102 -124 -49 C ATOM 2013 CD1 TRP A 265 13.553 26.921 35.134 1.00 23.01 C ANISOU 2013 CD1 TRP A 265 2832 2695 3215 -94 -154 -58 C ATOM 2014 CD2 TRP A 265 12.922 26.818 32.978 1.00 21.01 C ANISOU 2014 CD2 TRP A 265 2619 2414 2948 -98 -107 -37 C ATOM 2015 NE1 TRP A 265 12.549 25.983 35.030 1.00 20.43 N ANISOU 2015 NE1 TRP A 265 2544 2365 2854 -87 -152 -49 N ATOM 2016 CE2 TRP A 265 12.143 25.907 33.720 1.00 20.35 C ANISOU 2016 CE2 TRP A 265 2557 2338 2836 -92 -126 -40 C ATOM 2017 CE3 TRP A 265 12.708 26.929 31.593 1.00 21.50 C ANISOU 2017 CE3 TRP A 265 2700 2465 3003 -98 -78 -25 C ATOM 2018 CZ2 TRP A 265 11.161 25.109 33.133 1.00 20.50 C ANISOU 2018 CZ2 TRP A 265 2614 2351 2826 -90 -117 -37 C ATOM 2019 CZ3 TRP A 265 11.713 26.146 31.011 1.00 20.55 C ANISOU 2019 CZ3 TRP A 265 2616 2345 2846 -94 -73 -24 C ATOM 2020 CH2 TRP A 265 10.961 25.238 31.787 1.00 20.95 C ANISOU 2020 CH2 TRP A 265 2684 2399 2875 -92 -93 -32 C ATOM 2021 N LEU A 266 17.898 29.519 32.718 1.00 22.42 N ANISOU 2021 N LEU A 266 2627 2582 3311 -117 -61 -51 N ATOM 2022 CA LEU A 266 18.614 30.594 32.031 1.00 21.99 C ANISOU 2022 CA LEU A 266 2543 2506 3308 -131 -27 -48 C ATOM 2023 C LEU A 266 19.120 30.203 30.646 1.00 24.03 C ANISOU 2023 C LEU A 266 2812 2750 3567 -116 18 -18 C ATOM 2024 O LEU A 266 19.052 31.055 29.738 1.00 25.40 O ANISOU 2024 O LEU A 266 2990 2902 3761 -124 55 -1 O ATOM 2025 CB LEU A 266 19.775 31.099 32.891 1.00 23.30 C ANISOU 2025 CB LEU A 266 2647 2681 3524 -143 -42 -76 C ATOM 2026 CG LEU A 266 19.414 32.164 33.929 1.00 33.05 C ANISOU 2026 CG LEU A 266 3860 3917 4779 -168 -69 -112 C ATOM 2027 CD1 LEU A 266 20.676 32.619 34.641 1.00 30.35 C ANISOU 2027 CD1 LEU A 266 3451 3589 4490 -180 -82 -146 C ATOM 2028 CD2 LEU A 266 18.736 33.356 33.243 1.00 36.00 C ANISOU 2028 CD2 LEU A 266 4249 4255 5176 -187 -37 -102 C ATOM 2029 N PRO A 267 19.669 29.002 30.414 1.00 22.14 N ANISOU 2029 N PRO A 267 2578 2522 3311 -94 22 -8 N ATOM 2030 CA PRO A 267 20.084 28.678 29.033 1.00 22.27 C ANISOU 2030 CA PRO A 267 2608 2526 3326 -79 68 18 C ATOM 2031 C PRO A 267 18.921 28.736 28.054 1.00 22.21 C ANISOU 2031 C PRO A 267 2652 2512 3276 -76 86 35 C ATOM 2032 O PRO A 267 19.055 29.308 26.968 1.00 24.93 O ANISOU 2032 O PRO A 267 3001 2844 3628 -73 126 56 O ATOM 2033 CB PRO A 267 20.655 27.260 29.153 1.00 25.22 C ANISOU 2033 CB PRO A 267 2985 2915 3684 -55 63 20 C ATOM 2034 CG PRO A 267 21.068 27.125 30.637 1.00 27.41 C ANISOU 2034 CG PRO A 267 3226 3212 3975 -57 19 -2 C ATOM 2035 CD PRO A 267 20.004 27.911 31.364 1.00 23.99 C ANISOU 2035 CD PRO A 267 2804 2781 3530 -78 -11 -19 C ATOM 2036 N TYR A 268 17.779 28.150 28.421 1.00 21.72 N ANISOU 2036 N TYR A 268 2626 2460 3167 -74 57 26 N ATOM 2037 CA TYR A 268 16.598 28.223 27.561 1.00 22.23 C ANISOU 2037 CA TYR A 268 2732 2524 3189 -72 67 37 C ATOM 2038 C TYR A 268 16.170 29.681 27.351 1.00 24.76 C ANISOU 2038 C TYR A 268 3047 2832 3528 -86 79 47 C ATOM 2039 O TYR A 268 15.930 30.121 26.218 1.00 23.19 O ANISOU 2039 O TYR A 268 2865 2630 3317 -77 112 70 O ATOM 2040 CB TYR A 268 15.459 27.387 28.171 1.00 21.60 C ANISOU 2040 CB TYR A 268 2685 2456 3067 -72 33 22 C ATOM 2041 CG TYR A 268 14.243 27.377 27.290 1.00 22.64 C ANISOU 2041 CG TYR A 268 2856 2594 3154 -70 40 27 C ATOM 2042 CD1 TYR A 268 14.204 26.595 26.141 1.00 24.79 C ANISOU 2042 CD1 TYR A 268 3152 2872 3394 -53 64 32 C ATOM 2043 CD2 TYR A 268 13.135 28.176 27.587 1.00 22.61 C ANISOU 2043 CD2 TYR A 268 2861 2590 3138 -82 22 25 C ATOM 2044 CE1 TYR A 268 13.093 26.592 25.298 1.00 24.33 C ANISOU 2044 CE1 TYR A 268 3126 2827 3292 -50 67 32 C ATOM 2045 CE2 TYR A 268 12.017 28.192 26.744 1.00 23.89 C ANISOU 2045 CE2 TYR A 268 3055 2765 3259 -77 27 30 C ATOM 2046 CZ TYR A 268 12.021 27.402 25.596 1.00 24.99 C ANISOU 2046 CZ TYR A 268 3216 2915 3365 -61 48 33 C ATOM 2047 OH TYR A 268 10.944 27.390 24.744 1.00 24.06 O ANISOU 2047 OH TYR A 268 3124 2816 3201 -54 49 34 O ATOM 2048 N ALA A 269 16.116 30.462 28.429 1.00 23.38 N ANISOU 2048 N ALA A 269 2847 2652 3384 -105 55 30 N ATOM 2049 CA ALA A 269 15.675 31.857 28.308 1.00 21.62 C ANISOU 2049 CA ALA A 269 2619 2412 3185 -119 68 38 C ATOM 2050 C ALA A 269 16.617 32.665 27.417 1.00 25.03 C ANISOU 2050 C ALA A 269 3027 2822 3662 -118 119 61 C ATOM 2051 O ALA A 269 16.172 33.492 26.609 1.00 23.63 O ANISOU 2051 O ALA A 269 2863 2631 3485 -113 150 87 O ATOM 2052 CB ALA A 269 15.585 32.503 29.687 1.00 21.70 C ANISOU 2052 CB ALA A 269 2602 2418 3224 -141 35 8 C ATOM 2053 N GLY A 270 17.925 32.450 27.560 1.00 22.70 N ANISOU 2053 N GLY A 270 2695 2523 3406 -119 129 54 N ATOM 2054 CA GLY A 270 18.875 33.207 26.753 1.00 25.88 C ANISOU 2054 CA GLY A 270 3072 2904 3859 -119 180 76 C ATOM 2055 C GLY A 270 18.827 32.849 25.276 1.00 24.54 C ANISOU 2055 C GLY A 270 2933 2737 3654 -93 223 114 C ATOM 2056 O GLY A 270 18.913 33.729 24.411 1.00 24.44 O ANISOU 2056 O GLY A 270 2919 2705 3660 -87 270 146 O ATOM 2057 N VAL A 271 18.694 31.557 24.965 1.00 22.60 N ANISOU 2057 N VAL A 271 2715 2515 3357 -74 211 112 N ATOM 2058 CA VAL A 271 18.607 31.148 23.564 1.00 23.17 C ANISOU 2058 CA VAL A 271 2818 2597 3388 -47 248 140 C ATOM 2059 C VAL A 271 17.310 31.651 22.946 1.00 22.63 C ANISOU 2059 C VAL A 271 2786 2536 3273 -39 252 158 C ATOM 2060 O VAL A 271 17.295 32.164 21.820 1.00 24.92 O ANISOU 2060 O VAL A 271 3088 2827 3553 -20 295 192 O ATOM 2061 CB VAL A 271 18.755 29.619 23.443 1.00 25.54 C ANISOU 2061 CB VAL A 271 3138 2918 3648 -31 234 125 C ATOM 2062 CG1 VAL A 271 18.452 29.140 21.997 1.00 27.28 C ANISOU 2062 CG1 VAL A 271 3396 3155 3814 -4 267 145 C ATOM 2063 CG2 VAL A 271 20.159 29.213 23.878 1.00 28.76 C ANISOU 2063 CG2 VAL A 271 3505 3319 4103 -32 240 117 C ATOM 2064 N ALA A 272 16.208 31.525 23.677 1.00 22.27 N ANISOU 2064 N ALA A 272 2759 2501 3202 -50 208 137 N ATOM 2065 CA ALA A 272 14.937 32.056 23.211 1.00 27.12 C ANISOU 2065 CA ALA A 272 3403 3126 3777 -42 206 152 C ATOM 2066 C ALA A 272 15.051 33.541 22.890 1.00 25.15 C ANISOU 2066 C ALA A 272 3136 2851 3568 -43 244 184 C ATOM 2067 O ALA A 272 14.613 33.991 21.821 1.00 23.85 O ANISOU 2067 O ALA A 272 2991 2695 3375 -20 276 219 O ATOM 2068 CB ALA A 272 13.850 31.827 24.276 1.00 25.37 C ANISOU 2068 CB ALA A 272 3192 2911 3535 -59 154 123 C ATOM 2069 N PHE A 273 15.614 34.328 23.815 1.00 22.54 N ANISOU 2069 N PHE A 273 2769 2490 3305 -68 242 172 N ATOM 2070 CA PHE A 273 15.702 35.768 23.569 1.00 24.35 C ANISOU 2070 CA PHE A 273 2981 2686 3583 -72 283 199 C ATOM 2071 C PHE A 273 16.645 36.065 22.416 1.00 28.11 C ANISOU 2071 C PHE A 273 3448 3151 4081 -54 346 239 C ATOM 2072 O PHE A 273 16.408 37.004 21.644 1.00 27.73 O ANISOU 2072 O PHE A 273 3406 3088 4042 -38 391 281 O ATOM 2073 CB PHE A 273 16.147 36.524 24.827 1.00 30.96 C ANISOU 2073 CB PHE A 273 3778 3494 4493 -107 268 168 C ATOM 2074 CG PHE A 273 16.102 38.043 24.669 1.00 29.41 C ANISOU 2074 CG PHE A 273 3565 3256 4355 -114 312 190 C ATOM 2075 CD1 PHE A 273 14.897 38.716 24.684 1.00 39.09 C ANISOU 2075 CD1 PHE A 273 4814 4478 5562 -109 308 204 C ATOM 2076 CD2 PHE A 273 17.262 38.769 24.499 1.00 35.51 C ANISOU 2076 CD2 PHE A 273 4297 3992 5204 -126 359 199 C ATOM 2077 CE1 PHE A 273 14.852 40.100 24.542 1.00 48.09 C ANISOU 2077 CE1 PHE A 273 5939 5575 6760 -114 353 227 C ATOM 2078 CE2 PHE A 273 17.228 40.162 24.361 1.00 32.86 C ANISOU 2078 CE2 PHE A 273 3946 3611 4930 -134 405 220 C ATOM 2079 CZ PHE A 273 16.026 40.819 24.378 1.00 33.25 C ANISOU 2079 CZ PHE A 273 4020 3654 4960 -127 403 235 C ATOM 2080 N TYR A 274 17.706 35.274 22.270 1.00 23.71 N ANISOU 2080 N TYR A 274 2876 2600 3534 -52 353 230 N ATOM 2081 CA TYR A 274 18.577 35.437 21.111 1.00 23.86 C ANISOU 2081 CA TYR A 274 2888 2611 3565 -30 415 268 C ATOM 2082 C TYR A 274 17.804 35.219 19.817 1.00 25.10 C ANISOU 2082 C TYR A 274 3090 2798 3646 8 437 305 C ATOM 2083 O TYR A 274 17.946 35.984 18.856 1.00 27.95 O ANISOU 2083 O TYR A 274 3455 3151 4014 30 493 353 O ATOM 2084 CB TYR A 274 19.749 34.464 21.189 1.00 25.26 C ANISOU 2084 CB TYR A 274 3044 2796 3757 -31 414 250 C ATOM 2085 CG TYR A 274 20.653 34.586 19.986 1.00 28.56 C ANISOU 2085 CG TYR A 274 3456 3207 4187 -8 480 290 C ATOM 2086 CD1 TYR A 274 21.621 35.582 19.925 1.00 37.01 C ANISOU 2086 CD1 TYR A 274 4484 4239 5340 -20 530 308 C ATOM 2087 CD2 TYR A 274 20.519 33.733 18.901 1.00 34.14 C ANISOU 2087 CD2 TYR A 274 4200 3947 4826 26 496 307 C ATOM 2088 CE1 TYR A 274 22.441 35.714 18.818 1.00 38.29 C ANISOU 2088 CE1 TYR A 274 4640 4394 5515 2 596 349 C ATOM 2089 CE2 TYR A 274 21.335 33.861 17.792 1.00 36.41 C ANISOU 2089 CE2 TYR A 274 4483 4232 5121 50 560 344 C ATOM 2090 CZ TYR A 274 22.293 34.856 17.765 1.00 41.05 C ANISOU 2090 CZ TYR A 274 5028 4779 5791 39 610 368 C ATOM 2091 OH TYR A 274 23.115 34.987 16.668 1.00 46.04 O ANISOU 2091 OH TYR A 274 5654 5406 6432 64 678 409 O ATOM 2092 N ILE A 275 17.001 34.154 19.763 1.00 24.12 N ANISOU 2092 N ILE A 275 3001 2713 3449 18 394 283 N ATOM 2093 CA ILE A 275 16.284 33.855 18.526 1.00 27.99 C ANISOU 2093 CA ILE A 275 3532 3242 3862 54 410 309 C ATOM 2094 C ILE A 275 15.301 34.971 18.227 1.00 23.82 C ANISOU 2094 C ILE A 275 3016 2714 3322 66 422 343 C ATOM 2095 O ILE A 275 15.244 35.491 17.105 1.00 26.41 O ANISOU 2095 O ILE A 275 3357 3053 3626 99 469 390 O ATOM 2096 CB ILE A 275 15.607 32.471 18.626 1.00 24.82 C ANISOU 2096 CB ILE A 275 3159 2878 3394 56 360 268 C ATOM 2097 CG1 ILE A 275 16.678 31.369 18.551 1.00 27.81 C ANISOU 2097 CG1 ILE A 275 3530 3258 3780 57 367 248 C ATOM 2098 CG2 ILE A 275 14.552 32.269 17.530 1.00 26.28 C ANISOU 2098 CG2 ILE A 275 3382 3108 3494 87 362 282 C ATOM 2099 CD1 ILE A 275 16.130 29.940 18.845 1.00 28.31 C ANISOU 2099 CD1 ILE A 275 3617 3345 3794 53 321 204 C ATOM 2100 N PHE A 276 14.590 35.427 19.259 1.00 23.79 N ANISOU 2100 N PHE A 276 3005 2694 3339 41 385 322 N ATOM 2101 CA PHE A 276 13.575 36.462 19.088 1.00 26.33 C ANISOU 2101 CA PHE A 276 3338 3014 3652 53 393 352 C ATOM 2102 C PHE A 276 14.161 37.731 18.482 1.00 28.48 C ANISOU 2102 C PHE A 276 3594 3251 3976 67 462 407 C ATOM 2103 O PHE A 276 13.496 38.418 17.692 1.00 30.32 O ANISOU 2103 O PHE A 276 3844 3495 4180 99 491 453 O ATOM 2104 CB PHE A 276 12.939 36.757 20.448 1.00 24.54 C ANISOU 2104 CB PHE A 276 3101 2768 3455 20 346 317 C ATOM 2105 CG PHE A 276 11.886 37.829 20.416 1.00 26.57 C ANISOU 2105 CG PHE A 276 3366 3018 3710 29 353 344 C ATOM 2106 CD1 PHE A 276 10.720 37.645 19.700 1.00 27.16 C ANISOU 2106 CD1 PHE A 276 3473 3137 3709 60 341 362 C ATOM 2107 CD2 PHE A 276 12.038 38.991 21.164 1.00 31.12 C ANISOU 2107 CD2 PHE A 276 3918 3545 4362 8 369 346 C ATOM 2108 CE1 PHE A 276 9.737 38.614 19.678 1.00 34.42 C ANISOU 2108 CE1 PHE A 276 4399 4053 4626 73 347 389 C ATOM 2109 CE2 PHE A 276 11.046 39.969 21.163 1.00 31.05 C ANISOU 2109 CE2 PHE A 276 3917 3527 4354 18 378 371 C ATOM 2110 CZ PHE A 276 9.908 39.790 20.404 1.00 37.11 C ANISOU 2110 CZ PHE A 276 4716 4339 5045 53 368 397 C ATOM 2111 N THR A 277 15.400 38.062 18.836 1.00 27.73 N ANISOU 2111 N THR A 277 3462 3113 3959 45 492 403 N ATOM 2112 CA THR A 277 16.050 39.265 18.332 1.00 28.23 C ANISOU 2112 CA THR A 277 3505 3134 4087 53 564 451 C ATOM 2113 C THR A 277 16.906 39.006 17.102 1.00 30.84 C ANISOU 2113 C THR A 277 3839 3476 4402 85 620 491 C ATOM 2114 O THR A 277 17.558 39.938 16.612 1.00 32.86 O ANISOU 2114 O THR A 277 4076 3695 4714 94 688 536 O ATOM 2115 CB THR A 277 16.913 39.907 19.442 1.00 29.24 C ANISOU 2115 CB THR A 277 3584 3206 4320 8 568 420 C ATOM 2116 OG1 THR A 277 17.815 38.940 19.965 1.00 28.33 O ANISOU 2116 OG1 THR A 277 3448 3100 4216 -14 538 376 O ATOM 2117 CG2 THR A 277 16.042 40.389 20.583 1.00 31.45 C ANISOU 2117 CG2 THR A 277 3861 3471 4617 -19 523 387 C ATOM 2118 N HIS A 278 16.944 37.770 16.608 1.00 26.11 N ANISOU 2118 N HIS A 278 3262 2925 3732 102 598 475 N ATOM 2119 CA HIS A 278 17.757 37.398 15.447 1.00 27.58 C ANISOU 2119 CA HIS A 278 3455 3129 3897 134 649 507 C ATOM 2120 C HIS A 278 16.958 36.457 14.553 1.00 27.35 C ANISOU 2120 C HIS A 278 3470 3165 3756 170 627 506 C ATOM 2121 O HIS A 278 17.454 35.424 14.103 1.00 30.05 O ANISOU 2121 O HIS A 278 3821 3534 4062 180 625 489 O ATOM 2122 CB HIS A 278 19.078 36.744 15.848 1.00 30.95 C ANISOU 2122 CB HIS A 278 3850 3537 4374 110 651 476 C ATOM 2123 CG HIS A 278 19.974 37.642 16.633 1.00 35.42 C ANISOU 2123 CG HIS A 278 4366 4043 5049 74 675 472 C ATOM 2124 ND1 HIS A 278 19.773 37.901 17.971 1.00 29.89 N ANISOU 2124 ND1 HIS A 278 3642 3320 4396 33 627 427 N ATOM 2125 CD2 HIS A 278 21.061 38.365 16.265 1.00 36.70 C ANISOU 2125 CD2 HIS A 278 4494 4166 5285 73 743 504 C ATOM 2126 CE1 HIS A 278 20.698 38.748 18.394 1.00 36.72 C ANISOU 2126 CE1 HIS A 278 4460 4134 5359 6 662 427 C ATOM 2127 NE2 HIS A 278 21.496 39.036 17.382 1.00 37.68 N ANISOU 2127 NE2 HIS A 278 4573 4243 5501 28 733 473 N ATOM 2128 N GLN A 279 15.705 36.813 14.287 1.00 27.20 N ANISOU 2128 N GLN A 279 3477 3174 3682 191 610 523 N ATOM 2129 CA GLN A 279 14.817 35.901 13.571 1.00 32.94 C ANISOU 2129 CA GLN A 279 4242 3970 4304 220 577 509 C ATOM 2130 C GLN A 279 15.358 35.612 12.182 1.00 29.36 C ANISOU 2130 C GLN A 279 3804 3551 3800 264 629 543 C ATOM 2131 O GLN A 279 15.866 36.504 11.507 1.00 30.75 O ANISOU 2131 O GLN A 279 3974 3711 4000 291 695 604 O ATOM 2132 CB GLN A 279 13.405 36.485 13.484 1.00 28.48 C ANISOU 2132 CB GLN A 279 3696 3431 3694 237 555 526 C ATOM 2133 CG GLN A 279 12.664 36.414 14.814 1.00 28.49 C ANISOU 2133 CG GLN A 279 3690 3414 3722 195 492 479 C ATOM 2134 CD GLN A 279 11.273 36.973 14.732 1.00 33.42 C ANISOU 2134 CD GLN A 279 4330 4065 4304 213 471 496 C ATOM 2135 OE1 GLN A 279 10.920 37.641 13.755 1.00 34.26 O ANISOU 2135 OE1 GLN A 279 4448 4195 4374 258 508 551 O ATOM 2136 NE2 GLN A 279 10.459 36.691 15.743 1.00 27.88 N ANISOU 2136 NE2 GLN A 279 3628 3362 3604 183 412 451 N ATOM 2137 N GLY A 280 15.291 34.342 11.775 1.00 33.92 N ANISOU 2137 N GLY A 280 4402 4174 4312 272 601 504 N ATOM 2138 CA GLY A 280 15.734 33.958 10.449 1.00 34.99 C ANISOU 2138 CA GLY A 280 4555 4350 4388 316 646 527 C ATOM 2139 C GLY A 280 17.231 33.838 10.276 1.00 37.90 C ANISOU 2139 C GLY A 280 4902 4684 4813 313 698 540 C ATOM 2140 O GLY A 280 17.689 33.555 9.164 1.00 37.33 O ANISOU 2140 O GLY A 280 4845 4644 4696 352 742 563 O ATOM 2141 N SER A 281 18.006 34.020 11.338 1.00 35.88 N ANISOU 2141 N SER A 281 4612 4369 4652 270 694 524 N ATOM 2142 CA SER A 281 19.448 33.900 11.264 1.00 34.21 C ANISOU 2142 CA SER A 281 4373 4125 4501 264 740 532 C ATOM 2143 C SER A 281 19.840 32.428 11.178 1.00 37.56 C ANISOU 2143 C SER A 281 4808 4573 4889 263 716 482 C ATOM 2144 O SER A 281 19.014 31.517 11.301 1.00 31.50 O ANISOU 2144 O SER A 281 4066 3840 4061 260 662 437 O ATOM 2145 CB SER A 281 20.106 34.586 12.470 1.00 37.41 C ANISOU 2145 CB SER A 281 4733 4465 5018 218 739 525 C ATOM 2146 OG SER A 281 19.713 33.975 13.700 1.00 30.36 O ANISOU 2146 OG SER A 281 3833 3565 4136 179 666 464 O ATOM 2147 N ASP A 282 21.122 32.197 10.961 1.00 35.27 N ANISOU 2147 N ASP A 282 4496 4263 4642 265 760 490 N ATOM 2148 CA ASP A 282 21.609 30.861 10.633 1.00 39.09 C ANISOU 2148 CA ASP A 282 4991 4769 5092 274 754 453 C ATOM 2149 C ASP A 282 21.899 30.106 11.921 1.00 37.98 C ANISOU 2149 C ASP A 282 4829 4602 5001 232 701 399 C ATOM 2150 O ASP A 282 23.001 30.160 12.466 1.00 44.82 O ANISOU 2150 O ASP A 282 5656 5432 5943 214 717 399 O ATOM 2151 CB ASP A 282 22.849 30.955 9.750 1.00 41.85 C ANISOU 2151 CB ASP A 282 5327 5112 5462 300 830 491 C ATOM 2152 CG ASP A 282 23.246 29.618 9.163 1.00 48.99 C ANISOU 2152 CG ASP A 282 6250 6047 6317 320 833 458 C ATOM 2153 OD1 ASP A 282 22.449 28.658 9.267 1.00 51.14 O ANISOU 2153 OD1 ASP A 282 6551 6349 6530 317 782 408 O ATOM 2154 OD2 ASP A 282 24.354 29.533 8.597 1.00 58.51 O ANISOU 2154 OD2 ASP A 282 7442 7244 7547 337 891 480 O ATOM 2155 N PHE A 283 20.907 29.371 12.410 1.00 34.58 N ANISOU 2155 N PHE A 283 4421 4191 4526 219 639 354 N ATOM 2156 CA PHE A 283 21.123 28.434 13.501 1.00 33.79 C ANISOU 2156 CA PHE A 283 4309 4073 4457 189 592 304 C ATOM 2157 C PHE A 283 20.493 27.104 13.110 1.00 33.40 C ANISOU 2157 C PHE A 283 4297 4059 4334 201 565 261 C ATOM 2158 O PHE A 283 19.619 27.043 12.241 1.00 30.93 O ANISOU 2158 O PHE A 283 4019 3787 3948 223 565 260 O ATOM 2159 CB PHE A 283 20.565 28.958 14.837 1.00 29.92 C ANISOU 2159 CB PHE A 283 3800 3558 4008 152 541 290 C ATOM 2160 CG PHE A 283 19.101 29.333 14.795 1.00 28.77 C ANISOU 2160 CG PHE A 283 3685 3437 3810 153 508 288 C ATOM 2161 CD1 PHE A 283 18.126 28.379 15.061 1.00 33.27 C ANISOU 2161 CD1 PHE A 283 4282 4031 4329 146 458 244 C ATOM 2162 CD2 PHE A 283 18.708 30.646 14.555 1.00 32.49 C ANISOU 2162 CD2 PHE A 283 4152 3902 4290 159 529 330 C ATOM 2163 CE1 PHE A 283 16.776 28.711 15.049 1.00 32.46 C ANISOU 2163 CE1 PHE A 283 4201 3951 4180 146 426 240 C ATOM 2164 CE2 PHE A 283 17.354 30.994 14.526 1.00 29.28 C ANISOU 2164 CE2 PHE A 283 3770 3519 3835 162 499 330 C ATOM 2165 CZ PHE A 283 16.386 30.015 14.771 1.00 27.07 C ANISOU 2165 CZ PHE A 283 3515 3269 3501 156 445 284 C ATOM 2166 N GLY A 284 20.976 26.035 13.732 1.00 29.54 N ANISOU 2166 N GLY A 284 3800 3554 3869 188 546 224 N ATOM 2167 CA GLY A 284 20.564 24.700 13.371 1.00 28.94 C ANISOU 2167 CA GLY A 284 3756 3501 3738 197 530 180 C ATOM 2168 C GLY A 284 19.692 24.070 14.441 1.00 26.79 C ANISOU 2168 C GLY A 284 3492 3222 3466 169 469 139 C ATOM 2169 O GLY A 284 19.355 24.698 15.451 1.00 25.95 O ANISOU 2169 O GLY A 284 3368 3097 3394 145 436 144 O ATOM 2170 N PRO A 285 19.321 22.805 14.245 1.00 24.55 N ANISOU 2170 N PRO A 285 3234 2949 3146 173 457 95 N ATOM 2171 CA PRO A 285 18.352 22.187 15.170 1.00 26.50 C ANISOU 2171 CA PRO A 285 3492 3189 3389 148 404 57 C ATOM 2172 C PRO A 285 18.932 21.863 16.539 1.00 26.23 C ANISOU 2172 C PRO A 285 3431 3116 3421 127 382 53 C ATOM 2173 O PRO A 285 18.175 21.776 17.514 1.00 26.16 O ANISOU 2173 O PRO A 285 3423 3099 3419 105 339 38 O ATOM 2174 CB PRO A 285 17.897 20.918 14.428 1.00 25.80 C ANISOU 2174 CB PRO A 285 3436 3120 3248 158 407 10 C ATOM 2175 CG PRO A 285 18.920 20.670 13.373 1.00 29.54 C ANISOU 2175 CG PRO A 285 3911 3602 3712 188 461 20 C ATOM 2176 CD PRO A 285 19.622 21.966 13.069 1.00 26.94 C ANISOU 2176 CD PRO A 285 3559 3274 3404 200 493 77 C ATOM 2177 N ILE A 286 20.248 21.687 16.660 1.00 24.03 N ANISOU 2177 N ILE A 286 3125 2817 3188 137 411 69 N ATOM 2178 CA ILE A 286 20.784 21.354 17.976 1.00 26.21 C ANISOU 2178 CA ILE A 286 3373 3065 3521 122 387 65 C ATOM 2179 C ILE A 286 20.737 22.572 18.901 1.00 23.56 C ANISOU 2179 C ILE A 286 3007 2721 3223 101 361 86 C ATOM 2180 O ILE A 286 20.637 22.429 20.124 1.00 24.96 O ANISOU 2180 O ILE A 286 3170 2887 3428 84 323 76 O ATOM 2181 CB ILE A 286 22.209 20.774 17.826 1.00 31.73 C ANISOU 2181 CB ILE A 286 4050 3749 4258 141 424 74 C ATOM 2182 CG1 ILE A 286 22.176 19.556 16.908 1.00 36.05 C ANISOU 2182 CG1 ILE A 286 4629 4301 4767 162 451 48 C ATOM 2183 CG2 ILE A 286 22.730 20.295 19.174 1.00 30.41 C ANISOU 2183 CG2 ILE A 286 3854 3561 4141 133 396 70 C ATOM 2184 CD1 ILE A 286 21.283 18.441 17.463 1.00 39.58 C ANISOU 2184 CD1 ILE A 286 5103 4740 5198 152 420 8 C ATOM 2185 N PHE A 287 20.782 23.780 18.337 1.00 23.69 N ANISOU 2185 N PHE A 287 3016 2745 3241 102 382 115 N ATOM 2186 CA PHE A 287 20.902 25.009 19.132 1.00 26.56 C ANISOU 2186 CA PHE A 287 3346 3094 3650 81 368 134 C ATOM 2187 C PHE A 287 19.833 25.116 20.232 1.00 28.01 C ANISOU 2187 C PHE A 287 3536 3277 3828 58 312 114 C ATOM 2188 O PHE A 287 20.140 25.403 21.403 1.00 23.65 O ANISOU 2188 O PHE A 287 2954 2711 3319 40 285 109 O ATOM 2189 CB PHE A 287 20.838 26.190 18.158 1.00 27.72 C ANISOU 2189 CB PHE A 287 3495 3248 3790 90 405 169 C ATOM 2190 CG PHE A 287 21.019 27.555 18.770 1.00 26.08 C ANISOU 2190 CG PHE A 287 3253 3019 3636 70 404 189 C ATOM 2191 CD1 PHE A 287 22.134 27.861 19.540 1.00 34.08 C ANISOU 2191 CD1 PHE A 287 4218 4009 4721 56 408 190 C ATOM 2192 CD2 PHE A 287 20.124 28.566 18.462 1.00 27.01 C ANISOU 2192 CD2 PHE A 287 3386 3142 3735 68 406 209 C ATOM 2193 CE1 PHE A 287 22.306 29.143 20.056 1.00 39.82 C ANISOU 2193 CE1 PHE A 287 4911 4715 5502 34 410 202 C ATOM 2194 CE2 PHE A 287 20.285 29.837 18.964 1.00 30.89 C ANISOU 2194 CE2 PHE A 287 3847 3610 4281 50 412 226 C ATOM 2195 CZ PHE A 287 21.379 30.140 19.760 1.00 32.95 C ANISOU 2195 CZ PHE A 287 4059 3844 4616 31 415 220 C ATOM 2196 N MET A 288 18.571 24.905 19.883 1.00 22.96 N ANISOU 2196 N MET A 288 2935 2656 3133 58 295 101 N ATOM 2197 CA MET A 288 17.552 24.988 20.915 1.00 22.57 C ANISOU 2197 CA MET A 288 2891 2606 3079 36 246 83 C ATOM 2198 C MET A 288 17.237 23.637 21.536 1.00 22.39 C ANISOU 2198 C MET A 288 2884 2580 3045 33 220 51 C ATOM 2199 O MET A 288 16.662 23.609 22.621 1.00 22.85 O ANISOU 2199 O MET A 288 2939 2632 3110 16 182 39 O ATOM 2200 CB MET A 288 16.270 25.639 20.366 1.00 22.91 C ANISOU 2200 CB MET A 288 2960 2669 3076 35 238 88 C ATOM 2201 CG MET A 288 15.146 25.840 21.419 1.00 22.11 C ANISOU 2201 CG MET A 288 2863 2566 2971 13 190 71 C ATOM 2202 SD MET A 288 15.622 26.685 22.954 1.00 24.80 S ANISOU 2202 SD MET A 288 3164 2881 3377 -11 165 75 S ATOM 2203 CE MET A 288 14.856 28.317 22.769 1.00 25.47 C ANISOU 2203 CE MET A 288 3248 2967 3464 -18 169 99 C ATOM 2204 N THR A 289 17.606 22.522 20.891 1.00 22.60 N ANISOU 2204 N THR A 289 2925 2607 3054 50 242 38 N ATOM 2205 CA THR A 289 17.277 21.211 21.459 1.00 22.49 C ANISOU 2205 CA THR A 289 2927 2583 3035 48 224 10 C ATOM 2206 C THR A 289 17.865 21.021 22.856 1.00 22.35 C ANISOU 2206 C THR A 289 2880 2547 3063 42 202 15 C ATOM 2207 O THR A 289 17.161 20.600 23.784 1.00 22.11 O ANISOU 2207 O THR A 289 2858 2512 3030 31 170 1 O ATOM 2208 CB THR A 289 17.750 20.078 20.538 1.00 24.47 C ANISOU 2208 CB THR A 289 3196 2833 3271 68 260 -5 C ATOM 2209 OG1 THR A 289 17.023 20.137 19.303 1.00 22.97 O ANISOU 2209 OG1 THR A 289 3034 2667 3026 74 273 -18 O ATOM 2210 CG2 THR A 289 17.481 18.716 21.193 1.00 22.75 C ANISOU 2210 CG2 THR A 289 2991 2595 3058 66 248 -32 C ATOM 2211 N AILE A 290 19.159 21.303 23.032 0.61 22.53 N ANISOU 2211 N AILE A 290 2869 2564 3128 51 218 34 N ATOM 2212 N BILE A 290 19.159 21.304 23.027 0.39 22.53 N ANISOU 2212 N BILE A 290 2869 2564 3128 51 218 34 N ATOM 2213 CA AILE A 290 19.794 21.006 24.319 0.61 22.49 C ANISOU 2213 CA AILE A 290 2833 2550 3161 52 196 36 C ATOM 2214 CA BILE A 290 19.801 21.011 24.310 0.39 22.49 C ANISOU 2214 CA BILE A 290 2833 2550 3161 52 196 36 C ATOM 2215 C AILE A 290 19.196 21.835 25.453 0.61 22.20 C ANISOU 2215 C AILE A 290 2783 2519 3132 30 153 35 C ATOM 2216 C BILE A 290 19.213 21.836 25.452 0.39 22.20 C ANISOU 2216 C BILE A 290 2783 2520 3133 30 154 35 C ATOM 2217 O AILE A 290 18.798 21.249 26.472 0.61 22.36 O ANISOU 2217 O AILE A 290 2808 2538 3150 29 125 26 O ATOM 2218 O BILE A 290 18.834 21.246 26.476 0.39 22.37 O ANISOU 2218 O BILE A 290 2808 2540 3153 29 125 26 O ATOM 2219 CB AILE A 290 21.320 21.146 24.209 0.61 24.60 C ANISOU 2219 CB AILE A 290 3061 2815 3472 66 222 54 C ATOM 2220 CB BILE A 290 21.330 21.154 24.182 0.39 24.63 C ANISOU 2220 CB BILE A 290 3064 2818 3476 66 223 54 C ATOM 2221 CG1AILE A 290 21.834 20.340 23.004 0.61 30.86 C ANISOU 2221 CG1AILE A 290 3870 3602 4252 89 268 54 C ATOM 2222 CG1BILE A 290 21.859 20.098 23.195 0.39 30.70 C ANISOU 2222 CG1BILE A 290 3850 3580 4235 91 265 52 C ATOM 2223 CG2AILE A 290 21.968 20.640 25.506 0.61 26.52 C ANISOU 2223 CG2AILE A 290 3273 3057 3747 74 197 55 C ATOM 2224 CG2BILE A 290 21.981 21.009 25.556 0.39 27.09 C ANISOU 2224 CG2BILE A 290 3338 3132 3824 68 194 56 C ATOM 2225 CD1AILE A 290 21.509 18.864 23.094 0.61 33.13 C ANISOU 2225 CD1AILE A 290 4187 3878 4522 102 270 36 C ATOM 2226 CD1BILE A 290 23.343 20.185 22.892 0.39 28.81 C ANISOU 2226 CD1BILE A 290 3573 3337 4036 108 298 71 C ATOM 2227 N PRO A 291 19.104 23.170 25.361 1.00 22.16 N ANISOU 2227 N PRO A 291 2762 2518 3138 15 150 44 N ATOM 2228 CA PRO A 291 18.495 23.903 26.488 1.00 21.91 C ANISOU 2228 CA PRO A 291 2720 2490 3114 -5 111 37 C ATOM 2229 C PRO A 291 17.031 23.553 26.724 1.00 23.39 C ANISOU 2229 C PRO A 291 2945 2682 3260 -14 86 23 C ATOM 2230 O PRO A 291 16.591 23.538 27.878 1.00 21.41 O ANISOU 2230 O PRO A 291 2691 2435 3011 -23 52 14 O ATOM 2231 CB PRO A 291 18.682 25.383 26.116 1.00 24.55 C ANISOU 2231 CB PRO A 291 3034 2823 3472 -19 124 49 C ATOM 2232 CG PRO A 291 19.107 25.421 24.709 1.00 24.99 C ANISOU 2232 CG PRO A 291 3098 2875 3520 -5 170 66 C ATOM 2233 CD PRO A 291 19.653 24.084 24.336 1.00 22.74 C ANISOU 2233 CD PRO A 291 2825 2591 3225 17 187 62 C ATOM 2234 N ALA A 292 16.264 23.292 25.660 1.00 21.59 N ANISOU 2234 N ALA A 292 2752 2457 2994 -11 102 19 N ATOM 2235 CA ALA A 292 14.847 22.943 25.822 1.00 21.42 C ANISOU 2235 CA ALA A 292 2762 2441 2935 -21 79 2 C ATOM 2236 C ALA A 292 14.674 21.621 26.555 1.00 22.12 C ANISOU 2236 C ALA A 292 2862 2520 3022 -17 67 -12 C ATOM 2237 O ALA A 292 13.763 21.474 27.388 1.00 23.20 O ANISOU 2237 O ALA A 292 3008 2656 3149 -28 40 -22 O ATOM 2238 CB ALA A 292 14.160 22.881 24.454 1.00 21.68 C ANISOU 2238 CB ALA A 292 2825 2486 2927 -16 99 -4 C ATOM 2239 N PHE A 293 15.509 20.626 26.245 1.00 21.52 N ANISOU 2239 N PHE A 293 2786 2434 2957 1 92 -13 N ATOM 2240 CA PHE A 293 15.402 19.351 26.954 1.00 21.54 C ANISOU 2240 CA PHE A 293 2798 2421 2963 9 87 -21 C ATOM 2241 C PHE A 293 16.089 19.388 28.322 1.00 21.52 C ANISOU 2241 C PHE A 293 2767 2420 2991 17 66 -6 C ATOM 2242 O PHE A 293 15.620 18.740 29.264 1.00 21.45 O ANISOU 2242 O PHE A 293 2765 2405 2979 19 50 -7 O ATOM 2243 CB PHE A 293 15.963 18.221 26.066 1.00 21.83 C ANISOU 2243 CB PHE A 293 2850 2445 3001 27 125 -28 C ATOM 2244 CG PHE A 293 14.914 17.638 25.134 1.00 21.87 C ANISOU 2244 CG PHE A 293 2891 2448 2970 19 137 -58 C ATOM 2245 CD1 PHE A 293 14.450 18.366 24.054 1.00 22.54 C ANISOU 2245 CD1 PHE A 293 2987 2554 3024 12 141 -65 C ATOM 2246 CD2 PHE A 293 14.320 16.419 25.414 1.00 21.92 C ANISOU 2246 CD2 PHE A 293 2919 2434 2976 18 141 -78 C ATOM 2247 CE1 PHE A 293 13.428 17.860 23.228 1.00 23.32 C ANISOU 2247 CE1 PHE A 293 3115 2661 3085 5 146 -97 C ATOM 2248 CE2 PHE A 293 13.338 15.889 24.605 1.00 22.00 C ANISOU 2248 CE2 PHE A 293 2958 2444 2959 6 149 -112 C ATOM 2249 CZ PHE A 293 12.866 16.613 23.515 1.00 22.67 C ANISOU 2249 CZ PHE A 293 3050 2557 3006 -1 148 -125 C ATOM 2250 N PHE A 294 17.176 20.146 28.464 1.00 21.64 N ANISOU 2250 N PHE A 294 2745 2445 3033 21 66 8 N ATOM 2251 CA PHE A 294 17.754 20.304 29.794 1.00 23.92 C ANISOU 2251 CA PHE A 294 3001 2745 3345 28 39 17 C ATOM 2252 C PHE A 294 16.731 20.894 30.762 1.00 24.93 C ANISOU 2252 C PHE A 294 3133 2882 3457 10 2 9 C ATOM 2253 O PHE A 294 16.660 20.505 31.929 1.00 22.13 O ANISOU 2253 O PHE A 294 2772 2535 3102 18 -21 12 O ATOM 2254 CB PHE A 294 18.985 21.196 29.725 1.00 21.87 C ANISOU 2254 CB PHE A 294 2697 2495 3119 28 44 24 C ATOM 2255 CG PHE A 294 19.699 21.335 31.048 1.00 22.00 C ANISOU 2255 CG PHE A 294 2672 2530 3157 37 14 27 C ATOM 2256 CD1 PHE A 294 20.208 20.222 31.678 1.00 25.79 C ANISOU 2256 CD1 PHE A 294 3146 3014 3640 65 12 38 C ATOM 2257 CD2 PHE A 294 19.853 22.579 31.651 1.00 27.44 C ANISOU 2257 CD2 PHE A 294 3327 3234 3863 18 -11 17 C ATOM 2258 CE1 PHE A 294 20.874 20.336 32.909 1.00 35.46 C ANISOU 2258 CE1 PHE A 294 4330 4267 4878 78 -18 40 C ATOM 2259 CE2 PHE A 294 20.526 22.700 32.864 1.00 28.34 C ANISOU 2259 CE2 PHE A 294 3401 3374 3994 26 -42 13 C ATOM 2260 CZ PHE A 294 21.043 21.572 33.484 1.00 26.67 C ANISOU 2260 CZ PHE A 294 3182 3174 3777 58 -47 25 C ATOM 2261 N ALA A 295 15.922 21.835 30.284 1.00 21.23 N ANISOU 2261 N ALA A 295 2677 2415 2976 -13 -2 1 N ATOM 2262 CA ALA A 295 14.976 22.515 31.148 1.00 21.63 C ANISOU 2262 CA ALA A 295 2730 2474 3015 -30 -34 -7 C ATOM 2263 C ALA A 295 13.899 21.579 31.689 1.00 21.19 C ANISOU 2263 C ALA A 295 2705 2413 2934 -28 -46 -12 C ATOM 2264 O ALA A 295 13.265 21.909 32.698 1.00 21.24 O ANISOU 2264 O ALA A 295 2709 2428 2932 -36 -73 -16 O ATOM 2265 CB ALA A 295 14.347 23.672 30.380 1.00 23.08 C ANISOU 2265 CB ALA A 295 2920 2657 3191 -49 -30 -10 C ATOM 2266 N LYS A 296 13.671 20.432 31.047 1.00 20.89 N ANISOU 2266 N LYS A 296 2692 2359 2884 -20 -22 -15 N ATOM 2267 CA LYS A 296 12.656 19.500 31.537 1.00 20.80 C ANISOU 2267 CA LYS A 296 2709 2338 2858 -21 -26 -21 C ATOM 2268 C LYS A 296 13.075 18.798 32.832 1.00 23.12 C ANISOU 2268 C LYS A 296 2991 2631 3162 0 -36 -6 C ATOM 2269 O LYS A 296 12.215 18.195 33.499 1.00 20.86 O ANISOU 2269 O LYS A 296 2724 2337 2866 0 -40 -5 O ATOM 2270 CB LYS A 296 12.298 18.494 30.421 1.00 20.92 C ANISOU 2270 CB LYS A 296 2752 2333 2863 -20 4 -36 C ATOM 2271 CG LYS A 296 11.674 19.216 29.177 1.00 20.84 C ANISOU 2271 CG LYS A 296 2754 2333 2830 -38 9 -51 C ATOM 2272 CD LYS A 296 11.280 18.235 28.029 1.00 21.02 C ANISOU 2272 CD LYS A 296 2804 2345 2837 -38 36 -74 C ATOM 2273 CE LYS A 296 11.213 18.950 26.638 1.00 21.08 C ANISOU 2273 CE LYS A 296 2816 2373 2820 -41 46 -82 C ATOM 2274 NZ LYS A 296 10.184 19.982 26.580 1.00 20.88 N ANISOU 2274 NZ LYS A 296 2792 2367 2772 -57 23 -84 N ATOM 2275 N THR A 297 14.341 18.943 33.261 1.00 21.11 N ANISOU 2275 N THR A 297 2704 2389 2927 19 -39 8 N ATOM 2276 CA THR A 297 14.717 18.474 34.598 1.00 21.25 C ANISOU 2276 CA THR A 297 2707 2420 2948 42 -55 25 C ATOM 2277 C THR A 297 13.951 19.209 35.688 1.00 21.07 C ANISOU 2277 C THR A 297 2681 2418 2908 31 -90 20 C ATOM 2278 O THR A 297 13.919 18.738 36.832 1.00 22.62 O ANISOU 2278 O THR A 297 2873 2626 3096 51 -103 34 O ATOM 2279 CB THR A 297 16.234 18.623 34.856 1.00 22.67 C ANISOU 2279 CB THR A 297 2845 2619 3150 65 -59 37 C ATOM 2280 OG1 THR A 297 16.628 20.000 34.751 1.00 23.75 O ANISOU 2280 OG1 THR A 297 2952 2775 3297 45 -77 24 O ATOM 2281 CG2 THR A 297 17.028 17.811 33.832 1.00 24.60 C ANISOU 2281 CG2 THR A 297 3093 2842 3411 80 -20 44 C ATOM 2282 N SER A 298 13.287 20.308 35.337 1.00 20.83 N ANISOU 2282 N SER A 298 2653 2391 2871 2 -103 3 N ATOM 2283 CA SER A 298 12.489 21.085 36.272 1.00 21.78 C ANISOU 2283 CA SER A 298 2771 2527 2976 -11 -133 -6 C ATOM 2284 C SER A 298 11.390 20.263 36.911 1.00 23.73 C ANISOU 2284 C SER A 298 3048 2766 3203 -7 -132 0 C ATOM 2285 O SER A 298 10.917 20.614 38.005 1.00 24.29 O ANISOU 2285 O SER A 298 3114 2855 3260 -6 -156 0 O ATOM 2286 CB SER A 298 11.876 22.286 35.544 1.00 20.44 C ANISOU 2286 CB SER A 298 2605 2355 2806 -41 -136 -22 C ATOM 2287 OG SER A 298 11.106 21.844 34.426 1.00 24.57 O ANISOU 2287 OG SER A 298 3159 2858 3319 -51 -114 -26 O ATOM 2288 N ALA A 299 10.985 19.171 36.270 1.00 20.87 N ANISOU 2288 N ALA A 299 2713 2377 2842 -4 -104 4 N ATOM 2289 CA ALA A 299 9.939 18.343 36.843 1.00 23.55 C ANISOU 2289 CA ALA A 299 3078 2702 3170 -3 -97 10 C ATOM 2290 C ALA A 299 10.427 17.470 37.989 1.00 26.40 C ANISOU 2290 C ALA A 299 3432 3066 3531 32 -94 37 C ATOM 2291 O ALA A 299 9.588 16.883 38.671 1.00 24.60 O ANISOU 2291 O ALA A 299 3223 2830 3296 36 -87 47 O ATOM 2292 CB ALA A 299 9.330 17.449 35.769 1.00 21.97 C ANISOU 2292 CB ALA A 299 2905 2468 2975 -14 -65 -3 C ATOM 2293 N AVAL A 300 11.749 17.364 38.199 0.54 23.10 N ANISOU 2293 N AVAL A 300 2989 2665 3124 58 -96 52 N ATOM 2294 N BVAL A 300 11.734 17.334 38.207 0.46 23.12 N ANISOU 2294 N BVAL A 300 2992 2666 3126 59 -95 52 N ATOM 2295 CA AVAL A 300 12.307 16.386 39.133 0.54 23.18 C ANISOU 2295 CA AVAL A 300 2994 2680 3134 99 -87 84 C ATOM 2296 CA BVAL A 300 12.219 16.398 39.216 0.46 23.20 C ANISOU 2296 CA BVAL A 300 2997 2683 3134 99 -88 84 C ATOM 2297 C AVAL A 300 13.127 17.018 40.260 0.54 24.59 C ANISOU 2297 C AVAL A 300 3136 2909 3300 122 -123 93 C ATOM 2298 C BVAL A 300 13.111 17.037 40.276 0.46 24.60 C ANISOU 2298 C BVAL A 300 3136 2910 3299 122 -124 92 C ATOM 2299 O AVAL A 300 13.176 16.482 41.372 0.54 26.74 O ANISOU 2299 O AVAL A 300 3406 3199 3556 155 -127 119 O ATOM 2300 O BVAL A 300 13.197 16.505 41.394 0.46 26.72 O ANISOU 2300 O BVAL A 300 3402 3198 3552 156 -128 119 O ATOM 2301 CB AVAL A 300 13.172 15.360 38.371 0.54 25.77 C ANISOU 2301 CB AVAL A 300 3324 2981 3486 119 -51 96 C ATOM 2302 CB BVAL A 300 12.951 15.208 38.557 0.46 25.66 C ANISOU 2302 CB BVAL A 300 3315 2964 3470 121 -50 100 C ATOM 2303 CG1AVAL A 300 13.782 14.332 39.316 0.54 31.52 C ANISOU 2303 CG1AVAL A 300 4046 3713 4217 168 -38 136 C ATOM 2304 CG1BVAL A 300 14.195 15.680 37.852 0.46 24.48 C ANISOU 2304 CG1BVAL A 300 3138 2828 3336 124 -53 92 C ATOM 2305 CG2AVAL A 300 12.356 14.681 37.267 0.54 26.55 C ANISOU 2305 CG2AVAL A 300 3457 3033 3597 96 -16 79 C ATOM 2306 CG2BVAL A 300 13.288 14.117 39.579 0.46 31.94 C ANISOU 2306 CG2BVAL A 300 4111 3760 4265 167 -34 140 C ATOM 2307 N TYR A 301 13.790 18.153 40.016 1.00 23.88 N ANISOU 2307 N TYR A 301 3014 2842 3215 107 -148 71 N ATOM 2308 CA TYR A 301 14.872 18.488 40.958 1.00 25.14 C ANISOU 2308 CA TYR A 301 3132 3050 3370 134 -177 76 C ATOM 2309 C TYR A 301 14.383 19.061 42.297 1.00 25.74 C ANISOU 2309 C TYR A 301 3200 3165 3414 138 -212 70 C ATOM 2310 O TYR A 301 15.090 18.923 43.296 1.00 27.88 O ANISOU 2310 O TYR A 301 3444 3480 3670 173 -233 82 O ATOM 2311 CB TYR A 301 15.924 19.419 40.320 1.00 25.02 C ANISOU 2311 CB TYR A 301 3079 3046 3380 118 -187 54 C ATOM 2312 CG TYR A 301 15.478 20.837 40.108 1.00 25.72 C ANISOU 2312 CG TYR A 301 3160 3139 3473 77 -207 20 C ATOM 2313 CD1 TYR A 301 15.446 21.741 41.166 1.00 21.70 C ANISOU 2313 CD1 TYR A 301 2627 2669 2951 73 -245 0 C ATOM 2314 CD2 TYR A 301 15.129 21.293 38.844 1.00 25.30 C ANISOU 2314 CD2 TYR A 301 3123 3053 3436 46 -187 8 C ATOM 2315 CE1 TYR A 301 15.034 23.016 41.004 1.00 24.58 C ANISOU 2315 CE1 TYR A 301 2984 3031 3323 37 -258 -30 C ATOM 2316 CE2 TYR A 301 14.718 22.603 38.661 1.00 26.82 C ANISOU 2316 CE2 TYR A 301 3309 3247 3635 13 -200 -17 C ATOM 2317 CZ TYR A 301 14.670 23.456 39.743 1.00 25.82 C ANISOU 2317 CZ TYR A 301 3159 3152 3501 8 -234 -36 C ATOM 2318 OH TYR A 301 14.250 24.751 39.591 1.00 26.23 O ANISOU 2318 OH TYR A 301 3204 3199 3564 -24 -243 -61 O ATOM 2319 N ASN A 302 13.240 19.729 42.361 1.00 23.62 N ANISOU 2319 N ASN A 302 2951 2889 3134 108 -221 51 N ATOM 2320 CA ASN A 302 12.895 20.392 43.623 1.00 24.43 C ANISOU 2320 CA ASN A 302 3041 3033 3207 113 -255 41 C ATOM 2321 C ASN A 302 12.680 19.414 44.775 1.00 23.56 C ANISOU 2321 C ASN A 302 2943 2943 3066 156 -252 76 C ATOM 2322 O ASN A 302 13.195 19.679 45.878 1.00 24.33 O ANISOU 2322 O ASN A 302 3012 3094 3137 183 -283 75 O ATOM 2323 CB ASN A 302 11.671 21.305 43.428 1.00 25.18 C ANISOU 2323 CB ASN A 302 3156 3113 3298 73 -261 15 C ATOM 2324 CG ASN A 302 12.030 22.636 42.784 1.00 23.83 C ANISOU 2324 CG ASN A 302 2961 2941 3151 38 -274 -20 C ATOM 2325 OD1 ASN A 302 12.781 23.433 43.353 1.00 26.08 O ANISOU 2325 OD1 ASN A 302 3209 3261 3440 39 -302 -42 O ATOM 2326 ND2 ASN A 302 11.492 22.883 41.591 1.00 26.43 N ANISOU 2326 ND2 ASN A 302 3311 3232 3499 9 -254 -26 N ATOM 2327 N PRO A 303 11.960 18.300 44.612 1.00 25.57 N ANISOU 2327 N PRO A 303 3234 3160 3320 166 -216 106 N ATOM 2328 CA PRO A 303 11.872 17.324 45.713 1.00 22.26 C ANISOU 2328 CA PRO A 303 2824 2757 2875 213 -206 147 C ATOM 2329 C PRO A 303 13.194 16.717 46.099 1.00 27.48 C ANISOU 2329 C PRO A 303 3457 3449 3535 262 -209 175 C ATOM 2330 O PRO A 303 13.332 16.258 47.241 1.00 28.21 O ANISOU 2330 O PRO A 303 3544 3579 3596 308 -215 206 O ATOM 2331 CB PRO A 303 10.921 16.251 45.158 1.00 29.62 C ANISOU 2331 CB PRO A 303 3800 3628 3826 206 -158 168 C ATOM 2332 CG PRO A 303 10.155 16.940 44.080 1.00 29.28 C ANISOU 2332 CG PRO A 303 3771 3554 3802 151 -158 130 C ATOM 2333 CD PRO A 303 11.094 17.926 43.477 1.00 22.75 C ANISOU 2333 CD PRO A 303 2912 2746 2986 134 -183 100 C ATOM 2334 N VAL A 304 14.150 16.626 45.168 1.00 25.50 N ANISOU 2334 N VAL A 304 3190 3184 3316 258 -201 168 N ATOM 2335 CA VAL A 304 15.481 16.149 45.527 1.00 23.20 C ANISOU 2335 CA VAL A 304 2863 2926 3024 304 -206 192 C ATOM 2336 C VAL A 304 16.163 17.122 46.490 1.00 23.44 C ANISOU 2336 C VAL A 304 2848 3032 3028 316 -260 170 C ATOM 2337 O VAL A 304 16.680 16.708 47.531 1.00 27.33 O ANISOU 2337 O VAL A 304 3320 3574 3489 367 -274 197 O ATOM 2338 CB VAL A 304 16.337 15.932 44.269 1.00 30.22 C ANISOU 2338 CB VAL A 304 3743 3783 3956 293 -184 186 C ATOM 2339 CG1 VAL A 304 17.729 15.484 44.697 1.00 28.87 C ANISOU 2339 CG1 VAL A 304 3531 3652 3786 344 -192 211 C ATOM 2340 CG2 VAL A 304 15.716 14.904 43.362 1.00 33.52 C ANISOU 2340 CG2 VAL A 304 4205 4132 4399 285 -132 203 C ATOM 2341 N ILE A 305 16.180 18.422 46.152 1.00 23.19 N ANISOU 2341 N ILE A 305 2795 3008 3006 270 -288 119 N ATOM 2342 CA ILE A 305 16.663 19.449 47.091 1.00 23.43 C ANISOU 2342 CA ILE A 305 2782 3106 3015 273 -338 86 C ATOM 2343 C ILE A 305 15.959 19.320 48.441 1.00 23.77 C ANISOU 2343 C ILE A 305 2837 3190 3004 302 -355 99 C ATOM 2344 O ILE A 305 16.593 19.376 49.501 1.00 25.77 O ANISOU 2344 O ILE A 305 3057 3512 3223 340 -388 100 O ATOM 2345 CB ILE A 305 16.452 20.869 46.519 1.00 23.94 C ANISOU 2345 CB ILE A 305 2835 3158 3104 214 -355 31 C ATOM 2346 CG1 ILE A 305 17.271 21.125 45.247 1.00 27.90 C ANISOU 2346 CG1 ILE A 305 3317 3627 3656 189 -339 18 C ATOM 2347 CG2 ILE A 305 16.804 21.938 47.589 1.00 25.58 C ANISOU 2347 CG2 ILE A 305 2998 3430 3289 213 -405 -12 C ATOM 2348 CD1 ILE A 305 16.850 22.442 44.505 1.00 25.62 C ANISOU 2348 CD1 ILE A 305 3029 3310 3396 131 -341 -25 C ATOM 2349 N TYR A 306 14.638 19.142 48.413 1.00 24.17 N ANISOU 2349 N TYR A 306 2935 3203 3046 285 -333 109 N ATOM 2350 CA TYR A 306 13.842 19.044 49.643 1.00 24.98 C ANISOU 2350 CA TYR A 306 3054 3338 3099 310 -343 124 C ATOM 2351 C TYR A 306 14.374 17.961 50.560 1.00 27.61 C ANISOU 2351 C TYR A 306 3381 3711 3399 379 -337 176 C ATOM 2352 O TYR A 306 14.581 18.187 51.762 1.00 30.07 O ANISOU 2352 O TYR A 306 3672 4093 3662 415 -369 176 O ATOM 2353 CB TYR A 306 12.391 18.740 49.257 1.00 28.01 C ANISOU 2353 CB TYR A 306 3490 3662 3490 283 -307 135 C ATOM 2354 CG TYR A 306 11.278 18.992 50.275 1.00 25.66 C ANISOU 2354 CG TYR A 306 3212 3384 3152 287 -314 136 C ATOM 2355 CD1 TYR A 306 11.461 19.762 51.420 1.00 28.10 C ANISOU 2355 CD1 TYR A 306 3496 3764 3418 303 -356 113 C ATOM 2356 CD2 TYR A 306 9.999 18.476 50.031 1.00 28.53 C ANISOU 2356 CD2 TYR A 306 3620 3696 3523 272 -277 156 C ATOM 2357 CE1 TYR A 306 10.389 19.989 52.316 1.00 27.09 C ANISOU 2357 CE1 TYR A 306 3390 3652 3252 308 -358 114 C ATOM 2358 CE2 TYR A 306 8.946 18.700 50.890 1.00 27.31 C ANISOU 2358 CE2 TYR A 306 3485 3556 3337 274 -278 158 C ATOM 2359 CZ TYR A 306 9.134 19.454 52.021 1.00 30.24 C ANISOU 2359 CZ TYR A 306 3833 3995 3663 292 -317 139 C ATOM 2360 OH TYR A 306 8.038 19.646 52.838 1.00 32.73 O ANISOU 2360 OH TYR A 306 4169 4321 3945 295 -314 142 O ATOM 2361 N ILE A 307 14.610 16.769 50.007 1.00 26.90 N ANISOU 2361 N ILE A 307 3309 3578 3334 402 -294 222 N ATOM 2362 CA ILE A 307 15.047 15.647 50.836 1.00 26.04 C ANISOU 2362 CA ILE A 307 3199 3498 3198 473 -279 282 C ATOM 2363 C ILE A 307 16.426 15.924 51.428 1.00 32.95 C ANISOU 2363 C ILE A 307 4016 4452 4050 513 -322 276 C ATOM 2364 O ILE A 307 16.712 15.579 52.583 1.00 33.58 O ANISOU 2364 O ILE A 307 4082 4597 4080 572 -338 308 O ATOM 2365 CB ILE A 307 15.053 14.360 49.990 1.00 29.16 C ANISOU 2365 CB ILE A 307 3624 3821 3635 484 -220 327 C ATOM 2366 CG1 ILE A 307 13.617 13.912 49.680 1.00 41.67 C ANISOU 2366 CG1 ILE A 307 5262 5337 5235 455 -176 337 C ATOM 2367 CG2 ILE A 307 15.836 13.262 50.664 1.00 35.45 C ANISOU 2367 CG2 ILE A 307 4409 4645 4415 560 -203 389 C ATOM 2368 CD1 ILE A 307 13.546 12.937 48.514 1.00 41.10 C ANISOU 2368 CD1 ILE A 307 5216 5184 5216 442 -122 353 C ATOM 2369 N MET A 308 17.320 16.504 50.621 1.00 26.03 N ANISOU 2369 N MET A 308 3106 3574 3210 483 -340 238 N ATOM 2370 CA MET A 308 18.678 16.762 51.072 1.00 28.68 C ANISOU 2370 CA MET A 308 3380 3982 3534 516 -380 227 C ATOM 2371 C MET A 308 18.736 17.878 52.110 1.00 29.85 C ANISOU 2371 C MET A 308 3493 4211 3638 512 -439 178 C ATOM 2372 O MET A 308 19.640 17.894 52.953 1.00 33.74 O ANISOU 2372 O MET A 308 3939 4785 4097 558 -476 178 O ATOM 2373 CB MET A 308 19.555 17.106 49.869 1.00 29.30 C ANISOU 2373 CB MET A 308 3432 4031 3671 480 -377 197 C ATOM 2374 CG MET A 308 19.741 15.936 48.897 1.00 39.52 C ANISOU 2374 CG MET A 308 4753 5257 5005 493 -321 243 C ATOM 2375 SD MET A 308 20.729 16.394 47.457 1.00 66.04 S ANISOU 2375 SD MET A 308 8082 8582 8428 452 -313 208 S ATOM 2376 CE MET A 308 22.123 17.197 48.248 1.00 52.58 C ANISOU 2376 CE MET A 308 6294 6974 6710 473 -374 176 C ATOM 2377 N MET A 309 17.809 18.822 52.074 1.00 28.46 N ANISOU 2377 N MET A 309 3336 4018 3462 460 -449 134 N ATOM 2378 CA MET A 309 18.004 20.040 52.838 1.00 31.85 C ANISOU 2378 CA MET A 309 3725 4513 3865 445 -504 72 C ATOM 2379 C MET A 309 16.939 20.317 53.885 1.00 37.54 C ANISOU 2379 C MET A 309 4470 5263 4529 453 -516 68 C ATOM 2380 O MET A 309 17.005 21.372 54.530 1.00 35.11 O ANISOU 2380 O MET A 309 4132 5008 4199 437 -560 10 O ATOM 2381 CB MET A 309 18.114 21.236 51.885 1.00 29.68 C ANISOU 2381 CB MET A 309 3432 4200 3645 373 -513 9 C ATOM 2382 CG MET A 309 19.279 21.101 50.915 1.00 28.94 C ANISOU 2382 CG MET A 309 3306 4087 3604 365 -504 8 C ATOM 2383 SD MET A 309 19.643 22.663 50.082 1.00 30.90 S ANISOU 2383 SD MET A 309 3517 4311 3911 290 -520 -69 S ATOM 2384 CE MET A 309 20.445 23.557 51.423 1.00 27.86 C ANISOU 2384 CE MET A 309 3062 4031 3494 304 -586 -129 C ATOM 2385 N ASN A 310 15.968 19.425 54.083 1.00 30.14 N ANISOU 2385 N ASN A 310 3586 4293 3573 476 -477 123 N ATOM 2386 CA ASN A 310 14.974 19.608 55.144 1.00 31.14 C ANISOU 2386 CA ASN A 310 3737 4452 3644 491 -484 126 C ATOM 2387 C ASN A 310 14.925 18.348 56.002 1.00 31.70 C ANISOU 2387 C ASN A 310 3825 4551 3667 568 -461 202 C ATOM 2388 O ASN A 310 14.397 17.316 55.573 1.00 30.69 O ANISOU 2388 O ASN A 310 3740 4360 3561 578 -407 259 O ATOM 2389 CB ASN A 310 13.590 19.953 54.588 1.00 30.19 C ANISOU 2389 CB ASN A 310 3664 4258 3549 436 -455 114 C ATOM 2390 CG ASN A 310 12.641 20.455 55.690 1.00 40.60 C ANISOU 2390 CG ASN A 310 4998 5615 4813 443 -470 99 C ATOM 2391 OD1 ASN A 310 11.903 19.675 56.295 1.00 32.98 O ANISOU 2391 OD1 ASN A 310 4067 4649 3815 479 -441 151 O ATOM 2392 ND2 ASN A 310 12.695 21.755 55.976 1.00 35.37 N ANISOU 2392 ND2 ASN A 310 4308 4988 4144 410 -512 29 N ATOM 2393 N LYS A 311 15.478 18.444 57.213 1.00 31.45 N ANISOU 2393 N LYS A 311 3760 4618 3570 622 -500 202 N ATOM 2394 CA LYS A 311 15.590 17.287 58.095 1.00 37.91 C ANISOU 2394 CA LYS A 311 4590 5477 4338 706 -480 280 C ATOM 2395 C LYS A 311 14.221 16.715 58.442 1.00 32.13 C ANISOU 2395 C LYS A 311 3917 4701 3588 715 -431 328 C ATOM 2396 O LYS A 311 14.029 15.493 58.450 1.00 36.22 O ANISOU 2396 O LYS A 311 4467 5185 4112 758 -380 404 O ATOM 2397 CB LYS A 311 16.340 17.692 59.370 1.00 35.78 C ANISOU 2397 CB LYS A 311 4270 5332 3992 760 -538 260 C ATOM 2398 CG LYS A 311 16.528 16.587 60.368 1.00 43.86 C ANISOU 2398 CG LYS A 311 5300 6412 4953 855 -522 342 C ATOM 2399 CD LYS A 311 17.284 17.102 61.584 1.00 47.85 C ANISOU 2399 CD LYS A 311 5751 7052 5377 906 -588 312 C ATOM 2400 N GLN A 312 13.262 17.584 58.738 1.00 29.21 N ANISOU 2400 N GLN A 312 3564 4332 3202 676 -444 284 N ATOM 2401 CA GLN A 312 11.956 17.112 59.177 1.00 32.91 C ANISOU 2401 CA GLN A 312 4084 4768 3651 686 -400 327 C ATOM 2402 C GLN A 312 11.251 16.336 58.072 1.00 38.45 C ANISOU 2402 C GLN A 312 4830 5357 4423 651 -338 362 C ATOM 2403 O GLN A 312 10.705 15.255 58.317 1.00 33.55 O ANISOU 2403 O GLN A 312 4244 4703 3800 687 -285 430 O ATOM 2404 CB GLN A 312 11.117 18.296 59.635 1.00 34.58 C ANISOU 2404 CB GLN A 312 4300 5002 3837 647 -429 266 C ATOM 2405 CG GLN A 312 9.727 17.929 60.099 1.00 44.61 C ANISOU 2405 CG GLN A 312 5619 6241 5088 653 -385 304 C ATOM 2406 CD GLN A 312 8.904 19.148 60.478 1.00 51.87 C ANISOU 2406 CD GLN A 312 6542 7179 5988 612 -411 240 C ATOM 2407 OE1 GLN A 312 8.716 20.067 59.673 1.00 54.30 O ANISOU 2407 OE1 GLN A 312 6843 7446 6342 544 -427 179 O ATOM 2408 NE2 GLN A 312 8.411 19.162 61.712 1.00 50.76 N ANISOU 2408 NE2 GLN A 312 6411 7099 5777 657 -413 257 N ATOM 2409 N PHE A 313 11.281 16.858 56.839 1.00 30.02 N ANISOU 2409 N PHE A 313 3760 4230 3419 583 -341 314 N ATOM 2410 CA PHE A 313 10.647 16.153 55.733 1.00 28.89 C ANISOU 2410 CA PHE A 313 3653 3985 3338 548 -286 338 C ATOM 2411 C PHE A 313 11.345 14.829 55.455 1.00 34.20 C ANISOU 2411 C PHE A 313 4330 4632 4032 594 -247 400 C ATOM 2412 O PHE A 313 10.684 13.798 55.273 1.00 30.93 O ANISOU 2412 O PHE A 313 3953 4156 3642 604 -189 450 O ATOM 2413 CB PHE A 313 10.637 17.018 54.483 1.00 30.56 C ANISOU 2413 CB PHE A 313 3858 4151 3604 473 -301 275 C ATOM 2414 CG PHE A 313 10.065 16.312 53.286 1.00 33.92 C ANISOU 2414 CG PHE A 313 4317 4481 4089 438 -250 292 C ATOM 2415 CD1 PHE A 313 8.705 16.053 53.203 1.00 37.27 C ANISOU 2415 CD1 PHE A 313 4781 4854 4524 415 -214 303 C ATOM 2416 CD2 PHE A 313 10.889 15.859 52.275 1.00 32.82 C ANISOU 2416 CD2 PHE A 313 4168 4307 3995 432 -237 296 C ATOM 2417 CE1 PHE A 313 8.177 15.370 52.111 1.00 31.53 C ANISOU 2417 CE1 PHE A 313 4082 4045 3852 383 -169 312 C ATOM 2418 CE2 PHE A 313 10.366 15.173 51.183 1.00 35.42 C ANISOU 2418 CE2 PHE A 313 4529 4553 4375 402 -190 306 C ATOM 2419 CZ PHE A 313 9.007 14.940 51.103 1.00 35.19 C ANISOU 2419 CZ PHE A 313 4537 4477 4356 376 -158 312 C ATOM 2420 N ARG A 314 12.682 14.832 55.461 1.00 33.17 N ANISOU 2420 N ARG A 314 4158 4549 3897 624 -277 398 N ATOM 2421 CA ARG A 314 13.437 13.603 55.249 1.00 34.12 C ANISOU 2421 CA ARG A 314 4278 4650 4036 673 -241 459 C ATOM 2422 C ARG A 314 13.070 12.543 56.277 1.00 37.49 C ANISOU 2422 C ARG A 314 4728 5091 4424 746 -201 539 C ATOM 2423 O ARG A 314 12.892 11.367 55.933 1.00 35.29 O ANISOU 2423 O ARG A 314 4479 4748 4182 766 -140 595 O ATOM 2424 CB ARG A 314 14.937 13.898 55.303 1.00 33.07 C ANISOU 2424 CB ARG A 314 4089 4583 3893 700 -286 442 C ATOM 2425 CG ARG A 314 15.832 12.682 55.098 1.00 37.34 C ANISOU 2425 CG ARG A 314 4623 5111 4454 757 -252 505 C ATOM 2426 CD ARG A 314 17.283 13.119 54.801 1.00 41.95 C ANISOU 2426 CD ARG A 314 5148 5744 5046 763 -297 473 C ATOM 2427 NE ARG A 314 17.898 13.789 55.942 1.00 42.89 N ANISOU 2427 NE ARG A 314 5220 5977 5099 800 -359 453 N ATOM 2428 CZ ARG A 314 18.224 15.076 56.009 1.00 38.90 C ANISOU 2428 CZ ARG A 314 4675 5521 4585 760 -419 376 C ATOM 2429 NH1 ARG A 314 18.031 15.903 54.992 1.00 37.19 N ANISOU 2429 NH1 ARG A 314 4459 5250 4420 681 -424 315 N ATOM 2430 NH2 ARG A 314 18.767 15.545 57.127 1.00 41.71 N ANISOU 2430 NH2 ARG A 314 4986 5983 4876 800 -473 358 N ATOM 2431 N ASN A 315 12.984 12.936 57.549 1.00 36.33 N ANISOU 2431 N ASN A 315 4569 5029 4204 787 -233 544 N ATOM 2432 CA ASN A 315 12.638 11.983 58.594 1.00 34.24 C ANISOU 2432 CA ASN A 315 4328 4786 3896 862 -194 625 C ATOM 2433 C ASN A 315 11.227 11.437 58.405 1.00 38.43 C ANISOU 2433 C ASN A 315 4913 5229 4459 836 -130 653 C ATOM 2434 O ASN A 315 11.005 10.228 58.541 1.00 38.57 O ANISOU 2434 O ASN A 315 4958 5203 4494 878 -66 728 O ATOM 2435 CB ASN A 315 12.794 12.641 59.964 1.00 39.20 C ANISOU 2435 CB ASN A 315 4931 5530 4433 908 -246 615 C ATOM 2436 CG ASN A 315 14.245 12.839 60.337 1.00 46.55 C ANISOU 2436 CG ASN A 315 5804 6554 5327 955 -301 606 C ATOM 2437 OD1 ASN A 315 15.139 12.301 59.684 1.00 47.68 O ANISOU 2437 OD1 ASN A 315 5930 6675 5511 967 -291 624 O ATOM 2438 ND2 ASN A 315 14.493 13.594 61.404 1.00 55.52 N ANISOU 2438 ND2 ASN A 315 6909 7799 6386 984 -358 575 N ATOM 2439 N CYS A 316 10.260 12.309 58.092 1.00 32.78 N ANISOU 2439 N CYS A 316 4212 4487 3755 766 -143 595 N ATOM 2440 CA CYS A 316 8.900 11.842 57.823 1.00 36.50 C ANISOU 2440 CA CYS A 316 4729 4876 4263 734 -84 614 C ATOM 2441 C CYS A 316 8.866 10.910 56.624 1.00 41.88 C ANISOU 2441 C CYS A 316 5431 5456 5026 707 -30 631 C ATOM 2442 O CYS A 316 8.133 9.914 56.617 1.00 41.93 O ANISOU 2442 O CYS A 316 5470 5398 5062 717 36 680 O ATOM 2443 CB CYS A 316 7.954 13.014 57.561 1.00 37.46 C ANISOU 2443 CB CYS A 316 4857 4988 4388 662 -113 544 C ATOM 2444 SG CYS A 316 7.626 14.058 58.959 1.00 49.19 S ANISOU 2444 SG CYS A 316 6330 6573 5786 685 -162 520 S ATOM 2445 N MET A 317 9.626 11.237 55.582 1.00 35.73 N ANISOU 2445 N MET A 317 4630 4660 4284 670 -56 587 N ATOM 2446 CA MET A 317 9.642 10.384 54.402 1.00 36.23 C ANISOU 2446 CA MET A 317 4711 4633 4420 644 -7 596 C ATOM 2447 C MET A 317 10.194 9.004 54.732 1.00 43.77 C ANISOU 2447 C MET A 317 5675 5571 5387 715 46 676 C ATOM 2448 O MET A 317 9.611 7.988 54.337 1.00 39.82 O ANISOU 2448 O MET A 317 5206 4988 4937 710 114 709 O ATOM 2449 CB MET A 317 10.455 11.045 53.296 1.00 31.08 C ANISOU 2449 CB MET A 317 4032 3977 3798 599 -45 536 C ATOM 2450 CG MET A 317 10.432 10.256 51.997 1.00 50.15 C ANISOU 2450 CG MET A 317 6467 6302 6285 568 3 535 C ATOM 2451 SD MET A 317 11.878 10.641 51.022 1.00 64.78 S ANISOU 2451 SD MET A 317 8283 8170 8162 556 -32 499 S ATOM 2452 CE MET A 317 13.146 10.439 52.273 1.00 59.67 C ANISOU 2452 CE MET A 317 7597 7616 7459 645 -59 548 C ATOM 2453 N VAL A 318 11.298 8.948 55.492 1.00 37.78 N ANISOU 2453 N VAL A 318 4885 4890 4581 783 19 708 N ATOM 2454 CA VAL A 318 11.851 7.663 55.909 1.00 40.21 C ANISOU 2454 CA VAL A 318 5198 5189 4893 861 69 792 C ATOM 2455 C VAL A 318 10.844 6.911 56.765 1.00 50.69 C ANISOU 2455 C VAL A 318 6561 6491 6207 897 128 857 C ATOM 2456 O VAL A 318 10.674 5.694 56.630 1.00 44.97 O ANISOU 2456 O VAL A 318 5862 5696 5527 924 202 917 O ATOM 2457 CB VAL A 318 13.183 7.857 56.658 1.00 37.80 C ANISOU 2457 CB VAL A 318 4847 4987 4529 930 20 812 C ATOM 2458 CG1 VAL A 318 13.681 6.528 57.159 1.00 47.37 C ANISOU 2458 CG1 VAL A 318 6066 6192 5741 1018 76 907 C ATOM 2459 CG2 VAL A 318 14.235 8.493 55.755 1.00 49.82 C ANISOU 2459 CG2 VAL A 318 6330 6524 6075 895 -29 752 C ATOM 2460 N THR A 319 10.152 7.628 57.650 1.00 43.09 N ANISOU 2460 N THR A 319 5603 5584 5187 897 100 846 N ATOM 2461 CA THR A 319 9.169 6.999 58.527 1.00 46.26 C ANISOU 2461 CA THR A 319 6037 5968 5572 932 156 908 C ATOM 2462 C THR A 319 8.056 6.335 57.724 1.00 52.03 C ANISOU 2462 C THR A 319 6806 6579 6384 877 227 908 C ATOM 2463 O THR A 319 7.690 5.179 57.980 1.00 56.49 O ANISOU 2463 O THR A 319 7397 7087 6979 914 304 979 O ATOM 2464 CB THR A 319 8.603 8.048 59.487 1.00 45.11 C ANISOU 2464 CB THR A 319 5886 5903 5352 931 108 880 C ATOM 2465 OG1 THR A 319 9.556 8.290 60.527 1.00 49.57 O ANISOU 2465 OG1 THR A 319 6419 6581 5834 1006 62 904 O ATOM 2466 CG2 THR A 319 7.283 7.596 60.093 1.00 53.13 C ANISOU 2466 CG2 THR A 319 6940 6880 6366 938 168 924 C ATOM 2467 N THR A 320 7.514 7.050 56.738 1.00 47.35 N ANISOU 2467 N THR A 320 6215 5946 5829 789 203 829 N ATOM 2468 CA THR A 320 6.424 6.508 55.932 1.00 51.57 C ANISOU 2468 CA THR A 320 6781 6376 6438 731 261 816 C ATOM 2469 C THR A 320 6.893 5.372 55.035 1.00 56.61 C ANISOU 2469 C THR A 320 7428 6932 7150 733 316 838 C ATOM 2470 O THR A 320 6.227 4.335 54.933 1.00 58.12 O ANISOU 2470 O THR A 320 7646 7043 7395 734 393 875 O ATOM 2471 CB THR A 320 5.816 7.618 55.091 1.00 46.71 C ANISOU 2471 CB THR A 320 6161 5751 5837 643 215 726 C ATOM 2472 OG1 THR A 320 5.301 8.620 55.965 1.00 46.58 O ANISOU 2472 OG1 THR A 320 6139 5802 5757 643 172 708 O ATOM 2473 CG2 THR A 320 4.707 7.078 54.219 1.00 51.24 C ANISOU 2473 CG2 THR A 320 6761 6225 6484 583 269 707 C ATOM 2474 N LEU A 321 8.029 5.556 54.366 1.00 48.30 N ANISOU 2474 N LEU A 321 6351 5897 6103 732 281 812 N ATOM 2475 CA LEU A 321 8.501 4.574 53.402 1.00 51.45 C ANISOU 2475 CA LEU A 321 6757 6219 6572 728 330 821 C ATOM 2476 C LEU A 321 8.992 3.301 54.076 1.00 56.71 C ANISOU 2476 C LEU A 321 7431 6867 7247 812 394 914 C ATOM 2477 O LEU A 321 9.123 2.271 53.407 1.00 62.75 O ANISOU 2477 O LEU A 321 8211 7550 8081 812 456 932 O ATOM 2478 CB LEU A 321 9.612 5.192 52.556 1.00 49.71 C ANISOU 2478 CB LEU A 321 6506 6028 6352 708 274 770 C ATOM 2479 CG LEU A 321 9.637 4.862 51.068 1.00 52.70 C ANISOU 2479 CG LEU A 321 6894 6328 6803 650 298 723 C ATOM 2480 CD1 LEU A 321 8.284 5.173 50.452 1.00 56.35 C ANISOU 2480 CD1 LEU A 321 7378 6737 7295 573 307 669 C ATOM 2481 CD2 LEU A 321 10.729 5.641 50.367 1.00 60.37 C ANISOU 2481 CD2 LEU A 321 7832 7341 7763 634 239 675 C ATOM 2482 N CYS A 322 9.248 3.348 55.380 1.00 54.01 N ANISOU 2482 N CYS A 322 7081 6602 6837 886 382 974 N ATOM 2483 CA CYS A 322 9.773 2.208 56.123 1.00 64.40 C ANISOU 2483 CA CYS A 322 8403 7916 8151 978 440 1072 C ATOM 2484 C CYS A 322 8.856 1.847 57.287 1.00 64.54 C ANISOU 2484 C CYS A 322 8445 7938 8140 1020 485 1137 C ATOM 2485 O CYS A 322 9.312 1.666 58.415 1.00 72.26 O ANISOU 2485 O CYS A 322 9414 8987 9053 1106 484 1207 O ATOM 2486 CB CYS A 322 11.185 2.513 56.633 1.00 57.07 C ANISOU 2486 CB CYS A 322 7436 7089 7160 1046 384 1094 C ATOM 2487 SG CYS A 322 12.271 3.240 55.365 1.00 73.99 S ANISOU 2487 SG CYS A 322 9543 9244 9326 993 318 1009 S TER 2488 CYS A 322 ATOM 2489 N MET B 1 -14.378 22.545 70.875 1.00 36.59 N ANISOU 2489 N MET B 1 5010 5108 3784 600 223 403 N ATOM 2490 CA MET B 1 -14.710 23.379 69.725 1.00 35.27 C ANISOU 2490 CA MET B 1 4824 4885 3690 524 190 336 C ATOM 2491 C MET B 1 -13.884 24.657 69.794 1.00 35.23 C ANISOU 2491 C MET B 1 4805 4936 3645 516 115 252 C ATOM 2492 O MET B 1 -13.698 25.220 70.865 1.00 37.75 O ANISOU 2492 O MET B 1 5127 5331 3885 558 99 230 O ATOM 2493 CB MET B 1 -16.200 23.699 69.746 1.00 40.57 C ANISOU 2493 CB MET B 1 5498 5518 4398 497 234 333 C ATOM 2494 CG MET B 1 -16.827 24.082 68.428 1.00 52.59 C ANISOU 2494 CG MET B 1 7004 6965 6015 421 225 296 C ATOM 2495 SD MET B 1 -18.612 24.245 68.712 1.00 83.27 S ANISOU 2495 SD MET B 1 10890 10818 9933 406 286 309 S ATOM 2496 CE MET B 1 -18.627 25.444 70.034 1.00 49.92 C ANISOU 2496 CE MET B 1 6673 6680 5614 450 266 266 C ATOM 2497 N ASN B 2 -13.375 25.120 68.666 1.00 35.66 N ANISOU 2497 N ASN B 2 4841 4953 3754 463 70 204 N ATOM 2498 CA ASN B 2 -12.533 26.299 68.673 1.00 32.04 C ANISOU 2498 CA ASN B 2 4366 4540 3268 452 3 126 C ATOM 2499 C ASN B 2 -13.274 27.576 68.295 1.00 36.18 C ANISOU 2499 C ASN B 2 4880 5038 3829 403 -11 59 C ATOM 2500 O ASN B 2 -12.671 28.654 68.326 1.00 39.70 O ANISOU 2500 O ASN B 2 5310 5514 4259 391 -60 -11 O ATOM 2501 CB ASN B 2 -11.344 26.076 67.755 1.00 29.90 C ANISOU 2501 CB ASN B 2 4080 4252 3029 430 -38 115 C ATOM 2502 CG ASN B 2 -10.352 25.092 68.340 1.00 35.16 C ANISOU 2502 CG ASN B 2 4751 4966 3641 489 -38 165 C ATOM 2503 OD1 ASN B 2 -9.629 25.427 69.278 1.00 38.69 O ANISOU 2503 OD1 ASN B 2 5193 5497 4011 533 -70 144 O ATOM 2504 ND2 ASN B 2 -10.311 23.871 67.794 1.00 35.63 N ANISOU 2504 ND2 ASN B 2 4819 4977 3742 490 -3 230 N ATOM 2505 N GLY B 3 -14.560 27.485 67.961 1.00 32.22 N ANISOU 2505 N GLY B 3 4384 4482 3376 377 33 80 N ATOM 2506 CA GLY B 3 -15.365 28.634 67.603 1.00 27.74 C ANISOU 2506 CA GLY B 3 3806 3887 2845 337 27 26 C ATOM 2507 C GLY B 3 -16.573 28.698 68.512 1.00 31.07 C ANISOU 2507 C GLY B 3 4241 4323 3242 361 76 46 C ATOM 2508 O GLY B 3 -16.609 28.006 69.526 1.00 34.59 O ANISOU 2508 O GLY B 3 4704 4811 3630 413 107 92 O ATOM 2509 N THR B 4 -17.577 29.496 68.170 1.00 26.35 N ANISOU 2509 N THR B 4 3635 3690 2686 327 86 16 N ATOM 2510 CA THR B 4 -18.725 29.712 69.046 1.00 25.66 C ANISOU 2510 CA THR B 4 3557 3617 2576 349 131 26 C ATOM 2511 C THR B 4 -20.011 29.440 68.276 1.00 32.22 C ANISOU 2511 C THR B 4 4380 4379 3485 311 173 53 C ATOM 2512 O THR B 4 -20.336 30.174 67.343 1.00 28.56 O ANISOU 2512 O THR B 4 3899 3875 3079 266 153 16 O ATOM 2513 CB THR B 4 -18.711 31.134 69.592 1.00 29.34 C ANISOU 2513 CB THR B 4 4019 4121 3008 352 104 -49 C ATOM 2514 OG1 THR B 4 -17.491 31.339 70.326 1.00 28.89 O ANISOU 2514 OG1 THR B 4 3965 4135 2878 387 63 -80 O ATOM 2515 CG2 THR B 4 -19.927 31.385 70.519 1.00 29.35 C ANISOU 2515 CG2 THR B 4 4029 4138 2984 377 153 -39 C ATOM 2516 N GLU B 5 -20.761 28.410 68.672 1.00 29.47 N ANISOU 2516 N GLU B 5 4040 4017 3139 331 231 118 N ATOM 2517 CA GLU B 5 -21.997 28.082 67.967 1.00 29.18 C ANISOU 2517 CA GLU B 5 3990 3918 3179 294 272 142 C ATOM 2518 C GLU B 5 -23.181 28.733 68.663 1.00 33.19 C ANISOU 2518 C GLU B 5 4498 4437 3678 305 307 132 C ATOM 2519 O GLU B 5 -23.297 28.679 69.890 1.00 31.39 O ANISOU 2519 O GLU B 5 4286 4256 3384 353 335 150 O ATOM 2520 CB GLU B 5 -22.214 26.568 67.882 1.00 33.37 C ANISOU 2520 CB GLU B 5 4526 4415 3736 301 322 215 C ATOM 2521 CG GLU B 5 -23.481 26.202 67.092 1.00 34.21 C ANISOU 2521 CG GLU B 5 4612 4456 3928 256 361 231 C ATOM 2522 CD GLU B 5 -23.683 24.697 66.928 1.00 40.99 C ANISOU 2522 CD GLU B 5 5474 5274 4827 256 413 295 C ATOM 2523 OE1 GLU B 5 -22.770 23.933 67.294 1.00 40.14 O ANISOU 2523 OE1 GLU B 5 5384 5183 4684 288 416 331 O ATOM 2524 OE2 GLU B 5 -24.764 24.280 66.443 1.00 36.96 O ANISOU 2524 OE2 GLU B 5 4944 4714 4383 223 453 310 O ATOM 2525 N GLY B 6 -24.040 29.365 67.878 1.00 30.46 N ANISOU 2525 N GLY B 6 4130 4049 3394 262 305 105 N ATOM 2526 CA GLY B 6 -25.282 29.893 68.377 1.00 31.77 C ANISOU 2526 CA GLY B 6 4289 4215 3566 268 344 101 C ATOM 2527 C GLY B 6 -26.438 29.205 67.687 1.00 32.05 C ANISOU 2527 C GLY B 6 4303 4194 3679 235 386 138 C ATOM 2528 O GLY B 6 -26.248 28.262 66.900 1.00 30.69 O ANISOU 2528 O GLY B 6 4125 3986 3552 211 388 165 O ATOM 2529 N PRO B 7 -27.659 29.677 67.948 1.00 30.67 N ANISOU 2529 N PRO B 7 4116 4012 3525 233 421 134 N ATOM 2530 CA PRO B 7 -28.840 29.026 67.345 1.00 34.51 C ANISOU 2530 CA PRO B 7 4576 4449 4087 202 464 165 C ATOM 2531 C PRO B 7 -28.807 29.009 65.826 1.00 33.78 C ANISOU 2531 C PRO B 7 4456 4312 4065 148 426 144 C ATOM 2532 O PRO B 7 -29.226 28.017 65.211 1.00 31.56 O ANISOU 2532 O PRO B 7 4159 3994 3839 122 450 173 O ATOM 2533 CB PRO B 7 -30.016 29.871 67.867 1.00 32.66 C ANISOU 2533 CB PRO B 7 4330 4223 3856 211 494 151 C ATOM 2534 CG PRO B 7 -29.471 30.615 69.062 1.00 38.97 C ANISOU 2534 CG PRO B 7 5158 5080 4569 259 486 128 C ATOM 2535 CD PRO B 7 -28.020 30.835 68.787 1.00 39.78 C ANISOU 2535 CD PRO B 7 5276 5202 4637 259 424 98 C ATOM 2536 N ASN B 8 -28.294 30.081 65.204 1.00 29.68 N ANISOU 2536 N ASN B 8 3933 3799 3545 133 369 93 N ATOM 2537 CA ASN B 8 -28.284 30.227 63.750 1.00 28.69 C ANISOU 2537 CA ASN B 8 3783 3639 3480 87 331 72 C ATOM 2538 C ASN B 8 -26.967 30.817 63.242 1.00 26.61 C ANISOU 2538 C ASN B 8 3530 3385 3194 82 270 36 C ATOM 2539 O ASN B 8 -26.945 31.508 62.215 1.00 26.97 O ANISOU 2539 O ASN B 8 3559 3415 3276 54 235 6 O ATOM 2540 CB ASN B 8 -29.470 31.087 63.290 1.00 28.40 C ANISOU 2540 CB ASN B 8 3716 3589 3488 69 336 51 C ATOM 2541 CG ASN B 8 -29.587 32.380 64.071 1.00 34.26 C ANISOU 2541 CG ASN B 8 4467 4358 4192 96 333 19 C ATOM 2542 OD1 ASN B 8 -28.763 32.666 64.940 1.00 33.18 O ANISOU 2542 OD1 ASN B 8 4358 4254 3994 126 324 6 O ATOM 2543 ND2 ASN B 8 -30.591 33.185 63.745 1.00 33.50 N ANISOU 2543 ND2 ASN B 8 4346 4251 4133 86 341 2 N ATOM 2544 N PHE B 9 -25.854 30.549 63.931 1.00 26.63 N ANISOU 2544 N PHE B 9 3561 3418 3140 110 258 40 N ATOM 2545 CA PHE B 9 -24.566 31.066 63.483 1.00 24.59 C ANISOU 2545 CA PHE B 9 3309 3169 2864 104 202 6 C ATOM 2546 C PHE B 9 -23.455 30.202 64.061 1.00 27.60 C ANISOU 2546 C PHE B 9 3713 3576 3196 131 198 30 C ATOM 2547 O PHE B 9 -23.665 29.428 65.001 1.00 27.10 O ANISOU 2547 O PHE B 9 3666 3531 3102 162 238 70 O ATOM 2548 CB PHE B 9 -24.382 32.547 63.864 1.00 23.63 C ANISOU 2548 CB PHE B 9 3190 3071 2717 114 176 -47 C ATOM 2549 CG PHE B 9 -24.433 32.810 65.361 1.00 27.18 C ANISOU 2549 CG PHE B 9 3659 3567 3100 158 199 -52 C ATOM 2550 CD1 PHE B 9 -23.291 32.663 66.152 1.00 25.86 C ANISOU 2550 CD1 PHE B 9 3512 3445 2867 188 179 -60 C ATOM 2551 CD2 PHE B 9 -25.602 33.220 65.954 1.00 27.90 C ANISOU 2551 CD2 PHE B 9 3746 3662 3193 170 238 -51 C ATOM 2552 CE1 PHE B 9 -23.336 32.917 67.541 1.00 29.16 C ANISOU 2552 CE1 PHE B 9 3948 3915 3216 233 198 -68 C ATOM 2553 CE2 PHE B 9 -25.661 33.488 67.341 1.00 31.50 C ANISOU 2553 CE2 PHE B 9 4222 4165 3584 213 260 -58 C ATOM 2554 CZ PHE B 9 -24.523 33.329 68.126 1.00 29.90 C ANISOU 2554 CZ PHE B 9 4040 4011 3310 245 239 -67 C ATOM 2555 N TYR B 10 -22.274 30.319 63.454 1.00 26.20 N ANISOU 2555 N TYR B 10 3539 3400 3017 120 151 9 N ATOM 2556 CA TYR B 10 -21.060 29.686 63.962 1.00 28.17 C ANISOU 2556 CA TYR B 10 3807 3680 3217 147 137 24 C ATOM 2557 C TYR B 10 -19.917 30.673 63.736 1.00 26.87 C ANISOU 2557 C TYR B 10 3640 3535 3033 142 80 -30 C ATOM 2558 O TYR B 10 -19.427 30.821 62.609 1.00 24.93 O ANISOU 2558 O TYR B 10 3383 3262 2829 110 49 -46 O ATOM 2559 CB TYR B 10 -20.768 28.358 63.276 1.00 26.93 C ANISOU 2559 CB TYR B 10 3650 3490 3092 134 148 67 C ATOM 2560 CG TYR B 10 -19.549 27.714 63.873 1.00 27.30 C ANISOU 2560 CG TYR B 10 3714 3570 3086 170 138 87 C ATOM 2561 CD1 TYR B 10 -19.657 26.941 65.014 1.00 29.19 C ANISOU 2561 CD1 TYR B 10 3972 3838 3281 215 179 134 C ATOM 2562 CD2 TYR B 10 -18.281 27.921 63.333 1.00 26.01 C ANISOU 2562 CD2 TYR B 10 3549 3415 2918 162 88 62 C ATOM 2563 CE1 TYR B 10 -18.549 26.367 65.602 1.00 32.57 C ANISOU 2563 CE1 TYR B 10 4416 4304 3657 254 169 157 C ATOM 2564 CE2 TYR B 10 -17.145 27.343 63.929 1.00 29.29 C ANISOU 2564 CE2 TYR B 10 3978 3868 3283 198 77 81 C ATOM 2565 CZ TYR B 10 -17.308 26.570 65.071 1.00 30.66 C ANISOU 2565 CZ TYR B 10 4169 4072 3409 246 117 129 C ATOM 2566 OH TYR B 10 -16.233 25.978 65.682 1.00 29.53 O ANISOU 2566 OH TYR B 10 4038 3970 3213 289 108 154 O ATOM 2567 N VAL B 11 -19.495 31.339 64.803 1.00 25.33 N ANISOU 2567 N VAL B 11 3454 3390 2778 174 68 -59 N ATOM 2568 CA VAL B 11 -18.457 32.366 64.729 1.00 24.40 C ANISOU 2568 CA VAL B 11 3331 3293 2645 168 18 -118 C ATOM 2569 C VAL B 11 -17.102 31.682 64.868 1.00 26.15 C ANISOU 2569 C VAL B 11 3559 3545 2831 187 -9 -107 C ATOM 2570 O VAL B 11 -16.867 31.002 65.881 1.00 26.15 O ANISOU 2570 O VAL B 11 3574 3590 2772 230 6 -78 O ATOM 2571 CB VAL B 11 -18.635 33.437 65.812 1.00 27.18 C ANISOU 2571 CB VAL B 11 3688 3688 2952 192 17 -165 C ATOM 2572 CG1 VAL B 11 -17.471 34.435 65.773 1.00 31.01 C ANISOU 2572 CG1 VAL B 11 4163 4193 3424 184 -33 -232 C ATOM 2573 CG2 VAL B 11 -19.984 34.177 65.620 1.00 26.17 C ANISOU 2573 CG2 VAL B 11 3551 3527 2865 174 46 -176 C ATOM 2574 N PRO B 12 -16.183 31.866 63.929 1.00 27.30 N ANISOU 2574 N PRO B 12 3694 3672 3007 160 -47 -129 N ATOM 2575 CA PRO B 12 -14.854 31.233 64.025 1.00 26.77 C ANISOU 2575 CA PRO B 12 3629 3634 2909 177 -74 -119 C ATOM 2576 C PRO B 12 -13.930 31.969 64.992 1.00 26.54 C ANISOU 2576 C PRO B 12 3597 3669 2819 204 -108 -170 C ATOM 2577 O PRO B 12 -12.831 32.418 64.644 1.00 26.24 O ANISOU 2577 O PRO B 12 3545 3640 2786 192 -150 -208 O ATOM 2578 CB PRO B 12 -14.361 31.288 62.572 1.00 25.76 C ANISOU 2578 CB PRO B 12 3487 3457 2844 134 -98 -128 C ATOM 2579 CG PRO B 12 -15.005 32.498 62.011 1.00 28.12 C ANISOU 2579 CG PRO B 12 3773 3725 3185 102 -103 -169 C ATOM 2580 CD PRO B 12 -16.349 32.640 62.680 1.00 26.86 C ANISOU 2580 CD PRO B 12 3621 3567 3017 114 -64 -158 C ATOM 2581 N PHE B 13 -14.380 32.081 66.236 1.00 24.40 N ANISOU 2581 N PHE B 13 3337 3445 2489 242 -90 -171 N ATOM 2582 CA PHE B 13 -13.688 32.839 67.269 1.00 26.74 C ANISOU 2582 CA PHE B 13 3629 3808 2721 270 -120 -227 C ATOM 2583 C PHE B 13 -14.138 32.264 68.600 1.00 27.07 C ANISOU 2583 C PHE B 13 3690 3907 2687 325 -88 -192 C ATOM 2584 O PHE B 13 -15.340 32.060 68.796 1.00 28.71 O ANISOU 2584 O PHE B 13 3911 4093 2906 329 -41 -158 O ATOM 2585 CB PHE B 13 -14.042 34.335 67.172 1.00 26.49 C ANISOU 2585 CB PHE B 13 3587 3762 2718 240 -131 -300 C ATOM 2586 CG PHE B 13 -13.056 35.259 67.861 1.00 27.38 C ANISOU 2586 CG PHE B 13 3685 3930 2788 251 -174 -377 C ATOM 2587 CD1 PHE B 13 -13.243 35.637 69.178 1.00 29.72 C ANISOU 2587 CD1 PHE B 13 3989 4291 3014 289 -169 -408 C ATOM 2588 CD2 PHE B 13 -11.966 35.770 67.164 1.00 33.24 C ANISOU 2588 CD2 PHE B 13 4406 4659 3564 220 -216 -421 C ATOM 2589 CE1 PHE B 13 -12.338 36.498 69.818 1.00 37.93 C ANISOU 2589 CE1 PHE B 13 5012 5384 4014 296 -210 -489 C ATOM 2590 CE2 PHE B 13 -11.059 36.626 67.786 1.00 37.65 C ANISOU 2590 CE2 PHE B 13 4947 5267 4091 225 -254 -498 C ATOM 2591 CZ PHE B 13 -11.245 36.993 69.113 1.00 36.04 C ANISOU 2591 CZ PHE B 13 4748 5130 3815 262 -253 -536 C ATOM 2592 N SER B 14 -13.190 32.010 69.507 1.00 28.60 N ANISOU 2592 N SER B 14 3886 4176 2806 370 -111 -198 N ATOM 2593 CA SER B 14 -13.524 31.428 70.804 1.00 27.60 C ANISOU 2593 CA SER B 14 3777 4111 2597 432 -81 -159 C ATOM 2594 C SER B 14 -14.202 32.439 71.721 1.00 30.24 C ANISOU 2594 C SER B 14 4116 4482 2892 445 -72 -211 C ATOM 2595 O SER B 14 -13.832 33.615 71.758 1.00 29.53 O ANISOU 2595 O SER B 14 4011 4406 2804 424 -109 -294 O ATOM 2596 CB SER B 14 -12.259 30.901 71.492 1.00 29.74 C ANISOU 2596 CB SER B 14 4046 4462 2793 481 -113 -151 C ATOM 2597 OG SER B 14 -12.573 30.424 72.789 1.00 31.37 O ANISOU 2597 OG SER B 14 4271 4737 2913 546 -84 -114 O ATOM 2598 N ASN B 15 -15.179 31.973 72.505 1.00 31.55 N ANISOU 2598 N ASN B 15 4302 4662 3021 481 -20 -163 N ATOM 2599 CA ASN B 15 -15.814 32.835 73.487 1.00 29.02 C ANISOU 2599 CA ASN B 15 3988 4384 2653 502 -7 -208 C ATOM 2600 C ASN B 15 -15.249 32.626 74.899 1.00 28.75 C ANISOU 2600 C ASN B 15 3963 4457 2503 573 -16 -211 C ATOM 2601 O ASN B 15 -15.915 32.961 75.882 1.00 30.35 O ANISOU 2601 O ASN B 15 4179 4703 2652 606 11 -222 O ATOM 2602 CB ASN B 15 -17.336 32.648 73.497 1.00 31.17 C ANISOU 2602 CB ASN B 15 4274 4609 2960 497 57 -163 C ATOM 2603 CG ASN B 15 -18.064 33.860 74.081 1.00 33.50 C ANISOU 2603 CG ASN B 15 4568 4918 3240 496 66 -227 C ATOM 2604 OD1 ASN B 15 -17.554 34.978 74.047 1.00 30.11 O ANISOU 2604 OD1 ASN B 15 4126 4503 2814 476 24 -312 O ATOM 2605 ND2 ASN B 15 -19.258 33.645 74.608 1.00 32.53 N ANISOU 2605 ND2 ASN B 15 4461 4791 3109 517 124 -188 N ATOM 2606 N LYS B 16 -14.020 32.128 75.009 1.00 28.93 N ANISOU 2606 N LYS B 16 3979 4529 2486 597 -55 -204 N ATOM 2607 CA LYS B 16 -13.414 31.929 76.321 1.00 33.50 C ANISOU 2607 CA LYS B 16 4563 5219 2948 668 -70 -208 C ATOM 2608 C LYS B 16 -13.199 33.240 77.061 1.00 39.04 C ANISOU 2608 C LYS B 16 5252 5983 3599 671 -107 -315 C ATOM 2609 O LYS B 16 -13.073 33.225 78.289 1.00 39.19 O ANISOU 2609 O LYS B 16 5278 6098 3515 732 -108 -324 O ATOM 2610 CB LYS B 16 -12.084 31.178 76.185 1.00 37.70 C ANISOU 2610 CB LYS B 16 5083 5789 3454 692 -109 -182 C ATOM 2611 CG LYS B 16 -11.004 31.954 75.464 1.00 43.42 C ANISOU 2611 CG LYS B 16 5775 6505 4219 644 -176 -264 C ATOM 2612 CD LYS B 16 -9.770 31.109 75.175 1.00 48.04 C ANISOU 2612 CD LYS B 16 6348 7115 4792 663 -208 -228 C ATOM 2613 CE LYS B 16 -8.895 31.796 74.132 1.00 51.10 C ANISOU 2613 CE LYS B 16 6704 7462 5251 601 -261 -296 C ATOM 2614 NZ LYS B 16 -7.607 31.076 73.911 1.00 61.27 N ANISOU 2614 NZ LYS B 16 7975 8781 6524 621 -297 -271 N ATOM 2615 N THR B 17 -13.141 34.371 76.355 1.00 33.53 N ANISOU 2615 N THR B 17 4534 5235 2971 609 -136 -397 N ATOM 2616 CA THR B 17 -13.055 35.670 77.014 1.00 36.49 C ANISOU 2616 CA THR B 17 4897 5656 3313 605 -162 -504 C ATOM 2617 C THR B 17 -14.388 36.401 77.074 1.00 34.99 C ANISOU 2617 C THR B 17 4719 5417 3157 585 -117 -522 C ATOM 2618 O THR B 17 -14.444 37.511 77.606 1.00 35.34 O ANISOU 2618 O THR B 17 4756 5489 3181 580 -131 -612 O ATOM 2619 CB THR B 17 -12.015 36.554 76.317 1.00 39.75 C ANISOU 2619 CB THR B 17 5277 6050 3777 553 -222 -591 C ATOM 2620 OG1 THR B 17 -12.410 36.793 74.961 1.00 39.13 O ANISOU 2620 OG1 THR B 17 5193 5859 3815 488 -210 -579 O ATOM 2621 CG2 THR B 17 -10.656 35.858 76.326 1.00 45.74 C ANISOU 2621 CG2 THR B 17 6018 6864 4497 576 -269 -577 C ATOM 2622 N GLY B 18 -15.460 35.822 76.530 1.00 31.76 N ANISOU 2622 N GLY B 18 4328 4936 2804 572 -63 -444 N ATOM 2623 CA GLY B 18 -16.770 36.410 76.696 1.00 30.39 C ANISOU 2623 CA GLY B 18 4165 4726 2656 562 -16 -453 C ATOM 2624 C GLY B 18 -17.149 37.522 75.736 1.00 32.60 C ANISOU 2624 C GLY B 18 4429 4923 3035 496 -22 -510 C ATOM 2625 O GLY B 18 -18.194 38.150 75.944 1.00 32.22 O ANISOU 2625 O GLY B 18 4387 4851 3005 491 14 -527 O ATOM 2626 N VAL B 19 -16.353 37.786 74.690 1.00 31.17 N ANISOU 2626 N VAL B 19 4227 4698 2919 449 -63 -536 N ATOM 2627 CA VAL B 19 -16.614 38.948 73.832 1.00 30.20 C ANISOU 2627 CA VAL B 19 4089 4502 2885 392 -69 -594 C ATOM 2628 C VAL B 19 -17.507 38.643 72.630 1.00 35.48 C ANISOU 2628 C VAL B 19 4759 5077 3646 354 -37 -531 C ATOM 2629 O VAL B 19 -17.961 39.585 71.956 1.00 33.99 O ANISOU 2629 O VAL B 19 4559 4828 3529 314 -32 -566 O ATOM 2630 CB VAL B 19 -15.302 39.577 73.307 1.00 29.09 C ANISOU 2630 CB VAL B 19 3922 4359 2773 358 -127 -663 C ATOM 2631 CG1 VAL B 19 -14.401 40.042 74.480 1.00 34.95 C ANISOU 2631 CG1 VAL B 19 4656 5196 3429 390 -165 -743 C ATOM 2632 CG2 VAL B 19 -14.565 38.617 72.410 1.00 33.88 C ANISOU 2632 CG2 VAL B 19 4522 4942 3407 344 -149 -605 C ATOM 2633 N VAL B 20 -17.784 37.370 72.334 1.00 28.39 N ANISOU 2633 N VAL B 20 3871 4166 2750 365 -14 -441 N ATOM 2634 CA VAL B 20 -18.495 37.034 71.101 1.00 26.57 C ANISOU 2634 CA VAL B 20 3636 3852 2608 325 8 -390 C ATOM 2635 C VAL B 20 -19.957 37.457 71.179 1.00 33.47 C ANISOU 2635 C VAL B 20 4514 4691 3512 321 57 -381 C ATOM 2636 O VAL B 20 -20.660 37.205 72.175 1.00 31.06 O ANISOU 2636 O VAL B 20 4224 4423 3156 359 95 -360 O ATOM 2637 CB VAL B 20 -18.370 35.533 70.779 1.00 28.32 C ANISOU 2637 CB VAL B 20 3867 4068 2828 336 21 -304 C ATOM 2638 CG1 VAL B 20 -19.164 35.167 69.488 1.00 29.32 C ANISOU 2638 CG1 VAL B 20 3985 4110 3044 293 43 -258 C ATOM 2639 CG2 VAL B 20 -16.910 35.161 70.589 1.00 27.98 C ANISOU 2639 CG2 VAL B 20 3816 4052 2762 339 -28 -313 C ATOM 2640 N ARG B 21 -20.431 38.083 70.101 1.00 29.16 N ANISOU 2640 N ARG B 21 3953 4076 3050 276 58 -393 N ATOM 2641 CA ARG B 21 -21.823 38.472 69.949 1.00 30.22 C ANISOU 2641 CA ARG B 21 4085 4171 3228 268 101 -379 C ATOM 2642 C ARG B 21 -22.353 37.970 68.617 1.00 32.43 C ANISOU 2642 C ARG B 21 4352 4384 3586 231 110 -328 C ATOM 2643 O ARG B 21 -21.596 37.819 67.644 1.00 30.00 O ANISOU 2643 O ARG B 21 4034 4050 3313 203 76 -327 O ATOM 2644 CB ARG B 21 -21.991 39.994 70.034 1.00 37.33 C ANISOU 2644 CB ARG B 21 4976 5056 4152 255 96 -456 C ATOM 2645 CG ARG B 21 -21.562 40.559 71.384 1.00 41.43 C ANISOU 2645 CG ARG B 21 5506 5643 4593 290 89 -518 C ATOM 2646 CD ARG B 21 -22.395 41.755 71.770 1.00 53.59 C ANISOU 2646 CD ARG B 21 7043 7167 6150 291 117 -570 C ATOM 2647 NE ARG B 21 -21.781 43.005 71.342 1.00 63.57 N ANISOU 2647 NE ARG B 21 8293 8402 7459 260 88 -647 N ATOM 2648 CZ ARG B 21 -22.310 44.204 71.542 1.00 60.90 C ANISOU 2648 CZ ARG B 21 7950 8040 7149 255 108 -703 C ATOM 2649 NH1 ARG B 21 -23.481 44.351 72.141 1.00 61.77 N ANISOU 2649 NH1 ARG B 21 8068 8154 7247 279 155 -691 N ATOM 2650 NH2 ARG B 21 -21.652 45.281 71.124 1.00 61.69 N ANISOU 2650 NH2 ARG B 21 8036 8108 7295 226 85 -771 N ATOM 2651 N SER B 22 -23.663 37.724 68.585 1.00 29.70 N ANISOU 2651 N SER B 22 4003 4015 3267 233 155 -288 N ATOM 2652 CA SER B 22 -24.302 37.217 67.376 1.00 29.97 C ANISOU 2652 CA SER B 22 4021 3993 3372 200 165 -243 C ATOM 2653 C SER B 22 -24.067 38.169 66.206 1.00 26.94 C ANISOU 2653 C SER B 22 3619 3565 3051 162 134 -278 C ATOM 2654 O SER B 22 -24.189 39.387 66.366 1.00 27.13 O ANISOU 2654 O SER B 22 3639 3583 3086 161 132 -329 O ATOM 2655 CB SER B 22 -25.806 37.060 67.579 1.00 26.49 C ANISOU 2655 CB SER B 22 3574 3537 2954 206 218 -209 C ATOM 2656 OG SER B 22 -26.455 36.772 66.341 1.00 28.27 O ANISOU 2656 OG SER B 22 3777 3712 3253 172 222 -179 O ATOM 2657 N PRO B 23 -23.786 37.644 65.010 1.00 24.18 N ANISOU 2657 N PRO B 23 3258 3181 2746 133 114 -252 N ATOM 2658 CA PRO B 23 -23.650 38.508 63.831 1.00 24.95 C ANISOU 2658 CA PRO B 23 3338 3237 2904 101 90 -276 C ATOM 2659 C PRO B 23 -24.970 39.059 63.324 1.00 25.45 C ANISOU 2659 C PRO B 23 3383 3267 3019 92 117 -266 C ATOM 2660 O PRO B 23 -24.967 39.801 62.336 1.00 25.26 O ANISOU 2660 O PRO B 23 3344 3210 3045 71 102 -280 O ATOM 2661 CB PRO B 23 -22.991 37.586 62.786 1.00 27.41 C ANISOU 2661 CB PRO B 23 3645 3532 3237 78 64 -244 C ATOM 2662 CG PRO B 23 -23.421 36.185 63.181 1.00 28.63 C ANISOU 2662 CG PRO B 23 3808 3701 3370 91 92 -190 C ATOM 2663 CD PRO B 23 -23.536 36.220 64.717 1.00 24.69 C ANISOU 2663 CD PRO B 23 3327 3247 2806 130 115 -198 C ATOM 2664 N PHE B 24 -26.094 38.724 63.955 1.00 27.71 N ANISOU 2664 N PHE B 24 3668 3562 3297 108 158 -241 N ATOM 2665 CA PHE B 24 -27.371 39.368 63.672 1.00 27.77 C ANISOU 2665 CA PHE B 24 3656 3546 3349 106 186 -238 C ATOM 2666 C PHE B 24 -27.718 40.429 64.700 1.00 33.28 C ANISOU 2666 C PHE B 24 4362 4258 4025 131 208 -278 C ATOM 2667 O PHE B 24 -28.771 41.061 64.585 1.00 31.25 O ANISOU 2667 O PHE B 24 4089 3982 3802 134 234 -278 O ATOM 2668 CB PHE B 24 -28.487 38.314 63.614 1.00 31.54 C ANISOU 2668 CB PHE B 24 4122 4020 3843 105 221 -184 C ATOM 2669 CG PHE B 24 -28.245 37.261 62.570 1.00 34.57 C ANISOU 2669 CG PHE B 24 4495 4387 4254 78 202 -150 C ATOM 2670 CD1 PHE B 24 -28.108 37.621 61.235 1.00 28.88 C ANISOU 2670 CD1 PHE B 24 3756 3638 3581 51 172 -155 C ATOM 2671 CD2 PHE B 24 -28.125 35.924 62.920 1.00 30.52 C ANISOU 2671 CD2 PHE B 24 3991 3885 3719 81 218 -112 C ATOM 2672 CE1 PHE B 24 -27.868 36.660 60.252 1.00 28.40 C ANISOU 2672 CE1 PHE B 24 3685 3564 3542 26 155 -129 C ATOM 2673 CE2 PHE B 24 -27.884 34.949 61.935 1.00 30.58 C ANISOU 2673 CE2 PHE B 24 3989 3873 3756 55 203 -86 C ATOM 2674 CZ PHE B 24 -27.757 35.319 60.609 1.00 29.44 C ANISOU 2674 CZ PHE B 24 3826 3704 3656 27 170 -97 C ATOM 2675 N GLU B 25 -26.852 40.646 65.698 1.00 27.93 N ANISOU 2675 N GLU B 25 3707 3615 3289 150 197 -316 N ATOM 2676 CA GLU B 25 -27.145 41.572 66.785 1.00 28.74 C ANISOU 2676 CA GLU B 25 3819 3738 3362 176 220 -361 C ATOM 2677 C GLU B 25 -26.171 42.730 66.899 1.00 31.10 C ANISOU 2677 C GLU B 25 4122 4036 3659 171 191 -432 C ATOM 2678 O GLU B 25 -26.593 43.826 67.264 1.00 33.69 O ANISOU 2678 O GLU B 25 4448 4352 4000 179 210 -474 O ATOM 2679 CB GLU B 25 -27.182 40.817 68.125 1.00 31.14 C ANISOU 2679 CB GLU B 25 4144 4096 3590 211 242 -348 C ATOM 2680 CG GLU B 25 -28.254 39.737 68.136 1.00 35.93 C ANISOU 2680 CG GLU B 25 4745 4700 4205 217 283 -279 C ATOM 2681 CD GLU B 25 -28.380 39.032 69.483 1.00 44.73 C ANISOU 2681 CD GLU B 25 5882 5866 5246 258 316 -258 C ATOM 2682 OE1 GLU B 25 -27.608 39.362 70.414 1.00 44.30 O ANISOU 2682 OE1 GLU B 25 5848 5858 5127 283 302 -298 O ATOM 2683 OE2 GLU B 25 -29.254 38.144 69.591 1.00 44.73 O ANISOU 2683 OE2 GLU B 25 5878 5861 5255 264 356 -202 O ATOM 2684 N ALA B 26 -24.892 42.540 66.584 1.00 29.71 N ANISOU 2684 N ALA B 26 3950 3867 3471 157 148 -448 N ATOM 2685 CA ALA B 26 -23.948 43.607 66.881 1.00 33.38 C ANISOU 2685 CA ALA B 26 4416 4336 3930 152 124 -523 C ATOM 2686 C ALA B 26 -22.783 43.564 65.915 1.00 27.87 C ANISOU 2686 C ALA B 26 3711 3618 3261 123 81 -529 C ATOM 2687 O ALA B 26 -22.440 42.486 65.410 1.00 26.60 O ANISOU 2687 O ALA B 26 3551 3463 3093 116 64 -481 O ATOM 2688 CB ALA B 26 -23.416 43.488 68.322 1.00 35.75 C ANISOU 2688 CB ALA B 26 4735 4703 4146 184 120 -562 C ATOM 2689 N PRO B 27 -22.117 44.701 65.689 1.00 29.93 N ANISOU 2689 N PRO B 27 3963 3854 3554 107 66 -588 N ATOM 2690 CA PRO B 27 -20.919 44.711 64.843 1.00 27.12 C ANISOU 2690 CA PRO B 27 3598 3482 3224 80 27 -598 C ATOM 2691 C PRO B 27 -19.865 43.752 65.369 1.00 30.07 C ANISOU 2691 C PRO B 27 3980 3909 3534 90 -6 -598 C ATOM 2692 O PRO B 27 -19.648 43.638 66.578 1.00 30.09 O ANISOU 2692 O PRO B 27 3994 3967 3470 116 -7 -628 O ATOM 2693 CB PRO B 27 -20.421 46.161 64.934 1.00 33.42 C ANISOU 2693 CB PRO B 27 4387 4253 4058 68 25 -675 C ATOM 2694 CG PRO B 27 -21.582 46.950 65.354 1.00 35.81 C ANISOU 2694 CG PRO B 27 4692 4538 4378 82 67 -689 C ATOM 2695 CD PRO B 27 -22.462 46.049 66.177 1.00 33.15 C ANISOU 2695 CD PRO B 27 4369 4246 3983 112 88 -650 C ATOM 2696 N GLN B 28 -19.156 43.121 64.439 1.00 27.50 N ANISOU 2696 N GLN B 28 3650 3571 3228 70 -32 -566 N ATOM 2697 CA GLN B 28 -18.209 42.042 64.730 1.00 25.85 C ANISOU 2697 CA GLN B 28 3448 3407 2966 80 -60 -548 C ATOM 2698 C GLN B 28 -16.781 42.551 64.903 1.00 26.45 C ANISOU 2698 C GLN B 28 3514 3502 3033 70 -99 -610 C ATOM 2699 O GLN B 28 -15.826 41.903 64.481 1.00 26.34 O ANISOU 2699 O GLN B 28 3496 3498 3013 63 -128 -594 O ATOM 2700 CB GLN B 28 -18.301 41.000 63.614 1.00 26.33 C ANISOU 2700 CB GLN B 28 3508 3442 3056 65 -64 -479 C ATOM 2701 CG GLN B 28 -19.691 40.383 63.494 1.00 23.60 C ANISOU 2701 CG GLN B 28 3166 3082 2718 73 -27 -421 C ATOM 2702 CD GLN B 28 -20.028 39.495 64.707 1.00 26.58 C ANISOU 2702 CD GLN B 28 3561 3512 3028 108 -8 -397 C ATOM 2703 OE1 GLN B 28 -19.462 38.418 64.863 1.00 26.51 O ANISOU 2703 OE1 GLN B 28 3560 3528 2984 119 -18 -365 O ATOM 2704 NE2 GLN B 28 -20.938 39.955 65.560 1.00 25.92 N ANISOU 2704 NE2 GLN B 28 3482 3440 2925 129 24 -410 N ATOM 2705 N TYR B 29 -16.611 43.738 65.495 1.00 27.87 N ANISOU 2705 N TYR B 29 3687 3685 3217 69 -98 -685 N ATOM 2706 CA TYR B 29 -15.294 44.346 65.654 1.00 29.49 C ANISOU 2706 CA TYR B 29 3877 3905 3424 55 -133 -755 C ATOM 2707 C TYR B 29 -14.412 43.626 66.666 1.00 34.57 C ANISOU 2707 C TYR B 29 4523 4629 3983 81 -165 -772 C ATOM 2708 O TYR B 29 -13.219 43.937 66.749 1.00 31.93 O ANISOU 2708 O TYR B 29 4171 4315 3646 70 -199 -825 O ATOM 2709 CB TYR B 29 -15.430 45.812 66.080 1.00 31.27 C ANISOU 2709 CB TYR B 29 4093 4109 3679 45 -119 -836 C ATOM 2710 CG TYR B 29 -16.209 46.689 65.122 1.00 33.06 C ANISOU 2710 CG TYR B 29 4314 4255 3991 23 -86 -824 C ATOM 2711 CD1 TYR B 29 -16.015 46.620 63.741 1.00 36.31 C ANISOU 2711 CD1 TYR B 29 4717 4612 4466 -3 -89 -780 C ATOM 2712 CD2 TYR B 29 -17.107 47.602 65.612 1.00 34.26 C ANISOU 2712 CD2 TYR B 29 4470 4389 4159 31 -51 -857 C ATOM 2713 CE1 TYR B 29 -16.735 47.461 62.863 1.00 35.86 C ANISOU 2713 CE1 TYR B 29 4654 4486 4484 -17 -58 -766 C ATOM 2714 CE2 TYR B 29 -17.823 48.423 64.768 1.00 38.01 C ANISOU 2714 CE2 TYR B 29 4939 4792 4712 17 -19 -843 C ATOM 2715 CZ TYR B 29 -17.642 48.351 63.407 1.00 36.42 C ANISOU 2715 CZ TYR B 29 4728 4541 4570 -6 -23 -796 C ATOM 2716 OH TYR B 29 -18.392 49.202 62.637 1.00 34.98 O ANISOU 2716 OH TYR B 29 4539 4293 4458 -13 10 -780 O ATOM 2717 N TYR B 30 -14.955 42.687 67.442 1.00 31.79 N ANISOU 2717 N TYR B 30 4190 4326 3563 118 -152 -728 N ATOM 2718 CA TYR B 30 -14.093 41.897 68.314 1.00 35.36 C ANISOU 2718 CA TYR B 30 4645 4857 3933 150 -181 -731 C ATOM 2719 C TYR B 30 -13.209 40.932 67.536 1.00 28.36 C ANISOU 2719 C TYR B 30 3752 3967 3055 141 -207 -683 C ATOM 2720 O TYR B 30 -12.210 40.463 68.077 1.00 35.58 O ANISOU 2720 O TYR B 30 4661 4941 3915 161 -240 -695 O ATOM 2721 CB TYR B 30 -14.931 41.132 69.346 1.00 32.14 C ANISOU 2721 CB TYR B 30 4261 4500 3451 196 -153 -688 C ATOM 2722 CG TYR B 30 -15.875 40.147 68.728 1.00 27.50 C ANISOU 2722 CG TYR B 30 3688 3874 2887 197 -119 -595 C ATOM 2723 CD1 TYR B 30 -17.150 40.535 68.328 1.00 30.73 C ANISOU 2723 CD1 TYR B 30 4101 4230 3346 184 -80 -576 C ATOM 2724 CD2 TYR B 30 -15.499 38.827 68.539 1.00 27.80 C ANISOU 2724 CD2 TYR B 30 3733 3928 2901 212 -125 -528 C ATOM 2725 CE1 TYR B 30 -18.037 39.620 67.741 1.00 28.86 C ANISOU 2725 CE1 TYR B 30 3872 3960 3134 182 -50 -496 C ATOM 2726 CE2 TYR B 30 -16.373 37.907 67.949 1.00 27.87 C ANISOU 2726 CE2 TYR B 30 3752 3898 2939 208 -92 -449 C ATOM 2727 CZ TYR B 30 -17.643 38.316 67.562 1.00 27.01 C ANISOU 2727 CZ TYR B 30 3644 3740 2878 192 -56 -436 C ATOM 2728 OH TYR B 30 -18.501 37.404 66.972 1.00 33.67 O ANISOU 2728 OH TYR B 30 4493 4548 3753 186 -25 -364 O ATOM 2729 N LEU B 31 -13.539 40.600 66.287 1.00 31.05 N ANISOU 2729 N LEU B 31 4094 4244 3461 114 -195 -628 N ATOM 2730 CA LEU B 31 -12.733 39.630 65.559 1.00 32.12 C ANISOU 2730 CA LEU B 31 4226 4375 3603 107 -217 -583 C ATOM 2731 C LEU B 31 -11.957 40.217 64.382 1.00 31.55 C ANISOU 2731 C LEU B 31 4133 4252 3602 66 -238 -606 C ATOM 2732 O LEU B 31 -11.268 39.462 63.683 1.00 28.37 O ANISOU 2732 O LEU B 31 3727 3843 3211 58 -254 -571 O ATOM 2733 CB LEU B 31 -13.608 38.458 65.084 1.00 34.35 C ANISOU 2733 CB LEU B 31 4526 4634 3892 115 -187 -495 C ATOM 2734 CG LEU B 31 -14.898 38.702 64.314 1.00 29.68 C ANISOU 2734 CG LEU B 31 3938 3980 3358 94 -152 -465 C ATOM 2735 CD1 LEU B 31 -14.611 39.212 62.903 1.00 27.86 C ANISOU 2735 CD1 LEU B 31 3692 3689 3204 53 -163 -470 C ATOM 2736 CD2 LEU B 31 -15.671 37.416 64.236 1.00 25.92 C ANISOU 2736 CD2 LEU B 31 3477 3502 2871 108 -124 -389 C ATOM 2737 N ALA B 32 -12.073 41.523 64.122 1.00 30.13 N ANISOU 2737 N ALA B 32 3940 4033 3473 40 -232 -661 N ATOM 2738 CA ALA B 32 -11.352 42.183 63.028 1.00 31.27 C ANISOU 2738 CA ALA B 32 4065 4127 3689 2 -245 -683 C ATOM 2739 C ALA B 32 -11.504 43.691 63.179 1.00 35.42 C ANISOU 2739 C ALA B 32 4578 4621 4258 -16 -233 -754 C ATOM 2740 O ALA B 32 -12.531 44.165 63.663 1.00 32.62 O ANISOU 2740 O ALA B 32 4234 4260 3900 -6 -205 -763 O ATOM 2741 CB ALA B 32 -11.873 41.758 61.659 1.00 27.70 C ANISOU 2741 CB ALA B 32 3619 3617 3291 -16 -228 -615 C ATOM 2742 N AGLU B 33 -10.483 44.435 62.738 0.54 33.91 N ANISOU 2742 N AGLU B 33 4364 4407 4114 -44 -250 -803 N ATOM 2743 N BGLU B 33 -10.489 44.428 62.719 0.46 33.91 N ANISOU 2743 N BGLU B 33 4363 4405 4114 -45 -250 -802 N ATOM 2744 CA AGLU B 33 -10.519 45.879 62.923 0.54 33.80 C ANISOU 2744 CA AGLU B 33 4335 4359 4147 -64 -235 -877 C ATOM 2745 CA BGLU B 33 -10.468 45.880 62.846 0.46 33.84 C ANISOU 2745 CA BGLU B 33 4340 4361 4156 -65 -236 -875 C ATOM 2746 C AGLU B 33 -11.478 46.541 61.933 0.54 31.21 C ANISOU 2746 C AGLU B 33 4013 3953 3893 -79 -196 -844 C ATOM 2747 C BGLU B 33 -11.508 46.525 61.928 0.46 31.20 C ANISOU 2747 C BGLU B 33 4012 3951 3891 -79 -195 -842 C ATOM 2748 O AGLU B 33 -11.710 46.015 60.839 0.54 29.77 O ANISOU 2748 O AGLU B 33 3836 3737 3737 -86 -189 -775 O ATOM 2749 O BGLU B 33 -11.838 45.972 60.874 0.46 29.89 O ANISOU 2749 O BGLU B 33 3853 3754 3749 -84 -187 -771 O ATOM 2750 CB AGLU B 33 -9.127 46.472 62.751 0.54 39.61 C ANISOU 2750 CB AGLU B 33 5042 5091 4919 -91 -261 -940 C ATOM 2751 CB BGLU B 33 -9.086 46.417 62.485 0.46 39.50 C ANISOU 2751 CB BGLU B 33 5027 5067 4916 -94 -260 -928 C ATOM 2752 CG AGLU B 33 -8.094 45.927 63.718 0.54 36.75 C ANISOU 2752 CG AGLU B 33 4666 4811 4485 -74 -305 -980 C ATOM 2753 CG BGLU B 33 -7.931 45.687 63.155 0.46 40.88 C ANISOU 2753 CG BGLU B 33 5188 5316 5027 -82 -306 -952 C ATOM 2754 CD AGLU B 33 -6.791 46.686 63.621 0.54 40.34 C ANISOU 2754 CD AGLU B 33 5085 5260 4983 -104 -328 -1057 C ATOM 2755 CD BGLU B 33 -7.388 46.434 64.349 0.46 41.60 C ANISOU 2755 CD BGLU B 33 5260 5456 5091 -80 -325 -1053 C ATOM 2756 OE1AGLU B 33 -6.834 47.934 63.692 0.54 46.44 O ANISOU 2756 OE1AGLU B 33 5843 5992 5811 -128 -310 -1124 O ATOM 2757 OE1BGLU B 33 -8.145 46.659 65.315 0.46 46.27 O ANISOU 2757 OE1BGLU B 33 5865 6077 5637 -57 -312 -1079 O ATOM 2758 OE2AGLU B 33 -5.732 46.043 63.461 0.54 44.71 O ANISOU 2758 OE2AGLU B 33 5622 5847 5520 -105 -362 -1050 O ATOM 2759 OE2BGLU B 33 -6.199 46.809 64.317 0.46 47.72 O ANISOU 2759 OE2BGLU B 33 6004 6240 5888 -101 -351 -1110 O ATOM 2760 N PRO B 34 -12.009 47.717 62.283 1.00 30.40 N ANISOU 2760 N PRO B 34 3907 3819 3823 -84 -168 -894 N ATOM 2761 CA PRO B 34 -12.984 48.379 61.392 1.00 31.61 C ANISOU 2761 CA PRO B 34 4064 3900 4044 -92 -127 -858 C ATOM 2762 C PRO B 34 -12.470 48.621 59.973 1.00 24.60 C ANISOU 2762 C PRO B 34 3164 2954 3228 -118 -124 -826 C ATOM 2763 O PRO B 34 -13.265 48.545 59.028 1.00 29.17 O ANISOU 2763 O PRO B 34 3751 3495 3838 -115 -102 -763 O ATOM 2764 CB PRO B 34 -13.282 49.692 62.133 1.00 31.24 C ANISOU 2764 CB PRO B 34 4012 3833 4024 -95 -102 -935 C ATOM 2765 CG PRO B 34 -13.018 49.356 63.588 1.00 40.29 C ANISOU 2765 CG PRO B 34 5162 5058 5087 -75 -125 -989 C ATOM 2766 CD PRO B 34 -11.819 48.474 63.543 1.00 35.58 C ANISOU 2766 CD PRO B 34 4557 4509 4454 -79 -171 -984 C ATOM 2767 N TRP B 35 -11.168 48.864 59.789 1.00 28.07 N ANISOU 2767 N TRP B 35 3584 3390 3690 -140 -146 -867 N ATOM 2768 CA TRP B 35 -10.627 49.096 58.448 1.00 30.60 C ANISOU 2768 CA TRP B 35 3892 3656 4078 -162 -139 -835 C ATOM 2769 C TRP B 35 -10.691 47.846 57.566 1.00 36.95 C ANISOU 2769 C TRP B 35 4709 4475 4858 -155 -155 -751 C ATOM 2770 O TRP B 35 -10.823 47.954 56.335 1.00 29.29 O ANISOU 2770 O TRP B 35 3737 3458 3933 -163 -139 -702 O ATOM 2771 CB TRP B 35 -9.196 49.629 58.548 1.00 29.95 C ANISOU 2771 CB TRP B 35 3784 3570 4028 -189 -157 -902 C ATOM 2772 CG TRP B 35 -8.151 48.624 59.032 1.00 30.78 C ANISOU 2772 CG TRP B 35 3880 3744 4071 -186 -205 -915 C ATOM 2773 CD1 TRP B 35 -7.665 48.505 60.304 1.00 37.61 C ANISOU 2773 CD1 TRP B 35 4736 4673 4879 -177 -234 -980 C ATOM 2774 CD2 TRP B 35 -7.462 47.641 58.247 1.00 30.39 C ANISOU 2774 CD2 TRP B 35 3830 3707 4012 -188 -228 -862 C ATOM 2775 NE1 TRP B 35 -6.728 47.501 60.359 1.00 39.81 N ANISOU 2775 NE1 TRP B 35 5009 5005 5114 -171 -274 -965 N ATOM 2776 CE2 TRP B 35 -6.585 46.955 59.113 1.00 38.24 C ANISOU 2776 CE2 TRP B 35 4813 4771 4944 -179 -270 -894 C ATOM 2777 CE3 TRP B 35 -7.489 47.285 56.899 1.00 33.03 C ANISOU 2777 CE3 TRP B 35 4169 4001 4381 -195 -217 -792 C ATOM 2778 CZ2 TRP B 35 -5.765 45.925 58.679 1.00 42.07 C ANISOU 2778 CZ2 TRP B 35 5295 5283 5406 -176 -297 -856 C ATOM 2779 CZ3 TRP B 35 -6.676 46.249 56.473 1.00 52.16 C ANISOU 2779 CZ3 TRP B 35 6589 6451 6778 -194 -246 -758 C ATOM 2780 CH2 TRP B 35 -5.823 45.588 57.356 1.00 47.94 C ANISOU 2780 CH2 TRP B 35 6045 5982 6188 -185 -284 -790 C ATOM 2781 N GLN B 36 -10.613 46.653 58.164 1.00 26.44 N ANISOU 2781 N GLN B 36 3388 3205 3452 -138 -183 -733 N ATOM 2782 CA GLN B 36 -10.818 45.425 57.400 1.00 26.06 C ANISOU 2782 CA GLN B 36 3353 3167 3382 -130 -192 -656 C ATOM 2783 C GLN B 36 -12.237 45.313 56.847 1.00 22.75 C ANISOU 2783 C GLN B 36 2947 2721 2974 -120 -164 -599 C ATOM 2784 O GLN B 36 -12.424 44.940 55.679 1.00 26.08 O ANISOU 2784 O GLN B 36 3371 3119 3420 -125 -159 -545 O ATOM 2785 CB GLN B 36 -10.503 44.213 58.275 1.00 30.25 C ANISOU 2785 CB GLN B 36 3893 3766 3836 -110 -220 -649 C ATOM 2786 CG GLN B 36 -9.106 44.243 58.860 1.00 35.36 C ANISOU 2786 CG GLN B 36 4522 4450 4464 -116 -253 -704 C ATOM 2787 CD GLN B 36 -8.847 43.031 59.728 1.00 38.53 C ANISOU 2787 CD GLN B 36 4933 4922 4785 -88 -279 -689 C ATOM 2788 OE1 GLN B 36 -8.597 43.161 60.908 1.00 40.46 O ANISOU 2788 OE1 GLN B 36 5173 5217 4982 -72 -293 -737 O ATOM 2789 NE2 GLN B 36 -8.920 41.842 59.134 1.00 50.37 N ANISOU 2789 NE2 GLN B 36 6445 6425 6269 -80 -282 -620 N ATOM 2790 N PHE B 37 -13.247 45.655 57.651 1.00 22.88 N ANISOU 2790 N PHE B 37 2973 2746 2974 -104 -144 -613 N ATOM 2791 CA PHE B 37 -14.604 45.632 57.131 1.00 26.27 C ANISOU 2791 CA PHE B 37 3410 3152 3420 -94 -116 -562 C ATOM 2792 C PHE B 37 -14.762 46.681 56.034 1.00 27.30 C ANISOU 2792 C PHE B 37 3529 3220 3623 -107 -93 -553 C ATOM 2793 O PHE B 37 -15.502 46.476 55.067 1.00 24.63 O ANISOU 2793 O PHE B 37 3192 2863 3304 -103 -81 -497 O ATOM 2794 CB PHE B 37 -15.615 45.873 58.241 1.00 22.97 C ANISOU 2794 CB PHE B 37 3001 2753 2972 -74 -96 -582 C ATOM 2795 CG PHE B 37 -15.717 44.752 59.252 1.00 23.01 C ANISOU 2795 CG PHE B 37 3020 2819 2902 -55 -110 -573 C ATOM 2796 CD1 PHE B 37 -14.956 44.778 60.403 1.00 25.89 C ANISOU 2796 CD1 PHE B 37 3386 3229 3222 -47 -128 -627 C ATOM 2797 CD2 PHE B 37 -16.605 43.707 59.062 1.00 25.84 C ANISOU 2797 CD2 PHE B 37 3389 3191 3239 -43 -102 -512 C ATOM 2798 CE1 PHE B 37 -15.069 43.762 61.365 1.00 24.35 C ANISOU 2798 CE1 PHE B 37 3204 3092 2954 -22 -137 -613 C ATOM 2799 CE2 PHE B 37 -16.715 42.678 60.007 1.00 26.41 C ANISOU 2799 CE2 PHE B 37 3474 3314 3246 -23 -107 -499 C ATOM 2800 CZ PHE B 37 -15.954 42.705 61.141 1.00 25.70 C ANISOU 2800 CZ PHE B 37 3388 3269 3107 -10 -123 -545 C ATOM 2801 N ASER B 38 -14.077 47.816 56.177 0.53 25.25 N ANISOU 2801 N ASER B 38 3257 2930 3405 -120 -84 -607 N ATOM 2802 N BSER B 38 -14.078 47.822 56.186 0.47 25.25 N ANISOU 2802 N BSER B 38 3258 2930 3406 -120 -84 -608 N ATOM 2803 CA ASER B 38 -14.192 48.876 55.185 0.53 25.44 C ANISOU 2803 CA ASER B 38 3271 2891 3503 -128 -55 -596 C ATOM 2804 CA BSER B 38 -14.150 48.887 55.189 0.47 25.45 C ANISOU 2804 CA BSER B 38 3272 2892 3505 -129 -55 -597 C ATOM 2805 C ASER B 38 -13.614 48.443 53.844 0.53 22.66 C ANISOU 2805 C ASER B 38 2914 2523 3172 -138 -65 -546 C ATOM 2806 C BSER B 38 -13.638 48.405 53.845 0.47 22.65 C ANISOU 2806 C BSER B 38 2913 2523 3169 -138 -66 -544 C ATOM 2807 O ASER B 38 -14.142 48.827 52.797 0.53 25.89 O ANISOU 2807 O ASER B 38 3321 2896 3621 -133 -43 -501 O ATOM 2808 O BSER B 38 -14.214 48.730 52.801 0.47 25.88 O ANISOU 2808 O BSER B 38 3320 2898 3614 -131 -44 -497 O ATOM 2809 CB ASER B 38 -13.510 50.146 55.710 0.53 25.82 C ANISOU 2809 CB ASER B 38 3306 2906 3597 -143 -39 -671 C ATOM 2810 CB BSER B 38 -13.338 50.101 55.650 0.47 25.90 C ANISOU 2810 CB BSER B 38 3315 2917 3608 -146 -43 -672 C ATOM 2811 OG ASER B 38 -13.962 51.285 55.004 0.53 24.71 O ANISOU 2811 OG ASER B 38 3159 2700 3528 -143 2 -659 O ATOM 2812 OG BSER B 38 -13.920 50.720 56.773 0.47 24.34 O ANISOU 2812 OG BSER B 38 3121 2726 3402 -136 -26 -723 O ATOM 2813 N MET B 39 -12.545 47.634 53.852 1.00 23.97 N ANISOU 2813 N MET B 39 3078 2718 3310 -150 -98 -552 N ATOM 2814 CA MET B 39 -12.039 47.056 52.605 1.00 23.25 C ANISOU 2814 CA MET B 39 2985 2619 3230 -157 -109 -503 C ATOM 2815 C MET B 39 -13.092 46.168 51.951 1.00 23.17 C ANISOU 2815 C MET B 39 2987 2624 3194 -142 -109 -437 C ATOM 2816 O MET B 39 -13.246 46.184 50.731 1.00 22.60 O ANISOU 2816 O MET B 39 2911 2529 3146 -141 -100 -392 O ATOM 2817 CB MET B 39 -10.754 46.251 52.849 1.00 22.11 C ANISOU 2817 CB MET B 39 2837 2509 3056 -168 -144 -522 C ATOM 2818 CG MET B 39 -9.632 47.085 53.438 1.00 41.44 C ANISOU 2818 CG MET B 39 5267 4948 5532 -186 -148 -592 C ATOM 2819 SD MET B 39 -8.105 46.127 53.567 1.00 49.78 S ANISOU 2819 SD MET B 39 6313 6046 6556 -196 -190 -606 S ATOM 2820 CE MET B 39 -7.709 45.932 51.834 1.00 40.97 C ANISOU 2820 CE MET B 39 5194 4891 5482 -206 -180 -545 C ATOM 2821 N LEU B 40 -13.834 45.390 52.742 1.00 24.00 N ANISOU 2821 N LEU B 40 3102 2767 3248 -129 -117 -431 N ATOM 2822 CA LEU B 40 -14.897 44.577 52.149 1.00 27.77 C ANISOU 2822 CA LEU B 40 3586 3257 3708 -118 -115 -375 C ATOM 2823 C LEU B 40 -15.977 45.450 51.500 1.00 21.50 C ANISOU 2823 C LEU B 40 2785 2430 2954 -108 -85 -350 C ATOM 2824 O LEU B 40 -16.404 45.191 50.369 1.00 24.50 O ANISOU 2824 O LEU B 40 3161 2804 3345 -104 -84 -304 O ATOM 2825 CB LEU B 40 -15.524 43.669 53.209 1.00 21.64 C ANISOU 2825 CB LEU B 40 2821 2522 2878 -107 -121 -375 C ATOM 2826 CG LEU B 40 -14.681 42.555 53.826 1.00 33.28 C ANISOU 2826 CG LEU B 40 4304 4036 4305 -108 -147 -382 C ATOM 2827 CD1 LEU B 40 -15.552 41.795 54.844 1.00 29.84 C ANISOU 2827 CD1 LEU B 40 3880 3635 3822 -91 -141 -373 C ATOM 2828 CD2 LEU B 40 -14.061 41.587 52.761 1.00 29.92 C ANISOU 2828 CD2 LEU B 40 3878 3612 3879 -118 -166 -345 C ATOM 2829 N ALA B 41 -16.439 46.489 52.208 1.00 21.77 N ANISOU 2829 N ALA B 41 2818 2446 3009 -100 -61 -382 N ATOM 2830 CA ALA B 41 -17.445 47.375 51.626 1.00 26.81 C ANISOU 2830 CA ALA B 41 3448 3051 3688 -86 -30 -357 C ATOM 2831 C ALA B 41 -16.939 48.041 50.337 1.00 21.90 C ANISOU 2831 C ALA B 41 2816 2389 3115 -89 -19 -332 C ATOM 2832 O ALA B 41 -17.682 48.141 49.350 1.00 23.17 O ANISOU 2832 O ALA B 41 2971 2542 3290 -74 -8 -282 O ATOM 2833 CB ALA B 41 -17.877 48.428 52.650 1.00 22.95 C ANISOU 2833 CB ALA B 41 2958 2543 3217 -78 -3 -401 C ATOM 2834 N ALA B 42 -15.690 48.512 50.324 1.00 22.33 N ANISOU 2834 N ALA B 42 2869 2421 3196 -106 -20 -364 N ATOM 2835 CA ALA B 42 -15.169 49.169 49.118 1.00 29.78 C ANISOU 2835 CA ALA B 42 3803 3323 4189 -107 -3 -337 C ATOM 2836 C ALA B 42 -15.106 48.198 47.939 1.00 30.47 C ANISOU 2836 C ALA B 42 3892 3434 4252 -104 -24 -282 C ATOM 2837 O ALA B 42 -15.461 48.543 46.797 1.00 26.60 O ANISOU 2837 O ALA B 42 3396 2928 3785 -90 -7 -234 O ATOM 2838 CB ALA B 42 -13.780 49.754 49.382 1.00 22.31 C ANISOU 2838 CB ALA B 42 2851 2349 3277 -130 -1 -386 C ATOM 2839 N TYR B 43 -14.581 47.001 48.185 1.00 23.73 N ANISOU 2839 N TYR B 43 3045 2619 3352 -117 -58 -288 N ATOM 2840 CA TYR B 43 -14.562 45.955 47.158 1.00 21.03 C ANISOU 2840 CA TYR B 43 2704 2302 2983 -116 -78 -243 C ATOM 2841 C TYR B 43 -15.966 45.652 46.631 1.00 23.52 C ANISOU 2841 C TYR B 43 3018 2635 3285 -97 -74 -201 C ATOM 2842 O TYR B 43 -16.166 45.493 45.413 1.00 23.38 O ANISOU 2842 O TYR B 43 2994 2620 3268 -88 -74 -159 O ATOM 2843 CB TYR B 43 -13.910 44.702 47.754 1.00 20.79 C ANISOU 2843 CB TYR B 43 2683 2309 2908 -130 -111 -261 C ATOM 2844 CG TYR B 43 -13.944 43.450 46.919 1.00 22.52 C ANISOU 2844 CG TYR B 43 2906 2555 3096 -131 -131 -224 C ATOM 2845 CD1 TYR B 43 -12.996 43.229 45.914 1.00 30.20 C ANISOU 2845 CD1 TYR B 43 3876 3520 4077 -138 -138 -208 C ATOM 2846 CD2 TYR B 43 -14.873 42.446 47.181 1.00 22.72 C ANISOU 2846 CD2 TYR B 43 2936 2612 3085 -127 -141 -209 C ATOM 2847 CE1 TYR B 43 -12.999 42.032 45.165 1.00 31.16 C ANISOU 2847 CE1 TYR B 43 4002 3667 4170 -140 -156 -180 C ATOM 2848 CE2 TYR B 43 -14.894 41.278 46.451 1.00 20.88 C ANISOU 2848 CE2 TYR B 43 2704 2400 2828 -131 -157 -182 C ATOM 2849 CZ TYR B 43 -13.949 41.070 45.450 1.00 27.73 C ANISOU 2849 CZ TYR B 43 3571 3261 3702 -137 -166 -170 C ATOM 2850 OH TYR B 43 -13.975 39.883 44.753 1.00 24.81 O ANISOU 2850 OH TYR B 43 3204 2912 3309 -142 -181 -149 O ATOM 2851 N MET B 44 -16.952 45.566 47.517 1.00 21.00 N ANISOU 2851 N MET B 44 2700 2331 2950 -90 -70 -212 N ATOM 2852 CA MET B 44 -18.300 45.248 47.047 1.00 21.43 C ANISOU 2852 CA MET B 44 2746 2405 2993 -74 -67 -174 C ATOM 2853 C MET B 44 -18.904 46.411 46.281 1.00 24.84 C ANISOU 2853 C MET B 44 3165 2809 3464 -51 -39 -146 C ATOM 2854 O MET B 44 -19.655 46.193 45.327 1.00 22.92 O ANISOU 2854 O MET B 44 2911 2584 3215 -36 -42 -106 O ATOM 2855 CB MET B 44 -19.235 44.869 48.209 1.00 23.01 C ANISOU 2855 CB MET B 44 2948 2626 3168 -70 -64 -191 C ATOM 2856 CG MET B 44 -18.922 43.554 48.888 1.00 20.79 C ANISOU 2856 CG MET B 44 2679 2377 2844 -84 -87 -204 C ATOM 2857 SD MET B 44 -18.757 42.173 47.741 1.00 24.08 S ANISOU 2857 SD MET B 44 3093 2818 3238 -95 -113 -169 S ATOM 2858 CE MET B 44 -20.345 42.176 46.870 1.00 20.90 C ANISOU 2858 CE MET B 44 2669 2430 2844 -80 -105 -132 C ATOM 2859 N PHE B 45 -18.591 47.648 46.681 1.00 25.01 N ANISOU 2859 N PHE B 45 3187 2788 3526 -48 -11 -168 N ATOM 2860 CA PHE B 45 -19.078 48.807 45.941 1.00 23.10 C ANISOU 2860 CA PHE B 45 2934 2513 3328 -23 22 -137 C ATOM 2861 C PHE B 45 -18.551 48.776 44.519 1.00 24.19 C ANISOU 2861 C PHE B 45 3068 2649 3473 -16 20 -94 C ATOM 2862 O PHE B 45 -19.291 49.043 43.564 1.00 24.68 O ANISOU 2862 O PHE B 45 3119 2718 3540 11 30 -46 O ATOM 2863 CB PHE B 45 -18.652 50.102 46.652 1.00 23.27 C ANISOU 2863 CB PHE B 45 2959 2483 3401 -25 56 -175 C ATOM 2864 CG PHE B 45 -19.245 51.355 46.065 1.00 24.15 C ANISOU 2864 CG PHE B 45 3060 2553 3564 4 99 -143 C ATOM 2865 CD1 PHE B 45 -20.615 51.498 45.941 1.00 29.53 C ANISOU 2865 CD1 PHE B 45 3732 3250 4240 33 110 -111 C ATOM 2866 CD2 PHE B 45 -18.430 52.404 45.706 1.00 25.88 C ANISOU 2866 CD2 PHE B 45 3278 2717 3839 3 132 -146 C ATOM 2867 CE1 PHE B 45 -21.166 52.671 45.419 1.00 31.87 C ANISOU 2867 CE1 PHE B 45 4018 3508 4584 65 152 -77 C ATOM 2868 CE2 PHE B 45 -18.965 53.591 45.215 1.00 26.65 C ANISOU 2868 CE2 PHE B 45 3367 2770 3988 33 178 -113 C ATOM 2869 CZ PHE B 45 -20.334 53.716 45.066 1.00 28.60 C ANISOU 2869 CZ PHE B 45 3604 3034 4226 66 188 -77 C ATOM 2870 N ALEU B 46 -17.273 48.444 44.351 0.68 25.21 N ANISOU 2870 N ALEU B 46 3206 2772 3602 -38 6 -110 N ATOM 2871 N BLEU B 46 -17.273 48.440 44.360 0.32 25.18 N ANISOU 2871 N BLEU B 46 3201 2768 3597 -38 6 -110 N ATOM 2872 CA ALEU B 46 -16.696 48.362 43.014 0.68 21.68 C ANISOU 2872 CA ALEU B 46 2755 2324 3157 -32 5 -70 C ATOM 2873 CA BLEU B 46 -16.673 48.347 43.036 0.32 21.83 C ANISOU 2873 CA BLEU B 46 2775 2344 3177 -33 5 -71 C ATOM 2874 C ALEU B 46 -17.378 47.289 42.176 0.68 26.37 C ANISOU 2874 C ALEU B 46 3345 2971 3704 -22 -23 -34 C ATOM 2875 C BLEU B 46 -17.373 47.291 42.187 0.32 26.29 C ANISOU 2875 C BLEU B 46 3335 2960 3694 -22 -23 -34 C ATOM 2876 O ALEU B 46 -17.675 47.508 40.989 0.68 23.10 O ANISOU 2876 O ALEU B 46 2923 2565 3290 2 -15 12 O ATOM 2877 O BLEU B 46 -17.685 47.527 41.010 0.32 23.22 O ANISOU 2877 O BLEU B 46 2938 2579 3306 2 -15 12 O ATOM 2878 CB ALEU B 46 -15.200 48.074 43.108 0.68 25.39 C ANISOU 2878 CB ALEU B 46 3232 2782 3632 -59 -6 -98 C ATOM 2879 CB BLEU B 46 -15.184 48.033 43.187 0.32 25.38 C ANISOU 2879 CB BLEU B 46 3232 2782 3630 -61 -8 -102 C ATOM 2880 CG ALEU B 46 -14.463 48.048 41.771 0.68 27.65 C ANISOU 2880 CG ALEU B 46 3517 3063 3925 -54 -2 -60 C ATOM 2881 CG BLEU B 46 -14.254 48.037 41.977 0.32 27.73 C ANISOU 2881 CG BLEU B 46 3528 3070 3938 -60 -3 -71 C ATOM 2882 CD1ALEU B 46 -14.358 49.464 41.189 0.68 28.24 C ANISOU 2882 CD1ALEU B 46 3585 3086 4059 -34 46 -33 C ATOM 2883 CD1BLEU B 46 -14.376 46.732 41.206 0.32 29.05 C ANISOU 2883 CD1BLEU B 46 3698 3287 4052 -59 -37 -46 C ATOM 2884 CD2ALEU B 46 -13.080 47.418 41.947 0.68 29.70 C ANISOU 2884 CD2ALEU B 46 3783 3325 4178 -82 -22 -90 C ATOM 2885 CD2BLEU B 46 -14.521 49.249 41.086 0.32 28.35 C ANISOU 2885 CD2BLEU B 46 3599 3112 4061 -31 39 -27 C ATOM 2886 N LEU B 47 -17.622 46.113 42.770 1.00 21.00 N ANISOU 2886 N LEU B 47 2670 2327 2983 -39 -53 -56 N ATOM 2887 CA LEU B 47 -18.246 45.024 42.016 1.00 24.63 C ANISOU 2887 CA LEU B 47 3123 2834 3403 -35 -79 -31 C ATOM 2888 C LEU B 47 -19.651 45.396 41.556 1.00 27.28 C ANISOU 2888 C LEU B 47 3440 3187 3738 -7 -70 1 C ATOM 2889 O LEU B 47 -20.078 45.004 40.461 1.00 25.69 O ANISOU 2889 O LEU B 47 3226 3020 3516 7 -83 32 O ATOM 2890 CB LEU B 47 -18.280 43.748 42.863 1.00 25.31 C ANISOU 2890 CB LEU B 47 3216 2946 3454 -59 -105 -60 C ATOM 2891 CG LEU B 47 -16.970 42.985 43.092 1.00 22.40 C ANISOU 2891 CG LEU B 47 2863 2577 3073 -84 -122 -83 C ATOM 2892 CD1 LEU B 47 -17.292 41.624 43.814 1.00 26.32 C ANISOU 2892 CD1 LEU B 47 3365 3104 3533 -99 -143 -99 C ATOM 2893 CD2 LEU B 47 -16.303 42.726 41.716 1.00 28.89 C ANISOU 2893 CD2 LEU B 47 3683 3404 3889 -82 -130 -56 C ATOM 2894 N ILE B 48 -20.407 46.093 42.406 1.00 23.88 N ANISOU 2894 N ILE B 48 3005 2741 3328 3 -50 -9 N ATOM 2895 CA ILE B 48 -21.731 46.568 42.010 1.00 24.71 C ANISOU 2895 CA ILE B 48 3090 2861 3439 34 -38 23 C ATOM 2896 C ILE B 48 -21.626 47.601 40.889 1.00 29.57 C ANISOU 2896 C ILE B 48 3698 3460 4080 66 -15 67 C ATOM 2897 O ILE B 48 -22.365 47.539 39.889 1.00 23.12 O ANISOU 2897 O ILE B 48 2862 2678 3246 94 -22 107 O ATOM 2898 CB ILE B 48 -22.474 47.136 43.238 1.00 27.37 C ANISOU 2898 CB ILE B 48 3425 3179 3795 38 -16 0 C ATOM 2899 CG1 ILE B 48 -22.843 46.009 44.216 1.00 25.23 C ANISOU 2899 CG1 ILE B 48 3158 2936 3493 14 -37 -31 C ATOM 2900 CG2 ILE B 48 -23.716 47.923 42.815 1.00 27.43 C ANISOU 2900 CG2 ILE B 48 3410 3191 3820 76 4 36 C ATOM 2901 CD1 ILE B 48 -23.212 46.522 45.635 1.00 29.36 C ANISOU 2901 CD1 ILE B 48 3688 3438 4030 13 -15 -64 C ATOM 2902 N MET B 49 -20.712 48.578 41.038 1.00 25.00 N ANISOU 2902 N MET B 49 3130 2826 3541 66 15 62 N ATOM 2903 CA MET B 49 -20.674 49.673 40.073 1.00 28.05 C ANISOU 2903 CA MET B 49 3510 3188 3959 101 48 109 C ATOM 2904 C MET B 49 -20.120 49.233 38.729 1.00 32.27 C ANISOU 2904 C MET B 49 4044 3749 4468 110 33 145 C ATOM 2905 O MET B 49 -20.439 49.845 37.706 1.00 29.52 O ANISOU 2905 O MET B 49 3686 3406 4126 148 52 197 O ATOM 2906 CB MET B 49 -19.857 50.851 40.633 1.00 31.06 C ANISOU 2906 CB MET B 49 3903 3499 4401 94 89 89 C ATOM 2907 CG MET B 49 -20.504 51.437 41.866 1.00 31.06 C ANISOU 2907 CG MET B 49 3901 3472 4426 93 109 55 C ATOM 2908 SD MET B 49 -22.041 52.298 41.502 1.00 41.78 S ANISOU 2908 SD MET B 49 5240 4833 5803 145 139 105 S ATOM 2909 CE MET B 49 -21.398 53.590 40.457 1.00 43.74 C ANISOU 2909 CE MET B 49 5488 5026 6106 175 189 155 C ATOM 2910 N LEU B 50 -19.267 48.209 38.707 1.00 27.93 N ANISOU 2910 N LEU B 50 3506 3217 3891 78 3 120 N ATOM 2911 CA LEU B 50 -18.848 47.630 37.433 1.00 28.83 C ANISOU 2911 CA LEU B 50 3618 3364 3972 86 -14 149 C ATOM 2912 C LEU B 50 -19.858 46.604 36.948 1.00 29.84 C ANISOU 2912 C LEU B 50 3731 3559 4048 92 -50 157 C ATOM 2913 O LEU B 50 -20.163 46.525 35.748 1.00 28.28 O ANISOU 2913 O LEU B 50 3521 3399 3824 120 -58 195 O ATOM 2914 CB LEU B 50 -17.491 46.936 37.581 1.00 27.83 C ANISOU 2914 CB LEU B 50 3508 3226 3839 50 -29 119 C ATOM 2915 CG LEU B 50 -16.299 47.854 37.813 1.00 41.08 C ANISOU 2915 CG LEU B 50 5196 4843 5567 40 4 110 C ATOM 2916 CD1 LEU B 50 -15.010 47.036 37.865 1.00 36.57 C ANISOU 2916 CD1 LEU B 50 4637 4273 4984 7 -16 82 C ATOM 2917 CD2 LEU B 50 -16.246 48.917 36.713 1.00 50.37 C ANISOU 2917 CD2 LEU B 50 6367 5998 6771 78 43 167 C ATOM 2918 N GLY B 51 -20.362 45.803 37.887 1.00 26.01 N ANISOU 2918 N GLY B 51 3244 3089 3548 66 -72 119 N ATOM 2919 CA GLY B 51 -21.203 44.664 37.540 1.00 23.40 C ANISOU 2919 CA GLY B 51 2898 2817 3175 62 -107 114 C ATOM 2920 C GLY B 51 -22.509 45.049 36.866 1.00 31.80 C ANISOU 2920 C GLY B 51 3933 3919 4229 99 -107 148 C ATOM 2921 O GLY B 51 -22.962 44.367 35.941 1.00 26.89 O ANISOU 2921 O GLY B 51 3294 3351 3571 108 -133 158 O ATOM 2922 N PHE B 52 -23.158 46.128 37.332 1.00 25.23 N ANISOU 2922 N PHE B 52 3093 3062 3429 124 -78 164 N ATOM 2923 CA PHE B 52 -24.432 46.497 36.712 1.00 29.46 C ANISOU 2923 CA PHE B 52 3599 3638 3956 164 -78 199 C ATOM 2924 C PHE B 52 -24.259 46.949 35.262 1.00 31.92 C ANISOU 2924 C PHE B 52 3902 3975 4251 205 -74 250 C ATOM 2925 O PHE B 52 -24.901 46.368 34.371 1.00 31.71 O ANISOU 2925 O PHE B 52 3852 4014 4183 221 -104 263 O ATOM 2926 CB PHE B 52 -25.162 47.533 37.574 1.00 27.77 C ANISOU 2926 CB PHE B 52 3379 3390 3783 182 -45 205 C ATOM 2927 CG PHE B 52 -26.207 48.301 36.824 1.00 33.05 C ANISOU 2927 CG PHE B 52 4019 4086 4453 236 -32 255 C ATOM 2928 CD1 PHE B 52 -27.296 47.648 36.266 1.00 34.78 C ANISOU 2928 CD1 PHE B 52 4203 4375 4636 249 -64 262 C ATOM 2929 CD2 PHE B 52 -26.085 49.673 36.638 1.00 41.61 C ANISOU 2929 CD2 PHE B 52 5107 5127 5577 274 12 295 C ATOM 2930 CE1 PHE B 52 -28.255 48.346 35.559 1.00 34.94 C ANISOU 2930 CE1 PHE B 52 4194 4429 4654 302 -56 310 C ATOM 2931 CE2 PHE B 52 -27.046 50.380 35.919 1.00 48.45 C ANISOU 2931 CE2 PHE B 52 5946 6021 6442 330 25 348 C ATOM 2932 CZ PHE B 52 -28.133 49.707 35.382 1.00 49.09 C ANISOU 2932 CZ PHE B 52 5992 6179 6481 345 -11 355 C ATOM 2933 N PRO B 53 -23.429 47.953 34.946 1.00 30.47 N ANISOU 2933 N PRO B 53 3735 3745 4096 224 -39 281 N ATOM 2934 CA PRO B 53 -23.326 48.371 33.538 1.00 27.12 C ANISOU 2934 CA PRO B 53 3303 3350 3652 270 -32 337 C ATOM 2935 C PRO B 53 -22.807 47.297 32.601 1.00 25.34 C ANISOU 2935 C PRO B 53 3080 3175 3374 258 -68 330 C ATOM 2936 O PRO B 53 -23.330 47.174 31.489 1.00 25.24 O ANISOU 2936 O PRO B 53 3046 3224 3319 294 -84 362 O ATOM 2937 CB PRO B 53 -22.373 49.575 33.574 1.00 35.11 C ANISOU 2937 CB PRO B 53 4335 4288 4715 282 20 363 C ATOM 2938 CG PRO B 53 -22.281 49.970 35.020 1.00 46.47 C ANISOU 2938 CG PRO B 53 5787 5666 6205 251 40 321 C ATOM 2939 CD PRO B 53 -22.575 48.753 35.831 1.00 31.87 C ANISOU 2939 CD PRO B 53 3936 3845 4327 207 -2 265 C ATOM 2940 N AILE B 54 -21.792 46.520 32.989 0.53 24.92 N ANISOU 2940 N AILE B 54 3049 3101 3319 211 -81 289 N ATOM 2941 N BILE B 54 -21.797 46.528 33.007 0.48 24.94 N ANISOU 2941 N BILE B 54 3052 3103 3323 210 -80 288 N ATOM 2942 CA AILE B 54 -21.254 45.573 32.019 0.53 28.18 C ANISOU 2942 CA AILE B 54 3464 3557 3685 204 -109 285 C ATOM 2943 CA BILE B 54 -21.224 45.535 32.106 0.48 28.16 C ANISOU 2943 CA BILE B 54 3463 3552 3684 200 -110 281 C ATOM 2944 C AILE B 54 -22.262 44.460 31.723 0.53 28.83 C ANISOU 2944 C AILE B 54 3521 3712 3721 196 -154 260 C ATOM 2945 C BILE B 54 -22.265 44.480 31.738 0.48 28.82 C ANISOU 2945 C BILE B 54 3520 3709 3720 196 -153 261 C ATOM 2946 O AILE B 54 -22.334 43.976 30.585 0.53 27.81 O ANISOU 2946 O AILE B 54 3381 3641 3546 214 -176 271 O ATOM 2947 O BILE B 54 -22.374 44.072 30.574 0.48 27.80 O ANISOU 2947 O BILE B 54 3378 3638 3545 217 -174 275 O ATOM 2948 CB AILE B 54 -19.884 45.016 32.456 0.53 29.97 C ANISOU 2948 CB AILE B 54 3719 3744 3923 159 -110 250 C ATOM 2949 CB BILE B 54 -19.965 44.914 32.735 0.48 29.75 C ANISOU 2949 CB BILE B 54 3692 3712 3899 151 -113 240 C ATOM 2950 CG1AILE B 54 -19.188 44.388 31.240 0.53 30.14 C ANISOU 2950 CG1AILE B 54 3746 3802 3904 165 -125 261 C ATOM 2951 CG1BILE B 54 -18.832 45.944 32.740 0.48 31.24 C ANISOU 2951 CG1BILE B 54 3900 3838 4131 158 -71 262 C ATOM 2952 CG2AILE B 54 -20.012 44.001 33.589 0.53 27.35 C ANISOU 2952 CG2AILE B 54 3392 3407 3592 111 -135 192 C ATOM 2953 CG2BILE B 54 -19.549 43.667 31.982 0.48 29.81 C ANISOU 2953 CG2BILE B 54 3702 3765 3860 134 -146 221 C ATOM 2954 CD1AILE B 54 -17.695 44.170 31.411 0.53 32.85 C ANISOU 2954 CD1AILE B 54 4115 4101 4264 135 -114 245 C ATOM 2955 CD1BILE B 54 -17.570 45.453 33.406 0.48 35.33 C ANISOU 2955 CD1BILE B 54 4440 4317 4666 112 -73 222 C ATOM 2956 N ASN B 55 -23.056 44.041 32.716 1.00 23.83 N ANISOU 2956 N ASN B 55 2877 3078 3099 171 -167 226 N ATOM 2957 CA ASN B 55 -24.076 43.025 32.450 1.00 23.67 C ANISOU 2957 CA ASN B 55 2827 3122 3044 162 -204 200 C ATOM 2958 C ASN B 55 -25.297 43.604 31.745 1.00 27.58 C ANISOU 2958 C ASN B 55 3286 3672 3522 212 -209 236 C ATOM 2959 O ASN B 55 -25.877 42.946 30.872 1.00 25.43 O ANISOU 2959 O ASN B 55 2986 3470 3206 221 -242 229 O ATOM 2960 CB ASN B 55 -24.472 42.323 33.747 1.00 24.87 C ANISOU 2960 CB ASN B 55 2979 3252 3216 118 -211 154 C ATOM 2961 CG ASN B 55 -23.418 41.364 34.196 1.00 25.36 C ANISOU 2961 CG ASN B 55 3070 3287 3278 73 -219 116 C ATOM 2962 OD1 ASN B 55 -23.238 40.301 33.591 1.00 23.00 O ANISOU 2962 OD1 ASN B 55 2768 3022 2950 55 -245 95 O ATOM 2963 ND2 ASN B 55 -22.685 41.728 35.248 1.00 24.18 N ANISOU 2963 ND2 ASN B 55 2948 3078 3161 55 -197 106 N ATOM 2964 N PHE B 56 -25.707 44.827 32.105 1.00 24.23 N ANISOU 2964 N PHE B 56 2858 3218 3131 245 -177 272 N ATOM 2965 CA PHE B 56 -26.835 45.437 31.399 1.00 26.44 C ANISOU 2965 CA PHE B 56 3101 3550 3394 299 -179 314 C ATOM 2966 C PHE B 56 -26.485 45.693 29.938 1.00 29.18 C ANISOU 2966 C PHE B 56 3444 3943 3698 344 -183 358 C ATOM 2967 O PHE B 56 -27.328 45.507 29.046 1.00 31.34 O ANISOU 2967 O PHE B 56 3682 4296 3928 378 -210 373 O ATOM 2968 CB PHE B 56 -27.254 46.738 32.083 1.00 31.13 C ANISOU 2968 CB PHE B 56 3696 4095 4037 328 -136 347 C ATOM 2969 CG PHE B 56 -28.443 47.418 31.424 1.00 33.28 C ANISOU 2969 CG PHE B 56 3928 4419 4296 389 -135 394 C ATOM 2970 CD1 PHE B 56 -29.738 47.016 31.706 1.00 40.24 C ANISOU 2970 CD1 PHE B 56 4771 5349 5170 389 -159 375 C ATOM 2971 CD2 PHE B 56 -28.244 48.443 30.523 1.00 36.16 C ANISOU 2971 CD2 PHE B 56 4295 4787 4658 449 -107 460 C ATOM 2972 CE1 PHE B 56 -30.834 47.644 31.085 1.00 39.67 C ANISOU 2972 CE1 PHE B 56 4658 5330 5084 448 -160 420 C ATOM 2973 CE2 PHE B 56 -29.322 49.070 29.894 1.00 36.28 C ANISOU 2973 CE2 PHE B 56 4272 4855 4657 512 -106 510 C ATOM 2974 CZ PHE B 56 -30.619 48.672 30.195 1.00 39.31 C ANISOU 2974 CZ PHE B 56 4615 5290 5031 511 -134 488 C ATOM 2975 N ALEU B 57 -25.251 46.130 29.672 0.44 25.62 N ANISOU 2975 N ALEU B 57 3027 3446 3259 347 -155 381 N ATOM 2976 N BLEU B 57 -25.251 46.135 29.672 0.56 25.58 N ANISOU 2976 N BLEU B 57 3023 3442 3255 347 -155 381 N ATOM 2977 CA ALEU B 57 -24.840 46.388 28.294 0.44 27.81 C ANISOU 2977 CA ALEU B 57 3305 3764 3496 392 -153 428 C ATOM 2978 CA BLEU B 57 -24.838 46.388 28.293 0.56 27.79 C ANISOU 2978 CA BLEU B 57 3303 3762 3494 392 -153 428 C ATOM 2979 C ALEU B 57 -24.819 45.101 27.474 0.44 29.61 C ANISOU 2979 C ALEU B 57 3522 4067 3661 375 -202 392 C ATOM 2980 C BLEU B 57 -24.820 45.100 27.474 0.56 29.62 C ANISOU 2980 C BLEU B 57 3523 4068 3662 375 -202 392 C ATOM 2981 O ALEU B 57 -25.196 45.099 26.296 0.44 28.52 O ANISOU 2981 O ALEU B 57 3362 4004 3470 420 -219 420 O ATOM 2982 O BLEU B 57 -25.198 45.097 26.297 0.56 28.51 O ANISOU 2982 O BLEU B 57 3361 4003 3469 420 -219 420 O ATOM 2983 CB ALEU B 57 -23.474 47.069 28.276 0.44 30.48 C ANISOU 2983 CB ALEU B 57 3681 4031 3868 392 -109 454 C ATOM 2984 CB BLEU B 57 -23.467 47.063 28.265 0.56 30.48 C ANISOU 2984 CB BLEU B 57 3682 4032 3868 392 -109 454 C ATOM 2985 CG ALEU B 57 -22.888 47.469 26.920 0.44 34.06 C ANISOU 2985 CG ALEU B 57 4142 4513 4288 440 -93 511 C ATOM 2986 CG BLEU B 57 -23.432 48.578 28.492 0.56 30.14 C ANISOU 2986 CG BLEU B 57 3646 3927 3878 431 -51 510 C ATOM 2987 CD1ALEU B 57 -23.829 48.374 26.140 0.44 34.92 C ANISOU 2987 CD1ALEU B 57 4223 4667 4377 516 -78 579 C ATOM 2988 CD1BLEU B 57 -22.006 49.096 28.537 0.56 36.65 C ANISOU 2988 CD1BLEU B 57 4505 4678 4743 419 -9 523 C ATOM 2989 CD2ALEU B 57 -21.535 48.136 27.118 0.44 35.01 C ANISOU 2989 CD2ALEU B 57 4297 4549 4458 430 -44 530 C ATOM 2990 CD2BLEU B 57 -24.213 49.296 27.417 0.56 36.22 C ANISOU 2990 CD2BLEU B 57 4391 4753 4619 507 -41 580 C ATOM 2991 N THR B 58 -24.375 43.997 28.079 1.00 27.01 N ANISOU 2991 N THR B 58 3207 3720 3338 313 -223 330 N ATOM 2992 CA THR B 58 -24.388 42.715 27.384 1.00 26.91 C ANISOU 2992 CA THR B 58 3182 3770 3272 292 -267 288 C ATOM 2993 C THR B 58 -25.813 42.312 27.012 1.00 28.41 C ANISOU 2993 C THR B 58 3323 4041 3429 307 -304 272 C ATOM 2994 O THR B 58 -26.081 41.920 25.865 1.00 29.37 O ANISOU 2994 O THR B 58 3422 4242 3494 332 -333 272 O ATOM 2995 CB THR B 58 -23.715 41.662 28.272 1.00 26.89 C ANISOU 2995 CB THR B 58 3202 3721 3292 224 -275 228 C ATOM 2996 OG1 THR B 58 -22.335 42.006 28.424 1.00 26.81 O ANISOU 2996 OG1 THR B 58 3232 3649 3306 214 -246 243 O ATOM 2997 CG2 THR B 58 -23.814 40.273 27.653 1.00 34.96 C ANISOU 2997 CG2 THR B 58 4212 4801 4272 197 -316 178 C ATOM 2998 N LEU B 59 -26.749 42.454 27.962 1.00 26.37 N ANISOU 2998 N LEU B 59 3046 3768 3206 295 -303 259 N ATOM 2999 CA LEU B 59 -28.159 42.175 27.702 1.00 29.77 C ANISOU 2999 CA LEU B 59 3425 4273 3614 310 -334 245 C ATOM 3000 C LEU B 59 -28.688 43.070 26.596 1.00 33.56 C ANISOU 3000 C LEU B 59 3878 4817 4055 384 -335 305 C ATOM 3001 O LEU B 59 -29.341 42.603 25.652 1.00 32.13 O ANISOU 3001 O LEU B 59 3659 4728 3822 405 -374 293 O ATOM 3002 CB LEU B 59 -28.970 42.375 28.997 1.00 28.34 C ANISOU 3002 CB LEU B 59 3232 4052 3485 289 -321 231 C ATOM 3003 CG LEU B 59 -30.484 42.126 29.134 1.00 38.67 C ANISOU 3003 CG LEU B 59 4485 5415 4791 294 -345 212 C ATOM 3004 CD1 LEU B 59 -30.882 42.053 30.638 1.00 34.17 C ANISOU 3004 CD1 LEU B 59 3921 4785 4278 255 -325 187 C ATOM 3005 CD2 LEU B 59 -31.308 43.221 28.459 1.00 45.18 C ANISOU 3005 CD2 LEU B 59 5277 6290 5599 366 -341 272 C ATOM 3006 N TYR B 60 -28.399 44.371 26.695 1.00 27.47 N ANISOU 3006 N TYR B 60 3126 4001 3312 427 -291 369 N ATOM 3007 CA TYR B 60 -28.945 45.327 25.743 1.00 29.55 C ANISOU 3007 CA TYR B 60 3366 4319 3545 506 -283 437 C ATOM 3008 C TYR B 60 -28.465 45.034 24.327 1.00 30.14 C ANISOU 3008 C TYR B 60 3440 4464 3550 538 -303 454 C ATOM 3009 O TYR B 60 -29.266 44.969 23.382 1.00 33.75 O ANISOU 3009 O TYR B 60 3856 5018 3950 583 -335 467 O ATOM 3010 CB TYR B 60 -28.553 46.742 26.161 1.00 29.07 C ANISOU 3010 CB TYR B 60 3331 4179 3536 540 -223 501 C ATOM 3011 CG TYR B 60 -29.255 47.793 25.317 1.00 32.55 C ANISOU 3011 CG TYR B 60 3744 4669 3954 626 -208 578 C ATOM 3012 CD1 TYR B 60 -30.477 48.288 25.698 1.00 39.56 C ANISOU 3012 CD1 TYR B 60 4595 5575 4860 654 -206 594 C ATOM 3013 CD2 TYR B 60 -28.674 48.274 24.157 1.00 42.50 C ANISOU 3013 CD2 TYR B 60 5016 5957 5176 681 -192 638 C ATOM 3014 CE1 TYR B 60 -31.132 49.253 24.933 1.00 52.80 C ANISOU 3014 CE1 TYR B 60 6246 7299 6516 738 -191 669 C ATOM 3015 CE2 TYR B 60 -29.308 49.240 23.381 1.00 41.25 C ANISOU 3015 CE2 TYR B 60 4833 5845 4994 766 -174 715 C ATOM 3016 CZ TYR B 60 -30.543 49.722 23.777 1.00 46.70 C ANISOU 3016 CZ TYR B 60 5486 6556 5703 795 -175 731 C ATOM 3017 OH TYR B 60 -31.192 50.674 23.016 1.00 49.30 O ANISOU 3017 OH TYR B 60 5788 6933 6009 884 -157 811 O ATOM 3018 N VAL B 61 -27.156 44.847 24.165 1.00 30.50 N ANISOU 3018 N VAL B 61 3528 4464 3597 516 -286 452 N ATOM 3019 CA VAL B 61 -26.596 44.596 22.843 1.00 31.47 C ANISOU 3019 CA VAL B 61 3655 4648 3654 547 -299 469 C ATOM 3020 C VAL B 61 -27.196 43.330 22.245 1.00 35.44 C ANISOU 3020 C VAL B 61 4124 5246 4097 527 -360 405 C ATOM 3021 O VAL B 61 -27.562 43.295 21.062 1.00 36.50 O ANISOU 3021 O VAL B 61 4231 5475 4161 577 -385 422 O ATOM 3022 CB VAL B 61 -25.061 44.512 22.922 1.00 29.92 C ANISOU 3022 CB VAL B 61 3511 4380 3478 517 -268 470 C ATOM 3023 CG1 VAL B 61 -24.484 44.059 21.584 1.00 34.56 C ANISOU 3023 CG1 VAL B 61 4102 5033 3994 542 -284 477 C ATOM 3024 CG2 VAL B 61 -24.475 45.868 23.347 1.00 34.37 C ANISOU 3024 CG2 VAL B 61 4103 4856 4101 543 -205 535 C ATOM 3025 N THR B 62 -27.305 42.271 23.047 1.00 31.30 N ANISOU 3025 N THR B 62 3597 4698 3598 455 -384 329 N ATOM 3026 CA THR B 62 -27.802 41.004 22.522 1.00 31.14 C ANISOU 3026 CA THR B 62 3544 4755 3531 428 -437 260 C ATOM 3027 C THR B 62 -29.238 41.132 22.028 1.00 37.40 C ANISOU 3027 C THR B 62 4276 5646 4289 468 -472 261 C ATOM 3028 O THR B 62 -29.573 40.647 20.945 1.00 36.78 O ANISOU 3028 O THR B 62 4166 5665 4143 490 -511 240 O ATOM 3029 CB THR B 62 -27.694 39.911 23.579 1.00 31.35 C ANISOU 3029 CB THR B 62 3580 4727 3604 345 -446 185 C ATOM 3030 OG1 THR B 62 -26.329 39.786 24.003 1.00 29.57 O ANISOU 3030 OG1 THR B 62 3409 4420 3407 313 -417 185 O ATOM 3031 CG2 THR B 62 -28.167 38.576 22.995 1.00 34.05 C ANISOU 3031 CG2 THR B 62 3888 5144 3905 314 -496 110 C ATOM 3032 N VAL B 63 -30.099 41.781 22.810 1.00 33.64 N ANISOU 3032 N VAL B 63 3779 5147 3856 478 -459 282 N ATOM 3033 CA VAL B 63 -31.496 41.920 22.405 1.00 40.05 C ANISOU 3033 CA VAL B 63 4527 6050 4638 517 -491 284 C ATOM 3034 C VAL B 63 -31.627 42.806 21.169 1.00 40.87 C ANISOU 3034 C VAL B 63 4616 6232 4679 607 -492 356 C ATOM 3035 O VAL B 63 -32.493 42.567 20.313 1.00 42.54 O ANISOU 3035 O VAL B 63 4776 6556 4832 642 -535 344 O ATOM 3036 CB VAL B 63 -32.339 42.441 23.585 1.00 41.06 C ANISOU 3036 CB VAL B 63 4640 6130 4832 508 -471 293 C ATOM 3037 CG1 VAL B 63 -33.734 42.757 23.143 1.00 44.50 C ANISOU 3037 CG1 VAL B 63 5010 6658 5241 557 -499 307 C ATOM 3038 CG2 VAL B 63 -32.373 41.389 24.701 1.00 42.61 C ANISOU 3038 CG2 VAL B 63 4842 6271 5078 422 -478 217 C ATOM 3039 N AGLN B 64 -30.776 43.824 21.040 0.62 40.35 N ANISOU 3039 N AGLN B 64 4594 6112 4624 648 -442 432 N ATOM 3040 N BGLN B 64 -30.763 43.811 21.038 0.38 40.36 N ANISOU 3040 N BGLN B 64 4596 6114 4626 647 -442 431 N ATOM 3041 CA AGLN B 64 -30.877 44.803 19.963 0.62 40.06 C ANISOU 3041 CA AGLN B 64 4548 6136 4536 741 -429 516 C ATOM 3042 CA BGLN B 64 -30.852 44.807 19.977 0.38 40.11 C ANISOU 3042 CA BGLN B 64 4555 6140 4543 740 -428 516 C ATOM 3043 C AGLN B 64 -30.369 44.283 18.618 0.62 44.16 C ANISOU 3043 C AGLN B 64 5068 6741 4969 766 -456 510 C ATOM 3044 C BGLN B 64 -30.300 44.320 18.637 0.38 44.15 C ANISOU 3044 C BGLN B 64 5070 6734 4970 766 -453 513 C ATOM 3045 O AGLN B 64 -30.656 44.901 17.585 0.62 46.74 O ANISOU 3045 O AGLN B 64 5376 7148 5234 848 -458 571 O ATOM 3046 O BGLN B 64 -30.489 45.003 17.624 0.38 46.63 O ANISOU 3046 O BGLN B 64 5370 7119 5227 849 -449 579 O ATOM 3047 CB AGLN B 64 -30.110 46.072 20.348 0.62 42.17 C ANISOU 3047 CB AGLN B 64 4862 6303 4857 771 -358 597 C ATOM 3048 CB BGLN B 64 -30.117 46.080 20.418 0.38 42.20 C ANISOU 3048 CB BGLN B 64 4866 6302 4865 768 -357 596 C ATOM 3049 CG AGLN B 64 -30.592 47.344 19.679 0.62 47.41 C ANISOU 3049 CG AGLN B 64 5509 7006 5500 869 -330 695 C ATOM 3050 CG BGLN B 64 -30.505 47.347 19.678 0.38 47.38 C ANISOU 3050 CG BGLN B 64 5508 6996 5496 868 -328 696 C ATOM 3051 CD AGLN B 64 -29.563 48.462 19.731 0.62 46.97 C ANISOU 3051 CD AGLN B 64 5504 6856 5486 899 -256 774 C ATOM 3052 CD BGLN B 64 -31.814 47.952 20.161 0.38 47.27 C ANISOU 3052 CD BGLN B 64 5450 7000 5510 900 -328 718 C ATOM 3053 OE1AGLN B 64 -28.385 48.221 19.984 0.62 53.12 O ANISOU 3053 OE1AGLN B 64 6328 7562 6292 853 -234 755 O ATOM 3054 OE1BGLN B 64 -32.615 47.296 20.829 0.38 49.59 O ANISOU 3054 OE1BGLN B 64 5713 7307 5822 853 -364 653 O ATOM 3055 NE2AGLN B 64 -30.006 49.689 19.497 0.62 53.23 N ANISOU 3055 NE2AGLN B 64 6286 7649 6290 977 -217 861 N ATOM 3056 NE2BGLN B 64 -32.034 49.215 19.822 0.38 49.94 N ANISOU 3056 NE2BGLN B 64 5787 7336 5853 981 -285 812 N ATOM 3057 N HIS B 65 -29.661 43.154 18.585 1.00 39.42 N ANISOU 3057 N HIS B 65 4489 6130 4359 703 -477 439 N ATOM 3058 CA HIS B 65 -29.022 42.655 17.361 1.00 40.86 C ANISOU 3058 CA HIS B 65 4680 6382 4464 724 -496 430 C ATOM 3059 C HIS B 65 -29.499 41.232 17.078 1.00 41.53 C ANISOU 3059 C HIS B 65 4729 6541 4511 673 -560 327 C ATOM 3060 O HIS B 65 -28.996 40.275 17.675 1.00 43.59 O ANISOU 3060 O HIS B 65 5010 6744 4808 596 -564 258 O ATOM 3061 CB HIS B 65 -27.493 42.685 17.471 1.00 44.82 C ANISOU 3061 CB HIS B 65 5246 6793 4990 698 -453 447 C ATOM 3062 CG HIS B 65 -26.906 44.063 17.585 1.00 49.61 C ANISOU 3062 CG HIS B 65 5887 7329 5633 748 -387 546 C ATOM 3063 ND1 HIS B 65 -26.451 44.773 16.492 1.00 56.90 N ANISOU 3063 ND1 HIS B 65 6822 8292 6505 823 -361 622 N ATOM 3064 CD2 HIS B 65 -26.664 44.845 18.666 1.00 44.26 C ANISOU 3064 CD2 HIS B 65 5234 6541 5040 731 -339 577 C ATOM 3065 CE1 HIS B 65 -25.973 45.939 16.893 1.00 55.21 C ANISOU 3065 CE1 HIS B 65 6639 7991 6350 850 -297 698 C ATOM 3066 NE2 HIS B 65 -26.091 46.008 18.208 1.00 47.70 N ANISOU 3066 NE2 HIS B 65 5695 6948 5481 793 -284 669 N ATOM 3067 N LYS B 66 -30.422 41.091 16.124 1.00 42.15 N ANISOU 3067 N LYS B 66 4752 6748 4514 720 -606 316 N ATOM 3068 CA LYS B 66 -31.010 39.790 15.800 1.00 45.70 C ANISOU 3068 CA LYS B 66 5158 7276 4929 675 -668 211 C ATOM 3069 C LYS B 66 -30.001 38.797 15.234 1.00 43.82 C ANISOU 3069 C LYS B 66 4951 7041 4657 637 -678 155 C ATOM 3070 O LYS B 66 -30.268 37.593 15.248 1.00 47.90 O ANISOU 3070 O LYS B 66 5444 7584 5172 578 -716 58 O ATOM 3071 CB LYS B 66 -32.169 39.966 14.816 1.00 51.77 C ANISOU 3071 CB LYS B 66 5859 8192 5619 741 -717 215 C ATOM 3072 N LYS B 67 -28.849 39.259 14.747 1.00 45.22 N ANISOU 3072 N LYS B 67 5180 7190 4812 670 -640 213 N ATOM 3073 CA LYS B 67 -27.807 38.341 14.301 1.00 39.80 C ANISOU 3073 CA LYS B 67 4527 6493 4100 633 -643 163 C ATOM 3074 C LYS B 67 -27.197 37.535 15.444 1.00 44.49 C ANISOU 3074 C LYS B 67 5154 6971 4778 538 -626 105 C ATOM 3075 O LYS B 67 -26.496 36.552 15.186 1.00 46.60 O ANISOU 3075 O LYS B 67 5442 7231 5034 496 -635 46 O ATOM 3076 CB LYS B 67 -26.692 39.113 13.601 1.00 47.37 C ANISOU 3076 CB LYS B 67 5534 7439 5025 690 -598 247 C ATOM 3077 CG LYS B 67 -25.856 39.957 14.555 1.00 51.08 C ANISOU 3077 CG LYS B 67 6056 7774 5580 679 -534 314 C ATOM 3078 CD LYS B 67 -24.891 40.864 13.799 1.00 54.41 C ANISOU 3078 CD LYS B 67 6515 8187 5971 744 -485 405 C ATOM 3079 N LEU B 68 -27.399 37.936 16.695 1.00 42.54 N ANISOU 3079 N LEU B 68 4917 6634 4615 508 -601 123 N ATOM 3080 CA LEU B 68 -26.723 37.269 17.815 1.00 42.20 C ANISOU 3080 CA LEU B 68 4908 6478 4646 428 -580 80 C ATOM 3081 C LEU B 68 -27.654 36.224 18.429 1.00 42.89 C ANISOU 3081 C LEU B 68 4956 6574 4765 365 -616 -8 C ATOM 3082 O LEU B 68 -28.197 36.387 19.525 1.00 36.63 O ANISOU 3082 O LEU B 68 4156 5727 4036 337 -605 -8 O ATOM 3083 CB LEU B 68 -26.270 38.292 18.850 1.00 36.22 C ANISOU 3083 CB LEU B 68 4188 5613 3960 430 -528 148 C ATOM 3084 CG LEU B 68 -25.260 39.348 18.398 1.00 41.06 C ANISOU 3084 CG LEU B 68 4842 6195 4562 483 -482 234 C ATOM 3085 CD1 LEU B 68 -25.144 40.445 19.464 1.00 37.16 C ANISOU 3085 CD1 LEU B 68 4370 5606 4143 487 -435 292 C ATOM 3086 CD2 LEU B 68 -23.899 38.718 18.133 1.00 45.14 C ANISOU 3086 CD2 LEU B 68 5404 6675 5074 453 -468 213 C ATOM 3087 N ARG B 69 -27.824 35.115 17.699 1.00 39.17 N ANISOU 3087 N ARG B 69 4461 6172 4251 341 -655 -85 N ATOM 3088 CA ARG B 69 -28.720 34.056 18.151 1.00 36.42 C ANISOU 3088 CA ARG B 69 4070 5837 3933 280 -687 -174 C ATOM 3089 C ARG B 69 -28.074 32.669 18.067 1.00 36.71 C ANISOU 3089 C ARG B 69 4123 5848 3977 216 -694 -258 C ATOM 3090 O ARG B 69 -28.776 31.667 17.919 1.00 40.82 O ANISOU 3090 O ARG B 69 4601 6411 4498 176 -727 -343 O ATOM 3091 CB ARG B 69 -30.031 34.099 17.365 1.00 41.57 C ANISOU 3091 CB ARG B 69 4651 6615 4531 317 -737 -199 C ATOM 3092 CG ARG B 69 -30.805 35.425 17.489 1.00 44.73 C ANISOU 3092 CG ARG B 69 5027 7041 4927 382 -730 -117 C ATOM 3093 CD ARG B 69 -31.322 35.669 18.924 1.00 45.80 C ANISOU 3093 CD ARG B 69 5161 7089 5152 345 -706 -107 C ATOM 3094 NE ARG B 69 -32.106 36.899 19.043 1.00 48.53 N ANISOU 3094 NE ARG B 69 5482 7459 5498 407 -698 -34 N ATOM 3095 CZ ARG B 69 -31.614 38.067 19.439 1.00 49.93 C ANISOU 3095 CZ ARG B 69 5700 7573 5700 446 -652 54 C ATOM 3096 NH1 ARG B 69 -30.341 38.201 19.783 1.00 39.55 N ANISOU 3096 NH1 ARG B 69 4449 6168 4411 428 -612 80 N ATOM 3097 NH2 ARG B 69 -32.416 39.127 19.489 1.00 41.56 N ANISOU 3097 NH2 ARG B 69 4612 6540 4640 504 -645 116 N ATOM 3098 N THR B 70 -26.749 32.577 18.198 1.00 34.33 N ANISOU 3098 N THR B 70 3880 5474 3689 203 -660 -238 N ATOM 3099 CA THR B 70 -26.111 31.273 18.349 1.00 34.55 C ANISOU 3099 CA THR B 70 3929 5459 3741 138 -658 -311 C ATOM 3100 C THR B 70 -26.244 30.766 19.787 1.00 37.34 C ANISOU 3100 C THR B 70 4290 5713 4183 73 -637 -335 C ATOM 3101 O THR B 70 -26.538 31.544 20.699 1.00 35.37 O ANISOU 3101 O THR B 70 4044 5417 3976 80 -617 -286 O ATOM 3102 CB THR B 70 -24.632 31.347 17.991 1.00 33.75 C ANISOU 3102 CB THR B 70 3885 5316 3622 150 -628 -279 C ATOM 3103 OG1 THR B 70 -23.918 32.051 19.010 1.00 36.08 O ANISOU 3103 OG1 THR B 70 4224 5510 3975 146 -584 -215 O ATOM 3104 CG2 THR B 70 -24.405 32.015 16.634 1.00 40.12 C ANISOU 3104 CG2 THR B 70 4690 6212 4341 223 -637 -237 C ATOM 3105 N PRO B 71 -26.000 29.467 20.023 1.00 37.29 N ANISOU 3105 N PRO B 71 4288 5673 4209 11 -637 -410 N ATOM 3106 CA PRO B 71 -26.020 28.972 21.410 1.00 34.94 C ANISOU 3106 CA PRO B 71 4004 5278 3993 -46 -610 -424 C ATOM 3107 C PRO B 71 -25.110 29.746 22.344 1.00 34.22 C ANISOU 3107 C PRO B 71 3966 5097 3939 -37 -569 -351 C ATOM 3108 O PRO B 71 -25.504 30.017 23.482 1.00 31.15 O ANISOU 3108 O PRO B 71 3577 4656 3603 -54 -552 -332 O ATOM 3109 CB PRO B 71 -25.575 27.509 21.262 1.00 32.62 C ANISOU 3109 CB PRO B 71 3717 4961 3716 -101 -610 -503 C ATOM 3110 CG PRO B 71 -26.078 27.120 19.897 1.00 31.67 C ANISOU 3110 CG PRO B 71 3555 4949 3530 -85 -651 -560 C ATOM 3111 CD PRO B 71 -25.860 28.357 19.056 1.00 39.58 C ANISOU 3111 CD PRO B 71 4563 6014 4460 -9 -661 -489 C ATOM 3112 N LEU B 72 -23.914 30.138 21.898 1.00 29.45 N ANISOU 3112 N LEU B 72 3405 4477 3308 -11 -552 -311 N ATOM 3113 CA LEU B 72 -23.066 30.957 22.756 1.00 30.34 C ANISOU 3113 CA LEU B 72 3562 4509 3457 -2 -515 -245 C ATOM 3114 C LEU B 72 -23.767 32.263 23.135 1.00 31.05 C ANISOU 3114 C LEU B 72 3637 4606 3554 38 -510 -185 C ATOM 3115 O LEU B 72 -23.720 32.688 24.291 1.00 27.74 O ANISOU 3115 O LEU B 72 3235 4119 3187 24 -486 -158 O ATOM 3116 CB LEU B 72 -21.732 31.240 22.057 1.00 25.92 C ANISOU 3116 CB LEU B 72 3043 3941 2866 25 -498 -211 C ATOM 3117 CG LEU B 72 -20.730 32.094 22.836 1.00 31.73 C ANISOU 3117 CG LEU B 72 3822 4596 3639 33 -459 -149 C ATOM 3118 CD1 LEU B 72 -20.213 31.338 24.028 1.00 31.56 C ANISOU 3118 CD1 LEU B 72 3824 4491 3677 -21 -441 -176 C ATOM 3119 CD2 LEU B 72 -19.572 32.525 21.924 1.00 40.46 C ANISOU 3119 CD2 LEU B 72 4957 5709 4707 69 -442 -110 C ATOM 3120 N ASN B 73 -24.428 32.909 22.172 1.00 30.60 N ANISOU 3120 N ASN B 73 3550 4634 3445 89 -531 -162 N ATOM 3121 CA ASN B 73 -25.072 34.196 22.445 1.00 31.18 C ANISOU 3121 CA ASN B 73 3610 4714 3524 134 -523 -99 C ATOM 3122 C ASN B 73 -26.208 34.056 23.451 1.00 30.48 C ANISOU 3122 C ASN B 73 3488 4610 3483 105 -529 -123 C ATOM 3123 O ASN B 73 -26.393 34.923 24.312 1.00 26.90 O ANISOU 3123 O ASN B 73 3044 4110 3068 116 -505 -78 O ATOM 3124 CB ASN B 73 -25.616 34.825 21.158 1.00 27.90 C ANISOU 3124 CB ASN B 73 3162 4400 3037 200 -546 -70 C ATOM 3125 CG ASN B 73 -24.542 35.062 20.104 1.00 31.42 C ANISOU 3125 CG ASN B 73 3639 4867 3431 237 -535 -38 C ATOM 3126 OD1 ASN B 73 -24.769 34.798 18.918 1.00 34.23 O ANISOU 3126 OD1 ASN B 73 3973 5316 3719 267 -564 -56 O ATOM 3127 ND2 ASN B 73 -23.384 35.564 20.518 1.00 30.17 N ANISOU 3127 ND2 ASN B 73 3530 4630 3304 237 -494 7 N ATOM 3128 N TYR B 74 -27.015 32.997 23.332 1.00 29.74 N ANISOU 3128 N TYR B 74 3355 4556 3388 69 -559 -194 N ATOM 3129 CA TYR B 74 -28.087 32.780 24.304 1.00 28.91 C ANISOU 3129 CA TYR B 74 3217 4433 3332 38 -560 -218 C ATOM 3130 C TYR B 74 -27.538 32.530 25.697 1.00 28.24 C ANISOU 3130 C TYR B 74 3172 4243 3314 -7 -524 -216 C ATOM 3131 O TYR B 74 -28.083 33.030 26.690 1.00 28.29 O ANISOU 3131 O TYR B 74 3173 4214 3361 -9 -508 -193 O ATOM 3132 CB TYR B 74 -28.947 31.591 23.896 1.00 27.52 C ANISOU 3132 CB TYR B 74 2992 4313 3151 1 -594 -301 C ATOM 3133 CG TYR B 74 -29.967 31.908 22.865 1.00 33.77 C ANISOU 3133 CG TYR B 74 3726 5217 3890 42 -635 -309 C ATOM 3134 CD1 TYR B 74 -31.142 32.554 23.209 1.00 43.34 C ANISOU 3134 CD1 TYR B 74 4895 6458 5115 64 -643 -288 C ATOM 3135 CD2 TYR B 74 -29.777 31.538 21.547 1.00 35.14 C ANISOU 3135 CD2 TYR B 74 3886 5470 3996 61 -666 -340 C ATOM 3136 CE1 TYR B 74 -32.099 32.837 22.258 1.00 48.93 C ANISOU 3136 CE1 TYR B 74 5545 7276 5772 106 -682 -296 C ATOM 3137 CE2 TYR B 74 -30.721 31.825 20.594 1.00 43.44 C ANISOU 3137 CE2 TYR B 74 4881 6634 4991 104 -706 -349 C ATOM 3138 CZ TYR B 74 -31.883 32.469 20.956 1.00 42.71 C ANISOU 3138 CZ TYR B 74 4744 6571 4914 126 -715 -326 C ATOM 3139 OH TYR B 74 -32.836 32.755 20.008 1.00 46.89 O ANISOU 3139 OH TYR B 74 5212 7218 5385 172 -758 -333 O ATOM 3140 N ILE B 75 -26.483 31.723 25.796 1.00 28.69 N ANISOU 3140 N ILE B 75 3266 4253 3380 -41 -512 -240 N ATOM 3141 CA ILE B 75 -25.921 31.398 27.102 1.00 26.92 C ANISOU 3141 CA ILE B 75 3078 3936 3213 -81 -480 -239 C ATOM 3142 C ILE B 75 -25.315 32.641 27.761 1.00 26.65 C ANISOU 3142 C ILE B 75 3081 3852 3195 -51 -451 -171 C ATOM 3143 O ILE B 75 -25.461 32.844 28.971 1.00 26.04 O ANISOU 3143 O ILE B 75 3014 3720 3161 -67 -430 -160 O ATOM 3144 CB ILE B 75 -24.899 30.256 26.963 1.00 28.07 C ANISOU 3144 CB ILE B 75 3253 4049 3362 -118 -474 -278 C ATOM 3145 CG1 ILE B 75 -25.612 28.956 26.569 1.00 32.49 C ANISOU 3145 CG1 ILE B 75 3776 4643 3925 -157 -494 -355 C ATOM 3146 CG2 ILE B 75 -24.137 30.056 28.245 1.00 30.72 C ANISOU 3146 CG2 ILE B 75 3630 4295 3746 -146 -440 -265 C ATOM 3147 CD1 ILE B 75 -26.431 28.388 27.703 1.00 37.78 C ANISOU 3147 CD1 ILE B 75 4427 5274 4654 -198 -481 -380 C ATOM 3148 N LEU B 76 -24.618 33.490 26.993 1.00 27.27 N ANISOU 3148 N LEU B 76 3177 3945 3238 -8 -447 -126 N ATOM 3149 CA LEU B 76 -24.080 34.710 27.602 1.00 23.97 C ANISOU 3149 CA LEU B 76 2789 3476 2842 18 -417 -66 C ATOM 3150 C LEU B 76 -25.189 35.680 28.002 1.00 24.79 C ANISOU 3150 C LEU B 76 2866 3593 2960 46 -414 -35 C ATOM 3151 O LEU B 76 -25.042 36.424 28.977 1.00 27.40 O ANISOU 3151 O LEU B 76 3214 3866 3328 49 -386 -6 O ATOM 3152 CB LEU B 76 -23.078 35.389 26.657 1.00 24.94 C ANISOU 3152 CB LEU B 76 2937 3609 2932 58 -407 -23 C ATOM 3153 CG LEU B 76 -21.594 35.035 26.893 1.00 29.00 C ANISOU 3153 CG LEU B 76 3496 4063 3461 34 -387 -26 C ATOM 3154 CD1 LEU B 76 -21.088 35.694 28.172 1.00 29.42 C ANISOU 3154 CD1 LEU B 76 3576 4036 3564 23 -356 0 C ATOM 3155 CD2 LEU B 76 -21.373 33.522 26.949 1.00 27.68 C ANISOU 3155 CD2 LEU B 76 3331 3892 3294 -15 -401 -88 C ATOM 3156 N LEU B 77 -26.292 35.702 27.253 1.00 26.64 N ANISOU 3156 N LEU B 77 3053 3904 3163 70 -441 -42 N ATOM 3157 CA LEU B 77 -27.436 36.518 27.642 1.00 25.21 C ANISOU 3157 CA LEU B 77 2841 3740 2998 96 -439 -17 C ATOM 3158 C LEU B 77 -28.027 36.026 28.960 1.00 27.07 C ANISOU 3158 C LEU B 77 3070 3931 3286 51 -429 -48 C ATOM 3159 O LEU B 77 -28.329 36.824 29.860 1.00 26.79 O ANISOU 3159 O LEU B 77 3039 3857 3285 62 -405 -18 O ATOM 3160 CB LEU B 77 -28.481 36.491 26.527 1.00 26.61 C ANISOU 3160 CB LEU B 77 2965 4018 3128 129 -475 -25 C ATOM 3161 CG LEU B 77 -29.827 37.144 26.839 1.00 33.02 C ANISOU 3161 CG LEU B 77 3732 4860 3953 155 -480 -7 C ATOM 3162 CD1 LEU B 77 -29.663 38.606 27.263 1.00 35.66 C ANISOU 3162 CD1 LEU B 77 4088 5152 4308 201 -443 67 C ATOM 3163 CD2 LEU B 77 -30.730 37.029 25.605 1.00 34.10 C ANISOU 3163 CD2 LEU B 77 3814 5110 4035 190 -522 -19 C ATOM 3164 N ASN B 78 -28.153 34.707 29.109 1.00 26.66 N ANISOU 3164 N ASN B 78 3007 3880 3243 1 -443 -108 N ATOM 3165 CA ASN B 78 -28.610 34.135 30.373 1.00 26.57 C ANISOU 3165 CA ASN B 78 2992 3820 3281 -42 -428 -136 C ATOM 3166 C ASN B 78 -27.658 34.479 31.528 1.00 22.95 C ANISOU 3166 C ASN B 78 2586 3277 2856 -54 -392 -110 C ATOM 3167 O ASN B 78 -28.111 34.821 32.632 1.00 25.04 O ANISOU 3167 O ASN B 78 2852 3506 3155 -59 -372 -100 O ATOM 3168 CB ASN B 78 -28.762 32.619 30.205 1.00 31.83 C ANISOU 3168 CB ASN B 78 3642 4498 3953 -92 -443 -202 C ATOM 3169 CG ASN B 78 -29.408 31.951 31.413 1.00 29.26 C ANISOU 3169 CG ASN B 78 3306 4132 3680 -135 -425 -229 C ATOM 3170 OD1 ASN B 78 -30.445 32.388 31.894 1.00 37.66 O ANISOU 3170 OD1 ASN B 78 4339 5206 4763 -126 -421 -220 O ATOM 3171 ND2 ASN B 78 -28.799 30.880 31.883 1.00 31.82 N ANISOU 3171 ND2 ASN B 78 3655 4408 4027 -178 -411 -260 N ATOM 3172 N LEU B 79 -26.336 34.401 31.308 1.00 24.62 N ANISOU 3172 N LEU B 79 2839 3458 3056 -56 -384 -102 N ATOM 3173 CA LEU B 79 -25.402 34.770 32.381 1.00 22.58 C ANISOU 3173 CA LEU B 79 2625 3126 2826 -65 -354 -82 C ATOM 3174 C LEU B 79 -25.542 36.241 32.757 1.00 23.89 C ANISOU 3174 C LEU B 79 2798 3276 3006 -27 -335 -33 C ATOM 3175 O LEU B 79 -25.444 36.597 33.934 1.00 22.97 O ANISOU 3175 O LEU B 79 2699 3109 2921 -36 -312 -27 O ATOM 3176 CB LEU B 79 -23.948 34.473 31.986 1.00 21.88 C ANISOU 3176 CB LEU B 79 2575 3013 2724 -72 -351 -81 C ATOM 3177 CG LEU B 79 -23.656 32.990 31.762 1.00 29.59 C ANISOU 3177 CG LEU B 79 3553 3992 3696 -112 -362 -129 C ATOM 3178 CD1 LEU B 79 -22.285 32.784 31.148 1.00 27.38 C ANISOU 3178 CD1 LEU B 79 3306 3700 3398 -110 -360 -125 C ATOM 3179 CD2 LEU B 79 -23.770 32.255 33.084 1.00 27.24 C ANISOU 3179 CD2 LEU B 79 3265 3646 3438 -150 -345 -151 C ATOM 3180 N ALA B 80 -25.737 37.115 31.771 1.00 23.75 N ANISOU 3180 N ALA B 80 2766 3298 2962 18 -341 1 N ATOM 3181 CA ALA B 80 -25.924 38.533 32.073 1.00 22.35 C ANISOU 3181 CA ALA B 80 2590 3099 2801 56 -318 49 C ATOM 3182 C ALA B 80 -27.121 38.740 32.994 1.00 24.36 C ANISOU 3182 C ALA B 80 2821 3351 3084 54 -311 44 C ATOM 3183 O ALA B 80 -27.050 39.518 33.949 1.00 24.22 O ANISOU 3183 O ALA B 80 2819 3284 3098 59 -283 61 O ATOM 3184 CB ALA B 80 -26.106 39.330 30.787 1.00 24.28 C ANISOU 3184 CB ALA B 80 2818 3396 3011 110 -325 91 C ATOM 3185 N VAL B 81 -28.217 38.020 32.747 1.00 22.72 N ANISOU 3185 N VAL B 81 2571 3195 2868 43 -335 15 N ATOM 3186 CA VAL B 81 -29.399 38.145 33.598 1.00 22.85 C ANISOU 3186 CA VAL B 81 2560 3211 2913 39 -327 9 C ATOM 3187 C VAL B 81 -29.125 37.601 34.998 1.00 23.58 C ANISOU 3187 C VAL B 81 2678 3242 3040 -3 -305 -15 C ATOM 3188 O VAL B 81 -29.446 38.243 36.009 1.00 24.61 O ANISOU 3188 O VAL B 81 2814 3338 3199 3 -280 -2 O ATOM 3189 CB VAL B 81 -30.597 37.439 32.932 1.00 26.38 C ANISOU 3189 CB VAL B 81 2950 3730 3343 35 -359 -20 C ATOM 3190 CG1 VAL B 81 -31.789 37.387 33.879 1.00 29.53 C ANISOU 3190 CG1 VAL B 81 3318 4125 3778 23 -348 -32 C ATOM 3191 CG2 VAL B 81 -30.968 38.152 31.652 1.00 25.98 C ANISOU 3191 CG2 VAL B 81 2871 3748 3254 88 -379 11 C ATOM 3192 N ALA B 82 -28.525 36.412 35.085 1.00 22.85 N ANISOU 3192 N ALA B 82 2602 3136 2946 -44 -312 -51 N ATOM 3193 CA ALA B 82 -28.193 35.859 36.394 1.00 24.38 C ANISOU 3193 CA ALA B 82 2822 3275 3167 -79 -290 -69 C ATOM 3194 C ALA B 82 -27.225 36.770 37.154 1.00 22.89 C ANISOU 3194 C ALA B 82 2676 3032 2989 -67 -266 -43 C ATOM 3195 O ALA B 82 -27.330 36.921 38.377 1.00 23.74 O ANISOU 3195 O ALA B 82 2797 3103 3119 -75 -243 -45 O ATOM 3196 CB ALA B 82 -27.589 34.464 36.235 1.00 24.43 C ANISOU 3196 CB ALA B 82 2840 3274 3168 -119 -300 -105 C ATOM 3197 N ASP B 83 -26.260 37.362 36.449 1.00 21.47 N ANISOU 3197 N ASP B 83 2517 2847 2793 -47 -268 -21 N ATOM 3198 CA ASP B 83 -25.348 38.312 37.087 1.00 22.54 C ANISOU 3198 CA ASP B 83 2688 2933 2945 -36 -244 -1 C ATOM 3199 C ASP B 83 -26.100 39.512 37.667 1.00 22.48 C ANISOU 3199 C ASP B 83 2670 2912 2959 -8 -223 22 C ATOM 3200 O ASP B 83 -25.734 40.024 38.733 1.00 22.64 O ANISOU 3200 O ASP B 83 2713 2887 3001 -12 -200 20 O ATOM 3201 CB ASP B 83 -24.302 38.808 36.078 1.00 21.23 C ANISOU 3201 CB ASP B 83 2538 2765 2761 -16 -247 22 C ATOM 3202 CG ASP B 83 -23.302 37.726 35.640 1.00 24.86 C ANISOU 3202 CG ASP B 83 3017 3226 3203 -43 -262 0 C ATOM 3203 OD1 ASP B 83 -23.246 36.642 36.269 1.00 24.11 O ANISOU 3203 OD1 ASP B 83 2928 3120 3113 -78 -266 -32 O ATOM 3204 OD2 ASP B 83 -22.572 37.973 34.631 1.00 23.22 O ANISOU 3204 OD2 ASP B 83 2816 3028 2976 -27 -267 17 O ATOM 3205 N LEU B 84 -27.112 40.021 36.947 1.00 22.74 N ANISOU 3205 N LEU B 84 2668 2986 2986 23 -229 43 N ATOM 3206 CA LEU B 84 -27.863 41.165 37.458 1.00 23.79 C ANISOU 3206 CA LEU B 84 2790 3107 3143 53 -206 67 C ATOM 3207 C LEU B 84 -28.651 40.784 38.706 1.00 24.23 C ANISOU 3207 C LEU B 84 2838 3150 3220 32 -194 43 C ATOM 3208 O LEU B 84 -28.803 41.602 39.620 1.00 24.16 O ANISOU 3208 O LEU B 84 2839 3106 3235 43 -167 50 O ATOM 3209 CB LEU B 84 -28.790 41.730 36.372 1.00 23.23 C ANISOU 3209 CB LEU B 84 2679 3088 3057 96 -216 99 C ATOM 3210 CG LEU B 84 -27.992 42.445 35.265 1.00 27.99 C ANISOU 3210 CG LEU B 84 3296 3696 3644 130 -215 136 C ATOM 3211 CD1 LEU B 84 -28.856 42.766 34.046 1.00 31.73 C ANISOU 3211 CD1 LEU B 84 3730 4238 4090 175 -232 167 C ATOM 3212 CD2 LEU B 84 -27.386 43.724 35.795 1.00 25.85 C ANISOU 3212 CD2 LEU B 84 3053 3363 3406 150 -176 163 C ATOM 3213 N PHE B 85 -29.188 39.559 38.752 1.00 23.28 N ANISOU 3213 N PHE B 85 2698 3056 3092 2 -212 14 N ATOM 3214 CA PHE B 85 -29.798 39.095 40.000 1.00 23.26 C ANISOU 3214 CA PHE B 85 2692 3035 3110 -21 -195 -7 C ATOM 3215 C PHE B 85 -28.766 39.020 41.120 1.00 25.43 C ANISOU 3215 C PHE B 85 3013 3257 3391 -40 -176 -18 C ATOM 3216 O PHE B 85 -29.067 39.362 42.273 1.00 25.32 O ANISOU 3216 O PHE B 85 3008 3218 3394 -39 -151 -22 O ATOM 3217 CB PHE B 85 -30.472 37.734 39.808 1.00 22.97 C ANISOU 3217 CB PHE B 85 2626 3031 3070 -52 -212 -36 C ATOM 3218 CG PHE B 85 -31.860 37.833 39.214 1.00 27.70 C ANISOU 3218 CG PHE B 85 3170 3683 3673 -36 -225 -34 C ATOM 3219 CD1 PHE B 85 -32.940 38.171 40.010 1.00 36.61 C ANISOU 3219 CD1 PHE B 85 4275 4810 4826 -28 -204 -30 C ATOM 3220 CD2 PHE B 85 -32.068 37.636 37.863 1.00 34.88 C ANISOU 3220 CD2 PHE B 85 4049 4646 4558 -26 -257 -35 C ATOM 3221 CE1 PHE B 85 -34.218 38.283 39.465 1.00 41.23 C ANISOU 3221 CE1 PHE B 85 4804 5446 5415 -12 -216 -27 C ATOM 3222 CE2 PHE B 85 -33.343 37.739 37.312 1.00 33.15 C ANISOU 3222 CE2 PHE B 85 3774 4482 4338 -8 -272 -35 C ATOM 3223 CZ PHE B 85 -34.412 38.064 38.113 1.00 35.93 C ANISOU 3223 CZ PHE B 85 4100 4832 4718 -2 -252 -31 C ATOM 3224 N MET B 86 -27.546 38.559 40.819 1.00 21.66 N ANISOU 3224 N MET B 86 2565 2767 2900 -56 -187 -26 N ATOM 3225 CA MET B 86 -26.527 38.544 41.873 1.00 24.64 C ANISOU 3225 CA MET B 86 2982 3100 3281 -70 -171 -37 C ATOM 3226 C MET B 86 -26.246 39.947 42.399 1.00 23.51 C ANISOU 3226 C MET B 86 2854 2926 3154 -46 -150 -24 C ATOM 3227 O MET B 86 -26.149 40.149 43.618 1.00 24.19 O ANISOU 3227 O MET B 86 2957 2986 3248 -50 -130 -37 O ATOM 3228 CB MET B 86 -25.209 37.923 41.389 1.00 20.73 C ANISOU 3228 CB MET B 86 2512 2596 2769 -87 -187 -45 C ATOM 3229 CG MET B 86 -25.324 36.492 40.872 1.00 24.34 C ANISOU 3229 CG MET B 86 2958 3077 3214 -114 -205 -63 C ATOM 3230 SD MET B 86 -23.675 35.932 40.328 1.00 28.57 S ANISOU 3230 SD MET B 86 3526 3598 3733 -128 -218 -69 S ATOM 3231 CE MET B 86 -22.795 35.923 41.865 1.00 26.01 C ANISOU 3231 CE MET B 86 3237 3230 3416 -138 -198 -78 C ATOM 3232 N VAL B 87 -26.118 40.921 41.495 1.00 21.31 N ANISOU 3232 N VAL B 87 2568 2648 2878 -18 -150 1 N ATOM 3233 CA VAL B 87 -25.712 42.274 41.874 1.00 21.25 C ANISOU 3233 CA VAL B 87 2577 2604 2894 3 -125 12 C ATOM 3234 C VAL B 87 -26.793 42.952 42.715 1.00 26.38 C ANISOU 3234 C VAL B 87 3214 3246 3564 20 -101 13 C ATOM 3235 O VAL B 87 -26.520 43.492 43.800 1.00 26.10 O ANISOU 3235 O VAL B 87 3198 3176 3544 18 -79 -3 O ATOM 3236 CB VAL B 87 -25.384 43.078 40.599 1.00 26.42 C ANISOU 3236 CB VAL B 87 3226 3262 3550 31 -125 46 C ATOM 3237 CG1 VAL B 87 -25.256 44.588 40.890 1.00 26.07 C ANISOU 3237 CG1 VAL B 87 3189 3176 3539 59 -91 62 C ATOM 3238 CG2 VAL B 87 -24.106 42.513 39.949 1.00 26.11 C ANISOU 3238 CG2 VAL B 87 3207 3221 3493 14 -142 41 C ATOM 3239 N PHE B 88 -28.041 42.913 42.247 1.00 28.01 N ANISOU 3239 N PHE B 88 3384 3487 3770 36 -105 30 N ATOM 3240 CA PHE B 88 -29.108 43.634 42.938 1.00 25.92 C ANISOU 3240 CA PHE B 88 3103 3217 3527 57 -80 36 C ATOM 3241 C PHE B 88 -29.777 42.802 44.017 1.00 27.48 C ANISOU 3241 C PHE B 88 3295 3422 3723 34 -75 10 C ATOM 3242 O PHE B 88 -30.167 43.349 45.057 1.00 28.43 O ANISOU 3242 O PHE B 88 3422 3521 3860 42 -47 3 O ATOM 3243 CB PHE B 88 -30.140 44.124 41.920 1.00 27.93 C ANISOU 3243 CB PHE B 88 3318 3510 3786 93 -85 69 C ATOM 3244 CG PHE B 88 -29.613 45.223 41.061 1.00 37.46 C ANISOU 3244 CG PHE B 88 4532 4702 5001 126 -75 103 C ATOM 3245 CD1 PHE B 88 -29.427 46.496 41.592 1.00 35.14 C ANISOU 3245 CD1 PHE B 88 4253 4359 4740 148 -38 113 C ATOM 3246 CD2 PHE B 88 -29.259 44.990 39.740 1.00 32.55 C ANISOU 3246 CD2 PHE B 88 3902 4112 4355 136 -99 124 C ATOM 3247 CE1 PHE B 88 -28.905 47.518 40.815 1.00 40.43 C ANISOU 3247 CE1 PHE B 88 4930 5007 5425 179 -22 147 C ATOM 3248 CE2 PHE B 88 -28.753 46.023 38.949 1.00 37.53 C ANISOU 3248 CE2 PHE B 88 4539 4727 4993 171 -84 162 C ATOM 3249 CZ PHE B 88 -28.564 47.282 39.491 1.00 36.70 C ANISOU 3249 CZ PHE B 88 4450 4568 4928 191 -44 175 C ATOM 3250 N GLY B 89 -29.897 41.491 43.815 1.00 24.25 N ANISOU 3250 N GLY B 89 2877 3040 3297 6 -96 -3 N ATOM 3251 CA GLY B 89 -30.533 40.661 44.832 1.00 23.05 C ANISOU 3251 CA GLY B 89 2720 2891 3147 -15 -85 -22 C ATOM 3252 C GLY B 89 -29.604 40.332 45.989 1.00 26.04 C ANISOU 3252 C GLY B 89 3140 3237 3517 -34 -73 -43 C ATOM 3253 O GLY B 89 -30.037 40.288 47.149 1.00 25.93 O ANISOU 3253 O GLY B 89 3132 3213 3508 -35 -49 -53 O ATOM 3254 N GLY B 90 -28.324 40.085 45.687 1.00 21.33 N ANISOU 3254 N GLY B 90 2571 2628 2906 -46 -88 -49 N ATOM 3255 CA GLY B 90 -27.401 39.667 46.734 1.00 24.04 C ANISOU 3255 CA GLY B 90 2950 2949 3237 -63 -81 -69 C ATOM 3256 C GLY B 90 -26.406 40.712 47.174 1.00 24.00 C ANISOU 3256 C GLY B 90 2972 2914 3235 -52 -73 -78 C ATOM 3257 O GLY B 90 -26.281 40.965 48.383 1.00 22.79 O ANISOU 3257 O GLY B 90 2836 2746 3078 -50 -55 -95 O ATOM 3258 N PHE B 91 -25.730 41.373 46.216 1.00 21.02 N ANISOU 3258 N PHE B 91 2597 2526 2864 -44 -84 -67 N ATOM 3259 CA PHE B 91 -24.562 42.196 46.581 1.00 23.08 C ANISOU 3259 CA PHE B 91 2882 2754 3132 -42 -77 -81 C ATOM 3260 C PHE B 91 -24.973 43.468 47.293 1.00 23.99 C ANISOU 3260 C PHE B 91 2999 2846 3271 -21 -48 -88 C ATOM 3261 O PHE B 91 -24.173 44.043 48.061 1.00 21.27 O ANISOU 3261 O PHE B 91 2674 2475 2932 -24 -38 -115 O ATOM 3262 CB PHE B 91 -23.721 42.592 45.370 1.00 20.89 C ANISOU 3262 CB PHE B 91 2608 2469 2862 -38 -89 -66 C ATOM 3263 CG PHE B 91 -22.945 41.443 44.736 1.00 23.95 C ANISOU 3263 CG PHE B 91 3001 2872 3226 -59 -115 -66 C ATOM 3264 CD1 PHE B 91 -23.028 40.163 45.247 1.00 21.69 C ANISOU 3264 CD1 PHE B 91 2720 2602 2920 -79 -125 -79 C ATOM 3265 CD2 PHE B 91 -22.139 41.673 43.624 1.00 23.94 C ANISOU 3265 CD2 PHE B 91 3003 2867 3228 -56 -125 -51 C ATOM 3266 CE1 PHE B 91 -22.327 39.124 44.656 1.00 26.48 C ANISOU 3266 CE1 PHE B 91 3333 3219 3510 -97 -146 -80 C ATOM 3267 CE2 PHE B 91 -21.412 40.624 43.040 1.00 25.78 C ANISOU 3267 CE2 PHE B 91 3243 3113 3439 -74 -147 -54 C ATOM 3268 CZ PHE B 91 -21.533 39.348 43.549 1.00 20.21 C ANISOU 3268 CZ PHE B 91 2541 2422 2715 -95 -158 -69 C ATOM 3269 N THR B 92 -26.195 43.936 47.051 1.00 22.00 N ANISOU 3269 N THR B 92 2722 2602 3035 0 -34 -69 N ATOM 3270 CA THR B 92 -26.657 45.083 47.817 1.00 23.64 C ANISOU 3270 CA THR B 92 2930 2785 3266 20 -3 -78 C ATOM 3271 C THR B 92 -26.731 44.759 49.302 1.00 26.98 C ANISOU 3271 C THR B 92 3369 3208 3674 10 9 -110 C ATOM 3272 O THR B 92 -26.473 45.640 50.136 1.00 25.91 O ANISOU 3272 O THR B 92 3248 3047 3551 17 31 -136 O ATOM 3273 CB THR B 92 -28.017 45.553 47.303 1.00 25.93 C ANISOU 3273 CB THR B 92 3189 3089 3576 47 10 -47 C ATOM 3274 OG1 THR B 92 -28.896 44.429 47.235 1.00 26.61 O ANISOU 3274 OG1 THR B 92 3254 3215 3643 37 -4 -41 O ATOM 3275 CG2 THR B 92 -27.861 46.190 45.917 1.00 26.06 C ANISOU 3275 CG2 THR B 92 3192 3104 3607 67 5 -13 C ATOM 3276 N THR B 93 -27.073 43.508 49.656 1.00 21.65 N ANISOU 3276 N THR B 93 2693 2562 2973 -6 -1 -111 N ATOM 3277 CA THR B 93 -27.000 43.108 51.064 1.00 21.69 C ANISOU 3277 CA THR B 93 2717 2570 2956 -12 11 -137 C ATOM 3278 C THR B 93 -25.548 42.936 51.530 1.00 23.13 C ANISOU 3278 C THR B 93 2928 2743 3116 -27 -3 -163 C ATOM 3279 O THR B 93 -25.209 43.339 52.645 1.00 25.11 O ANISOU 3279 O THR B 93 3196 2988 3356 -22 9 -194 O ATOM 3280 CB THR B 93 -27.826 41.832 51.313 1.00 25.44 C ANISOU 3280 CB THR B 93 3179 3073 3414 -23 11 -124 C ATOM 3281 OG1 THR B 93 -29.235 42.150 51.276 1.00 26.40 O ANISOU 3281 OG1 THR B 93 3272 3203 3555 -7 31 -109 O ATOM 3282 CG2 THR B 93 -27.512 41.226 52.704 1.00 25.22 C ANISOU 3282 CG2 THR B 93 3176 3052 3355 -28 23 -144 C ATOM 3283 N THR B 94 -24.664 42.357 50.701 1.00 21.63 N ANISOU 3283 N THR B 94 2742 2555 2920 -42 -30 -155 N ATOM 3284 CA THR B 94 -23.257 42.255 51.098 1.00 22.95 C ANISOU 3284 CA THR B 94 2933 2716 3071 -54 -44 -180 C ATOM 3285 C THR B 94 -22.679 43.623 51.442 1.00 24.88 C ANISOU 3285 C THR B 94 3185 2931 3337 -46 -32 -209 C ATOM 3286 O THR B 94 -21.940 43.768 52.418 1.00 21.43 O ANISOU 3286 O THR B 94 2764 2494 2884 -50 -32 -244 O ATOM 3287 CB THR B 94 -22.414 41.647 49.980 1.00 21.15 C ANISOU 3287 CB THR B 94 2705 2489 2841 -69 -70 -165 C ATOM 3288 OG1 THR B 94 -23.162 40.619 49.308 1.00 22.71 O ANISOU 3288 OG1 THR B 94 2888 2708 3032 -75 -78 -139 O ATOM 3289 CG2 THR B 94 -21.119 41.085 50.577 1.00 20.73 C ANISOU 3289 CG2 THR B 94 2673 2440 2762 -82 -85 -187 C ATOM 3290 N LEU B 95 -22.983 44.629 50.625 1.00 21.45 N ANISOU 3290 N LEU B 95 2737 2472 2940 -35 -20 -194 N ATOM 3291 CA LEU B 95 -22.466 45.980 50.849 1.00 22.75 C ANISOU 3291 CA LEU B 95 2906 2601 3137 -29 -1 -220 C ATOM 3292 C LEU B 95 -23.002 46.583 52.146 1.00 22.02 C ANISOU 3292 C LEU B 95 2819 2503 3044 -18 24 -254 C ATOM 3293 O LEU B 95 -22.248 47.147 52.948 1.00 22.95 O ANISOU 3293 O LEU B 95 2948 2606 3163 -23 29 -299 O ATOM 3294 CB LEU B 95 -22.862 46.869 49.658 1.00 23.75 C ANISOU 3294 CB LEU B 95 3016 2702 3305 -12 14 -186 C ATOM 3295 CG LEU B 95 -22.537 48.348 49.829 1.00 25.30 C ANISOU 3295 CG LEU B 95 3215 2851 3548 -3 44 -207 C ATOM 3296 CD1 LEU B 95 -21.038 48.484 49.932 1.00 28.42 C ANISOU 3296 CD1 LEU B 95 3622 3227 3948 -24 33 -240 C ATOM 3297 CD2 LEU B 95 -23.051 49.106 48.630 1.00 31.54 C ANISOU 3297 CD2 LEU B 95 3988 3621 4375 20 62 -161 C ATOM 3298 N TYR B 96 -24.316 46.512 52.351 1.00 24.86 N ANISOU 3298 N TYR B 96 3167 2875 3402 -2 41 -235 N ATOM 3299 CA TYR B 96 -24.901 47.100 53.557 1.00 25.40 C ANISOU 3299 CA TYR B 96 3241 2940 3471 11 69 -265 C ATOM 3300 C TYR B 96 -24.356 46.416 54.811 1.00 28.01 C ANISOU 3300 C TYR B 96 3591 3297 3753 2 59 -301 C ATOM 3301 O TYR B 96 -24.020 47.076 55.800 1.00 26.66 O ANISOU 3301 O TYR B 96 3432 3120 3578 6 71 -347 O ATOM 3302 CB TYR B 96 -26.422 46.982 53.489 1.00 25.54 C ANISOU 3302 CB TYR B 96 3239 2970 3494 30 88 -233 C ATOM 3303 CG TYR B 96 -27.142 47.859 54.462 1.00 32.23 C ANISOU 3303 CG TYR B 96 4087 3805 4354 49 124 -257 C ATOM 3304 CD1 TYR B 96 -27.421 49.182 54.149 1.00 35.18 C ANISOU 3304 CD1 TYR B 96 4452 4140 4776 67 151 -258 C ATOM 3305 CD2 TYR B 96 -27.533 47.379 55.703 1.00 36.08 C ANISOU 3305 CD2 TYR B 96 4585 4319 4806 52 134 -278 C ATOM 3306 CE1 TYR B 96 -28.080 50.001 55.050 1.00 52.79 C ANISOU 3306 CE1 TYR B 96 6683 6356 7020 86 188 -284 C ATOM 3307 CE2 TYR B 96 -28.191 48.189 56.610 1.00 33.71 C ANISOU 3307 CE2 TYR B 96 4286 4008 4514 72 169 -303 C ATOM 3308 CZ TYR B 96 -28.462 49.494 56.286 1.00 42.26 C ANISOU 3308 CZ TYR B 96 5359 5050 5646 87 196 -308 C ATOM 3309 OH TYR B 96 -29.122 50.304 57.187 1.00 56.91 O ANISOU 3309 OH TYR B 96 7217 6893 7513 107 233 -335 O ATOM 3310 N THR B 97 -24.234 45.091 54.764 1.00 24.93 N ANISOU 3310 N THR B 97 3205 2940 3328 -9 37 -281 N ATOM 3311 CA THR B 97 -23.694 44.330 55.888 1.00 22.23 C ANISOU 3311 CA THR B 97 2882 2627 2936 -12 28 -304 C ATOM 3312 C THR B 97 -22.239 44.710 56.168 1.00 24.73 C ANISOU 3312 C THR B 97 3211 2939 3246 -22 9 -346 C ATOM 3313 O THR B 97 -21.837 44.891 57.329 1.00 23.76 O ANISOU 3313 O THR B 97 3101 2833 3094 -17 10 -388 O ATOM 3314 CB THR B 97 -23.834 42.846 55.549 1.00 25.16 C ANISOU 3314 CB THR B 97 3252 3024 3283 -21 12 -266 C ATOM 3315 OG1 THR B 97 -25.230 42.549 55.342 1.00 23.16 O ANISOU 3315 OG1 THR B 97 2982 2777 3042 -14 31 -234 O ATOM 3316 CG2 THR B 97 -23.270 41.966 56.648 1.00 22.68 C ANISOU 3316 CG2 THR B 97 2958 2742 2918 -20 6 -280 C ATOM 3317 N SER B 98 -21.437 44.867 55.111 1.00 22.04 N ANISOU 3317 N SER B 98 2866 2577 2932 -37 -9 -338 N ATOM 3318 CA SER B 98 -20.027 45.167 55.299 1.00 22.12 C ANISOU 3318 CA SER B 98 2882 2581 2940 -50 -28 -377 C ATOM 3319 C SER B 98 -19.826 46.582 55.836 1.00 27.94 C ANISOU 3319 C SER B 98 3618 3291 3708 -47 -8 -428 C ATOM 3320 O SER B 98 -18.898 46.819 56.613 1.00 23.65 O ANISOU 3320 O SER B 98 3080 2757 3148 -53 -19 -479 O ATOM 3321 CB SER B 98 -19.269 44.985 53.977 1.00 25.26 C ANISOU 3321 CB SER B 98 3274 2962 3362 -65 -46 -351 C ATOM 3322 OG SER B 98 -19.309 43.638 53.500 1.00 29.73 O ANISOU 3322 OG SER B 98 3842 3553 3900 -70 -66 -313 O ATOM 3323 N LEU B 99 -20.679 47.525 55.432 1.00 22.65 N ANISOU 3323 N LEU B 99 2938 2586 3082 -36 22 -417 N ATOM 3324 CA LEU B 99 -20.601 48.878 55.977 1.00 24.70 C ANISOU 3324 CA LEU B 99 3197 2813 3376 -33 48 -467 C ATOM 3325 C LEU B 99 -20.795 48.895 57.489 1.00 24.79 C ANISOU 3325 C LEU B 99 3219 2854 3346 -24 55 -516 C ATOM 3326 O LEU B 99 -20.148 49.681 58.187 1.00 30.53 O ANISOU 3326 O LEU B 99 3948 3571 4082 -29 59 -579 O ATOM 3327 CB LEU B 99 -21.649 49.783 55.324 1.00 25.08 C ANISOU 3327 CB LEU B 99 3233 2821 3476 -16 84 -437 C ATOM 3328 CG LEU B 99 -21.330 50.165 53.888 1.00 27.42 C ANISOU 3328 CG LEU B 99 3518 3082 3820 -20 85 -398 C ATOM 3329 CD1 LEU B 99 -22.570 50.776 53.292 1.00 32.69 C ANISOU 3329 CD1 LEU B 99 4172 3726 4522 5 116 -356 C ATOM 3330 CD2 LEU B 99 -20.179 51.169 53.840 1.00 26.27 C ANISOU 3330 CD2 LEU B 99 3371 2891 3718 -35 95 -442 C ATOM 3331 N HIS B 100 -21.722 48.087 58.013 1.00 26.34 N ANISOU 3331 N HIS B 100 3420 3086 3500 -8 58 -491 N ATOM 3332 CA HIS B 100 -22.058 48.142 59.435 1.00 25.31 C ANISOU 3332 CA HIS B 100 3302 2987 3329 7 71 -530 C ATOM 3333 C HIS B 100 -21.332 47.113 60.286 1.00 27.42 C ANISOU 3333 C HIS B 100 3583 3309 3528 7 43 -545 C ATOM 3334 O HIS B 100 -21.327 47.239 61.529 1.00 29.52 O ANISOU 3334 O HIS B 100 3859 3607 3752 21 49 -588 O ATOM 3335 CB HIS B 100 -23.562 47.961 59.639 1.00 32.80 C ANISOU 3335 CB HIS B 100 4247 3941 4273 28 101 -495 C ATOM 3336 CG HIS B 100 -24.361 49.093 59.117 1.00 30.54 C ANISOU 3336 CG HIS B 100 3948 3609 4048 37 134 -488 C ATOM 3337 ND1 HIS B 100 -24.645 50.201 59.881 1.00 33.74 N ANISOU 3337 ND1 HIS B 100 4355 3994 4470 49 165 -536 N ATOM 3338 CD2 HIS B 100 -24.904 49.319 57.899 1.00 30.85 C ANISOU 3338 CD2 HIS B 100 3970 3618 4134 38 142 -439 C ATOM 3339 CE1 HIS B 100 -25.351 51.055 59.164 1.00 33.61 C ANISOU 3339 CE1 HIS B 100 4324 3933 4513 58 194 -514 C ATOM 3340 NE2 HIS B 100 -25.511 50.551 57.955 1.00 31.38 N ANISOU 3340 NE2 HIS B 100 4030 3646 4246 54 179 -454 N ATOM 3341 N GLY B 101 -20.731 46.117 59.663 1.00 28.45 N ANISOU 3341 N GLY B 101 3713 3452 3643 -5 14 -510 N ATOM 3342 CA GLY B 101 -19.980 45.102 60.354 1.00 27.02 C ANISOU 3342 CA GLY B 101 3545 3321 3402 -2 -12 -516 C ATOM 3343 C GLY B 101 -20.792 43.940 60.869 1.00 26.10 C ANISOU 3343 C GLY B 101 3438 3241 3239 16 -2 -472 C ATOM 3344 O GLY B 101 -20.263 43.171 61.676 1.00 24.96 O ANISOU 3344 O GLY B 101 3306 3141 3038 27 -15 -477 O ATOM 3345 N TYR B 102 -22.049 43.791 60.437 1.00 23.13 N ANISOU 3345 N TYR B 102 3055 2848 2886 20 24 -429 N ATOM 3346 CA TYR B 102 -22.890 42.653 60.817 1.00 28.46 C ANISOU 3346 CA TYR B 102 3734 3549 3529 33 39 -385 C ATOM 3347 C TYR B 102 -24.168 42.688 59.975 1.00 29.83 C ANISOU 3347 C TYR B 102 3891 3696 3748 29 60 -344 C ATOM 3348 O TYR B 102 -24.440 43.662 59.261 1.00 24.92 O ANISOU 3348 O TYR B 102 3255 3040 3174 24 66 -350 O ATOM 3349 CB TYR B 102 -23.207 42.670 62.329 1.00 26.82 C ANISOU 3349 CB TYR B 102 3542 3380 3269 60 60 -409 C ATOM 3350 CG TYR B 102 -24.238 43.704 62.758 1.00 25.81 C ANISOU 3350 CG TYR B 102 3408 3237 3161 73 95 -431 C ATOM 3351 CD1 TYR B 102 -23.931 45.053 62.809 1.00 27.30 C ANISOU 3351 CD1 TYR B 102 3594 3402 3378 70 96 -485 C ATOM 3352 CD2 TYR B 102 -25.507 43.318 63.155 1.00 27.43 C ANISOU 3352 CD2 TYR B 102 3611 3451 3359 90 130 -398 C ATOM 3353 CE1 TYR B 102 -24.883 46.006 63.224 1.00 32.32 C ANISOU 3353 CE1 TYR B 102 4226 4020 4034 85 133 -505 C ATOM 3354 CE2 TYR B 102 -26.461 44.252 63.561 1.00 28.85 C ANISOU 3354 CE2 TYR B 102 3787 3618 3558 104 164 -416 C ATOM 3355 CZ TYR B 102 -26.144 45.592 63.591 1.00 37.03 C ANISOU 3355 CZ TYR B 102 4821 4629 4622 103 165 -470 C ATOM 3356 OH TYR B 102 -27.097 46.511 63.999 1.00 38.42 O ANISOU 3356 OH TYR B 102 4991 4788 4818 119 203 -488 O ATOM 3357 N PHE B 103 -24.938 41.599 60.047 1.00 24.66 N ANISOU 3357 N PHE B 103 3234 3057 3080 33 74 -300 N ATOM 3358 CA PHE B 103 -26.171 41.471 59.262 1.00 28.49 C ANISOU 3358 CA PHE B 103 3696 3524 3604 28 91 -263 C ATOM 3359 C PHE B 103 -27.290 42.255 59.942 1.00 26.89 C ANISOU 3359 C PHE B 103 3487 3319 3411 49 128 -273 C ATOM 3360 O PHE B 103 -28.094 41.727 60.712 1.00 27.52 O ANISOU 3360 O PHE B 103 3567 3418 3470 62 156 -258 O ATOM 3361 CB PHE B 103 -26.551 40.008 59.077 1.00 25.73 C ANISOU 3361 CB PHE B 103 3343 3189 3246 21 94 -219 C ATOM 3362 CG PHE B 103 -25.890 39.377 57.883 1.00 24.41 C ANISOU 3362 CG PHE B 103 3169 3010 3094 -3 63 -201 C ATOM 3363 CD1 PHE B 103 -26.457 39.503 56.624 1.00 27.76 C ANISOU 3363 CD1 PHE B 103 3570 3417 3563 -16 56 -182 C ATOM 3364 CD2 PHE B 103 -24.672 38.729 58.007 1.00 24.17 C ANISOU 3364 CD2 PHE B 103 3157 2991 3035 -8 40 -206 C ATOM 3365 CE1 PHE B 103 -25.833 38.962 55.508 1.00 27.15 C ANISOU 3365 CE1 PHE B 103 3487 3332 3497 -36 28 -170 C ATOM 3366 CE2 PHE B 103 -24.046 38.165 56.899 1.00 26.51 C ANISOU 3366 CE2 PHE B 103 3449 3277 3347 -29 13 -191 C ATOM 3367 CZ PHE B 103 -24.627 38.264 55.650 1.00 23.74 C ANISOU 3367 CZ PHE B 103 3076 2908 3038 -44 8 -174 C ATOM 3368 N VAL B 104 -27.322 43.554 59.648 1.00 28.05 N ANISOU 3368 N VAL B 104 3627 3439 3592 52 132 -299 N ATOM 3369 CA VAL B 104 -28.358 44.424 60.195 1.00 29.18 C ANISOU 3369 CA VAL B 104 3762 3573 3750 72 169 -311 C ATOM 3370 C VAL B 104 -29.738 43.858 59.885 1.00 34.01 C ANISOU 3370 C VAL B 104 4351 4190 4381 77 191 -265 C ATOM 3371 O VAL B 104 -30.645 43.888 60.726 1.00 34.54 O ANISOU 3371 O VAL B 104 4416 4269 4438 95 225 -264 O ATOM 3372 CB VAL B 104 -28.207 45.846 59.626 1.00 35.31 C ANISOU 3372 CB VAL B 104 4530 4310 4574 74 171 -335 C ATOM 3373 CG1 VAL B 104 -29.312 46.758 60.173 1.00 41.53 C ANISOU 3373 CG1 VAL B 104 5310 5087 5383 97 213 -346 C ATOM 3374 CG2 VAL B 104 -26.838 46.418 59.943 1.00 35.62 C ANISOU 3374 CG2 VAL B 104 4588 4342 4603 65 152 -386 C ATOM 3375 N PHE B 105 -29.920 43.341 58.665 1.00 31.92 N ANISOU 3375 N PHE B 105 4066 3919 4144 60 172 -230 N ATOM 3376 CA PHE B 105 -31.207 42.811 58.229 1.00 37.22 C ANISOU 3376 CA PHE B 105 4707 4596 4840 60 188 -192 C ATOM 3377 C PHE B 105 -31.526 41.442 58.805 1.00 39.83 C ANISOU 3377 C PHE B 105 5040 4951 5142 54 199 -170 C ATOM 3378 O PHE B 105 -32.509 40.834 58.362 1.00 35.52 O ANISOU 3378 O PHE B 105 4466 4410 4620 47 210 -141 O ATOM 3379 CB PHE B 105 -31.279 42.638 56.709 1.00 41.78 C ANISOU 3379 CB PHE B 105 5260 5165 5451 44 160 -165 C ATOM 3380 CG PHE B 105 -30.899 43.832 55.915 1.00 47.75 C ANISOU 3380 CG PHE B 105 6011 5896 6236 50 149 -174 C ATOM 3381 CD1 PHE B 105 -31.238 45.106 56.328 1.00 42.58 C ANISOU 3381 CD1 PHE B 105 5357 5221 5602 72 175 -192 C ATOM 3382 CD2 PHE B 105 -30.231 43.662 54.696 1.00 45.92 C ANISOU 3382 CD2 PHE B 105 5774 5658 6016 35 116 -161 C ATOM 3383 CE1 PHE B 105 -30.897 46.206 55.554 1.00 53.89 C ANISOU 3383 CE1 PHE B 105 6784 6623 7067 80 170 -195 C ATOM 3384 CE2 PHE B 105 -29.881 44.750 53.922 1.00 44.21 C ANISOU 3384 CE2 PHE B 105 5553 5416 5827 43 110 -162 C ATOM 3385 CZ PHE B 105 -30.221 46.032 54.348 1.00 50.70 C ANISOU 3385 CZ PHE B 105 6376 6215 6674 66 139 -178 C ATOM 3386 N GLY B 106 -30.683 40.893 59.677 1.00 33.59 N ANISOU 3386 N GLY B 106 4280 4176 4306 55 197 -182 N ATOM 3387 CA GLY B 106 -30.964 39.614 60.285 1.00 28.33 C ANISOU 3387 CA GLY B 106 3619 3530 3615 55 215 -156 C ATOM 3388 C GLY B 106 -30.871 38.425 59.344 1.00 29.54 C ANISOU 3388 C GLY B 106 3759 3679 3786 28 197 -126 C ATOM 3389 O GLY B 106 -30.239 38.476 58.279 1.00 29.63 O ANISOU 3389 O GLY B 106 3766 3680 3814 10 162 -129 O ATOM 3390 N PRO B 107 -31.486 37.307 59.753 1.00 29.33 N ANISOU 3390 N PRO B 107 3727 3661 3757 26 225 -98 N ATOM 3391 CA PRO B 107 -31.450 36.095 58.913 1.00 24.58 C ANISOU 3391 CA PRO B 107 3111 3052 3176 -2 214 -74 C ATOM 3392 C PRO B 107 -32.016 36.305 57.524 1.00 29.80 C ANISOU 3392 C PRO B 107 3735 3703 3886 -22 192 -72 C ATOM 3393 O PRO B 107 -31.552 35.651 56.587 1.00 28.67 O ANISOU 3393 O PRO B 107 3586 3554 3754 -45 166 -68 O ATOM 3394 CB PRO B 107 -32.279 35.086 59.720 1.00 28.47 C ANISOU 3394 CB PRO B 107 3599 3550 3669 2 261 -46 C ATOM 3395 CG PRO B 107 -32.069 35.528 61.170 1.00 30.51 C ANISOU 3395 CG PRO B 107 3888 3827 3876 36 287 -54 C ATOM 3396 CD PRO B 107 -32.017 37.039 61.108 1.00 32.61 C ANISOU 3396 CD PRO B 107 4154 4092 4143 49 270 -89 C ATOM 3397 N THR B 108 -33.003 37.195 57.360 1.00 25.42 N ANISOU 3397 N THR B 108 3153 3147 3357 -12 204 -76 N ATOM 3398 CA THR B 108 -33.511 37.489 56.025 1.00 27.56 C ANISOU 3398 CA THR B 108 3388 3416 3668 -24 180 -73 C ATOM 3399 C THR B 108 -32.412 38.018 55.118 1.00 25.72 C ANISOU 3399 C THR B 108 3168 3175 3429 -29 138 -85 C ATOM 3400 O THR B 108 -32.305 37.591 53.965 1.00 27.41 O ANISOU 3400 O THR B 108 3364 3391 3659 -48 110 -79 O ATOM 3401 CB THR B 108 -34.665 38.484 56.103 1.00 31.34 C ANISOU 3401 CB THR B 108 3838 3897 4171 -4 201 -72 C ATOM 3402 OG1 THR B 108 -35.700 37.907 56.894 1.00 31.59 O ANISOU 3402 OG1 THR B 108 3854 3936 4212 -2 243 -59 O ATOM 3403 CG2 THR B 108 -35.209 38.785 54.702 1.00 34.95 C ANISOU 3403 CG2 THR B 108 4254 4360 4665 -11 175 -65 C ATOM 3404 N GLY B 109 -31.571 38.931 55.626 1.00 25.90 N ANISOU 3404 N GLY B 109 3221 3189 3429 -13 133 -105 N ATOM 3405 CA GLY B 109 -30.461 39.432 54.828 1.00 25.18 C ANISOU 3405 CA GLY B 109 3143 3088 3338 -19 98 -116 C ATOM 3406 C GLY B 109 -29.445 38.355 54.503 1.00 28.16 C ANISOU 3406 C GLY B 109 3536 3467 3696 -40 73 -113 C ATOM 3407 O GLY B 109 -28.907 38.305 53.384 1.00 25.40 O ANISOU 3407 O GLY B 109 3180 3113 3356 -53 44 -111 O ATOM 3408 N CYS B 110 -29.176 37.470 55.476 1.00 22.39 N ANISOU 3408 N CYS B 110 2826 2744 2936 -41 88 -111 N ATOM 3409 CA CYS B 110 -28.286 36.336 55.238 1.00 21.87 C ANISOU 3409 CA CYS B 110 2774 2679 2855 -58 72 -103 C ATOM 3410 C CYS B 110 -28.830 35.424 54.138 1.00 24.93 C ANISOU 3410 C CYS B 110 3134 3065 3274 -82 64 -87 C ATOM 3411 O CYS B 110 -28.075 34.972 53.272 1.00 23.42 O ANISOU 3411 O CYS B 110 2945 2869 3083 -98 37 -87 O ATOM 3412 CB CYS B 110 -28.103 35.555 56.543 1.00 23.31 C ANISOU 3412 CB CYS B 110 2980 2872 3003 -47 98 -95 C ATOM 3413 SG CYS B 110 -27.013 34.115 56.479 1.00 23.51 S ANISOU 3413 SG CYS B 110 3026 2897 3008 -60 86 -80 S ATOM 3414 N ASN B 111 -30.145 35.158 54.151 1.00 23.75 N ANISOU 3414 N ASN B 111 2955 2920 3150 -85 88 -75 N ATOM 3415 CA ASN B 111 -30.766 34.342 53.105 1.00 24.78 C ANISOU 3415 CA ASN B 111 3051 3052 3312 -110 80 -68 C ATOM 3416 C ASN B 111 -30.623 34.981 51.729 1.00 27.27 C ANISOU 3416 C ASN B 111 3348 3373 3641 -114 42 -76 C ATOM 3417 O ASN B 111 -30.388 34.280 50.736 1.00 24.62 O ANISOU 3417 O ASN B 111 3000 3040 3313 -135 20 -78 O ATOM 3418 CB ASN B 111 -32.251 34.110 53.410 1.00 25.43 C ANISOU 3418 CB ASN B 111 3099 3141 3424 -112 113 -59 C ATOM 3419 CG ASN B 111 -32.474 33.060 54.490 1.00 29.19 C ANISOU 3419 CG ASN B 111 3586 3609 3895 -115 155 -45 C ATOM 3420 OD1 ASN B 111 -31.581 32.286 54.812 1.00 27.50 O ANISOU 3420 OD1 ASN B 111 3401 3386 3660 -119 156 -39 O ATOM 3421 ND2 ASN B 111 -33.683 33.033 55.054 1.00 30.56 N ANISOU 3421 ND2 ASN B 111 3735 3786 4089 -110 192 -36 N ATOM 3422 N LEU B 112 -30.811 36.301 51.638 1.00 22.50 N ANISOU 3422 N LEU B 112 2740 2771 3039 -93 38 -79 N ATOM 3423 CA LEU B 112 -30.676 36.986 50.349 1.00 21.75 C ANISOU 3423 CA LEU B 112 2629 2682 2955 -90 8 -79 C ATOM 3424 C LEU B 112 -29.258 36.868 49.812 1.00 24.61 C ANISOU 3424 C LEU B 112 3018 3034 3298 -98 -20 -85 C ATOM 3425 O LEU B 112 -29.044 36.553 48.630 1.00 22.05 O ANISOU 3425 O LEU B 112 2680 2719 2978 -109 -46 -83 O ATOM 3426 CB LEU B 112 -31.040 38.465 50.506 1.00 26.15 C ANISOU 3426 CB LEU B 112 3182 3234 3521 -61 17 -78 C ATOM 3427 CG LEU B 112 -32.529 38.749 50.684 1.00 31.76 C ANISOU 3427 CG LEU B 112 3855 3957 4255 -48 40 -68 C ATOM 3428 CD1 LEU B 112 -32.738 40.168 51.077 1.00 29.78 C ANISOU 3428 CD1 LEU B 112 3609 3695 4012 -18 57 -69 C ATOM 3429 CD2 LEU B 112 -33.255 38.450 49.386 1.00 35.91 C ANISOU 3429 CD2 LEU B 112 4336 4508 4799 -55 18 -59 C ATOM 3430 N GLU B 113 -28.276 37.141 50.673 1.00 21.32 N ANISOU 3430 N GLU B 113 2637 2603 2860 -92 -16 -94 N ATOM 3431 CA GLU B 113 -26.879 37.137 50.258 1.00 22.03 C ANISOU 3431 CA GLU B 113 2752 2684 2935 -98 -40 -101 C ATOM 3432 C GLU B 113 -26.471 35.749 49.781 1.00 22.76 C ANISOU 3432 C GLU B 113 2845 2780 3021 -121 -53 -97 C ATOM 3433 O GLU B 113 -25.888 35.588 48.697 1.00 23.32 O ANISOU 3433 O GLU B 113 2914 2852 3094 -131 -78 -97 O ATOM 3434 CB GLU B 113 -26.009 37.590 51.447 1.00 23.48 C ANISOU 3434 CB GLU B 113 2968 2858 3096 -87 -32 -118 C ATOM 3435 CG GLU B 113 -24.768 38.415 51.113 1.00 20.89 C ANISOU 3435 CG GLU B 113 2657 2516 2766 -84 -51 -132 C ATOM 3436 CD GLU B 113 -23.615 37.549 50.597 1.00 23.16 C ANISOU 3436 CD GLU B 113 2958 2804 3039 -100 -75 -130 C ATOM 3437 OE1 GLU B 113 -23.509 36.379 51.035 1.00 23.40 O ANISOU 3437 OE1 GLU B 113 2996 2842 3053 -109 -71 -125 O ATOM 3438 OE2 GLU B 113 -22.820 38.050 49.756 1.00 21.46 O ANISOU 3438 OE2 GLU B 113 2743 2578 2831 -103 -93 -133 O ATOM 3439 N GLY B 114 -26.785 34.729 50.579 1.00 21.01 N ANISOU 3439 N GLY B 114 2628 2560 2795 -129 -32 -93 N ATOM 3440 CA GLY B 114 -26.398 33.372 50.223 1.00 22.15 C ANISOU 3440 CA GLY B 114 2775 2700 2939 -150 -36 -89 C ATOM 3441 C GLY B 114 -27.146 32.826 49.020 1.00 20.98 C ANISOU 3441 C GLY B 114 2594 2562 2818 -170 -47 -91 C ATOM 3442 O GLY B 114 -26.550 32.209 48.127 1.00 20.84 O ANISOU 3442 O GLY B 114 2576 2544 2800 -186 -67 -96 O ATOM 3443 N PHE B 115 -28.459 33.059 48.967 1.00 21.37 N ANISOU 3443 N PHE B 115 2609 2622 2887 -169 -35 -89 N ATOM 3444 CA PHE B 115 -29.272 32.504 47.889 1.00 21.37 C ANISOU 3444 CA PHE B 115 2570 2639 2912 -188 -46 -96 C ATOM 3445 C PHE B 115 -28.832 33.040 46.527 1.00 24.01 C ANISOU 3445 C PHE B 115 2896 2989 3239 -184 -84 -101 C ATOM 3446 O PHE B 115 -28.628 32.269 45.579 1.00 21.66 O ANISOU 3446 O PHE B 115 2587 2698 2943 -204 -102 -112 O ATOM 3447 CB PHE B 115 -30.754 32.822 48.123 1.00 23.00 C ANISOU 3447 CB PHE B 115 2738 2859 3142 -183 -28 -93 C ATOM 3448 CG PHE B 115 -31.638 32.428 46.965 1.00 22.60 C ANISOU 3448 CG PHE B 115 2639 2833 3113 -199 -46 -106 C ATOM 3449 CD1 PHE B 115 -32.022 31.116 46.801 1.00 25.18 C ANISOU 3449 CD1 PHE B 115 2946 3158 3464 -231 -36 -120 C ATOM 3450 CD2 PHE B 115 -32.071 33.388 46.040 1.00 25.54 C ANISOU 3450 CD2 PHE B 115 2985 3234 3485 -181 -71 -104 C ATOM 3451 CE1 PHE B 115 -32.846 30.739 45.715 1.00 23.31 C ANISOU 3451 CE1 PHE B 115 2660 2949 3248 -248 -55 -140 C ATOM 3452 CE2 PHE B 115 -32.882 33.028 44.961 1.00 27.09 C ANISOU 3452 CE2 PHE B 115 3133 3464 3695 -193 -92 -118 C ATOM 3453 CZ PHE B 115 -33.264 31.707 44.803 1.00 26.81 C ANISOU 3453 CZ PHE B 115 3075 3429 3682 -228 -86 -140 C ATOM 3454 N PHE B 116 -28.681 34.361 46.401 1.00 21.17 N ANISOU 3454 N PHE B 116 2541 2632 2870 -159 -93 -93 N ATOM 3455 CA PHE B 116 -28.390 34.896 45.071 1.00 22.04 C ANISOU 3455 CA PHE B 116 2640 2758 2974 -151 -123 -91 C ATOM 3456 C PHE B 116 -26.977 34.571 44.603 1.00 21.79 C ANISOU 3456 C PHE B 116 2638 2715 2924 -159 -140 -94 C ATOM 3457 O PHE B 116 -26.751 34.426 43.389 1.00 23.54 O ANISOU 3457 O PHE B 116 2848 2954 3140 -162 -164 -97 O ATOM 3458 CB PHE B 116 -28.670 36.397 45.022 1.00 26.46 C ANISOU 3458 CB PHE B 116 3195 3321 3538 -119 -120 -76 C ATOM 3459 CG PHE B 116 -30.140 36.689 44.834 1.00 24.28 C ANISOU 3459 CG PHE B 116 2875 3070 3279 -108 -114 -70 C ATOM 3460 CD1 PHE B 116 -30.754 36.416 43.617 1.00 25.31 C ANISOU 3460 CD1 PHE B 116 2967 3237 3411 -110 -138 -71 C ATOM 3461 CD2 PHE B 116 -30.916 37.151 45.886 1.00 25.07 C ANISOU 3461 CD2 PHE B 116 2971 3162 3394 -96 -86 -66 C ATOM 3462 CE1 PHE B 116 -32.115 36.623 43.434 1.00 26.90 C ANISOU 3462 CE1 PHE B 116 3124 3469 3629 -99 -136 -68 C ATOM 3463 CE2 PHE B 116 -32.288 37.374 45.717 1.00 25.90 C ANISOU 3463 CE2 PHE B 116 3032 3292 3518 -86 -79 -60 C ATOM 3464 CZ PHE B 116 -32.892 37.100 44.489 1.00 28.95 C ANISOU 3464 CZ PHE B 116 3376 3716 3906 -88 -105 -61 C ATOM 3465 N ALA B 117 -26.020 34.447 45.526 1.00 22.58 N ANISOU 3465 N ALA B 117 2775 2791 3015 -161 -130 -96 N ATOM 3466 CA ALA B 117 -24.670 34.066 45.125 1.00 22.77 C ANISOU 3466 CA ALA B 117 2823 2803 3023 -169 -145 -99 C ATOM 3467 C ALA B 117 -24.617 32.599 44.709 1.00 25.20 C ANISOU 3467 C ALA B 117 3127 3114 3334 -195 -149 -109 C ATOM 3468 O ALA B 117 -23.967 32.252 43.711 1.00 23.00 O ANISOU 3468 O ALA B 117 2850 2840 3048 -202 -168 -114 O ATOM 3469 CB ALA B 117 -23.679 34.349 46.261 1.00 22.63 C ANISOU 3469 CB ALA B 117 2841 2764 2993 -162 -135 -101 C ATOM 3470 N THR B 118 -25.302 31.728 45.457 1.00 20.94 N ANISOU 3470 N THR B 118 2580 2569 2807 -208 -126 -111 N ATOM 3471 CA THR B 118 -25.349 30.310 45.109 1.00 20.63 C ANISOU 3471 CA THR B 118 2534 2525 2779 -234 -122 -122 C ATOM 3472 C THR B 118 -26.049 30.114 43.772 1.00 20.82 C ANISOU 3472 C THR B 118 2521 2575 2814 -247 -143 -139 C ATOM 3473 O THR B 118 -25.574 29.369 42.906 1.00 21.12 O ANISOU 3473 O THR B 118 2559 2616 2851 -263 -157 -154 O ATOM 3474 CB THR B 118 -26.088 29.528 46.199 1.00 21.98 C ANISOU 3474 CB THR B 118 2701 2682 2968 -243 -86 -118 C ATOM 3475 OG1 THR B 118 -25.463 29.759 47.472 1.00 21.28 O ANISOU 3475 OG1 THR B 118 2646 2578 2861 -226 -69 -102 O ATOM 3476 CG2 THR B 118 -26.087 28.022 45.899 1.00 21.23 C ANISOU 3476 CG2 THR B 118 2601 2572 2894 -272 -74 -129 C ATOM 3477 N LEU B 119 -27.187 30.791 43.595 1.00 21.29 N ANISOU 3477 N LEU B 119 2548 2658 2883 -238 -146 -138 N ATOM 3478 CA LEU B 119 -27.929 30.714 42.341 1.00 24.21 C ANISOU 3478 CA LEU B 119 2878 3064 3258 -244 -169 -154 C ATOM 3479 C LEU B 119 -27.076 31.176 41.169 1.00 22.71 C ANISOU 3479 C LEU B 119 2697 2891 3042 -232 -200 -153 C ATOM 3480 O LEU B 119 -27.012 30.505 40.131 1.00 25.04 O ANISOU 3480 O LEU B 119 2977 3206 3331 -246 -219 -174 O ATOM 3481 CB LEU B 119 -29.202 31.558 42.434 1.00 22.40 C ANISOU 3481 CB LEU B 119 2613 2859 3039 -227 -167 -147 C ATOM 3482 CG LEU B 119 -30.071 31.592 41.164 1.00 27.44 C ANISOU 3482 CG LEU B 119 3203 3546 3678 -227 -194 -162 C ATOM 3483 CD1 LEU B 119 -30.859 30.279 41.002 1.00 27.96 C ANISOU 3483 CD1 LEU B 119 3233 3620 3771 -264 -189 -196 C ATOM 3484 CD2 LEU B 119 -31.034 32.794 41.228 1.00 30.07 C ANISOU 3484 CD2 LEU B 119 3509 3903 4013 -196 -195 -143 C ATOM 3485 N GLY B 120 -26.429 32.334 41.300 1.00 21.84 N ANISOU 3485 N GLY B 120 2610 2774 2916 -204 -203 -130 N ATOM 3486 CA GLY B 120 -25.643 32.846 40.179 1.00 24.79 C ANISOU 3486 CA GLY B 120 2991 3161 3267 -190 -226 -124 C ATOM 3487 C GLY B 120 -24.470 31.946 39.826 1.00 25.74 C ANISOU 3487 C GLY B 120 3136 3266 3377 -208 -233 -136 C ATOM 3488 O GLY B 120 -24.172 31.723 38.649 1.00 23.75 O ANISOU 3488 O GLY B 120 2877 3038 3110 -208 -253 -144 O ATOM 3489 N GLY B 121 -23.787 31.428 40.844 1.00 22.66 N ANISOU 3489 N GLY B 121 2775 2841 2993 -219 -215 -136 N ATOM 3490 CA GLY B 121 -22.660 30.542 40.607 1.00 23.62 C ANISOU 3490 CA GLY B 121 2920 2946 3108 -234 -217 -144 C ATOM 3491 C GLY B 121 -23.085 29.225 39.985 1.00 22.46 C ANISOU 3491 C GLY B 121 2755 2808 2972 -261 -220 -171 C ATOM 3492 O GLY B 121 -22.410 28.704 39.093 1.00 22.63 O ANISOU 3492 O GLY B 121 2781 2834 2982 -268 -232 -183 O ATOM 3493 N GLU B 122 -24.233 28.685 40.414 1.00 20.86 N ANISOU 3493 N GLU B 122 2526 2607 2791 -276 -206 -183 N ATOM 3494 CA GLU B 122 -24.696 27.428 39.826 1.00 20.95 C ANISOU 3494 CA GLU B 122 2516 2624 2821 -306 -205 -215 C ATOM 3495 C GLU B 122 -25.267 27.622 38.422 1.00 21.90 C ANISOU 3495 C GLU B 122 2601 2793 2929 -306 -236 -237 C ATOM 3496 O GLU B 122 -25.155 26.715 37.580 1.00 21.70 O ANISOU 3496 O GLU B 122 2564 2776 2904 -326 -245 -269 O ATOM 3497 CB GLU B 122 -25.712 26.746 40.751 1.00 21.19 C ANISOU 3497 CB GLU B 122 2528 2637 2887 -326 -174 -221 C ATOM 3498 CG GLU B 122 -25.051 26.042 41.968 1.00 21.64 C ANISOU 3498 CG GLU B 122 2621 2647 2955 -330 -140 -204 C ATOM 3499 CD GLU B 122 -24.206 24.840 41.572 1.00 25.29 C ANISOU 3499 CD GLU B 122 3098 3085 3425 -349 -133 -219 C ATOM 3500 OE1 GLU B 122 -24.536 24.224 40.544 1.00 25.90 O ANISOU 3500 OE1 GLU B 122 3151 3176 3514 -371 -145 -253 O ATOM 3501 OE2 GLU B 122 -23.204 24.518 42.269 1.00 24.17 O ANISOU 3501 OE2 GLU B 122 2993 2914 3277 -341 -117 -199 O ATOM 3502 N ILE B 123 -25.886 28.771 38.129 1.00 21.27 N ANISOU 3502 N ILE B 123 2500 2746 2835 -281 -252 -222 N ATOM 3503 CA ILE B 123 -26.291 29.008 36.743 1.00 21.53 C ANISOU 3503 CA ILE B 123 2502 2834 2846 -272 -284 -238 C ATOM 3504 C ILE B 123 -25.066 29.004 35.834 1.00 23.07 C ANISOU 3504 C ILE B 123 2724 3033 3011 -263 -299 -236 C ATOM 3505 O ILE B 123 -25.099 28.465 34.716 1.00 24.73 O ANISOU 3505 O ILE B 123 2916 3276 3204 -270 -319 -265 O ATOM 3506 CB ILE B 123 -27.088 30.317 36.616 1.00 22.54 C ANISOU 3506 CB ILE B 123 2607 2995 2963 -238 -294 -213 C ATOM 3507 CG1 ILE B 123 -28.504 30.098 37.159 1.00 26.05 C ANISOU 3507 CG1 ILE B 123 3011 3450 3437 -251 -284 -226 C ATOM 3508 CG2 ILE B 123 -27.131 30.775 35.112 1.00 23.08 C ANISOU 3508 CG2 ILE B 123 2654 3121 2994 -214 -328 -214 C ATOM 3509 CD1 ILE B 123 -29.301 31.369 37.339 1.00 29.74 C ANISOU 3509 CD1 ILE B 123 3458 3939 3901 -217 -286 -197 C ATOM 3510 N ALA B 124 -23.963 29.593 36.300 1.00 21.00 N ANISOU 3510 N ALA B 124 2501 2737 2740 -247 -289 -206 N ATOM 3511 CA ALA B 124 -22.735 29.587 35.504 1.00 25.84 C ANISOU 3511 CA ALA B 124 3139 3351 3329 -239 -299 -202 C ATOM 3512 C ALA B 124 -22.208 28.163 35.289 1.00 23.14 C ANISOU 3512 C ALA B 124 2807 2992 2995 -269 -295 -234 C ATOM 3513 O ALA B 124 -21.865 27.787 34.169 1.00 23.79 O ANISOU 3513 O ALA B 124 2884 3098 3056 -270 -311 -254 O ATOM 3514 CB ALA B 124 -21.680 30.475 36.178 1.00 21.83 C ANISOU 3514 CB ALA B 124 2668 2808 2820 -220 -287 -167 C ATOM 3515 N LEU B 125 -22.144 27.349 36.347 1.00 20.78 N ANISOU 3515 N LEU B 125 2520 2650 2724 -292 -270 -240 N ATOM 3516 CA LEU B 125 -21.615 25.985 36.203 1.00 20.87 C ANISOU 3516 CA LEU B 125 2541 2638 2749 -318 -259 -267 C ATOM 3517 C LEU B 125 -22.458 25.165 35.234 1.00 22.50 C ANISOU 3517 C LEU B 125 2712 2875 2962 -341 -271 -314 C ATOM 3518 O LEU B 125 -21.933 24.506 34.328 1.00 24.96 O ANISOU 3518 O LEU B 125 3026 3194 3263 -351 -279 -340 O ATOM 3519 CB LEU B 125 -21.555 25.281 37.577 1.00 21.38 C ANISOU 3519 CB LEU B 125 2623 2653 2846 -333 -226 -258 C ATOM 3520 CG LEU B 125 -21.008 23.831 37.631 1.00 25.28 C ANISOU 3520 CG LEU B 125 3130 3111 3362 -358 -204 -278 C ATOM 3521 CD1 LEU B 125 -19.669 23.698 36.892 1.00 23.50 C ANISOU 3521 CD1 LEU B 125 2930 2883 3115 -349 -214 -278 C ATOM 3522 CD2 LEU B 125 -20.850 23.347 39.076 1.00 25.30 C ANISOU 3522 CD2 LEU B 125 3155 3070 3390 -360 -168 -254 C ATOM 3523 N TRP B 126 -23.770 25.177 35.418 1.00 21.54 N ANISOU 3523 N TRP B 126 2553 2772 2858 -352 -272 -328 N ATOM 3524 CA TRP B 126 -24.604 24.374 34.542 1.00 22.01 C ANISOU 3524 CA TRP B 126 2572 2864 2928 -377 -284 -380 C ATOM 3525 C TRP B 126 -24.624 24.955 33.128 1.00 25.28 C ANISOU 3525 C TRP B 126 2968 3343 3296 -356 -323 -392 C ATOM 3526 O TRP B 126 -24.791 24.201 32.167 1.00 24.54 O ANISOU 3526 O TRP B 126 2853 3277 3196 -373 -338 -440 O ATOM 3527 CB TRP B 126 -26.005 24.231 35.152 1.00 26.39 C ANISOU 3527 CB TRP B 126 3087 3422 3517 -394 -273 -393 C ATOM 3528 CG TRP B 126 -26.027 23.261 36.330 1.00 24.85 C ANISOU 3528 CG TRP B 126 2906 3165 3372 -421 -229 -392 C ATOM 3529 CD1 TRP B 126 -26.129 23.568 37.678 1.00 26.11 C ANISOU 3529 CD1 TRP B 126 3084 3290 3548 -412 -200 -353 C ATOM 3530 CD2 TRP B 126 -25.946 21.828 36.256 1.00 24.62 C ANISOU 3530 CD2 TRP B 126 2873 3101 3380 -458 -205 -430 C ATOM 3531 NE1 TRP B 126 -26.108 22.406 38.422 1.00 23.99 N ANISOU 3531 NE1 TRP B 126 2823 2970 3322 -439 -160 -360 N ATOM 3532 CE2 TRP B 126 -25.998 21.331 37.572 1.00 25.05 C ANISOU 3532 CE2 TRP B 126 2945 3100 3473 -468 -161 -406 C ATOM 3533 CE3 TRP B 126 -25.817 20.917 35.193 1.00 28.04 C ANISOU 3533 CE3 TRP B 126 3291 3545 3818 -483 -215 -484 C ATOM 3534 CZ2 TRP B 126 -25.933 19.965 37.855 1.00 25.70 C ANISOU 3534 CZ2 TRP B 126 3029 3133 3603 -500 -122 -428 C ATOM 3535 CZ3 TRP B 126 -25.754 19.559 35.479 1.00 27.71 C ANISOU 3535 CZ3 TRP B 126 3251 3452 3827 -519 -178 -512 C ATOM 3536 CH2 TRP B 126 -25.814 19.099 36.799 1.00 27.49 C ANISOU 3536 CH2 TRP B 126 3241 3365 3841 -526 -130 -481 C ATOM 3537 N SER B 127 -24.397 26.275 32.975 1.00 22.01 N ANISOU 3537 N SER B 127 2564 2951 2848 -316 -338 -349 N ATOM 3538 CA SER B 127 -24.219 26.858 31.636 1.00 23.84 C ANISOU 3538 CA SER B 127 2786 3241 3031 -288 -369 -349 C ATOM 3539 C SER B 127 -22.985 26.286 30.926 1.00 25.51 C ANISOU 3539 C SER B 127 3027 3443 3223 -291 -369 -362 C ATOM 3540 O SER B 127 -22.994 26.113 29.702 1.00 27.06 O ANISOU 3540 O SER B 127 3207 3689 3384 -284 -392 -388 O ATOM 3541 CB SER B 127 -24.092 28.388 31.731 1.00 24.31 C ANISOU 3541 CB SER B 127 2856 3312 3068 -244 -373 -292 C ATOM 3542 OG SER B 127 -25.339 28.995 32.040 1.00 24.70 O ANISOU 3542 OG SER B 127 2871 3388 3128 -233 -378 -284 O ATOM 3543 N LEU B 128 -21.897 26.051 31.673 1.00 24.02 N ANISOU 3543 N LEU B 128 2881 3195 3052 -298 -344 -341 N ATOM 3544 CA LEU B 128 -20.700 25.442 31.092 1.00 24.51 C ANISOU 3544 CA LEU B 128 2969 3242 3100 -302 -341 -352 C ATOM 3545 C LEU B 128 -20.961 24.001 30.664 1.00 28.98 C ANISOU 3545 C LEU B 128 3520 3806 3684 -338 -338 -412 C ATOM 3546 O LEU B 128 -20.392 23.534 29.667 1.00 28.17 O ANISOU 3546 O LEU B 128 3423 3723 3559 -339 -346 -438 O ATOM 3547 CB LEU B 128 -19.523 25.499 32.072 1.00 23.23 C ANISOU 3547 CB LEU B 128 2851 3020 2956 -299 -316 -317 C ATOM 3548 CG LEU B 128 -19.050 26.892 32.517 1.00 27.21 C ANISOU 3548 CG LEU B 128 3373 3517 3448 -267 -315 -264 C ATOM 3549 CD1 LEU B 128 -17.961 26.789 33.583 1.00 25.40 C ANISOU 3549 CD1 LEU B 128 3179 3232 3238 -270 -293 -241 C ATOM 3550 CD2 LEU B 128 -18.547 27.679 31.307 1.00 30.89 C ANISOU 3550 CD2 LEU B 128 3841 4022 3874 -237 -332 -248 C ATOM 3551 N VAL B 129 -21.791 23.275 31.424 1.00 24.72 N ANISOU 3551 N VAL B 129 2961 3241 3188 -369 -321 -435 N ATOM 3552 CA VAL B 129 -22.223 21.936 31.013 1.00 24.14 C ANISOU 3552 CA VAL B 129 2865 3164 3141 -408 -315 -498 C ATOM 3553 C VAL B 129 -22.931 21.999 29.663 1.00 26.12 C ANISOU 3553 C VAL B 129 3075 3491 3358 -406 -352 -544 C ATOM 3554 O VAL B 129 -22.643 21.214 28.755 1.00 31.51 O ANISOU 3554 O VAL B 129 3754 4189 4031 -420 -358 -593 O ATOM 3555 CB VAL B 129 -23.124 21.320 32.103 1.00 26.00 C ANISOU 3555 CB VAL B 129 3084 3361 3435 -439 -287 -508 C ATOM 3556 CG1 VAL B 129 -23.765 20.012 31.613 1.00 29.73 C ANISOU 3556 CG1 VAL B 129 3523 3832 3943 -482 -280 -580 C ATOM 3557 CG2 VAL B 129 -22.331 21.086 33.358 1.00 24.71 C ANISOU 3557 CG2 VAL B 129 2962 3128 3298 -438 -250 -466 C ATOM 3558 N VAL B 130 -23.859 22.949 29.501 1.00 25.87 N ANISOU 3558 N VAL B 130 3013 3512 3306 -385 -377 -530 N ATOM 3559 CA VAL B 130 -24.575 23.094 28.229 1.00 26.51 C ANISOU 3559 CA VAL B 130 3050 3676 3346 -375 -415 -570 C ATOM 3560 C VAL B 130 -23.611 23.428 27.094 1.00 28.38 C ANISOU 3560 C VAL B 130 3310 3950 3524 -344 -433 -562 C ATOM 3561 O VAL B 130 -23.691 22.861 25.994 1.00 28.33 O ANISOU 3561 O VAL B 130 3284 3992 3490 -350 -454 -616 O ATOM 3562 CB VAL B 130 -25.674 24.163 28.362 1.00 25.57 C ANISOU 3562 CB VAL B 130 2897 3605 3215 -350 -435 -543 C ATOM 3563 CG1 VAL B 130 -26.275 24.477 26.987 1.00 30.33 C ANISOU 3563 CG1 VAL B 130 3458 4304 3762 -326 -479 -572 C ATOM 3564 CG2 VAL B 130 -26.770 23.636 29.317 1.00 26.69 C ANISOU 3564 CG2 VAL B 130 3007 3719 3416 -386 -418 -566 C ATOM 3565 N LEU B 131 -22.693 24.366 27.333 1.00 26.55 N ANISOU 3565 N LEU B 131 3118 3698 3272 -309 -425 -497 N ATOM 3566 CA LEU B 131 -21.737 24.724 26.282 1.00 27.29 C ANISOU 3566 CA LEU B 131 3233 3823 3313 -278 -436 -483 C ATOM 3567 C LEU B 131 -20.808 23.562 25.939 1.00 32.86 C ANISOU 3567 C LEU B 131 3962 4497 4025 -303 -421 -522 C ATOM 3568 O LEU B 131 -20.434 23.378 24.773 1.00 30.84 O ANISOU 3568 O LEU B 131 3706 4286 3726 -290 -436 -547 O ATOM 3569 CB LEU B 131 -20.914 25.936 26.709 1.00 23.65 C ANISOU 3569 CB LEU B 131 2808 3335 2842 -241 -423 -407 C ATOM 3570 CG LEU B 131 -21.694 27.250 26.724 1.00 31.32 C ANISOU 3570 CG LEU B 131 3760 4346 3796 -205 -437 -364 C ATOM 3571 CD1 LEU B 131 -20.882 28.343 27.423 1.00 33.97 C ANISOU 3571 CD1 LEU B 131 4132 4635 4141 -180 -415 -296 C ATOM 3572 CD2 LEU B 131 -22.016 27.671 25.308 1.00 34.35 C ANISOU 3572 CD2 LEU B 131 4119 4816 4118 -169 -467 -369 C ATOM 3573 N ALA B 132 -20.379 22.803 26.945 1.00 26.63 N ANISOU 3573 N ALA B 132 3196 3633 3290 -334 -390 -524 N ATOM 3574 CA ALA B 132 -19.509 21.657 26.680 1.00 26.92 C ANISOU 3574 CA ALA B 132 3254 3634 3340 -357 -371 -560 C ATOM 3575 C ALA B 132 -20.198 20.646 25.784 1.00 29.83 C ANISOU 3575 C ALA B 132 3588 4040 3707 -385 -385 -641 C ATOM 3576 O ALA B 132 -19.590 20.105 24.854 1.00 32.01 O ANISOU 3576 O ALA B 132 3872 4332 3958 -385 -388 -676 O ATOM 3577 CB ALA B 132 -19.096 20.991 27.995 1.00 28.79 C ANISOU 3577 CB ALA B 132 3516 3786 3637 -383 -333 -545 C ATOM 3578 N ILE B 133 -21.473 20.379 26.052 1.00 28.39 N ANISOU 3578 N ILE B 133 3363 3872 3552 -410 -392 -676 N ATOM 3579 CA ILE B 133 -22.235 19.460 25.219 1.00 32.05 C ANISOU 3579 CA ILE B 133 3784 4376 4018 -441 -408 -762 C ATOM 3580 C ILE B 133 -22.407 20.014 23.812 1.00 35.20 C ANISOU 3580 C ILE B 133 4161 4873 4340 -408 -452 -782 C ATOM 3581 O ILE B 133 -22.297 19.273 22.824 1.00 35.40 O ANISOU 3581 O ILE B 133 4175 4932 4345 -420 -462 -847 O ATOM 3582 CB ILE B 133 -23.580 19.165 25.892 1.00 32.49 C ANISOU 3582 CB ILE B 133 3795 4424 4124 -474 -405 -790 C ATOM 3583 CG1 ILE B 133 -23.343 18.287 27.128 1.00 33.74 C ANISOU 3583 CG1 ILE B 133 3976 4485 4359 -509 -355 -782 C ATOM 3584 CG2 ILE B 133 -24.557 18.528 24.907 1.00 35.58 C ANISOU 3584 CG2 ILE B 133 4130 4881 4509 -499 -433 -880 C ATOM 3585 CD1 ILE B 133 -24.532 18.208 28.025 1.00 39.85 C ANISOU 3585 CD1 ILE B 133 4716 5242 5184 -534 -343 -786 C ATOM 3586 N GLU B 134 -22.704 21.315 23.693 1.00 34.52 N ANISOU 3586 N GLU B 134 4068 4836 4210 -364 -475 -727 N ATOM 3587 CA GLU B 134 -22.847 21.937 22.373 1.00 35.61 C ANISOU 3587 CA GLU B 134 4188 5072 4271 -323 -514 -732 C ATOM 3588 C GLU B 134 -21.549 21.845 21.572 1.00 35.89 C ANISOU 3588 C GLU B 134 4263 5109 4263 -301 -506 -724 C ATOM 3589 O GLU B 134 -21.563 21.516 20.379 1.00 38.39 O ANISOU 3589 O GLU B 134 4564 5493 4530 -292 -529 -774 O ATOM 3590 CB GLU B 134 -23.278 23.404 22.527 1.00 35.79 C ANISOU 3590 CB GLU B 134 4203 5131 4263 -275 -529 -660 C ATOM 3591 CG GLU B 134 -23.558 24.126 21.197 1.00 32.11 C ANISOU 3591 CG GLU B 134 3714 4772 3715 -224 -567 -656 C ATOM 3592 CD GLU B 134 -22.401 24.991 20.690 1.00 37.51 C ANISOU 3592 CD GLU B 134 4442 5460 4350 -174 -558 -588 C ATOM 3593 OE1 GLU B 134 -21.335 25.055 21.342 1.00 37.44 O ANISOU 3593 OE1 GLU B 134 4480 5373 4372 -180 -524 -548 O ATOM 3594 OE2 GLU B 134 -22.566 25.618 19.622 1.00 41.45 O ANISOU 3594 OE2 GLU B 134 4925 6043 4779 -126 -583 -574 O ATOM 3595 N ARG B 135 -20.411 22.143 22.206 1.00 30.08 N ANISOU 3595 N ARG B 135 3578 4305 3546 -291 -475 -664 N ATOM 3596 CA ARG B 135 -19.132 21.989 21.511 1.00 33.90 C ANISOU 3596 CA ARG B 135 4099 4784 3998 -274 -464 -657 C ATOM 3597 C ARG B 135 -18.895 20.537 21.095 1.00 45.09 C ANISOU 3597 C ARG B 135 5514 6184 5433 -313 -454 -738 C ATOM 3598 O ARG B 135 -18.406 20.269 19.988 1.00 41.86 O ANISOU 3598 O ARG B 135 5110 5818 4976 -299 -462 -768 O ATOM 3599 CB ARG B 135 -17.986 22.484 22.390 1.00 31.53 C ANISOU 3599 CB ARG B 135 3847 4409 3726 -262 -431 -585 C ATOM 3600 CG ARG B 135 -17.982 24.002 22.626 1.00 32.39 C ANISOU 3600 CG ARG B 135 3962 4532 3812 -219 -436 -506 C ATOM 3601 CD ARG B 135 -17.637 24.776 21.341 1.00 34.46 C ANISOU 3601 CD ARG B 135 4227 4865 4003 -169 -451 -481 C ATOM 3602 NE ARG B 135 -18.804 25.103 20.527 1.00 31.10 N ANISOU 3602 NE ARG B 135 3757 4530 3529 -148 -487 -502 N ATOM 3603 CZ ARG B 135 -18.726 25.548 19.280 1.00 38.46 C ANISOU 3603 CZ ARG B 135 4683 5541 4390 -104 -505 -495 C ATOM 3604 NH1 ARG B 135 -17.559 25.674 18.666 1.00 37.63 N ANISOU 3604 NH1 ARG B 135 4611 5431 4254 -80 -488 -470 N ATOM 3605 NH2 ARG B 135 -19.843 25.873 18.635 1.00 38.35 N ANISOU 3605 NH2 ARG B 135 4626 5613 4332 -81 -540 -511 N ATOM 3606 N TYR B 136 -19.234 19.582 21.967 1.00 40.15 N ANISOU 3606 N TYR B 136 4882 5495 4878 -362 -432 -773 N ATOM 3607 CA TYR B 136 -19.050 18.173 21.618 1.00 41.72 C ANISOU 3607 CA TYR B 136 5078 5668 5104 -402 -416 -852 C ATOM 3608 C TYR B 136 -19.876 17.791 20.385 1.00 45.67 C ANISOU 3608 C TYR B 136 5533 6257 5562 -409 -452 -936 C ATOM 3609 O TYR B 136 -19.354 17.198 19.431 1.00 43.98 O ANISOU 3609 O TYR B 136 5325 6066 5318 -408 -453 -986 O ATOM 3610 CB TYR B 136 -19.389 17.303 22.834 1.00 42.40 C ANISOU 3610 CB TYR B 136 5163 5670 5278 -450 -382 -866 C ATOM 3611 CG TYR B 136 -19.450 15.824 22.547 1.00 49.14 C ANISOU 3611 CG TYR B 136 6004 6492 6174 -496 -361 -952 C ATOM 3612 CD1 TYR B 136 -18.350 15.154 22.021 1.00 52.40 C ANISOU 3612 CD1 TYR B 136 6449 6879 6582 -495 -340 -972 C ATOM 3613 CD2 TYR B 136 -20.603 15.093 22.805 1.00 52.98 C ANISOU 3613 CD2 TYR B 136 6447 6970 6712 -541 -358 -1015 C ATOM 3614 CE1 TYR B 136 -18.401 13.804 21.756 1.00 59.16 C ANISOU 3614 CE1 TYR B 136 7296 7702 7482 -537 -317 -1053 C ATOM 3615 CE2 TYR B 136 -20.663 13.742 22.540 1.00 56.32 C ANISOU 3615 CE2 TYR B 136 6859 7358 7183 -586 -334 -1097 C ATOM 3616 CZ TYR B 136 -19.558 13.103 22.016 1.00 57.80 C ANISOU 3616 CZ TYR B 136 7080 7519 7363 -583 -313 -1116 C ATOM 3617 OH TYR B 136 -19.602 11.756 21.748 1.00 67.00 O ANISOU 3617 OH TYR B 136 8234 8644 8579 -627 -285 -1200 O ATOM 3618 N VAL B 137 -21.160 18.160 20.366 1.00 38.77 N ANISOU 3618 N VAL B 137 4610 5438 4682 -412 -483 -954 N ATOM 3619 CA VAL B 137 -22.010 17.869 19.211 1.00 42.31 C ANISOU 3619 CA VAL B 137 5008 5982 5086 -415 -523 -1036 C ATOM 3620 C VAL B 137 -21.484 18.576 17.963 1.00 50.28 C ANISOU 3620 C VAL B 137 6029 7078 5998 -359 -551 -1018 C ATOM 3621 O VAL B 137 -21.381 17.979 16.885 1.00 56.36 O ANISOU 3621 O VAL B 137 6787 7902 6727 -360 -566 -1088 O ATOM 3622 CB VAL B 137 -23.472 18.263 19.504 1.00 47.32 C ANISOU 3622 CB VAL B 137 5586 6661 5732 -423 -552 -1048 C ATOM 3623 CG1 VAL B 137 -24.323 18.180 18.235 1.00 49.17 C ANISOU 3623 CG1 VAL B 137 5764 7013 5904 -414 -602 -1124 C ATOM 3624 CG2 VAL B 137 -24.068 17.382 20.591 1.00 45.72 C ANISOU 3624 CG2 VAL B 137 5367 6379 5626 -482 -521 -1081 C ATOM 3625 N VAL B 138 -21.141 19.859 18.092 1.00 46.40 N ANISOU 3625 N VAL B 138 5560 6601 5470 -307 -554 -923 N ATOM 3626 CA VAL B 138 -20.748 20.659 16.934 1.00 43.48 C ANISOU 3626 CA VAL B 138 5197 6315 5007 -247 -577 -894 C ATOM 3627 C VAL B 138 -19.436 20.151 16.341 1.00 53.22 C ANISOU 3627 C VAL B 138 6474 7527 6219 -241 -553 -903 C ATOM 3628 O VAL B 138 -19.321 19.950 15.125 1.00 56.09 O ANISOU 3628 O VAL B 138 6829 7967 6516 -220 -573 -946 O ATOM 3629 CB VAL B 138 -20.656 22.146 17.327 1.00 42.24 C ANISOU 3629 CB VAL B 138 5057 6162 4831 -197 -576 -786 C ATOM 3630 CG1 VAL B 138 -19.805 22.920 16.333 1.00 56.39 C ANISOU 3630 CG1 VAL B 138 6875 8004 6546 -136 -577 -736 C ATOM 3631 CG2 VAL B 138 -22.046 22.748 17.411 1.00 43.27 C ANISOU 3631 CG2 VAL B 138 5136 6354 4952 -185 -610 -785 C ATOM 3632 N VAL B 139 -18.426 19.944 17.181 1.00 45.87 N ANISOU 3632 N VAL B 139 5589 6496 5344 -257 -511 -863 N ATOM 3633 CA VAL B 139 -17.105 19.611 16.660 1.00 50.88 C ANISOU 3633 CA VAL B 139 6265 7108 5959 -245 -486 -859 C ATOM 3634 C VAL B 139 -17.011 18.127 16.315 1.00 57.26 C ANISOU 3634 C VAL B 139 7067 7896 6792 -290 -475 -957 C ATOM 3635 O VAL B 139 -16.473 17.761 15.267 1.00 65.77 O ANISOU 3635 O VAL B 139 8154 9015 7821 -276 -477 -995 O ATOM 3636 CB VAL B 139 -16.016 20.040 17.656 1.00 54.49 C ANISOU 3636 CB VAL B 139 6770 7474 6461 -239 -448 -775 C ATOM 3637 CG1 VAL B 139 -14.635 19.738 17.095 1.00 56.58 C ANISOU 3637 CG1 VAL B 139 7074 7718 6706 -224 -422 -768 C ATOM 3638 CG2 VAL B 139 -16.152 21.526 17.988 1.00 54.36 C ANISOU 3638 CG2 VAL B 139 6756 7474 6424 -197 -457 -686 C ATOM 3639 N CYS B 140 -17.532 17.252 17.172 1.00 54.06 N ANISOU 3639 N CYS B 140 6647 7427 6465 -345 -460 -1000 N ATOM 3640 CA CYS B 140 -17.391 15.816 16.978 1.00 49.78 C ANISOU 3640 CA CYS B 140 6102 6847 5964 -391 -440 -1089 C ATOM 3641 C CYS B 140 -18.521 15.192 16.177 1.00 66.58 C ANISOU 3641 C CYS B 140 8175 9047 8074 -417 -472 -1196 C ATOM 3642 O CYS B 140 -18.424 14.014 15.825 1.00 73.82 O ANISOU 3642 O CYS B 140 9087 9943 9019 -454 -457 -1282 O ATOM 3643 CB CYS B 140 -17.282 15.107 18.332 1.00 54.43 C ANISOU 3643 CB CYS B 140 6707 7322 6654 -436 -397 -1079 C ATOM 3644 SG CYS B 140 -15.733 15.463 19.183 1.00 61.49 S ANISOU 3644 SG CYS B 140 7664 8127 7571 -412 -355 -978 S ATOM 3645 N LYS B 141 -19.580 15.948 15.888 1.00 58.65 N ANISOU 3645 N LYS B 141 7129 8128 7027 -398 -517 -1195 N ATOM 3646 CA LYS B 141 -20.741 15.518 15.109 1.00 64.20 C ANISOU 3646 CA LYS B 141 7771 8918 7705 -417 -557 -1294 C ATOM 3647 C LYS B 141 -21.181 14.083 15.438 1.00 73.08 C ANISOU 3647 C LYS B 141 8871 9981 8914 -490 -534 -1394 C ATOM 3648 O LYS B 141 -21.246 13.231 14.541 1.00 85.25 O ANISOU 3648 O LYS B 141 10393 11560 10440 -510 -542 -1494 O ATOM 3649 CB LYS B 141 -20.477 15.679 13.616 1.00 66.39 C ANISOU 3649 CB LYS B 141 8043 9303 7879 -376 -589 -1330 C ATOM 3650 CG LYS B 141 -20.136 17.096 13.215 1.00 62.80 C ANISOU 3650 CG LYS B 141 7607 8911 7340 -302 -608 -1231 C ATOM 3651 N PRO B 142 -21.488 13.781 16.712 1.00 75.07 N ANISOU 3651 N PRO B 142 9124 10141 9260 -529 -502 -1372 N ATOM 3652 CA PRO B 142 -21.892 12.400 16.978 1.00 81.83 C ANISOU 3652 CA PRO B 142 9957 10935 10201 -596 -474 -1465 C ATOM 3653 C PRO B 142 -23.378 12.170 16.716 1.00 84.02 C ANISOU 3653 C PRO B 142 10159 11276 10490 -629 -509 -1550 C ATOM 3654 O PRO B 142 -23.727 11.500 15.742 1.00 87.50 O ANISOU 3654 O PRO B 142 10563 11773 10910 -650 -530 -1657 O ATOM 3655 CB PRO B 142 -21.558 12.223 18.455 1.00 74.49 C ANISOU 3655 CB PRO B 142 9061 9882 9360 -617 -421 -1396 C ATOM 3656 CG PRO B 142 -21.808 13.572 19.026 1.00 71.25 C ANISOU 3656 CG PRO B 142 8655 9498 8919 -576 -443 -1297 C ATOM 3657 CD PRO B 142 -21.432 14.575 17.958 1.00 70.42 C ANISOU 3657 CD PRO B 142 8558 9493 8706 -515 -485 -1267 C ATOM 3658 N ARG B 147 -28.162 18.399 15.020 1.00 78.92 N ANISOU 3658 N ARG B 147 9295 11199 9492 -381 -789 -1355 N ATOM 3659 CA ARG B 147 -27.459 19.674 15.132 1.00 79.43 C ANISOU 3659 CA ARG B 147 9410 11261 9507 -314 -781 -1231 C ATOM 3660 C ARG B 147 -27.989 20.503 16.303 1.00 73.14 C ANISOU 3660 C ARG B 147 8612 10418 8761 -308 -767 -1149 C ATOM 3661 O ARG B 147 -29.200 20.658 16.460 1.00 79.13 O ANISOU 3661 O ARG B 147 9311 11222 9533 -315 -794 -1172 O ATOM 3662 CB ARG B 147 -27.585 20.468 13.831 1.00 78.92 C ANISOU 3662 CB ARG B 147 9326 11334 9324 -242 -828 -1218 C ATOM 3663 N PHE B 148 -27.079 21.036 17.118 1.00 62.25 N ANISOU 3663 N PHE B 148 7296 8948 7408 -293 -726 -1056 N ATOM 3664 CA PHE B 148 -27.449 21.831 18.290 1.00 59.45 C ANISOU 3664 CA PHE B 148 6947 8541 7101 -287 -708 -978 C ATOM 3665 C PHE B 148 -27.854 23.214 17.805 1.00 62.11 C ANISOU 3665 C PHE B 148 7268 8964 7367 -215 -739 -909 C ATOM 3666 O PHE B 148 -27.005 24.065 17.539 1.00 60.73 O ANISOU 3666 O PHE B 148 7137 8790 7146 -164 -729 -832 O ATOM 3667 CB PHE B 148 -26.291 21.907 19.279 1.00 52.23 C ANISOU 3667 CB PHE B 148 6102 7507 6234 -296 -656 -911 C ATOM 3668 CG PHE B 148 -26.700 22.247 20.698 1.00 49.77 C ANISOU 3668 CG PHE B 148 5795 7121 5994 -313 -630 -861 C ATOM 3669 CD1 PHE B 148 -27.049 23.543 21.053 1.00 47.84 C ANISOU 3669 CD1 PHE B 148 5549 6894 5732 -268 -636 -782 C ATOM 3670 CD2 PHE B 148 -26.681 21.273 21.686 1.00 49.24 C ANISOU 3670 CD2 PHE B 148 5737 6962 6011 -372 -594 -891 C ATOM 3671 CE1 PHE B 148 -27.404 23.856 22.372 1.00 43.87 C ANISOU 3671 CE1 PHE B 148 5053 6324 5293 -284 -610 -740 C ATOM 3672 CE2 PHE B 148 -27.023 21.577 23.005 1.00 50.48 C ANISOU 3672 CE2 PHE B 148 5900 7052 6227 -385 -567 -844 C ATOM 3673 CZ PHE B 148 -27.386 22.867 23.351 1.00 44.83 C ANISOU 3673 CZ PHE B 148 5183 6359 5492 -342 -576 -771 C ATOM 3674 N GLY B 149 -29.156 23.439 17.689 1.00 56.03 N ANISOU 3674 N GLY B 149 6433 8266 6591 -210 -774 -934 N ATOM 3675 CA GLY B 149 -29.692 24.673 17.174 1.00 55.56 C ANISOU 3675 CA GLY B 149 6349 8297 6464 -140 -804 -875 C ATOM 3676 C GLY B 149 -30.220 25.594 18.255 1.00 51.82 C ANISOU 3676 C GLY B 149 5874 7779 6036 -127 -787 -798 C ATOM 3677 O GLY B 149 -29.829 25.525 19.426 1.00 46.78 O ANISOU 3677 O GLY B 149 5274 7032 5469 -159 -745 -766 O ATOM 3678 N GLU B 150 -31.144 26.463 17.844 1.00 45.37 N ANISOU 3678 N GLU B 150 5010 7052 5175 -76 -820 -770 N ATOM 3679 CA GLU B 150 -31.677 27.501 18.719 1.00 53.53 C ANISOU 3679 CA GLU B 150 6042 8058 6241 -51 -805 -692 C ATOM 3680 C GLU B 150 -32.613 26.916 19.772 1.00 48.39 C ANISOU 3680 C GLU B 150 5352 7358 5675 -111 -796 -736 C ATOM 3681 O GLU B 150 -32.604 27.355 20.931 1.00 43.50 O ANISOU 3681 O GLU B 150 4758 6656 5113 -119 -760 -682 O ATOM 3682 CB GLU B 150 -32.395 28.550 17.863 1.00 53.04 C ANISOU 3682 CB GLU B 150 5937 8113 6103 26 -843 -651 C ATOM 3683 CG GLU B 150 -32.576 29.916 18.489 1.00 60.24 C ANISOU 3683 CG GLU B 150 6864 8998 7028 77 -821 -546 C ATOM 3684 CD GLU B 150 -32.767 31.013 17.445 1.00 59.72 C ANISOU 3684 CD GLU B 150 6782 9036 6874 167 -845 -484 C ATOM 3685 OE1 GLU B 150 -32.543 30.748 16.245 1.00 70.22 O ANISOU 3685 OE1 GLU B 150 8101 10453 8126 194 -876 -513 O ATOM 3686 OE2 GLU B 150 -33.142 32.141 17.817 1.00 57.58 O ANISOU 3686 OE2 GLU B 150 6509 8760 6610 214 -832 -404 O ATOM 3687 N ASN B 151 -33.433 25.930 19.380 1.00 45.11 N ANISOU 3687 N ASN B 151 4875 6994 5270 -153 -826 -836 N ATOM 3688 CA ASN B 151 -34.339 25.276 20.323 1.00 45.47 C ANISOU 3688 CA ASN B 151 4881 6994 5402 -214 -813 -883 C ATOM 3689 C ASN B 151 -33.564 24.599 21.443 1.00 38.58 C ANISOU 3689 C ASN B 151 4065 5985 4608 -270 -757 -878 C ATOM 3690 O ASN B 151 -33.962 24.658 22.613 1.00 41.58 O ANISOU 3690 O ASN B 151 4446 6295 5056 -294 -726 -853 O ATOM 3691 CB ASN B 151 -35.211 24.239 19.600 1.00 42.08 C ANISOU 3691 CB ASN B 151 4376 6640 4972 -255 -852 -1001 C ATOM 3692 CG ASN B 151 -36.342 24.861 18.798 1.00 46.26 C ANISOU 3692 CG ASN B 151 4830 7305 5443 -208 -908 -1012 C ATOM 3693 OD1 ASN B 151 -36.781 25.977 19.073 1.00 55.73 O ANISOU 3693 OD1 ASN B 151 6022 8526 6628 -156 -910 -933 O ATOM 3694 ND2 ASN B 151 -36.829 24.127 17.806 1.00 43.49 N ANISOU 3694 ND2 ASN B 151 4420 7047 5058 -225 -953 -1112 N ATOM 3695 N HIS B 152 -32.457 23.941 21.100 1.00 38.48 N ANISOU 3695 N HIS B 152 4100 5936 4585 -288 -743 -901 N ATOM 3696 CA HIS B 152 -31.645 23.289 22.122 1.00 44.71 C ANISOU 3696 CA HIS B 152 4944 6601 5443 -334 -691 -892 C ATOM 3697 C HIS B 152 -30.972 24.300 23.038 1.00 39.27 C ANISOU 3697 C HIS B 152 4314 5843 4763 -301 -657 -787 C ATOM 3698 O HIS B 152 -30.793 24.025 24.230 1.00 39.59 O ANISOU 3698 O HIS B 152 4382 5790 4871 -334 -616 -767 O ATOM 3699 CB HIS B 152 -30.599 22.386 21.473 1.00 46.61 C ANISOU 3699 CB HIS B 152 5219 6824 5667 -355 -684 -939 C ATOM 3700 CG HIS B 152 -31.169 21.474 20.439 1.00 52.25 C ANISOU 3700 CG HIS B 152 5876 7613 6362 -382 -719 -1048 C ATOM 3701 ND1 HIS B 152 -31.151 21.777 19.094 1.00 56.57 N ANISOU 3701 ND1 HIS B 152 6404 8271 6818 -339 -765 -1070 N ATOM 3702 CD2 HIS B 152 -31.815 20.290 20.553 1.00 52.48 C ANISOU 3702 CD2 HIS B 152 5863 7627 6452 -447 -715 -1142 C ATOM 3703 CE1 HIS B 152 -31.744 20.807 18.423 1.00 63.57 C ANISOU 3703 CE1 HIS B 152 7237 9210 7707 -377 -791 -1179 C ATOM 3704 NE2 HIS B 152 -32.154 19.892 19.284 1.00 55.47 N ANISOU 3704 NE2 HIS B 152 6195 8106 6776 -445 -760 -1226 N ATOM 3705 N ALA B 153 -30.570 25.454 22.503 1.00 39.29 N ANISOU 3705 N ALA B 153 4337 5890 4700 -236 -672 -720 N ATOM 3706 CA ALA B 153 -29.943 26.475 23.342 1.00 38.77 C ANISOU 3706 CA ALA B 153 4324 5759 4646 -206 -640 -625 C ATOM 3707 C ALA B 153 -30.916 26.981 24.398 1.00 33.90 C ANISOU 3707 C ALA B 153 3682 5119 4078 -209 -628 -596 C ATOM 3708 O ALA B 153 -30.571 27.094 25.582 1.00 37.33 O ANISOU 3708 O ALA B 153 4154 5467 4564 -226 -589 -559 O ATOM 3709 CB ALA B 153 -29.454 27.633 22.469 1.00 41.13 C ANISOU 3709 CB ALA B 153 4642 6116 4871 -135 -655 -562 C ATOM 3710 N ILE B 154 -32.142 27.295 23.975 1.00 35.23 N ANISOU 3710 N ILE B 154 3786 5369 4230 -191 -661 -613 N ATOM 3711 CA ILE B 154 -33.163 27.807 24.884 1.00 36.72 C ANISOU 3711 CA ILE B 154 3945 5546 4462 -190 -651 -587 C ATOM 3712 C ILE B 154 -33.558 26.746 25.902 1.00 39.17 C ANISOU 3712 C ILE B 154 4243 5785 4853 -259 -622 -636 C ATOM 3713 O ILE B 154 -33.726 27.042 27.094 1.00 33.20 O ANISOU 3713 O ILE B 154 3504 4964 4146 -267 -588 -597 O ATOM 3714 CB ILE B 154 -34.373 28.303 24.070 1.00 37.95 C ANISOU 3714 CB ILE B 154 4028 5815 4577 -153 -696 -600 C ATOM 3715 CG1 ILE B 154 -33.953 29.490 23.195 1.00 39.04 C ANISOU 3715 CG1 ILE B 154 4184 6013 4638 -76 -714 -532 C ATOM 3716 CG2 ILE B 154 -35.555 28.661 24.991 1.00 39.64 C ANISOU 3716 CG2 ILE B 154 4201 6019 4843 -159 -686 -586 C ATOM 3717 CD1 ILE B 154 -34.966 29.844 22.125 1.00 48.66 C ANISOU 3717 CD1 ILE B 154 5332 7359 5797 -32 -764 -549 C ATOM 3718 N MET B 155 -33.715 25.494 25.454 1.00 34.40 N ANISOU 3718 N MET B 155 3612 5194 4266 -308 -633 -722 N ATOM 3719 CA MET B 155 -33.907 24.392 26.394 1.00 37.14 C ANISOU 3719 CA MET B 155 3956 5461 4693 -374 -596 -764 C ATOM 3720 C MET B 155 -32.758 24.325 27.396 1.00 32.04 C ANISOU 3720 C MET B 155 3388 4709 4078 -384 -548 -713 C ATOM 3721 O MET B 155 -32.982 24.117 28.594 1.00 32.65 O ANISOU 3721 O MET B 155 3474 4716 4215 -409 -509 -696 O ATOM 3722 CB MET B 155 -34.049 23.077 25.618 1.00 39.00 C ANISOU 3722 CB MET B 155 4157 5722 4940 -423 -612 -865 C ATOM 3723 CG MET B 155 -34.301 21.819 26.443 1.00 45.80 C ANISOU 3723 CG MET B 155 5010 6503 5890 -494 -570 -917 C ATOM 3724 SD MET B 155 -35.386 20.681 25.513 1.00 58.78 S ANISOU 3724 SD MET B 155 6563 8215 7556 -545 -602 -1046 S ATOM 3725 CE MET B 155 -34.884 21.092 23.847 1.00 41.39 C ANISOU 3725 CE MET B 155 4359 6126 5243 -496 -663 -1067 C ATOM 3726 N GLY B 156 -31.522 24.544 26.933 1.00 30.92 N ANISOU 3726 N GLY B 156 3300 4557 3891 -359 -549 -686 N ATOM 3727 CA GLY B 156 -30.392 24.545 27.851 1.00 30.15 C ANISOU 3727 CA GLY B 156 3272 4367 3818 -364 -507 -637 C ATOM 3728 C GLY B 156 -30.471 25.662 28.879 1.00 30.95 C ANISOU 3728 C GLY B 156 3395 4435 3931 -334 -487 -560 C ATOM 3729 O GLY B 156 -30.140 25.465 30.049 1.00 29.34 O ANISOU 3729 O GLY B 156 3224 4153 3771 -353 -449 -536 O ATOM 3730 N VAL B 157 -30.911 26.849 28.454 1.00 29.10 N ANISOU 3730 N VAL B 157 3142 4260 3655 -284 -512 -521 N ATOM 3731 CA VAL B 157 -31.091 27.970 29.380 1.00 30.06 C ANISOU 3731 CA VAL B 157 3279 4353 3789 -254 -492 -454 C ATOM 3732 C VAL B 157 -32.073 27.597 30.492 1.00 28.33 C ANISOU 3732 C VAL B 157 3032 4100 3632 -287 -469 -467 C ATOM 3733 O VAL B 157 -31.783 27.762 31.688 1.00 27.14 O ANISOU 3733 O VAL B 157 2917 3880 3516 -294 -432 -432 O ATOM 3734 CB VAL B 157 -31.571 29.218 28.613 1.00 31.84 C ANISOU 3734 CB VAL B 157 3479 4654 3965 -195 -522 -415 C ATOM 3735 CG1 VAL B 157 -32.031 30.315 29.587 1.00 33.69 C ANISOU 3735 CG1 VAL B 157 3717 4861 4222 -168 -500 -356 C ATOM 3736 CG2 VAL B 157 -30.484 29.732 27.674 1.00 35.41 C ANISOU 3736 CG2 VAL B 157 3968 5127 4358 -156 -533 -385 C ATOM 3737 N ALA B 158 -33.245 27.065 30.118 1.00 28.14 N ANISOU 3737 N ALA B 158 2943 4125 3623 -309 -488 -521 N ATOM 3738 CA ALA B 158 -34.248 26.703 31.128 1.00 27.82 C ANISOU 3738 CA ALA B 158 2871 4055 3646 -340 -463 -534 C ATOM 3739 C ALA B 158 -33.704 25.648 32.079 1.00 30.53 C ANISOU 3739 C ALA B 158 3250 4308 4042 -389 -418 -548 C ATOM 3740 O ALA B 158 -33.921 25.714 33.297 1.00 28.19 O ANISOU 3740 O ALA B 158 2968 3958 3787 -397 -380 -519 O ATOM 3741 CB ALA B 158 -35.520 26.184 30.448 1.00 28.31 C ANISOU 3741 CB ALA B 158 2852 4188 3719 -361 -492 -600 C ATOM 3742 N PHE B 159 -32.989 24.669 31.532 1.00 26.82 N ANISOU 3742 N PHE B 159 2796 3825 3570 -417 -420 -591 N ATOM 3743 CA PHE B 159 -32.349 23.631 32.339 1.00 27.28 C ANISOU 3743 CA PHE B 159 2891 3797 3675 -457 -376 -600 C ATOM 3744 C PHE B 159 -31.413 24.223 33.389 1.00 28.23 C ANISOU 3744 C PHE B 159 3078 3856 3793 -434 -345 -530 C ATOM 3745 O PHE B 159 -31.375 23.748 34.536 1.00 25.69 O ANISOU 3745 O PHE B 159 2776 3469 3517 -454 -303 -515 O ATOM 3746 CB PHE B 159 -31.600 22.681 31.394 1.00 30.63 C ANISOU 3746 CB PHE B 159 3326 4225 4087 -480 -387 -652 C ATOM 3747 CG PHE B 159 -30.684 21.696 32.082 1.00 30.60 C ANISOU 3747 CG PHE B 159 3370 4134 4122 -510 -343 -652 C ATOM 3748 CD1 PHE B 159 -31.188 20.532 32.637 1.00 36.84 C ANISOU 3748 CD1 PHE B 159 4139 4876 4981 -559 -306 -691 C ATOM 3749 CD2 PHE B 159 -29.318 21.915 32.124 1.00 35.00 C ANISOU 3749 CD2 PHE B 159 3990 4661 4649 -488 -336 -612 C ATOM 3750 CE1 PHE B 159 -30.348 19.626 33.266 1.00 34.39 C ANISOU 3750 CE1 PHE B 159 3874 4487 4707 -581 -262 -684 C ATOM 3751 CE2 PHE B 159 -28.472 21.005 32.744 1.00 37.38 C ANISOU 3751 CE2 PHE B 159 4332 4887 4984 -511 -296 -610 C ATOM 3752 CZ PHE B 159 -29.000 19.859 33.320 1.00 34.08 C ANISOU 3752 CZ PHE B 159 3895 4421 4633 -556 -259 -644 C ATOM 3753 N THR B 160 -30.633 25.249 33.028 1.00 24.93 N ANISOU 3753 N THR B 160 2694 3456 3322 -390 -364 -485 N ATOM 3754 CA THR B 160 -29.690 25.780 34.015 1.00 23.37 C ANISOU 3754 CA THR B 160 2556 3200 3124 -371 -337 -427 C ATOM 3755 C THR B 160 -30.408 26.424 35.191 1.00 24.97 C ANISOU 3755 C THR B 160 2753 3383 3353 -361 -314 -392 C ATOM 3756 O THR B 160 -29.911 26.358 36.321 1.00 24.42 O ANISOU 3756 O THR B 160 2722 3255 3303 -364 -280 -363 O ATOM 3757 CB THR B 160 -28.721 26.809 33.402 1.00 25.22 C ANISOU 3757 CB THR B 160 2824 3454 3304 -328 -358 -388 C ATOM 3758 OG1 THR B 160 -29.419 28.013 33.045 1.00 25.65 O ANISOU 3758 OG1 THR B 160 2851 3561 3333 -289 -380 -362 O ATOM 3759 CG2 THR B 160 -27.971 26.235 32.207 1.00 27.25 C ANISOU 3759 CG2 THR B 160 3088 3736 3531 -333 -379 -420 C ATOM 3760 N TRP B 161 -31.558 27.060 34.955 1.00 24.75 N ANISOU 3760 N TRP B 161 2678 3405 3323 -345 -331 -392 N ATOM 3761 CA TRP B 161 -32.302 27.637 36.079 1.00 24.15 C ANISOU 3761 CA TRP B 161 2594 3310 3274 -336 -306 -361 C ATOM 3762 C TRP B 161 -32.871 26.549 36.977 1.00 26.76 C ANISOU 3762 C TRP B 161 2909 3596 3660 -379 -269 -386 C ATOM 3763 O TRP B 161 -32.877 26.692 38.205 1.00 25.15 O ANISOU 3763 O TRP B 161 2730 3347 3479 -377 -232 -354 O ATOM 3764 CB TRP B 161 -33.429 28.542 35.576 1.00 25.17 C ANISOU 3764 CB TRP B 161 2671 3503 3389 -307 -332 -355 C ATOM 3765 CG TRP B 161 -32.933 29.865 35.157 1.00 28.41 C ANISOU 3765 CG TRP B 161 3104 3936 3755 -256 -349 -309 C ATOM 3766 CD1 TRP B 161 -32.443 30.212 33.924 1.00 29.92 C ANISOU 3766 CD1 TRP B 161 3296 4173 3898 -230 -383 -308 C ATOM 3767 CD2 TRP B 161 -32.851 31.039 35.972 1.00 27.60 C ANISOU 3767 CD2 TRP B 161 3027 3808 3652 -222 -330 -256 C ATOM 3768 NE1 TRP B 161 -32.062 31.533 33.928 1.00 30.24 N ANISOU 3768 NE1 TRP B 161 3362 4216 3914 -183 -382 -253 N ATOM 3769 CE2 TRP B 161 -32.300 32.065 35.171 1.00 30.78 C ANISOU 3769 CE2 TRP B 161 3445 4239 4013 -178 -350 -224 C ATOM 3770 CE3 TRP B 161 -33.188 31.321 37.298 1.00 27.28 C ANISOU 3770 CE3 TRP B 161 2998 3724 3643 -223 -294 -234 C ATOM 3771 CZ2 TRP B 161 -32.083 33.361 35.655 1.00 33.72 C ANISOU 3771 CZ2 TRP B 161 3842 4590 4380 -140 -335 -173 C ATOM 3772 CZ3 TRP B 161 -32.969 32.617 37.784 1.00 30.73 C ANISOU 3772 CZ3 TRP B 161 3461 4146 4070 -184 -283 -188 C ATOM 3773 CH2 TRP B 161 -32.421 33.612 36.964 1.00 30.23 C ANISOU 3773 CH2 TRP B 161 3410 4105 3971 -144 -302 -159 C ATOM 3774 N VAL B 162 -33.387 25.467 36.386 1.00 25.96 N ANISOU 3774 N VAL B 162 2768 3511 3585 -418 -275 -442 N ATOM 3775 CA VAL B 162 -33.955 24.390 37.198 1.00 24.48 C ANISOU 3775 CA VAL B 162 2563 3277 3460 -461 -233 -466 C ATOM 3776 C VAL B 162 -32.879 23.746 38.070 1.00 26.59 C ANISOU 3776 C VAL B 162 2891 3469 3742 -472 -192 -443 C ATOM 3777 O VAL B 162 -33.085 23.524 39.271 1.00 25.46 O ANISOU 3777 O VAL B 162 2762 3280 3632 -478 -148 -418 O ATOM 3778 CB VAL B 162 -34.648 23.345 36.310 1.00 29.52 C ANISOU 3778 CB VAL B 162 3144 3944 4128 -503 -247 -539 C ATOM 3779 CG1 VAL B 162 -35.157 22.184 37.177 1.00 30.96 C ANISOU 3779 CG1 VAL B 162 3312 4068 4385 -550 -194 -560 C ATOM 3780 CG2 VAL B 162 -35.792 23.984 35.571 1.00 28.99 C ANISOU 3780 CG2 VAL B 162 3011 3957 4046 -489 -286 -560 C ATOM 3781 N MET B 163 -31.718 23.425 37.487 1.00 23.81 N ANISOU 3781 N MET B 163 2576 3108 3363 -472 -205 -449 N ATOM 3782 CA MET B 163 -30.660 22.809 38.296 1.00 25.11 C ANISOU 3782 CA MET B 163 2796 3204 3539 -478 -168 -426 C ATOM 3783 C MET B 163 -30.155 23.766 39.368 1.00 27.19 C ANISOU 3783 C MET B 163 3104 3447 3781 -442 -155 -364 C ATOM 3784 O MET B 163 -29.892 23.360 40.516 1.00 25.51 O ANISOU 3784 O MET B 163 2920 3184 3589 -445 -114 -338 O ATOM 3785 CB MET B 163 -29.487 22.352 37.416 1.00 26.73 C ANISOU 3785 CB MET B 163 3030 3407 3719 -481 -186 -444 C ATOM 3786 CG MET B 163 -29.856 21.273 36.407 1.00 29.06 C ANISOU 3786 CG MET B 163 3287 3717 4038 -520 -196 -512 C ATOM 3787 SD MET B 163 -30.670 19.842 37.174 1.00 34.44 S ANISOU 3787 SD MET B 163 3940 4340 4804 -572 -139 -545 S ATOM 3788 CE MET B 163 -29.402 19.201 38.244 1.00 36.76 C ANISOU 3788 CE MET B 163 4304 4552 5113 -567 -89 -498 C ATOM 3789 N ALA B 164 -29.974 25.039 39.011 1.00 25.24 N ANISOU 3789 N ALA B 164 2863 3238 3490 -405 -187 -340 N ATOM 3790 CA ALA B 164 -29.472 26.002 39.984 1.00 24.03 C ANISOU 3790 CA ALA B 164 2749 3063 3317 -373 -175 -290 C ATOM 3791 C ALA B 164 -30.458 26.198 41.133 1.00 24.55 C ANISOU 3791 C ALA B 164 2800 3116 3411 -372 -143 -273 C ATOM 3792 O ALA B 164 -30.049 26.319 42.301 1.00 24.80 O ANISOU 3792 O ALA B 164 2868 3112 3443 -360 -113 -241 O ATOM 3793 CB ALA B 164 -29.170 27.337 39.293 1.00 22.68 C ANISOU 3793 CB ALA B 164 2583 2932 3102 -336 -210 -270 C ATOM 3794 N LEU B 165 -31.757 26.248 40.825 1.00 24.42 N ANISOU 3794 N LEU B 165 2729 3132 3416 -381 -148 -293 N ATOM 3795 CA LEU B 165 -32.755 26.358 41.885 1.00 24.02 C ANISOU 3795 CA LEU B 165 2660 3069 3397 -381 -114 -279 C ATOM 3796 C LEU B 165 -32.783 25.102 42.744 1.00 26.82 C ANISOU 3796 C LEU B 165 3024 3372 3794 -412 -66 -283 C ATOM 3797 O LEU B 165 -33.018 25.198 43.948 1.00 25.64 O ANISOU 3797 O LEU B 165 2890 3195 3657 -403 -28 -254 O ATOM 3798 CB LEU B 165 -34.152 26.634 41.299 1.00 24.28 C ANISOU 3798 CB LEU B 165 2626 3151 3448 -385 -132 -303 C ATOM 3799 CG LEU B 165 -34.367 28.078 40.806 1.00 26.06 C ANISOU 3799 CG LEU B 165 2842 3425 3636 -343 -166 -281 C ATOM 3800 CD1 LEU B 165 -35.613 28.209 39.956 1.00 25.87 C ANISOU 3800 CD1 LEU B 165 2748 3460 3622 -345 -192 -309 C ATOM 3801 CD2 LEU B 165 -34.458 29.053 41.981 1.00 27.05 C ANISOU 3801 CD2 LEU B 165 2992 3528 3758 -312 -139 -237 C ATOM 3802 N ALA B 166 -32.531 23.924 42.160 1.00 24.34 N ANISOU 3802 N ALA B 166 2703 3043 3504 -447 -63 -318 N ATOM 3803 CA ALA B 166 -32.509 22.704 42.968 1.00 23.78 C ANISOU 3803 CA ALA B 166 2642 2915 3477 -474 -10 -317 C ATOM 3804 C ALA B 166 -31.344 22.690 43.957 1.00 27.82 C ANISOU 3804 C ALA B 166 3218 3385 3965 -451 14 -272 C ATOM 3805 O ALA B 166 -31.370 21.909 44.917 1.00 28.41 O ANISOU 3805 O ALA B 166 3307 3416 4070 -459 64 -254 O ATOM 3806 CB ALA B 166 -32.464 21.470 42.062 1.00 26.60 C ANISOU 3806 CB ALA B 166 2977 3262 3868 -515 -12 -369 C ATOM 3807 N CYS B 167 -30.324 23.527 43.740 1.00 23.64 N ANISOU 3807 N CYS B 167 2726 2871 3384 -421 -18 -253 N ATOM 3808 CA CYS B 167 -29.222 23.711 44.678 1.00 23.96 C ANISOU 3808 CA CYS B 167 2822 2884 3396 -395 -3 -213 C ATOM 3809 C CYS B 167 -29.479 24.857 45.661 1.00 23.11 C ANISOU 3809 C CYS B 167 2727 2787 3266 -362 3 -180 C ATOM 3810 O CYS B 167 -29.311 24.684 46.877 1.00 28.04 O ANISOU 3810 O CYS B 167 3379 3387 3890 -350 39 -151 O ATOM 3811 CB CYS B 167 -27.912 23.966 43.900 1.00 25.77 C ANISOU 3811 CB CYS B 167 3082 3121 3587 -384 -40 -216 C ATOM 3812 SG CYS B 167 -26.455 24.049 44.990 1.00 27.65 S ANISOU 3812 SG CYS B 167 3383 3329 3794 -356 -24 -174 S ATOM 3813 N ALA B 168 -29.924 26.021 45.165 1.00 22.16 N ANISOU 3813 N ALA B 168 2587 2705 3127 -346 -29 -184 N ATOM 3814 CA ALA B 168 -29.984 27.236 45.987 1.00 21.99 C ANISOU 3814 CA ALA B 168 2582 2692 3082 -312 -27 -156 C ATOM 3815 C ALA B 168 -31.251 27.347 46.840 1.00 23.75 C ANISOU 3815 C ALA B 168 2779 2915 3331 -311 7 -147 C ATOM 3816 O ALA B 168 -31.229 28.026 47.878 1.00 23.41 O ANISOU 3816 O ALA B 168 2758 2867 3271 -286 25 -123 O ATOM 3817 CB ALA B 168 -29.871 28.479 45.082 1.00 23.50 C ANISOU 3817 CB ALA B 168 2765 2918 3246 -292 -70 -159 C ATOM 3818 N ALA B 169 -32.359 26.728 46.432 1.00 22.70 N ANISOU 3818 N ALA B 169 2598 2790 3238 -337 16 -169 N ATOM 3819 CA ALA B 169 -33.647 26.901 47.112 1.00 23.22 C ANISOU 3819 CA ALA B 169 2630 2861 3333 -336 47 -163 C ATOM 3820 C ALA B 169 -33.852 26.066 48.383 1.00 24.15 C ANISOU 3820 C ALA B 169 2762 2939 3474 -343 106 -142 C ATOM 3821 O ALA B 169 -34.476 26.567 49.324 1.00 27.19 O ANISOU 3821 O ALA B 169 3146 3325 3860 -325 134 -121 O ATOM 3822 CB ALA B 169 -34.813 26.614 46.149 1.00 24.38 C ANISOU 3822 CB ALA B 169 2711 3037 3516 -362 32 -198 C ATOM 3823 N PRO B 170 -33.427 24.806 48.458 1.00 23.37 N ANISOU 3823 N PRO B 170 2676 2806 3398 -367 130 -146 N ATOM 3824 CA PRO B 170 -33.727 23.999 49.670 1.00 27.43 C ANISOU 3824 CA PRO B 170 3200 3283 3938 -370 194 -119 C ATOM 3825 C PRO B 170 -33.257 24.644 50.970 1.00 23.62 C ANISOU 3825 C PRO B 170 2765 2797 3413 -329 214 -78 C ATOM 3826 O PRO B 170 -33.989 24.570 51.973 1.00 23.93 O ANISOU 3826 O PRO B 170 2799 2828 3467 -320 261 -56 O ATOM 3827 CB PRO B 170 -33.011 22.667 49.398 1.00 28.32 C ANISOU 3827 CB PRO B 170 3329 3358 4073 -395 210 -126 C ATOM 3828 CG PRO B 170 -33.074 22.545 47.874 1.00 26.04 C ANISOU 3828 CG PRO B 170 3006 3091 3798 -424 163 -175 C ATOM 3829 CD PRO B 170 -32.822 23.969 47.391 1.00 25.98 C ANISOU 3829 CD PRO B 170 3003 3129 3738 -395 108 -175 C ATOM 3830 N PRO B 171 -32.078 25.303 51.023 1.00 23.83 N ANISOU 3830 N PRO B 171 2834 2833 3386 -303 182 -69 N ATOM 3831 CA PRO B 171 -31.664 25.935 52.295 1.00 24.57 C ANISOU 3831 CA PRO B 171 2969 2930 3438 -264 200 -38 C ATOM 3832 C PRO B 171 -32.556 27.096 52.718 1.00 28.22 C ANISOU 3832 C PRO B 171 3414 3416 3893 -244 202 -36 C ATOM 3833 O PRO B 171 -32.435 27.579 53.855 1.00 23.49 O ANISOU 3833 O PRO B 171 2842 2820 3263 -214 223 -15 O ATOM 3834 CB PRO B 171 -30.218 26.407 52.014 1.00 25.76 C ANISOU 3834 CB PRO B 171 3159 3088 3542 -248 158 -40 C ATOM 3835 CG PRO B 171 -29.766 25.626 50.841 1.00 29.22 C ANISOU 3835 CG PRO B 171 3588 3516 4000 -277 135 -61 C ATOM 3836 CD PRO B 171 -30.991 25.393 50.019 1.00 25.39 C ANISOU 3836 CD PRO B 171 3048 3037 3561 -307 134 -86 C ATOM 3837 N LEU B 172 -33.436 27.578 51.841 1.00 23.48 N ANISOU 3837 N LEU B 172 2768 2835 3317 -257 179 -58 N ATOM 3838 CA LEU B 172 -34.428 28.562 52.258 1.00 24.76 C ANISOU 3838 CA LEU B 172 2908 3017 3482 -238 189 -54 C ATOM 3839 C LEU B 172 -35.595 27.953 53.012 1.00 26.28 C ANISOU 3839 C LEU B 172 3074 3198 3714 -247 244 -42 C ATOM 3840 O LEU B 172 -36.314 28.691 53.697 1.00 29.28 O ANISOU 3840 O LEU B 172 3446 3590 4091 -225 265 -32 O ATOM 3841 CB LEU B 172 -35.010 29.291 51.042 1.00 23.84 C ANISOU 3841 CB LEU B 172 2748 2930 3379 -244 147 -78 C ATOM 3842 CG LEU B 172 -34.099 30.161 50.186 1.00 23.36 C ANISOU 3842 CG LEU B 172 2706 2885 3284 -231 95 -86 C ATOM 3843 CD1 LEU B 172 -34.958 30.697 49.040 1.00 33.69 C ANISOU 3843 CD1 LEU B 172 3962 4226 4610 -234 64 -103 C ATOM 3844 CD2 LEU B 172 -33.520 31.291 51.008 1.00 26.75 C ANISOU 3844 CD2 LEU B 172 3175 3313 3676 -195 96 -72 C ATOM 3845 N VAL B 173 -35.835 26.646 52.853 1.00 24.00 N ANISOU 3845 N VAL B 173 2768 2886 3467 -279 271 -45 N ATOM 3846 CA VAL B 173 -37.078 26.035 53.317 1.00 24.53 C ANISOU 3846 CA VAL B 173 2795 2940 3585 -295 323 -40 C ATOM 3847 C VAL B 173 -36.845 24.767 54.135 1.00 29.73 C ANISOU 3847 C VAL B 173 3475 3557 4262 -304 382 -14 C ATOM 3848 O VAL B 173 -37.755 23.937 54.262 1.00 29.78 O ANISOU 3848 O VAL B 173 3446 3543 4327 -329 427 -14 O ATOM 3849 CB VAL B 173 -38.016 25.746 52.121 1.00 29.61 C ANISOU 3849 CB VAL B 173 3372 3598 4282 -333 302 -78 C ATOM 3850 CG1 VAL B 173 -38.438 27.055 51.470 1.00 31.30 C ANISOU 3850 CG1 VAL B 173 3560 3856 4477 -315 254 -92 C ATOM 3851 CG2 VAL B 173 -37.312 24.851 51.104 1.00 27.11 C ANISOU 3851 CG2 VAL B 173 3056 3269 3977 -365 275 -105 C ATOM 3852 N GLY B 174 -35.652 24.603 54.717 1.00 27.79 N ANISOU 3852 N GLY B 174 3288 3301 3972 -281 384 10 N ATOM 3853 CA GLY B 174 -35.474 23.588 55.745 1.00 29.63 C ANISOU 3853 CA GLY B 174 3546 3499 4212 -273 447 48 C ATOM 3854 C GLY B 174 -34.548 22.427 55.432 1.00 28.21 C ANISOU 3854 C GLY B 174 3389 3286 4043 -289 453 53 C ATOM 3855 O GLY B 174 -34.451 21.504 56.249 1.00 27.48 O ANISOU 3855 O GLY B 174 3316 3163 3964 -281 512 89 O ATOM 3856 N TRP B 175 -33.873 22.415 54.294 1.00 25.90 N ANISOU 3856 N TRP B 175 3095 2999 3748 -308 400 21 N ATOM 3857 CA TRP B 175 -32.841 21.413 54.040 1.00 24.42 C ANISOU 3857 CA TRP B 175 2934 2781 3562 -317 404 26 C ATOM 3858 C TRP B 175 -31.524 22.177 53.966 1.00 23.88 C ANISOU 3858 C TRP B 175 2910 2737 3425 -288 352 28 C ATOM 3859 O TRP B 175 -31.305 22.937 53.026 1.00 25.31 O ANISOU 3859 O TRP B 175 3082 2945 3592 -295 295 -3 O ATOM 3860 CB TRP B 175 -33.113 20.616 52.765 1.00 24.64 C ANISOU 3860 CB TRP B 175 2924 2790 3648 -367 391 -16 C ATOM 3861 CG TRP B 175 -32.221 19.402 52.623 1.00 25.88 C ANISOU 3861 CG TRP B 175 3106 2905 3823 -378 413 -8 C ATOM 3862 CD1 TRP B 175 -31.534 18.763 53.625 1.00 27.63 C ANISOU 3862 CD1 TRP B 175 3370 3099 4029 -350 459 40 C ATOM 3863 CD2 TRP B 175 -31.935 18.674 51.416 1.00 24.78 C ANISOU 3863 CD2 TRP B 175 2949 2749 3719 -416 392 -50 C ATOM 3864 NE1 TRP B 175 -30.833 17.690 53.109 1.00 28.13 N ANISOU 3864 NE1 TRP B 175 3444 3124 4120 -368 469 34 N ATOM 3865 CE2 TRP B 175 -31.056 17.622 51.757 1.00 28.02 C ANISOU 3865 CE2 TRP B 175 3394 3116 4137 -410 429 -23 C ATOM 3866 CE3 TRP B 175 -32.314 18.827 50.076 1.00 32.58 C ANISOU 3866 CE3 TRP B 175 3894 3757 4726 -451 345 -106 C ATOM 3867 CZ2 TRP B 175 -30.561 16.714 50.807 1.00 29.84 C ANISOU 3867 CZ2 TRP B 175 3620 3318 4401 -441 423 -54 C ATOM 3868 CZ3 TRP B 175 -31.805 17.936 49.130 1.00 31.29 C ANISOU 3868 CZ3 TRP B 175 3728 3572 4591 -481 336 -140 C ATOM 3869 CH2 TRP B 175 -30.948 16.890 49.506 1.00 30.08 C ANISOU 3869 CH2 TRP B 175 3610 3369 4450 -477 376 -114 C ATOM 3870 N SER B 176 -30.651 21.976 54.961 1.00 27.40 N ANISOU 3870 N SER B 176 3402 3178 3830 -253 373 67 N ATOM 3871 CA SER B 176 -29.541 22.895 55.240 1.00 23.44 C ANISOU 3871 CA SER B 176 2940 2708 3260 -219 330 70 C ATOM 3872 C SER B 176 -30.056 24.299 55.561 1.00 24.46 C ANISOU 3872 C SER B 176 3062 2872 3360 -200 309 60 C ATOM 3873 O SER B 176 -31.244 24.482 55.837 1.00 24.91 O ANISOU 3873 O SER B 176 3091 2931 3443 -205 336 61 O ATOM 3874 CB SER B 176 -28.548 22.950 54.070 1.00 25.52 C ANISOU 3874 CB SER B 176 3208 2972 3514 -234 275 42 C ATOM 3875 OG SER B 176 -27.365 23.659 54.452 1.00 26.45 O ANISOU 3875 OG SER B 176 3364 3114 3572 -202 243 49 O ATOM 3876 N ARG B 177 -29.159 25.290 55.577 1.00 22.95 N ANISOU 3876 N ARG B 177 2895 2707 3117 -178 264 50 N ATOM 3877 CA ARG B 177 -29.521 26.672 55.871 1.00 22.85 C ANISOU 3877 CA ARG B 177 2879 2723 3078 -159 245 37 C ATOM 3878 C ARG B 177 -28.374 27.561 55.418 1.00 22.84 C ANISOU 3878 C ARG B 177 2899 2740 3040 -149 190 17 C ATOM 3879 O ARG B 177 -27.247 27.100 55.254 1.00 23.08 O ANISOU 3879 O ARG B 177 2953 2764 3052 -147 174 20 O ATOM 3880 CB ARG B 177 -29.791 26.899 57.357 1.00 23.15 C ANISOU 3880 CB ARG B 177 2938 2774 3084 -123 286 63 C ATOM 3881 CG ARG B 177 -28.623 26.454 58.251 1.00 28.24 C ANISOU 3881 CG ARG B 177 3627 3425 3679 -93 294 87 C ATOM 3882 CD ARG B 177 -29.009 26.562 59.718 1.00 25.58 C ANISOU 3882 CD ARG B 177 3307 3104 3307 -56 339 114 C ATOM 3883 NE ARG B 177 -27.932 26.130 60.591 1.00 25.67 N ANISOU 3883 NE ARG B 177 3358 3131 3266 -21 346 140 N ATOM 3884 CZ ARG B 177 -27.943 26.306 61.903 1.00 29.31 C ANISOU 3884 CZ ARG B 177 3841 3618 3676 20 375 160 C ATOM 3885 NH1 ARG B 177 -28.986 26.841 62.513 1.00 26.15 N ANISOU 3885 NH1 ARG B 177 3431 3229 3276 31 405 161 N ATOM 3886 NH2 ARG B 177 -26.888 25.925 62.617 1.00 28.64 N ANISOU 3886 NH2 ARG B 177 3790 3555 3538 54 374 182 N ATOM 3887 N TYR B 178 -28.680 28.835 55.205 1.00 23.12 N ANISOU 3887 N TYR B 178 2924 2793 3067 -142 166 -3 N ATOM 3888 CA TYR B 178 -27.639 29.823 54.958 1.00 22.00 C ANISOU 3888 CA TYR B 178 2802 2665 2893 -129 122 -21 C ATOM 3889 C TYR B 178 -27.171 30.369 56.297 1.00 24.65 C ANISOU 3889 C TYR B 178 3169 3017 3181 -95 134 -17 C ATOM 3890 O TYR B 178 -27.982 30.585 57.202 1.00 23.20 O ANISOU 3890 O TYR B 178 2982 2840 2991 -79 167 -8 O ATOM 3891 CB TYR B 178 -28.150 30.950 54.051 1.00 21.80 C ANISOU 3891 CB TYR B 178 2751 2647 2886 -136 94 -43 C ATOM 3892 CG TYR B 178 -28.376 30.457 52.619 1.00 22.14 C ANISOU 3892 CG TYR B 178 2765 2684 2964 -166 72 -52 C ATOM 3893 CD1 TYR B 178 -27.299 30.072 51.823 1.00 21.42 C ANISOU 3893 CD1 TYR B 178 2686 2587 2866 -177 42 -59 C ATOM 3894 CD2 TYR B 178 -29.665 30.345 52.081 1.00 25.09 C ANISOU 3894 CD2 TYR B 178 3096 3061 3375 -182 81 -56 C ATOM 3895 CE1 TYR B 178 -27.487 29.604 50.520 1.00 21.36 C ANISOU 3895 CE1 TYR B 178 2654 2579 2885 -203 23 -71 C ATOM 3896 CE2 TYR B 178 -29.862 29.883 50.756 1.00 24.38 C ANISOU 3896 CE2 TYR B 178 2978 2974 3312 -208 57 -71 C ATOM 3897 CZ TYR B 178 -28.758 29.508 49.993 1.00 22.90 C ANISOU 3897 CZ TYR B 178 2807 2782 3113 -218 29 -79 C ATOM 3898 OH TYR B 178 -28.914 29.031 48.695 1.00 22.36 O ANISOU 3898 OH TYR B 178 2712 2720 3066 -243 6 -97 O ATOM 3899 N ILE B 179 -25.861 30.581 56.418 1.00 21.88 N ANISOU 3899 N ILE B 179 2844 2673 2795 -84 106 -25 N ATOM 3900 CA ILE B 179 -25.246 30.928 57.696 1.00 22.05 C ANISOU 3900 CA ILE B 179 2894 2717 2766 -51 113 -25 C ATOM 3901 C ILE B 179 -24.045 31.836 57.411 1.00 22.67 C ANISOU 3901 C ILE B 179 2985 2805 2823 -47 68 -55 C ATOM 3902 O ILE B 179 -23.400 31.689 56.356 1.00 21.49 O ANISOU 3902 O ILE B 179 2831 2643 2691 -67 39 -61 O ATOM 3903 CB ILE B 179 -24.871 29.631 58.444 1.00 23.99 C ANISOU 3903 CB ILE B 179 3159 2964 2990 -37 142 9 C ATOM 3904 CG1 ILE B 179 -24.568 29.863 59.919 1.00 28.00 C ANISOU 3904 CG1 ILE B 179 3693 3504 3441 3 159 15 C ATOM 3905 CG2 ILE B 179 -23.744 28.891 57.707 1.00 22.61 C ANISOU 3905 CG2 ILE B 179 2993 2778 2819 -50 117 12 C ATOM 3906 CD1 ILE B 179 -24.391 28.551 60.714 1.00 29.66 C ANISOU 3906 CD1 ILE B 179 3921 3717 3630 24 197 60 C ATOM 3907 N PRO B 180 -23.757 32.829 58.257 1.00 22.22 N ANISOU 3907 N PRO B 180 2941 2769 2733 -25 63 -78 N ATOM 3908 CA PRO B 180 -22.640 33.738 57.968 1.00 22.31 C ANISOU 3908 CA PRO B 180 2960 2785 2734 -26 24 -111 C ATOM 3909 C PRO B 180 -21.291 33.036 58.022 1.00 22.29 C ANISOU 3909 C PRO B 180 2974 2793 2705 -22 3 -106 C ATOM 3910 O PRO B 180 -21.086 32.090 58.781 1.00 22.53 O ANISOU 3910 O PRO B 180 3018 2838 2704 -4 21 -82 O ATOM 3911 CB PRO B 180 -22.739 34.796 59.076 1.00 22.02 C ANISOU 3911 CB PRO B 180 2931 2769 2666 -1 32 -139 C ATOM 3912 CG PRO B 180 -24.183 34.788 59.488 1.00 24.64 C ANISOU 3912 CG PRO B 180 3253 3099 3011 5 71 -123 C ATOM 3913 CD PRO B 180 -24.573 33.304 59.390 1.00 22.28 C ANISOU 3913 CD PRO B 180 2951 2793 2720 -1 95 -80 C ATOM 3914 N GLU B 181 -20.351 33.549 57.244 1.00 21.38 N ANISOU 3914 N GLU B 181 2855 2670 2600 -35 -32 -128 N ATOM 3915 CA GLU B 181 -19.041 32.921 57.102 1.00 25.10 C ANISOU 3915 CA GLU B 181 3337 3147 3053 -34 -54 -125 C ATOM 3916 C GLU B 181 -17.951 33.962 57.281 1.00 21.30 C ANISOU 3916 C GLU B 181 2858 2680 2557 -30 -85 -165 C ATOM 3917 O GLU B 181 -18.171 35.141 57.022 1.00 21.25 O ANISOU 3917 O GLU B 181 2842 2661 2570 -38 -92 -193 O ATOM 3918 CB GLU B 181 -18.848 32.277 55.719 1.00 21.50 C ANISOU 3918 CB GLU B 181 2871 2664 2634 -61 -66 -110 C ATOM 3919 CG GLU B 181 -19.974 31.390 55.237 1.00 22.48 C ANISOU 3919 CG GLU B 181 2984 2769 2787 -76 -40 -82 C ATOM 3920 CD GLU B 181 -19.502 30.485 54.117 1.00 21.84 C ANISOU 3920 CD GLU B 181 2900 2670 2730 -96 -51 -70 C ATOM 3921 OE1 GLU B 181 -18.802 29.501 54.430 1.00 23.16 O ANISOU 3921 OE1 GLU B 181 3081 2839 2882 -88 -45 -53 O ATOM 3922 OE2 GLU B 181 -19.753 30.793 52.926 1.00 22.66 O ANISOU 3922 OE2 GLU B 181 2987 2759 2864 -118 -66 -80 O ATOM 3923 N GLY B 182 -16.766 33.507 57.697 1.00 21.35 N ANISOU 3923 N GLY B 182 2875 2708 2530 -18 -103 -167 N ATOM 3924 CA GLY B 182 -15.596 34.366 57.776 1.00 21.52 C ANISOU 3924 CA GLY B 182 2892 2742 2542 -18 -134 -208 C ATOM 3925 C GLY B 182 -15.741 35.472 58.806 1.00 21.71 C ANISOU 3925 C GLY B 182 2917 2789 2543 -3 -134 -250 C ATOM 3926 O GLY B 182 -16.035 35.193 59.977 1.00 22.58 O ANISOU 3926 O GLY B 182 3038 2932 2608 24 -119 -246 O ATOM 3927 N MET B 183 -15.568 36.743 58.372 1.00 21.66 N ANISOU 3927 N MET B 183 2899 2762 2568 -19 -146 -290 N ATOM 3928 CA MET B 183 -15.817 37.927 59.210 1.00 23.07 C ANISOU 3928 CA MET B 183 3076 2951 2738 -10 -140 -336 C ATOM 3929 C MET B 183 -17.299 38.196 59.428 1.00 26.45 C ANISOU 3929 C MET B 183 3506 3368 3177 -4 -106 -323 C ATOM 3930 O MET B 183 -17.631 39.192 60.097 1.00 23.79 O ANISOU 3930 O MET B 183 3167 3035 2836 4 -97 -361 O ATOM 3931 CB MET B 183 -15.160 39.192 58.609 1.00 21.96 C ANISOU 3931 CB MET B 183 2920 2783 2639 -31 -157 -381 C ATOM 3932 CG MET B 183 -13.640 39.100 58.627 1.00 30.07 C ANISOU 3932 CG MET B 183 3942 3829 3655 -36 -189 -406 C ATOM 3933 SD MET B 183 -12.743 40.336 57.641 1.00 27.15 S ANISOU 3933 SD MET B 183 3552 3416 3346 -66 -204 -446 S ATOM 3934 CE MET B 183 -13.497 41.882 58.138 1.00 25.65 C ANISOU 3934 CE MET B 183 3358 3206 3184 -67 -181 -494 C ATOM 3935 N GLN B 184 -18.162 37.307 58.924 1.00 21.86 N ANISOU 3935 N GLN B 184 2924 2772 2609 -8 -88 -274 N ATOM 3936 CA GLN B 184 -19.609 37.270 59.151 1.00 21.96 C ANISOU 3936 CA GLN B 184 2934 2777 2630 -2 -54 -253 C ATOM 3937 C GLN B 184 -20.387 38.257 58.289 1.00 22.43 C ANISOU 3937 C GLN B 184 2977 2801 2742 -17 -47 -260 C ATOM 3938 O GLN B 184 -21.513 38.632 58.655 1.00 24.47 O ANISOU 3938 O GLN B 184 3231 3057 3008 -8 -20 -257 O ATOM 3939 CB GLN B 184 -19.943 37.497 60.633 1.00 22.41 C ANISOU 3939 CB GLN B 184 3004 2870 2640 27 -34 -271 C ATOM 3940 CG GLN B 184 -19.165 36.546 61.568 1.00 23.45 C ANISOU 3940 CG GLN B 184 3152 3045 2712 51 -41 -260 C ATOM 3941 CD GLN B 184 -19.587 35.077 61.411 1.00 27.22 C ANISOU 3941 CD GLN B 184 3635 3519 3187 54 -20 -199 C ATOM 3942 OE1 GLN B 184 -20.652 34.681 61.883 1.00 25.65 O ANISOU 3942 OE1 GLN B 184 3439 3322 2984 66 17 -172 O ATOM 3943 NE2 GLN B 184 -18.743 34.267 60.752 1.00 22.29 N ANISOU 3943 NE2 GLN B 184 3012 2888 2570 44 -39 -180 N ATOM 3944 N CYS B 185 -19.818 38.678 57.155 1.00 22.66 N ANISOU 3944 N CYS B 185 2997 2805 2807 -37 -68 -265 N ATOM 3945 CA CYS B 185 -20.439 39.646 56.274 1.00 23.99 C ANISOU 3945 CA CYS B 185 3149 2942 3023 -46 -61 -267 C ATOM 3946 C CYS B 185 -20.893 39.044 54.946 1.00 24.60 C ANISOU 3946 C CYS B 185 3213 3003 3130 -61 -65 -228 C ATOM 3947 O CYS B 185 -21.370 39.785 54.074 1.00 23.08 O ANISOU 3947 O CYS B 185 3006 2789 2974 -66 -62 -223 O ATOM 3948 CB CYS B 185 -19.474 40.814 56.040 1.00 27.11 C ANISOU 3948 CB CYS B 185 3542 3319 3439 -53 -76 -306 C ATOM 3949 SG CYS B 185 -19.338 41.820 57.517 1.00 30.02 S ANISOU 3949 SG CYS B 185 3920 3702 3786 -36 -65 -363 S ATOM 3950 N SER B 186 -20.751 37.734 54.770 1.00 21.01 N ANISOU 3950 N SER B 186 2763 2559 2660 -68 -71 -202 N ATOM 3951 CA SER B 186 -21.404 37.018 53.682 1.00 20.81 C ANISOU 3951 CA SER B 186 2723 2525 2659 -82 -70 -172 C ATOM 3952 C SER B 186 -21.996 35.750 54.260 1.00 20.91 C ANISOU 3952 C SER B 186 2739 2551 2655 -80 -51 -148 C ATOM 3953 O SER B 186 -21.659 35.348 55.382 1.00 22.12 O ANISOU 3953 O SER B 186 2909 2721 2773 -66 -42 -150 O ATOM 3954 CB SER B 186 -20.435 36.702 52.530 1.00 23.15 C ANISOU 3954 CB SER B 186 3019 2812 2966 -98 -97 -167 C ATOM 3955 OG SER B 186 -19.416 35.785 52.926 1.00 24.86 O ANISOU 3955 OG SER B 186 3251 3039 3156 -99 -107 -165 O ATOM 3956 N CYS B 187 -22.896 35.115 53.508 1.00 21.17 N ANISOU 3956 N CYS B 187 2754 2578 2713 -94 -43 -127 N ATOM 3957 CA CYS B 187 -23.484 33.869 53.963 1.00 20.98 C ANISOU 3957 CA CYS B 187 2730 2558 2684 -96 -19 -104 C ATOM 3958 C CYS B 187 -23.269 32.767 52.943 1.00 22.21 C ANISOU 3958 C CYS B 187 2878 2704 2857 -118 -30 -91 C ATOM 3959 O CYS B 187 -23.162 33.018 51.740 1.00 22.69 O ANISOU 3959 O CYS B 187 2925 2758 2937 -132 -52 -96 O ATOM 3960 CB CYS B 187 -24.985 34.032 54.260 1.00 21.22 C ANISOU 3960 CB CYS B 187 2740 2590 2732 -93 10 -96 C ATOM 3961 SG CYS B 187 -25.226 34.877 55.828 1.00 22.22 S ANISOU 3961 SG CYS B 187 2883 2731 2829 -63 34 -108 S ATOM 3962 N GLY B 188 -23.188 31.541 53.450 1.00 22.25 N ANISOU 3962 N GLY B 188 2894 2708 2854 -119 -10 -73 N ATOM 3963 CA GLY B 188 -23.042 30.381 52.598 1.00 22.57 C ANISOU 3963 CA GLY B 188 2927 2734 2914 -141 -13 -63 C ATOM 3964 C GLY B 188 -23.822 29.214 53.165 1.00 23.72 C ANISOU 3964 C GLY B 188 3069 2871 3072 -145 27 -41 C ATOM 3965 O GLY B 188 -24.590 29.373 54.119 1.00 21.66 O ANISOU 3965 O GLY B 188 2808 2617 2806 -131 56 -32 O ATOM 3966 N ILE B 189 -23.625 28.039 52.578 1.00 22.27 N ANISOU 3966 N ILE B 189 2882 2670 2908 -164 33 -33 N ATOM 3967 CA ILE B 189 -24.233 26.807 53.076 1.00 22.31 C ANISOU 3967 CA ILE B 189 2885 2659 2934 -169 76 -11 C ATOM 3968 C ILE B 189 -23.600 26.421 54.412 1.00 24.19 C ANISOU 3968 C ILE B 189 3154 2901 3134 -138 101 16 C ATOM 3969 O ILE B 189 -22.425 26.712 54.681 1.00 23.88 O ANISOU 3969 O ILE B 189 3138 2876 3058 -119 78 14 O ATOM 3970 CB ILE B 189 -24.052 25.711 52.008 1.00 23.69 C ANISOU 3970 CB ILE B 189 3048 2809 3142 -199 74 -17 C ATOM 3971 CG1 ILE B 189 -24.818 26.103 50.759 1.00 25.56 C ANISOU 3971 CG1 ILE B 189 3251 3052 3409 -225 51 -44 C ATOM 3972 CG2 ILE B 189 -24.466 24.312 52.523 1.00 23.07 C ANISOU 3972 CG2 ILE B 189 2972 2704 3092 -205 126 7 C ATOM 3973 CD1 ILE B 189 -26.314 26.216 50.998 1.00 28.99 C ANISOU 3973 CD1 ILE B 189 3654 3489 3871 -233 76 -46 C ATOM 3974 N ASP B 190 -24.379 25.769 55.273 1.00 22.09 N ANISOU 3974 N ASP B 190 2888 2627 2877 -130 149 42 N ATOM 3975 CA ASP B 190 -23.875 25.451 56.611 1.00 24.23 C ANISOU 3975 CA ASP B 190 3188 2911 3106 -93 175 72 C ATOM 3976 C ASP B 190 -22.968 24.215 56.536 1.00 25.59 C ANISOU 3976 C ASP B 190 3378 3064 3280 -90 187 96 C ATOM 3977 O ASP B 190 -23.408 23.079 56.710 1.00 24.89 O ANISOU 3977 O ASP B 190 3288 2948 3223 -95 233 124 O ATOM 3978 CB ASP B 190 -25.038 25.275 57.592 1.00 22.93 C ANISOU 3978 CB ASP B 190 3019 2747 2947 -80 227 95 C ATOM 3979 CG ASP B 190 -24.566 25.120 59.050 1.00 24.63 C ANISOU 3979 CG ASP B 190 3265 2986 3106 -34 253 127 C ATOM 3980 OD1 ASP B 190 -23.343 25.105 59.290 1.00 22.88 O ANISOU 3980 OD1 ASP B 190 3066 2782 2843 -12 229 130 O ATOM 3981 OD2 ASP B 190 -25.433 25.001 59.946 1.00 27.41 O ANISOU 3981 OD2 ASP B 190 3617 3342 3455 -17 298 150 O ATOM 3982 N TYR B 191 -21.662 24.461 56.312 1.00 23.14 N ANISOU 3982 N TYR B 191 3084 2768 2939 -79 148 86 N ATOM 3983 CA TYR B 191 -20.585 23.476 56.461 1.00 25.62 C ANISOU 3983 CA TYR B 191 3418 3074 3241 -64 155 112 C ATOM 3984 C TYR B 191 -20.181 23.241 57.908 1.00 24.58 C ANISOU 3984 C TYR B 191 3312 2969 3058 -16 180 148 C ATOM 3985 O TYR B 191 -19.396 22.319 58.169 1.00 25.82 O ANISOU 3985 O TYR B 191 3485 3120 3204 5 195 179 O ATOM 3986 CB TYR B 191 -19.319 23.932 55.708 1.00 21.74 C ANISOU 3986 CB TYR B 191 2932 2594 2735 -68 102 86 C ATOM 3987 CG TYR B 191 -19.660 24.640 54.421 1.00 25.44 C ANISOU 3987 CG TYR B 191 3378 3053 3234 -105 69 48 C ATOM 3988 CD1 TYR B 191 -20.345 23.977 53.415 1.00 22.55 C ANISOU 3988 CD1 TYR B 191 2992 2657 2919 -139 80 41 C ATOM 3989 CD2 TYR B 191 -19.334 25.976 54.229 1.00 23.28 C ANISOU 3989 CD2 TYR B 191 3102 2804 2940 -103 28 18 C ATOM 3990 CE1 TYR B 191 -20.700 24.619 52.253 1.00 24.31 C ANISOU 3990 CE1 TYR B 191 3193 2880 3163 -167 50 8 C ATOM 3991 CE2 TYR B 191 -19.681 26.636 53.050 1.00 23.61 C ANISOU 3991 CE2 TYR B 191 3123 2838 3009 -130 2 -10 C ATOM 3992 CZ TYR B 191 -20.367 25.949 52.072 1.00 24.87 C ANISOU 3992 CZ TYR B 191 3263 2974 3211 -160 11 -13 C ATOM 3993 OH TYR B 191 -20.738 26.587 50.909 1.00 25.90 O ANISOU 3993 OH TYR B 191 3373 3107 3362 -182 -15 -38 O ATOM 3994 N TYR B 192 -20.673 24.063 58.840 1.00 24.69 N ANISOU 3994 N TYR B 192 3328 3014 3037 6 184 145 N ATOM 3995 CA TYR B 192 -20.035 24.281 60.132 1.00 25.66 C ANISOU 3995 CA TYR B 192 3474 3182 3092 55 185 161 C ATOM 3996 C TYR B 192 -20.609 23.450 61.254 1.00 32.52 C ANISOU 3996 C TYR B 192 4356 4053 3946 88 246 212 C ATOM 3997 O TYR B 192 -19.874 23.116 62.188 1.00 25.31 O ANISOU 3997 O TYR B 192 3464 3172 2980 133 254 241 O ATOM 3998 CB TYR B 192 -20.153 25.756 60.538 1.00 23.37 C ANISOU 3998 CB TYR B 192 3182 2929 2768 62 154 120 C ATOM 3999 CG TYR B 192 -19.489 26.656 59.535 1.00 23.48 C ANISOU 3999 CG TYR B 192 3184 2942 2794 36 98 74 C ATOM 4000 CD1 TYR B 192 -18.152 27.000 59.677 1.00 22.39 C ANISOU 4000 CD1 TYR B 192 3056 2832 2618 52 58 57 C ATOM 4001 CD2 TYR B 192 -20.203 27.123 58.417 1.00 22.05 C ANISOU 4001 CD2 TYR B 192 2982 2732 2664 -4 86 49 C ATOM 4002 CE1 TYR B 192 -17.521 27.821 58.729 1.00 22.01 C ANISOU 4002 CE1 TYR B 192 2997 2778 2587 27 12 17 C ATOM 4003 CE2 TYR B 192 -19.609 27.919 57.481 1.00 22.37 C ANISOU 4003 CE2 TYR B 192 3014 2771 2717 -24 41 14 C ATOM 4004 CZ TYR B 192 -18.258 28.268 57.633 1.00 22.06 C ANISOU 4004 CZ TYR B 192 2985 2753 2643 -10 6 -2 C ATOM 4005 OH TYR B 192 -17.673 29.072 56.688 1.00 23.18 O ANISOU 4005 OH TYR B 192 3117 2889 2802 -31 -33 -34 O ATOM 4006 N THR B 193 -21.904 23.165 61.218 1.00 28.54 N ANISOU 4006 N THR B 193 3838 3520 3485 70 290 224 N ATOM 4007 CA THR B 193 -22.582 22.516 62.326 1.00 29.73 C ANISOU 4007 CA THR B 193 3999 3672 3625 101 354 274 C ATOM 4008 C THR B 193 -23.371 21.321 61.808 1.00 34.29 C ANISOU 4008 C THR B 193 4562 4190 4277 71 408 301 C ATOM 4009 O THR B 193 -23.733 21.268 60.627 1.00 32.45 O ANISOU 4009 O THR B 193 4304 3921 4103 22 392 270 O ATOM 4010 CB THR B 193 -23.533 23.479 63.053 1.00 30.32 C ANISOU 4010 CB THR B 193 4069 3775 3677 112 365 260 C ATOM 4011 OG1 THR B 193 -24.718 23.672 62.284 1.00 30.22 O ANISOU 4011 OG1 THR B 193 4026 3727 3729 67 375 239 O ATOM 4012 CG2 THR B 193 -22.869 24.852 63.301 1.00 30.14 C ANISOU 4012 CG2 THR B 193 4053 3802 3598 126 306 213 C ATOM 4013 N PRO B 194 -23.630 20.331 62.662 1.00 31.24 N ANISOU 4013 N PRO B 194 4188 3790 3890 101 474 359 N ATOM 4014 CA PRO B 194 -24.458 19.201 62.211 1.00 36.63 C ANISOU 4014 CA PRO B 194 4853 4410 4654 69 532 382 C ATOM 4015 C PRO B 194 -25.929 19.553 62.088 1.00 36.18 C ANISOU 4015 C PRO B 194 4766 4337 4642 37 557 364 C ATOM 4016 O PRO B 194 -26.617 19.001 61.215 1.00 43.60 O ANISOU 4016 O PRO B 194 5677 5229 5659 -10 575 348 O ATOM 4017 CB PRO B 194 -24.223 18.131 63.291 1.00 42.88 C ANISOU 4017 CB PRO B 194 5670 5195 5426 119 600 455 C ATOM 4018 CG PRO B 194 -23.073 18.631 64.122 1.00 43.81 C ANISOU 4018 CG PRO B 194 5819 5378 5449 175 564 466 C ATOM 4019 CD PRO B 194 -23.093 20.118 64.016 1.00 42.02 C ANISOU 4019 CD PRO B 194 5584 5197 5184 166 499 407 C ATOM 4020 N HIS B 195 -26.442 20.382 63.002 1.00 31.32 N ANISOU 4020 N HIS B 195 4155 3761 3982 65 564 366 N ATOM 4021 CA HIS B 195 -27.805 20.913 63.010 1.00 35.77 C ANISOU 4021 CA HIS B 195 4692 4321 4580 43 583 349 C ATOM 4022 C HIS B 195 -28.813 19.939 62.414 1.00 40.91 C ANISOU 4022 C HIS B 195 5310 4912 5323 -1 634 357 C ATOM 4023 O HIS B 195 -29.280 20.139 61.282 1.00 35.60 O ANISOU 4023 O HIS B 195 4603 4220 4703 -50 604 311 O ATOM 4024 CB HIS B 195 -27.929 22.271 62.329 1.00 33.58 C ANISOU 4024 CB HIS B 195 4396 4069 4294 20 516 287 C ATOM 4025 CG HIS B 195 -29.103 23.045 62.837 1.00 35.86 C ANISOU 4025 CG HIS B 195 4669 4374 4584 24 537 279 C ATOM 4026 ND1 HIS B 195 -30.211 23.324 62.066 1.00 37.45 N ANISOU 4026 ND1 HIS B 195 4829 4554 4846 -18 536 251 N ATOM 4027 CD2 HIS B 195 -29.369 23.537 64.071 1.00 35.89 C ANISOU 4027 CD2 HIS B 195 4690 4413 4534 67 563 298 C ATOM 4028 CE1 HIS B 195 -31.095 23.984 62.794 1.00 39.09 C ANISOU 4028 CE1 HIS B 195 5030 4782 5042 0 561 253 C ATOM 4029 NE2 HIS B 195 -30.605 24.131 64.013 1.00 36.02 N ANISOU 4029 NE2 HIS B 195 4676 4426 4582 50 578 280 N ATOM 4030 N GLU B 196 -29.064 18.833 63.113 1.00 39.19 N ANISOU 4030 N GLU B 196 5100 4663 5126 18 710 413 N ATOM 4031 CA GLU B 196 -29.856 17.747 62.544 1.00 38.35 C ANISOU 4031 CA GLU B 196 4964 4493 5115 -26 764 420 C ATOM 4032 C GLU B 196 -31.273 18.168 62.176 1.00 34.24 C ANISOU 4032 C GLU B 196 4397 3963 4650 -66 774 387 C ATOM 4033 O GLU B 196 -31.884 17.521 61.317 1.00 37.09 O ANISOU 4033 O GLU B 196 4721 4278 5094 -117 790 364 O ATOM 4034 CB GLU B 196 -29.899 16.569 63.515 1.00 41.24 C ANISOU 4034 CB GLU B 196 5350 4828 5493 8 853 494 C ATOM 4035 CG GLU B 196 -28.579 15.813 63.577 1.00 49.18 C ANISOU 4035 CG GLU B 196 6390 5825 6472 37 851 527 C ATOM 4036 CD GLU B 196 -27.555 16.484 64.481 1.00 59.77 C ANISOU 4036 CD GLU B 196 7772 7235 7703 101 815 547 C ATOM 4037 OE1 GLU B 196 -27.844 17.582 65.036 1.00 53.20 O ANISOU 4037 OE1 GLU B 196 6942 6456 6815 121 789 530 O ATOM 4038 OE2 GLU B 196 -26.457 15.901 64.638 1.00 61.09 O ANISOU 4038 OE2 GLU B 196 7966 7404 7842 132 813 579 O ATOM 4039 N GLU B 197 -31.807 19.231 62.786 1.00 32.97 N ANISOU 4039 N GLU B 197 4234 3844 4447 -45 764 380 N ATOM 4040 CA GLU B 197 -33.156 19.678 62.430 1.00 32.30 C ANISOU 4040 CA GLU B 197 4103 3754 4415 -79 772 350 C ATOM 4041 C GLU B 197 -33.284 20.031 60.942 1.00 41.06 C ANISOU 4041 C GLU B 197 5176 4858 5567 -133 708 286 C ATOM 4042 O GLU B 197 -34.367 19.891 60.360 1.00 35.45 O ANISOU 4042 O GLU B 197 4417 4127 4924 -174 721 261 O ATOM 4043 CB GLU B 197 -33.559 20.877 63.279 1.00 40.90 C ANISOU 4043 CB GLU B 197 5201 4893 5445 -44 765 349 C ATOM 4044 CG GLU B 197 -35.052 21.170 63.237 1.00 59.12 C ANISOU 4044 CG GLU B 197 7463 7194 7807 -67 796 336 C ATOM 4045 CD GLU B 197 -35.417 22.480 63.914 1.00 68.80 C ANISOU 4045 CD GLU B 197 8695 8469 8978 -35 781 326 C ATOM 4046 OE1 GLU B 197 -34.495 23.201 64.356 1.00 68.66 O ANISOU 4046 OE1 GLU B 197 8716 8490 8881 2 741 322 O ATOM 4047 OE2 GLU B 197 -36.626 22.788 63.999 1.00 78.07 O ANISOU 4047 OE2 GLU B 197 9832 9640 10189 -47 809 320 O ATOM 4048 N THR B 198 -32.207 20.490 60.311 1.00 31.39 N ANISOU 4048 N THR B 198 3971 3654 4303 -132 638 258 N ATOM 4049 CA THR B 198 -32.217 20.818 58.885 1.00 29.15 C ANISOU 4049 CA THR B 198 3657 3370 4051 -177 577 202 C ATOM 4050 C THR B 198 -31.419 19.821 58.049 1.00 29.56 C ANISOU 4050 C THR B 198 3714 3388 4132 -202 567 194 C ATOM 4051 O THR B 198 -31.120 20.102 56.878 1.00 30.71 O ANISOU 4051 O THR B 198 3844 3538 4286 -230 510 150 O ATOM 4052 CB THR B 198 -31.679 22.234 58.671 1.00 26.55 C ANISOU 4052 CB THR B 198 3340 3088 3660 -159 506 173 C ATOM 4053 OG1 THR B 198 -30.452 22.383 59.395 1.00 31.16 O ANISOU 4053 OG1 THR B 198 3973 3692 4175 -117 493 196 O ATOM 4054 CG2 THR B 198 -32.681 23.274 59.150 1.00 32.28 C ANISOU 4054 CG2 THR B 198 4048 3841 4376 -147 511 166 C ATOM 4055 N ASN B 199 -31.061 18.668 58.623 1.00 30.10 N ANISOU 4055 N ASN B 199 3803 3420 4213 -189 624 238 N ATOM 4056 CA ASN B 199 -30.397 17.581 57.895 1.00 30.59 C ANISOU 4056 CA ASN B 199 3869 3440 4314 -213 628 234 C ATOM 4057 C ASN B 199 -29.198 18.088 57.094 1.00 30.76 C ANISOU 4057 C ASN B 199 3909 3486 4292 -211 552 203 C ATOM 4058 O ASN B 199 -29.049 17.815 55.898 1.00 27.36 O ANISOU 4058 O ASN B 199 3459 3040 3897 -250 521 162 O ATOM 4059 CB ASN B 199 -31.398 16.842 57.001 1.00 32.87 C ANISOU 4059 CB ASN B 199 4107 3686 4697 -271 653 199 C ATOM 4060 CG ASN B 199 -32.390 16.017 57.813 1.00 48.68 C ANISOU 4060 CG ASN B 199 6093 5648 6755 -274 743 237 C ATOM 4061 OD1 ASN B 199 -33.584 16.319 57.857 1.00 47.57 O ANISOU 4061 OD1 ASN B 199 5914 5512 6650 -294 761 222 O ATOM 4062 ND2 ASN B 199 -31.889 14.983 58.472 1.00 40.35 N ANISOU 4062 ND2 ASN B 199 5068 4554 5710 -252 804 289 N ATOM 4063 N ASN B 200 -28.314 18.816 57.788 1.00 28.32 N ANISOU 4063 N ASN B 200 3638 3218 3905 -165 524 223 N ATOM 4064 CA ASN B 200 -27.232 19.541 57.124 1.00 27.37 C ANISOU 4064 CA ASN B 200 3532 3127 3740 -162 450 192 C ATOM 4065 C ASN B 200 -26.309 18.613 56.362 1.00 30.47 C ANISOU 4065 C ASN B 200 3934 3489 4155 -177 443 189 C ATOM 4066 O ASN B 200 -25.838 18.952 55.260 1.00 26.50 O ANISOU 4066 O ASN B 200 3422 2993 3652 -200 389 148 O ATOM 4067 CB ASN B 200 -26.398 20.308 58.162 1.00 30.62 C ANISOU 4067 CB ASN B 200 3982 3584 4069 -109 431 215 C ATOM 4068 CG ASN B 200 -27.014 21.617 58.561 1.00 32.90 C ANISOU 4068 CG ASN B 200 4262 3912 4326 -98 410 197 C ATOM 4069 OD1 ASN B 200 -28.135 21.936 58.161 1.00 32.52 O ANISOU 4069 OD1 ASN B 200 4180 3858 4317 -125 415 175 O ATOM 4070 ND2 ASN B 200 -26.284 22.397 59.372 1.00 30.84 N ANISOU 4070 ND2 ASN B 200 4031 3694 3995 -57 387 203 N ATOM 4071 N GLU B 201 -25.958 17.477 56.967 1.00 24.55 N ANISOU 4071 N GLU B 201 3204 2707 3417 -158 498 234 N ATOM 4072 CA GLU B 201 -24.905 16.660 56.380 1.00 30.27 C ANISOU 4072 CA GLU B 201 3944 3405 4153 -163 492 236 C ATOM 4073 C GLU B 201 -25.334 16.101 55.032 1.00 27.20 C ANISOU 4073 C GLU B 201 3521 2977 3836 -221 486 189 C ATOM 4074 O GLU B 201 -24.538 16.083 54.082 1.00 28.17 O ANISOU 4074 O GLU B 201 3648 3101 3956 -235 443 159 O ATOM 4075 CB GLU B 201 -24.510 15.539 57.344 1.00 32.70 C ANISOU 4075 CB GLU B 201 4279 3683 4463 -126 559 301 C ATOM 4076 CG GLU B 201 -23.635 14.456 56.737 1.00 34.61 C ANISOU 4076 CG GLU B 201 4532 3882 4737 -134 571 307 C ATOM 4077 CD GLU B 201 -23.291 13.361 57.755 1.00 53.92 C ANISOU 4077 CD GLU B 201 7004 6298 7186 -91 645 379 C ATOM 4078 OE1 GLU B 201 -24.212 12.643 58.196 1.00 55.58 O ANISOU 4078 OE1 GLU B 201 7204 6467 7449 -98 717 407 O ATOM 4079 OE2 GLU B 201 -22.105 13.234 58.130 1.00 64.23 O ANISOU 4079 OE2 GLU B 201 8340 7622 8441 -48 632 411 O ATOM 4080 N SER B 202 -26.590 15.668 54.910 1.00 25.25 N ANISOU 4080 N SER B 202 3240 2700 3653 -254 528 177 N ATOM 4081 CA SER B 202 -27.004 15.104 53.626 1.00 27.77 C ANISOU 4081 CA SER B 202 3524 2988 4039 -310 520 124 C ATOM 4082 C SER B 202 -27.059 16.174 52.541 1.00 28.50 C ANISOU 4082 C SER B 202 3595 3126 4109 -332 442 67 C ATOM 4083 O SER B 202 -26.776 15.881 51.373 1.00 28.25 O ANISOU 4083 O SER B 202 3549 3085 4099 -364 412 24 O ATOM 4084 CB SER B 202 -28.353 14.384 53.750 1.00 33.81 C ANISOU 4084 CB SER B 202 4251 3713 4883 -344 584 120 C ATOM 4085 OG SER B 202 -29.392 15.272 54.122 1.00 30.93 O ANISOU 4085 OG SER B 202 3862 3381 4508 -344 577 114 O ATOM 4086 N PHE B 203 -27.408 17.415 52.890 1.00 26.32 N ANISOU 4086 N PHE B 203 3316 2896 3787 -314 409 66 N ATOM 4087 CA PHE B 203 -27.438 18.435 51.854 1.00 26.36 C ANISOU 4087 CA PHE B 203 3302 2941 3772 -330 339 19 C ATOM 4088 C PHE B 203 -26.047 18.694 51.293 1.00 27.94 C ANISOU 4088 C PHE B 203 3531 3156 3930 -317 290 12 C ATOM 4089 O PHE B 203 -25.881 18.854 50.076 1.00 26.95 O ANISOU 4089 O PHE B 203 3389 3039 3810 -342 248 -30 O ATOM 4090 CB PHE B 203 -28.037 19.742 52.362 1.00 27.12 C ANISOU 4090 CB PHE B 203 3392 3081 3833 -310 319 22 C ATOM 4091 CG PHE B 203 -28.051 20.802 51.309 1.00 23.52 C ANISOU 4091 CG PHE B 203 2916 2661 3357 -321 253 -19 C ATOM 4092 CD1 PHE B 203 -29.125 20.911 50.445 1.00 27.42 C ANISOU 4092 CD1 PHE B 203 3363 3165 3891 -354 240 -57 C ATOM 4093 CD2 PHE B 203 -26.960 21.644 51.126 1.00 28.35 C ANISOU 4093 CD2 PHE B 203 3557 3301 3915 -298 204 -20 C ATOM 4094 CE1 PHE B 203 -29.127 21.861 49.438 1.00 25.84 C ANISOU 4094 CE1 PHE B 203 3145 3002 3670 -359 182 -89 C ATOM 4095 CE2 PHE B 203 -26.947 22.581 50.101 1.00 26.25 C ANISOU 4095 CE2 PHE B 203 3275 3065 3635 -306 150 -53 C ATOM 4096 CZ PHE B 203 -28.047 22.693 49.274 1.00 26.91 C ANISOU 4096 CZ PHE B 203 3312 3158 3752 -334 139 -84 C ATOM 4097 N VAL B 204 -25.041 18.785 52.167 1.00 26.16 N ANISOU 4097 N VAL B 204 3347 2937 3657 -276 294 51 N ATOM 4098 CA VAL B 204 -23.690 19.095 51.699 1.00 25.99 C ANISOU 4098 CA VAL B 204 3350 2931 3595 -262 248 44 C ATOM 4099 C VAL B 204 -23.197 18.011 50.739 1.00 29.64 C ANISOU 4099 C VAL B 204 3809 3357 4096 -288 254 27 C ATOM 4100 O VAL B 204 -22.575 18.312 49.714 1.00 23.29 O ANISOU 4100 O VAL B 204 3003 2565 3280 -300 208 -4 O ATOM 4101 CB VAL B 204 -22.740 19.274 52.901 1.00 27.31 C ANISOU 4101 CB VAL B 204 3555 3114 3706 -213 255 88 C ATOM 4102 CG1 VAL B 204 -21.307 19.475 52.433 1.00 31.62 C ANISOU 4102 CG1 VAL B 204 4122 3673 4218 -200 212 81 C ATOM 4103 CG2 VAL B 204 -23.178 20.472 53.755 1.00 28.47 C ANISOU 4103 CG2 VAL B 204 3705 3301 3812 -188 243 94 C ATOM 4104 N AILE B 205 -23.460 16.740 51.057 0.36 27.17 N ANISOU 4104 N AILE B 205 3496 2997 3831 -297 314 46 N ATOM 4105 N BILE B 205 -23.469 16.736 51.056 0.64 27.17 N ANISOU 4105 N BILE B 205 3495 2997 3831 -297 314 46 N ATOM 4106 CA AILE B 205 -23.079 15.654 50.150 0.36 25.40 C ANISOU 4106 CA AILE B 205 3267 2732 3651 -325 326 24 C ATOM 4107 CA BILE B 205 -23.087 15.635 50.161 0.64 25.34 C ANISOU 4107 CA BILE B 205 3259 2723 3644 -325 327 25 C ATOM 4108 C AILE B 205 -23.822 15.786 48.828 0.36 28.01 C ANISOU 4108 C AILE B 205 3557 3070 4016 -373 296 -39 C ATOM 4109 C BILE B 205 -23.831 15.752 48.834 0.64 28.03 C ANISOU 4109 C BILE B 205 3560 3071 4020 -373 297 -39 C ATOM 4110 O AILE B 205 -23.240 15.626 47.748 0.36 30.50 O ANISOU 4110 O AILE B 205 3870 3385 4332 -390 264 -74 O ATOM 4111 O BILE B 205 -23.256 15.558 47.756 0.64 30.61 O ANISOU 4111 O BILE B 205 3884 3397 4350 -390 267 -74 O ATOM 4112 CB AILE B 205 -23.338 14.288 50.811 0.36 26.47 C ANISOU 4112 CB AILE B 205 3408 2810 3840 -325 405 58 C ATOM 4113 CB BILE B 205 -23.338 14.271 50.845 0.64 26.43 C ANISOU 4113 CB BILE B 205 3402 2803 3835 -324 407 60 C ATOM 4114 CG1AILE B 205 -22.616 14.199 52.157 0.36 30.52 C ANISOU 4114 CG1AILE B 205 3960 3326 4310 -269 434 127 C ATOM 4115 CG1BILE B 205 -22.417 14.102 52.068 0.64 30.67 C ANISOU 4115 CG1BILE B 205 3983 3342 4329 -268 432 127 C ATOM 4116 CG2AILE B 205 -22.917 13.151 49.877 0.36 31.25 C ANISOU 4116 CG2AILE B 205 4009 3368 4498 -354 422 32 C ATOM 4117 CG2BILE B 205 -23.116 13.114 49.857 0.64 31.42 C ANISOU 4117 CG2BILE B 205 4025 3387 4527 -360 426 28 C ATOM 4118 CD1AILE B 205 -21.111 14.298 52.066 0.36 25.40 C ANISOU 4118 CD1AILE B 205 3343 2694 3613 -238 400 140 C ATOM 4119 CD1BILE B 205 -22.811 12.943 53.049 0.64 28.56 C ANISOU 4119 CD1BILE B 205 3724 3024 4104 -254 520 180 C ATOM 4120 N TYR B 206 -25.121 16.077 48.894 1.00 28.21 N ANISOU 4120 N TYR B 206 3548 3104 4067 -393 304 -56 N ATOM 4121 CA TYR B 206 -25.901 16.295 47.682 1.00 29.82 C ANISOU 4121 CA TYR B 206 3708 3325 4296 -434 271 -116 C ATOM 4122 C TYR B 206 -25.338 17.449 46.859 1.00 28.89 C ANISOU 4122 C TYR B 206 3594 3259 4122 -423 198 -138 C ATOM 4123 O TYR B 206 -25.150 17.329 45.643 1.00 27.08 O ANISOU 4123 O TYR B 206 3350 3040 3898 -446 166 -181 O ATOM 4124 CB TYR B 206 -27.353 16.564 48.076 1.00 27.25 C ANISOU 4124 CB TYR B 206 3345 3008 4000 -448 291 -121 C ATOM 4125 CG TYR B 206 -28.169 17.347 47.059 1.00 29.48 C ANISOU 4125 CG TYR B 206 3584 3336 4281 -472 241 -172 C ATOM 4126 CD1 TYR B 206 -28.618 16.746 45.895 1.00 30.03 C ANISOU 4126 CD1 TYR B 206 3614 3402 4393 -514 230 -229 C ATOM 4127 CD2 TYR B 206 -28.527 18.675 47.297 1.00 29.25 C ANISOU 4127 CD2 TYR B 206 3550 3354 4210 -448 207 -162 C ATOM 4128 CE1 TYR B 206 -29.398 17.430 44.993 1.00 30.02 C ANISOU 4128 CE1 TYR B 206 3570 3449 4387 -531 184 -273 C ATOM 4129 CE2 TYR B 206 -29.297 19.375 46.386 1.00 26.62 C ANISOU 4129 CE2 TYR B 206 3176 3063 3876 -464 164 -201 C ATOM 4130 CZ TYR B 206 -29.724 18.745 45.230 1.00 31.73 C ANISOU 4130 CZ TYR B 206 3784 3712 4560 -503 151 -255 C ATOM 4131 OH TYR B 206 -30.493 19.430 44.312 1.00 30.33 O ANISOU 4131 OH TYR B 206 3563 3586 4377 -514 107 -293 O ATOM 4132 N MET B 207 -25.017 18.564 47.513 1.00 27.15 N ANISOU 4132 N MET B 207 3395 3072 3849 -387 175 -108 N ATOM 4133 CA MET B 207 -24.484 19.710 46.777 1.00 23.33 C ANISOU 4133 CA MET B 207 2914 2631 3317 -376 113 -125 C ATOM 4134 C MET B 207 -23.153 19.386 46.096 1.00 26.79 C ANISOU 4134 C MET B 207 3378 3063 3738 -373 92 -131 C ATOM 4135 O MET B 207 -22.960 19.694 44.915 1.00 26.96 O ANISOU 4135 O MET B 207 3386 3105 3750 -385 52 -164 O ATOM 4136 CB MET B 207 -24.318 20.919 47.716 1.00 21.91 C ANISOU 4136 CB MET B 207 2755 2480 3090 -339 100 -94 C ATOM 4137 CG MET B 207 -23.720 22.114 46.988 1.00 27.44 C ANISOU 4137 CG MET B 207 3460 3217 3750 -327 43 -108 C ATOM 4138 SD MET B 207 -23.632 23.582 48.028 1.00 32.25 S ANISOU 4138 SD MET B 207 4086 3855 4313 -290 30 -83 S ATOM 4139 CE MET B 207 -22.203 23.225 48.987 1.00 26.77 C ANISOU 4139 CE MET B 207 3437 3147 3586 -260 42 -51 C ATOM 4140 N PHE B 208 -22.206 18.783 46.822 1.00 24.57 N ANISOU 4140 N PHE B 208 3131 2755 3449 -352 118 -97 N ATOM 4141 CA PHE B 208 -20.900 18.519 46.209 1.00 24.20 C ANISOU 4141 CA PHE B 208 3106 2703 3386 -345 98 -101 C ATOM 4142 C PHE B 208 -20.965 17.434 45.134 1.00 29.45 C ANISOU 4142 C PHE B 208 3755 3340 4094 -380 109 -138 C ATOM 4143 O PHE B 208 -20.154 17.452 44.200 1.00 27.86 O ANISOU 4143 O PHE B 208 3560 3146 3878 -383 80 -158 O ATOM 4144 CB PHE B 208 -19.860 18.139 47.258 1.00 27.47 C ANISOU 4144 CB PHE B 208 3557 3101 3779 -310 122 -54 C ATOM 4145 CG PHE B 208 -19.138 19.329 47.844 1.00 21.37 C ANISOU 4145 CG PHE B 208 2804 2366 2949 -276 87 -34 C ATOM 4146 CD1 PHE B 208 -18.114 19.928 47.162 1.00 25.50 C ANISOU 4146 CD1 PHE B 208 3336 2909 3443 -269 44 -47 C ATOM 4147 CD2 PHE B 208 -19.520 19.846 49.060 1.00 33.50 C ANISOU 4147 CD2 PHE B 208 4348 3918 4464 -251 101 -7 C ATOM 4148 CE1 PHE B 208 -17.471 21.042 47.685 1.00 31.40 C ANISOU 4148 CE1 PHE B 208 4097 3688 4146 -241 15 -35 C ATOM 4149 CE2 PHE B 208 -18.882 20.941 49.589 1.00 31.59 C ANISOU 4149 CE2 PHE B 208 4121 3710 4172 -223 70 2 C ATOM 4150 CZ PHE B 208 -17.856 21.536 48.896 1.00 32.14 C ANISOU 4150 CZ PHE B 208 4198 3797 4219 -220 27 -14 C ATOM 4151 N VAL B 209 -21.910 16.496 45.226 1.00 27.91 N ANISOU 4151 N VAL B 209 3539 3112 3955 -408 152 -151 N ATOM 4152 CA VAL B 209 -21.971 15.414 44.241 1.00 25.56 C ANISOU 4152 CA VAL B 209 3225 2784 3704 -443 166 -194 C ATOM 4153 C VAL B 209 -22.716 15.850 42.985 1.00 26.90 C ANISOU 4153 C VAL B 209 3355 2990 3875 -474 124 -253 C ATOM 4154 O VAL B 209 -22.198 15.752 41.867 1.00 27.23 O ANISOU 4154 O VAL B 209 3395 3046 3907 -485 94 -288 O ATOM 4155 CB VAL B 209 -22.621 14.154 44.847 1.00 30.96 C ANISOU 4155 CB VAL B 209 3900 3410 4455 -463 236 -186 C ATOM 4156 CG1 VAL B 209 -22.970 13.161 43.730 1.00 33.69 C ANISOU 4156 CG1 VAL B 209 4217 3728 4856 -509 247 -247 C ATOM 4157 CG2 VAL B 209 -21.712 13.521 45.890 1.00 28.68 C ANISOU 4157 CG2 VAL B 209 3651 3083 4163 -428 280 -126 C ATOM 4158 N AVAL B 210 -23.961 16.312 43.161 0.76 24.11 N ANISOU 4158 N AVAL B 210 2968 2658 3534 -486 121 -263 N ATOM 4159 N BVAL B 210 -23.950 16.317 43.126 0.24 24.25 N ANISOU 4159 N BVAL B 210 2986 2677 3551 -487 120 -264 N ATOM 4160 CA AVAL B 210 -24.833 16.662 42.039 0.76 26.09 C ANISOU 4160 CA AVAL B 210 3174 2949 3789 -513 84 -318 C ATOM 4161 CA BVAL B 210 -24.707 16.609 41.914 0.24 26.16 C ANISOU 4161 CA BVAL B 210 3185 2958 3796 -514 81 -322 C ATOM 4162 C AVAL B 210 -24.429 17.997 41.420 0.76 26.61 C ANISOU 4162 C AVAL B 210 3245 3073 3791 -489 23 -317 C ATOM 4163 C BVAL B 210 -24.452 18.022 41.392 0.24 26.56 C ANISOU 4163 C BVAL B 210 3238 3068 3785 -489 22 -318 C ATOM 4164 O AVAL B 210 -24.494 18.177 40.198 0.76 26.44 O ANISOU 4164 O AVAL B 210 3203 3086 3756 -500 -15 -358 O ATOM 4165 O BVAL B 210 -24.633 18.275 40.196 0.24 26.42 O ANISOU 4165 O BVAL B 210 3196 3088 3753 -501 -17 -359 O ATOM 4166 CB AVAL B 210 -26.307 16.685 42.492 0.76 26.55 C ANISOU 4166 CB AVAL B 210 3192 3010 3886 -532 106 -327 C ATOM 4167 CB BVAL B 210 -26.208 16.370 42.122 0.24 25.99 C ANISOU 4167 CB BVAL B 210 3117 2935 3824 -543 104 -344 C ATOM 4168 CG1AVAL B 210 -27.211 17.170 41.366 0.76 23.68 C ANISOU 4168 CG1AVAL B 210 2778 2699 3519 -554 61 -381 C ATOM 4169 CG1BVAL B 210 -26.468 14.964 42.646 0.24 25.59 C ANISOU 4169 CG1BVAL B 210 3062 2816 3843 -569 172 -346 C ATOM 4170 CG2AVAL B 210 -26.756 15.295 42.994 0.76 24.42 C ANISOU 4170 CG2AVAL B 210 2911 2677 3689 -562 173 -332 C ATOM 4171 CG2BVAL B 210 -26.748 17.371 43.068 0.24 24.86 C ANISOU 4171 CG2BVAL B 210 2974 2813 3658 -517 103 -304 C ATOM 4172 N HIS B 211 -24.038 18.962 42.245 1.00 23.47 N ANISOU 4172 N HIS B 211 2874 2688 3355 -453 14 -270 N ATOM 4173 CA HIS B 211 -23.852 20.334 41.788 1.00 25.94 C ANISOU 4173 CA HIS B 211 3188 3050 3618 -430 -35 -266 C ATOM 4174 C HIS B 211 -22.403 20.762 41.778 1.00 28.74 C ANISOU 4174 C HIS B 211 3584 3406 3932 -403 -53 -241 C ATOM 4175 O HIS B 211 -22.131 21.967 41.802 1.00 24.13 O ANISOU 4175 O HIS B 211 3007 2850 3310 -378 -82 -224 O ATOM 4176 CB HIS B 211 -24.691 21.288 42.641 1.00 27.60 C ANISOU 4176 CB HIS B 211 3388 3279 3821 -414 -33 -241 C ATOM 4177 CG HIS B 211 -26.154 21.035 42.505 1.00 27.33 C ANISOU 4177 CG HIS B 211 3306 3254 3825 -439 -22 -268 C ATOM 4178 ND1 HIS B 211 -26.841 21.309 41.342 1.00 27.12 N ANISOU 4178 ND1 HIS B 211 3239 3269 3798 -454 -57 -309 N ATOM 4179 CD2 HIS B 211 -27.059 20.503 43.365 1.00 23.70 C ANISOU 4179 CD2 HIS B 211 2830 2768 3406 -453 21 -261 C ATOM 4180 CE1 HIS B 211 -28.107 20.948 41.485 1.00 27.85 C ANISOU 4180 CE1 HIS B 211 3290 3362 3931 -478 -38 -329 C ATOM 4181 NE2 HIS B 211 -28.265 20.444 42.696 1.00 26.42 N ANISOU 4181 NE2 HIS B 211 3122 3138 3779 -479 11 -301 N ATOM 4182 N PHE B 212 -21.469 19.819 41.885 1.00 26.94 N ANISOU 4182 N PHE B 212 3381 3142 3714 -404 -32 -235 N ATOM 4183 CA PHE B 212 -20.081 20.122 41.575 1.00 26.12 C ANISOU 4183 CA PHE B 212 3307 3041 3576 -383 -53 -222 C ATOM 4184 C PHE B 212 -19.381 19.006 40.789 1.00 27.84 C ANISOU 4184 C PHE B 212 3532 3236 3812 -399 -44 -246 C ATOM 4185 O PHE B 212 -18.914 19.214 39.661 1.00 28.29 O ANISOU 4185 O PHE B 212 3586 3314 3848 -402 -73 -269 O ATOM 4186 CB PHE B 212 -19.388 20.444 42.899 1.00 24.10 C ANISOU 4186 CB PHE B 212 3083 2773 3300 -353 -39 -175 C ATOM 4187 CG PHE B 212 -17.940 20.756 42.773 1.00 24.92 C ANISOU 4187 CG PHE B 212 3215 2881 3373 -330 -58 -160 C ATOM 4188 CD1 PHE B 212 -17.517 21.920 42.155 1.00 31.40 C ANISOU 4188 CD1 PHE B 212 4035 3734 4162 -319 -97 -164 C ATOM 4189 CD2 PHE B 212 -16.996 19.883 43.277 1.00 30.73 C ANISOU 4189 CD2 PHE B 212 3975 3586 4115 -320 -33 -139 C ATOM 4190 CE1 PHE B 212 -16.166 22.199 42.047 1.00 32.75 C ANISOU 4190 CE1 PHE B 212 4228 3906 4309 -301 -112 -152 C ATOM 4191 CE2 PHE B 212 -15.650 20.160 43.164 1.00 38.56 C ANISOU 4191 CE2 PHE B 212 4988 4584 5080 -299 -51 -126 C ATOM 4192 CZ PHE B 212 -15.237 21.321 42.564 1.00 35.13 C ANISOU 4192 CZ PHE B 212 4551 4180 4615 -291 -91 -134 C ATOM 4193 N ILE B 213 -19.379 17.785 41.341 1.00 28.60 N ANISOU 4193 N ILE B 213 3636 3285 3948 -410 2 -240 N ATOM 4194 CA AILE B 213 -18.610 16.694 40.739 0.80 27.18 C ANISOU 4194 CA AILE B 213 3467 3073 3788 -421 19 -258 C ATOM 4195 CA BILE B 213 -18.605 16.705 40.733 0.21 27.15 C ANISOU 4195 CA BILE B 213 3463 3070 3783 -421 18 -258 C ATOM 4196 C ILE B 213 -19.228 16.264 39.410 1.00 25.87 C ANISOU 4196 C ILE B 213 3270 2919 3642 -457 6 -320 C ATOM 4197 O ILE B 213 -18.535 16.139 38.395 1.00 28.47 O ANISOU 4197 O ILE B 213 3604 3259 3955 -459 -14 -345 O ATOM 4198 CB AILE B 213 -18.499 15.501 41.711 0.80 24.93 C ANISOU 4198 CB AILE B 213 3198 2731 3545 -421 77 -231 C ATOM 4199 CB BILE B 213 -18.459 15.527 41.712 0.21 25.10 C ANISOU 4199 CB BILE B 213 3220 2753 3564 -420 76 -230 C ATOM 4200 CG1AILE B 213 -17.454 15.739 42.798 0.80 29.16 C ANISOU 4200 CG1AILE B 213 3769 3260 4050 -379 86 -173 C ATOM 4201 CG1BILE B 213 -17.537 15.910 42.869 0.21 29.19 C ANISOU 4201 CG1BILE B 213 3772 3270 4050 -378 82 -171 C ATOM 4202 CG2AILE B 213 -18.133 14.222 40.929 0.80 31.19 C ANISOU 4202 CG2AILE B 213 3990 3484 4378 -444 103 -264 C ATOM 4203 CG2BILE B 213 -17.910 14.305 40.984 0.21 30.88 C ANISOU 4203 CG2BILE B 213 3957 3446 4331 -437 100 -257 C ATOM 4204 CD1AILE B 213 -17.616 14.790 44.030 0.80 33.98 C ANISOU 4204 CD1AILE B 213 4393 3825 4694 -369 146 -132 C ATOM 4205 CD1BILE B 213 -16.131 16.269 42.440 0.21 30.81 C ANISOU 4205 CD1BILE B 213 3999 3489 4217 -355 52 -163 C ATOM 4206 N ILE B 214 -20.545 16.023 39.395 1.00 25.42 N ANISOU 4206 N ILE B 214 3177 2863 3619 -485 17 -348 N ATOM 4207 CA ILE B 214 -21.192 15.554 38.167 1.00 24.25 C ANISOU 4207 CA ILE B 214 2993 2731 3490 -520 3 -415 C ATOM 4208 C ILE B 214 -21.054 16.554 37.019 1.00 26.81 C ANISOU 4208 C ILE B 214 3307 3120 3759 -509 -55 -436 C ATOM 4209 O ILE B 214 -20.693 16.136 35.906 1.00 26.58 O ANISOU 4209 O ILE B 214 3273 3102 3723 -521 -70 -479 O ATOM 4210 CB ILE B 214 -22.650 15.153 38.460 1.00 26.83 C ANISOU 4210 CB ILE B 214 3279 3050 3867 -552 26 -441 C ATOM 4211 CG1 ILE B 214 -22.646 13.835 39.256 1.00 31.94 C ANISOU 4211 CG1 ILE B 214 3936 3622 4578 -568 94 -430 C ATOM 4212 CG2 ILE B 214 -23.471 15.050 37.139 1.00 35.32 C ANISOU 4212 CG2 ILE B 214 4307 4166 4948 -584 -5 -515 C ATOM 4213 CD1 ILE B 214 -23.959 13.400 39.824 1.00 30.65 C ANISOU 4213 CD1 ILE B 214 3738 3437 4472 -596 131 -442 C ATOM 4214 N PRO B 215 -21.325 17.851 37.197 1.00 27.44 N ANISOU 4214 N PRO B 215 3383 3243 3800 -485 -87 -410 N ATOM 4215 CA PRO B 215 -21.060 18.801 36.095 1.00 27.38 C ANISOU 4215 CA PRO B 215 3370 3293 3741 -468 -136 -421 C ATOM 4216 C PRO B 215 -19.627 18.771 35.601 1.00 26.91 C ANISOU 4216 C PRO B 215 3344 3226 3652 -451 -144 -410 C ATOM 4217 O PRO B 215 -19.383 18.834 34.389 1.00 28.35 O ANISOU 4217 O PRO B 215 3520 3443 3810 -451 -170 -441 O ATOM 4218 CB PRO B 215 -21.372 20.170 36.724 1.00 28.81 C ANISOU 4218 CB PRO B 215 3552 3500 3894 -440 -154 -378 C ATOM 4219 CG PRO B 215 -22.250 19.894 37.871 1.00 28.55 C ANISOU 4219 CG PRO B 215 3508 3440 3898 -451 -122 -365 C ATOM 4220 CD PRO B 215 -22.005 18.496 38.336 1.00 28.33 C ANISOU 4220 CD PRO B 215 3492 3355 3916 -473 -77 -372 C ATOM 4221 N LEU B 216 -18.664 18.702 36.520 1.00 28.72 N ANISOU 4221 N LEU B 216 3610 3418 3884 -433 -123 -366 N ATOM 4222 CA LEU B 216 -17.268 18.686 36.110 1.00 28.84 C ANISOU 4222 CA LEU B 216 3655 3426 3875 -415 -128 -354 C ATOM 4223 C LEU B 216 -16.957 17.435 35.297 1.00 31.82 C ANISOU 4223 C LEU B 216 4032 3782 4276 -438 -112 -397 C ATOM 4224 O LEU B 216 -16.237 17.498 34.296 1.00 31.44 O ANISOU 4224 O LEU B 216 3991 3754 4202 -431 -130 -413 O ATOM 4225 CB LEU B 216 -16.369 18.789 37.340 1.00 28.16 C ANISOU 4225 CB LEU B 216 3602 3308 3789 -392 -109 -302 C ATOM 4226 CG LEU B 216 -16.168 20.189 37.934 1.00 37.26 C ANISOU 4226 CG LEU B 216 4763 4485 4908 -363 -131 -263 C ATOM 4227 CD1 LEU B 216 -14.999 20.190 38.928 1.00 40.55 C ANISOU 4227 CD1 LEU B 216 5212 4877 5319 -340 -118 -222 C ATOM 4228 CD2 LEU B 216 -15.938 21.234 36.861 1.00 32.66 C ANISOU 4228 CD2 LEU B 216 4174 3946 4288 -352 -169 -270 C ATOM 4229 N ILE B 217 -17.513 16.291 35.696 1.00 30.62 N ANISOU 4229 N ILE B 217 3871 3589 4176 -464 -75 -417 N ATOM 4230 CA ILE B 217 -17.291 15.061 34.944 1.00 30.17 C ANISOU 4230 CA ILE B 217 3810 3504 4148 -489 -54 -464 C ATOM 4231 C ILE B 217 -17.778 15.214 33.508 1.00 31.10 C ANISOU 4231 C ILE B 217 3899 3675 4243 -505 -90 -525 C ATOM 4232 O ILE B 217 -17.085 14.808 32.565 1.00 33.93 O ANISOU 4232 O ILE B 217 4266 4038 4588 -506 -95 -554 O ATOM 4233 CB ILE B 217 -17.978 13.877 35.643 1.00 32.16 C ANISOU 4233 CB ILE B 217 4052 3700 4468 -518 -3 -477 C ATOM 4234 CG1 ILE B 217 -17.231 13.505 36.911 1.00 33.45 C ANISOU 4234 CG1 ILE B 217 4250 3811 4649 -495 38 -416 C ATOM 4235 CG2 ILE B 217 -18.059 12.668 34.719 1.00 37.29 C ANISOU 4235 CG2 ILE B 217 4688 4326 5156 -552 17 -543 C ATOM 4236 CD1 ILE B 217 -17.975 12.461 37.726 1.00 38.06 C ANISOU 4236 CD1 ILE B 217 4824 4338 5298 -517 94 -415 C ATOM 4237 N VAL B 218 -18.965 15.820 33.320 1.00 28.56 N ANISOU 4237 N VAL B 218 3541 3397 3912 -514 -116 -544 N ATOM 4238 CA VAL B 218 -19.538 15.995 31.982 1.00 25.19 C ANISOU 4238 CA VAL B 218 3082 3032 3458 -525 -153 -601 C ATOM 4239 C VAL B 218 -18.669 16.907 31.133 1.00 30.77 C ANISOU 4239 C VAL B 218 3807 3786 4100 -491 -189 -583 C ATOM 4240 O VAL B 218 -18.431 16.642 29.950 1.00 31.86 O ANISOU 4240 O VAL B 218 3937 3954 4212 -494 -206 -626 O ATOM 4241 CB VAL B 218 -20.970 16.551 32.066 1.00 30.69 C ANISOU 4241 CB VAL B 218 3735 3770 4157 -535 -174 -615 C ATOM 4242 CG1 VAL B 218 -21.500 16.878 30.670 1.00 35.11 C ANISOU 4242 CG1 VAL B 218 4259 4405 4675 -536 -219 -667 C ATOM 4243 CG2 VAL B 218 -21.897 15.564 32.772 1.00 35.30 C ANISOU 4243 CG2 VAL B 218 4295 4308 4811 -574 -134 -641 C ATOM 4244 N ILE B 219 -18.245 18.035 31.709 1.00 30.88 N ANISOU 4244 N ILE B 219 3841 3808 4085 -458 -201 -521 N ATOM 4245 CA ILE B 219 -17.424 19.002 30.985 1.00 29.87 C ANISOU 4245 CA ILE B 219 3728 3718 3901 -424 -229 -497 C ATOM 4246 C ILE B 219 -16.116 18.358 30.534 1.00 37.40 C ANISOU 4246 C ILE B 219 4713 4647 4852 -420 -214 -502 C ATOM 4247 O ILE B 219 -15.704 18.488 29.372 1.00 34.25 O ANISOU 4247 O ILE B 219 4313 4285 4415 -409 -233 -522 O ATOM 4248 CB ILE B 219 -17.166 20.237 31.871 1.00 33.27 C ANISOU 4248 CB ILE B 219 4176 4148 4317 -395 -235 -432 C ATOM 4249 CG1 ILE B 219 -18.438 21.077 32.025 1.00 29.67 C ANISOU 4249 CG1 ILE B 219 3688 3729 3854 -392 -255 -428 C ATOM 4250 CG2 ILE B 219 -16.037 21.090 31.315 1.00 36.71 C ANISOU 4250 CG2 ILE B 219 4634 4602 4710 -362 -250 -401 C ATOM 4251 CD1 ILE B 219 -18.365 21.998 33.264 1.00 28.81 C ANISOU 4251 CD1 ILE B 219 3596 3600 3749 -372 -247 -373 C ATOM 4252 N PHE B 220 -15.438 17.659 31.445 1.00 29.39 N ANISOU 4252 N PHE B 220 3723 3570 3873 -424 -179 -480 N ATOM 4253 CA PHE B 220 -14.158 17.082 31.059 1.00 34.50 C ANISOU 4253 CA PHE B 220 4397 4193 4519 -416 -164 -480 C ATOM 4254 C PHE B 220 -14.323 15.856 30.168 1.00 34.31 C ANISOU 4254 C PHE B 220 4362 4161 4514 -444 -150 -546 C ATOM 4255 O PHE B 220 -13.433 15.564 29.368 1.00 37.61 O ANISOU 4255 O PHE B 220 4794 4581 4914 -436 -149 -560 O ATOM 4256 CB PHE B 220 -13.333 16.786 32.307 1.00 34.53 C ANISOU 4256 CB PHE B 220 4430 4140 4550 -406 -133 -432 C ATOM 4257 CG PHE B 220 -12.696 18.023 32.888 1.00 47.85 C ANISOU 4257 CG PHE B 220 6132 5841 6207 -374 -150 -375 C ATOM 4258 CD1 PHE B 220 -11.619 18.633 32.252 1.00 44.34 C ANISOU 4258 CD1 PHE B 220 5703 5416 5730 -350 -165 -359 C ATOM 4259 CD2 PHE B 220 -13.194 18.605 34.041 1.00 47.25 C ANISOU 4259 CD2 PHE B 220 6056 5760 6139 -368 -149 -342 C ATOM 4260 CE1 PHE B 220 -11.042 19.776 32.772 1.00 50.21 C ANISOU 4260 CE1 PHE B 220 6457 6169 6453 -325 -178 -313 C ATOM 4261 CE2 PHE B 220 -12.615 19.749 34.565 1.00 49.78 C ANISOU 4261 CE2 PHE B 220 6388 6091 6434 -341 -164 -298 C ATOM 4262 CZ PHE B 220 -11.544 20.337 33.931 1.00 53.75 C ANISOU 4262 CZ PHE B 220 6903 6610 6910 -321 -179 -285 C ATOM 4263 N PHE B 221 -15.452 15.145 30.255 1.00 35.54 N ANISOU 4263 N PHE B 221 4490 4307 4708 -478 -139 -591 N ATOM 4264 CA PHE B 221 -15.722 14.109 29.264 1.00 38.55 C ANISOU 4264 CA PHE B 221 4854 4690 5105 -507 -132 -666 C ATOM 4265 C PHE B 221 -15.820 14.717 27.867 1.00 35.21 C ANISOU 4265 C PHE B 221 4414 4345 4620 -495 -176 -701 C ATOM 4266 O PHE B 221 -15.161 14.260 26.925 1.00 37.34 O ANISOU 4266 O PHE B 221 4693 4624 4871 -493 -175 -734 O ATOM 4267 CB PHE B 221 -17.006 13.360 29.614 1.00 36.24 C ANISOU 4267 CB PHE B 221 4526 4377 4867 -548 -114 -710 C ATOM 4268 CG PHE B 221 -17.409 12.359 28.573 1.00 40.60 C ANISOU 4268 CG PHE B 221 5053 4936 5438 -582 -110 -799 C ATOM 4269 CD1 PHE B 221 -18.192 12.737 27.493 1.00 40.36 C ANISOU 4269 CD1 PHE B 221 4985 4982 5368 -589 -154 -855 C ATOM 4270 CD2 PHE B 221 -16.984 11.044 28.662 1.00 48.86 C ANISOU 4270 CD2 PHE B 221 6111 5913 6540 -605 -62 -829 C ATOM 4271 CE1 PHE B 221 -18.550 11.823 26.517 1.00 48.93 C ANISOU 4271 CE1 PHE B 221 6044 6080 6467 -621 -153 -945 C ATOM 4272 CE2 PHE B 221 -17.347 10.115 27.688 1.00 52.22 C ANISOU 4272 CE2 PHE B 221 6511 6343 6987 -640 -57 -919 C ATOM 4273 CZ PHE B 221 -18.127 10.510 26.617 1.00 48.14 C ANISOU 4273 CZ PHE B 221 5957 5908 6428 -649 -104 -980 C ATOM 4274 N CYS B 222 -16.622 15.774 27.728 1.00 33.71 N ANISOU 4274 N CYS B 222 4201 4214 4395 -483 -213 -689 N ATOM 4275 CA CYS B 222 -16.807 16.420 26.429 1.00 40.86 C ANISOU 4275 CA CYS B 222 5088 5200 5236 -465 -255 -714 C ATOM 4276 C CYS B 222 -15.496 16.988 25.896 1.00 45.42 C ANISOU 4276 C CYS B 222 5701 5791 5767 -428 -260 -675 C ATOM 4277 O CYS B 222 -15.184 16.848 24.705 1.00 45.11 O ANISOU 4277 O CYS B 222 5659 5793 5687 -419 -273 -711 O ATOM 4278 CB CYS B 222 -17.859 17.523 26.549 1.00 37.55 C ANISOU 4278 CB CYS B 222 4641 4836 4792 -452 -288 -693 C ATOM 4279 SG CYS B 222 -19.535 16.903 26.788 1.00 37.91 S ANISOU 4279 SG CYS B 222 4633 4890 4883 -495 -290 -754 S ATOM 4280 N TYR B 223 -14.712 17.624 26.765 1.00 40.17 N ANISOU 4280 N TYR B 223 5065 5090 5106 -406 -248 -605 N ATOM 4281 CA TYR B 223 -13.411 18.148 26.355 1.00 47.78 C ANISOU 4281 CA TYR B 223 6059 6059 6036 -373 -248 -567 C ATOM 4282 C TYR B 223 -12.474 17.033 25.911 1.00 45.83 C ANISOU 4282 C TYR B 223 5831 5779 5804 -382 -221 -598 C ATOM 4283 O TYR B 223 -11.759 17.175 24.913 1.00 44.80 O ANISOU 4283 O TYR B 223 5711 5678 5633 -363 -228 -604 O ATOM 4284 CB TYR B 223 -12.799 18.946 27.508 1.00 48.84 C ANISOU 4284 CB TYR B 223 6216 6158 6183 -354 -238 -495 C ATOM 4285 CG TYR B 223 -11.281 18.931 27.608 1.00 58.40 C ANISOU 4285 CG TYR B 223 7460 7337 7393 -335 -220 -461 C ATOM 4286 CD1 TYR B 223 -10.512 19.911 26.993 1.00 61.29 C ANISOU 4286 CD1 TYR B 223 7836 7732 7718 -303 -232 -428 C ATOM 4287 CD2 TYR B 223 -10.621 17.960 28.363 1.00 55.90 C ANISOU 4287 CD2 TYR B 223 7162 6958 7120 -346 -188 -457 C ATOM 4288 CE1 TYR B 223 -9.128 19.915 27.102 1.00 57.07 C ANISOU 4288 CE1 TYR B 223 7327 7169 7188 -287 -215 -398 C ATOM 4289 CE2 TYR B 223 -9.248 17.951 28.475 1.00 59.11 C ANISOU 4289 CE2 TYR B 223 7593 7339 7526 -327 -172 -426 C ATOM 4290 CZ TYR B 223 -8.503 18.929 27.842 1.00 69.92 C ANISOU 4290 CZ TYR B 223 8970 8741 8857 -300 -187 -398 C ATOM 4291 OH TYR B 223 -7.129 18.914 27.958 1.00 75.49 O ANISOU 4291 OH TYR B 223 9696 9420 9566 -282 -171 -369 O ATOM 4292 N GLY B 224 -12.453 15.920 26.653 1.00 44.05 N ANISOU 4292 N GLY B 224 5612 5490 5636 -409 -188 -614 N ATOM 4293 CA GLY B 224 -11.599 14.806 26.281 1.00 43.55 C ANISOU 4293 CA GLY B 224 5566 5387 5592 -417 -158 -643 C ATOM 4294 C GLY B 224 -11.952 14.239 24.923 1.00 54.45 C ANISOU 4294 C GLY B 224 6929 6810 6951 -432 -169 -720 C ATOM 4295 O GLY B 224 -11.069 13.901 24.131 1.00 57.53 O ANISOU 4295 O GLY B 224 7335 7203 7321 -420 -160 -737 O ATOM 4296 N GLN B 225 -13.251 14.123 24.639 1.00 51.93 N ANISOU 4296 N GLN B 225 6573 6525 6633 -456 -188 -771 N ATOM 4297 CA GLN B 225 -13.685 13.736 23.306 1.00 49.67 C ANISOU 4297 CA GLN B 225 6263 6295 6314 -467 -208 -849 C ATOM 4298 C GLN B 225 -13.246 14.759 22.267 1.00 56.49 C ANISOU 4298 C GLN B 225 7133 7236 7096 -425 -241 -829 C ATOM 4299 O GLN B 225 -12.941 14.399 21.126 1.00 56.72 O ANISOU 4299 O GLN B 225 7161 7302 7088 -420 -246 -877 O ATOM 4300 CB GLN B 225 -15.205 13.561 23.280 1.00 46.70 C ANISOU 4300 CB GLN B 225 5841 5949 5952 -499 -227 -904 C ATOM 4301 CG GLN B 225 -15.711 12.374 24.084 1.00 49.39 C ANISOU 4301 CG GLN B 225 6171 6215 6378 -545 -188 -939 C ATOM 4302 CD GLN B 225 -15.312 11.044 23.477 1.00 59.55 C ANISOU 4302 CD GLN B 225 7462 7467 7698 -571 -157 -1011 C ATOM 4303 OE1 GLN B 225 -14.594 10.255 24.095 1.00 61.51 O ANISOU 4303 OE1 GLN B 225 7738 7635 7999 -578 -109 -994 O ATOM 4304 NE2 GLN B 225 -15.780 10.783 22.261 1.00 61.36 N ANISOU 4304 NE2 GLN B 225 7662 7758 7893 -583 -182 -1094 N ATOM 4305 N LEU B 226 -13.229 16.043 22.635 1.00 48.36 N ANISOU 4305 N LEU B 226 6108 6230 6038 -394 -261 -759 N ATOM 4306 CA LEU B 226 -12.731 17.064 21.716 1.00 56.28 C ANISOU 4306 CA LEU B 226 7119 7296 6969 -351 -284 -727 C ATOM 4307 C LEU B 226 -11.246 16.875 21.426 1.00 59.65 C ANISOU 4307 C LEU B 226 7582 7693 7388 -332 -258 -704 C ATOM 4308 O LEU B 226 -10.809 16.992 20.276 1.00 62.23 O ANISOU 4308 O LEU B 226 7913 8069 7662 -310 -266 -720 O ATOM 4309 CB LEU B 226 -12.968 18.465 22.288 1.00 60.26 C ANISOU 4309 CB LEU B 226 7622 7817 7456 -324 -302 -654 C ATOM 4310 CG LEU B 226 -14.275 19.212 22.027 1.00 60.93 C ANISOU 4310 CG LEU B 226 7671 7969 7511 -317 -338 -660 C ATOM 4311 CD1 LEU B 226 -14.023 20.715 22.022 1.00 59.26 C ANISOU 4311 CD1 LEU B 226 7468 7786 7262 -272 -350 -584 C ATOM 4312 CD2 LEU B 226 -14.890 18.781 20.726 1.00 57.59 C ANISOU 4312 CD2 LEU B 226 7219 7620 7042 -319 -363 -732 C ATOM 4313 N VAL B 227 -10.451 16.596 22.461 1.00 51.78 N ANISOU 4313 N VAL B 227 6611 6622 6442 -338 -227 -665 N ATOM 4314 CA VAL B 227 -9.000 16.585 22.302 1.00 59.03 C ANISOU 4314 CA VAL B 227 7560 7513 7355 -315 -204 -632 C ATOM 4315 C VAL B 227 -8.550 15.356 21.523 1.00 64.07 C ANISOU 4315 C VAL B 227 8205 8138 7999 -328 -182 -694 C ATOM 4316 O VAL B 227 -7.738 15.453 20.596 1.00 68.42 O ANISOU 4316 O VAL B 227 8769 8716 8510 -305 -178 -695 O ATOM 4317 CB VAL B 227 -8.312 16.674 23.674 1.00 59.62 C ANISOU 4317 CB VAL B 227 7654 7518 7478 -314 -182 -572 C ATOM 4318 CG1 VAL B 227 -6.899 16.115 23.594 1.00 58.85 C ANISOU 4318 CG1 VAL B 227 7584 7381 7396 -303 -150 -560 C ATOM 4319 CG2 VAL B 227 -8.297 18.118 24.147 1.00 56.12 C ANISOU 4319 CG2 VAL B 227 7212 7095 7015 -290 -201 -507 C ATOM 4320 N PHE B 228 -9.068 14.185 21.880 1.00 63.99 N ANISOU 4320 N PHE B 228 8187 8087 8041 -366 -164 -746 N ATOM 4321 CA PHE B 228 -8.703 12.943 21.197 1.00 69.06 C ANISOU 4321 CA PHE B 228 8833 8708 8697 -382 -138 -812 C ATOM 4322 C PHE B 228 -9.684 12.629 20.061 1.00 79.65 C ANISOU 4322 C PHE B 228 10145 10114 10004 -399 -163 -898 C ATOM 4323 O PHE B 228 -10.280 11.552 19.986 1.00 83.95 O ANISOU 4323 O PHE B 228 10673 10636 10588 -437 -149 -971 O ATOM 4324 CB PHE B 228 -8.627 11.801 22.203 1.00 70.85 C ANISOU 4324 CB PHE B 228 9068 8845 9006 -412 -96 -820 C ATOM 4325 N THR B 229 -9.836 13.596 19.158 1.00 84.36 N ANISOU 4325 N THR B 229 10732 10795 10524 -369 -199 -890 N ATOM 4326 CA THR B 229 -10.658 13.431 17.955 1.00 87.25 C ANISOU 4326 CA THR B 229 11069 11242 10839 -374 -229 -968 C ATOM 4327 C THR B 229 -10.422 14.580 16.980 1.00 97.18 C ANISOU 4327 C THR B 229 12330 12587 12008 -325 -259 -933 C ATOM 4328 O THR B 229 -11.166 15.563 16.973 1.00 95.86 O ANISOU 4328 O THR B 229 12143 12474 11806 -308 -292 -903 O ATOM 4329 CB THR B 229 -12.167 13.364 18.278 1.00 84.23 C ANISOU 4329 CB THR B 229 10646 10882 10477 -406 -255 -1009 C ATOM 4330 N GLN B 244 -15.456 26.853 10.389 1.00 69.73 N ANISOU 4330 N GLN B 244 8695 9990 7808 220 -523 -439 N ATOM 4331 CA GLN B 244 -14.245 26.261 10.950 1.00 73.65 C ANISOU 4331 CA GLN B 244 9232 10385 8367 179 -484 -445 C ATOM 4332 C GLN B 244 -13.500 27.275 11.809 1.00 69.00 C ANISOU 4332 C GLN B 244 8673 9708 7835 189 -444 -347 C ATOM 4333 O GLN B 244 -13.313 27.064 13.004 1.00 68.22 O ANISOU 4333 O GLN B 244 8585 9517 7818 142 -431 -348 O ATOM 4334 CB GLN B 244 -13.329 25.741 9.841 1.00 76.52 C ANISOU 4334 CB GLN B 244 9617 10784 8672 200 -469 -470 C ATOM 4335 N LYS B 245 -13.066 28.371 11.180 1.00 69.30 N ANISOU 4335 N LYS B 245 8725 9776 7829 252 -422 -265 N ATOM 4336 CA LYS B 245 -12.438 29.453 11.931 1.00 70.57 C ANISOU 4336 CA LYS B 245 8909 9859 8044 264 -384 -174 C ATOM 4337 C LYS B 245 -13.423 30.070 12.914 1.00 62.05 C ANISOU 4337 C LYS B 245 7809 8757 7012 252 -400 -153 C ATOM 4338 O LYS B 245 -13.054 30.409 14.046 1.00 54.09 O ANISOU 4338 O LYS B 245 6815 7656 6079 224 -377 -122 O ATOM 4339 CB LYS B 245 -11.899 30.514 10.972 1.00 73.00 C ANISOU 4339 CB LYS B 245 9231 10209 8296 337 -354 -91 C ATOM 4340 CG LYS B 245 -11.113 31.626 11.644 1.00 77.38 C ANISOU 4340 CG LYS B 245 9810 10678 8912 348 -307 -1 C ATOM 4341 CD LYS B 245 -10.545 32.593 10.617 1.00 81.83 C ANISOU 4341 CD LYS B 245 10388 11281 9423 420 -271 80 C ATOM 4342 N ALA B 246 -14.681 30.229 12.490 1.00 61.48 N ANISOU 4342 N ALA B 246 7699 8769 6892 275 -438 -169 N ATOM 4343 CA ALA B 246 -15.713 30.724 13.392 1.00 53.95 C ANISOU 4343 CA ALA B 246 6719 7798 5980 263 -455 -156 C ATOM 4344 C ALA B 246 -15.940 29.760 14.546 1.00 47.54 C ANISOU 4344 C ALA B 246 5904 6916 5242 187 -465 -221 C ATOM 4345 O ALA B 246 -16.112 30.185 15.694 1.00 48.19 O ANISOU 4345 O ALA B 246 5989 6930 5391 165 -454 -194 O ATOM 4346 CB ALA B 246 -17.014 30.956 12.627 1.00 63.13 C ANISOU 4346 CB ALA B 246 7838 9075 7073 303 -497 -169 C ATOM 4347 N GLU B 247 -15.959 28.457 14.264 1.00 46.24 N ANISOU 4347 N GLU B 247 5733 6768 5070 149 -483 -308 N ATOM 4348 CA GLU B 247 -16.171 27.501 15.341 1.00 49.40 C ANISOU 4348 CA GLU B 247 6129 7098 5542 80 -486 -366 C ATOM 4349 C GLU B 247 -14.966 27.435 16.266 1.00 42.07 C ANISOU 4349 C GLU B 247 5243 6061 4681 52 -445 -336 C ATOM 4350 O GLU B 247 -15.125 27.230 17.473 1.00 37.19 O ANISOU 4350 O GLU B 247 4626 5373 4131 12 -439 -341 O ATOM 4351 CB GLU B 247 -16.498 26.113 14.782 1.00 46.28 C ANISOU 4351 CB GLU B 247 5715 6743 5128 44 -510 -469 C ATOM 4352 CG GLU B 247 -17.852 26.009 14.057 1.00 48.58 C ANISOU 4352 CG GLU B 247 5954 7140 5364 58 -558 -519 C ATOM 4353 CD GLU B 247 -19.073 26.187 14.965 1.00 53.77 C ANISOU 4353 CD GLU B 247 6576 7788 6068 34 -577 -525 C ATOM 4354 OE1 GLU B 247 -18.925 26.501 16.169 1.00 49.87 O ANISOU 4354 OE1 GLU B 247 6099 7207 5644 11 -554 -485 O ATOM 4355 OE2 GLU B 247 -20.203 26.019 14.460 1.00 59.51 O ANISOU 4355 OE2 GLU B 247 7254 8598 6758 39 -617 -573 O ATOM 4356 N LYS B 248 -13.760 27.611 15.724 1.00 38.85 N ANISOU 4356 N LYS B 248 4866 5641 4253 76 -417 -303 N ATOM 4357 CA LYS B 248 -12.563 27.605 16.563 1.00 42.18 C ANISOU 4357 CA LYS B 248 5323 5966 4736 54 -380 -273 C ATOM 4358 C LYS B 248 -12.586 28.748 17.580 1.00 32.40 C ANISOU 4358 C LYS B 248 4090 4674 3546 61 -365 -204 C ATOM 4359 O LYS B 248 -12.159 28.575 18.731 1.00 35.10 O ANISOU 4359 O LYS B 248 4446 4936 3953 25 -349 -202 O ATOM 4360 CB LYS B 248 -11.320 27.681 15.672 1.00 48.82 C ANISOU 4360 CB LYS B 248 6192 6814 5543 84 -352 -248 C ATOM 4361 CG LYS B 248 -10.002 27.573 16.396 1.00 51.68 C ANISOU 4361 CG LYS B 248 6586 7086 5964 62 -315 -224 C ATOM 4362 CD LYS B 248 -8.832 27.596 15.406 1.00 55.40 C ANISOU 4362 CD LYS B 248 7080 7571 6399 93 -288 -204 C ATOM 4363 CE LYS B 248 -8.768 28.913 14.635 1.00 58.49 C ANISOU 4363 CE LYS B 248 7471 8007 6744 154 -273 -129 C ATOM 4364 NZ LYS B 248 -7.540 29.007 13.785 1.00 67.01 N ANISOU 4364 NZ LYS B 248 8575 9090 7798 184 -238 -100 N ATOM 4365 N GLU B 249 -13.067 29.928 17.171 1.00 35.21 N ANISOU 4365 N GLU B 249 4435 5074 3870 109 -367 -149 N ATOM 4366 CA GLU B 249 -13.159 31.065 18.088 1.00 34.73 C ANISOU 4366 CA GLU B 249 4377 4964 3856 117 -350 -87 C ATOM 4367 C GLU B 249 -14.074 30.747 19.269 1.00 32.60 C ANISOU 4367 C GLU B 249 4090 4662 3636 74 -369 -120 C ATOM 4368 O GLU B 249 -13.757 31.076 20.418 1.00 32.50 O ANISOU 4368 O GLU B 249 4091 4577 3683 53 -351 -98 O ATOM 4369 CB GLU B 249 -13.663 32.309 17.336 1.00 38.17 C ANISOU 4369 CB GLU B 249 4800 5457 4246 179 -348 -25 C ATOM 4370 CG GLU B 249 -13.779 33.578 18.206 1.00 39.74 C ANISOU 4370 CG GLU B 249 5001 5603 4494 192 -326 40 C ATOM 4371 CD GLU B 249 -14.419 34.782 17.490 1.00 47.22 C ANISOU 4371 CD GLU B 249 5933 6607 5401 257 -322 103 C ATOM 4372 OE1 GLU B 249 -15.466 34.616 16.820 1.00 46.45 O ANISOU 4372 OE1 GLU B 249 5805 6594 5248 280 -356 84 O ATOM 4373 OE2 GLU B 249 -13.878 35.904 17.616 1.00 40.14 O ANISOU 4373 OE2 GLU B 249 5051 5669 4530 285 -284 173 O ATOM 4374 N VAL B 250 -15.211 30.101 19.002 1.00 33.37 N ANISOU 4374 N VAL B 250 4156 4815 3708 63 -404 -174 N ATOM 4375 CA VAL B 250 -16.134 29.730 20.071 1.00 35.55 C ANISOU 4375 CA VAL B 250 4412 5063 4030 22 -419 -206 C ATOM 4376 C VAL B 250 -15.513 28.678 20.985 1.00 29.44 C ANISOU 4376 C VAL B 250 3659 4215 3313 -32 -405 -245 C ATOM 4377 O VAL B 250 -15.603 28.770 22.213 1.00 29.47 O ANISOU 4377 O VAL B 250 3667 4158 3371 -58 -395 -235 O ATOM 4378 CB VAL B 250 -17.471 29.238 19.487 1.00 34.96 C ANISOU 4378 CB VAL B 250 4294 5070 3919 21 -459 -259 C ATOM 4379 CG1 VAL B 250 -18.362 28.723 20.615 1.00 35.19 C ANISOU 4379 CG1 VAL B 250 4304 5064 4004 -26 -468 -296 C ATOM 4380 CG2 VAL B 250 -18.178 30.362 18.728 1.00 35.96 C ANISOU 4380 CG2 VAL B 250 4398 5273 3993 81 -473 -213 C ATOM 4381 N THR B 251 -14.892 27.648 20.403 1.00 29.89 N ANISOU 4381 N THR B 251 3726 4276 3355 -48 -403 -290 N ATOM 4382 CA THR B 251 -14.262 26.616 21.229 1.00 28.67 C ANISOU 4382 CA THR B 251 3591 4049 3253 -95 -386 -322 C ATOM 4383 C THR B 251 -13.189 27.208 22.145 1.00 31.35 C ANISOU 4383 C THR B 251 3961 4314 3635 -94 -356 -267 C ATOM 4384 O THR B 251 -13.093 26.846 23.327 1.00 30.00 O ANISOU 4384 O THR B 251 3799 4083 3517 -126 -346 -272 O ATOM 4385 CB THR B 251 -13.660 25.530 20.330 1.00 30.75 C ANISOU 4385 CB THR B 251 3863 4330 3491 -104 -384 -373 C ATOM 4386 OG1 THR B 251 -14.688 24.998 19.482 1.00 29.89 O ANISOU 4386 OG1 THR B 251 3721 4294 3342 -107 -414 -432 O ATOM 4387 CG2 THR B 251 -13.077 24.410 21.173 1.00 33.05 C ANISOU 4387 CG2 THR B 251 4172 4545 3839 -150 -364 -405 C ATOM 4388 N ARG B 252 -12.387 28.139 21.627 1.00 28.37 N ANISOU 4388 N ARG B 252 3600 3943 3236 -56 -340 -214 N ATOM 4389 CA ARG B 252 -11.362 28.770 22.461 1.00 26.08 C ANISOU 4389 CA ARG B 252 3334 3586 2989 -56 -313 -167 C ATOM 4390 C ARG B 252 -11.976 29.552 23.622 1.00 27.16 C ANISOU 4390 C ARG B 252 3463 3691 3164 -62 -314 -140 C ATOM 4391 O ARG B 252 -11.455 29.525 24.744 1.00 26.75 O ANISOU 4391 O ARG B 252 3425 3579 3160 -84 -300 -133 O ATOM 4392 CB ARG B 252 -10.493 29.694 21.607 1.00 29.65 C ANISOU 4392 CB ARG B 252 3799 4052 3414 -14 -292 -115 C ATOM 4393 CG ARG B 252 -9.578 28.926 20.675 1.00 28.59 C ANISOU 4393 CG ARG B 252 3680 3932 3251 -11 -282 -136 C ATOM 4394 CD ARG B 252 -9.005 29.836 19.620 1.00 31.30 C ANISOU 4394 CD ARG B 252 4030 4307 3555 38 -263 -86 C ATOM 4395 NE ARG B 252 -7.876 29.192 18.967 1.00 38.21 N ANISOU 4395 NE ARG B 252 4923 5178 4416 39 -244 -98 N ATOM 4396 CZ ARG B 252 -7.082 29.799 18.100 1.00 43.50 C ANISOU 4396 CZ ARG B 252 5605 5863 5059 76 -219 -56 C ATOM 4397 NH1 ARG B 252 -7.272 31.062 17.758 1.00 40.15 N ANISOU 4397 NH1 ARG B 252 5177 5458 4621 116 -207 5 N ATOM 4398 NH2 ARG B 252 -6.073 29.120 17.563 1.00 55.15 N ANISOU 4398 NH2 ARG B 252 7096 7333 6525 75 -201 -71 N ATOM 4399 N MET B 253 -13.061 30.283 23.366 1.00 26.02 N ANISOU 4399 N MET B 253 3296 3591 2999 -40 -329 -125 N ATOM 4400 CA MET B 253 -13.699 31.036 24.439 1.00 25.65 C ANISOU 4400 CA MET B 253 3241 3515 2988 -43 -328 -102 C ATOM 4401 C MET B 253 -14.221 30.117 25.533 1.00 26.00 C ANISOU 4401 C MET B 253 3281 3529 3070 -88 -336 -144 C ATOM 4402 O MET B 253 -14.106 30.428 26.721 1.00 24.94 O ANISOU 4402 O MET B 253 3155 3344 2978 -102 -325 -130 O ATOM 4403 CB MET B 253 -14.839 31.884 23.884 1.00 25.71 C ANISOU 4403 CB MET B 253 3224 3582 2965 -8 -343 -79 C ATOM 4404 CG MET B 253 -15.550 32.677 24.990 1.00 26.71 C ANISOU 4404 CG MET B 253 3341 3678 3130 -11 -339 -57 C ATOM 4405 SD MET B 253 -16.619 33.922 24.289 1.00 31.24 S ANISOU 4405 SD MET B 253 3888 4312 3671 42 -347 -12 S ATOM 4406 CE MET B 253 -17.697 34.220 25.711 1.00 31.91 C ANISOU 4406 CE MET B 253 3956 4364 3804 21 -350 -18 C ATOM 4407 N VAL B 254 -14.805 28.979 25.154 1.00 26.09 N ANISOU 4407 N VAL B 254 3277 3569 3068 -110 -354 -198 N ATOM 4408 CA VAL B 254 -15.366 28.080 26.158 1.00 27.12 C ANISOU 4408 CA VAL B 254 3399 3667 3237 -151 -356 -236 C ATOM 4409 C VAL B 254 -14.264 27.512 27.055 1.00 27.99 C ANISOU 4409 C VAL B 254 3539 3708 3386 -174 -333 -234 C ATOM 4410 O VAL B 254 -14.448 27.356 28.270 1.00 27.17 O ANISOU 4410 O VAL B 254 3439 3562 3321 -194 -324 -233 O ATOM 4411 CB VAL B 254 -16.193 26.986 25.457 1.00 29.39 C ANISOU 4411 CB VAL B 254 3661 3998 3506 -170 -376 -298 C ATOM 4412 CG1 VAL B 254 -16.656 25.910 26.444 1.00 31.81 C ANISOU 4412 CG1 VAL B 254 3962 4263 3861 -216 -369 -338 C ATOM 4413 CG2 VAL B 254 -17.403 27.636 24.765 1.00 28.12 C ANISOU 4413 CG2 VAL B 254 3465 3911 3309 -145 -403 -297 C ATOM 4414 N ILE B 255 -13.098 27.209 26.477 1.00 26.64 N ANISOU 4414 N ILE B 255 3389 3529 3203 -168 -322 -233 N ATOM 4415 CA ILE B 255 -11.953 26.753 27.270 1.00 29.74 C ANISOU 4415 CA ILE B 255 3808 3862 3630 -184 -300 -226 C ATOM 4416 C ILE B 255 -11.605 27.777 28.335 1.00 26.45 C ANISOU 4416 C ILE B 255 3400 3409 3240 -176 -290 -183 C ATOM 4417 O ILE B 255 -11.362 27.433 29.502 1.00 26.95 O ANISOU 4417 O ILE B 255 3474 3429 3338 -194 -281 -184 O ATOM 4418 CB ILE B 255 -10.735 26.486 26.359 1.00 29.20 C ANISOU 4418 CB ILE B 255 3757 3796 3542 -172 -289 -225 C ATOM 4419 CG1 ILE B 255 -10.960 25.253 25.499 1.00 32.06 C ANISOU 4419 CG1 ILE B 255 4112 4183 3885 -186 -295 -279 C ATOM 4420 CG2 ILE B 255 -9.448 26.369 27.198 1.00 30.88 C ANISOU 4420 CG2 ILE B 255 3993 3951 3789 -178 -268 -205 C ATOM 4421 CD1 ILE B 255 -9.913 25.105 24.398 1.00 40.77 C ANISOU 4421 CD1 ILE B 255 5230 5302 4958 -168 -285 -278 C ATOM 4422 N ILE B 256 -11.539 29.053 27.947 1.00 24.41 N ANISOU 4422 N ILE B 256 3139 3167 2967 -146 -290 -145 N ATOM 4423 CA ILE B 256 -11.185 30.081 28.921 1.00 24.74 C ANISOU 4423 CA ILE B 256 3189 3172 3038 -140 -278 -110 C ATOM 4424 C ILE B 256 -12.309 30.290 29.941 1.00 24.29 C ANISOU 4424 C ILE B 256 3119 3109 3000 -151 -285 -114 C ATOM 4425 O ILE B 256 -12.039 30.586 31.111 1.00 24.70 O ANISOU 4425 O ILE B 256 3180 3124 3083 -159 -277 -104 O ATOM 4426 CB ILE B 256 -10.817 31.394 28.196 1.00 27.89 C ANISOU 4426 CB ILE B 256 3589 3585 3425 -106 -268 -67 C ATOM 4427 CG1 ILE B 256 -9.578 31.188 27.310 1.00 28.58 C ANISOU 4427 CG1 ILE B 256 3689 3671 3498 -95 -254 -59 C ATOM 4428 CG2 ILE B 256 -10.536 32.493 29.205 1.00 26.15 C ANISOU 4428 CG2 ILE B 256 3372 3323 3240 -102 -254 -38 C ATOM 4429 CD1 ILE B 256 -8.308 30.877 28.139 1.00 28.44 C ANISOU 4429 CD1 ILE B 256 3688 3602 3515 -113 -240 -61 C ATOM 4430 N MET B 257 -13.577 30.160 29.532 1.00 24.18 N ANISOU 4430 N MET B 257 3083 3135 2969 -150 -302 -130 N ATOM 4431 CA MET B 257 -14.650 30.250 30.523 1.00 24.83 C ANISOU 4431 CA MET B 257 3152 3210 3073 -162 -306 -136 C ATOM 4432 C MET B 257 -14.523 29.161 31.583 1.00 24.84 C ANISOU 4432 C MET B 257 3163 3173 3103 -194 -298 -161 C ATOM 4433 O MET B 257 -14.782 29.410 32.764 1.00 22.22 O ANISOU 4433 O MET B 257 2833 2814 2795 -201 -291 -152 O ATOM 4434 CB MET B 257 -16.027 30.173 29.856 1.00 24.84 C ANISOU 4434 CB MET B 257 3122 3264 3052 -157 -325 -153 C ATOM 4435 CG MET B 257 -16.341 31.342 28.953 1.00 25.96 C ANISOU 4435 CG MET B 257 3251 3447 3164 -118 -331 -120 C ATOM 4436 SD MET B 257 -17.893 31.076 28.050 1.00 28.64 S ANISOU 4436 SD MET B 257 3549 3862 3470 -109 -360 -147 S ATOM 4437 CE MET B 257 -19.098 31.180 29.361 1.00 27.67 C ANISOU 4437 CE MET B 257 3407 3719 3386 -128 -360 -153 C ATOM 4438 N VAL B 258 -14.143 27.943 31.187 1.00 23.02 N ANISOU 4438 N VAL B 258 2937 2939 2869 -212 -297 -191 N ATOM 4439 CA VAL B 258 -14.005 26.871 32.176 1.00 24.37 C ANISOU 4439 CA VAL B 258 3118 3071 3070 -239 -284 -208 C ATOM 4440 C VAL B 258 -12.816 27.131 33.099 1.00 25.83 C ANISOU 4440 C VAL B 258 3328 3216 3272 -234 -270 -183 C ATOM 4441 O VAL B 258 -12.909 26.968 34.323 1.00 24.66 O ANISOU 4441 O VAL B 258 3185 3040 3144 -242 -260 -177 O ATOM 4442 CB VAL B 258 -13.899 25.504 31.472 1.00 24.89 C ANISOU 4442 CB VAL B 258 3182 3140 3134 -258 -282 -248 C ATOM 4443 CG1 VAL B 258 -13.688 24.412 32.502 1.00 29.31 C ANISOU 4443 CG1 VAL B 258 3754 3653 3728 -281 -261 -258 C ATOM 4444 CG2 VAL B 258 -15.163 25.236 30.626 1.00 24.95 C ANISOU 4444 CG2 VAL B 258 3159 3193 3126 -266 -299 -283 C ATOM 4445 N ILE B 259 -11.683 27.562 32.539 1.00 23.97 N ANISOU 4445 N ILE B 259 3105 2979 3025 -218 -268 -166 N ATOM 4446 CA ILE B 259 -10.533 27.873 33.385 1.00 23.00 C ANISOU 4446 CA ILE B 259 2999 2822 2919 -214 -257 -146 C ATOM 4447 C ILE B 259 -10.880 28.981 34.371 1.00 23.39 C ANISOU 4447 C ILE B 259 3046 2863 2980 -206 -257 -127 C ATOM 4448 O ILE B 259 -10.506 28.923 35.548 1.00 24.04 O ANISOU 4448 O ILE B 259 3136 2921 3079 -210 -252 -123 O ATOM 4449 CB ILE B 259 -9.325 28.267 32.518 1.00 24.96 C ANISOU 4449 CB ILE B 259 3256 3072 3157 -199 -253 -132 C ATOM 4450 CG1 ILE B 259 -8.804 27.047 31.753 1.00 28.48 C ANISOU 4450 CG1 ILE B 259 3709 3519 3594 -207 -248 -154 C ATOM 4451 CG2 ILE B 259 -8.242 28.921 33.383 1.00 24.74 C ANISOU 4451 CG2 ILE B 259 3237 3015 3149 -193 -245 -112 C ATOM 4452 CD1 ILE B 259 -7.674 27.399 30.816 1.00 29.30 C ANISOU 4452 CD1 ILE B 259 3820 3628 3686 -190 -241 -140 C ATOM 4453 N ALA B 260 -11.559 30.028 33.900 1.00 23.22 N ANISOU 4453 N ALA B 260 3011 2862 2949 -192 -263 -114 N ATOM 4454 CA ALA B 260 -11.858 31.153 34.779 1.00 22.63 C ANISOU 4454 CA ALA B 260 2933 2776 2889 -184 -260 -97 C ATOM 4455 C ALA B 260 -12.798 30.728 35.896 1.00 23.69 C ANISOU 4455 C ALA B 260 3063 2903 3034 -197 -260 -110 C ATOM 4456 O ALA B 260 -12.693 31.223 37.023 1.00 22.11 O ANISOU 4456 O ALA B 260 2868 2684 2847 -196 -254 -104 O ATOM 4457 CB ALA B 260 -12.463 32.309 33.974 1.00 25.48 C ANISOU 4457 CB ALA B 260 3281 3160 3241 -162 -262 -77 C ATOM 4458 N PHE B 261 -13.757 29.849 35.581 1.00 22.12 N ANISOU 4458 N PHE B 261 2853 2723 2830 -209 -265 -128 N ATOM 4459 CA PHE B 261 -14.676 29.352 36.601 1.00 22.25 C ANISOU 4459 CA PHE B 261 2864 2731 2860 -223 -260 -138 C ATOM 4460 C PHE B 261 -13.921 28.609 37.695 1.00 22.71 C ANISOU 4460 C PHE B 261 2940 2757 2930 -232 -247 -139 C ATOM 4461 O PHE B 261 -14.175 28.807 38.891 1.00 21.30 O ANISOU 4461 O PHE B 261 2766 2567 2760 -231 -239 -133 O ATOM 4462 CB PHE B 261 -15.730 28.435 35.960 1.00 22.30 C ANISOU 4462 CB PHE B 261 2850 2759 2864 -239 -265 -164 C ATOM 4463 CG PHE B 261 -16.728 27.878 36.965 1.00 24.00 C ANISOU 4463 CG PHE B 261 3057 2964 3100 -254 -254 -173 C ATOM 4464 CD1 PHE B 261 -16.433 26.740 37.684 1.00 24.17 C ANISOU 4464 CD1 PHE B 261 3090 2956 3137 -271 -236 -181 C ATOM 4465 CD2 PHE B 261 -17.924 28.545 37.216 1.00 23.68 C ANISOU 4465 CD2 PHE B 261 2995 2941 3063 -250 -257 -169 C ATOM 4466 CE1 PHE B 261 -17.321 26.247 38.653 1.00 26.18 C ANISOU 4466 CE1 PHE B 261 3338 3198 3412 -283 -219 -184 C ATOM 4467 CE2 PHE B 261 -18.839 28.047 38.146 1.00 28.18 C ANISOU 4467 CE2 PHE B 261 3555 3500 3652 -263 -242 -176 C ATOM 4468 CZ PHE B 261 -18.515 26.901 38.891 1.00 26.17 C ANISOU 4468 CZ PHE B 261 3315 3214 3414 -280 -222 -182 C ATOM 4469 N LEU B 262 -12.976 27.751 37.307 1.00 22.16 N ANISOU 4469 N LEU B 262 2884 2678 2859 -238 -244 -145 N ATOM 4470 CA LEU B 262 -12.194 27.021 38.301 1.00 20.91 C ANISOU 4470 CA LEU B 262 2742 2492 2710 -240 -231 -141 C ATOM 4471 C LEU B 262 -11.365 27.965 39.162 1.00 19.86 C ANISOU 4471 C LEU B 262 2618 2351 2575 -225 -233 -125 C ATOM 4472 O LEU B 262 -11.273 27.780 40.381 1.00 23.62 O ANISOU 4472 O LEU B 262 3102 2818 3055 -222 -226 -119 O ATOM 4473 CB LEU B 262 -11.303 25.985 37.605 1.00 23.13 C ANISOU 4473 CB LEU B 262 3032 2764 2992 -246 -226 -150 C ATOM 4474 CG LEU B 262 -12.112 24.887 36.901 1.00 27.16 C ANISOU 4474 CG LEU B 262 3533 3278 3509 -265 -220 -176 C ATOM 4475 CD1 LEU B 262 -11.215 23.956 36.062 1.00 31.13 C ANISOU 4475 CD1 LEU B 262 4046 3772 4012 -269 -214 -189 C ATOM 4476 CD2 LEU B 262 -12.908 24.082 37.919 1.00 30.06 C ANISOU 4476 CD2 LEU B 262 3898 3626 3896 -277 -202 -178 C ATOM 4477 N ILE B 263 -10.731 28.980 38.560 1.00 22.01 N ANISOU 4477 N ILE B 263 2888 2629 2844 -215 -242 -118 N ATOM 4478 CA ILE B 263 -9.964 29.923 39.384 1.00 20.86 C ANISOU 4478 CA ILE B 263 2748 2475 2704 -205 -243 -110 C ATOM 4479 C ILE B 263 -10.876 30.602 40.407 1.00 25.33 C ANISOU 4479 C ILE B 263 3310 3043 3273 -202 -241 -110 C ATOM 4480 O ILE B 263 -10.505 30.794 41.572 1.00 22.56 O ANISOU 4480 O ILE B 263 2964 2686 2922 -197 -240 -112 O ATOM 4481 CB ILE B 263 -9.267 30.969 38.491 1.00 24.67 C ANISOU 4481 CB ILE B 263 3226 2958 3190 -196 -246 -102 C ATOM 4482 CG1 ILE B 263 -8.104 30.342 37.723 1.00 25.50 C ANISOU 4482 CG1 ILE B 263 3337 3059 3293 -197 -244 -101 C ATOM 4483 CG2 ILE B 263 -8.751 32.148 39.365 1.00 20.94 C ANISOU 4483 CG2 ILE B 263 2752 2474 2731 -190 -245 -101 C ATOM 4484 CD1 ILE B 263 -7.624 31.197 36.560 1.00 29.06 C ANISOU 4484 CD1 ILE B 263 3783 3514 3745 -187 -242 -90 C ATOM 4485 N CYS B 264 -12.074 30.995 39.974 1.00 22.40 N ANISOU 4485 N CYS B 264 2926 2683 2902 -202 -242 -109 N ATOM 4486 CA CYS B 264 -12.997 31.758 40.830 1.00 18.98 C ANISOU 4486 CA CYS B 264 2487 2252 2474 -197 -238 -109 C ATOM 4487 C CYS B 264 -13.549 30.913 41.980 1.00 21.59 C ANISOU 4487 C CYS B 264 2822 2579 2801 -203 -229 -113 C ATOM 4488 O CYS B 264 -13.705 31.403 43.108 1.00 24.41 O ANISOU 4488 O CYS B 264 3182 2934 3158 -196 -224 -114 O ATOM 4489 CB CYS B 264 -14.143 32.266 39.954 1.00 21.99 C ANISOU 4489 CB CYS B 264 2851 2650 2856 -194 -240 -104 C ATOM 4490 SG CYS B 264 -15.424 33.237 40.787 1.00 24.87 S ANISOU 4490 SG CYS B 264 3204 3018 3229 -185 -233 -101 S ATOM 4491 N TRP B 265 -13.890 29.650 41.711 1.00 19.07 N ANISOU 4491 N TRP B 265 2503 2261 2483 -215 -223 -116 N ATOM 4492 CA TRP B 265 -14.676 28.870 42.662 1.00 21.17 C ANISOU 4492 CA TRP B 265 2769 2522 2752 -221 -208 -116 C ATOM 4493 C TRP B 265 -13.919 27.755 43.369 1.00 25.05 C ANISOU 4493 C TRP B 265 3277 2998 3241 -220 -196 -111 C ATOM 4494 O TRP B 265 -14.369 27.320 44.434 1.00 24.24 O ANISOU 4494 O TRP B 265 3180 2892 3140 -216 -179 -103 O ATOM 4495 CB TRP B 265 -15.903 28.260 41.963 1.00 19.55 C ANISOU 4495 CB TRP B 265 2545 2324 2558 -236 -204 -126 C ATOM 4496 CG TRP B 265 -16.955 29.288 41.651 1.00 20.19 C ANISOU 4496 CG TRP B 265 2607 2424 2641 -231 -211 -127 C ATOM 4497 CD1 TRP B 265 -17.241 29.834 40.430 1.00 20.24 C ANISOU 4497 CD1 TRP B 265 2598 2450 2643 -229 -227 -130 C ATOM 4498 CD2 TRP B 265 -17.853 29.906 42.591 1.00 19.46 C ANISOU 4498 CD2 TRP B 265 2508 2334 2553 -224 -202 -121 C ATOM 4499 NE1 TRP B 265 -18.256 30.758 40.553 1.00 20.91 N ANISOU 4499 NE1 TRP B 265 2666 2549 2731 -219 -228 -124 N ATOM 4500 CE2 TRP B 265 -18.644 30.823 41.870 1.00 21.70 C ANISOU 4500 CE2 TRP B 265 2770 2636 2837 -217 -212 -121 C ATOM 4501 CE3 TRP B 265 -18.041 29.789 43.976 1.00 21.49 C ANISOU 4501 CE3 TRP B 265 2774 2580 2809 -219 -184 -115 C ATOM 4502 CZ2 TRP B 265 -19.625 31.604 42.483 1.00 22.79 C ANISOU 4502 CZ2 TRP B 265 2898 2780 2983 -208 -204 -116 C ATOM 4503 CZ3 TRP B 265 -19.029 30.580 44.594 1.00 20.61 C ANISOU 4503 CZ3 TRP B 265 2652 2476 2702 -211 -176 -113 C ATOM 4504 CH2 TRP B 265 -19.799 31.461 43.841 1.00 19.66 C ANISOU 4504 CH2 TRP B 265 2511 2371 2588 -206 -186 -114 C ATOM 4505 N LEU B 266 -12.824 27.231 42.796 1.00 23.76 N ANISOU 4505 N LEU B 266 3123 2828 3077 -221 -200 -111 N ATOM 4506 CA LEU B 266 -12.119 26.147 43.483 1.00 22.78 C ANISOU 4506 CA LEU B 266 3014 2691 2952 -216 -186 -101 C ATOM 4507 C LEU B 266 -11.621 26.530 44.872 1.00 21.83 C ANISOU 4507 C LEU B 266 2903 2576 2815 -196 -185 -89 C ATOM 4508 O LEU B 266 -11.708 25.680 45.772 1.00 22.26 O ANISOU 4508 O LEU B 266 2967 2625 2867 -187 -166 -75 O ATOM 4509 CB LEU B 266 -10.950 25.608 42.634 1.00 24.18 C ANISOU 4509 CB LEU B 266 3197 2860 3131 -217 -191 -103 C ATOM 4510 CG LEU B 266 -11.332 24.609 41.542 1.00 33.47 C ANISOU 4510 CG LEU B 266 4369 4026 4322 -235 -182 -116 C ATOM 4511 CD1 LEU B 266 -10.093 24.087 40.816 1.00 32.33 C ANISOU 4511 CD1 LEU B 266 4233 3874 4178 -232 -184 -117 C ATOM 4512 CD2 LEU B 266 -12.143 23.423 42.089 1.00 32.84 C ANISOU 4512 CD2 LEU B 266 4290 3928 4260 -245 -155 -114 C ATOM 4513 N PRO B 267 -11.069 27.735 45.119 1.00 21.38 N ANISOU 4513 N PRO B 267 2844 2532 2748 -186 -203 -96 N ATOM 4514 CA PRO B 267 -10.655 28.048 46.486 1.00 20.48 C ANISOU 4514 CA PRO B 267 2737 2430 2615 -167 -204 -92 C ATOM 4515 C PRO B 267 -11.815 27.984 47.466 1.00 27.91 C ANISOU 4515 C PRO B 267 3680 3376 3550 -162 -187 -86 C ATOM 4516 O PRO B 267 -11.676 27.400 48.544 1.00 23.12 O ANISOU 4516 O PRO B 267 3084 2776 2926 -146 -175 -73 O ATOM 4517 CB PRO B 267 -10.072 29.463 46.368 1.00 27.88 C ANISOU 4517 CB PRO B 267 3666 3375 3553 -165 -224 -109 C ATOM 4518 CG PRO B 267 -9.645 29.575 44.901 1.00 27.69 C ANISOU 4518 CG PRO B 267 3635 3339 3545 -178 -231 -111 C ATOM 4519 CD PRO B 267 -10.699 28.811 44.172 1.00 23.30 C ANISOU 4519 CD PRO B 267 3079 2778 2998 -190 -220 -106 C ATOM 4520 N TYR B 268 -12.970 28.551 47.105 1.00 24.56 N ANISOU 4520 N TYR B 268 3244 2950 3138 -173 -184 -93 N ATOM 4521 CA TYR B 268 -14.142 28.477 47.984 1.00 22.69 C ANISOU 4521 CA TYR B 268 3007 2717 2898 -169 -165 -87 C ATOM 4522 C TYR B 268 -14.581 27.029 48.215 1.00 25.72 C ANISOU 4522 C TYR B 268 3396 3088 3290 -173 -138 -69 C ATOM 4523 O TYR B 268 -14.842 26.622 49.353 1.00 21.70 O ANISOU 4523 O TYR B 268 2894 2582 2768 -158 -118 -54 O ATOM 4524 CB TYR B 268 -15.303 29.283 47.381 1.00 21.72 C ANISOU 4524 CB TYR B 268 2866 2595 2791 -181 -167 -97 C ATOM 4525 CG TYR B 268 -16.518 29.299 48.270 1.00 22.45 C ANISOU 4525 CG TYR B 268 2955 2692 2884 -176 -146 -91 C ATOM 4526 CD1 TYR B 268 -16.575 30.134 49.367 1.00 19.75 C ANISOU 4526 CD1 TYR B 268 2619 2362 2525 -159 -144 -95 C ATOM 4527 CD2 TYR B 268 -17.600 28.465 48.017 1.00 23.91 C ANISOU 4527 CD2 TYR B 268 3129 2869 3088 -190 -127 -85 C ATOM 4528 CE1 TYR B 268 -17.694 30.152 50.204 1.00 23.25 C ANISOU 4528 CE1 TYR B 268 3059 2810 2967 -153 -121 -89 C ATOM 4529 CE2 TYR B 268 -18.727 28.467 48.848 1.00 22.64 C ANISOU 4529 CE2 TYR B 268 2961 2711 2930 -186 -104 -79 C ATOM 4530 CZ TYR B 268 -18.753 29.312 49.946 1.00 26.44 C ANISOU 4530 CZ TYR B 268 3451 3204 3390 -166 -100 -78 C ATOM 4531 OH TYR B 268 -19.846 29.326 50.783 1.00 23.71 O ANISOU 4531 OH TYR B 268 3100 2862 3046 -160 -74 -71 O ATOM 4532 N ALA B 269 -14.714 26.250 47.135 1.00 21.39 N ANISOU 4532 N ALA B 269 2840 2524 2763 -192 -135 -72 N ATOM 4533 CA ALA B 269 -15.135 24.864 47.285 1.00 23.32 C ANISOU 4533 CA ALA B 269 3087 2748 3025 -200 -105 -60 C ATOM 4534 C ALA B 269 -14.145 24.082 48.137 1.00 22.56 C ANISOU 4534 C ALA B 269 3011 2647 2914 -178 -91 -37 C ATOM 4535 O ALA B 269 -14.544 23.258 48.960 1.00 25.11 O ANISOU 4535 O ALA B 269 3342 2960 3241 -169 -58 -15 O ATOM 4536 CB ALA B 269 -15.290 24.191 45.911 1.00 26.85 C ANISOU 4536 CB ALA B 269 3523 3180 3498 -226 -106 -76 C ATOM 4537 N GLY B 270 -12.842 24.324 47.952 1.00 24.69 N ANISOU 4537 N GLY B 270 3289 2925 3168 -167 -113 -38 N ATOM 4538 CA GLY B 270 -11.861 23.600 48.747 1.00 25.65 C ANISOU 4538 CA GLY B 270 3425 3047 3272 -141 -102 -15 C ATOM 4539 C GLY B 270 -11.953 23.921 50.228 1.00 23.22 C ANISOU 4539 C GLY B 270 3126 2763 2933 -113 -96 1 C ATOM 4540 O GLY B 270 -11.895 23.031 51.081 1.00 24.63 O ANISOU 4540 O GLY B 270 3316 2940 3102 -91 -68 30 O ATOM 4541 N VAL B 271 -12.066 25.204 50.557 1.00 20.64 N ANISOU 4541 N VAL B 271 2794 2461 2589 -110 -119 -19 N ATOM 4542 CA VAL B 271 -12.118 25.602 51.960 1.00 22.18 C ANISOU 4542 CA VAL B 271 2995 2684 2747 -82 -115 -12 C ATOM 4543 C VAL B 271 -13.411 25.114 52.604 1.00 25.69 C ANISOU 4543 C VAL B 271 3443 3121 3197 -80 -78 8 C ATOM 4544 O VAL B 271 -13.398 24.611 53.733 1.00 23.06 O ANISOU 4544 O VAL B 271 3121 2801 2838 -51 -56 34 O ATOM 4545 CB VAL B 271 -11.936 27.127 52.082 1.00 23.48 C ANISOU 4545 CB VAL B 271 3151 2871 2899 -83 -146 -44 C ATOM 4546 CG1 VAL B 271 -12.179 27.606 53.526 1.00 24.37 C ANISOU 4546 CG1 VAL B 271 3270 3015 2974 -57 -141 -46 C ATOM 4547 CG2 VAL B 271 -10.521 27.505 51.642 1.00 26.07 C ANISOU 4547 CG2 VAL B 271 3475 3207 3223 -82 -176 -60 C ATOM 4548 N ALA B 272 -14.533 25.201 51.877 1.00 25.63 N ANISOU 4548 N ALA B 272 3423 3093 3222 -108 -69 -2 N ATOM 4549 CA ALA B 272 -15.801 24.664 52.377 1.00 24.07 C ANISOU 4549 CA ALA B 272 3223 2883 3039 -110 -31 15 C ATOM 4550 C ALA B 272 -15.710 23.173 52.655 1.00 23.05 C ANISOU 4550 C ALA B 272 3105 2731 2923 -102 8 49 C ATOM 4551 O ALA B 272 -16.216 22.694 53.681 1.00 26.07 O ANISOU 4551 O ALA B 272 3495 3114 3296 -82 44 77 O ATOM 4552 CB ALA B 272 -16.931 24.930 51.378 1.00 23.41 C ANISOU 4552 CB ALA B 272 3118 2784 2994 -143 -31 -5 C ATOM 4553 N PHE B 273 -15.104 22.410 51.749 1.00 22.84 N ANISOU 4553 N PHE B 273 3078 2681 2920 -116 6 48 N ATOM 4554 CA PHE B 273 -15.040 20.975 51.989 1.00 25.55 C ANISOU 4554 CA PHE B 273 3432 2995 3283 -109 48 80 C ATOM 4555 C PHE B 273 -14.106 20.661 53.146 1.00 27.35 C ANISOU 4555 C PHE B 273 3680 3243 3470 -63 57 115 C ATOM 4556 O PHE B 273 -14.368 19.742 53.928 1.00 24.35 O ANISOU 4556 O PHE B 273 3310 2849 3092 -42 102 154 O ATOM 4557 CB PHE B 273 -14.603 20.232 50.721 1.00 26.89 C ANISOU 4557 CB PHE B 273 3596 3133 3488 -134 46 65 C ATOM 4558 CG PHE B 273 -14.673 18.730 50.854 1.00 28.02 C ANISOU 4558 CG PHE B 273 3746 3234 3664 -133 96 93 C ATOM 4559 CD1 PHE B 273 -15.876 18.063 50.695 1.00 35.02 C ANISOU 4559 CD1 PHE B 273 4622 4088 4598 -159 135 91 C ATOM 4560 CD2 PHE B 273 -13.529 17.994 51.155 1.00 35.86 C ANISOU 4560 CD2 PHE B 273 4757 4221 4647 -104 107 122 C ATOM 4561 CE1 PHE B 273 -15.935 16.681 50.836 1.00 39.29 C ANISOU 4561 CE1 PHE B 273 5168 4584 5177 -158 188 116 C ATOM 4562 CE2 PHE B 273 -13.583 16.608 51.297 1.00 35.11 C ANISOU 4562 CE2 PHE B 273 4671 4083 4587 -99 160 152 C ATOM 4563 CZ PHE B 273 -14.789 15.961 51.141 1.00 38.46 C ANISOU 4563 CZ PHE B 273 5084 4469 5061 -127 202 148 C ATOM 4564 N TYR B 274 -13.036 21.447 53.300 1.00 23.80 N ANISOU 4564 N TYR B 274 3233 2828 2982 -45 16 103 N ATOM 4565 CA TYR B 274 -12.151 21.258 54.442 1.00 26.35 C ANISOU 4565 CA TYR B 274 3570 3184 3258 1 17 132 C ATOM 4566 C TYR B 274 -12.892 21.492 55.753 1.00 24.34 C ANISOU 4566 C TYR B 274 3323 2955 2971 28 39 151 C ATOM 4567 O TYR B 274 -12.809 20.684 56.692 1.00 25.17 O ANISOU 4567 O TYR B 274 3441 3065 3055 64 74 195 O ATOM 4568 CB TYR B 274 -10.938 22.186 54.327 1.00 27.58 C ANISOU 4568 CB TYR B 274 3722 3375 3384 9 -35 105 C ATOM 4569 CG TYR B 274 -10.065 22.081 55.551 1.00 30.45 C ANISOU 4569 CG TYR B 274 4093 3782 3693 58 -39 128 C ATOM 4570 CD1 TYR B 274 -9.087 21.089 55.654 1.00 34.56 C ANISOU 4570 CD1 TYR B 274 4622 4302 4208 86 -29 160 C ATOM 4571 CD2 TYR B 274 -10.253 22.933 56.626 1.00 32.89 C ANISOU 4571 CD2 TYR B 274 4404 4137 3957 81 -52 117 C ATOM 4572 CE1 TYR B 274 -8.301 20.992 56.801 1.00 39.33 C ANISOU 4572 CE1 TYR B 274 5231 4955 4758 136 -36 184 C ATOM 4573 CE2 TYR B 274 -9.486 22.839 57.760 1.00 39.19 C ANISOU 4573 CE2 TYR B 274 5207 4984 4699 128 -59 135 C ATOM 4574 CZ TYR B 274 -8.514 21.875 57.845 1.00 37.52 C ANISOU 4574 CZ TYR B 274 5001 4777 4479 157 -52 169 C ATOM 4575 OH TYR B 274 -7.768 21.810 59.000 1.00 43.54 O ANISOU 4575 OH TYR B 274 5766 5597 5181 210 -62 188 O ATOM 4576 N ILE B 275 -13.653 22.578 55.829 1.00 23.24 N ANISOU 4576 N ILE B 275 3174 2830 2826 13 24 121 N ATOM 4577 CA ILE B 275 -14.408 22.870 57.053 1.00 21.96 C ANISOU 4577 CA ILE B 275 3018 2692 2632 38 46 136 C ATOM 4578 C ILE B 275 -15.405 21.756 57.357 1.00 23.30 C ANISOU 4578 C ILE B 275 3193 2829 2831 39 106 177 C ATOM 4579 O ILE B 275 -15.524 21.292 58.505 1.00 26.83 O ANISOU 4579 O ILE B 275 3654 3293 3247 78 141 216 O ATOM 4580 CB ILE B 275 -15.107 24.232 56.912 1.00 21.73 C ANISOU 4580 CB ILE B 275 2976 2676 2603 17 22 94 C ATOM 4581 CG1 ILE B 275 -14.030 25.328 56.855 1.00 22.24 C ANISOU 4581 CG1 ILE B 275 3037 2774 2639 22 -30 56 C ATOM 4582 CG2 ILE B 275 -16.126 24.417 58.081 1.00 22.80 C ANISOU 4582 CG2 ILE B 275 3118 2830 2716 38 54 109 C ATOM 4583 CD1 ILE B 275 -14.553 26.743 56.447 1.00 29.33 C ANISOU 4583 CD1 ILE B 275 3922 3674 3549 -3 -56 12 C ATOM 4584 N PHE B 276 -16.149 21.321 56.333 1.00 22.21 N ANISOU 4584 N PHE B 276 3042 2646 2753 -3 122 167 N ATOM 4585 CA PHE B 276 -17.159 20.275 56.502 1.00 24.55 C ANISOU 4585 CA PHE B 276 3336 2902 3089 -10 182 198 C ATOM 4586 C PHE B 276 -16.560 19.013 57.114 1.00 27.39 C ANISOU 4586 C PHE B 276 3716 3248 3444 24 224 251 C ATOM 4587 O PHE B 276 -17.211 18.325 57.914 1.00 26.95 O ANISOU 4587 O PHE B 276 3667 3179 3396 43 280 292 O ATOM 4588 CB PHE B 276 -17.787 19.963 55.133 1.00 22.59 C ANISOU 4588 CB PHE B 276 3066 2610 2906 -63 182 168 C ATOM 4589 CG PHE B 276 -18.825 18.851 55.154 1.00 24.62 C ANISOU 4589 CG PHE B 276 3315 2821 3217 -80 243 189 C ATOM 4590 CD1 PHE B 276 -19.967 18.960 55.920 1.00 26.67 C ANISOU 4590 CD1 PHE B 276 3569 3083 3483 -76 279 204 C ATOM 4591 CD2 PHE B 276 -18.664 17.723 54.362 1.00 30.45 C ANISOU 4591 CD2 PHE B 276 4049 3512 4006 -103 266 190 C ATOM 4592 CE1 PHE B 276 -20.929 17.951 55.925 1.00 31.54 C ANISOU 4592 CE1 PHE B 276 4174 3654 4157 -95 339 222 C ATOM 4593 CE2 PHE B 276 -19.642 16.719 54.342 1.00 32.25 C ANISOU 4593 CE2 PHE B 276 4266 3693 4294 -125 325 202 C ATOM 4594 CZ PHE B 276 -20.763 16.835 55.117 1.00 30.87 C ANISOU 4594 CZ PHE B 276 4083 3520 4126 -121 361 219 C ATOM 4595 N THR B 277 -15.333 18.683 56.731 1.00 27.91 N ANISOU 4595 N THR B 277 3789 3316 3502 35 202 253 N ATOM 4596 CA THR B 277 -14.673 17.479 57.208 1.00 31.49 C ANISOU 4596 CA THR B 277 4258 3753 3952 70 240 305 C ATOM 4597 C THR B 277 -13.822 17.732 58.449 1.00 34.26 C ANISOU 4597 C THR B 277 4626 4163 4229 131 229 336 C ATOM 4598 O THR B 277 -13.273 16.777 59.002 1.00 28.23 O ANISOU 4598 O THR B 277 3876 3396 3453 172 262 387 O ATOM 4599 CB THR B 277 -13.812 16.869 56.076 1.00 29.62 C ANISOU 4599 CB THR B 277 4019 3483 3751 50 227 292 C ATOM 4600 OG1 THR B 277 -12.923 17.845 55.526 1.00 29.30 O ANISOU 4600 OG1 THR B 277 3973 3478 3683 42 162 252 O ATOM 4601 CG2 THR B 277 -14.689 16.362 54.957 1.00 29.70 C ANISOU 4601 CG2 THR B 277 4014 3436 3834 -4 249 266 C ATOM 4602 N HIS B 278 -13.714 18.985 58.907 1.00 25.35 N ANISOU 4602 N HIS B 278 3493 3088 3048 140 184 305 N ATOM 4603 CA HIS B 278 -12.955 19.343 60.113 1.00 29.13 C ANISOU 4603 CA HIS B 278 3984 3634 3451 196 167 322 C ATOM 4604 C HIS B 278 -13.748 20.334 60.957 1.00 28.70 C ANISOU 4604 C HIS B 278 3929 3618 3358 204 162 304 C ATOM 4605 O HIS B 278 -13.253 21.398 61.325 1.00 28.70 O ANISOU 4605 O HIS B 278 3924 3669 3310 215 115 268 O ATOM 4606 CB HIS B 278 -11.580 19.929 59.785 1.00 30.60 C ANISOU 4606 CB HIS B 278 4163 3855 3608 201 105 290 C ATOM 4607 CG HIS B 278 -10.726 19.030 58.948 1.00 30.51 C ANISOU 4607 CG HIS B 278 4152 3810 3632 195 107 304 C ATOM 4608 ND1 HIS B 278 -10.874 18.922 57.580 1.00 29.58 N ANISOU 4608 ND1 HIS B 278 4023 3640 3575 143 101 275 N ATOM 4609 CD2 HIS B 278 -9.734 18.168 59.289 1.00 32.43 C ANISOU 4609 CD2 HIS B 278 4403 4063 3856 238 118 346 C ATOM 4610 CE1 HIS B 278 -10.011 18.034 57.114 1.00 30.97 C ANISOU 4610 CE1 HIS B 278 4203 3794 3770 152 109 296 C ATOM 4611 NE2 HIS B 278 -9.304 17.567 58.128 1.00 35.63 N ANISOU 4611 NE2 HIS B 278 4804 4419 4314 209 120 340 N ATOM 4612 N GLN B 279 -15.005 20.005 61.245 1.00 24.83 N ANISOU 4612 N GLN B 279 3440 3100 2893 197 213 326 N ATOM 4613 CA GLN B 279 -15.870 20.926 61.966 1.00 28.03 C ANISOU 4613 CA GLN B 279 3844 3536 3269 202 213 309 C ATOM 4614 C GLN B 279 -15.323 21.197 63.363 1.00 31.60 C ANISOU 4614 C GLN B 279 4311 4059 3635 264 208 327 C ATOM 4615 O GLN B 279 -14.843 20.287 64.046 1.00 29.30 O ANISOU 4615 O GLN B 279 4036 3784 3315 312 237 382 O ATOM 4616 CB GLN B 279 -17.286 20.341 62.054 1.00 27.48 C ANISOU 4616 CB GLN B 279 3772 3423 3246 187 277 337 C ATOM 4617 CG GLN B 279 -18.002 20.281 60.679 1.00 28.29 C ANISOU 4617 CG GLN B 279 3853 3466 3429 122 275 304 C ATOM 4618 CD GLN B 279 -19.430 19.818 60.798 1.00 34.28 C ANISOU 4618 CD GLN B 279 4602 4188 4236 104 334 324 C ATOM 4619 OE1 GLN B 279 -19.816 19.224 61.813 1.00 36.06 O ANISOU 4619 OE1 GLN B 279 4840 4416 4446 139 388 374 O ATOM 4620 NE2 GLN B 279 -20.233 20.093 59.775 1.00 29.82 N ANISOU 4620 NE2 GLN B 279 4013 3590 3727 51 324 285 N ATOM 4621 N GLY B 280 -15.407 22.457 63.797 1.00 29.02 N ANISOU 4621 N GLY B 280 3980 3779 3267 267 171 281 N ATOM 4622 CA GLY B 280 -14.910 22.812 65.123 1.00 32.14 C ANISOU 4622 CA GLY B 280 4386 4249 3576 324 161 286 C ATOM 4623 C GLY B 280 -13.405 22.968 65.216 1.00 30.84 C ANISOU 4623 C GLY B 280 4219 4132 3367 349 108 270 C ATOM 4624 O GLY B 280 -12.895 23.291 66.299 1.00 32.58 O ANISOU 4624 O GLY B 280 4444 4424 3511 397 92 267 O ATOM 4625 N SER B 281 -12.680 22.756 64.122 1.00 29.46 N ANISOU 4625 N SER B 281 4034 3924 3236 317 82 256 N ATOM 4626 CA SER B 281 -11.228 22.885 64.112 1.00 30.84 C ANISOU 4626 CA SER B 281 4202 4139 3377 337 33 239 C ATOM 4627 C SER B 281 -10.800 24.356 64.199 1.00 33.37 C ANISOU 4627 C SER B 281 4506 4503 3671 322 -27 164 C ATOM 4628 O SER B 281 -11.605 25.293 64.096 1.00 28.26 O ANISOU 4628 O SER B 281 3854 3845 3039 292 -31 124 O ATOM 4629 CB SER B 281 -10.638 22.224 62.861 1.00 26.98 C ANISOU 4629 CB SER B 281 3706 3596 2948 305 27 247 C ATOM 4630 OG SER B 281 -11.025 22.914 61.672 1.00 29.79 O ANISOU 4630 OG SER B 281 4049 3907 3364 243 6 198 O ATOM 4631 N ASP B 282 -9.491 24.551 64.380 1.00 33.46 N ANISOU 4631 N ASP B 282 4506 4561 3644 343 -72 144 N ATOM 4632 CA ASP B 282 -8.936 25.856 64.755 1.00 31.48 C ANISOU 4632 CA ASP B 282 4240 4364 3359 340 -125 73 C ATOM 4633 C ASP B 282 -8.648 26.689 63.510 1.00 36.53 C ANISOU 4633 C ASP B 282 4861 4960 4060 280 -160 18 C ATOM 4634 O ASP B 282 -7.523 26.754 63.017 1.00 42.58 O ANISOU 4634 O ASP B 282 5610 5732 4835 273 -195 -1 O ATOM 4635 CB ASP B 282 -7.671 25.666 65.587 1.00 37.18 C ANISOU 4635 CB ASP B 282 4953 5163 4010 393 -157 74 C ATOM 4636 CG ASP B 282 -7.255 26.928 66.344 1.00 45.83 C ANISOU 4636 CG ASP B 282 6032 6327 5054 401 -204 1 C ATOM 4637 OD1 ASP B 282 -8.069 27.875 66.456 1.00 46.78 O ANISOU 4637 OD1 ASP B 282 6153 6438 5183 376 -201 -42 O ATOM 4638 OD2 ASP B 282 -6.106 26.960 66.841 1.00 54.66 O ANISOU 4638 OD2 ASP B 282 7134 7511 6124 433 -242 -16 O ATOM 4639 N PHE B 283 -9.682 27.365 63.012 1.00 31.63 N ANISOU 4639 N PHE B 283 4239 4296 3481 240 -148 -6 N ATOM 4640 CA PHE B 283 -9.500 28.328 61.936 1.00 27.13 C ANISOU 4640 CA PHE B 283 3652 3691 2964 189 -178 -58 C ATOM 4641 C PHE B 283 -10.124 29.655 62.356 1.00 29.39 C ANISOU 4641 C PHE B 283 3934 3990 3244 177 -186 -111 C ATOM 4642 O PHE B 283 -10.983 29.707 63.242 1.00 28.91 O ANISOU 4642 O PHE B 283 3884 3949 3150 199 -161 -102 O ATOM 4643 CB PHE B 283 -10.080 27.824 60.594 1.00 32.75 C ANISOU 4643 CB PHE B 283 4367 4330 3747 148 -156 -33 C ATOM 4644 CG PHE B 283 -11.542 27.462 60.647 1.00 28.43 C ANISOU 4644 CG PHE B 283 3831 3751 3219 141 -110 -4 C ATOM 4645 CD1 PHE B 283 -12.515 28.428 60.417 1.00 30.10 C ANISOU 4645 CD1 PHE B 283 4037 3944 3455 114 -107 -35 C ATOM 4646 CD2 PHE B 283 -11.936 26.157 60.875 1.00 30.69 C ANISOU 4646 CD2 PHE B 283 4132 4023 3506 161 -67 56 C ATOM 4647 CE1 PHE B 283 -13.860 28.096 60.463 1.00 31.01 C ANISOU 4647 CE1 PHE B 283 4159 4033 3591 107 -66 -8 C ATOM 4648 CE2 PHE B 283 -13.280 25.816 60.923 1.00 31.09 C ANISOU 4648 CE2 PHE B 283 4190 4043 3581 152 -23 81 C ATOM 4649 CZ PHE B 283 -14.241 26.785 60.733 1.00 32.43 C ANISOU 4649 CZ PHE B 283 4351 4200 3771 125 -24 48 C ATOM 4650 N GLY B 284 -9.640 30.736 61.748 1.00 28.58 N ANISOU 4650 N GLY B 284 3813 3876 3171 144 -220 -167 N ATOM 4651 CA GLY B 284 -10.077 32.073 62.100 1.00 25.65 C ANISOU 4651 CA GLY B 284 3435 3512 2800 132 -228 -223 C ATOM 4652 C GLY B 284 -10.991 32.680 61.049 1.00 28.19 C ANISOU 4652 C GLY B 284 3754 3770 3188 89 -214 -230 C ATOM 4653 O GLY B 284 -11.349 32.031 60.064 1.00 24.72 O ANISOU 4653 O GLY B 284 3318 3287 2790 69 -198 -193 O ATOM 4654 N PRO B 285 -11.396 33.939 61.260 1.00 24.77 N ANISOU 4654 N PRO B 285 3314 3335 2764 77 -217 -280 N ATOM 4655 CA PRO B 285 -12.354 34.588 60.334 1.00 24.57 C ANISOU 4655 CA PRO B 285 3284 3253 2797 43 -201 -283 C ATOM 4656 C PRO B 285 -11.792 34.889 58.949 1.00 26.51 C ANISOU 4656 C PRO B 285 3516 3456 3100 8 -218 -290 C ATOM 4657 O PRO B 285 -12.559 34.988 57.981 1.00 25.09 O ANISOU 4657 O PRO B 285 3334 3232 2965 -14 -203 -272 O ATOM 4658 CB PRO B 285 -12.744 35.887 61.060 1.00 29.24 C ANISOU 4658 CB PRO B 285 3871 3858 3381 45 -200 -337 C ATOM 4659 CG PRO B 285 -11.981 35.933 62.332 1.00 34.53 C ANISOU 4659 CG PRO B 285 4542 4592 3987 77 -219 -368 C ATOM 4660 CD PRO B 285 -11.087 34.744 62.457 1.00 27.75 C ANISOU 4660 CD PRO B 285 3687 3764 3094 98 -232 -332 C ATOM 4661 N ILE B 286 -10.483 35.083 58.817 1.00 23.78 N ANISOU 4661 N ILE B 286 3158 3124 2753 5 -249 -316 N ATOM 4662 CA ILE B 286 -9.923 35.401 57.501 1.00 23.68 C ANISOU 4662 CA ILE B 286 3133 3071 2794 -26 -261 -320 C ATOM 4663 C ILE B 286 -9.952 34.199 56.581 1.00 26.72 C ANISOU 4663 C ILE B 286 3525 3433 3193 -32 -253 -267 C ATOM 4664 O ILE B 286 -9.986 34.358 55.345 1.00 22.45 O ANISOU 4664 O ILE B 286 2979 2854 2699 -57 -252 -259 O ATOM 4665 CB ILE B 286 -8.493 35.947 57.672 1.00 29.12 C ANISOU 4665 CB ILE B 286 3804 3782 3481 -30 -293 -366 C ATOM 4666 CG1 ILE B 286 -8.536 37.221 58.517 1.00 39.38 C ANISOU 4666 CG1 ILE B 286 5093 5097 4774 -30 -299 -429 C ATOM 4667 CG2 ILE B 286 -7.824 36.226 56.310 1.00 30.42 C ANISOU 4667 CG2 ILE B 286 3954 3903 3700 -59 -302 -366 C ATOM 4668 CD1 ILE B 286 -9.498 38.265 57.977 1.00 42.22 C ANISOU 4668 CD1 ILE B 286 5452 5408 5182 -51 -277 -441 C ATOM 4669 N PHE B 287 -9.965 32.997 57.165 1.00 23.72 N ANISOU 4669 N PHE B 287 3159 3078 2777 -7 -243 -231 N ATOM 4670 CA PHE B 287 -9.840 31.755 56.406 1.00 27.21 C ANISOU 4670 CA PHE B 287 3607 3499 3232 -10 -234 -185 C ATOM 4671 C PHE B 287 -10.897 31.662 55.310 1.00 25.41 C ANISOU 4671 C PHE B 287 3380 3224 3049 -37 -214 -166 C ATOM 4672 O PHE B 287 -10.574 31.415 54.137 1.00 24.92 O ANISOU 4672 O PHE B 287 3313 3135 3020 -58 -219 -157 O ATOM 4673 CB PHE B 287 -9.938 30.575 57.393 1.00 22.75 C ANISOU 4673 CB PHE B 287 3057 2964 2622 25 -216 -146 C ATOM 4674 CG PHE B 287 -9.727 29.201 56.778 1.00 27.40 C ANISOU 4674 CG PHE B 287 3654 3531 3226 26 -201 -99 C ATOM 4675 CD1 PHE B 287 -8.605 28.921 56.021 1.00 33.66 C ANISOU 4675 CD1 PHE B 287 4440 4316 4035 18 -221 -100 C ATOM 4676 CD2 PHE B 287 -10.630 28.172 57.029 1.00 26.91 C ANISOU 4676 CD2 PHE B 287 3606 3455 3162 36 -163 -56 C ATOM 4677 CE1 PHE B 287 -8.396 27.638 55.488 1.00 36.29 C ANISOU 4677 CE1 PHE B 287 4780 4626 4381 20 -204 -60 C ATOM 4678 CE2 PHE B 287 -10.428 26.881 56.503 1.00 31.11 C ANISOU 4678 CE2 PHE B 287 4145 3962 3712 36 -145 -16 C ATOM 4679 CZ PHE B 287 -9.308 26.620 55.734 1.00 31.83 C ANISOU 4679 CZ PHE B 287 4230 4046 3818 29 -166 -19 C ATOM 4680 N MET B 288 -12.180 31.866 55.653 1.00 22.39 N ANISOU 4680 N MET B 288 3002 2837 2668 -37 -190 -160 N ATOM 4681 CA MET B 288 -13.202 31.760 54.606 1.00 21.74 C ANISOU 4681 CA MET B 288 2916 2717 2628 -61 -174 -144 C ATOM 4682 C MET B 288 -13.532 33.112 53.965 1.00 20.52 C ANISOU 4682 C MET B 288 2749 2545 2505 -80 -183 -173 C ATOM 4683 O MET B 288 -14.072 33.137 52.847 1.00 22.25 O ANISOU 4683 O MET B 288 2960 2738 2758 -99 -179 -163 O ATOM 4684 CB MET B 288 -14.495 31.096 55.157 1.00 23.12 C ANISOU 4684 CB MET B 288 3097 2891 2796 -52 -140 -116 C ATOM 4685 CG MET B 288 -15.628 30.861 54.114 1.00 23.01 C ANISOU 4685 CG MET B 288 3074 2845 2825 -78 -124 -102 C ATOM 4686 SD MET B 288 -15.108 30.042 52.602 1.00 24.64 S ANISOU 4686 SD MET B 288 3274 3024 3063 -102 -135 -90 S ATOM 4687 CE MET B 288 -15.933 28.418 52.659 1.00 21.88 C ANISOU 4687 CE MET B 288 2929 2659 2726 -105 -98 -54 C ATOM 4688 N THR B 289 -13.176 34.219 54.619 1.00 20.58 N ANISOU 4688 N THR B 289 2752 2566 2502 -73 -194 -210 N ATOM 4689 CA THR B 289 -13.477 35.546 54.078 1.00 21.02 C ANISOU 4689 CA THR B 289 2796 2600 2592 -87 -196 -235 C ATOM 4690 C THR B 289 -12.877 35.743 52.687 1.00 22.29 C ANISOU 4690 C THR B 289 2947 2733 2789 -108 -208 -232 C ATOM 4691 O THR B 289 -13.575 36.166 51.759 1.00 21.17 O ANISOU 4691 O THR B 289 2798 2567 2678 -119 -200 -222 O ATOM 4692 CB THR B 289 -12.972 36.640 55.029 1.00 21.60 C ANISOU 4692 CB THR B 289 2866 2689 2652 -79 -205 -282 C ATOM 4693 OG1 THR B 289 -13.673 36.554 56.267 1.00 22.94 O ANISOU 4693 OG1 THR B 289 3045 2886 2785 -58 -190 -286 O ATOM 4694 CG2 THR B 289 -13.234 38.038 54.436 1.00 21.30 C ANISOU 4694 CG2 THR B 289 2815 2618 2658 -94 -200 -307 C ATOM 4695 N AILE B 290 -11.578 35.458 52.526 0.51 22.22 N ANISOU 4695 N AILE B 290 2938 2731 2776 -110 -228 -238 N ATOM 4696 N BILE B 290 -11.585 35.455 52.520 0.49 22.23 N ANISOU 4696 N BILE B 290 2938 2732 2777 -110 -228 -238 N ATOM 4697 CA AILE B 290 -10.925 35.703 51.231 0.51 23.06 C ANISOU 4697 CA AILE B 290 3034 2812 2915 -127 -237 -235 C ATOM 4698 CA BILE B 290 -10.939 35.715 51.227 0.49 23.06 C ANISOU 4698 CA BILE B 290 3034 2812 2916 -127 -236 -235 C ATOM 4699 C AILE B 290 -11.540 34.880 50.104 0.51 21.80 C ANISOU 4699 C AILE B 290 2877 2636 2768 -136 -228 -199 C ATOM 4700 C BILE B 290 -11.533 34.881 50.095 0.49 21.80 C ANISOU 4700 C BILE B 290 2877 2637 2769 -136 -228 -199 C ATOM 4701 O AILE B 290 -11.900 35.467 49.067 0.51 20.04 O ANISOU 4701 O AILE B 290 2646 2394 2575 -146 -225 -194 O ATOM 4702 O BILE B 290 -11.879 35.459 49.050 0.49 20.06 O ANISOU 4702 O BILE B 290 2649 2396 2577 -146 -225 -194 O ATOM 4703 CB AILE B 290 -9.405 35.494 51.351 0.51 27.05 C ANISOU 4703 CB AILE B 290 3535 3331 3413 -126 -258 -250 C ATOM 4704 CB BILE B 290 -9.413 35.560 51.355 0.49 27.04 C ANISOU 4704 CB BILE B 290 3533 3328 3412 -126 -257 -251 C ATOM 4705 CG1AILE B 290 -8.838 36.310 52.505 0.51 24.89 C ANISOU 4705 CG1AILE B 290 3254 3079 3124 -118 -269 -294 C ATOM 4706 CG1BILE B 290 -8.897 36.464 52.473 0.49 24.97 C ANISOU 4706 CG1BILE B 290 3263 3086 3138 -119 -268 -296 C ATOM 4707 CG2AILE B 290 -8.724 35.870 50.040 0.51 28.35 C ANISOU 4707 CG2AILE B 290 3689 3467 3614 -143 -262 -247 C ATOM 4708 CG2BILE B 290 -8.742 35.887 50.025 0.49 28.34 C ANISOU 4708 CG2BILE B 290 3688 3466 3614 -143 -262 -247 C ATOM 4709 CD1AILE B 290 -9.143 37.770 52.387 0.51 30.16 C ANISOU 4709 CD1AILE B 290 3911 3722 3825 -129 -261 -325 C ATOM 4710 CD1BILE B 290 -7.409 36.500 52.602 0.49 30.46 C ANISOU 4710 CD1BILE B 290 3946 3796 3831 -120 -290 -320 C ATOM 4711 N PRO B 291 -11.664 33.544 50.208 1.00 19.92 N ANISOU 4711 N PRO B 291 2649 2408 2513 -132 -224 -175 N ATOM 4712 CA PRO B 291 -12.297 32.797 49.101 1.00 19.51 C ANISOU 4712 CA PRO B 291 2596 2341 2477 -144 -216 -151 C ATOM 4713 C PRO B 291 -13.728 33.204 48.825 1.00 20.31 C ANISOU 4713 C PRO B 291 2690 2436 2593 -149 -202 -146 C ATOM 4714 O PRO B 291 -14.120 33.284 47.657 1.00 19.78 O ANISOU 4714 O PRO B 291 2613 2357 2545 -160 -203 -138 O ATOM 4715 CB PRO B 291 -12.245 31.326 49.550 1.00 22.27 C ANISOU 4715 CB PRO B 291 2956 2697 2808 -138 -206 -130 C ATOM 4716 CG PRO B 291 -11.294 31.276 50.699 1.00 27.25 C ANISOU 4716 CG PRO B 291 3594 3350 3409 -118 -214 -137 C ATOM 4717 CD PRO B 291 -11.196 32.644 51.288 1.00 22.99 C ANISOU 4717 CD PRO B 291 3048 2821 2866 -114 -224 -168 C ATOM 4718 N ALA B 292 -14.514 33.489 49.871 1.00 20.44 N ANISOU 4718 N ALA B 292 2708 2461 2598 -139 -189 -150 N ATOM 4719 CA ALA B 292 -15.934 33.770 49.652 1.00 22.44 C ANISOU 4719 CA ALA B 292 2951 2710 2866 -142 -174 -143 C ATOM 4720 C ALA B 292 -16.101 35.103 48.944 1.00 20.12 C ANISOU 4720 C ALA B 292 2645 2404 2596 -144 -179 -153 C ATOM 4721 O ALA B 292 -16.949 35.236 48.052 1.00 20.76 O ANISOU 4721 O ALA B 292 2712 2480 2694 -149 -176 -142 O ATOM 4722 CB ALA B 292 -16.707 33.746 50.989 1.00 19.94 C ANISOU 4722 CB ALA B 292 2640 2406 2532 -128 -155 -144 C ATOM 4723 N PHE B 293 -15.274 36.096 49.296 1.00 19.75 N ANISOU 4723 N PHE B 293 2600 2352 2551 -139 -186 -175 N ATOM 4724 CA PHE B 293 -15.372 37.378 48.601 1.00 20.92 C ANISOU 4724 CA PHE B 293 2737 2481 2729 -140 -184 -181 C ATOM 4725 C PHE B 293 -14.722 37.335 47.222 1.00 21.12 C ANISOU 4725 C PHE B 293 2757 2496 2770 -148 -194 -168 C ATOM 4726 O PHE B 293 -15.206 37.994 46.295 1.00 21.12 O ANISOU 4726 O PHE B 293 2747 2486 2791 -146 -189 -155 O ATOM 4727 CB PHE B 293 -14.789 38.511 49.470 1.00 22.51 C ANISOU 4727 CB PHE B 293 2940 2676 2936 -134 -182 -214 C ATOM 4728 CG PHE B 293 -15.826 39.095 50.392 1.00 26.18 C ANISOU 4728 CG PHE B 293 3404 3144 3398 -123 -164 -226 C ATOM 4729 CD1 PHE B 293 -16.224 38.390 51.526 1.00 22.81 C ANISOU 4729 CD1 PHE B 293 2987 2741 2938 -114 -160 -228 C ATOM 4730 CD2 PHE B 293 -16.489 40.281 50.063 1.00 21.10 C ANISOU 4730 CD2 PHE B 293 2751 2479 2785 -118 -149 -228 C ATOM 4731 CE1 PHE B 293 -17.229 38.878 52.370 1.00 25.90 C ANISOU 4731 CE1 PHE B 293 3378 3137 3325 -103 -140 -237 C ATOM 4732 CE2 PHE B 293 -17.493 40.788 50.904 1.00 24.20 C ANISOU 4732 CE2 PHE B 293 3143 2874 3177 -106 -130 -238 C ATOM 4733 CZ PHE B 293 -17.875 40.083 52.052 1.00 25.22 C ANISOU 4733 CZ PHE B 293 3282 3030 3272 -99 -126 -243 C ATOM 4734 N PHE B 294 -13.618 36.593 47.063 1.00 22.07 N ANISOU 4734 N PHE B 294 2885 2620 2880 -155 -208 -168 N ATOM 4735 CA PHE B 294 -13.030 36.444 45.730 1.00 21.25 C ANISOU 4735 CA PHE B 294 2777 2508 2788 -161 -215 -155 C ATOM 4736 C PHE B 294 -14.028 35.822 44.753 1.00 22.11 C ANISOU 4736 C PHE B 294 2880 2625 2895 -164 -213 -133 C ATOM 4737 O PHE B 294 -14.103 36.228 43.579 1.00 22.62 O ANISOU 4737 O PHE B 294 2937 2687 2972 -162 -214 -120 O ATOM 4738 CB PHE B 294 -11.759 35.598 45.809 1.00 19.27 C ANISOU 4738 CB PHE B 294 2534 2262 2525 -166 -227 -158 C ATOM 4739 CG PHE B 294 -11.076 35.387 44.464 1.00 22.26 C ANISOU 4739 CG PHE B 294 2911 2634 2914 -172 -232 -145 C ATOM 4740 CD1 PHE B 294 -10.560 36.470 43.759 1.00 27.49 C ANISOU 4740 CD1 PHE B 294 3565 3279 3600 -172 -228 -145 C ATOM 4741 CD2 PHE B 294 -10.930 34.112 43.936 1.00 25.94 C ANISOU 4741 CD2 PHE B 294 3382 3107 3367 -177 -237 -134 C ATOM 4742 CE1 PHE B 294 -9.905 36.276 42.520 1.00 32.09 C ANISOU 4742 CE1 PHE B 294 4147 3858 4190 -174 -230 -131 C ATOM 4743 CE2 PHE B 294 -10.305 33.909 42.690 1.00 22.52 C ANISOU 4743 CE2 PHE B 294 2948 2670 2940 -181 -240 -124 C ATOM 4744 CZ PHE B 294 -9.775 34.996 42.006 1.00 29.25 C ANISOU 4744 CZ PHE B 294 3792 3510 3811 -178 -237 -121 C ATOM 4745 N ALA B 295 -14.798 34.823 45.212 1.00 19.28 N ANISOU 4745 N ALA B 295 2524 2279 2523 -167 -210 -129 N ATOM 4746 CA ALA B 295 -15.761 34.169 44.330 1.00 20.66 C ANISOU 4746 CA ALA B 295 2688 2464 2700 -174 -209 -117 C ATOM 4747 C ALA B 295 -16.834 35.117 43.808 1.00 20.01 C ANISOU 4747 C ALA B 295 2589 2386 2630 -165 -205 -109 C ATOM 4748 O ALA B 295 -17.468 34.807 42.787 1.00 21.61 O ANISOU 4748 O ALA B 295 2776 2601 2832 -167 -210 -101 O ATOM 4749 CB ALA B 295 -16.437 32.996 45.053 1.00 22.35 C ANISOU 4749 CB ALA B 295 2905 2684 2905 -180 -200 -116 C ATOM 4750 N LYS B 296 -17.061 36.251 44.475 1.00 22.68 N ANISOU 4750 N LYS B 296 2925 2714 2977 -154 -195 -114 N ATOM 4751 CA LYS B 296 -18.094 37.176 44.006 1.00 20.92 C ANISOU 4751 CA LYS B 296 2686 2494 2769 -141 -188 -103 C ATOM 4752 C LYS B 296 -17.692 37.907 42.723 1.00 23.64 C ANISOU 4752 C LYS B 296 3023 2834 3123 -132 -192 -87 C ATOM 4753 O LYS B 296 -18.543 38.575 42.119 1.00 20.19 O ANISOU 4753 O LYS B 296 2571 2406 2696 -116 -186 -71 O ATOM 4754 CB LYS B 296 -18.454 38.178 45.121 1.00 20.31 C ANISOU 4754 CB LYS B 296 2610 2405 2703 -130 -171 -114 C ATOM 4755 CG LYS B 296 -19.069 37.473 46.362 1.00 20.13 C ANISOU 4755 CG LYS B 296 2592 2391 2665 -134 -163 -123 C ATOM 4756 CD LYS B 296 -19.391 38.481 47.509 1.00 20.01 C ANISOU 4756 CD LYS B 296 2580 2366 2655 -121 -146 -139 C ATOM 4757 CE LYS B 296 -19.516 37.797 48.914 1.00 20.19 C ANISOU 4757 CE LYS B 296 2615 2400 2654 -121 -138 -151 C ATOM 4758 NZ LYS B 296 -20.563 36.781 48.938 1.00 20.10 N ANISOU 4758 NZ LYS B 296 2595 2403 2638 -126 -130 -135 N ATOM 4759 N THR B 297 -16.440 37.772 42.272 1.00 19.62 N ANISOU 4759 N THR B 297 2526 2317 2614 -137 -199 -88 N ATOM 4760 CA THR B 297 -16.076 38.253 40.936 1.00 21.21 C ANISOU 4760 CA THR B 297 2720 2518 2820 -127 -200 -68 C ATOM 4761 C THR B 297 -16.830 37.516 39.845 1.00 20.49 C ANISOU 4761 C THR B 297 2616 2458 2710 -126 -212 -56 C ATOM 4762 O THR B 297 -16.846 37.976 38.691 1.00 22.42 O ANISOU 4762 O THR B 297 2852 2714 2952 -110 -212 -36 O ATOM 4763 CB THR B 297 -14.564 38.102 40.679 1.00 21.18 C ANISOU 4763 CB THR B 297 2730 2500 2818 -136 -204 -73 C ATOM 4764 OG1 THR B 297 -14.190 36.725 40.814 1.00 23.13 O ANISOU 4764 OG1 THR B 297 2985 2759 3045 -152 -217 -84 O ATOM 4765 CG2 THR B 297 -13.758 38.920 41.652 1.00 22.33 C ANISOU 4765 CG2 THR B 297 2882 2617 2984 -138 -194 -91 C ATOM 4766 N SER B 298 -17.454 36.386 40.190 1.00 21.77 N ANISOU 4766 N SER B 298 2775 2638 2860 -140 -220 -69 N ATOM 4767 CA SER B 298 -18.268 35.623 39.262 1.00 21.92 C ANISOU 4767 CA SER B 298 2776 2687 2864 -143 -232 -68 C ATOM 4768 C SER B 298 -19.368 36.451 38.616 1.00 23.29 C ANISOU 4768 C SER B 298 2926 2884 3039 -121 -232 -51 C ATOM 4769 O SER B 298 -19.864 36.073 37.553 1.00 24.24 O ANISOU 4769 O SER B 298 3028 3038 3143 -117 -246 -48 O ATOM 4770 CB SER B 298 -18.916 34.438 39.989 1.00 21.22 C ANISOU 4770 CB SER B 298 2685 2604 2775 -164 -232 -87 C ATOM 4771 OG SER B 298 -19.660 34.902 41.103 1.00 21.52 O ANISOU 4771 OG SER B 298 2720 2634 2824 -159 -218 -87 O ATOM 4772 N ALA B 299 -19.807 37.526 39.256 1.00 21.18 N ANISOU 4772 N ALA B 299 2656 2602 2789 -106 -217 -41 N ATOM 4773 CA ALA B 299 -20.864 38.355 38.664 1.00 24.87 C ANISOU 4773 CA ALA B 299 3099 3090 3259 -80 -214 -20 C ATOM 4774 C ALA B 299 -20.360 39.237 37.530 1.00 24.37 C ANISOU 4774 C ALA B 299 3036 3030 3194 -54 -211 9 C ATOM 4775 O ALA B 299 -21.182 39.817 36.810 1.00 26.18 O ANISOU 4775 O ALA B 299 3244 3286 3418 -27 -211 33 O ATOM 4776 CB ALA B 299 -21.512 39.242 39.735 1.00 24.72 C ANISOU 4776 CB ALA B 299 3078 3051 3263 -70 -194 -18 C ATOM 4777 N VAL B 300 -19.046 39.350 37.359 1.00 21.57 N ANISOU 4777 N VAL B 300 2703 2651 2842 -59 -206 10 N ATOM 4778 CA VAL B 300 -18.471 40.323 36.441 1.00 24.31 C ANISOU 4778 CA VAL B 300 3052 2990 3195 -34 -193 42 C ATOM 4779 C VAL B 300 -17.709 39.674 35.281 1.00 24.50 C ANISOU 4779 C VAL B 300 3081 3036 3193 -35 -206 47 C ATOM 4780 O VAL B 300 -17.721 40.198 34.169 1.00 26.51 O ANISOU 4780 O VAL B 300 3328 3309 3436 -6 -201 78 O ATOM 4781 CB VAL B 300 -17.551 41.304 37.201 1.00 32.09 C ANISOU 4781 CB VAL B 300 4054 3922 4217 -36 -168 40 C ATOM 4782 CG1 VAL B 300 -16.950 42.335 36.250 1.00 40.15 C ANISOU 4782 CG1 VAL B 300 5076 4927 5252 -10 -147 76 C ATOM 4783 CG2 VAL B 300 -18.337 42.018 38.317 1.00 34.03 C ANISOU 4783 CG2 VAL B 300 4294 4148 4486 -32 -153 32 C ATOM 4784 N TYR B 301 -16.989 38.566 35.523 1.00 26.88 N ANISOU 4784 N TYR B 301 3395 3333 3484 -64 -219 20 N ATOM 4785 CA TYR B 301 -15.877 38.233 34.617 1.00 23.50 C ANISOU 4785 CA TYR B 301 2978 2907 3043 -64 -221 26 C ATOM 4786 C TYR B 301 -16.330 37.646 33.271 1.00 25.38 C ANISOU 4786 C TYR B 301 3203 3196 3243 -52 -238 32 C ATOM 4787 O TYR B 301 -15.609 37.803 32.269 1.00 23.65 O ANISOU 4787 O TYR B 301 2990 2986 3010 -37 -234 50 O ATOM 4788 CB TYR B 301 -14.855 37.299 35.321 1.00 25.34 C ANISOU 4788 CB TYR B 301 3230 3118 3281 -95 -226 -3 C ATOM 4789 CG TYR B 301 -15.299 35.862 35.496 1.00 26.46 C ANISOU 4789 CG TYR B 301 3370 3280 3404 -118 -245 -31 C ATOM 4790 CD1 TYR B 301 -15.349 34.996 34.407 1.00 21.74 C ANISOU 4790 CD1 TYR B 301 2766 2714 2779 -119 -259 -37 C ATOM 4791 CD2 TYR B 301 -15.631 35.351 36.755 1.00 27.24 C ANISOU 4791 CD2 TYR B 301 3472 3365 3514 -137 -245 -51 C ATOM 4792 CE1 TYR B 301 -15.757 33.700 34.534 1.00 24.67 C ANISOU 4792 CE1 TYR B 301 3133 3098 3141 -142 -271 -66 C ATOM 4793 CE2 TYR B 301 -16.051 34.024 36.897 1.00 26.71 C ANISOU 4793 CE2 TYR B 301 3402 3310 3436 -157 -255 -73 C ATOM 4794 CZ TYR B 301 -16.106 33.207 35.779 1.00 26.51 C ANISOU 4794 CZ TYR B 301 3369 3311 3391 -161 -267 -82 C ATOM 4795 OH TYR B 301 -16.529 31.902 35.870 1.00 29.45 O ANISOU 4795 OH TYR B 301 3737 3691 3761 -184 -272 -107 O ATOM 4796 N ASN B 302 -17.491 36.962 33.200 1.00 25.04 N ANISOU 4796 N ASN B 302 3141 3191 3183 -57 -257 15 N ATOM 4797 CA ASN B 302 -17.866 36.321 31.936 1.00 22.47 C ANISOU 4797 CA ASN B 302 2800 2918 2818 -49 -277 10 C ATOM 4798 C ASN B 302 -18.078 37.319 30.799 1.00 24.43 C ANISOU 4798 C ASN B 302 3038 3199 3047 -5 -273 50 C ATOM 4799 O ASN B 302 -17.599 37.055 29.678 1.00 22.59 O ANISOU 4799 O ASN B 302 2807 2996 2782 8 -279 57 O ATOM 4800 CB ASN B 302 -19.099 35.425 32.131 1.00 21.43 C ANISOU 4800 CB ASN B 302 2644 2818 2679 -67 -298 -22 C ATOM 4801 CG ASN B 302 -18.738 34.084 32.735 1.00 25.22 C ANISOU 4801 CG ASN B 302 3136 3278 3169 -107 -302 -62 C ATOM 4802 OD1 ASN B 302 -18.010 33.297 32.131 1.00 25.98 O ANISOU 4802 OD1 ASN B 302 3243 3380 3250 -118 -308 -77 O ATOM 4803 ND2 ASN B 302 -19.213 33.832 33.945 1.00 25.60 N ANISOU 4803 ND2 ASN B 302 3184 3302 3242 -127 -295 -75 N ATOM 4804 N PRO B 303 -18.803 38.434 30.977 1.00 24.94 N ANISOU 4804 N PRO B 303 3089 3262 3124 23 -260 81 N ATOM 4805 CA PRO B 303 -18.878 39.418 29.881 1.00 24.88 C ANISOU 4805 CA PRO B 303 3074 3281 3098 71 -250 129 C ATOM 4806 C PRO B 303 -17.528 39.969 29.466 1.00 26.52 C ANISOU 4806 C PRO B 303 3306 3455 3316 82 -223 157 C ATOM 4807 O PRO B 303 -17.354 40.335 28.295 1.00 27.71 O ANISOU 4807 O PRO B 303 3453 3637 3437 118 -217 191 O ATOM 4808 CB PRO B 303 -19.768 40.528 30.455 1.00 27.73 C ANISOU 4808 CB PRO B 303 3421 3628 3486 95 -233 155 C ATOM 4809 CG PRO B 303 -20.558 39.878 31.491 1.00 29.10 C ANISOU 4809 CG PRO B 303 3584 3799 3674 62 -248 116 C ATOM 4810 CD PRO B 303 -19.698 38.808 32.091 1.00 26.52 C ANISOU 4810 CD PRO B 303 3279 3444 3354 17 -255 75 C ATOM 4811 N VAL B 304 -16.576 40.070 30.394 1.00 24.63 N ANISOU 4811 N VAL B 304 3088 3154 3115 55 -207 144 N ATOM 4812 CA VAL B 304 -15.239 40.543 30.027 1.00 27.35 C ANISOU 4812 CA VAL B 304 3452 3465 3475 61 -181 166 C ATOM 4813 C VAL B 304 -14.563 39.554 29.083 1.00 28.31 C ANISOU 4813 C VAL B 304 3581 3618 3558 55 -196 154 C ATOM 4814 O VAL B 304 -13.968 39.954 28.078 1.00 25.34 O ANISOU 4814 O VAL B 304 3209 3251 3167 82 -179 188 O ATOM 4815 CB VAL B 304 -14.384 40.807 31.280 1.00 28.46 C ANISOU 4815 CB VAL B 304 3608 3540 3665 30 -165 146 C ATOM 4816 CG1 VAL B 304 -12.945 41.267 30.872 1.00 29.50 C ANISOU 4816 CG1 VAL B 304 3755 3637 3817 32 -138 164 C ATOM 4817 CG2 VAL B 304 -15.077 41.837 32.186 1.00 22.25 C ANISOU 4817 CG2 VAL B 304 2815 2723 2915 37 -148 153 C ATOM 4818 N ILE B 305 -14.682 38.249 29.358 1.00 23.53 N ANISOU 4818 N ILE B 305 2976 3029 2936 22 -223 109 N ATOM 4819 CA ILE B 305 -14.157 37.245 28.427 1.00 20.96 C ANISOU 4819 CA ILE B 305 2655 2735 2573 17 -237 92 C ATOM 4820 C ILE B 305 -14.818 37.390 27.062 1.00 24.53 C ANISOU 4820 C ILE B 305 3091 3254 2976 56 -247 114 C ATOM 4821 O ILE B 305 -14.151 37.341 26.017 1.00 24.33 O ANISOU 4821 O ILE B 305 3073 3250 2922 75 -240 130 O ATOM 4822 CB ILE B 305 -14.351 35.825 29.000 1.00 25.41 C ANISOU 4822 CB ILE B 305 3219 3302 3134 -24 -261 39 C ATOM 4823 CG1 ILE B 305 -13.533 35.628 30.278 1.00 25.08 C ANISOU 4823 CG1 ILE B 305 3195 3201 3133 -55 -251 23 C ATOM 4824 CG2 ILE B 305 -13.999 34.749 27.950 1.00 24.44 C ANISOU 4824 CG2 ILE B 305 3098 3216 2972 -28 -275 17 C ATOM 4825 CD1 ILE B 305 -13.847 34.281 31.015 1.00 26.64 C ANISOU 4825 CD1 ILE B 305 3393 3396 3332 -91 -268 -22 C ATOM 4826 N TYR B 306 -16.142 37.559 27.061 1.00 24.44 N ANISOU 4826 N TYR B 306 3055 3280 2951 69 -264 114 N ATOM 4827 CA TYR B 306 -16.950 37.649 25.842 1.00 24.77 C ANISOU 4827 CA TYR B 306 3074 3396 2940 108 -280 129 C ATOM 4828 C TYR B 306 -16.469 38.766 24.926 1.00 26.38 C ANISOU 4828 C TYR B 306 3285 3608 3130 159 -252 191 C ATOM 4829 O TYR B 306 -16.336 38.592 23.705 1.00 26.16 O ANISOU 4829 O TYR B 306 3254 3635 3051 188 -258 204 O ATOM 4830 CB TYR B 306 -18.393 37.915 26.275 1.00 24.13 C ANISOU 4830 CB TYR B 306 2964 3340 2864 115 -296 126 C ATOM 4831 CG TYR B 306 -19.511 37.692 25.285 1.00 24.98 C ANISOU 4831 CG TYR B 306 3038 3535 2919 143 -326 121 C ATOM 4832 CD1 TYR B 306 -19.343 36.916 24.143 1.00 25.12 C ANISOU 4832 CD1 TYR B 306 3050 3612 2882 149 -347 99 C ATOM 4833 CD2 TYR B 306 -20.776 38.226 25.546 1.00 22.99 C ANISOU 4833 CD2 TYR B 306 2756 3308 2672 162 -334 132 C ATOM 4834 CE1 TYR B 306 -20.408 36.701 23.265 1.00 29.14 C ANISOU 4834 CE1 TYR B 306 3523 4208 3340 175 -379 86 C ATOM 4835 CE2 TYR B 306 -21.838 38.018 24.681 1.00 26.73 C ANISOU 4835 CE2 TYR B 306 3193 3868 3097 188 -365 124 C ATOM 4836 CZ TYR B 306 -21.648 37.257 23.550 1.00 30.53 C ANISOU 4836 CZ TYR B 306 3667 4411 3523 194 -389 100 C ATOM 4837 OH TYR B 306 -22.721 37.058 22.715 1.00 31.09 O ANISOU 4837 OH TYR B 306 3696 4572 3544 220 -423 86 O ATOM 4838 N ILE B 307 -16.280 39.948 25.498 1.00 24.39 N ANISOU 4838 N ILE B 307 3040 3303 2923 173 -219 232 N ATOM 4839 CA ILE B 307 -15.806 41.089 24.727 1.00 27.80 C ANISOU 4839 CA ILE B 307 3479 3729 3354 221 -182 296 C ATOM 4840 C ILE B 307 -14.414 40.808 24.184 1.00 24.39 C ANISOU 4840 C ILE B 307 3070 3279 2917 215 -164 300 C ATOM 4841 O ILE B 307 -14.093 41.164 23.052 1.00 29.19 O ANISOU 4841 O ILE B 307 3681 3919 3492 256 -147 342 O ATOM 4842 CB ILE B 307 -15.822 42.350 25.607 1.00 30.40 C ANISOU 4842 CB ILE B 307 3812 3992 3746 228 -146 328 C ATOM 4843 CG1 ILE B 307 -17.261 42.721 25.971 1.00 31.12 C ANISOU 4843 CG1 ILE B 307 3878 4108 3836 244 -159 332 C ATOM 4844 CG2 ILE B 307 -15.093 43.489 24.905 1.00 38.43 C ANISOU 4844 CG2 ILE B 307 4840 4984 4778 270 -97 393 C ATOM 4845 CD1 ILE B 307 -17.355 43.734 27.119 1.00 40.66 C ANISOU 4845 CD1 ILE B 307 5091 5247 5112 238 -128 344 C ATOM 4846 N AMET B 308 -13.568 40.156 24.978 0.56 25.47 N ANISOU 4846 N AMET B 308 3223 3368 3086 166 -167 259 N ATOM 4847 N BMET B 308 -13.568 40.159 24.980 0.44 25.49 N ANISOU 4847 N BMET B 308 3226 3370 3089 166 -166 260 N ATOM 4848 CA AMET B 308 -12.187 39.934 24.547 0.56 30.37 C ANISOU 4848 CA AMET B 308 3863 3966 3710 159 -147 264 C ATOM 4849 CA BMET B 308 -12.190 39.930 24.554 0.44 30.36 C ANISOU 4849 CA BMET B 308 3863 3965 3709 159 -147 264 C ATOM 4850 C AMET B 308 -12.069 38.830 23.504 0.56 31.65 C ANISOU 4850 C AMET B 308 4026 4189 3810 162 -171 241 C ATOM 4851 C BMET B 308 -12.061 38.822 23.520 0.44 31.64 C ANISOU 4851 C BMET B 308 4025 4187 3810 162 -171 240 C ATOM 4852 O AMET B 308 -11.130 38.848 22.697 0.56 33.98 O ANISOU 4852 O AMET B 308 4334 4487 4091 178 -150 262 O ATOM 4853 O BMET B 308 -11.105 38.830 22.734 0.44 33.97 O ANISOU 4853 O BMET B 308 4333 4484 4091 177 -150 261 O ATOM 4854 CB AMET B 308 -11.293 39.597 25.741 0.56 30.29 C ANISOU 4854 CB AMET B 308 3867 3890 3752 109 -143 228 C ATOM 4855 CB BMET B 308 -11.309 39.589 25.754 0.44 30.29 C ANISOU 4855 CB BMET B 308 3867 3890 3752 109 -143 228 C ATOM 4856 CG AMET B 308 -11.073 40.737 26.705 0.56 36.27 C ANISOU 4856 CG AMET B 308 4626 4582 4573 104 -113 246 C ATOM 4857 CG BMET B 308 -11.123 40.740 26.695 0.44 36.24 C ANISOU 4857 CG BMET B 308 4622 4580 4568 105 -114 246 C ATOM 4858 SD AMET B 308 -10.108 40.236 28.152 0.56 45.37 S ANISOU 4858 SD AMET B 308 5790 5674 5775 48 -118 196 S ATOM 4859 SD BMET B 308 -10.358 42.119 25.835 0.44 45.42 S ANISOU 4859 SD BMET B 308 5789 5715 5753 148 -58 315 S ATOM 4860 CE AMET B 308 -8.868 39.188 27.403 0.56 38.51 C ANISOU 4860 CE AMET B 308 4934 4816 4882 37 -121 183 C ATOM 4861 CE BMET B 308 -8.845 41.368 25.239 0.44 34.90 C ANISOU 4861 CE BMET B 308 4472 4378 4412 133 -50 305 C ATOM 4862 N MET B 309 -12.978 37.853 23.508 1.00 28.08 N ANISOU 4862 N MET B 309 3560 3784 3326 146 -211 195 N ATOM 4863 CA MET B 309 -12.785 36.648 22.708 1.00 27.87 C ANISOU 4863 CA MET B 309 3534 3803 3250 137 -234 157 C ATOM 4864 C MET B 309 -13.850 36.380 21.653 1.00 38.37 C ANISOU 4864 C MET B 309 4842 5224 4514 168 -263 150 C ATOM 4865 O MET B 309 -13.801 35.321 21.014 1.00 36.74 O ANISOU 4865 O MET B 309 4632 5059 4267 157 -285 107 O ATOM 4866 CB MET B 309 -12.672 35.423 23.628 1.00 29.46 C ANISOU 4866 CB MET B 309 3740 3976 3476 81 -254 94 C ATOM 4867 CG MET B 309 -11.497 35.533 24.589 1.00 27.62 C ANISOU 4867 CG MET B 309 3529 3666 3298 53 -230 96 C ATOM 4868 SD MET B 309 -11.107 34.008 25.428 1.00 28.34 S ANISOU 4868 SD MET B 309 3630 3730 3409 -2 -248 34 S ATOM 4869 CE MET B 309 -10.294 33.104 24.094 1.00 27.82 C ANISOU 4869 CE MET B 309 3574 3699 3298 6 -247 18 C ATOM 4870 N ASN B 310 -14.811 37.275 21.446 1.00 28.92 N ANISOU 4870 N ASN B 310 3625 4060 3304 207 -264 187 N ATOM 4871 CA ASN B 310 -15.784 37.083 20.377 1.00 27.86 C ANISOU 4871 CA ASN B 310 3464 4020 3101 242 -294 182 C ATOM 4872 C ASN B 310 -15.843 38.359 19.546 1.00 34.56 C ANISOU 4872 C ASN B 310 4311 4898 3923 311 -267 260 C ATOM 4873 O ASN B 310 -16.330 39.397 20.012 1.00 31.49 O ANISOU 4873 O ASN B 310 3914 4484 3565 332 -250 304 O ATOM 4874 CB ASN B 310 -17.155 36.706 20.925 1.00 27.14 C ANISOU 4874 CB ASN B 310 3341 3957 3012 223 -330 142 C ATOM 4875 CG ASN B 310 -18.103 36.273 19.840 1.00 32.75 C ANISOU 4875 CG ASN B 310 4020 4772 3652 251 -368 120 C ATOM 4876 OD1 ASN B 310 -18.815 37.093 19.261 1.00 30.15 O ANISOU 4876 OD1 ASN B 310 3670 4496 3289 304 -371 163 O ATOM 4877 ND2 ASN B 310 -18.108 34.975 19.537 1.00 34.85 N ANISOU 4877 ND2 ASN B 310 4280 5068 3894 216 -396 50 N ATOM 4878 N LYS B 311 -15.347 38.269 18.309 1.00 31.66 N ANISOU 4878 N LYS B 311 3950 4581 3497 348 -261 279 N ATOM 4879 CA LYS B 311 -15.196 39.458 17.483 1.00 32.22 C ANISOU 4879 CA LYS B 311 4025 4674 3545 416 -226 362 C ATOM 4880 C LYS B 311 -16.553 40.013 17.070 1.00 33.57 C ANISOU 4880 C LYS B 311 4162 4918 3675 466 -246 390 C ATOM 4881 O LYS B 311 -16.759 41.229 17.085 1.00 34.82 O ANISOU 4881 O LYS B 311 4319 5059 3853 511 -213 460 O ATOM 4882 CB LYS B 311 -14.321 39.124 16.272 1.00 38.96 C ANISOU 4882 CB LYS B 311 4893 5568 4341 444 -214 373 C ATOM 4883 CG LYS B 311 -14.167 40.251 15.271 1.00 49.39 C ANISOU 4883 CG LYS B 311 6218 6920 5627 521 -174 462 C ATOM 4884 CD LYS B 311 -13.541 39.752 13.962 1.00 50.45 C ANISOU 4884 CD LYS B 311 6363 7120 5686 552 -172 464 C ATOM 4885 N GLN B 312 -17.510 39.137 16.740 1.00 32.41 N ANISOU 4885 N GLN B 312 3986 4851 3477 459 -300 333 N ATOM 4886 CA GLN B 312 -18.835 39.607 16.339 1.00 31.32 C ANISOU 4886 CA GLN B 312 3810 4792 3298 507 -324 354 C ATOM 4887 C GLN B 312 -19.516 40.374 17.464 1.00 33.82 C ANISOU 4887 C GLN B 312 4116 5052 3681 498 -313 376 C ATOM 4888 O GLN B 312 -20.092 41.444 17.244 1.00 31.75 O ANISOU 4888 O GLN B 312 3840 4810 3414 555 -296 441 O ATOM 4889 CB GLN B 312 -19.697 38.426 15.906 1.00 34.82 C ANISOU 4889 CB GLN B 312 4219 5325 3685 488 -385 273 C ATOM 4890 CG GLN B 312 -21.111 38.800 15.521 1.00 39.87 C ANISOU 4890 CG GLN B 312 4812 6054 4282 533 -418 285 C ATOM 4891 CD GLN B 312 -21.902 37.593 15.061 1.00 49.69 C ANISOU 4891 CD GLN B 312 6019 7388 5474 509 -478 196 C ATOM 4892 OE1 GLN B 312 -22.118 36.651 15.826 1.00 54.42 O ANISOU 4892 OE1 GLN B 312 6610 7952 6114 440 -500 122 O ATOM 4893 NE2 GLN B 312 -22.314 37.601 13.796 1.00 50.39 N ANISOU 4893 NE2 GLN B 312 6083 7592 5472 566 -504 202 N ATOM 4894 N PHE B 313 -19.470 39.835 18.684 1.00 33.06 N ANISOU 4894 N PHE B 313 4026 4887 3648 430 -320 323 N ATOM 4895 CA PHE B 313 -20.092 40.536 19.800 1.00 32.58 C ANISOU 4895 CA PHE B 313 3957 4772 3650 420 -308 340 C ATOM 4896 C PHE B 313 -19.392 41.860 20.085 1.00 30.33 C ANISOU 4896 C PHE B 313 3698 4412 3414 448 -249 414 C ATOM 4897 O PHE B 313 -20.056 42.886 20.299 1.00 29.71 O ANISOU 4897 O PHE B 313 3606 4326 3356 485 -231 463 O ATOM 4898 CB PHE B 313 -20.097 39.665 21.055 1.00 29.07 C ANISOU 4898 CB PHE B 313 3517 4269 3258 344 -323 270 C ATOM 4899 CG PHE B 313 -20.741 40.344 22.233 1.00 27.44 C ANISOU 4899 CG PHE B 313 3303 4010 3112 334 -310 283 C ATOM 4900 CD1 PHE B 313 -22.121 40.499 22.278 1.00 35.69 C ANISOU 4900 CD1 PHE B 313 4308 5107 4144 352 -335 280 C ATOM 4901 CD2 PHE B 313 -19.972 40.856 23.255 1.00 27.32 C ANISOU 4901 CD2 PHE B 313 3318 3900 3164 308 -274 296 C ATOM 4902 CE1 PHE B 313 -22.734 41.146 23.360 1.00 36.88 C ANISOU 4902 CE1 PHE B 313 4452 5210 4350 346 -320 293 C ATOM 4903 CE2 PHE B 313 -20.576 41.510 24.327 1.00 32.07 C ANISOU 4903 CE2 PHE B 313 3912 4455 3817 301 -260 305 C ATOM 4904 CZ PHE B 313 -21.946 41.653 24.376 1.00 30.80 C ANISOU 4904 CZ PHE B 313 3715 4343 3645 320 -282 305 C ATOM 4905 N ARG B 314 -18.052 41.855 20.096 1.00 31.79 N ANISOU 4905 N ARG B 314 3917 4538 3622 430 -217 422 N ATOM 4906 CA ARG B 314 -17.303 43.088 20.340 1.00 35.89 C ANISOU 4906 CA ARG B 314 4459 4982 4196 451 -158 487 C ATOM 4907 C ARG B 314 -17.672 44.166 19.319 1.00 35.55 C ANISOU 4907 C ARG B 314 4405 4983 4118 534 -131 571 C ATOM 4908 O ARG B 314 -17.933 45.320 19.685 1.00 37.17 O ANISOU 4908 O ARG B 314 4609 5145 4368 562 -93 624 O ATOM 4909 CB ARG B 314 -15.797 42.783 20.319 1.00 33.88 C ANISOU 4909 CB ARG B 314 4236 4674 3963 422 -133 479 C ATOM 4910 CG ARG B 314 -14.886 43.982 20.461 1.00 45.16 C ANISOU 4910 CG ARG B 314 5684 6024 5449 439 -70 540 C ATOM 4911 CD ARG B 314 -13.436 43.563 20.753 1.00 37.47 C ANISOU 4911 CD ARG B 314 4737 4989 4510 394 -51 514 C ATOM 4912 NE ARG B 314 -12.782 42.934 19.612 1.00 39.14 N ANISOU 4912 NE ARG B 314 4958 5250 4664 411 -54 517 N ATOM 4913 CZ ARG B 314 -12.496 41.641 19.532 1.00 39.94 C ANISOU 4913 CZ ARG B 314 5064 5378 4735 374 -91 455 C ATOM 4914 NH1 ARG B 314 -12.795 40.798 20.512 1.00 36.45 N ANISOU 4914 NH1 ARG B 314 4617 4918 4313 318 -127 389 N ATOM 4915 NH2 ARG B 314 -11.894 41.178 18.446 1.00 40.35 N ANISOU 4915 NH2 ARG B 314 5124 5473 4733 394 -87 461 N ATOM 4916 N ASN B 315 -17.741 43.800 18.035 1.00 35.15 N ANISOU 4916 N ASN B 315 4348 5023 3986 576 -148 584 N ATOM 4917 CA ASN B 315 -18.116 44.777 17.013 1.00 35.04 C ANISOU 4917 CA ASN B 315 4322 5061 3928 662 -123 669 C ATOM 4918 C ASN B 315 -19.549 45.267 17.186 1.00 41.20 C ANISOU 4918 C ASN B 315 5068 5885 4700 696 -143 686 C ATOM 4919 O ASN B 315 -19.826 46.462 17.000 1.00 38.62 O ANISOU 4919 O ASN B 315 4737 5547 4389 756 -102 765 O ATOM 4920 CB ASN B 315 -17.910 44.184 15.621 1.00 39.26 C ANISOU 4920 CB ASN B 315 4856 5694 4368 700 -142 671 C ATOM 4921 CG ASN B 315 -16.444 43.992 15.296 1.00 43.51 C ANISOU 4921 CG ASN B 315 5429 6186 4915 684 -107 677 C ATOM 4922 OD1 ASN B 315 -15.568 44.413 16.059 1.00 49.19 O ANISOU 4922 OD1 ASN B 315 6173 6803 5715 650 -65 687 O ATOM 4923 ND2 ASN B 315 -16.165 43.360 14.165 1.00 51.38 N ANISOU 4923 ND2 ASN B 315 6428 7262 5831 709 -123 669 N ATOM 4924 N CYS B 316 -20.480 44.370 17.532 1.00 39.20 N ANISOU 4924 N CYS B 316 4787 5681 4427 662 -202 615 N ATOM 4925 CA CYS B 316 -21.850 44.806 17.799 1.00 37.27 C ANISOU 4925 CA CYS B 316 4505 5474 4182 689 -221 627 C ATOM 4926 C CYS B 316 -21.904 45.777 18.970 1.00 36.35 C ANISOU 4926 C CYS B 316 4399 5256 4157 676 -178 656 C ATOM 4927 O CYS B 316 -22.689 46.729 18.958 1.00 39.62 O ANISOU 4927 O CYS B 316 4794 5680 4581 728 -160 712 O ATOM 4928 CB CYS B 316 -22.766 43.611 18.083 1.00 39.41 C ANISOU 4928 CB CYS B 316 4743 5802 4428 643 -288 538 C ATOM 4929 SG CYS B 316 -23.149 42.566 16.667 1.00 47.58 S ANISOU 4929 SG CYS B 316 5749 6979 5350 667 -347 497 S ATOM 4930 N MET B 317 -21.103 45.533 20.009 1.00 34.01 N ANISOU 4930 N MET B 317 4130 4864 3928 609 -162 616 N ATOM 4931 CA MET B 317 -21.111 46.429 21.157 1.00 37.40 C ANISOU 4931 CA MET B 317 4569 5198 4442 594 -123 634 C ATOM 4932 C MET B 317 -20.584 47.814 20.791 1.00 39.65 C ANISOU 4932 C MET B 317 4871 5434 4760 649 -55 723 C ATOM 4933 O MET B 317 -21.147 48.832 21.217 1.00 39.15 O ANISOU 4933 O MET B 317 4799 5335 4740 678 -24 764 O ATOM 4934 CB MET B 317 -20.290 45.836 22.302 1.00 34.10 C ANISOU 4934 CB MET B 317 4176 4697 4081 513 -123 570 C ATOM 4935 CG MET B 317 -20.305 46.714 23.550 1.00 43.48 C ANISOU 4935 CG MET B 317 5373 5792 5354 494 -86 577 C ATOM 4936 SD MET B 317 -19.422 45.953 24.916 1.00 57.44 S ANISOU 4936 SD MET B 317 7168 7481 7177 404 -94 499 S ATOM 4937 CE MET B 317 -17.829 45.779 24.138 1.00 54.76 C ANISOU 4937 CE MET B 317 6857 7121 6828 401 -70 514 C ATOM 4938 N VAL B 318 -19.494 47.870 20.024 1.00 40.29 N ANISOU 4938 N VAL B 318 4976 5508 4825 664 -27 752 N ATOM 4939 CA VAL B 318 -18.948 49.154 19.591 1.00 42.63 C ANISOU 4939 CA VAL B 318 5288 5756 5155 717 44 840 C ATOM 4940 C VAL B 318 -19.964 49.890 18.733 1.00 49.93 C ANISOU 4940 C VAL B 318 6187 6752 6033 806 52 916 C ATOM 4941 O VAL B 318 -20.150 51.105 18.869 1.00 50.07 O ANISOU 4941 O VAL B 318 6204 6720 6100 848 106 983 O ATOM 4942 CB VAL B 318 -17.619 48.949 18.843 1.00 44.96 C ANISOU 4942 CB VAL B 318 5609 6040 5434 717 70 857 C ATOM 4943 CG1 VAL B 318 -17.228 50.223 18.109 1.00 52.02 C ANISOU 4943 CG1 VAL B 318 6513 6907 6345 788 143 959 C ATOM 4944 CG2 VAL B 318 -16.536 48.516 19.807 1.00 42.32 C ANISOU 4944 CG2 VAL B 318 5299 5618 5164 637 76 796 C ATOM 4945 N THR B 319 -20.647 49.160 17.845 1.00 42.70 N ANISOU 4945 N THR B 319 5247 5954 5023 836 -2 904 N ATOM 4946 CA THR B 319 -21.698 49.756 17.024 1.00 46.72 C ANISOU 4946 CA THR B 319 5725 6549 5477 922 -5 970 C ATOM 4947 C THR B 319 -22.823 50.325 17.885 1.00 46.90 C ANISOU 4947 C THR B 319 5723 6551 5547 927 -7 973 C ATOM 4948 O THR B 319 -23.282 51.451 17.662 1.00 56.96 O ANISOU 4948 O THR B 319 6988 7818 6836 996 36 1054 O ATOM 4949 CB THR B 319 -22.238 48.710 16.045 1.00 48.04 C ANISOU 4949 CB THR B 319 5866 6852 5535 940 -74 934 C ATOM 4950 OG1 THR B 319 -21.220 48.379 15.095 1.00 52.72 O ANISOU 4950 OG1 THR B 319 6484 7470 6080 954 -62 947 O ATOM 4951 CG2 THR B 319 -23.463 49.230 15.306 1.00 57.87 C ANISOU 4951 CG2 THR B 319 7071 8198 6719 1027 -89 990 C ATOM 4952 N THR B 320 -23.286 49.557 18.869 1.00 44.41 N ANISOU 4952 N THR B 320 5396 6224 5254 858 -52 888 N ATOM 4953 CA THR B 320 -24.326 50.049 19.770 1.00 49.32 C ANISOU 4953 CA THR B 320 5994 6821 5923 857 -52 886 C ATOM 4954 C THR B 320 -23.834 51.240 20.586 1.00 56.99 C ANISOU 4954 C THR B 320 6992 7669 6992 856 21 927 C ATOM 4955 O THR B 320 -24.532 52.253 20.713 1.00 58.30 O ANISOU 4955 O THR B 320 7143 7820 7188 906 54 983 O ATOM 4956 CB THR B 320 -24.788 48.923 20.698 1.00 48.91 C ANISOU 4956 CB THR B 320 5929 6774 5880 778 -109 785 C ATOM 4957 OG1 THR B 320 -25.519 47.954 19.941 1.00 50.60 O ANISOU 4957 OG1 THR B 320 6108 7107 6009 787 -174 749 O ATOM 4958 CG2 THR B 320 -25.668 49.460 21.852 1.00 51.14 C ANISOU 4958 CG2 THR B 320 6196 7008 6226 767 -98 778 C ATOM 4959 N LEU B 321 -22.622 51.138 21.140 1.00 48.99 N ANISOU 4959 N LEU B 321 6015 6566 6032 798 47 898 N ATOM 4960 CA LEU B 321 -22.110 52.160 22.046 1.00 54.27 C ANISOU 4960 CA LEU B 321 6706 7114 6799 782 111 916 C ATOM 4961 C LEU B 321 -21.755 53.452 21.318 1.00 62.29 C ANISOU 4961 C LEU B 321 7732 8097 7839 855 185 1017 C ATOM 4962 O LEU B 321 -21.754 54.520 21.939 1.00 67.26 O ANISOU 4962 O LEU B 321 8368 8640 8548 863 242 1047 O ATOM 4963 CB LEU B 321 -20.888 51.612 22.791 1.00 54.82 C ANISOU 4963 CB LEU B 321 6807 7111 6913 701 113 852 C ATOM 4964 CG LEU B 321 -20.809 51.706 24.314 1.00 56.59 C ANISOU 4964 CG LEU B 321 7040 7247 7214 636 119 793 C ATOM 4965 CD1 LEU B 321 -22.150 51.353 24.920 1.00 58.48 C ANISOU 4965 CD1 LEU B 321 7252 7530 7440 630 76 758 C ATOM 4966 CD2 LEU B 321 -19.699 50.783 24.847 1.00 54.94 C ANISOU 4966 CD2 LEU B 321 6854 7004 7016 560 98 722 C ATOM 4967 N CYS B 322 -21.475 53.383 20.022 1.00 61.16 N ANISOU 4967 N CYS B 322 7590 8019 7629 908 189 1070 N ATOM 4968 CA CYS B 322 -21.089 54.559 19.248 1.00 67.77 C ANISOU 4968 CA CYS B 322 8438 8828 8485 982 265 1174 C ATOM 4969 C CYS B 322 -22.072 54.844 18.119 1.00 69.55 C ANISOU 4969 C CYS B 322 8635 9162 8629 1079 255 1249 C ATOM 4970 O CYS B 322 -21.667 55.051 16.975 1.00 75.57 O ANISOU 4970 O CYS B 322 9404 9967 9342 1139 280 1316 O ATOM 4971 CB CYS B 322 -19.683 54.375 18.684 1.00 62.15 C ANISOU 4971 CB CYS B 322 7756 8087 7771 967 294 1183 C ATOM 4972 SG CYS B 322 -18.474 53.898 19.946 1.00 77.60 S ANISOU 4972 SG CYS B 322 9741 9934 9812 854 295 1090 S TER 4973 CYS B 322 HETATM 4974 C1 NAG C 1 10.606 21.922 0.403 1.00 32.60 C ANISOU 4974 C1 NAG C 1 4508 4830 3049 538 443 -136 C HETATM 4975 C2 NAG C 1 9.130 22.021 0.777 1.00 32.93 C ANISOU 4975 C2 NAG C 1 4539 4907 3066 518 375 -171 C HETATM 4976 C3 NAG C 1 8.302 20.992 0.006 1.00 35.79 C ANISOU 4976 C3 NAG C 1 4907 5348 3344 520 339 -274 C HETATM 4977 C4 NAG C 1 8.572 21.059 -1.491 1.00 32.94 C ANISOU 4977 C4 NAG C 1 4561 5081 2872 585 372 -271 C HETATM 4978 C5 NAG C 1 10.076 20.961 -1.739 1.00 32.73 C ANISOU 4978 C5 NAG C 1 4548 5006 2880 602 443 -232 C HETATM 4979 C6 NAG C 1 10.464 21.110 -3.195 1.00 35.91 C ANISOU 4979 C6 NAG C 1 4969 5499 3177 671 485 -216 C HETATM 4980 C7 NAG C 1 8.304 22.728 2.964 1.00 36.66 C ANISOU 4980 C7 NAG C 1 4983 5276 3670 444 316 -138 C HETATM 4981 C8 NAG C 1 8.143 22.368 4.414 1.00 32.33 C ANISOU 4981 C8 NAG C 1 4422 4642 3219 382 286 -161 C HETATM 4982 N2 NAG C 1 8.940 21.836 2.205 1.00 29.35 N ANISOU 4982 N2 NAG C 1 4072 4368 2713 457 344 -183 N HETATM 4983 O3 NAG C 1 6.928 21.236 0.290 1.00 39.88 O ANISOU 4983 O3 NAG C 1 5410 5906 3836 506 278 -297 O HETATM 4984 O4 NAG C 1 7.944 19.946 -2.121 1.00 37.52 O ANISOU 4984 O4 NAG C 1 5145 5725 3386 578 341 -383 O HETATM 4985 O5 NAG C 1 10.750 22.001 -1.020 1.00 32.55 O ANISOU 4985 O5 NAG C 1 4517 4912 2937 600 474 -130 O HETATM 4986 O6 NAG C 1 9.977 22.339 -3.720 1.00 35.64 O ANISOU 4986 O6 NAG C 1 4933 5533 3077 725 487 -136 O HETATM 4987 O7 NAG C 1 7.879 23.777 2.504 1.00 35.05 O ANISOU 4987 O7 NAG C 1 4777 5122 3420 483 318 -79 O HETATM 4988 C1 NAG C 2 7.047 20.316 -3.193 1.00 39.21 C ANISOU 4988 C1 NAG C 2 5357 6065 3475 629 315 -393 C HETATM 4989 C2 NAG C 2 6.745 19.060 -4.008 1.00 40.21 C ANISOU 4989 C2 NAG C 2 5490 6256 3533 626 298 -517 C HETATM 4990 C3 NAG C 2 5.738 19.368 -5.111 1.00 45.31 C ANISOU 4990 C3 NAG C 2 6129 7044 4042 678 262 -541 C HETATM 4991 C4 NAG C 2 4.494 20.023 -4.531 1.00 48.26 C ANISOU 4991 C4 NAG C 2 6478 7440 4420 664 202 -522 C HETATM 4992 C5 NAG C 2 4.892 21.248 -3.710 1.00 47.32 C ANISOU 4992 C5 NAG C 2 6358 7245 4376 669 228 -394 C HETATM 4993 C6 NAG C 2 3.723 21.890 -3.005 1.00 55.56 C ANISOU 4993 C6 NAG C 2 7378 8295 5439 651 174 -374 C HETATM 4994 C7 NAG C 2 8.536 17.393 -4.085 1.00 43.16 C ANISOU 4994 C7 NAG C 2 5891 6528 3980 595 373 -591 C HETATM 4995 C8 NAG C 2 9.779 16.941 -4.782 1.00 42.28 C ANISOU 4995 C8 NAG C 2 5800 6407 3856 624 439 -592 C HETATM 4996 N2 NAG C 2 7.958 18.493 -4.575 1.00 38.95 N ANISOU 4996 N2 NAG C 2 5352 6077 3371 644 358 -527 N HETATM 4997 O3 NAG C 2 5.398 18.143 -5.749 1.00 46.97 O ANISOU 4997 O3 NAG C 2 6340 7308 4198 664 240 -670 O HETATM 4998 O4 NAG C 2 3.601 20.397 -5.577 1.00 55.00 O ANISOU 4998 O4 NAG C 2 7323 8432 5144 721 170 -533 O HETATM 4999 O5 NAG C 2 5.827 20.865 -2.689 1.00 41.65 O ANISOU 4999 O5 NAG C 2 5646 6397 3782 616 258 -385 O HETATM 5000 O6 NAG C 2 3.242 21.063 -1.955 1.00 64.69 O ANISOU 5000 O6 NAG C 2 8520 9381 6677 574 134 -450 O HETATM 5001 O7 NAG C 2 8.082 16.799 -3.107 1.00 48.51 O ANISOU 5001 O7 NAG C 2 6557 7141 4735 533 339 -641 O HETATM 5002 C1 NAG D 1 -20.017 34.736 75.170 1.00 35.24 C ANISOU 5002 C1 NAG D 1 4805 5145 3440 518 139 -244 C HETATM 5003 C2 NAG D 1 -21.506 34.661 74.777 1.00 34.80 C ANISOU 5003 C2 NAG D 1 4750 5023 3451 497 198 -203 C HETATM 5004 C3 NAG D 1 -22.320 35.724 75.513 1.00 38.50 C ANISOU 5004 C3 NAG D 1 5222 5509 3898 509 220 -255 C HETATM 5005 C4 NAG D 1 -22.053 35.702 77.013 1.00 35.38 C ANISOU 5005 C4 NAG D 1 4845 5211 3387 575 228 -268 C HETATM 5006 C5 NAG D 1 -20.554 35.811 77.265 1.00 31.40 C ANISOU 5006 C5 NAG D 1 4337 4770 2825 589 163 -315 C HETATM 5007 C6 NAG D 1 -20.180 35.755 78.730 1.00 37.90 C ANISOU 5007 C6 NAG D 1 5176 5702 3524 658 163 -331 C HETATM 5008 C7 NAG D 1 -22.288 33.904 72.574 1.00 37.72 C ANISOU 5008 C7 NAG D 1 5097 5251 3984 414 215 -136 C HETATM 5009 C8 NAG D 1 -22.426 34.244 71.110 1.00 35.01 C ANISOU 5009 C8 NAG D 1 4732 4832 3736 352 194 -150 C HETATM 5010 N2 NAG D 1 -21.684 34.818 73.339 1.00 31.97 N ANISOU 5010 N2 NAG D 1 4373 4580 3196 435 184 -204 N HETATM 5011 O3 NAG D 1 -23.699 35.485 75.262 1.00 42.04 O ANISOU 5011 O3 NAG D 1 5669 5905 4400 497 279 -207 O HETATM 5012 O4 NAG D 1 -22.697 36.820 77.613 1.00 41.99 O ANISOU 5012 O4 NAG D 1 5683 6062 4208 580 243 -331 O HETATM 5013 O5 NAG D 1 -19.889 34.716 76.617 1.00 37.67 O ANISOU 5013 O5 NAG D 1 5129 5546 3639 583 149 -252 O HETATM 5014 O6 NAG D 1 -20.667 34.564 79.333 1.00 38.62 O ANISOU 5014 O6 NAG D 1 5287 5817 3569 709 217 -233 O HETATM 5015 O7 NAG D 1 -22.688 32.846 73.033 1.00 39.91 O ANISOU 5015 O7 NAG D 1 5387 5537 4238 444 259 -67 O HETATM 5016 C1 NAG D 2 -23.638 36.426 78.634 1.00 46.23 C ANISOU 5016 C1 NAG D 2 6240 6635 4692 630 305 -286 C HETATM 5017 C2 NAG D 2 -23.973 37.671 79.456 1.00 49.40 C ANISOU 5017 C2 NAG D 2 6643 7073 5052 645 309 -371 C HETATM 5018 C3 NAG D 2 -25.051 37.360 80.491 1.00 56.82 C ANISOU 5018 C3 NAG D 2 7602 8046 5939 696 379 -326 C HETATM 5019 C4 NAG D 2 -26.256 36.708 79.831 1.00 64.42 C ANISOU 5019 C4 NAG D 2 8560 8930 6985 673 438 -243 C HETATM 5020 C5 NAG D 2 -25.810 35.496 79.022 1.00 59.14 C ANISOU 5020 C5 NAG D 2 7887 8226 6356 656 429 -168 C HETATM 5021 C6 NAG D 2 -26.938 34.866 78.243 1.00 68.23 C ANISOU 5021 C6 NAG D 2 9027 9296 7599 624 480 -98 C HETATM 5022 C7 NAG D 2 -22.160 39.305 79.695 1.00 50.47 C ANISOU 5022 C7 NAG D 2 6761 7273 5144 627 202 -544 C HETATM 5023 C8 NAG D 2 -20.960 39.718 80.498 1.00 52.97 C ANISOU 5023 C8 NAG D 2 7074 7680 5372 654 148 -623 C HETATM 5024 N2 NAG D 2 -22.788 38.202 80.108 1.00 47.27 N ANISOU 5024 N2 NAG D 2 6373 6882 4704 667 253 -449 N HETATM 5025 O3 NAG D 2 -25.452 38.577 81.110 1.00 59.22 O ANISOU 5025 O3 NAG D 2 7908 8373 6221 704 385 -408 O HETATM 5026 O4 NAG D 2 -27.195 36.313 80.826 1.00 66.25 O ANISOU 5026 O4 NAG D 2 8809 9194 7167 723 507 -195 O HETATM 5027 O5 NAG D 2 -24.824 35.899 78.061 1.00 51.74 O ANISOU 5027 O5 NAG D 2 6934 7262 5463 609 360 -217 O HETATM 5028 O6 NAG D 2 -27.523 35.808 77.355 1.00 74.59 O ANISOU 5028 O6 NAG D 2 9812 10037 8493 570 470 -144 O HETATM 5029 O7 NAG D 2 -22.540 39.939 78.714 1.00 57.51 O ANISOU 5029 O7 NAG D 2 7638 8082 6134 573 202 -565 O HETATM 5030 C ACE A 401 17.543 34.882 4.959 1.00 77.70 C ANISOU 5030 C ACE A 401 10020 9899 9603 540 917 747 C HETATM 5031 O ACE A 401 18.520 34.368 5.498 1.00 83.34 O ANISOU 5031 O ACE A 401 10713 10568 10382 504 920 715 O HETATM 5032 CH3 ACE A 401 17.718 36.004 3.982 1.00 77.76 C ANISOU 5032 CH3 ACE A 401 10032 9915 9598 596 997 842 C HETATM 5033 C1 RET A 402 10.837 31.682 30.520 1.00 24.34 C ANISOU 5033 C1 RET A 402 3050 2790 3406 -138 -46 -4 C HETATM 5034 C2 RET A 402 11.799 32.136 31.654 1.00 27.85 C ANISOU 5034 C2 RET A 402 3456 3228 3896 -152 -60 -27 C HETATM 5035 C3 RET A 402 12.011 31.198 32.829 1.00 30.15 C ANISOU 5035 C3 RET A 402 3742 3540 4175 -150 -95 -49 C HETATM 5036 C4 RET A 402 10.740 30.483 33.225 1.00 24.22 C ANISOU 5036 C4 RET A 402 3024 2802 3377 -146 -118 -52 C HETATM 5037 C5 RET A 402 10.027 29.869 32.070 1.00 23.50 C ANISOU 5037 C5 RET A 402 2967 2712 3251 -136 -101 -34 C HETATM 5038 C6 RET A 402 10.109 30.377 30.829 1.00 20.80 C ANISOU 5038 C6 RET A 402 2630 2361 2912 -132 -71 -14 C HETATM 5039 C7 RET A 402 9.361 29.837 29.708 1.00 24.71 C ANISOU 5039 C7 RET A 402 3156 2866 3368 -120 -59 -2 C HETATM 5040 C8 RET A 402 9.502 28.566 29.255 1.00 23.53 C ANISOU 5040 C8 RET A 402 3023 2725 3194 -110 -55 -5 C HETATM 5041 C9 RET A 402 8.784 27.909 28.184 1.00 23.39 C ANISOU 5041 C9 RET A 402 3032 2720 3134 -101 -46 -4 C HETATM 5042 C10 RET A 402 8.906 26.566 28.027 1.00 21.89 C ANISOU 5042 C10 RET A 402 2856 2534 2928 -95 -45 -16 C HETATM 5043 C11 RET A 402 8.242 25.744 27.054 1.00 25.08 C ANISOU 5043 C11 RET A 402 3286 2952 3294 -88 -37 -27 C HETATM 5044 C12 RET A 402 8.493 24.466 26.678 1.00 22.47 C ANISOU 5044 C12 RET A 402 2968 2619 2952 -82 -27 -42 C HETATM 5045 C13 RET A 402 9.587 23.560 27.013 1.00 21.63 C ANISOU 5045 C13 RET A 402 2855 2496 2868 -75 -16 -43 C HETATM 5046 C14 RET A 402 9.490 22.259 26.646 1.00 20.61 C ANISOU 5046 C14 RET A 402 2743 2362 2726 -70 -5 -62 C HETATM 5047 C15 RET A 402 10.448 21.264 26.833 1.00 20.75 C ANISOU 5047 C15 RET A 402 2758 2363 2764 -59 11 -63 C HETATM 5048 C16 RET A 402 11.642 31.524 29.229 1.00 28.33 C ANISOU 5048 C16 RET A 402 3556 3292 3916 -124 -8 19 C HETATM 5049 C17 RET A 402 9.822 32.824 30.332 1.00 28.36 C ANISOU 5049 C17 RET A 402 3569 3291 3917 -143 -39 6 C HETATM 5050 C18 RET A 402 9.182 28.685 32.461 1.00 23.45 C ANISOU 5050 C18 RET A 402 2986 2716 3206 -131 -120 -40 C HETATM 5051 C19 RET A 402 7.923 28.757 27.287 1.00 23.70 C ANISOU 5051 C19 RET A 402 3082 2771 3152 -96 -36 11 C HETATM 5052 C20 RET A 402 10.812 24.116 27.691 1.00 21.03 C ANISOU 5052 C20 RET A 402 2749 2410 2832 -72 -14 -26 C HETATM 5053 C1 NAG A 403 21.122 33.954 7.223 1.00 43.57 C ANISOU 5053 C1 NAG A 403 5598 5391 5564 410 946 669 C HETATM 5054 C2 NAG A 403 20.802 35.370 7.710 1.00 55.17 C ANISOU 5054 C2 NAG A 403 7048 6817 7098 398 962 715 C HETATM 5055 C3 NAG A 403 21.781 36.368 7.094 1.00 54.78 C ANISOU 5055 C3 NAG A 403 6977 6729 7108 419 1058 788 C HETATM 5056 C4 NAG A 403 23.210 35.957 7.417 1.00 59.22 C ANISOU 5056 C4 NAG A 403 7502 7250 7748 392 1084 768 C HETATM 5057 C5 NAG A 403 23.451 34.523 6.946 1.00 61.06 C ANISOU 5057 C5 NAG A 403 7757 7533 7910 407 1062 724 C HETATM 5058 C6 NAG A 403 24.825 33.997 7.301 1.00 60.02 C ANISOU 5058 C6 NAG A 403 7589 7366 7852 382 1082 701 C HETATM 5059 C7 NAG A 403 18.680 36.434 8.289 1.00 54.22 C ANISOU 5059 C7 NAG A 403 6950 6711 6941 396 900 727 C HETATM 5060 C8 NAG A 403 17.286 36.750 7.847 1.00 49.11 C ANISOU 5060 C8 NAG A 403 6333 6116 6210 430 875 746 C HETATM 5061 N2 NAG A 403 19.431 35.750 7.420 1.00 50.11 N ANISOU 5061 N2 NAG A 403 6438 6218 6384 423 935 731 N HETATM 5062 O3 NAG A 403 21.521 37.672 7.598 1.00 58.95 O ANISOU 5062 O3 NAG A 403 7486 7207 7706 404 1077 825 O HETATM 5063 O4 NAG A 403 24.134 36.837 6.785 1.00 59.68 O ANISOU 5063 O4 NAG A 403 7538 7274 7864 412 1178 835 O HETATM 5064 O5 NAG A 403 22.492 33.635 7.548 1.00 52.42 O ANISOU 5064 O5 NAG A 403 6685 6469 6763 387 974 658 O HETATM 5065 O6 NAG A 403 25.060 34.056 8.702 1.00 66.06 O ANISOU 5065 O6 NAG A 403 8314 8082 8702 325 1035 659 O HETATM 5066 O7 NAG A 403 19.109 36.777 9.391 1.00 54.39 O ANISOU 5066 O7 NAG A 403 6937 6671 7056 348 888 706 O HETATM 5067 O1 DAO A 404 22.952 24.838 22.274 1.00 50.96 O ANISOU 5067 O1 DAO A 404 6328 6150 6884 50 309 114 O HETATM 5068 O2 DAO A 404 23.337 26.922 22.942 1.00 57.98 O ANISOU 5068 O2 DAO A 404 7161 7024 7845 16 306 126 O HETATM 5069 C1 DAO A 404 23.372 25.681 23.087 1.00 56.07 C ANISOU 5069 C1 DAO A 404 6935 6792 7579 32 293 114 C HETATM 5070 C2 DAO A 404 23.995 25.168 24.398 1.00 51.64 C ANISOU 5070 C2 DAO A 404 6338 6235 7049 29 257 97 C HETATM 5071 C3 DAO A 404 23.358 25.673 25.682 1.00 48.72 C ANISOU 5071 C3 DAO A 404 5958 5871 6684 7 205 78 C HETATM 5072 C4 DAO A 404 23.695 24.799 26.879 1.00 42.85 C ANISOU 5072 C4 DAO A 404 5195 5140 5944 16 167 64 C HETATM 5073 C5 DAO A 404 22.474 24.410 27.688 1.00 40.37 C ANISOU 5073 C5 DAO A 404 4916 4835 5590 10 125 50 C HETATM 5074 C6 DAO A 404 22.691 23.149 28.507 1.00 43.47 C ANISOU 5074 C6 DAO A 404 5308 5238 5972 32 104 46 C HETATM 5075 C7 DAO A 404 23.712 23.259 29.629 1.00 55.13 C ANISOU 5075 C7 DAO A 404 6728 6734 7485 38 78 41 C HETATM 5076 C8 DAO A 404 24.200 21.890 30.097 1.00 52.71 C ANISOU 5076 C8 DAO A 404 6421 6436 7171 71 74 50 C HETATM 5077 C9 DAO A 404 24.890 21.916 31.455 1.00 52.67 C ANISOU 5077 C9 DAO A 404 6365 6462 7184 82 36 44 C HETATM 5078 C10 DAO A 404 25.451 20.552 31.834 1.00 65.19 C ANISOU 5078 C10 DAO A 404 7949 8056 8765 122 39 62 C HETATM 5079 C11 DAO A 404 25.545 20.330 33.336 1.00 54.47 C ANISOU 5079 C11 DAO A 404 6564 6734 7396 140 -8 60 C HETATM 5080 C18 OLC A 405 23.680 31.629 38.238 1.00 54.54 C ANISOU 5080 C18 OLC A 405 6345 6804 7573 -153 -214 -250 C HETATM 5081 C10 OLC A 405 24.670 30.655 29.221 1.00 74.04 C ANISOU 5081 C10 OLC A 405 8964 9064 10104 -109 131 -2 C HETATM 5082 C9 OLC A 405 23.551 31.141 28.749 1.00 72.34 C ANISOU 5082 C9 OLC A 405 8793 8832 9862 -116 141 11 C HETATM 5083 C17 OLC A 405 24.042 30.358 37.511 1.00 54.10 C ANISOU 5083 C17 OLC A 405 6312 6748 7494 -119 -193 -203 C HETATM 5084 C11 OLC A 405 25.095 30.743 30.652 1.00 67.18 C ANISOU 5084 C11 OLC A 405 8049 8222 9256 -120 80 -42 C HETATM 5085 C8 OLC A 405 23.023 30.934 27.365 1.00 61.68 C ANISOU 5085 C8 OLC A 405 7492 7469 8476 -98 184 48 C HETATM 5086 C24 OLC A 405 24.200 30.027 16.949 1.00 69.80 C ANISOU 5086 C24 OLC A 405 8697 8503 9319 92 582 297 C HETATM 5087 C16 OLC A 405 23.761 30.387 36.035 1.00 51.75 C ANISOU 5087 C16 OLC A 405 6054 6400 7210 -124 -138 -165 C HETATM 5088 C12 OLC A 405 24.177 30.003 31.570 1.00 64.52 C ANISOU 5088 C12 OLC A 405 7745 7912 8859 -109 30 -53 C HETATM 5089 C7 OLC A 405 23.039 32.184 26.550 1.00 60.52 C ANISOU 5089 C7 OLC A 405 7339 7291 8366 -110 232 69 C HETATM 5090 C15 OLC A 405 24.160 29.115 35.347 1.00 52.02 C ANISOU 5090 C15 OLC A 405 6108 6435 7222 -91 -117 -125 C HETATM 5091 C13 OLC A 405 24.606 30.008 33.024 1.00 59.49 C ANISOU 5091 C13 OLC A 405 7062 7310 8231 -113 -22 -90 C HETATM 5092 C6 OLC A 405 22.638 31.967 25.100 1.00 56.81 C ANISOU 5092 C6 OLC A 405 6914 6816 7854 -86 277 110 C HETATM 5093 C14 OLC A 405 23.811 29.067 33.885 1.00 56.38 C ANISOU 5093 C14 OLC A 405 6703 6945 7776 -92 -65 -91 C HETATM 5094 C5 OLC A 405 23.158 33.013 24.152 1.00 59.73 C ANISOU 5094 C5 OLC A 405 7267 7157 8270 -87 340 141 C HETATM 5095 C4 OLC A 405 23.062 32.582 22.720 1.00 58.21 C ANISOU 5095 C4 OLC A 405 7113 6971 8033 -55 385 180 C HETATM 5096 C3 OLC A 405 24.044 33.238 21.767 1.00 54.80 C ANISOU 5096 C3 OLC A 405 6655 6516 7649 -48 454 214 C HETATM 5097 C2 OLC A 405 24.372 32.300 20.662 1.00 60.76 C ANISOU 5097 C2 OLC A 405 7437 7290 8360 -14 486 237 C HETATM 5098 C21 OLC A 405 25.154 32.353 17.185 1.00 71.24 C ANISOU 5098 C21 OLC A 405 8809 8626 9633 63 644 342 C HETATM 5099 C1 OLC A 405 25.077 32.903 19.490 1.00 65.29 C ANISOU 5099 C1 OLC A 405 8001 7847 8961 2 561 281 C HETATM 5100 C22 OLC A 405 25.123 31.079 16.371 1.00 80.64 C ANISOU 5100 C22 OLC A 405 10038 9851 10752 96 648 339 C HETATM 5101 O19 OLC A 405 25.439 34.045 19.379 1.00 67.32 O ANISOU 5101 O19 OLC A 405 8228 8072 9278 -11 601 301 O HETATM 5102 O25 OLC A 405 24.182 28.849 16.149 1.00 71.34 O ANISOU 5102 O25 OLC A 405 8927 8726 9452 121 591 290 O HETATM 5103 O23 OLC A 405 24.744 31.374 15.028 1.00 89.89 O ANISOU 5103 O23 OLC A 405 11245 11039 11871 130 697 380 O HETATM 5104 O20 OLC A 405 25.288 31.968 18.569 1.00 71.50 O ANISOU 5104 O20 OLC A 405 8814 8655 9697 33 583 294 O HETATM 5105 C10 OLC A 406 -3.536 22.679 43.366 1.00 54.09 C ANISOU 5105 C10 OLC A 406 7020 6627 6906 -134 -185 -45 C HETATM 5106 C9 OLC A 406 -3.025 22.168 44.451 1.00 53.96 C ANISOU 5106 C9 OLC A 406 7007 6617 6877 -108 -179 -24 C HETATM 5107 C11 OLC A 406 -4.441 21.866 42.497 1.00 54.33 C ANISOU 5107 C11 OLC A 406 7058 6632 6955 -154 -164 -52 C HETATM 5108 C8 OLC A 406 -2.283 22.830 45.566 1.00 49.92 C ANISOU 5108 C8 OLC A 406 6486 6139 6341 -85 -200 -20 C HETATM 5109 C12 OLC A 406 -4.947 22.584 41.289 1.00 45.48 C ANISOU 5109 C12 OLC A 406 5929 5514 5837 -176 -176 -75 C HETATM 5110 C7 OLC A 406 -2.428 22.036 46.818 1.00 59.57 C ANISOU 5110 C7 OLC A 406 7719 7370 7546 -57 -185 8 C HETATM 5111 C15 OLC A 406 -7.272 21.499 38.361 1.00 63.44 C ANISOU 5111 C15 OLC A 406 8195 7774 8136 -234 -160 -135 C HETATM 5112 C13 OLC A 406 -5.836 21.707 40.429 1.00 55.43 C ANISOU 5112 C13 OLC A 406 7192 6756 7113 -197 -159 -90 C HETATM 5113 C6 OLC A 406 -2.481 22.855 48.098 1.00 63.16 C ANISOU 5113 C6 OLC A 406 8166 7863 7968 -39 -204 4 C HETATM 5114 C14 OLC A 406 -6.375 22.378 39.198 1.00 62.85 C ANISOU 5114 C14 OLC A 406 8122 7710 8049 -214 -173 -112 C HETATM 5115 C5 OLC A 406 -3.717 22.575 48.919 1.00 64.25 C ANISOU 5115 C5 OLC A 406 8317 7999 8094 -34 -183 19 C HETATM 5116 C4 OLC A 406 -3.594 22.915 50.377 1.00 61.66 C ANISOU 5116 C4 OLC A 406 7989 7714 7727 -3 -193 26 C HETATM 5117 C3 OLC A 406 -3.297 21.716 51.254 1.00 67.82 C ANISOU 5117 C3 OLC A 406 8780 8501 8488 37 -169 69 C HETATM 5118 C2 OLC A 406 -4.515 20.888 51.505 1.00 66.79 C ANISOU 5118 C2 OLC A 406 8667 8342 8369 36 -127 96 C HETATM 5119 C1 OLC A 406 -4.209 19.549 52.108 1.00 77.95 C ANISOU 5119 C1 OLC A 406 10093 9748 9777 73 -92 145 C HETATM 5120 O19 OLC A 406 -3.658 18.652 51.530 1.00 87.66 O ANISOU 5120 O19 OLC A 406 11327 10950 11032 76 -74 162 O HETATM 5121 O20 OLC A 406 -4.612 19.469 53.373 1.00 76.80 O ANISOU 5121 O20 OLC A 406 9955 9630 9596 105 -79 171 O HETATM 5122 C10 OLC A 407 15.965 38.970 28.202 1.00 44.46 C ANISOU 5122 C10 OLC A 407 5405 5137 6352 -194 214 67 C HETATM 5123 C9 OLC A 407 15.396 40.069 28.607 1.00 42.08 C ANISOU 5123 C9 OLC A 407 5098 4807 6084 -208 222 60 C HETATM 5124 C11 OLC A 407 17.277 38.418 28.659 1.00 48.29 C ANISOU 5124 C11 OLC A 407 5850 5631 6867 -206 202 37 C HETATM 5125 C8 OLC A 407 14.096 40.590 28.076 1.00 46.52 C ANISOU 5125 C8 OLC A 407 5699 5362 6614 -190 237 95 C HETATM 5126 C12 OLC A 407 17.263 36.938 28.833 1.00 37.60 C ANISOU 5126 C12 OLC A 407 4516 4321 5450 -190 160 29 C HETATM 5127 C7 OLC A 407 13.901 42.058 28.302 1.00 48.45 C ANISOU 5127 C7 OLC A 407 5926 5558 6926 -205 272 96 C HETATM 5128 C13 OLC A 407 18.614 36.348 29.204 1.00 42.64 C ANISOU 5128 C13 OLC A 407 5113 4971 6117 -196 152 7 C HETATM 5129 C10 OLC A 408 19.614 15.842 25.400 1.00 55.41 C ANISOU 5129 C10 OLC A 408 7066 6658 7329 106 221 0 C HETATM 5130 C9 OLC A 408 20.365 14.967 24.764 1.00 56.86 C ANISOU 5130 C9 OLC A 408 7253 6826 7525 128 260 -1 C HETATM 5131 C11 OLC A 408 19.437 15.978 26.881 1.00 50.74 C ANISOU 5131 C11 OLC A 408 6456 6071 6750 104 182 14 C HETATM 5132 C8 OLC A 408 20.238 14.649 23.304 1.00 54.38 C ANISOU 5132 C8 OLC A 408 6967 6509 7187 130 297 -24 C HETATM 5133 C12 OLC A 408 20.103 17.185 27.468 1.00 42.57 C ANISOU 5133 C12 OLC A 408 5380 5060 5734 99 158 30 C HETATM 5134 C7 OLC A 408 21.387 15.118 22.463 1.00 62.42 C ANISOU 5134 C7 OLC A 408 7964 7537 8216 145 328 -9 C HETATM 5135 C13 OLC A 408 20.491 17.011 28.923 1.00 43.55 C ANISOU 5135 C13 OLC A 408 5476 5194 5876 112 128 46 C HETATM 5136 C6 OLC A 408 21.206 14.876 20.968 1.00 62.41 C ANISOU 5136 C6 OLC A 408 7991 7540 8180 149 364 -32 C HETATM 5137 C14 OLC A 408 21.763 17.723 29.314 1.00 48.48 C ANISOU 5137 C14 OLC A 408 6047 5839 6532 120 119 59 C HETATM 5138 C5 OLC A 408 22.390 15.283 20.117 1.00 56.87 C ANISOU 5138 C5 OLC A 408 7270 6848 7490 168 402 -14 C HETATM 5139 C10 OLC A 409 23.913 22.544 45.963 1.00 63.02 C ANISOU 5139 C10 OLC A 409 7460 8281 8204 244 -445 -71 C HETATM 5140 C9 OLC A 409 24.081 21.663 46.918 1.00 65.37 C ANISOU 5140 C9 OLC A 409 7753 8629 8455 302 -463 -39 C HETATM 5141 C11 OLC A 409 24.123 22.382 44.490 1.00 62.90 C ANISOU 5141 C11 OLC A 409 7462 8197 8239 221 -397 -55 C HETATM 5142 C8 OLC A 409 23.833 21.976 48.362 1.00 52.68 C ANISOU 5142 C8 OLC A 409 6128 7095 6792 323 -512 -60 C HETATM 5143 C12 OLC A 409 24.875 23.520 43.875 1.00 45.06 C ANISOU 5143 C12 OLC A 409 5155 5929 6037 177 -398 -100 C HETATM 5144 C7 OLC A 409 23.897 20.800 49.285 1.00 50.02 C ANISOU 5144 C7 OLC A 409 5800 6806 6400 396 -518 -7 C HETATM 5145 C13 OLC A 409 24.726 23.611 42.365 1.00 42.32 C ANISOU 5145 C13 OLC A 409 4840 5509 5733 145 -346 -87 C HETATM 5146 C6 OLC A 409 23.890 21.206 50.751 1.00 48.45 C ANISOU 5146 C6 OLC A 409 5570 6698 6142 423 -572 -33 C HETATM 5147 C5 OLC A 409 23.418 20.146 51.706 1.00 51.67 C ANISOU 5147 C5 OLC A 409 6009 7140 6483 490 -570 26 C HETATM 5148 C4 OLC A 409 23.161 20.667 53.097 1.00 46.45 C ANISOU 5148 C4 OLC A 409 5328 6564 5757 510 -620 -4 C HETATM 5149 C3 OLC A 409 22.487 19.674 54.024 1.00 57.65 C ANISOU 5149 C3 OLC A 409 6788 8009 7108 574 -609 59 C HETATM 5150 C2 OLC A 409 22.325 20.211 55.412 1.00 62.90 C ANISOU 5150 C2 OLC A 409 7429 8767 7702 599 -660 27 C HETATM 5151 C1 PLM A 410 12.725 2.210 54.004 1.00 73.01 C ANISOU 5151 C1 PLM A 410 9429 9011 9300 972 379 1007 C HETATM 5152 O2 PLM A 410 12.554 1.271 54.831 1.00 84.90 O ANISOU 5152 O2 PLM A 410 10953 10503 10804 1039 438 1091 O HETATM 5153 C2 PLM A 410 13.470 1.814 52.703 1.00 69.78 C ANISOU 5153 C2 PLM A 410 9014 8543 8958 945 395 976 C HETATM 5154 C3 PLM A 410 14.461 2.836 52.160 1.00 79.55 C ANISOU 5154 C3 PLM A 410 10210 9844 10171 920 316 914 C HETATM 5155 C4 PLM A 410 15.059 2.429 50.816 1.00 80.51 C ANISOU 5155 C4 PLM A 410 10330 9901 10360 890 340 882 C HETATM 5156 C5 PLM A 410 15.905 3.517 50.137 1.00 83.02 C ANISOU 5156 C5 PLM A 410 10610 10271 10663 852 268 815 C HETATM 5157 C6 PLM A 410 16.703 2.990 48.932 1.00 80.05 C ANISOU 5157 C6 PLM A 410 10229 9841 10347 842 297 799 C HETATM 5158 C7 PLM A 410 17.095 4.047 47.901 1.00 78.00 C ANISOU 5158 C7 PLM A 410 9946 9599 10091 777 244 719 C HETATM 5159 C8 PLM A 410 17.628 3.450 46.588 1.00 70.24 C ANISOU 5159 C8 PLM A 410 8968 8547 9171 758 285 698 C HETATM 5160 C9 PLM A 410 17.606 4.429 45.424 1.00 74.00 C ANISOU 5160 C9 PLM A 410 9438 9022 9658 682 248 617 C HETATM 5161 CA PLM A 410 18.291 3.911 44.151 1.00 70.26 C ANISOU 5161 CA PLM A 410 8965 8495 9237 671 283 597 C HETATM 5162 CB PLM A 410 18.117 4.856 42.937 1.00 76.38 C ANISOU 5162 CB PLM A 410 9738 9263 10019 596 254 519 C HETATM 5163 C8 OLC A 411 25.213 34.719 45.514 1.00 61.76 C ANISOU 5163 C8 OLC A 411 6981 8003 8481 -204 -488 -606 C HETATM 5164 C7 OLC A 411 24.989 34.140 46.874 1.00 57.09 C ANISOU 5164 C7 OLC A 411 6388 7494 7808 -166 -547 -622 C HETATM 5165 C6 OLC A 411 26.201 34.204 47.793 1.00 57.74 C ANISOU 5165 C6 OLC A 411 6385 7658 7895 -156 -596 -680 C HETATM 5166 C5 OLC A 411 26.466 35.557 48.403 1.00 60.92 C ANISOU 5166 C5 OLC A 411 6729 8071 8346 -204 -616 -776 C HETATM 5167 C4 OLC A 411 25.556 35.909 49.555 1.00 75.35 C ANISOU 5167 C4 OLC A 411 8577 9937 10116 -200 -654 -818 C HETATM 5168 C3 OLC A 411 25.825 35.145 50.840 1.00 63.88 C ANISOU 5168 C3 OLC A 411 7102 8594 8576 -148 -718 -830 C HETATM 5169 C2 OLC A 411 24.670 35.231 51.789 1.00 70.09 C ANISOU 5169 C2 OLC A 411 7933 9408 9290 -134 -742 -842 C HETATM 5170 C1 OLC A 411 24.860 34.428 53.041 1.00 71.56 C ANISOU 5170 C1 OLC A 411 8104 9704 9383 -74 -799 -844 C HETATM 5171 O19 OLC A 411 24.020 33.397 53.090 1.00 71.73 O ANISOU 5171 O19 OLC A 411 8196 9724 9335 -29 -790 -765 O HETATM 5172 O20 OLC A 411 25.666 34.669 53.901 1.00 68.00 O ANISOU 5172 O20 OLC A 411 7584 9334 8920 -66 -848 -908 O HETATM 5173 C18 OLC A 412 -7.320 25.137 37.251 1.00 57.07 C ANISOU 5173 C18 OLC A 412 7364 7028 7291 -223 -215 -130 C HETATM 5174 C10 OLC A 412 -6.305 26.354 46.434 1.00 65.88 C ANISOU 5174 C10 OLC A 412 8498 8184 8349 -133 -223 -73 C HETATM 5175 C9 OLC A 412 -6.856 25.449 47.202 1.00 70.58 C ANISOU 5175 C9 OLC A 412 9104 8777 8935 -122 -203 -54 C HETATM 5176 C17 OLC A 412 -6.725 26.298 38.009 1.00 57.09 C ANISOU 5176 C17 OLC A 412 7365 7033 7292 -210 -225 -116 C HETATM 5177 C11 OLC A 412 -5.799 26.116 45.046 1.00 66.02 C ANISOU 5177 C11 OLC A 412 8514 8185 8387 -147 -224 -77 C HETATM 5178 C8 OLC A 412 -7.572 25.678 48.497 1.00 57.26 C ANISOU 5178 C8 OLC A 412 7421 7108 7227 -107 -197 -49 C HETATM 5179 C24 OLC A 412 -5.901 27.269 58.197 1.00 71.64 C ANISOU 5179 C24 OLC A 412 9249 9243 8728 121 -249 -59 C HETATM 5180 C16 OLC A 412 -6.969 26.269 39.494 1.00 50.73 C ANISOU 5180 C16 OLC A 412 6563 6223 6489 -206 -223 -109 C HETATM 5181 C12 OLC A 412 -6.587 26.875 44.028 1.00 65.84 C ANISOU 5181 C12 OLC A 412 8484 8156 8377 -167 -228 -90 C HETATM 5182 C7 OLC A 412 -7.725 24.421 49.297 1.00 58.58 C ANISOU 5182 C7 OLC A 412 7601 7272 7384 -87 -170 -18 C HETATM 5183 C15 OLC A 412 -6.421 27.481 40.195 1.00 50.34 C ANISOU 5183 C15 OLC A 412 6508 6180 6438 -196 -234 -105 C HETATM 5184 C13 OLC A 412 -6.129 26.704 42.593 1.00 60.83 C ANISOU 5184 C13 OLC A 412 7847 7510 7755 -178 -229 -94 C HETATM 5185 C6 OLC A 412 -8.056 24.653 50.764 1.00 51.85 C ANISOU 5185 C6 OLC A 412 6754 6448 6498 -61 -165 -8 C HETATM 5186 C14 OLC A 412 -6.844 27.619 41.632 1.00 53.45 C ANISOU 5186 C14 OLC A 412 6904 6577 6826 -190 -234 -103 C HETATM 5187 C5 OLC A 412 -7.495 23.607 51.699 1.00 53.54 C ANISOU 5187 C5 OLC A 412 6979 6674 6689 -26 -147 26 C HETATM 5188 C4 OLC A 412 -7.604 23.973 53.156 1.00 48.66 C ANISOU 5188 C4 OLC A 412 6365 6097 6028 6 -149 33 C HETATM 5189 C3 OLC A 412 -6.501 23.400 54.025 1.00 52.18 C ANISOU 5189 C3 OLC A 412 6814 6576 6437 49 -153 57 C HETATM 5190 C2 OLC A 412 -6.628 23.823 55.452 1.00 57.76 C ANISOU 5190 C2 OLC A 412 7523 7331 7092 82 -158 59 C HETATM 5191 C21 OLC A 412 -6.406 24.801 57.971 1.00 65.45 C ANISOU 5191 C21 OLC A 412 8495 8413 7959 148 -182 45 C HETATM 5192 C1 OLC A 412 -5.435 23.461 56.289 1.00 63.38 C ANISOU 5192 C1 OLC A 412 8232 8089 7760 128 -172 76 C HETATM 5193 C22 OLC A 412 -6.008 25.930 58.896 1.00 66.91 C ANISOU 5193 C22 OLC A 412 8668 8658 8098 164 -218 1 C HETATM 5194 O19 OLC A 412 -4.776 22.465 56.152 1.00 72.40 O ANISOU 5194 O19 OLC A 412 9378 9224 8907 147 -159 109 O HETATM 5195 O25 OLC A 412 -5.800 28.345 59.126 1.00 75.55 O ANISOU 5195 O25 OLC A 412 9734 9785 9186 132 -274 -105 O HETATM 5196 O23 OLC A 412 -6.922 26.003 59.989 1.00 64.78 O ANISOU 5196 O23 OLC A 412 8411 8414 7789 188 -196 12 O HETATM 5197 O20 OLC A 412 -5.233 24.339 57.266 1.00 68.15 O ANISOU 5197 O20 OLC A 412 8828 8747 8318 147 -198 50 O HETATM 5198 C8 OLC A 413 -5.890 22.242 30.693 1.00 61.14 C ANISOU 5198 C8 OLC A 413 7888 7584 7758 -235 -193 -224 C HETATM 5199 C7 OLC A 413 -5.838 22.693 29.268 1.00 53.32 C ANISOU 5199 C7 OLC A 413 6894 6632 6735 -224 -200 -232 C HETATM 5200 C6 OLC A 413 -5.065 21.760 28.347 1.00 54.05 C ANISOU 5200 C6 OLC A 413 6995 6720 6820 -223 -185 -254 C HETATM 5201 C5 OLC A 413 -5.145 22.135 26.891 1.00 64.09 C ANISOU 5201 C5 OLC A 413 8263 8038 8052 -210 -192 -266 C HETATM 5202 C4 OLC A 413 -4.443 21.175 25.967 1.00 61.94 C ANISOU 5202 C4 OLC A 413 7999 7764 7770 -208 -176 -294 C HETATM 5203 C3 OLC A 413 -4.496 21.580 24.507 1.00 57.33 C ANISOU 5203 C3 OLC A 413 7413 7232 7138 -190 -182 -304 C HETATM 5204 C2 OLC A 413 -5.896 21.720 24.000 1.00 64.50 C ANISOU 5204 C2 OLC A 413 8303 8188 8017 -196 -206 -332 C HETATM 5205 C1 OLC A 413 -5.971 22.399 22.665 1.00 72.03 C ANISOU 5205 C1 OLC A 413 9252 9202 8915 -168 -215 -328 C HETATM 5206 O19 OLC A 413 -5.188 21.804 21.773 1.00 66.65 O ANISOU 5206 O19 OLC A 413 8581 8528 8214 -160 -200 -348 O HETATM 5207 O20 OLC A 413 -6.637 23.372 22.417 1.00 75.21 O ANISOU 5207 O20 OLC A 413 9642 9642 9291 -152 -232 -307 O HETATM 5208 C10 OLC A 414 -6.503 34.743 28.987 1.00 63.87 C ANISOU 5208 C10 OLC A 414 8176 8003 8089 -76 -180 41 C HETATM 5209 C9 OLC A 414 -6.409 34.720 27.682 1.00 52.18 C ANISOU 5209 C9 OLC A 414 6696 6553 6576 -53 -172 58 C HETATM 5210 C11 OLC A 414 -6.130 33.622 29.908 1.00 56.49 C ANISOU 5210 C11 OLC A 414 7248 7053 7165 -105 -194 5 C HETATM 5211 C8 OLC A 414 -6.942 35.751 26.741 1.00 54.06 C ANISOU 5211 C8 OLC A 414 6928 6817 6796 -16 -158 99 C HETATM 5212 C12 OLC A 414 -6.300 33.974 31.356 1.00 56.24 C ANISOU 5212 C12 OLC A 414 7213 6992 7165 -121 -199 -5 C HETATM 5213 C7 OLC A 414 -6.491 35.538 25.330 1.00 47.20 C ANISOU 5213 C7 OLC A 414 6065 5982 5888 9 -147 116 C HETATM 5214 C13 OLC A 414 -6.194 32.802 32.314 1.00 49.27 C ANISOU 5214 C13 OLC A 414 6335 6100 6283 -144 -214 -36 C HETATM 5215 C6 OLC A 414 -7.258 36.366 24.312 1.00 47.29 C ANISOU 5215 C6 OLC A 414 6068 6036 5866 52 -139 157 C HETATM 5216 C14 OLC A 414 -6.147 33.206 33.776 1.00 50.31 C ANISOU 5216 C14 OLC A 414 6466 6208 6442 -155 -217 -44 C HETATM 5217 C5 OLC A 414 -6.998 35.974 22.882 1.00 46.73 C ANISOU 5217 C5 OLC A 414 6002 6014 5740 80 -134 167 C HETATM 5218 C4 OLC A 414 -7.947 36.596 21.897 1.00 50.14 C ANISOU 5218 C4 OLC A 414 6424 6504 6125 126 -135 202 C HETATM 5219 C3 OLC A 414 -7.775 36.098 20.474 1.00 57.57 C ANISOU 5219 C3 OLC A 414 7368 7506 7000 156 -136 205 C HETATM 5220 C2 OLC A 414 -8.619 36.857 19.495 1.00 64.51 C ANISOU 5220 C2 OLC A 414 8235 8446 7829 210 -133 249 C HETATM 5221 C ACE B 401 -13.187 22.028 71.143 1.00 38.24 C ANISOU 5221 C ACE B 401 5221 5362 3948 644 201 427 C HETATM 5222 O ACE B 401 -12.208 22.194 70.424 1.00 40.17 O ANISOU 5222 O ACE B 401 5450 5602 4212 621 149 393 O HETATM 5223 CH3 ACE B 401 -13.141 21.213 72.403 1.00 38.27 C ANISOU 5223 CH3 ACE B 401 5245 5421 3875 728 247 505 C HETATM 5224 C1 RET B 402 -19.871 24.965 45.111 1.00 27.74 C ANISOU 5224 C1 RET B 402 3555 3317 3667 -275 -93 -117 C HETATM 5225 C2 RET B 402 -19.062 24.445 43.908 1.00 36.55 C ANISOU 5225 C2 RET B 402 4674 4429 4785 -287 -110 -133 C HETATM 5226 C3 RET B 402 -18.656 25.467 42.864 1.00 35.13 C ANISOU 5226 C3 RET B 402 4488 4274 4585 -281 -146 -143 C HETATM 5227 C4 RET B 402 -19.851 26.276 42.426 1.00 24.78 C ANISOU 5227 C4 RET B 402 3149 2989 3277 -283 -158 -153 C HETATM 5228 C5 RET B 402 -20.636 26.834 43.576 1.00 21.88 C ANISOU 5228 C5 RET B 402 2779 2622 2913 -273 -143 -139 C HETATM 5229 C6 RET B 402 -20.630 26.260 44.797 1.00 21.69 C ANISOU 5229 C6 RET B 402 2769 2578 2894 -269 -114 -124 C HETATM 5230 C7 RET B 402 -21.349 26.828 45.923 1.00 24.17 C ANISOU 5230 C7 RET B 402 3082 2896 3206 -256 -98 -111 C HETATM 5231 C8 RET B 402 -21.274 28.153 46.284 1.00 22.59 C ANISOU 5231 C8 RET B 402 2886 2710 2986 -236 -111 -106 C HETATM 5232 C9 RET B 402 -21.967 28.807 47.374 1.00 24.14 C ANISOU 5232 C9 RET B 402 3082 2912 3179 -221 -94 -97 C HETATM 5233 C10 RET B 402 -21.850 30.154 47.521 1.00 24.75 C ANISOU 5233 C10 RET B 402 3162 3000 3243 -204 -108 -98 C HETATM 5234 C11 RET B 402 -22.488 30.980 48.511 1.00 23.27 C ANISOU 5234 C11 RET B 402 2973 2818 3050 -187 -94 -95 C HETATM 5235 C12 RET B 402 -22.223 32.267 48.917 1.00 22.18 C ANISOU 5235 C12 RET B 402 2844 2685 2900 -168 -101 -99 C HETATM 5236 C13 RET B 402 -21.146 33.183 48.573 1.00 22.91 C ANISOU 5236 C13 RET B 402 2947 2774 2983 -161 -123 -108 C HETATM 5237 C14 RET B 402 -21.249 34.487 48.936 1.00 20.52 C ANISOU 5237 C14 RET B 402 2644 2470 2681 -146 -122 -116 C HETATM 5238 C15 RET B 402 -20.296 35.488 48.724 1.00 19.99 C ANISOU 5238 C15 RET B 402 2586 2396 2613 -139 -136 -127 C HETATM 5239 C16 RET B 402 -20.858 23.829 45.405 1.00 24.38 C ANISOU 5239 C16 RET B 402 3115 2872 3277 -295 -57 -119 C HETATM 5240 C17 RET B 402 -18.951 25.157 46.336 1.00 21.34 C ANISOU 5240 C17 RET B 402 2775 2502 2833 -249 -85 -92 C HETATM 5241 C18 RET B 402 -21.606 27.900 43.139 1.00 23.41 C ANISOU 5241 C18 RET B 402 2947 2843 3106 -267 -158 -143 C HETATM 5242 C19 RET B 402 -22.790 27.949 48.301 1.00 22.66 C ANISOU 5242 C19 RET B 402 2891 2714 3005 -225 -58 -86 C HETATM 5243 C20 RET B 402 -19.906 32.632 47.919 1.00 22.12 C ANISOU 5243 C20 RET B 402 2859 2668 2876 -169 -141 -109 C HETATM 5244 C1 NAG B 403 -9.386 22.870 68.291 1.00 36.65 C ANISOU 5244 C1 NAG B 403 4954 5145 3827 548 3 286 C HETATM 5245 C2 NAG B 403 -9.739 21.445 67.896 1.00 41.03 C ANISOU 5245 C2 NAG B 403 5524 5634 4430 555 66 369 C HETATM 5246 C3 NAG B 403 -8.806 20.466 68.608 1.00 41.18 C ANISOU 5246 C3 NAG B 403 5551 5703 4394 628 76 433 C HETATM 5247 C4 NAG B 403 -7.354 20.809 68.290 1.00 46.42 C ANISOU 5247 C4 NAG B 403 6190 6407 5038 630 8 392 C HETATM 5248 C5 NAG B 403 -7.063 22.283 68.595 1.00 46.93 C ANISOU 5248 C5 NAG B 403 6235 6533 5062 614 -57 301 C HETATM 5249 C6 NAG B 403 -5.687 22.718 68.142 1.00 46.36 C ANISOU 5249 C6 NAG B 403 6135 6492 4988 603 -123 252 C HETATM 5250 C7 NAG B 403 -11.908 20.509 67.267 1.00 42.37 C ANISOU 5250 C7 NAG B 403 5714 5676 4707 506 173 428 C HETATM 5251 C8 NAG B 403 -13.332 20.260 67.675 1.00 42.57 C ANISOU 5251 C8 NAG B 403 5752 5671 4752 504 237 461 C HETATM 5252 N2 NAG B 403 -11.134 21.133 68.165 1.00 34.17 N ANISOU 5252 N2 NAG B 403 4673 4727 3584 550 129 405 N HETATM 5253 O3 NAG B 403 -9.088 19.143 68.171 1.00 47.26 O ANISOU 5253 O3 NAG B 403 6335 6402 5219 631 138 507 O HETATM 5254 O4 NAG B 403 -6.476 19.992 69.059 1.00 48.80 O ANISOU 5254 O4 NAG B 403 6495 6768 5278 706 13 450 O HETATM 5255 O5 NAG B 403 -8.011 23.140 67.932 1.00 42.79 O ANISOU 5255 O5 NAG B 403 5710 5954 4595 547 -57 250 O HETATM 5256 O6 NAG B 403 -5.506 22.533 66.744 1.00 44.10 O ANISOU 5256 O6 NAG B 403 5842 6124 4790 546 -126 244 O HETATM 5257 O7 NAG B 403 -11.475 20.156 66.171 1.00 37.80 O ANISOU 5257 O7 NAG B 403 5127 5047 4189 469 160 421 O HETATM 5258 C10 OLC B 404 -34.192 34.194 30.940 1.00 55.85 C ANISOU 5258 C10 OLC B 404 6480 7692 7049 -34 -471 -192 C HETATM 5259 C9 OLC B 404 -33.175 34.087 30.123 1.00 50.40 C ANISOU 5259 C9 OLC B 404 5820 7010 6319 -26 -483 -189 C HETATM 5260 C11 OLC B 404 -34.344 33.747 32.359 1.00 44.88 C ANISOU 5260 C11 OLC B 404 5106 6231 5717 -77 -436 -204 C HETATM 5261 C8 OLC B 404 -33.176 34.805 28.810 1.00 58.64 C ANISOU 5261 C8 OLC B 404 6848 8129 7305 30 -511 -161 C HETATM 5262 C12 OLC B 404 -35.114 34.734 33.175 1.00 56.40 C ANISOU 5262 C12 OLC B 404 6552 7675 7201 -49 -413 -164 C HETATM 5263 C7 OLC B 404 -33.498 33.934 27.636 1.00 65.89 C ANISOU 5263 C7 OLC B 404 7724 9129 8183 21 -554 -216 C HETATM 5264 C15 OLC B 404 -37.181 34.623 36.464 1.00 60.61 C ANISOU 5264 C15 OLC B 404 7054 8115 7862 -94 -328 -167 C HETATM 5265 C13 OLC B 404 -35.650 34.198 34.491 1.00 41.16 C ANISOU 5265 C13 OLC B 404 4618 5696 5325 -89 -382 -183 C HETATM 5266 C6 OLC B 404 -34.183 34.677 26.495 1.00 67.25 C ANISOU 5266 C6 OLC B 404 7851 9402 8299 83 -587 -192 C HETATM 5267 C14 OLC B 404 -36.559 35.165 35.203 1.00 55.83 C ANISOU 5267 C14 OLC B 404 6457 7551 7206 -59 -361 -149 C HETATM 5268 C5 OLC B 404 -34.140 33.962 25.172 1.00 59.30 C ANISOU 5268 C5 OLC B 404 6817 8479 7235 84 -630 -240 C HETATM 5269 C4 OLC B 404 -34.842 34.689 24.051 1.00 70.00 C ANISOU 5269 C4 OLC B 404 8124 9944 8528 152 -665 -214 C HETATM 5270 C3 OLC B 404 -34.507 36.167 23.960 1.00 70.72 C ANISOU 5270 C3 OLC B 404 8245 10025 8600 224 -640 -118 C HETATM 5271 C2 OLC B 404 -35.128 36.834 22.766 1.00 74.62 C ANISOU 5271 C2 OLC B 404 8694 10632 9026 297 -673 -86 C HETATM 5272 C21 OLC B 404 -35.932 38.088 20.619 1.00 68.32 C ANISOU 5272 C21 OLC B 404 7831 10031 8095 442 -723 -13 C HETATM 5273 C1 OLC B 404 -34.971 38.332 22.786 1.00 79.18 C ANISOU 5273 C1 OLC B 404 9296 11192 9598 369 -641 13 C HETATM 5274 C22 OLC B 404 -36.419 38.988 19.505 1.00 67.16 C ANISOU 5274 C22 OLC B 404 7650 9994 7875 536 -744 46 C HETATM 5275 O19 OLC B 404 -34.464 38.942 23.692 1.00 81.00 O ANISOU 5275 O19 OLC B 404 9571 11327 9877 364 -596 56 O HETATM 5276 O20 OLC B 404 -35.451 38.926 21.692 1.00 78.93 O ANISOU 5276 O20 OLC B 404 9227 11261 9502 442 -666 49 O HETATM 5277 C10 OLC B 405 -4.543 38.401 41.394 1.00 69.83 C ANISOU 5277 C10 OLC B 405 8893 8572 9069 -193 -214 -160 C HETATM 5278 C9 OLC B 405 -4.531 37.116 41.644 1.00 67.17 C ANISOU 5278 C9 OLC B 405 8565 8258 8697 -192 -232 -158 C HETATM 5279 C11 OLC B 405 -4.532 39.019 40.030 1.00 78.23 C ANISOU 5279 C11 OLC B 405 9954 9616 10155 -187 -192 -131 C HETATM 5280 C8 OLC B 405 -4.509 36.473 42.996 1.00 55.59 C ANISOU 5280 C8 OLC B 405 7102 6813 7206 -191 -250 -180 C HETATM 5281 C24 OLC B 405 -7.857 31.843 52.941 1.00 48.68 C ANISOU 5281 C24 OLC B 405 6299 6142 6054 -73 -269 -189 C HETATM 5282 C7 OLC B 405 -5.677 35.566 43.229 1.00 57.59 C ANISOU 5282 C7 OLC B 405 7370 7082 7428 -186 -254 -167 C HETATM 5283 C6 OLC B 405 -5.653 34.869 44.582 1.00 55.05 C ANISOU 5283 C6 OLC B 405 7055 6783 7080 -180 -266 -181 C HETATM 5284 C5 OLC B 405 -6.901 34.085 44.915 1.00 51.20 C ANISOU 5284 C5 OLC B 405 6580 6306 6569 -176 -262 -167 C HETATM 5285 C4 OLC B 405 -6.913 33.577 46.331 1.00 49.89 C ANISOU 5285 C4 OLC B 405 6419 6160 6375 -165 -268 -177 C HETATM 5286 C3 OLC B 405 -8.218 32.961 46.782 1.00 46.51 C ANISOU 5286 C3 OLC B 405 6002 5740 5930 -161 -258 -163 C HETATM 5287 C2 OLC B 405 -8.298 32.851 48.271 1.00 43.65 C ANISOU 5287 C2 OLC B 405 5645 5400 5542 -147 -260 -174 C HETATM 5288 C21 OLC B 405 -7.245 30.539 50.850 1.00 57.32 C ANISOU 5288 C21 OLC B 405 7396 7192 7191 -96 -263 -150 C HETATM 5289 C1 OLC B 405 -7.508 31.718 48.842 1.00 48.54 C ANISOU 5289 C1 OLC B 405 6270 6036 6137 -133 -265 -163 C HETATM 5290 C22 OLC B 405 -6.993 30.766 52.324 1.00 53.73 C ANISOU 5290 C22 OLC B 405 6941 6776 6698 -71 -272 -164 C HETATM 5291 O19 OLC B 405 -7.006 30.836 48.202 1.00 57.73 O ANISOU 5291 O19 OLC B 405 7438 7193 7304 -135 -264 -146 O HETATM 5292 O25 OLC B 405 -7.323 33.135 52.682 1.00 57.93 O ANISOU 5292 O25 OLC B 405 7455 7308 7248 -88 -285 -228 O HETATM 5293 O23 OLC B 405 -7.180 29.540 53.029 1.00 61.74 O ANISOU 5293 O23 OLC B 405 7970 7806 7684 -47 -256 -130 O HETATM 5294 O20 OLC B 405 -7.408 31.800 50.165 1.00 54.14 O ANISOU 5294 O20 OLC B 405 6982 6772 6818 -116 -270 -174 O HETATM 5295 C18 OLC B 406 -8.442 40.329 42.864 1.00 63.03 C ANISOU 5295 C18 OLC B 406 8038 7701 8210 -173 -191 -166 C HETATM 5296 C10 OLC B 406 -10.290 41.597 50.843 1.00 56.88 C ANISOU 5296 C10 OLC B 406 7270 6996 7345 -157 -209 -361 C HETATM 5297 C9 OLC B 406 -10.346 42.328 51.934 1.00 47.47 C ANISOU 5297 C9 OLC B 406 6075 5811 6151 -154 -205 -406 C HETATM 5298 C17 OLC B 406 -9.218 40.068 44.133 1.00 58.56 C ANISOU 5298 C17 OLC B 406 7478 7152 7621 -172 -200 -187 C HETATM 5299 C11 OLC B 406 -11.012 41.850 49.554 1.00 45.76 C ANISOU 5299 C11 OLC B 406 5860 5558 5967 -158 -191 -320 C HETATM 5300 C8 OLC B 406 -9.432 42.149 53.106 1.00 51.72 C ANISOU 5300 C8 OLC B 406 6609 6385 6657 -153 -228 -451 C HETATM 5301 C16 OLC B 406 -8.368 39.655 45.311 1.00 53.86 C ANISOU 5301 C16 OLC B 406 6883 6571 7011 -179 -216 -221 C HETATM 5302 C12 OLC B 406 -11.731 40.653 48.997 1.00 44.01 C ANISOU 5302 C12 OLC B 406 5648 5354 5719 -152 -196 -276 C HETATM 5303 C7 OLC B 406 -10.134 41.921 54.407 1.00 42.95 C ANISOU 5303 C7 OLC B 406 5509 5311 5499 -134 -228 -467 C HETATM 5304 C15 OLC B 406 -9.142 39.137 46.504 1.00 48.48 C ANISOU 5304 C15 OLC B 406 6210 5915 6296 -173 -224 -232 C HETATM 5305 C13 OLC B 406 -10.859 39.610 48.308 1.00 43.07 C ANISOU 5305 C13 OLC B 406 5532 5246 5588 -159 -213 -256 C HETATM 5306 C6 OLC B 406 -9.258 41.232 55.445 1.00 50.68 C ANISOU 5306 C6 OLC B 406 6488 6343 6426 -123 -255 -491 C HETATM 5307 C14 OLC B 406 -10.195 40.081 47.037 1.00 46.95 C ANISOU 5307 C14 OLC B 406 6015 5711 6113 -167 -208 -243 C HETATM 5308 C5 OLC B 406 -7.816 41.687 55.431 1.00 57.80 C ANISOU 5308 C5 OLC B 406 7368 7248 7347 -137 -276 -535 C HETATM 5309 C4 OLC B 406 -6.922 40.938 56.388 1.00 60.13 C ANISOU 5309 C4 OLC B 406 7658 7602 7586 -122 -306 -554 C HETATM 5310 C3 OLC B 406 -5.437 41.094 56.113 1.00 68.53 C ANISOU 5310 C3 OLC B 406 8697 8671 8671 -136 -330 -584 C HETATM 5311 C2 OLC B 406 -4.600 40.208 56.985 1.00 71.21 C ANISOU 5311 C2 OLC B 406 9031 9075 8951 -114 -361 -592 C HETATM 5312 C1 PLM B 407 -17.632 53.754 21.492 1.00 67.82 C ANISOU 5312 C1 PLM B 407 8521 8578 8670 752 301 1003 C HETATM 5313 O2 PLM B 407 -17.562 55.017 21.542 1.00 71.34 O ANISOU 5313 O2 PLM B 407 8969 8954 9182 788 372 1064 O HETATM 5314 C2 PLM B 407 -17.170 53.004 22.781 1.00 69.90 C ANISOU 5314 C2 PLM B 407 8793 8792 8973 658 265 901 C HETATM 5315 C3 PLM B 407 -16.299 53.839 23.728 1.00 70.29 C ANISOU 5315 C3 PLM B 407 8858 8719 9130 619 323 888 C HETATM 5316 C4 PLM B 407 -15.681 53.053 24.905 1.00 72.06 C ANISOU 5316 C4 PLM B 407 9092 8905 9383 531 287 791 C HETATM 5317 C5 PLM B 407 -14.692 53.884 25.749 1.00 71.01 C ANISOU 5317 C5 PLM B 407 8972 8658 9353 493 342 773 C HETATM 5318 C6 PLM B 407 -14.162 53.182 27.011 1.00 80.96 C ANISOU 5318 C6 PLM B 407 10237 9885 10638 413 306 679 C HETATM 5319 C10 OLC B 408 -14.752 18.010 46.796 1.00 44.37 C ANISOU 5319 C10 OLC B 408 5780 5254 5826 -233 58 -13 C HETATM 5320 C9 OLC B 408 -15.207 16.865 46.352 1.00 53.26 C ANISOU 5320 C9 OLC B 408 6898 6340 6998 -257 94 -23 C HETATM 5321 C11 OLC B 408 -13.813 18.848 45.989 1.00 53.69 C ANISOU 5321 C11 OLC B 408 6960 6460 6978 -231 10 -32 C HETATM 5322 C8 OLC B 408 -15.857 15.766 47.133 1.00 52.35 C ANISOU 5322 C8 OLC B 408 6786 6185 6922 -257 154 2 C HETATM 5323 C12 OLC B 408 -13.383 20.112 46.657 1.00 39.06 C ANISOU 5323 C12 OLC B 408 5114 4646 5082 -207 -21 -21 C HETATM 5324 C7 OLC B 408 -15.048 14.509 47.129 1.00 62.04 C ANISOU 5324 C7 OLC B 408 8030 7370 8174 -246 191 23 C HETATM 5325 C13 OLC B 408 -12.317 20.859 45.875 1.00 45.87 C ANISOU 5325 C13 OLC B 408 5977 5528 5924 -204 -61 -37 C HETATM 5326 O HOH A 501 12.768 14.723 62.420 1.00 58.45 O ANISOU 5326 O HOH A 501 7316 8198 6694 948 -373 526 O HETATM 5327 O HOH A 502 10.511 32.314 63.237 1.00 65.72 O ANISOU 5327 O HOH A 502 7978 9239 7755 257 -807 -649 O HETATM 5328 O HOH A 503 4.877 15.758 4.312 1.00 53.14 O ANISOU 5328 O HOH A 503 7056 7311 5825 207 146 -696 O HETATM 5329 O HOH A 504 2.141 20.947 8.905 1.00 45.87 O ANISOU 5329 O HOH A 504 6065 6296 5069 164 17 -378 O HETATM 5330 O HOH A 505 16.649 30.203 10.854 1.00 34.58 O ANISOU 5330 O HOH A 505 4520 4327 4291 276 570 368 O HETATM 5331 O HOH A 506 13.683 20.408 59.399 1.00 37.59 O ANISOU 5331 O HOH A 506 4551 5502 4230 605 -561 110 O HETATM 5332 O HOH A 507 0.599 14.291 26.594 1.00 30.83 O ANISOU 5332 O HOH A 507 4131 3581 4002 -211 1 -354 O HETATM 5333 O HOH A 508 6.918 31.068 58.059 1.00 47.50 O ANISOU 5333 O HOH A 508 5862 6492 5694 121 -596 -411 O HETATM 5334 O HOH A 509 12.062 25.710 15.381 1.00 26.23 O ANISOU 5334 O HOH A 509 3504 3271 3192 117 254 75 O HETATM 5335 O HOH A 510 9.592 20.514 57.269 1.00 35.43 O ANISOU 5335 O HOH A 510 4431 4952 4080 450 -430 128 O HETATM 5336 O HOH A 511 17.952 27.816 10.360 1.00 36.49 O ANISOU 5336 O HOH A 511 4774 4579 4510 279 581 295 O HETATM 5337 O HOH A 512 12.649 7.503 15.525 1.00 35.44 O ANISOU 5337 O HOH A 512 4826 4093 4548 23 427 -556 O HETATM 5338 O HOH A 513 2.207 26.343 15.747 1.00 34.86 O ANISOU 5338 O HOH A 513 4617 4596 4033 82 -6 -60 O HETATM 5339 O HOH A 514 -0.069 15.137 12.586 1.00 48.83 O ANISOU 5339 O HOH A 514 6415 6422 5715 -79 -33 -706 O HETATM 5340 O HOH A 515 10.781 19.911 40.568 1.00 23.39 O ANISOU 5340 O HOH A 515 2993 2780 3113 38 -183 28 O HETATM 5341 O HOH A 516 4.106 40.116 15.646 1.00 40.44 O ANISOU 5341 O HOH A 516 5249 5053 5063 286 345 566 O HETATM 5342 O HOH A 517 5.707 19.251 51.611 1.00 30.35 O ANISOU 5342 O HOH A 517 3932 3902 3698 228 -249 149 O HETATM 5343 O HOH A 518 10.287 25.453 0.760 1.00 49.75 O ANISOU 5343 O HOH A 518 6658 6998 5247 600 475 103 O HETATM 5344 O HOH A 519 5.574 18.369 4.611 1.00 39.61 O ANISOU 5344 O HOH A 519 5340 5602 4107 268 166 -494 O HETATM 5345 O HOH A 520 -2.717 30.629 19.551 1.00 32.17 O ANISOU 5345 O HOH A 520 4215 4228 3779 53 -113 35 O HETATM 5346 O HOH A 521 -3.739 38.015 19.390 1.00 39.89 O ANISOU 5346 O HOH A 521 5161 5146 4849 198 14 336 O HETATM 5347 O HOH A 522 4.802 34.659 10.119 1.00 38.93 O ANISOU 5347 O HOH A 522 5139 5214 4440 408 303 454 O HETATM 5348 O HOH A 523 10.507 23.409 23.582 1.00 22.36 O ANISOU 5348 O HOH A 523 2967 2618 2909 -38 56 -36 O HETATM 5349 O HOH A 524 18.700 22.030 1.999 1.00 39.64 O ANISOU 5349 O HOH A 524 5354 5332 4374 521 754 92 O HETATM 5350 O HOH A 525 3.908 30.741 10.101 1.00 30.76 O ANISOU 5350 O HOH A 525 4120 4267 3298 338 176 225 O HETATM 5351 O HOH A 526 -0.777 27.074 20.050 1.00 27.37 O ANISOU 5351 O HOH A 526 3632 3557 3209 -15 -107 -81 O HETATM 5352 O HOH A 527 19.276 10.688 8.786 1.00 41.79 O ANISOU 5352 O HOH A 527 5630 5126 5123 253 638 -408 O HETATM 5353 O HOH A 528 17.523 32.797 58.106 1.00 44.36 O ANISOU 5353 O HOH A 528 5002 6404 5448 105 -844 -726 O HETATM 5354 O HOH A 529 -3.758 20.782 58.049 1.00 61.14 O ANISOU 5354 O HOH A 529 7966 7864 7402 255 -130 200 O HETATM 5355 O HOH A 530 10.237 23.079 38.973 1.00 30.00 O ANISOU 5355 O HOH A 530 3810 3614 3973 -40 -207 -33 O HETATM 5356 O HOH A 531 5.069 34.822 20.050 1.00 28.45 O ANISOU 5356 O HOH A 531 3720 3487 3601 72 130 250 O HETATM 5357 O HOH A 532 13.586 20.741 21.074 1.00 26.70 O ANISOU 5357 O HOH A 532 3531 3154 3459 18 164 -53 O HETATM 5358 O HOH A 533 17.282 25.133 17.216 1.00 25.26 O ANISOU 5358 O HOH A 533 3289 3006 3303 98 339 114 O HETATM 5359 O HOH A 534 -7.278 30.509 60.011 1.00 38.93 O ANISOU 5359 O HOH A 534 5094 5161 4537 111 -276 -183 O HETATM 5360 O HOH A 535 13.394 32.604 13.102 1.00 29.42 O ANISOU 5360 O HOH A 535 3858 3648 3673 225 459 384 O HETATM 5361 O HOH A 536 23.243 26.357 15.294 1.00 39.43 O ANISOU 5361 O HOH A 536 4964 4738 5279 156 561 238 O HETATM 5362 O HOH A 537 17.781 25.343 29.736 1.00 23.58 O ANISOU 5362 O HOH A 537 2884 2719 3357 -43 13 10 O HETATM 5363 O HOH A 538 13.596 7.714 18.777 1.00 28.18 O ANISOU 5363 O HOH A 538 3874 3084 3750 34 410 -413 O HETATM 5364 O HOH A 539 18.786 23.512 54.592 1.00 38.19 O ANISOU 5364 O HOH A 539 4403 5478 4629 382 -645 -129 O HETATM 5365 O HOH A 540 10.103 17.837 1.047 1.00 34.50 O ANISOU 5365 O HOH A 540 4759 5006 3343 421 383 -433 O HETATM 5366 O HOH A 541 8.557 24.368 14.215 1.00 25.86 O ANISOU 5366 O HOH A 541 3503 3345 2978 119 170 -31 O HETATM 5367 O HOH A 542 14.531 23.488 54.769 1.00 41.29 O ANISOU 5367 O HOH A 542 4968 5741 4978 335 -566 -81 O HETATM 5368 O HOH A 543 14.367 25.867 17.013 1.00 23.10 O ANISOU 5368 O HOH A 543 3058 2784 2934 90 278 100 O HETATM 5369 O HOH A 544 7.922 36.044 17.409 1.00 34.98 O ANISOU 5369 O HOH A 544 4541 4294 4456 142 284 370 O HETATM 5370 O HOH A 545 13.651 25.902 42.078 1.00 29.84 O ANISOU 5370 O HOH A 545 3635 3718 3986 -25 -308 -102 O HETATM 5371 O HOH A 546 -9.541 33.224 19.997 1.00 42.51 O ANISOU 5371 O HOH A 546 5440 5712 5001 111 -229 64 O HETATM 5372 O HOH A 547 6.223 19.031 28.195 1.00 25.89 O ANISOU 5372 O HOH A 547 3462 2996 3379 -108 -31 -136 O HETATM 5373 O HOH A 548 21.595 17.295 13.673 1.00 51.90 O ANISOU 5373 O HOH A 548 6731 6353 6635 215 533 -34 O HETATM 5374 O HOH A 549 22.205 33.006 14.664 1.00 48.04 O ANISOU 5374 O HOH A 549 6002 5755 6494 139 678 420 O HETATM 5375 O HOH A 550 20.209 24.336 6.737 1.00 38.51 O ANISOU 5375 O HOH A 550 5091 4929 4611 383 711 221 O HETATM 5376 O HOH A 551 -3.275 41.181 14.208 1.00 57.43 O ANISOU 5376 O HOH A 551 7399 7508 6914 456 190 628 O HETATM 5377 O HOH A 552 12.834 14.300 4.316 1.00 35.97 O ANISOU 5377 O HOH A 552 4943 4840 3885 283 452 -520 O HETATM 5378 O HOH A 553 19.548 16.077 4.760 1.00 55.10 O ANISOU 5378 O HOH A 553 7316 7083 6535 381 689 -207 O HETATM 5379 O HOH A 554 2.928 13.538 19.186 1.00 34.76 O ANISOU 5379 O HOH A 554 4658 4235 4312 -149 59 -518 O HETATM 5380 O HOH A 555 22.951 34.606 10.593 1.00 45.21 O ANISOU 5380 O HOH A 555 5685 5430 6063 267 902 602 O HETATM 5381 O HOH A 556 0.666 24.010 18.189 1.00 33.43 O ANISOU 5381 O HOH A 556 4428 4345 3928 -17 -75 -182 O HETATM 5382 O HOH A 557 18.965 19.375 56.618 1.00 45.93 O ANISOU 5382 O HOH A 557 5438 6561 5453 624 -596 113 O HETATM 5383 O HOH A 558 11.902 24.937 37.677 1.00 29.66 O ANISOU 5383 O HOH A 558 3717 3570 3983 -64 -202 -54 O HETATM 5384 O HOH A 559 -0.837 28.823 13.757 1.00 46.52 O ANISOU 5384 O HOH A 559 6073 6255 5347 180 -46 13 O HETATM 5385 O HOH A 560 -3.875 18.031 16.114 1.00 38.76 O ANISOU 5385 O HOH A 560 5073 5143 4512 -132 -157 -584 O HETATM 5386 O HOH A 561 20.478 24.202 9.742 1.00 36.35 O ANISOU 5386 O HOH A 561 4764 4544 4504 292 630 194 O HETATM 5387 O HOH A 562 14.946 6.871 16.315 1.00 33.02 O ANISOU 5387 O HOH A 562 4508 3713 4325 71 488 -477 O HETATM 5388 O HOH A 563 22.428 22.129 14.726 1.00 34.11 O ANISOU 5388 O HOH A 563 4379 4099 4480 187 524 121 O HETATM 5389 O HOH A 564 7.328 22.977 38.915 1.00 30.94 O ANISOU 5389 O HOH A 564 3987 3709 4061 -70 -201 -39 O HETATM 5390 O HOH A 565 14.582 39.446 15.071 1.00 34.78 O ANISOU 5390 O HOH A 565 4418 4063 4733 182 640 583 O HETATM 5391 O HOH A 566 14.169 27.394 3.092 1.00 37.24 O ANISOU 5391 O HOH A 566 5025 5114 4011 540 627 302 O HETATM 5392 O HOH A 567 8.294 28.041 55.808 1.00 36.81 O ANISOU 5392 O HOH A 567 4529 5063 4395 156 -546 -249 O HETATM 5393 O HOH A 568 -1.852 24.671 13.866 1.00 41.98 O ANISOU 5393 O HOH A 568 5498 5700 4751 84 -115 -224 O HETATM 5394 O HOH A 569 2.246 42.028 18.527 1.00 37.90 O ANISOU 5394 O HOH A 569 4899 4628 4875 227 303 541 O HETATM 5395 O HOH A 570 13.694 18.223 19.712 1.00 28.51 O ANISOU 5395 O HOH A 570 3801 3378 3656 35 208 -119 O HETATM 5396 O HOH A 571 -0.244 36.120 10.200 1.00 42.98 O ANISOU 5396 O HOH A 571 5626 5892 4812 475 171 473 O HETATM 5397 O HOH A 572 5.580 19.316 30.853 1.00 34.91 O ANISOU 5397 O HOH A 572 4593 4125 4547 -115 -65 -108 O HETATM 5398 O HOH A 573 21.070 6.234 13.321 1.00 42.65 O ANISOU 5398 O HOH A 573 5708 4926 5572 234 696 -399 O HETATM 5399 O HOH A 574 13.804 17.657 -3.687 1.00 47.07 O ANISOU 5399 O HOH A 574 6420 6768 4694 634 620 -375 O HETATM 5400 O HOH A 575 14.051 34.088 2.914 1.00 57.28 O ANISOU 5400 O HOH A 575 7517 7565 6682 653 809 714 O HETATM 5401 O HOH A 576 20.606 12.780 7.952 1.00 60.44 O ANISOU 5401 O HOH A 576 7967 7544 7452 301 673 -292 O HETATM 5402 O HOH A 577 -0.781 20.595 10.648 1.00 45.86 O ANISOU 5402 O HOH A 577 6020 6288 5115 83 -85 -457 O HETATM 5403 O HOH A 578 12.428 41.503 17.957 1.00 56.94 O ANISOU 5403 O HOH A 578 7199 6784 7650 110 562 535 O HETATM 5404 O HOH A 579 10.278 29.307 3.854 1.00 46.07 O ANISOU 5404 O HOH A 579 6135 6320 5048 545 492 333 O HETATM 5405 O HOH A 580 7.854 38.658 16.594 1.00 41.41 O ANISOU 5405 O HOH A 580 5344 5069 5320 193 379 488 O HETATM 5406 O HOH A 581 21.186 23.559 55.677 1.00 41.75 O ANISOU 5406 O HOH A 581 4728 6088 5049 447 -725 -169 O HETATM 5407 O HOH A 582 -0.488 26.074 15.802 1.00 52.16 O ANISOU 5407 O HOH A 582 6792 6860 6165 67 -79 -120 O HETATM 5408 O HOH A 583 11.767 27.865 2.108 1.00 60.28 O ANISOU 5408 O HOH A 583 7962 8176 6765 591 559 292 O HETATM 5409 O HOH A 584 -2.011 27.132 17.614 1.00 42.10 O ANISOU 5409 O HOH A 584 5496 5553 4947 38 -120 -97 O HETATM 5410 O HOH A 585 9.612 25.058 -2.527 1.00 53.36 O ANISOU 5410 O HOH A 585 7151 7711 5414 739 496 68 O HETATM 5411 O HOH A 586 22.911 20.370 13.015 1.00 61.98 O ANISOU 5411 O HOH A 586 7952 7652 7946 231 583 84 O HETATM 5412 O HOH A 587 22.274 22.056 10.470 1.00 51.35 O ANISOU 5412 O HOH A 587 6642 6385 6483 280 648 138 O HETATM 5413 O HOH B 501 -17.014 36.214 16.156 1.00 37.40 O ANISOU 5413 O HOH B 501 4618 5541 4049 371 -366 165 O HETATM 5414 O HOH B 502 -23.897 25.592 17.585 1.00 47.25 O ANISOU 5414 O HOH B 502 5583 6972 5399 -82 -655 -645 O HETATM 5415 O HOH B 503 -21.800 49.505 62.337 1.00 53.62 O ANISOU 5415 O HOH B 503 6906 6610 6858 29 98 -681 O HETATM 5416 O HOH B 504 -28.554 35.401 66.607 1.00 39.39 O ANISOU 5416 O HOH B 504 5169 5101 4696 178 309 -92 O HETATM 5417 O HOH B 505 -30.094 42.383 48.916 1.00 29.19 O ANISOU 5417 O HOH B 505 3573 3579 3940 4 4 -65 O HETATM 5418 O HOH B 506 -26.580 25.876 65.510 1.00 33.50 O ANISOU 5418 O HOH B 506 4460 4248 4020 160 437 238 O HETATM 5419 O HOH B 507 -13.930 26.605 64.625 1.00 33.45 O ANISOU 5419 O HOH B 507 4514 4486 3708 266 7 89 O HETATM 5420 O HOH B 508 -26.522 16.706 59.941 1.00 39.14 O ANISOU 5420 O HOH B 508 5094 4557 5221 -66 634 363 O HETATM 5421 O HOH B 509 -25.672 21.939 55.500 1.00 30.03 O ANISOU 5421 O HOH B 509 3876 3538 3998 -167 288 108 O HETATM 5422 O HOH B 510 -25.131 37.438 24.030 1.00 30.46 O ANISOU 5422 O HOH B 510 3551 4510 3513 212 -445 71 O HETATM 5423 O HOH B 511 -20.499 33.691 36.578 1.00 28.52 O ANISOU 5423 O HOH B 511 3550 3627 3661 -154 -273 -90 O HETATM 5424 O HOH B 512 -25.831 41.157 71.258 1.00 54.35 O ANISOU 5424 O HOH B 512 7135 7180 6337 294 238 -439 O HETATM 5425 O HOH B 513 -18.680 31.046 60.060 1.00 23.47 O ANISOU 5425 O HOH B 513 3172 3012 2734 41 -5 -70 O HETATM 5426 O HOH B 514 -4.451 24.906 66.143 1.00 55.85 O ANISOU 5426 O HOH B 514 7281 7652 6290 474 -238 81 O HETATM 5427 O HOH B 515 -25.883 22.034 65.531 1.00 38.24 O ANISOU 5427 O HOH B 515 5083 4766 4680 176 549 382 O HETATM 5428 O HOH B 516 -11.907 34.693 73.276 1.00 44.08 O ANISOU 5428 O HOH B 516 5826 6402 4519 470 -198 -423 O HETATM 5429 O HOH B 517 -21.197 36.296 18.325 1.00 37.56 O ANISOU 5429 O HOH B 517 4525 5605 4140 325 -455 94 O HETATM 5430 O HOH B 518 -12.084 33.250 21.052 1.00 37.64 O ANISOU 5430 O HOH B 518 4780 5130 4392 92 -284 27 O HETATM 5431 O HOH B 519 -20.452 31.228 74.738 1.00 45.38 O ANISOU 5431 O HOH B 519 6114 6378 4751 556 232 -7 O HETATM 5432 O HOH B 520 -17.137 30.818 33.472 1.00 28.08 O ANISOU 5432 O HOH B 520 3535 3587 3545 -185 -299 -136 O HETATM 5433 O HOH B 521 -13.070 23.993 17.566 1.00 44.39 O ANISOU 5433 O HOH B 521 5588 6171 5106 -86 -397 -477 O HETATM 5434 O HOH B 522 -20.144 33.323 52.061 1.00 22.24 O ANISOU 5434 O HOH B 522 2912 2703 2834 -121 -94 -117 O HETATM 5435 O HOH B 523 -8.402 23.678 60.853 1.00 42.81 O ANISOU 5435 O HOH B 523 5670 5600 4996 238 -94 136 O HETATM 5436 O HOH B 524 -19.997 36.834 34.953 1.00 22.69 O ANISOU 5436 O HOH B 524 2808 2902 2910 -72 -263 -11 O HETATM 5437 O HOH B 525 -28.436 30.393 59.871 1.00 34.77 O ANISOU 5437 O HOH B 525 4484 4335 4394 -21 242 26 O HETATM 5438 O HOH B 526 -15.675 49.779 59.230 1.00 32.84 O ANISOU 5438 O HOH B 526 4227 3905 4344 -89 -30 -746 O HETATM 5439 O HOH B 527 -12.727 28.915 65.179 1.00 34.39 O ANISOU 5439 O HOH B 527 4612 4684 3769 264 -83 -36 O HETATM 5440 O HOH B 528 -12.382 18.905 63.896 1.00 37.66 O ANISOU 5440 O HOH B 528 5103 4862 4344 369 215 435 O HETATM 5441 O HOH B 529 -16.379 33.345 20.931 1.00 41.18 O ANISOU 5441 O HOH B 529 5132 5734 4780 113 -374 -22 O HETATM 5442 O HOH B 530 -33.506 26.045 56.032 1.00 28.80 O ANISOU 5442 O HOH B 530 3521 3458 3964 -202 347 42 O HETATM 5443 O HOH B 531 -22.075 32.364 61.403 1.00 25.46 O ANISOU 5443 O HOH B 531 3411 3264 2999 56 78 -74 O HETATM 5444 O HOH B 532 -34.466 18.733 56.297 1.00 40.30 O ANISOU 5444 O HOH B 532 4931 4686 5695 -325 618 117 O HETATM 5445 O HOH B 533 -22.766 20.602 58.117 1.00 31.09 O ANISOU 5445 O HOH B 533 4111 3694 4007 -49 332 219 O HETATM 5446 O HOH B 534 -31.515 29.557 55.575 1.00 26.07 O ANISOU 5446 O HOH B 534 3232 3177 3497 -144 217 -2 O HETATM 5447 O HOH B 535 -12.881 31.365 45.768 1.00 24.88 O ANISOU 5447 O HOH B 535 3264 2994 3197 -179 -216 -120 O HETATM 5448 O HOH B 536 -13.470 31.536 58.318 1.00 25.19 O ANISOU 5448 O HOH B 536 3379 3251 2940 20 -148 -143 O HETATM 5449 O HOH B 537 -16.428 30.888 58.607 1.00 23.99 O ANISOU 5449 O HOH B 537 3233 3066 2816 17 -70 -90 O HETATM 5450 O HOH B 538 -20.483 38.853 74.506 1.00 39.37 O ANISOU 5450 O HOH B 538 5288 5596 4075 421 89 -492 O HETATM 5451 O HOH B 539 -17.990 42.337 71.461 1.00 42.73 O ANISOU 5451 O HOH B 539 5638 5864 4735 254 -46 -720 O HETATM 5452 O HOH B 540 -11.433 40.712 70.757 1.00 50.56 O ANISOU 5452 O HOH B 540 6556 7011 5644 236 -274 -794 O HETATM 5453 O HOH B 541 -10.242 32.544 65.707 1.00 33.45 O ANISOU 5453 O HOH B 541 4438 4667 3606 237 -228 -265 O HETATM 5454 O HOH B 542 -17.142 36.049 54.548 1.00 26.53 O ANISOU 5454 O HOH B 542 3489 3281 3309 -79 -132 -208 O HETATM 5455 O HOH B 543 -31.633 27.649 62.018 1.00 43.29 O ANISOU 5455 O HOH B 543 5532 5379 5536 -6 443 141 O HETATM 5456 O HOH B 544 -17.323 24.265 62.470 1.00 29.27 O ANISOU 5456 O HOH B 544 3979 3758 3384 171 150 191 O HETATM 5457 O HOH B 545 -27.781 43.154 56.362 1.00 33.19 O ANISOU 5457 O HOH B 545 4229 4054 4330 19 94 -222 O HETATM 5458 O HOH B 546 -7.658 22.261 64.912 1.00 39.03 O ANISOU 5458 O HOH B 546 5222 5306 4302 436 -52 255 O HETATM 5459 O HOH B 547 -24.644 37.699 47.261 1.00 23.73 O ANISOU 5459 O HOH B 547 2972 2890 3153 -108 -108 -96 O HETATM 5460 O HOH B 548 -3.304 29.665 17.172 1.00 45.72 O ANISOU 5460 O HOH B 548 5936 6069 5369 98 -124 -1 O HETATM 5461 O HOH B 549 -34.540 38.688 59.386 1.00 36.53 O ANISOU 5461 O HOH B 549 4562 4564 4754 42 280 -87 O HETATM 5462 O HOH B 550 -25.129 38.081 71.080 1.00 38.83 O ANISOU 5462 O HOH B 550 5185 5247 4320 310 236 -296 O HETATM 5463 O HOH B 551 -11.350 46.125 66.473 1.00 43.46 O ANISOU 5463 O HOH B 551 5579 5738 5197 10 -237 -990 O HETATM 5464 O HOH B 552 -10.423 32.612 68.911 1.00 38.26 O ANISOU 5464 O HOH B 552 5066 5446 4026 350 -221 -286 O HETATM 5465 O HOH B 553 -8.236 34.868 60.644 1.00 37.76 O ANISOU 5465 O HOH B 553 4913 5007 4425 53 -304 -367 O HETATM 5466 O HOH B 554 -17.166 49.130 56.935 1.00 31.82 O ANISOU 5466 O HOH B 554 4100 3728 4262 -79 -6 -594 O HETATM 5467 O HOH B 555 -31.319 43.255 14.399 1.00 56.72 O ANISOU 5467 O HOH B 555 6555 8750 6246 926 -592 495 O HETATM 5468 O HOH B 556 -22.567 28.571 19.838 1.00 37.38 O ANISOU 5468 O HOH B 556 4429 5548 4227 -17 -571 -395 O HETATM 5469 O HOH B 557 -31.034 20.630 65.243 1.00 42.94 O ANISOU 5469 O HOH B 557 5571 5217 5529 76 764 429 O HETATM 5470 O HOH B 558 -23.486 33.729 36.622 1.00 29.70 O ANISOU 5470 O HOH B 558 3629 3836 3821 -149 -282 -102 O HETATM 5471 O HOH B 559 -18.833 31.826 37.862 1.00 26.20 O ANISOU 5471 O HOH B 559 3301 3276 3380 -198 -259 -118 O HETATM 5472 O HOH B 560 -32.484 32.059 61.752 1.00 43.78 O ANISOU 5472 O HOH B 560 5569 5494 5570 18 361 34 O HETATM 5473 O HOH B 561 -30.101 32.672 57.412 1.00 32.72 O ANISOU 5473 O HOH B 561 4145 4060 4226 -64 186 -31 O HETATM 5474 O HOH B 562 -16.194 17.342 60.578 1.00 34.32 O ANISOU 5474 O HOH B 562 4646 4172 4223 170 342 409 O HETATM 5475 O HOH B 563 -25.258 37.496 44.676 1.00 34.88 O ANISOU 5475 O HOH B 563 4341 4337 4574 -109 -142 -75 O HETATM 5476 O HOH B 564 -28.395 14.574 57.050 1.00 40.23 O ANISOU 5476 O HOH B 564 5129 4546 5611 -230 688 268 O HETATM 5477 O HOH B 565 -17.814 44.032 68.949 1.00 51.68 O ANISOU 5477 O HOH B 565 6734 6835 6066 156 -57 -759 O HETATM 5478 O HOH B 566 -16.641 29.270 72.444 1.00 35.42 O ANISOU 5478 O HOH B 566 4828 5086 3543 519 104 36 O HETATM 5479 O HOH B 567 -28.769 42.276 13.769 1.00 60.87 O ANISOU 5479 O HOH B 567 7181 9199 6746 868 -558 461 O HETATM 5480 O HOH B 568 -31.382 36.001 64.899 1.00 44.62 O ANISOU 5480 O HOH B 568 5757 5688 5510 128 350 -71 O HETATM 5481 O HOH B 569 -26.660 11.701 56.421 1.00 50.70 O ANISOU 5481 O HOH B 569 6492 5749 7025 -236 769 310 O HETATM 5482 O HOH B 570 -16.955 38.436 55.815 1.00 31.24 O ANISOU 5482 O HOH B 570 4083 3882 3905 -65 -131 -283 O HETATM 5483 O HOH B 571 -20.404 27.405 71.665 1.00 47.04 O ANISOU 5483 O HOH B 571 6313 6380 5181 475 295 200 O HETATM 5484 O HOH B 572 -18.505 15.287 58.358 1.00 57.54 O ANISOU 5484 O HOH B 572 7547 6931 7386 43 449 392 O HETATM 5485 O HOH B 573 -11.725 37.726 19.469 1.00 45.12 O ANISOU 5485 O HOH B 573 5731 6090 5322 258 -185 265 O HETATM 5486 O HOH B 574 -22.790 18.048 58.919 1.00 46.33 O ANISOU 5486 O HOH B 574 6061 5556 5988 -26 450 311 O HETATM 5487 O HOH B 575 -25.447 11.356 54.490 1.00 55.83 O ANISOU 5487 O HOH B 575 7138 6382 7695 -280 696 234 O HETATM 5488 O HOH B 576 -18.827 29.031 73.471 1.00 47.79 O ANISOU 5488 O HOH B 576 6418 6641 5101 549 210 96 O HETATM 5489 O HOH B 577 -31.091 30.519 59.950 1.00 46.11 O ANISOU 5489 O HOH B 577 5864 5758 5900 -34 306 40 O HETATM 5490 O HOH B 578 -18.078 44.319 73.265 1.00 59.52 O ANISOU 5490 O HOH B 578 7762 8051 6803 277 -40 -884 O HETATM 5491 O HOH B 579 -35.028 16.287 53.822 1.00 58.17 O ANISOU 5491 O HOH B 579 7107 6859 8137 -454 634 19 O HETATM 5492 O HOH B 580 -18.659 42.649 74.990 1.00 54.01 O ANISOU 5492 O HOH B 580 7100 7477 5946 368 -10 -800 O HETATM 5493 O HOH B 581 -32.715 29.553 58.074 1.00 40.18 O ANISOU 5493 O HOH B 581 5034 4971 5262 -99 312 38 O HETATM 5494 O HOH B 582 -21.352 31.329 77.740 1.00 59.95 O ANISOU 5494 O HOH B 582 8000 8377 6403 690 310 16 O HETATM 5495 O HOH B 583 -12.683 42.565 71.994 1.00 60.99 O ANISOU 5495 O HOH B 583 7883 8339 6952 240 -238 -907 O HETATM 5496 O HOH B 584 -34.105 27.065 58.350 1.00 47.76 O ANISOU 5496 O HOH B 584 5955 5885 6308 -137 409 82 O HETATM 5497 O HOH B 585 -8.805 34.686 65.247 1.00 46.60 O ANISOU 5497 O HOH B 585 6059 6337 5312 186 -300 -405 O HETATM 5498 O HOH B 586 -7.580 36.422 62.542 1.00 47.11 O ANISOU 5498 O HOH B 586 6076 6277 5546 76 -338 -481 O HETATM 5499 O HOH B 587 -17.147 46.725 71.928 1.00 56.28 O ANISOU 5499 O HOH B 587 7308 7524 6553 188 -66 -1023 O CONECT 1 5030 CONECT 13 5053 CONECT 114 4974 CONECT 920 1471 CONECT 1471 920 CONECT 2274 5047 CONECT 2487 5151 CONECT 2489 5221 CONECT 2504 5244 CONECT 2605 5002 CONECT 3413 3961 CONECT 3961 3413 CONECT 4758 5238 CONECT 4972 5312 CONECT 4974 114 4975 4985 CONECT 4975 4974 4976 4982 CONECT 4976 4975 4977 4983 CONECT 4977 4976 4978 4984 CONECT 4978 4977 4979 4985 CONECT 4979 4978 4986 CONECT 4980 4981 4982 4987 CONECT 4981 4980 CONECT 4982 4975 4980 CONECT 4983 4976 CONECT 4984 4977 4988 CONECT 4985 4974 4978 CONECT 4986 4979 CONECT 4987 4980 CONECT 4988 4984 4989 4999 CONECT 4989 4988 4990 4996 CONECT 4990 4989 4991 4997 CONECT 4991 4990 4992 4998 CONECT 4992 4991 4993 4999 CONECT 4993 4992 5000 CONECT 4994 4995 4996 5001 CONECT 4995 4994 CONECT 4996 4989 4994 CONECT 4997 4990 CONECT 4998 4991 CONECT 4999 4988 4992 CONECT 5000 4993 CONECT 5001 4994 CONECT 5002 2605 5003 5013 CONECT 5003 5002 5004 5010 CONECT 5004 5003 5005 5011 CONECT 5005 5004 5006 5012 CONECT 5006 5005 5007 5013 CONECT 5007 5006 5014 CONECT 5008 5009 5010 5015 CONECT 5009 5008 CONECT 5010 5003 5008 CONECT 5011 5004 CONECT 5012 5005 5016 CONECT 5013 5002 5006 CONECT 5014 5007 CONECT 5015 5008 CONECT 5016 5012 5017 5027 CONECT 5017 5016 5018 5024 CONECT 5018 5017 5019 5025 CONECT 5019 5018 5020 5026 CONECT 5020 5019 5021 5027 CONECT 5021 5020 5028 CONECT 5022 5023 5024 5029 CONECT 5023 5022 CONECT 5024 5017 5022 CONECT 5025 5018 CONECT 5026 5019 CONECT 5027 5016 5020 CONECT 5028 5021 CONECT 5029 5022 CONECT 5030 1 5031 5032 CONECT 5031 5030 CONECT 5032 5030 CONECT 5033 5034 5038 5048 5049 CONECT 5034 5033 5035 CONECT 5035 5034 5036 CONECT 5036 5035 5037 CONECT 5037 5036 5038 5050 CONECT 5038 5033 5037 5039 CONECT 5039 5038 5040 CONECT 5040 5039 5041 CONECT 5041 5040 5042 5051 CONECT 5042 5041 5043 CONECT 5043 5042 5044 CONECT 5044 5043 5045 CONECT 5045 5044 5046 5052 CONECT 5046 5045 5047 CONECT 5047 2274 5046 CONECT 5048 5033 CONECT 5049 5033 CONECT 5050 5037 CONECT 5051 5041 CONECT 5052 5045 CONECT 5053 13 5054 5064 CONECT 5054 5053 5055 5061 CONECT 5055 5054 5056 5062 CONECT 5056 5055 5057 5063 CONECT 5057 5056 5058 5064 CONECT 5058 5057 5065 CONECT 5059 5060 5061 5066 CONECT 5060 5059 CONECT 5061 5054 5059 CONECT 5062 5055 CONECT 5063 5056 CONECT 5064 5053 5057 CONECT 5065 5058 CONECT 5066 5059 CONECT 5067 5069 CONECT 5068 5069 CONECT 5069 5067 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 5076 CONECT 5076 5075 5077 CONECT 5077 5076 5078 CONECT 5078 5077 5079 CONECT 5079 5078 CONECT 5080 5083 CONECT 5081 5082 5084 CONECT 5082 5081 5085 CONECT 5083 5080 5087 CONECT 5084 5081 5088 CONECT 5085 5082 5089 CONECT 5086 5100 5102 CONECT 5087 5083 5090 CONECT 5088 5084 5091 CONECT 5089 5085 5092 CONECT 5090 5087 5093 CONECT 5091 5088 5093 CONECT 5092 5089 5094 CONECT 5093 5090 5091 CONECT 5094 5092 5095 CONECT 5095 5094 5096 CONECT 5096 5095 5097 CONECT 5097 5096 5099 CONECT 5098 5100 5104 CONECT 5099 5097 5101 5104 CONECT 5100 5086 5098 5103 CONECT 5101 5099 CONECT 5102 5086 CONECT 5103 5100 CONECT 5104 5098 5099 CONECT 5105 5106 5107 CONECT 5106 5105 5108 CONECT 5107 5105 5109 CONECT 5108 5106 5110 CONECT 5109 5107 5112 CONECT 5110 5108 5113 CONECT 5111 5114 CONECT 5112 5109 5114 CONECT 5113 5110 5115 CONECT 5114 5111 5112 CONECT 5115 5113 5116 CONECT 5116 5115 5117 CONECT 5117 5116 5118 CONECT 5118 5117 5119 CONECT 5119 5118 5120 5121 CONECT 5120 5119 CONECT 5121 5119 CONECT 5122 5123 5124 CONECT 5123 5122 5125 CONECT 5124 5122 5126 CONECT 5125 5123 5127 CONECT 5126 5124 5128 CONECT 5127 5125 CONECT 5128 5126 CONECT 5129 5130 5131 CONECT 5130 5129 5132 CONECT 5131 5129 5133 CONECT 5132 5130 5134 CONECT 5133 5131 5135 CONECT 5134 5132 5136 CONECT 5135 5133 5137 CONECT 5136 5134 5138 CONECT 5137 5135 CONECT 5138 5136 CONECT 5139 5140 5141 CONECT 5140 5139 5142 CONECT 5141 5139 5143 CONECT 5142 5140 5144 CONECT 5143 5141 5145 CONECT 5144 5142 5146 CONECT 5145 5143 CONECT 5146 5144 5147 CONECT 5147 5146 5148 CONECT 5148 5147 5149 CONECT 5149 5148 5150 CONECT 5150 5149 CONECT 5151 2487 5152 5153 CONECT 5152 5151 CONECT 5153 5151 5154 CONECT 5154 5153 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 CONECT 5163 5164 CONECT 5164 5163 5165 CONECT 5165 5164 5166 CONECT 5166 5165 5167 CONECT 5167 5166 5168 CONECT 5168 5167 5169 CONECT 5169 5168 5170 CONECT 5170 5169 5171 5172 CONECT 5171 5170 CONECT 5172 5170 CONECT 5173 5176 CONECT 5174 5175 5177 CONECT 5175 5174 5178 CONECT 5176 5173 5180 CONECT 5177 5174 5181 CONECT 5178 5175 5182 CONECT 5179 5193 5195 CONECT 5180 5176 5183 CONECT 5181 5177 5184 CONECT 5182 5178 5185 CONECT 5183 5180 5186 CONECT 5184 5181 5186 CONECT 5185 5182 5187 CONECT 5186 5183 5184 CONECT 5187 5185 5188 CONECT 5188 5187 5189 CONECT 5189 5188 5190 CONECT 5190 5189 5192 CONECT 5191 5193 5197 CONECT 5192 5190 5194 5197 CONECT 5193 5179 5191 5196 CONECT 5194 5192 CONECT 5195 5179 CONECT 5196 5193 CONECT 5197 5191 5192 CONECT 5198 5199 CONECT 5199 5198 5200 CONECT 5200 5199 5201 CONECT 5201 5200 5202 CONECT 5202 5201 5203 CONECT 5203 5202 5204 CONECT 5204 5203 5205 CONECT 5205 5204 5206 5207 CONECT 5206 5205 CONECT 5207 5205 CONECT 5208 5209 5210 CONECT 5209 5208 5211 CONECT 5210 5208 5212 CONECT 5211 5209 5213 CONECT 5212 5210 5214 CONECT 5213 5211 5215 CONECT 5214 5212 5216 CONECT 5215 5213 5217 CONECT 5216 5214 CONECT 5217 5215 5218 CONECT 5218 5217 5219 CONECT 5219 5218 5220 CONECT 5220 5219 CONECT 5221 2489 5222 5223 CONECT 5222 5221 CONECT 5223 5221 CONECT 5224 5225 5229 5239 5240 CONECT 5225 5224 5226 CONECT 5226 5225 5227 CONECT 5227 5226 5228 CONECT 5228 5227 5229 5241 CONECT 5229 5224 5228 5230 CONECT 5230 5229 5231 CONECT 5231 5230 5232 CONECT 5232 5231 5233 5242 CONECT 5233 5232 5234 CONECT 5234 5233 5235 CONECT 5235 5234 5236 CONECT 5236 5235 5237 5243 CONECT 5237 5236 5238 CONECT 5238 4758 5237 CONECT 5239 5224 CONECT 5240 5224 CONECT 5241 5228 CONECT 5242 5232 CONECT 5243 5236 CONECT 5244 2504 5245 5255 CONECT 5245 5244 5246 5252 CONECT 5246 5245 5247 5253 CONECT 5247 5246 5248 5254 CONECT 5248 5247 5249 5255 CONECT 5249 5248 5256 CONECT 5250 5251 5252 5257 CONECT 5251 5250 CONECT 5252 5245 5250 CONECT 5253 5246 CONECT 5254 5247 CONECT 5255 5244 5248 CONECT 5256 5249 CONECT 5257 5250 CONECT 5258 5259 5260 CONECT 5259 5258 5261 CONECT 5260 5258 5262 CONECT 5261 5259 5263 CONECT 5262 5260 5265 CONECT 5263 5261 5266 CONECT 5264 5267 CONECT 5265 5262 5267 CONECT 5266 5263 5268 CONECT 5267 5264 5265 CONECT 5268 5266 5269 CONECT 5269 5268 5270 CONECT 5270 5269 5271 CONECT 5271 5270 5273 CONECT 5272 5274 5276 CONECT 5273 5271 5275 5276 CONECT 5274 5272 CONECT 5275 5273 CONECT 5276 5272 5273 CONECT 5277 5278 5279 CONECT 5278 5277 5280 CONECT 5279 5277 CONECT 5280 5278 5282 CONECT 5281 5290 5292 CONECT 5282 5280 5283 CONECT 5283 5282 5284 CONECT 5284 5283 5285 CONECT 5285 5284 5286 CONECT 5286 5285 5287 CONECT 5287 5286 5289 CONECT 5288 5290 5294 CONECT 5289 5287 5291 5294 CONECT 5290 5281 5288 5293 CONECT 5291 5289 CONECT 5292 5281 CONECT 5293 5290 CONECT 5294 5288 5289 CONECT 5295 5298 CONECT 5296 5297 5299 CONECT 5297 5296 5300 CONECT 5298 5295 5301 CONECT 5299 5296 5302 CONECT 5300 5297 5303 CONECT 5301 5298 5304 CONECT 5302 5299 5305 CONECT 5303 5300 5306 CONECT 5304 5301 5307 CONECT 5305 5302 5307 CONECT 5306 5303 5308 CONECT 5307 5304 5305 CONECT 5308 5306 5309 CONECT 5309 5308 5310 CONECT 5310 5309 5311 CONECT 5311 5310 CONECT 5312 4972 5313 5314 CONECT 5313 5312 CONECT 5314 5312 5315 CONECT 5315 5314 5316 CONECT 5316 5315 5317 CONECT 5317 5316 5318 CONECT 5318 5317 CONECT 5319 5320 5321 CONECT 5320 5319 5322 CONECT 5321 5319 5323 CONECT 5322 5320 5324 CONECT 5323 5321 5325 CONECT 5324 5322 CONECT 5325 5323 MASTER 409 0 26 28 8 0 0 6 5327 2 366 54 END